Authors,Author(s) ID,Title,Year,Source title,Volume,Issue,Art. No.,Page start,Page end,Page count,Cited by,DOI,Link,Affiliations,Authors with affiliations,Abstract,Author Keywords,Index Keywords,References,Correspondence Address,Editors,Publisher,ISSN,ISBN,CODEN,PubMed ID,Language of Original Document,Abbreviated Source Title,Document Type,Publication Stage,Access Type,Source,EID
"Wesseling J.G., Vennema H., Godeke G.-J., Horzinek M.C., Rottier P.J.M.","57214985161;7003697291;6603099700;7102624836;7006145490;","Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses",1994,"Journal of General Virology","75","7",,"1789","1794",,29,"10.1099/0022-1317-75-7-1789","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028231088&doi=10.1099%2f0022-1317-75-7-1789&partnerID=40&md5=8e8d41d62a8d944466471d79d72e4dbc","Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands","Wesseling, J.G., Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands; Vennema, H., Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands; Godeke, G.-J., Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands; Horzinek, M.C., Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands; Rottier, P.J.M., Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands","We have cloned, sequenced and expressed the spike (S) gene of canine coronavirus (CCV; strain K378). Its deduced amino acid sequence has revealed features in common with other coronavirus S proteins: a stretch of hydrophobic amino acids at the amino terminus (the putative signal sequence), another hydrophobic region at the carboxy terminus (the membrane anchor), heptad repeats preceding the anchor, and a cysteine-rich region located just downstream from it. Like other representatives of the same antigenic cluster (CCV-Insavc-1 strain, feline infectious peritonitis and enteric coronaviruses, porcine transmissible gastroenteritis and respiratory coronaviruses, and the human coronavirus HCV 229E), the CCV S polypeptide lacks a proteolytic cleavage site present in many other coronavirus S proteins. Pairwise comparisons of the S amino acid sequences within the antigenic cluster demonstrated that the two CCV strains (K378 and Insavc-1) are 93.3% identical about as similar to each other as they are to the two feline coronaviruses. The porcine sequences are clearly more divergent mainly due to the large differences in the amino-terminal (residues 1 to 300) domains of the proteins; when only the carboxy-terminal parts (residues 301 and on) are considered the homologies between the canine, feline and porcine S polypeptides are generally quite high, with identities ranging from 90.8% to 96.8%. The human coronavirus is less related to the other members of the antigenic group. A phylogenetic tree constructed on the basis of the S sequences showed that the two CCVs are evolutionarily more related to the feline than to the porcine viruses. Expression of the CCV S gene using the vaccinia virus T7 RNA polymerase system yielded a protein of the expected M(r) (approximately 200 K) which could be immunoprecipitated with an anti-feline infectious peritonitis virus polyclonal serum and which was indistinguishable from the S protein synthesized in CCV-infected cells.",,"polyclonal antibody; repetitive DNA; RNA polymerase; signal peptide; virus antibody; virus protein; vitronectin; amino acid sequence; amino terminal sequence; animal cell; antigenicity; article; carboxy terminal sequence; cat disease; controlled study; Coronavirus; dog disease; gene expression; human; human cell; immunoprecipitation; molecular cloning; nonhuman; nucleotide sequence; phylogeny; priority journal; protein synthesis; sequence homology; swine disease; Vaccinia virus; virus gene; Animalia; Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus; Hepatitis C virus; human coronavirus; Suidae; Sus scrofa; Vaccinia; Vaccinia virus",,"Rottier, P.J.M.; Virology Division, Dept Infectious Diseases Immunology, Veterin Faculty, Utrecht University, PO Box 80 165, 3508 TD Utrecht, Netherlands",,"Microbiology Society",00221317,,JGVIA,"8021609","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0028231088
"Athanassious R., Marsolais G., Assaf R., Dea S., Descôteaux J.P., Dulude S., Montpetit C.","6602950083;6604093082;6603787051;7006056287;7003863437;6504432464;6602189643;","Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: evaluation of three diagnostic methods.",1994,"The Canadian veterinary journal. La revue vétérinaire canadienne","35","3",,"163","169",,33,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028398255&partnerID=40&md5=7c35f9ce2b042ed4702e167f01235c3c","Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada","Athanassious, R., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Marsolais, G., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Assaf, R., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Dea, S., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Descôteaux, J.P., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Dulude, S., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada; Montpetit, C., Centre de recherche en Virologie, Pêcheries et de l'Alimentation du Québec, Laval, Canada","The use of direct electron microscopy, enzyme-linked immunosorbent assay, and protein A-gold immunoelectron microscopy for the identification of bovine coronavirus and type A rotavirus were examined. Two hundred and forty-nine samples from diarrheic calves and winter dysenteric cattle from seven geographic areas in Quebec were examined for the presence of viruses by direct electron microscopy of negatively stained preparations. In addition, all the samples were analyzed by enzyme-linked immunosorbent assay, and a random selection of 47 samples were also analyzed by protein A-gold immunoelectron microscopy. Thirty-nine percent of samples examined by direct electron microscopy contained viral particles; bovine coronavirus and type A rotavirus were the most common viruses involved. Overall agreement between any two of the methods used compared favorably with results obtained by others using similar methods. The presence of coronavirus and rotavirus in fecal samples obtained from neonatal calves and the presence of coronavirus in samples from winter dysenteric adult cattle suggested their etiological roles in the respective diseases. Furthermore, results from protein A-gold immunoelectron microscopy of coronavirus-like particles implied that a different coronavirus or some other viruses might be involved in these diseases. Finally, the efficiency of direct electron microscopy, enzyme-linked immunosorbent assay and protein A-gold immunoelectron microscopy as diagnostic tools is discussed.",,"animal; animal disease; article; Canada; cattle; cattle disease; comparative study; Coronavirus; diarrhea; dysentery; electron microscopy; enzyme linked immunosorbent assay; evaluation; immunoelectron microscopy; isolation and purification; microbiology; newborn; Rotavirus; season; ultrastructure; virion; virus infection; Animals; Animals, Newborn; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Dysentery; Enzyme-Linked Immunosorbent Assay; Evaluation Studies; Microscopy, Electron; Microscopy, Immunoelectron; Quebec; Rotavirus; Rotavirus Infections; Seasons; Virion",,"Athanassious, R.",,,00085286,,,"8055431","English","Can. Vet. J.",Article,"Final",,Scopus,2-s2.0-0028398255
"Jackwood D.J., Bae I., Jackwood R.J., Saif L.J.","7005468303;7004882628;7801609560;7102226747;","Transmissible gastroenteritis virus and porcine respiratory coronavirus: Molecular characterization of the S gene using cDNA probes and nucleotide sequence analysis",1994,"Advances in Experimental Medicine and Biology","342",,,"43","48",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028258307&partnerID=40&md5=6da04e97202c3de0078737eedc2bbb30","Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States","Jackwood, D.J., Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States; Bae, I., Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States; Jackwood, R.J., Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States","Two transmissible gastroenteritis virus (TGEV, Miller strain) cDNA clones were identified and their nucleotide sequences determined. The clones were non-overlapping and were located in the 5' region of the S glycoprotein gene. The TGEV clone pE21 contained 381 bp of the S glycoprotein gene and had >98% nucleotide and amino acid sequence homology with the Purdue (P115) strain of TGEV and over 87% sequence homology with feline infectious peritonitis virus (FIPV). The TGEV clone, pD24, contained 267 bp of the S glycoprotein gene. It had >98% nucleotide and amino acid sequence homology with P115 but only a 49% nucleotide sequence homology and a 24% amino acid sequence homology with FIPV. Using dot blot hybridization, a probe prepared from pD24 could differentiate TGEV from the antigenically related coronaviruses, FIPV, feline enteric coronavirus and canine coronavirus. This probe could also differentiate TGEV from porcine respiratory coronavirus (PRCV). Using polymerase chain reaction amplified regions of PRCV isolates and nucleotide sequencing, a 681 bp deletion in the 5' region of the S gene from PRCV isolate ISU-1 was identified. This deletion was located in the area of the S glycoprotein gene identified by the pD24 probe.",,"complementary dna; virus glycoprotein; amino acid sequence; animal cell; conference paper; coronavirus; dna probe; dog; dot hybridization; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; sequence homology; swine; virus gene; Amino Acid Sequence; Animal; Base Sequence; Comparative Study; Coronavirus, Feline; DNA, Complementary; Genes, Structural, Viral; Membrane Glycoproteins; Molecular Sequence Data; Polymerase Chain Reaction; Sequence Alignment; Sequence Deletion; Sequence Homology, Nucleic Acid; Species Specificity; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Jackwood, D.J.; Food Animal Health Research Program, Ohio State University, Ohio Agricultural Res./Devt. Center, Wooster, OH 44691, United States",,,00652598,,AEMBA,"8209764","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028258307
"Daniel C., Lamarre A., Talbot P.J.","11439494900;7004646746;7102670281;","Increased viral titers and enhanced reactivity of antibodies to the spike glycoprotein of murine coronavirus produced by infection at pH 6",1994,"Journal of Virological Methods","50","1-3",,"237","244",,,"10.1016/0166-0934(94)90180-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028578039&doi=10.1016%2f0166-0934%2894%2990180-5&partnerID=40&md5=31031cc6eeec9b606da872454deab95c","Virology Research Center, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Daniel, C., Virology Research Center, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Lamarre, A., Virology Research Center, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Talbot, P.J., Virology Research Center, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Infection of cell monolayers by murine coronavirus A59 at pH 6 rather than 7 yielded a ten-fold increase in the infectious titer and a remarkable enhancement of the reactivities of monoclonal and polyclonal antibodies against the spike glycoprotein in immunoblotting, immuno-precipitation and enzyme-linked immunosorbent assays. These observations are very useful for detecting antibodies against the S glycoprotein of coronaviruses and enhancing infectious titers. © 1994.","Antibody; Antigenicity; Coronavirus; Infectivity; S glycoprotein","animal cell; article; controlled study; enzyme linked immunosorbent assay; immunoblotting; immunoprecipitation; mouse; murine hepatitis coronavirus; nonhuman; ph; priority journal; virus detection; virus infectivity; virus titration; Animal; Antibodies; Coronavirus; Coronavirus Infections; Hydrogen-Ion Concentration; Membrane Glycoproteins; Mice; Support, Non-U.S. Gov't; Tumor Cells, Cultured; Viral Envelope Proteins; Virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Collins, Knobler, Powell, Buchmeier, Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Daniel, Talbot, Physico-chemical properties of murine hepatitis virus, strain A59 (1987) Arch. Virol., 96, pp. 241-248; Daniel, Talbot, Protection from lethal coronavirus infection by affinity-purified spike glycoprotein of murine hepatitis virus, strain A59 (1990) Virology, 174, pp. 87-94; Daniel, Anderson, Buchmeier, Fleming, Spaan, Wege, Talbot, Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of a complex tridimensional structure (1993) J. Virol., 67, pp. 1185-1194; Daniel, Lacroix, Talbot, Mapping of linear antigenic sites on the s glycoprotein of a neurotropic murine coronavirus with synthetic peptides a combination of nine prediction algorithms fails to identify relevant epitopes and peptide immunogenicity is drastically influenced by the nature of the protein carrier (1994) Virology, , (in press); Frana, Behnke, Sturman, Holmes, Proteolytic cleavage of the E2 glyco-protein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Hawkes, Niday, Gordon, A dot-immunobinding assay for monoclonal and other antibodies (1982) Anal. Biochem., 119, pp. 142-147; Hirano, Fujiwara, Hino, Matumoto, Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture. Arch (1974) Ges. Virusforsch., 44, pp. 298-302; Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Luytjes, Geerts, Posthumus, Meloen, Spaan, Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses (1989) J. Virol., 63, pp. 1408-1412; Sturman, Holmes, The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-112; Sturman, Ricard, Holmes, Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Talbot, Knobler, Buchmeier, Western and dot immunoblotting analysis of viral antigens and antibodies: application to murine hepatitis virus (1984) J. Immunol. Methods, 73, pp. 177-188; Talbot, Salmi, Knobler, Buchmeier, Topographical mapping of epitopes on the glycoproteins of murine hepatitis virus-4 (strain JHM): correlation with biological activities (1984) Virology, 132, pp. 250-260; ter Meulen, Massa, Dorries, Coronaviruses (1989) Viral Disease, 12, pp. 439-451. , R.R. McKendall, Handbook of Clinical Neurology, Elsevier Science, Amsterdam; Vennema, Heijnen, Zijderveld, Horzinek, Spaan, Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Wege, Dorries, Wege, Hybridoma antibodies to the murine coronavirus JHM: characterization of epitopes on the peplomer protein (E2) (1984) J. Gen. Virol., 65, pp. 1931-1942; Wege, Siddell, ter Meulen, The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Weismiller, Sturman, Buchmeier, Fleming, Holmes, Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions (1990) J. Virol., 64, pp. 3051-3055; Williams, Jiang, Holmes, Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536","Talbot, P.J.; Virology Research Center, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; email: Pierre_Talbot@iaf.uquebec.ca",,,01660934,,JVMED,"7714047","English","J. Virol. Methods",Article,"Final",,Scopus,2-s2.0-0028578039
"Enjuanes L., Sanchez C., Gebauer F., Mendez A., Dopazo J., Ballesteros M.L.","7006565392;57193985365;7004526580;36823007700;18133480200;7006110601;","Evolution and tropism of transmissible gastroenteritis coronavirus",1994,"Advances in Experimental Medicine and Biology","342",,,"35","42",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326924&partnerID=40&md5=704b6d8d7b943c1b02a464de5590fd61","Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain","Enjuanes, L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Sanchez, C., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Gebauer, F., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Mendez, A., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Dopazo, J., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Ballesteros, M.L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain","Transmissible gastroenteritis coronavirus (TGEV) is an enteropathogenic coronavirus isolated for the first time in 1946. Nonenteropathogenic porcine respiratory coronaviruses (PRCVs) have been derived from TGEV. The genetic relationship among six European PRCVs and five coronaviruses of the TGEV antigenic cluster has been determined based on their RNA sequences. The S proteins of six European PRCVs have an identical deletion of 224 amino acids starting at position 21. The deleted area includes the antigenic sites C and B of TGEV S glycoprotein. Interestingly, two viruses (NEB72 and TOY56) with respiratory tropism have the S protein with a similar size to the enteric viruses. NEB72 and TOY56 viruses have 2 and 15 specific amino acid differences with the enteric viruses, respectively. Four of the residues changed are located within the deletion present in the PRCVs and may influence the enteric tropism of TGEV in vivo. A receptor binding site (RBS) used by the virus to infect ST and other cell types might be located between sites A and D of the S glycoprotein, since monoclonal antibodies (MAbs) specific for these sites inhibit the binding of the virus to ST cells. An evolutionary tree relating 13 enteric and respiratory isolates has been proposed. According to this tree, a main virus lineage evolved from a recent progenitor which was circulating around 1941. From this, secondary lineages originated PUR46, NEB72, TOY56, MIL65, BRI70, and the PRCVs, in this order. Least squares estimation of the origin of TGEV-related coronaviruses showed a significant constancy in the mutation fixation rate. This rate was 7±2 x 10-4 nucleotide substitutions per site and per year and falls in the range reported for other RNA viruses. Point mutations and probably recombination events have occurred during TGEV evolution.",,"monoclonal antibody; virus glycoprotein; virus rna; animal cell; conference paper; coronavirus; gene deletion; genetic recombination; nonhuman; point mutation; priority journal; rna sequence; sequence analysis; swine; Amino Acid Sequence; Animal; Cell Line; Coronavirus; Genes, Structural, Viral; Male; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Sequence Alignment; Sequence Deletion; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Swine; Testis; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Enjuanes, L.; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"8209753","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028326924
"Myint S., Johnston S., Sanderson G., Simpson H.","35479862600;7401781716;7007146784;16186799200;","Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43",1994,"Molecular and Cellular Probes","8","5",,"357","364",,65,"10.1006/mcpr.1994.1052","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028035328&doi=10.1006%2fmcpr.1994.1052&partnerID=40&md5=9bcdd7f29a773383ae886c16a9c67d56","Department of Medicine, University of Southampton, United Kingdom; Departments of Microbiology, University of Leicester, United Kingdom; Departments of Child Health, University of Leicester, United Kingdom","Myint, S., Department of Medicine, University of Southampton, United Kingdom; Johnston, S., Departments of Microbiology, University of Leicester, United Kingdom; Sanderson, G., Departments of Microbiology, University of Leicester, United Kingdom; Simpson, H., Departments of Child Health, University of Leicester, United Kingdom","Currently the diagnosis of human respiratory coronavirus infection is either slow or insensitive. This paper describes nested polymerase chain reaction assays for the detection of human coronaviruses OC43 and 229E. The specificity and sensitivity of the assays have been determined and they have been applied to the detection of the viruses in nasal aspirates. These assays are more rapid and sensitive than cell culture and may replace the latter as the diagnostic method of choice. © 1994 Academic Press.","Coronavirus; Diagnosis; Polymerase chain reaction; Respiratory tract",,"McIntosh, K., Ellis, E.F., Hoffmann, L.S., Lybass, T.G., Eller, J.J., Fulginiti, V.A., The association of viral and bacterial respiratory infections with exacerbations of wheezing in young asthmatic children (1973) Journal of Paediatrics, 82, pp. 579-590; Myint, S., Siddell, S.G., Tyrrell, D.A.J., The detection of human coronavirus 229E in nasal washings using RNA:RNA hybridisation (1990) Journal of Medical Virology, 29, pp. 70-73; McIntosh, K., McQuillin, M.S., Reed, E., Gardner, P.S., Diagnosis of human coronavirus infection by immunofluorescence: Method and application to respiratory disease in hospitalised children (1978) Journal of Medical Virology, 2, pp. 341-346; Myint, S., Harmsen, D., Raabe, T., Siddell, S.G., Characterisation of a nucleic acid probe for the detection of human coronavirus 229E (1990) Journal of Medical Virology, 31, pp. 165-172; Kamahora, T., Soe, L.H., Lai, M.M., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Cirus Research, 12, pp. 1-9; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid-guanidium thi-ocyanate phenol-chloroform extraction (1987) Analytical Biochemistry, 162, pp. 156-159; Kraajeveld, G.A., Reed, S.E., Macnaughton, M.R., Enzyme-linked immunosorbent assay for cor-onaviruses HCV 229E and MHV 3 (1980) Journal of General Virology, 49, pp. 83-89; Balfour-Lynn, I.N., Valman, H.B., Stanway, G., Khan, M., Use of the polymerase chain reaction to detect rhinovirus in wheezy infants (1992) Archives of Disease in Childhood, 67, p. 760; Pisareva, M., Bechtereva, T., Plyusnin, A., Dobretsova, A., Kisselev, O., PCR-amplification of influenza A virus specific sequences (1992) Archives of Virology, 125, pp. 313-318; Myint, S., (1989) The Development of a Nucleic Acid Hybridisation Assay for the Detection of Human Cor-Onavirus, p. 229E. , MD thesis, University of London","Myint, S.; Department of Microbiology, University of Leicester, Leicester LE1 9HN, United Kingdom",,,08908508,,,,"English","MOL. CELL. PROBES",Article,"Final",Open Access,Scopus,2-s2.0-0028035328
"Barker M.G., Percy D.H., Hovland D.J., MacInnes J.I.","7202354148;16140219400;6602350019;57213630565;","Preliminary characterization of the structural proteins of the coronaviruses, sialodacryoadenitis virus and Parker's rat coronavirus.",1994,"Canadian journal of veterinary research = Revue canadienne de recherche vétérinaire","58","2",,"99","103",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028411076&partnerID=40&md5=6cea49b1a1230a05e7431129e579b0ed","Department of Pathology, University of GuelphOntario","Barker, M.G., Department of Pathology, University of GuelphOntario; Percy, D.H., Department of Pathology, University of GuelphOntario; Hovland, D.J., Department of Pathology, University of GuelphOntario; MacInnes, J.I., Department of Pathology, University of GuelphOntario","A procedure was developed for the partial purification of the rat coronaviruses, sialodacryoadenitis virus (SDAV) and Parker's rat coronavirus (PRC). The SDAV and PRC were replicated in L-2 cell monolayer cultures, precipitated with ammonium sulphate, and further concentrated using sucrose density gradient centrifugation. The major SDAV and PRC proteins were identified by immunoblotting and compared with those of the JHM strain of mouse hepatitis virus (MHV-JHM). Monoclonal antibodies (MAb) against the M protein of JHM recognized proteins interpreted to be slightly smaller in immunoblots of SDAV and PRC (22.8 vs 23K for JHM). Similarly, a monoclonal antibody against the JHM N protein reacted with proteins of 53K in SDAV and PRC (vs 56 K for JHM). Polyclonal antisera to all three viruses also cross-reacted with the M and N proteins. Some cross-reactivity amongst the S proteins was observed. Based on these data, the structural proteins of the rat coronaviruses, SDAV and PRC are closely related to those of MHV-JHM.",,"ammonium sulfate; antiserum; monoclonal antibody; virus protein; animal; article; cell line; chemistry; Coronavirus; density gradient centrifugation; immunoblotting; immunology; isolation and purification; molecular weight; precipitation; rat; Ammonium Sulfate; Animals; Antibodies, Monoclonal; Cell Line; Centrifugation, Density Gradient; Coronavirus, Rat; Immune Sera; Immunoblotting; Molecular Weight; Precipitation; Rats; Viral Structural Proteins",,"Barker, M.G.",,,08309000,,,"8004548","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028411076
"Lai M.M.C., Liao C.-L., Lin Y.-J., Zhang X.","7401808497;7401957370;7406589398;55715175900;","Coronavirus: How a large RNA viral genome is replicated and transcribed",1994,"Infectious Agents and Disease","3","2-3",,"98","105",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028047922&partnerID=40&md5=3dd2f7e94fe88242ea8edbe2d715fae4","Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States","Lai, M.M.C., Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States; Liao, C.-L., Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States; Lin, Y.-J., Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States; Zhang, X., Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States","Coronaviruses are important human and animal pathogens and contain an extraordinarily long (27-31 kb) RNA genome. Its RNA synthesis involves complex mechanisms of regulation, similar to those of DNA viruses. In this treatise, mouse hepatitis virus (MHV) is used as a model for the discussion of the mechanism of viral RNA synthesis. We show that MHV RNA synthesis requires interactions of multiple RNA components, which are likely mediated by protein-RNA and protein-protein, as well as RNA-RNA, interactions. This virus also provides a unique example of a discontinuous transcription mechanism, which involves a trans-acting RNA component. Finally, study of the cis-acting signals for the various steps of RNA synthesis revealed an insight into the regulation of viral RNA synthesis. This discussion suggests that the regulation of RNA synthesis in coronavirus is more complex than previously thought possible for RNA viruses. Coronavirus RNA transcription and replication may serve as a paradigm of RNA synthesis for RNA viruses in general.",,"virus rna; conference paper; coronavirus; murine hepatitis coronavirus; priority journal; protein protein interaction; regulatory mechanism; rna synthesis; transcription regulation; virus morphology; virus replication; virus transcription; Animal; Base Sequence; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Viral; RNA-Binding Proteins; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic",,"Lai, M.M.C.; Department of Microbiology, School of Medicine, University of Southern California, 2011 Zonal Avenue, Los Angeles, CA 90033-1054, United States",,,10562044,,IADIE,"7812660","English","INFECT. AGENTS DIS.",Conference Paper,"Final",,Scopus,2-s2.0-0028047922
"Gill E.P., Dominguez E.A., Greenberg S.B., Atmar R.L., Hogue B.G., Baxter B.D., Couch R.B.","7101827652;7103240390;7402294401;7005296248;7003393593;7102396651;7102611225;","Development and application of an enzyme immunoassay for coronavirus OC43 antibody in acute respiratory illness",1994,"Journal of Clinical Microbiology","32","10",,"2372","2376",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028059485&partnerID=40&md5=1d6553c63897a944ab2fc7870f4c1a39","Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Gill, E.P., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Dominguez, E.A., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Greenberg, S.B., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Atmar, R.L., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Hogue, B.G., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Baxter, B.D., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Couch, R.B., Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Study of coronavirus OC43 infections has been limited because of the lack of sensitive cell culture systems and serologic assays. To improve this circumstance, we developed an indirect enzyme immunoassay (EIA) to detect serum antibody to OC43. Antigen (100 ng) prepared by polyethylene glycol precipitation provided optimal results without a postcoat procedure. Evaluation of intraplate variation indicated that a ≥2.5-fold increase in serum titer was significant. Sixteen of 18 (89%) paired serum samples with previously identified, reproducible increases in the level of hemagglutination inhibition (HAI) antibody to OC43 also showed significant increases as detected by EIA. Specificity for the EIA was established with paired sera obtained from persons given influenza immunizations or experiencing a respiratory infection. No rises in antibody titers occurred among 33 persons with documented coronavirus 229E infection. EIA was then performed on each of 419 paired serum samples from ambulatory chronic obstructive pulmonary disease patients and healthy older adults, from asthmatic adults presenting for emergency room treatment, and from persons hospitalized with acute respiratory symptoms. Twenty-three antibody rises to OC43 were detected; only nine of these were detected by the HAI test, and the HAI test did not detect any increases in antibody titers that were not detected by EIA. Nineteen of 25 coronavirus OC43 infections for which a month of infection could be assigned occurred between November and February. Overall, 4.4% of acute respiratory illnesses in the studied populations were associated with a coronavirus OC43 infection.",,"hemagglutination inhibiting antibody; macrogol; neutralizing antibody; virus antibody; antibody titer; article; asthma; chronic obstructive lung disease; complement fixation; coronavirus; enzyme immunoassay; human; priority journal; respiratory tract infection; virus detection; virus infection; Acute Disease; Antibodies, Viral; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus OC43, Human; Human; Immunoenzyme Techniques; Reproducibility of Results; Respiratory Tract Infections; Support, U.S. Gov't, P.H.S.",,"Couch, R.B.; Microbiology/Immunology Department, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States",,,00951137,,JCMID,"7814468","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0028059485
"Cabirac G.F., Soike K.F., Zhang J.-Y., Hoel K., Butunoi C., Cai G.-Y., Johnson S., Murray R.S.","6602498805;7006220553;11641215100;6602461039;6507828683;57199040369;57207906756;7403022204;","Entry of coronavirus into primate CNS following peripheral infection",1994,"Microbial Pathogenesis","16","5",,"349","357",,18,"10.1006/mpat.1994.1035","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028124964&doi=10.1006%2fmpat.1994.1035&partnerID=40&md5=3961177b053ed1925012355fb3355061","Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States; Department of Biochemistry, Biophysics and Genetics, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Tulane Regional Primate Research Center, Covington, LA 70433, United States","Cabirac, G.F., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States, Department of Biochemistry, Biophysics and Genetics, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Soike, K.F., Tulane Regional Primate Research Center, Covington, LA 70433, United States; Zhang, J.-Y., Tulane Regional Primate Research Center, Covington, LA 70433, United States; Hoel, K., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States; Butunoi, C., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States; Cai, G.-Y., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States; Johnson, S., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States; Murray, R.S., Rocky Mountain Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80110, United States","A previous report demonstrated that intracerebrally inoculated coronavirus produced CNS disease in two species of primates (Murray RS, Cai G-Y, Hoel K, et al., Virol 1992; 188: 274-84). We were therefore interested in testing the potential of coronaviruses to infect primate CNS tissue following peripheral inoculation. Four Owl monkeys (Aotus trivirgatus) were inoculated intranasally and ocularly and four were inoculated intravenously with coronavirus JHM OMp1 (Murray RS, Cai G-Y, Hoel K, et al., Virol 1992; 188: 274-84). Two intranasally and two intravenously inoculated animals received a second intravenous inoculum at 153 days post-infection. The animals were sacrificed 16, 38, 194, and 215 days post-infection. Tissue sections from brain and spinal cord were screened for viral products by in situ hybridization and immunostaining. Virus RNA and/or antigen was detected in the brains of all animals and the distribution corresponded to areas of inflammation and edema. Viral products were predominantly found in blood vessels and perivascular regions, suggesting hematogenous spread with entry into the central nervous system through endothelium. © 1994 Academic Press. All rights reserved.","Brain endothelial cells; Coronavirus; Primate","animal experiment; article; central nervous system; controlled study; coronavirus; histology; monkey; nonhuman; priority journal; virus cell interaction; virus infection; virus pathogenesis; Administration, Intranasal; Animal; Antigens, Viral; Aotus trivirgatus; Brain; Central Nervous System; Comparative Study; Disease Susceptibility; Encephalomyelitis; Injections, Intravenous; Instillation, Drug; Mice; Murine hepatitis virus; RNA, Viral; Species Specificity; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Tumor Cells, Cultured; Virus Cultivation; Animalia; Aotus trivirgatus; Coronavirus; Primates; Strigiformes","Murray, R.S., Cai, G.-Y., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primate central nervous system (1992) Virol, 188, pp. 274-284; Hovi, T., Kainulainen, H., Ziola, B., Salmi, A., OC43 strain-related coronavirus antibodies in different age groups (1979) J Med Virol, 3, pp. 313-320; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann Neurol, 31, pp. 525-533; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brain of multiple sclerosis patients (1992) Virol, 191, pp. 502-505; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human Aminopeptidase, N., Is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Barthold, S.W., Smith, A.L., Mouse hepatitis virus S in weanling mice following intranasal inoculation (1983) Lab Anim Sei, 33, pp. 355-360; Barthold, S.W., Beck, D.S., Smith, A.L., Mouse hepatitis virus nasoencephalopathy is dependent upon virus strain and host genotype (1986) Arch Virol, 91, pp. 247-256; Goto, N., Hirano, N., Aiuchi, M., Hayashi, T., Fujiwara, K., Nasoencephalopathy of mice infected intranasally with a mouse hepatitis virus JHM strain (1977) Jpn J Exp Med, 47, pp. 59-70; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., The organ tropism of mouse hepatitis virus A59 in mice is dependent on dose and route of inoculation (1986) Lab Anim Sei, 36, pp. 130-135; Perlman, S., Jacobsen, G., Afifi, A., Spread of neurotropic murine coronavirus into the CNS via the trigeminal and olfactory nerves (1989) Virol, 170, pp. 556-560; Tardieu, M., Goffinet, A., Harmant-Van Rijckevorsel, G., Lyon, G., Ependymitis, leukoencephalitis, hydrocephalus, and thrombotic vasculitis following chronic infection by mouse hepatitis virus 3 (MHV 3) (1982) Acta Neuropathol, 58, pp. 168-176; Johnson, R.T., Mims, C.A., Pathogenesis of viral infections of the nervous system (1968) N Engl J Med, 278, pp. 23-30; Johnson, R.T., Pathophysiology and epidemiology of acute viral infections of the nervous system (1974) Adv Neurol, 6, pp. 27-40; Johnson, R.T., (1982) Viral Infections of the Nervous System, , New York: Raven Press; Barthold, S.W., Smith, A.L., Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice (1984) Arch Virol, 81, pp. 103-112; Furuta, T., Goto, Y., Tamura, T., Kai, C., Ueda, K., Pulmonary vascular lesions in nude mice persistently infected with mouse hepatitis virus (1979) Jpn J Exp Med, 49, pp. 423-428; Virelizier, J.L., Dayan, A.D., Allison, A.C., Neuropathological effects of persistent infection of mice by mouse hepatitis virus (1975) Infect Immun, 12, pp. 1127-1140; Joseph, J., Knobler, R.L., Lublin, F.D., Hart, M.N., Differential modulation of MHC class I antigen expression on mouse brain endothelial cells by MHV-4 infection (1989) J Neuroimmunol, 22, pp. 241-253; Fleming, J.O., El-Zaatari, F., Gilmore, W., Berne, J.D., Burks, J.S., Stohlman, S.A., Tourtellotte, W.W., Weiner, L.P., Antigenic assessment of coronaviruses isolated from patients with multiple sclerosis (1988) Arch Neurol, 45, pp. 629-633; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of Coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3' end of the viral mRNA leader sequence (1985) Virol, 53, pp. 834-840; Feinberg, A.P., Vogelstein, B., A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity (1983) Anal Biochem, 132, pp. 6-13","Cabirac, G.F.; Rocky Mountain MS Center, Department 7500LB, 501 East Hampden Avenue, Englewood, CO 80110, United States",,,08824010,,,"7815918","English","Microb. Pathog.",Article,"Final",Open Access,Scopus,2-s2.0-0028124964
"Greiff L., Andersson M., Akerlund A., Wollmer P., Svensson C., Alkner U., Persson C.G.A.","7006426396;7402879512;6701441885;7005123476;7202512750;6604092201;35493943900;","Microvascular exudative hyperresponsiveness in human coronavirus-induced common cold",1994,"Thorax","49","2",,"121","127",,25,"10.1136/thx.49.2.121","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028209479&doi=10.1136%2fthx.49.2.121&partnerID=40&md5=a7f12fa94c0e75610a90b33a72773ff8","Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden","Greiff, L., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Andersson, M., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Akerlund, A., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Wollmer, P., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Svensson, C., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Alkner, U., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden; Persson, C.G.A., Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden","Background - The inflammatory response of the airway microcirculation in rhinitis and asthma may be recorded as luminal entry of plasma macromolecules (mucosal exudation). This study examines the exudative responsiveness of the subepithelial microvessels in subjects with and without common cold after inoculation with coronavirus. Methods - The airway mucosa was exposed to exudative concentrations of histamine (40 and 400 μg/ml) before and six days after inoculation. To assess whether mucosal penetration of a topically applied agent was altered, nasal absorption of chromium-51 labelled ethylene diamine tetraacetic acid (51Cr-EDTA, MW 372) was also examined. A nasal pool technique kept the challenge and tracer solutes in contact with the same ipsilateral mucosal surface. Concentrations of albumin in lavage fluids were measured as an index of mucosal exudation of plasma. Nasal absorption of 51Cr-EDTA was determined by the cumulated 24 hour urinary excretion of radioactivity. Results - Nine subjects developed common cold after coronavirus inoculation and 10 remained healthy. Histamine produced concentration dependent mucosal exudation of plasma in all subjects before and after coronavirus inoculation. In subjects with common cold, however, the histamine-induced mucosal exudation was significantly augmented compared with the group without common cold. This exudative hyperresponsiveness is not explained by an increased baseline exudation because the lavage regimen used produced comparably low baseline exudation in both groups of subjects, nor is it explained by an increased penetration of topical histamine because the ability of the nasal mucosa to absorb 51Cr-EDTA was not significantly increased in the subjects with common cold. Conclusions - An increased proclivity of the airway subepithelial microcirculation to respond with plasma exudation develops during coronavirus-induced common cold. This specific exudative hyperresponsiveness may be a feature of inflammatory airway diseases.",,"albumin; chromium 51; edetate chromium cr 51; histamine; adult; article; bronchus hyperreactivity; clinical article; common cold; controlled study; Coronavirus; exudate; human; inflammation; intranasal drug administration; lung lavage; male; microcirculation; priority journal; topical drug administration",,"Greiff, L.; Department of Otorhinolaryngology, Lund University Hospital, S-221 85 Lund, Sweden",,"BMJ Publishing Group",00406376,,THORA,"8128400","English","THORAX",Article,"Final",Open Access,Scopus,2-s2.0-0028209479
"Delmas B., Gelfi J., Sjostrom H., Noren O., Laude H.","7003294168;8769591600;7005649072;7006675786;7006652624;","Further characterization of aminopeptidase-N as a receptor for coronaviruses",1994,"Advances in Experimental Medicine and Biology","342",,,"293","298",,65,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028258321&partnerID=40&md5=3e29e8125870e701b0bd6ac1d8530fef","Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France","Delmas, B., Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France; Gelfi, J., Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France; Sjostrom, H., Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France; Noren, O., Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France; Laude, H., Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France","We recently reported that porcine aminopeptidase-N (pAPN) acts as a receptor for transmissible gastroenteritis virus (TGEV). In the present work, we addressed the question of whether TGEV tropism is determined only by the virus-receptor interaction. To this end, different non-permissive cell lines were transfected with the porcine APN cDNA and tested for their susceptibility to TGEV infection. The four transfected cell lines shown to express pAPN at their membrane became sensitive to infection. Two of these cell lines were found to be defective for the production of viral particles. This suggests that other factor(s) than pAPN expression may be involved in the production of infectious virions. The pAPN-transfected cells were also tested for their susceptibility to several viruses which have a close antigenic relationship to TGEV. So far, we failed to evidence permissivity to the feline infectious peritonitis coronavirus FIPV and canine coronavirus CCV. In contrast, we found clear evidence that porcine respiratory coronavirus PRCV, a variant of TGEV which replicates efficiently in the respiratory tract but to a very low extent in the gut, may also utilise APN to gain entry into the host cells. This suggests that the switch between TGEV and PRCV tropisms in vivo may involve other determinant(s) than receptor recognition.",,"microsomal aminopeptidase; virus receptor; animal cell; cell strain bhk; conference paper; controlled study; coronavirus; dog; gene expression; infection sensitivity; nonhuman; priority journal; vero cell; virion; virus cell interaction; virus infection; virus particle; virus replication; virus transmission; Aminopeptidases; Animal; Antigens, CD13; Cell Line; Comparative Study; Coronavirus; Coronavirus, Canine; Coronavirus, Feline; Dogs; Hamsters; Membrane Glycoproteins; Membrane Proteins; Receptors, Virus; Recombinant Fusion Proteins; Species Specificity; Support, Non-U.S. Gov't; Swine; Transfection; Transmissible gastroenteritis virus; Vero Cells; Viral Envelope Proteins",,"Delmas, B.; Unite de Virol./Immunol. Molec., Institut Natl. de la Recher. Agron., 78352 Jouy-en-Josas, France",,,00652598,,AEMBA,"7911642","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028258321
"Reed A.P., Klepfer S., Miller T., Jones E.","7202692665;6507963520;57198615518;7404237166;","Cloning and sequence analysis of the spike gene from several feline coronaviruses",1994,"Advances in Experimental Medicine and Biology","342",,,"17","21",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028204242&partnerID=40&md5=dffbaaa4451f06f0ef3eeb0c5108e9b4","Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States","Reed, A.P., Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States; Klepfer, S., Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States; Miller, T., Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States; Jones, E., Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States","The DNA sequence encoding the spike gene from the DF2 strain of Type II feline infectious peritonitis virus (FIPV), a temperature sensitive FIPV virus (TS-DF2) and an isolate of feline enteric coronavirus (FECV 1683) were determined. Comparison of the published WSU 1146 and DF2 FIPV S genes showed that the viruses shared a high degree of homology (99.6%). Likewise, the S gene of the virulent DF2 FIPV virus was closely conserved to that isolated from the vaccine virus strain, TS-DF2 FIPV. In contrast, the FECV S gene had numerous DNA and amino acid differences when compared to the virulent FIPV sequences. Sequence differences among the feline coronavirus isolates were localized to the amino-terminus region of the S gene.",,"virus dna; virus protein; amino terminal sequence; cat; conference paper; coronavirus; dna sequence; molecular cloning; nonhuman; priority journal; sequence homology; virus gene; Amino Acid Sequence; Cloning, Molecular; Comparative Study; Coronavirus; Coronavirus, Feline; Genes, Structural, Viral; Membrane Glycoproteins; Molecular Sequence Data; Sequence Alignment; Sequence Homology; Species Specificity; Viral Envelope Proteins",,"Reed, A.P.; Department of Molecular Biology, SmithKline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA 19406-0939, United States",,,00652598,,AEMBA,"8209725","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028204242
"Vaughn E.M., Halbur P.G., Paul P.S.","7007145803;7005935318;7202714004;","Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions",1994,"Journal of Clinical Microbiology","32","7",,"1809","1812",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028245001&partnerID=40&md5=6a2a5cd9d374b91160aab525f2d6eb67","Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States","Vaughn, E.M., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States; Halbur, P.G., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States; Paul, P.S., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States","Three new isolates of porcine respiratory coronavirus (PRCV) were isolated and partially characterized. These PRCV isolates showed a selective tropism for respiratory tissue and were antigenically related to transmissible gastroenteritis virus. PCR amplification of the 5' half of the spike (S) genes of the three PRCV isolates indicated that a large deletion, characteristic of PRCV, was present. By using cDNA probes specific for the transmissible gastroenteritis virus S gene, the PCR products were shown to be specific in a Southern blot. The three new PRCV isolates were shown to vary in S gene deletion size. In a separate study, these isolates have also been shown to vary in pathogenicity. These new PRCV isolates should serve as important tools in gaining a better understanding of the pathogenesis of coronavirus infections.",,"dna polymerase; antigenicity; coronavirus; dna probe; gastroenteritis; gene amplification; gene deletion; note; pathogenicity; polymerase chain reaction; priority journal; southern blotting; virus infection; virus isolation; Animal; Base Sequence; Coronavirus; Coronavirus Infections; Gene Deletion; Membrane Glycoproteins; Molecular Sequence Data; Polymerase Chain Reaction; Species Specificity; Support, Non-U.S. Gov't; Swine; Swine Diseases; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Paul, P.S.; Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States",,,00951137,,JCMID,"7929779","English","J. CLIN. MICROBIOL.",Note,"Final",,Scopus,2-s2.0-0028245001
"Brian D.A., Chang R.Y., Hofmann M.A., Sethna P.B.","7006460232;36725275000;57203181972;7003358474;","Role of subgenomic minus-strand RNA in coronavirus replication.",1994,"Archives of virology. Supplementum","9",,,"173","180",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028313178&partnerID=40&md5=41bcfbd882bbe1f74ceabb1bccd21ed3","Department of Microbiology, University of Tennessee, Knoxville, United States","Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, United States; Chang, R.Y., Department of Microbiology, University of Tennessee, Knoxville, United States; Hofmann, M.A., Department of Microbiology, University of Tennessee, Knoxville, United States; Sethna, P.B., Department of Microbiology, University of Tennessee, Knoxville, United States","Coronavirus subgenomic minus-strand RNAs (negative-strand copies of the 3' coterminal subgenomic mRNAs) probably function in mRNA amplification by serving as templates for transcription from internal (intergenic) promoters, rather than by faithful (full-length) mRNA replication.",,"messenger RNA; virus RNA; article; biological model; cell culture; Coronavirus; defective virus; genetic transcription; genetics; growth, development and aging; metabolism; molecular genetics; nucleotide sequence; promoter region; virus replication; Base Sequence; Cells, Cultured; Coronavirus, Bovine; Defective Viruses; Models, Genetic; Molecular Sequence Data; Promoter Regions (Genetics); RNA, Messenger; RNA, Viral; Transcription, Genetic; Virus Replication",,"Brian, D.A.",,,09391983,,,"8032248","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028313178
"Brim T.A., VanCott J.L., Lunney J.K., Saif L.J.","6602281848;6603878315;7005634527;7102226747;","Lymphocyte proliferation responses of pigs inoculated with transmissible gastroenteritis virus or porcine respiratory coronavirus.",1994,"American journal of veterinary research","55","4",,"494","501",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028417669&partnerID=40&md5=f8c6fc74b1bf1e0de617e700bc62fd64","Department of Veterinary Preventive Medicine, Ohio State University, Wooster, 44691-4096., United States","Brim, T.A., Department of Veterinary Preventive Medicine, Ohio State University, Wooster, 44691-4096., United States; VanCott, J.L., Department of Veterinary Preventive Medicine, Ohio State University, Wooster, 44691-4096., United States; Lunney, J.K., Department of Veterinary Preventive Medicine, Ohio State University, Wooster, 44691-4096., United States; Saif, L.J., Department of Veterinary Preventive Medicine, Ohio State University, Wooster, 44691-4096., United States","Cell-mediated immunity was evaluated in intestinal, respiratory, and systemic lymphoid tissues of pigs exposed when 11 days old to virulent transmissible gastroenteritis virus (TGEV), attenuated TGEV, or porcine respiratory coronavirus (PRCV), 3 antigenically related porcine coronaviruses with distinct enteric and respiratory tissue tropisms. Mononuclear cells were prepared from mesenteric lymph nodes (MLN), bronchial lymph nodes (BLN), and spleens of pigs and tested for virus-specific responses by use of lymphocyte proliferation assays. Vigorous MLN and BLN proliferation responses to virulent TGEV and PRCV, respectively, at postinoculation days 8 to 24 were strongly associated with prior detection of TGEV in rectal swab samples and PRCV in nasal swab samples. Gastrointestinal disease and intestinal virus replication, assessed on the basis of rectal virus shedding, were almost exclusively found in the virulent TGEV-inoculated pigs, even though virulent TGEV and a high dose of attenuated TGEV elicited the highest proliferation responses in MLN. Pigs exposed to PRCV or attenuated TGEV did not have clinical signs of disease, and only 1 pig given a high dose of attenuated TGEV shed virus in feces. Porcine respiratory coronavirus replicated in the respiratory tract after either oronasal or aerosol inoculation of virus and induced strong BLN, but not MLN, proliferation responses. A high dose of attenuated TGEV (4 x 10(8) plaque-forming units) was more effective than a lower dose of attenuated TGEV (7 x 10(6) plaque-forming units) in eliciting significant lymphocyte proliferation in MLN and BLN.(ABSTRACT TRUNCATED AT 250 WORDS)",,"phytohemagglutinin; virus antibody; animal; animal disease; article; blood; cell culture; cellular immunity; Coronavirus; immunology; lymphocyte; lymphocyte activation; microbiology; serodiagnosis; swine; swine disease; Transmissible gastroenteritis virus; virus infection; Animals; Antibodies, Viral; Cells, Cultured; Coronaviridae; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Immunity, Cellular; Lymphocyte Activation; Lymphocytes; Neutralization Tests; Phytohemagglutinins; Swine; Swine Diseases; Transmissible gastroenteritis virus",,"Brim, T.A.",,,00029645,,,"8017695","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028417669
"Vennema H., Rossen J.W.A., Wesseling J., Horzinek M.C., Rottier P.J.M.","7003697291;7005977394;57214985161;7102624836;7006145490;","Genomic organization and expression of the 3' end of the canine and feline enteric coronaviruses",1994,"Advances in Experimental Medicine and Biology","342",,,"11","16",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028293987&partnerID=40&md5=3ea43042101b94819400fa8ca198c93b","Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands","Vennema, H., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Rossen, J.W.A., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Wesseling, J., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Horzinek, M.C., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Rottier, P.J.M., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands","The genomic organization at the 3' end of canine coronavirus (CCV) and feline enteric coronavirus (FECV) was determined by sequence analysis and compared to that of feline infectious peritonitis virus (FIPV) and transmissible gastroenteritis virus (TGEV) of swine. Comparison of the latter two has previously revealed an extra open reading frame (ORF) at the 3' end of the FIPV genome, lacking in TGEV, now designated ORF 6b. Both CCV and FECV possess 6b-related ORFs. The CCV ORF 6b is colinear with that of FIPV, but the predicted amino acid sequences are only 58% identical. The FECV ORF 6b contains a large deletion compared to that of FIPV, reducing the colinear part to 60%. The sequence homologies were highest between CCV and TGEV on the one hand and between FECV and FIPV on the other. The expression product of the CCV and the FECV ORF 6b can be detected in infected cells by immunoprecipitation.",,"complementary dna; virus protein; amino acid sequence; cat; conference paper; coronavirus; dog; gene deletion; immunoprecipitation; nonhuman; nucleotide sequence; open reading frame; priority journal; sequence homology; swine disease; virus genome; Animal; Base Sequence; Cats; Cells, Cultured; Comparative Study; Coronavirus; Coronavirus, Canine; Coronavirus, Feline; Genome, Viral; Hela Cells; Human; Molecular Sequence Data; Polymerase Chain Reaction; Transmissible gastroenteritis virus; Viral Nonstructural Proteins",,"Vennema, H.; Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands",,,00652598,,AEMBA,"8209715","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028293987
"Zhang X.M., Herbst W., Kousoulas K.G., Storz J.","55715175900;16161781000;7003476092;7006694594;","Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child",1994,"Journal of Medical Virology","44","2",,"152","161",,67,"10.1002/jmv.1890440207","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028097306&doi=10.1002%2fjmv.1890440207&partnerID=40&md5=afb1c333e6205c41cac52601b3eae41c","Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig University Giessen, Giessen, Germany","Zhang, X.M., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Herbst, W., Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig University Giessen, Giessen, Germany; Kousoulas, K.G., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Storz, J., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States","The coronavirus strain HECV‐4408 was isolated from diarrhea fluid of a 6‐year‐old child with acute diarrhea and propagated in human rectal tumor (HRT‐18) cells. Electron microscopy revealed coronavirus particles in the diarrhea fluid sample and the infected HRT‐18 cell cultures. This virus possessed hemagglutinating and acetylesterase activities and caused cytopathic effects in HRT‐18 cells but not in MDBK, GBK and FE cells. One of four S‐specific monoclonal antibodies reacted in Western blots with HECV‐4408, BCV‐L9 and BCV‐LY138 but not with HCV‐OC43, and two reacted with BCV‐L9 but not with HECV‐4408, BCV‐LY138 and HCV‐OC43. One S‐specific and two N‐specific monoclonal antibodies reacted with all of these strains. cDNA encompassing the 3′ 8.5 kb of the viral RNA genome was isolated by reverse transcription followed by polymerase chain reaction amplification had size and restriction endonuclease patterns similar to those of BCV‐L9 and BCV‐LY138. In contrast, the M gene of HCV‐OC43 differed in restriction patterns from HECV‐4408 and BCV. A genomic deletion located between the S and M within the nonstructural genes of HCV‐OC43 was not detected in HECV‐4408. DNA sequence analyses of the S and HE genes revealed more than 99% nucleotide and deduced amino acid homologies between HECV‐4408 and the virulent wild‐type BCV. Forty‐nine nucleotide and 22 amino acid differences were found between the HE genes of HECV‐4408 and HCV‐OC43, while only 16 nucleotide and 3 amino acid differences occurred between the HE genes of HECV‐4408 and BCVLY138. We thus conclude that the strain HECV‐4408 is a hemagglutinating enteric coronavirus that is biologically, antigenically and genomically more closely related to the virulent BCVLY138 than to HCV‐OC43. © 1994 Wiley‐Liss, Inc. Copyright © 1994 Wiley‐Liss, Inc., A Wiley Company","antigenic and nucleotide sequence comparisions; cytopathogenicity; enteritis; human and bovine HA coronaviruses","virus antigen; antigenicity; article; case report; child; coronavirus; diarrhea; hemagglutination; human; human cell; male; nucleotide sequence; ultrastructure; united kingdom; virus isolation; virus strain; Acetylesterase; Amino Acid Sequence; Antigens, Viral; Base Sequence; Case Report; Child; Coronavirus; Coronavirus Infections; Coronavirus OC43, Human; Cytopathogenic Effect, Viral; Diarrhea; DNA Primers; DNA, Viral; Hemagglutinins, Viral; Human; Male; Microscopy, Electron; Molecular Sequence Data; Polymerase Chain Reaction; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Bovinae; Bovine coronavirus; Coronavirus; Enteric coronavirus; Hepatitis C virus","Battaglia, M, Passarani, N, Di, MA, Gerna, G, Human enteric coronaviruses: Further characterization and immunoblotting of viral proteins (1987) Journal of Infectious Diseases, 155, pp. 140-143; Cavanagh, D, Brian, DA, Enjuanes, L, Holmes, KV, Lai, MM, Laude, H, Siddell, SG, Talbot, PJ, Recommendations of the coronavirus study group for the nomenclature of the structural proteins, mRNAs, and genes of coronaviruses (1990) Virology, 176, pp. 306-307; Cereda, PM, Pagani, L, Romero, E, Prevalence of antibody to human coronaviruses 229E, OC43 and neonatal calf diarrhea coronavirus (NCDCV) in patients of Northern Italy (1986) European Journal of Epidemiology, 2, pp. 112-117; Cohen, GH, Osola, VJ, Kuhns, J, Berman, PW, Eisenberg, RJ, Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: Use of a nondenaturing (“Native” Gel) system of polyacrylamide gel electrophoresis coupled with Western blotting (1985) Journal of Virology, 60, pp. 157-166; Dea, S, Verbeek, AJ, Tijssen, P, Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) Journal of Virology, 64, pp. 3112-3118; Debiaggi, M, Luini, M, Cereda, PM, Perduca, M, Romero, E, Serum inhibitor of coronaviruses OC43 and NCDCV: A study in vivo (1986) Microbiologica, 9, pp. 33-37; 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Huang, YN, Finding of coronavirus particles in the feces of patients with diarrhea (1987) Chung Hua Liu Hsing Pin Hsueh Tsa Chih, 8, pp. 25-27; Hussain, K, Storz, J, Kousoulas, KG, Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to glycoprotein gp100 distinguish between vaccine and wild‐type strains (1991) Virology, 183, pp. 442-445; Imagawa, H, Fukunaga, Y, Kamada, M, Detection of neutralizing antibody against calf diarrheal coronavirus in horse serum (1990) Bulletin of Equine Research Institute, 27, pp. 25-30; Kamahora, T, Soe, LH, Lai, MM, Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Research, 12, pp. 1-9; Kidd, AH, Esrey, SA, Ujfalusi, MJ, Shedding of coronavirus‐like particles by children in Lesotho (1989) Journal of Medical Virology, 27, pp. 164-169; Laemmli, UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Laporte, J, L'Haridon, R, Bobulesco, P, In vitro culture of bovine enteritic coronaviruses (BEC) (1979) INSERM, 90, pp. 99-102; 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Archives of Virology, 70, pp. 301-313; Marshall, JA, Thompson, WL, Gust, ID, Coronavirus‐like particles in adults in Melbourne, Australia (1989) Journal of Medical Virology, 29, pp. 238-243; Mathan, M, Mathan, VI, Swaminathan, SP, Yesudoss, S, Baker, SJ, Pleomophic virus‐like particles in human feces (1975) Lancet, 1, pp. 1068-1089; Mortensen, ML, Ray, CG, Payne, CM, Friedman, AD, Minnich, IL, Rousseau, C, Coronavirus‐like particles in human gastrointestinal disease (1985) Epidemiological, clinical, and laboratory observations. 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Archives of Virology, 87, pp. 331-337; Schnagl, RD, Brookes, S, Medvedec, S, Morey, F, Characteristics of Australian human enteric coronavirus‐like particles: Comparison with human respiratory coronavirus 229E and duodenal brush border vesicles (1987) Archives of Virology, 97, pp. 309-323; Schnagl, RD, Foti, R, Brookes, S, Bucens, M, Serum antibodies to human enteric coronavirus‐like particles in Australia, South Africa, Indonesia, Niue, and Papua New Guinea (1990) Acta Virologica (Praha), 34, pp. 239-345; Schultze, S, Gross, HJ, Brossmer, R, Herrler, G, The S protein of bovine coronavirus is a hemagglutinin recognizing 9‐0‐acetylated sialic acid as a receptor determinant (1991) Journal of Virology, 6, pp. 6232-6237; Singh, PB, Sreenivasan, MA, Pavri, KM, Viruses in acute gastroenteritis in children in Pune, India (1989) Epidemiology and Infection, 102, pp. 345-353; Sitbon, M, Human‐enteric‐coronaviruslike particles (CVLP) with different epidemiological characteristics (1985) Journal of Medical Virology, 16, pp. 67-76; Spaan, W, Cavanagh, D, Horzinek, MC, Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2953; St. Cyr‐Coats, K, Storz, J, Bovine coronavirus‐induced cytopathic expression and plaque formation: Host cell and virus strain determine trypsin dependence (1988) Journal of Veterinary Medicine, 35 B, pp. 48-56; St. Cyr‐Coats, K, Storz, J, Hussain, KA, Schnorr, KL, Structural proteins of bovine coronavirus strain L9: Effects of the host cell and trypsin treatment (1988) Archives of Virology, 103, pp. 35-43; Storz, J, Rott, R, Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Medical Microbiology and Immunology, 169, pp. 169-178; Storz, J, Zhang, XM, Rott, R, Comparison of hemagglutinating, receptor‐destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Archives of Virology, 125, pp. 193-204; Sturman, LS, Ricard, CS, Holmes, KV, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell‐fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) Journal of Virology, 56, pp. 904-911; Tompkins, WAF, Watrach, AM, Schmale, JD, Schultz, RM, Harris, JA, Cultural and antigenic properties of newly established cell strains from adenocarcinomas of human colon and rectum (1974) Journal of National Cancer Institute, 52, pp. 101-106; Vlasak, R, Luytjes, W, Spaan, W, Palese, P, Human and bovine coronaviruses recognize sialic acid‐containing receptors similar to those of influenza C viruses (1988) Proceeding of National Academy of Science USA, 85, pp. 4526-4529; Yeager, CL, Ashmun, RA, Williams, RK, Cardellichio, CB, Shipiro, LH, Look, AT, Holmes, KV, Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature (London), 357, pp. 420-422; Zhang, XM, Schliesser, T, Lange, H, Herbst, W, Zum Nachweis von Antikörpern gegen Influenza‐A‐Viren (H1N1, H3N2) beim Schwein mit dem Single Radial Hämolyse (SRH)‐und dem Hamagglutinationshemmungs (HAH)‐Test (1988) Journal of Veterinary Medicine, 35 B, pp. 57-63; Zhang, XM, Kousoulas, KG, Storz, J, Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Zhang, XM, Kousoulas, KG, Storz, J, The hemagglutinin/esterae glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852; Zhang, XM, Kousoulas, KG, Storz, J, The hemagglutin/esterase gene of human coronavirus strain OC43: Phylogenetic relationships to bovine and murine coronaviruses and influenza C virus (1992) Virology, 186, pp. 318-323","Zhang, X.M.; Department of Microbiology, University of Southern California School of Medicine, 2011 Zonal Avenue HMR-504, Los Angeles, California, 90033, United States",,,01466615,,,"7852955","English","J. Med. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0028097306
"Cavanagh D., Brian D.A., Brinton M.A., Enjuanes L., Holmes K.V., Horzinek M.C., Lai M.M.C., Laude H., Plagemann P.G.W., Siddell S.G., Spaan W.J.M., Taguchi F., Talbot P.J.","26642890500;7006460232;7004849890;7006565392;7201657724;7102624836;7401808497;7006652624;7102193015;7005260816;7007172944;7103209890;7102670281;","The Coronaviridae now comprises two genera, coronavirus and torovirus: Report of the Coronaviridae study group",1994,"Advances in Experimental Medicine and Biology","342",,,"255","257",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028330820&partnerID=40&md5=a008c7594cb1add8c5a05641e974401a","Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom","Cavanagh, D., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Brian, D.A., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Brinton, M.A., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Enjuanes, L., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Holmes, K.V., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Horzinek, M.C., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Lai, M.M.C., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Laude, H., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Plagemann, P.G.W., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Siddell, S.G., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Spaan, W.J.M., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Taguchi, F., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom; Talbot, P.J., Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom","At the April 1992, mid-term meeting of the International Committee on Taxonomy of Viruses (ICTV) a proposal from the Coronaviridae Study Group (CSG) to include the torovirus genus in the Coronaviridae was accepted. Following another proposal, the arterivirus genus was removed from the Togaviridae but not assigned to another family. The arteriviruses have some features in common with the Coronaviridae but also have major differences. After much debate, culminating in September 1992, it was decided that the CSG would not recommend inclusion of arterivirus in the Coronaviridae. It was agreed that (a) the nomenclature used for coronavirus genes, mRNAs and polypeptides (Cavanagh et al., 1990) should be used for toroviruses, (b) that the small (about 100 amino acids) membrane-associated protein, which is distinct from the integral membrane glycoprotein M, associated with virions of infectious bronchitis (Liu and Inglis, 1991) and transmissible gastroenteritis (Godet et al., 1992) coronaviruses would be referred to by the acronym sM (lower case 's') and (c) that 'pol' (polymerase) should be used as a working term for gene 1, which comprises open reading frames (ORFs) 1a and 1b in both genera of the Coronaviridae.",,"messenger rna; virus glycoprotein; virus rna; avian infectious bronchitis virus; conference paper; coronavirus; equine viral arteritis virus; nonhuman; open reading frame; priority journal; rna virus; taxonomy; torovirus; virion; virology; virus envelope; virus gene; Arterivirus; Comparative Study; Coronaviridae; Coronavirus; Genome, Viral; Species Specificity; Togaviridae; Torovirus",,"Cavanagh, D.; Compton Laboratory, Division of Molecular Biology, AFRC Institute for Animal Health, Compton, Newbury RG16 0NN, United Kingdom",,,00652598,,AEMBA,"8209739","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028330820
"Oleszak E.L., Perlman S., Parr R., Collisson E.W., Leibowitz J.L.","6603665574;7102708317;7006656431;57194517102;7006843902;","Molecular mimicry between S peplomer proteins of coronaviruses (MHV, BCV, TGEV and IBV) and Fc receptor",1994,"Advances in Experimental Medicine and Biology","342",,,"183","188",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028330818&partnerID=40&md5=92bc5acd879f25b36f02bb3e9c054b56","Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States","Oleszak, E.L., Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States; Perlman, S., Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States; Parr, R., Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States; Collisson, E.W., Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States; Leibowitz, J.L., Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States","In previous studies we have demonstrated molecular mimicry between the S peplomer protein of Mouse Hepatitis Virus (MHV) and Fcγ Receptor (FcγR) of IgG. Rabbit IgG, but not its F(ab')2 fragments, monoclonal rat and mouse IgG and the rat 2.4G2 anti-mouse FcγR monoclonal antibody (mab) immunoprecipitated natural and recombinant MHV S protein. On the basis of a number of criteria, MHV S peplomer protein exhibits Fc IgG binding ability. We report here a molecular mimicry between the S peplomer protein of Bovine Coronavirus (BCV) and FcγR. BCV S peplomer protein which belongs to the same antigenic subgroup as MHV also binds Fc portion of rabbit IgG and is immunoprecipitated by the 2.4G2 anti-FcγR mab. In contrast, Transmissible Gastroenteritis Coronavirus (TGEV) and Infectious Bronchitis Virus (IBV) S peplomer proteins which represent two distinct antigenic subgroups of Coronaviridae do not bind rabbit IgG and do not react with anti-FcγR mab. However, homologous swine IgG, but not its F(ab')2 fragments, immunoprecipitated from TGEV-infected cells a polypeptide chain with molecular mass of 195 kDa, identical to that immunoprecipitated by the T36 mab anti-TGEV S peplomer protein.",,"immunoglobulin f(ab) fragment; immunoglobulin g; virus protein; animal cell; avian infectious bronchitis virus; conference paper; cross reaction; enteric virus; immunoprecipitation; molecular genetics; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; rat; Animal; Antibodies, Monoclonal; Comparative Study; Coronavirus; Coronavirus, Bovine; Immunoglobulin G; Immunoglobulins, Fab; Infectious bronchitis virus; Membrane Glycoproteins; Mice; Murine hepatitis virus; Protein Binding; Rabbits; Rats; Receptors, IgG; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Oleszak, E.L.; Pathology/Laboratory Medicine Dept., Medical School, Texas University Health Science Ctr., Houston, TX, United States",,,00652598,,AEMBA,"8209728","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028330818
"Schultze B., Herrler G.","7006104520;7006339246;","Recognition of N-acetyl-9-O-acetylneuraminic acid by bovine coronavirus and hemagglutinating encephalomyelitis virus",1994,"Advances in Experimental Medicine and Biology","342",,,"299","304",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028295915&partnerID=40&md5=a881fd85651c524ef22dc8da061ba718","Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 3550 Marburg, Germany","Schultze, B., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 3550 Marburg, Germany; Herrler, G., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 3550 Marburg, Germany","The S protein of hemagglutinating encephalomyelitis virus is shown to be a hemagglutinin requiring N-acetyl-9-O-acetylneuraminic acid as a receptor determinant on the surface of erythrocytes. The ability of bovine coronavirus to recognize 9-O-acetylated sialic acid was used to establish a binding assay for the detection of glycoproteins containing this type of sugar. The assay is very fast, because it uses the acetylesterase of the viral HE protein to localize bound virus.",,"acetylesterase; hemagglutinin; n acetylneuraminic acid derivative; sialic acid derivative; virus glycoprotein; virus receptor; vitronectin; animal cell; cell strain; chicken; conference paper; controlled study; coronavirus; erythrocyte membrane; mouse; murine encephalomyelitis virus; newborn; nonhuman; priority journal; rat; virus adsorption; virus hemagglutination; Animal; Biological Assay; Blood Proteins; Cattle; Cell Line; Chickens; Coronavirus; Coronavirus, Bovine; Dogs; Glycoproteins; Hemagglutination Tests; Hemagglutinins, Viral; Membrane Glycoproteins; Protein Binding; Rats; Receptors, Virus; Sialic Acids; Support, Non-U.S. Gov't; Viral Envelope Proteins; Viral Proteins",,"Schultze, B.; Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 3550 Marburg, Germany",,,00652598,,AEMBA,"8209746","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028295915
"Tennant B.J., Gaskell R.M., Gaskell C.J.","7006083896;7005702877;7005318395;","Studies on the survival of canine coronavirus under different environmental conditions",1994,"Veterinary Microbiology","42","2-3",,"255","259",,17,"10.1016/0378-1135(94)90024-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028037428&doi=10.1016%2f0378-1135%2894%2990024-8&partnerID=40&md5=e670eabf6f5b06d25cac823e95628810","Department of Veterinary Clinical Science, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom; Department of Veterinary Pathology, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom","Tennant, B.J., Department of Veterinary Clinical Science, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom; Gaskell, R.M., Department of Veterinary Pathology, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom; Gaskell, C.J., Department of Veterinary Clinical Science, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom","Canine coronavirus (CCV) is a common faecal agent which is difficult to isolate. This study shows CCV to survive well at temperatures below -20°C but not at temperatures above 4°C. The presence of faecal material markedly reduced CCV survival times at temperatures ranging from 20°C to -70°C. Thus, it is suggested that diagnostic faecal material should be diluted 1:10 (w/v) with growth medium and examined at the earliest opportunity. © 1994.","Canine coronavirus; Diagnosis, Canine coronavirus; Faeces","article; controlled study; coronavirus; diagnostic accuracy; dog; environmental factor; feces analysis; nonhuman; survival; temperature; virus infection; Animal; Coronavirus Infections; Coronavirus, Canine; Culture Media; Dog Diseases; Dogs; Feces; Support, Non-U.S. Gov't; Temperature; Time Factors; Virology; Canine coronavirus; Canis familiaris; Coronavirus","Binn, Lazar, Keenan, Huxsoll, Marchwicki, Strano, Recovery and characterization of a coronavirus from military dogs with diarrhoea (1974) Proc. 78th Meet. U.S. Anim. Health Assoc., pp. 359-366; Carmichael, Binn, New Enteric Viruses in the Dog (1981) Adv., Vet. Sci. Comp. Med., 25, pp. 1-37; McIntosh, Coronaviruses: A Comparative review (1974) Curr. Top. Microbiol. Immunol., 63, pp. 86-129; Pensaert, Callebaut, The coronaviruses: Clinical and structural aspects with some practical implications (1978) Ann. Med. Vet., 122, pp. 301-322; Siddell, Wege, ter Meulen, Review article. The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Stoddart, Some studies on the pathogenesis of feline infectious peritonitis (1985) PhD Thesis, , University of Bristol; Tennant, Gaskell, Jones, Gaskell, Prevalence of antibodies to four major canine viral diseases in dogs in a Liverpool hospital population (1991) Journal of Small Animal Practice, 32, pp. 175-179; Tennant, Gaskell, Kelly, Carter, Gaskell, Canine coronavirus infection in the dog following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18","Tennant, B.J.; Department of Veterinary Clinical Science, Faculty of Veterinary Science, The University of Liverpool, PO Box 147, Liverpool, L69 3BX, United Kingdom",,,03781135,,VMICD,"7886936","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0028037428
"Baker S.C., Gao H., Baric R.S.","7403307881;57215705726;7004350435;","Altered proteolytic processing of the polymerase polyprotein in RNA(-) temperature sensitive mutants of murine coronavirus",1994,"Advances in Experimental Medicine and Biology","342",,,"215","219",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028218974&partnerID=40&md5=6ce8d0901f1f33be83decdcd2b926fc1","Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","Baker, S.C., Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Gao, H., Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Baric, R.S., Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","We examined the synthesis and processing of the polymerase polyprotein in RNA(-) temperature sensitive mutant of murine coronavirus strain A59. These temperature sensitive mutants of MHV-A59 synthesize viral RNA at the permissive temperature (33.0°C), but are unable to synthesize viral RNA at the nonpermissive temperature (39.5°C). The ts mutants have been mapped to five different complementation groups in the polymerase gene. The 5'-most complementation groups, Group A and B, map to a region encoding an autoproteinase responsible for the cleavage of p28, the amino-terminal product of the polymerase polyprotein. We screened six temperature sensitive mutants to determine if there was an alteration in the proteolytic processing of the polymerase polyprotein, particularly in the cleavage of the p28 protein. Two mutants, tsNC9 and tsLA16, had altered proteolytic products at both the permissive and nonpermissive temperatures. One Group B temperature sensitive mutant, designated tsNC11, was defective in the production of p28 protein at the nonpermissive temperature. To further localize the site of the mutation in tsNC11, RNA representing the 5'-most 5.3 kb region of the polymerase gene was transfected into tsNC11-infected cells and virus production monitored. The transfected RNA was able to complement the defect in tsNC11, resulting in viral RNA synthesis and production of viral particles at the nonpermissive temperature. These results indicate that a gene product from the 5.3 kb region of gene 1 is required for coronavirus RNA synthesis.",,"virus protein; virus rna; animal cell; conference paper; murine hepatitis coronavirus; nonhuman; priority journal; protein processing; rna synthesis; temperature sensitive mutant; virus mutation; Genetic Complementation Test; Murine hepatitis virus; Mutation; Protein Precursors; Protein Processing, Post-Translational; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Temperature; Transfection; Viral Proteins; Virus Replication",,"Baker, S.C.; Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States",,,00652598,,AEMBA,"8209733","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028218974
"Masters P.S., Koetzner C.A., Kerr C.A., Heo Y.","7006234572;6602982748;7202213986;36914406600;","Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus",1994,"Journal of Virology","68","1",,"328","337",,93,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028091057&partnerID=40&md5=df5a4b1afc7aa71883df7097db084372","New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States","Masters, P.S., New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States; Koetzner, C.A., New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States; Kerr, C.A., New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States; Heo, Y., New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States","We have recently described a method of introducing site-specific mutations into the genome of the coronavirus mouse hepatitis virus (MHV) by RNA recombination between cotransfected genomic RNA and a synthetic subgenomic mRNA (C. A. Koetzner, M. M. Parker, C. S. Ricard, L. S. Sturman, and P. S. Masters, J. Virol. 66:1841-1848, 1992). By using a thermolabile N protein mutant of MHV (Alb4) as the recipient virus and synthetic RNA7 (the mRNA for the nucleocapsid protein N) as the donor, we selected engineered recombinant viruses as heat-stable progeny resulting from cotransfection. We have now been able to greatly increase the efficiency of targeted recombination in this process by using a synthetic defective interfering (DI) RNA in place of RNA7. The frequency of recombination is sufficiently high that, with Alb4 as the recipient, recombinants can be directly identified without using thermal selection. The synthetic DI RNA has been used to demonstrate that the lesion in another temperature-sensitive and thermolabile MHV mutant, Alb1, maps to the N gene. Sequencing of the Alb1 N gene revealed two closely linked point mutations that fall in a region of the N molecule previously noted as being the most highly conserved region among all of the coronavirus N proteins. Analysis of revertants of the Alb1 mutant revealed that one of the two mutations is critical for the temperature-sensitive phenotype; the second mutation is phenotypically silent.",,"recombinant rna; animal cell; article; binding site; coronavirus; gene mapping; gene mutation; gene sequence; genetic transfection; hepatitis virus; mouse; nonhuman; point mutation; priority journal; target cell; virus nucleocapsid; Amino Acid Sequence; Animal; Base Sequence; Capsid; Chromosome Mapping; Clone Cells; Comparative Study; Defective Viruses; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutation; Recombination, Genetic; RNA, Viral; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Support, U.S. Gov't, P.H.S.; Viral Core Proteins; Viral Matrix Proteins",,"Masters, P.S.; New York State Department of Health, Wadsworth Center, Albany, NY 12201-0509, United States",,,0022538X,,JOVIA,"8254744","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028091057
"Martin‐Calvo M., Marcotegui M.A., Simarro I.","6507677556;6507074969;6602938097;","Canine‐coronavirus (CCV) Characterization in Spain Epidemiological Aspects",1994,"Journal of Veterinary Medicine, Series B","41","1-10",,"249","256",,1,"10.1111/j.1439-0450.1994.tb00225.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028459341&doi=10.1111%2fj.1439-0450.1994.tb00225.x&partnerID=40&md5=ba1b1a15b6f3457dc64c0568df3b170f","Dpto. Patalogia Animal I, Faculted de Veterinaria, Universidad Compultense, Spain","Martin‐Calvo, M., Dpto. Patalogia Animal I, Faculted de Veterinaria, Universidad Compultense, Spain; Marcotegui, M.A., Dpto. Patalogia Animal I, Faculted de Veterinaria, Universidad Compultense, Spain; Simarro, I., Dpto. Patalogia Animal I, Faculted de Veterinaria, Universidad Compultense, Spain","In this paper the characterization of a canine‐coronavirus (CCV) strain isolated in Spain is reported. The CCV cellular‐infection cycle on A‐72 cells was studied using electron‐microscopy techniques. The isolate was found to have similar electrophoretic profile and antigenic properties to an American reference strain. Sera samples were obtained from several canine populations and tested for viral antibodies using two immunoenzymatic methods. Sera specificity was confirmed using immunoblot analysis. The agreement between both ELISA tests produced adequate results (kappa value = 0.64). © 1994 Blackwell Verlag GmbH",,"virus antibody; animal; animal disease; article; blood; cell line; classification; Coronavirus; dog; dog disease; electron microscopy; immunology; Spain; ultrastructure; virology; virus infection; Animal; Antibodies, Viral; Cell Line; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Microscopy, Electron; Spain","Brian, D.A., Dennis, D.E., Guy, J.S., Genome of porcine‐transmissible gastroenteritis virus (1980) J. Virol, 34, pp. 410-415; Evermann, J.F., Update on canine coronavirus infections and interactions with other enteric pathogens of the dogs (1989) Can. Pract, 19, pp. 6-11; Garwes, D.J., Reynolds, D.J., The polypeptide structure of canine coronavirus and its relationship to porcine‐transmissible gastroenteritis virus (1981) J. Gen. Virol, 52, pp. 153-157; Helfer‐Baker, C., Evermann, J.F., McKeirnan, A.J., Morrison, W.B., Serological studies on the incidence of canine enteritis viruses (1980) Can. Pract, 7, pp. 37-42; Kojima, A., Takada, H., Okaniwa, H., Multiplication of canine coronavirus in CRFK cells (1986) Jpn. J. Vet. Sci., 48, pp. 1063-1070; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Martin‐Calvo, M.M., Marcotegui, M.A., Santurde, G., Miro, G., Simarro, I., Datos preliminares sobre coronavirus canino en España (1992) Med. Vet., 9, pp. 157-160; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhoea: propagation, attenuation and characteristics of a coronavirus‐like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H.A., Uytdehaag, F.G.C.M., Osterhaus, A.D.M.E., The use of enzyme‐linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in The Netherlands (1991) Vet. Microbiol, 26, pp. 25-40; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from gels to nitrocellulose sheets: procedure and some applications (1979) Proc. Natl. Acad. Sci. USA., 76, pp. 4350-4354","Martin‐Calvo, M.; Dpto Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, Avda, Puerta de Hierro s/n, Madrid, 28040, Spain",,,09311793,,,"7839745","English","Zentralbl. Veterinarmed. Reihe B",Article,"Final",Open Access,Scopus,2-s2.0-0028459341
"Mounir S., Labonte P., Talbot P.J.","6603891523;6507854410;7102670281;","Characterization of the nonstructural and spike proteins of the human respiratory coronavirus OC43: Comparison with bovine enteric coronavirus",1994,"Advances in Experimental Medicine and Biology","342",,,"61","67",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028204244&partnerID=40&md5=8ff510527c3af588c366f4705e6fa8f3","Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada","Mounir, S., Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada; Labonte, P., Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada; Talbot, P.J., Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada","The nucleotide sequence of the region between the spike (S) and the membrane (M) protein genes, and sequences of the S and ns2 genes of the OC43 strain of human coronavirus (HCV-OC43) were determined. The ns2 gene comprises an open reading frame (ORF) encoding a putative nonstructural (ns) protein of 279 amino acids with a predicted molecular mass of 32-kDa. The S gene comprises an ORF encoding a protein of 1353 amino acid residues, with a predicted molecular weight of 149,918. Sequence comparison between HCV-OC43 and the antigenically related bovine coronavirus (BCV) revealed more sequence divergence in the putative bulbous part of the S protein (S1) than in the stem region (S2). The cysteine residues near the transmembrane domain and the internal predicted protease cleavage site are conserved in the HCV-OC43 S protein. Nucleotide sequence analysis of the region between the S and M gene loci revealed the presence of an unexpected intragenomic partial leader sequence and two ORFs encoding potential proteins of 12.9 and 9.5-kDa. These two proteins were identified as nonstructural by comparison with the homologous BCV genes. In vitro translation analyses demonstrated that the HCV-OC43 9.5-kDa protein, like its BCV counterpart, is poorly translated when situated downstream of the 12.9-kDa ORF, but is expressed in infected cells, as shown by immunofluorescence. Interestingly, two ORFs, potentially encoding 4.9 and 4.8-kDa ns proteins in BCV are absent in HCV-OC43, indicating that they are not essential for viral replication in HRT-18 cells.",,"virus protein; virus rna; amino acid sequence; animal cell; cattle; conference paper; coronavirus; immunofluorescence; nonhuman; northern blotting; nucleotide sequence; open reading frame; priority journal; rna translation; virus replication; Amino Acid Sequence; Base Sequence; Comparative Study; Coronavirus; Coronavirus OC43, Human; Coronavirus, Bovine; Genes, Structural, Viral; Human; Membrane Glycoproteins; Molecular Sequence Data; Open Reading Frames; Recombinant Fusion Proteins; Rectal Neoplasms; RNA, Viral; Species Specificity; Support, Non-U.S. Gov't; Tumor Cells, Cultured; Viral Envelope Proteins; Viral Nonstructural Proteins",,"Mounir, S.; Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada",,,00652598,,AEMBA,"8209772","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028204244
"de Groot R., Heijnen L., van der Most R., Spaan W.","7103077066;7004331664;6701702352;7007172944;","Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs.",1994,"Archives of virology. Supplementum","9",,,"221","230",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028186988&partnerID=40&md5=40e940d5838dc4f44b9b8adf1f0457aa","Leiden University, Faculty of Medicine, Department of Virology, Netherlands","de Groot, R., Leiden University, Faculty of Medicine, Department of Virology, Netherlands; Heijnen, L., Leiden University, Faculty of Medicine, Department of Virology, Netherlands; van der Most, R., Leiden University, Faculty of Medicine, Department of Virology, Netherlands; Spaan, W., Leiden University, Faculty of Medicine, Department of Virology, Netherlands","We describe a novel strategy to site-specifically mutagenize the genome of an RNA virus by exploiting homologous RNA recombination between synthetic defective interfering (DI) RNA and viral RNA. Marker mutations introduced in the DI RNA were replaced by the wild-type residues during replication. More importantly, however, these genetic markers were introduced into the viral genome; even in the absence of positive selection, MHV recombinants were isolated. This finding provides new prospects for the study of coronavirus replication using recombinant DNA techniques. As a first application, we describe the rescue of the temperature sensitive mutant MHV Albany-4 using DI-directed mutagenesis. Possibilities and limitations of this strategy are discussed.",,"virus RNA; article; biosynthesis; defective virus; genetic recombination; genetics; growth, development and aging; molecular genetics; Murine hepatitis coronavirus; nucleotide sequence; point mutation; sequence analysis; site directed mutagenesis; synthesis; virus replication; Base Sequence; Defective Viruses; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Point Mutation; Recombination, Genetic; RNA, Viral; Sequence Analysis, RNA; Virus Replication",,"de Groot, R.",,,09391983,,,"8032253","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028186988
"Hierholzer J.C., Halonen P.E., Bingham P.G., Coombs R.A., Stone Y.O.","7007062289;7101941556;7004396774;7101929624;6507526306;","Antigen detection in human respiratory Coronavirus infections by monoclonal time-resolved fluoroimmunoassay",1994,"Clinical and Diagnostic Virology","2","3",,"165","179",,3,"10.1016/0928-0197(94)90020-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028364228&doi=10.1016%2f0928-0197%2894%2990020-5&partnerID=40&md5=0611a40ecfdb1032f5aad97fc9b01152","Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States; Department of Virology, University of Turku, Kiinamyllynkatu 13, SF-20520 Turku 52, Finland","Hierholzer, J.C., Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States; Halonen, P.E., Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States, Department of Virology, University of Turku, Kiinamyllynkatu 13, SF-20520 Turku 52, Finland; Bingham, P.G., Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States; Coombs, R.A., Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States; Stone, Y.O., Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States","Background: The diagnosis of respiratory infections by detecting viral antigens has received considerable attention using immunofluorescent assays (IFA) and enzyme immunoassays (EIA). Time-resolved fluoroimmunoassay (TR-FIA) has been developed for several viruses. Objectives: To prepare monoclonal antibodies to coronavirus strains, to incorporate them into a TR-FIA, and test the assay on clinical specimens. Study design: Monoclonal antibodies were prepared to the N nucleoprotein of the two human respiratory coronaviruses, HCV strains 229E and OC43. Monoclonals to both viruses were completely type-specific; they did not cross-react between themselves or with multiple strains of other respiratory viruses. These antibodies were configured into optimized EIA and TR-FIA tests. The all-monoclonal tests were then compared to polyclonal EIA tests in terms of their ability to detect virus in clinical specimens. Results: The all-monoclonal TR-FIA was uniformly the most sensitive, detecting virus in all 13 229E-positive specimens compared to 69% for the monoclonal EIA and 54% for the polyclonal EIA test. Similar results were obtained for 10 OC43-positive specimens: 100% in TR-FIA, 90% in monoclonal EIA, and 80% in polyclonal EIA. For 229E in TR-FIA, mean positive/negative (P/N) ratios were 143 for 229E-positive human embryonic lung fibroblast (HLF) cell culture fluids and 10 for positive nasopharyngeal aspirate specimens; for OC43 in TR-FIA, mean P/N values were 964 for OC43-positive rhabdomyosarcoma (RD) cell culture fluids and 174 for positive NPA specimens. The sensitivities of the TR-FIA were determined with purified virions to be 0.308 ng virus per well for HCV-229E and 0.098 ng virus per well for HCV-OC43. Conclusions: This rapid and sensitive test appears to be much more sensitive than traditional antigen detection assays but will require more extensive field testing on clinical specimens. © 1994.","Human coronavirus; Immunoassay; Monoclonal antibody; Rapid antigen test","monoclonal antibody; virus antigen; antigen detection; article; controlled study; coronavirus; diagnostic value; enzyme immunoassay; human; human cell; nonhuman; priority journal; respiratory tract infection; virus infection; Coronavirus; Hepatitis C virus; human coronavirus","Anderson, Hierholzer, Bingham, Stone, Microneutralization test for respiratory syncytial virus based on an enzyme immunoassay (1985) J. Clin. Microbiol., 22, pp. 1050-1052; Arpin, Talbot, Molecular characterization of the 229E strain of human coronavirus (1990) Adv. Exp. Med. Biol., 276, pp. 73-80. , D. Cavanagh, T.D. Brown, Coronaviruses and their diseases, Plenum Press, New York; Brown, Shami, Zywulko, Singh-Naz, Middleton, Time-resolved fluoroimmunoassay for enteric adenoviruses using the europium chelator 4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid (1990) J. Clin. Microbiol., 28, pp. 1398-1402; Bucher, Mikhail, Popple, Graves, Meiklejohn, Hodes, Johansson, Halonen, Rapid detection of type A influenza viruses with monoclonal antibodies to the M protein (M1) by enzyme-linked immunosorbent assay and time-resolved fluoroimmunoassay (1991) J. Clin. Microbiol., 29, pp. 2484-2488; Fleming, El Zaatari, Gilmore, Berne, Burks, Stohlman, Tourtellotte, Weiner, Antigenic assessment of coronaviruses isolated from patients with multiple sclerosis (1988) Arch. Neurol., 45, pp. 629-633; Grandien, Pettersson, Gardner, Linde, Stanton, Rapid viral diagnosis of acute respiratory infections: comparison of enzyme-linked immunosorbent assay and the immunofluorescence technique for detection of viral antigens in nasopharyngeal secretions (1985) J. Clin. Microbiol., 22, pp. 757-760; Halonen, Meurman, Lovgren, Hemmila, Soini, Detection of viral antigens by time-resolved fluoroimmunoassay (1983) Curr. Top. Microbiol. Immunol., 104, pp. 133-146; Halonen, Nikkari, Waris, Siitari, Orvell, Hierholzer, Kendal, Obert, One-step time-resolved fluoroimmunoassays based on monoclonal antibodies in detection of respiratory viruses (1989) Rapid Methods and Automation in Microbiology and Immunology, pp. 365-370. , A. Balows, R.C. Tilton, A. Turano, Brixia Academic Press, Brescia; Halonen, Obert, Hierholzer, Direct detection of viral antigens in respiratory infections by immunoassays: a four-year experience and new developments (1985) Med. Virol., 4, pp. 65-83; Hamre, Procknow, A new virus isolated from the human respiratory tract (1966) Proc. Soc. Exp. Biol. Med., 121, pp. 190-193; Hierholzer, Purification and biophysical properties of human coronavirus 229E (1976) Virology, 75, pp. 155-165; Hierholzer, Rapid diagnosis of viral infection (1991) Rapid Methods and Automation in Microbiology and Immunology, pp. 556-573. , A. Vaheri, R.C. Tilton, A. Balows, Springer, Berlin; Hierholzer, Anderson, Halonen, Monoclonal time-resolved fluoroimmunoassay: sensitive systems for the rapid diagnosis of respiratory virus infections (1990) Med. Virol., 9, pp. 17-45; Hierholzer, Bingham, Castells, Coombs, Time-resolved fluoroimmunoassays with monoclonal antibodies for rapid identification of parainfluenza type 4 and mumps viruses (1993) Arch. Virol., 130, pp. 335-352; Hierholzer, Bingham, Coombs, Johansson, Anderson, Halonen, Comparison of monoclonal antibody time-resolved fluoroimmunoassay with monoclonal antibody capture-biotinylated detector enzyme immunoassay for respiratory syncytial virus and parainfluenza virus antigen detection (1989) J. Clin. Microbiol., 27, pp. 1243-1249; Hierholzer, Johansson, Anderson, Tsou, Halonen, Comparison of monoclonal time-resolved fluoroimmunoassay with monoclonal capture-biotinylated detector enzyme immunoassay for adenovirus antigen detection (1987) J. Clin. Microbiol., 25, pp. 1662-1667; Hierholzer, Kemp, Tannock, The RNA and proteins of human coronaviruses (1981) Adv. Exp. Med. Biol., 142, pp. 43-67. , V. ter Meulen, S. Siddell, H. Wege, Plenum, London, Biochemistry and biology of coronaviruses; Hierholzer, Palmer, Whitfield, Kaye, Dowdle, Protein composition of coronavirus OC43 (1972) Virology, 48, pp. 516-527; Hierholzer, Suggs, Hall, Standardized viral hemagglutination and hemagglutination-inhibition tests. II. Description and statistical evaluation (1969) Appl. Microbiol., 18, pp. 824-833; Hierholzer, Tannock, Coronaviridae: The coronaviruses (1988) Laboratory Diagnosis of Infectious Diseases, Principles and Practice, 2, pp. 451-483. , E.H. Lennette, P. Halonen, F.A. Murphy, Viral, Rickettsial, and Chlamydial Diseases, Springer, New York; Hornsleth, Friis, Krasilnikof, Detection of respiratory syncytial virus in nasopharyngeal secretions by a biotin-avidin ELISA more sensitive than the fluorescent antibody technique (1986) J. Med. Virol., 18, pp. 113-117; Hughes, Mann, Hamparian, Detection of respiratory syncytial virus in clinical specimens by viral culture, direct and indirect immunofluorescence, and enzyme immunoassay (1988) J. Clin. Microbiol., 26, pp. 588-591; Isaacs, Flowers, Clarke, Valman, Macnaughton, Epidemiology of coronavirus respiratory infections (1983) Arch. Dis. Child., 58, pp. 500-503; Kamahora, Soe, Lai, Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Kaye, Hierholzer, Dowdle, Purification and further characterization of an ‘IBV-like’ virus (Coronavirus) (1970) Proc. Soc. Exp. Biol. Med., 135, pp. 457-463; Kemp, Hierholzer, Harrison, Burks, Characterization of viral proteins synthesized in 229E infected cells and effect(s) of inhibition of glycosylation and glycoprotein transport (1984) Molecular biology and pathogenesis of coronaviruses, 173, pp. 65-77. , P.J. Rottier, B.A. van der Zeijst, W.J. Spaan, M. Horzinek, Adv. Exp. Med. Biol., Plenum, London; Macnaughton, Flowers, Isaacs, Diagnosis of human coronavirus infections in children using enzyme-linked immunosorbent assay (1983) J. Med. Virol., 11, pp. 319-326; Macnaughton, Structural and antigenic relationships between human, murine, and avian coronaviruses (1981) Adv. Exp. Med. Biol., 142, pp. 19-28; McIntosh, Becker, Chanock, Growth in suckling mouse brain of ‘IBV-like’ viruses from patients with upper respiratory tract disease (1967) Proc. Nat. Acad. Sci. USA, 58, pp. 2268-2273; McIntosh, Halonen, Ruuskanen, Report of a workshop on respiratory viral infections: epidemiology, diagnosis, treatment, and prevention (1993) Clin. Infect. Dis., 16, pp. 151-164; McIntosh, McQuillin, Reed, Gardner, Diagnosis of human coronavirus infection by immunofluorescence: method and application to respiratory disease in hospitalized children (1978) J. Med. Virol., 2, pp. 341-346; Mertsola, Ziegler, Ruuskanen, Vanto, Koivikko, Halonen, Recurrent wheezy bronchitis and viral respiratory infections (1991) Arch. Dis. Child., 66, pp. 124-129; Myint, Harmsen, Raabe, Siddell, Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) J. Med. Virol., 31, pp. 165-172; Myint, Siddell, Tyrrell, Detection of human coronavirus 229E in nasal washings using RNA:RNA hybridisation (1989) J. Med. Virol., 29, pp. 70-73; Robb, Bond, Coronaviridae (1979) Compr. Virol., 14, pp. 193-247; Schmidt, Antigenic characterization of human coronaviruses 229E and OC43 by enzymelinked immunosorbent assay (1984) J. Clin. Microbiol., 20, pp. 175-180; Schmidt, Cooney, Kenny, Plaque assay and improved yield of human coronaviruses in a human rhabdomyosarcoma cell line (1979) J. Clin. Microbiol., 9, pp. 722-728; Schmidt, Kenny, Polypeptides and functions of antigens from human coronaviruses 229E and OC43 (1982) Infect. Immun., 35, pp. 515-522; Siddell, Wege, ter Meulen, The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Siitari, Dual-label time-resolved fluoroimmunoassay for the simultaneous detection of adenovirus and rotavirus in faeces (1990) J. Virol. Meth., 28, pp. 179-188; Stewart, Mounir, Talbot, Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Takimoto, Grandien, Ishida, Pereira, Paiva, Ishimaru, Makita, Martinez, Comparison of enzyme-linked immunosorbent assay, indirect immunofluorescence assay, and virus isolation for detection of respiratory viruses in nasopharyngeal secretions (1991) J. Clin. Microbiol., 29, pp. 470-474; Tsang, Peralta, Simons, Enzyme-linked immunoelectro-transfer blot techniques (EITB) for studying the specificities of antigens and antibodies separated by gel electrophoresis (1983) Meth. Enzymol., 92, pp. 377-391; Walls, Johansson, Harmon, Halonen, Kendal, Time-resolved fluoroimmunoassay with monoclonal antibodies for rapid diagnosis of influenza infections (1986) J. Clin. Microbiol., 24, pp. 907-912","Hierholzer, J.C.; Respiratory and Enteric Viruses Branch, Division of Viral and Rickettsial Diseases, Center for Infectious Diseases, 1600 Clifton Rd, N.E. Atlanta, GA 30333, United States",,,09280197,,CDVIE,,"English","Clin. Diagn. Virol.",Article,"Final",,Scopus,2-s2.0-0028364228
"Talbot P.J., Ekande S., Cashman N.R., Mounir S., Stewart J.N.","7102670281;6504317670;16169124200;6603891523;24318534100;","Neurotropism of human coronavirus 229E",1994,"Advances in Experimental Medicine and Biology","342",,,"339","346",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326939&partnerID=40&md5=99e65a33ac66f63674bc404a6536bd91","Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada","Talbot, P.J., Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada; Ekande, S., Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada; Cashman, N.R., Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada; Mounir, S., Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada; Stewart, J.N., Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada","The 299E prototype strain of human coronavirus (HCV-229E) has so far been mainly associated with infections of the respiratory tract. In the present study, we show evidence for infection of the central nervous system (CNS) by HCV-229E, both in vitro and in vivo. Various human cell lines of CNS origin were tested for their susceptibility to infection by HCV-229E. Production of viral antigens was monitored by indirect immunofluorescence with monoclonal antibodies and infectious progeny virions by plaque assay on the L132 human embryonic lung cell line. The SK-N-SH neuroblastoma and H4 neuroglioma cell lines were highly susceptible to infection. The U-87 MG and U-373 MG astrocytoma cell lines were also infectable by HCV-229E. We could also demonstrate infection of the MO3.13 cell line, which was established by fusion of human oligodendrocytes with a thioguanine-resistant mutant of the TE671 (RD) human rhabdomyosarcoma cell line. An apparently more extensive infection of the MO3.13 cells, when compared to the parental cells, supports the notion that human oligodendrocytes are differentially susceptible to infection by this virus. We also tested for HCV-229E gene expression in pathological brain specimens. For that purpose, we developed a reverse transcription-polymerase chain reaction (RT-PCR) assay to amplify a portion of the mRNA encoding the viral nucleocapsid protein. Using stringent laboratory conditions, viral RNA was detectable in brain tissue of 4 of 11 multiple sclerosis patients and none of 6 neurological and 5 normal controls. These results strongly suggest neurotropism on the part of HCV-229E and emphasize the importance of further studies on the possible involvement of human coronaviruses in neurological diseases such as multiple sclerosis.",,"capsid protein; messenger rna; rna directed dna polymerase; virus antigen; virus rna; central nervous system infection; conference paper; controlled study; coronavirus; gene expression; human; human cell; human tissue; infection sensitivity; multiple sclerosis; neurotropism; oligodendroglia; polymerase chain reaction; priority journal; virus genome; virus nucleocapsid; virus replication; Antigens, Viral; Brain; Capsid; Cell Line; Coronavirus; Coronavirus 229E, Human; Gene Expression; Human; Multiple Sclerosis; Neurons; Oligodendroglia; Organ Specificity; Polymerase Chain Reaction; RNA, Viral; Support, Non-U.S. Gov't; Viral Core Proteins; Virus Replication",,"Cashman, N.R.; Montreal Neurological Institute, McGill University, Montreal, Que. H3A 2B4, Canada",,,00652598,,AEMBA,"8209751","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028326939
"Bihun C.G.D., Percy D.H.","6506573763;16140219400;","Coronavirus infections in the laboratory rat: Degree of cross protection following immunization with a heterologous strain",1994,"Canadian Journal of Veterinary Research","58","3",,"224","229",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028131703&partnerID=40&md5=7f811a7632448b30f9f718796e8f73cc","Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","Bihun, C.G.D., Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Percy, D.H., Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","One hundred and twenty-one specific pathogen-free male Wistar rats eight to ten weeks of age were used to evaluate the efficacy of Parker's rat coronavirus (PRC) in affording cross protection on subsequent challenge with virulent sialodacryoadenitis (SDA) virus. Sixty-two animals were inoculated intranasally on day 0 and 21 days later with approximately 102 median tissue culture infective doses (TCID50) of the tenth passage of PRC replicated in L-2 cells. Animals were selected at random postvaccination to evaluate the safety and efficacy of PRC by histopathology, immunohistochemistry and serology. At three and six months postvaccination (PV), vaccinated and seronegative control rats were inoculated intranasally with approximately 103 TCID50 doses of virulent SDA virus. Challenged rats were then killed at 6, 10 and 14 days postchallenge and necropsied. Evaluations were based on lesion indices in lacrimal and salivary glands and respiratory tract, the presence of viral antigen by immunohistochemistry, and antibody response. Lesions were observed in rats killed PV, but in general, they were significantly reduced compared with those present in seronegative animals postexposure to virulent SDA virus (p ≤ 0.05). However, they were still considered to be an unacceptable level for a routine vaccination procedure. Postvaccination antibody titers to rat coronavirus were evident in all animals tested at three or six months prior to challenge with SDA virus. In PRC-vaccinated rats challenged with SDA virus at three or six months PV, there was a significant reduction in the incidence and extent of the lesions in the lacrimal and salivary glands and the upper and lower respiratory tract compared to challenged age-matched control rats (p ≤ 0.05). Significant cross protection to infection with SDA virus was provided in rats vaccinated with PRC for up to six months postvaccination.",,"protective agent; virus vaccine; animal experiment; antibody response; article; controlled study; coronavirus; cross reaction; immunization; male; nonhuman; rat; vaccination; virus infection; Administration, Intranasal; Animal; Animals, Laboratory; Antigens, Viral; Coronavirus Infections; Coronavirus, Rat; Cross Reactions; Male; Rats; Rats, Wistar; Specific Pathogen-Free Organisms; Support, Non-U.S. Gov't; Viral Vaccines",,"Percy, D.H.; Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada",,,08309000,,CJVRE,"7954126","English","CAN. J. VET. RES.",Article,"Final",,Scopus,2-s2.0-0028131703
"Van der Most R., Heijnen L., Spaan W., De Groot R.","6701702352;7004331664;7007172944;7103077066;","Homologous RNA recombination allows efficient introduction of site- specific mutations into the genome of coronavirus MHV-A59 via synthetic co- replicating RNAs",1994,"Advances in Experimental Medicine and Biology","342",,,"149","154",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028258312&partnerID=40&md5=c09e2557a629ecc6d34ffcb38f6b7711","Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands","Van der Most, R., Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands; Heijnen, L., Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands; Spaan, W., Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands; De Groot, R., Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands","We describe a novel strategy to site-specifically mutagenize the genome of an RNA virus by exploiting homologous RNA recombination between synthetic defective interfering (DI) RNA and the viral RNA. Marker mutations introduced in the DI RNA were replaced by the wild-type residues during replication. More importantly, however, these genetic markers were introduced into the viral genome; even in the absence of positive selection MHV recombinants could be isolated. This finding provides new prospects for the study of coronavirus replication using recombinant DNA techniques. As a first application, we describe the rescue of the temperature sensitive mutant MHV Albany-4 using DI-directed mutagenesis. Possibilities and limitations of this strategy are discussed.",,"recombinant rna; virus rna; conference paper; mouse; murine hepatitis coronavirus; nonhuman; point mutation; priority journal; rna replication; viral genetics; virus genome; virus recombination; virus replication; Base Sequence; Defective Viruses; Genetic Markers; Genome, Viral; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Recombination, Genetic; RNA, Viral; Support, Non-U.S. Gov't; Virus Replication",,"Van der Most, R.; Department of Virology, Institute of Medical Microbiology, Faculty of Medicine, Postbus 320, 2300 AH Leiden, Netherlands",,,00652598,,AEMBA,"8209722","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028258312
"Gallagher T.M., Buchmeier M.J., Perlman S.","7202310503;7006201704;7102708317;","Dissemination of MHV4 (strain JHM) infection does not require specific coronavirus receptors",1994,"Advances in Experimental Medicine and Biology","342",,,"279","284",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028210517&partnerID=40&md5=f24c35a2eb0faa8693fd098db9299ca2","Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States","Gallagher, T.M., Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States; Buchmeier, M.J., Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States; Perlman, S., Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States","In this report, we demonstrate the syncytial spread of MHV4 (strain JHM) infection through non-murine cell cultures which lack a specific MHV4 receptor and are therefore resistant to infection by free virions. This was achieved by allowing infected murine cells to settle onto confluent monolayers of non-murine cells in a straightforward infectious center assay. Receptor-independent syncytium formation induced by cells expressing the MHV4 spike (S) from recombinant vaccinia viruses (VV) indicated that spread was mediated by this coronavirus glycoprotein. We conclude that the S protein of MHV4 is so potently fusogenic that it does not require prior binding to a virus-specific surface receptor to induce fusion of closely-opposed plasma membranes.",,"virus glycoprotein; virus receptor; animal cell; cell strain bhk; conference paper; gene expression; human; human cell; infection resistance; infection sensitivity; mouse; murine hepatitis coronavirus; nonhuman; priority journal; syncytium; vaccinia virus; virus cell interaction; virus infection; virus recombinant; virus strain; virus transmission; Animal; Astrocytoma; Cell Fusion; Cell Line; Cytopathogenic Effect, Viral; Genetic Vectors; Hamsters; Kidney; Membrane Glycoproteins; Mesocricetus; Murine hepatitis virus; Rats; Receptors, Virus; Recombinant Fusion Proteins; Species Specificity; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Tumor Cells, Cultured; Viral Envelope Proteins; Virus Replication",,"Gallagher, T.M.; Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States",,,00652598,,AEMBA,"8209743","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028210517
"Collins A.R.","24439435400;","Virus-ligand interactions of OC43 coronavirus with cell membranes",1994,"Advances in Experimental Medicine and Biology","342",,,"285","291",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028211648&partnerID=40&md5=fc905f257862ea2a73d49dd0ecce9944","Department of Microbiology, State Univ. of NY, Buffalo, NY 14214, United States","Collins, A.R., Department of Microbiology, State Univ. of NY, Buffalo, NY 14214, United States","The binding of human coronavirus OC43 to human rhabdomyosarcoma cells which are highly susceptible to infection was studied by a solid phase virus binding assay and a receptor blockade assay. It was observed that whole virions and S(spike) bound to a 90 kD glycoprotein of RD cells even after treatment of the substrate with neuraminidase or 0.1 M NaOH. A second receptor of 45 kD also bound virus and was identified as HLA class I antigen. Antibody to both receptors reduced the virus yield in a receptor blockade assay. Sera from four patients with multiple sclerosis contained receptor blocking activity which correlated with antibodies to HLA. No receptor blocking antibodies to the 90 kD RD cell protein were found in human sera.",,"blocking antibody; cell protein; HLA antigen class 1; ligand; receptor antibody; sialidase; sodium hydroxide; virus receptor; animal cell; cell membrane; conference paper; controlled study; coronavirus; disease association; human; human cell; immunoblotting; infection sensitivity; monkey; multiple sclerosis; nonhuman; priority journal; receptor blocking; rhabdomyosarcoma; virion; virus adsorption; virus infection; Adolescent; Adult; Animal; Cell Line; Cell Membrane; Cercopithecus aethiops; Coronavirus; Coronavirus OC43, Human; Cytomegalovirus Infections; Disease Susceptibility; HLA Antigens; Human; Isoantibodies; Membrane Glycoproteins; Middle Age; Multiple Sclerosis; Receptors, Virus; Rhabdomyosarcoma; Tumor Cells, Cultured; Viral Envelope Proteins",,"Collins, A.R.; Department of Microbiology, State Univ. of NY, Buffalo, NY 14214, United States",,,00652598,,AEMBA,"8209744","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028211648
"Jabrane A., Girard C., Elazhary Y.","6602810138;7202447527;7003751362;","Pathogenicity of porcine respiratory coronavirus isolated in Québec.",1994,"The Canadian veterinary journal. La revue vétérinaire canadienne","35","2",,"86","92",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028377370&partnerID=40&md5=2fc822066ab2ca72c30ae50fb7f3e595","Département de pathologie et microbiologie, Faculté de Médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada","Jabrane, A., Département de pathologie et microbiologie, Faculté de Médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada; Girard, C., Département de pathologie et microbiologie, Faculté de Médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada; Elazhary, Y., Département de pathologie et microbiologie, Faculté de Médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada","Porcine respiratory coronavirus (PRCV) is present in many countries, including Canada, but controversy still exists concerning its pathogenicity. Eight-week-old piglets were inoculated intratracheally with a Quebec PRCV isolate (1Q90). Two contact piglets were kept with the inoculated animals. Three animals served as control. Polypnea and dyspnea were the main clinical signs observed. Diffuse bronchioloalveolar damage occurred 24 hours postinoculation. Changes compatible with bronchointerstitial pneumonia were present six days postinoculation. The inoculated virus was recovered from the respiratory tract and mesenteric lymph nodes, but not from the digestive tract, of the inoculated as well as the contact piglets. No virus was isolated from the control piglets. The development of clinical signs and histopathological changes in inoculated as well as in contact piglets and the reisolation of the inoculated virus demonstrated that PRCV can be an important respiratory pathogen.",,"animal; animal disease; article; Canada; cell line; Coronavirus; female; growth, development and aging; interstitial lung disease; isolation and purification; male; microbiology; pathogenicity; pathology; respiratory tract infection; swine; swine disease; virus infection; Animals; Cell Line; Coronavirus; Coronavirus Infections; Female; Lung Diseases, Interstitial; Male; Quebec; Respiratory Tract Infections; Swine; Swine Diseases",,"Jabrane, A.",,,00085286,,,"8069830","English","Can. Vet. J.",Article,"Final",,Scopus,2-s2.0-0028377370
"Flory E., Stuhler A., Wege H., Siddell S., Wege H.","7003965470;6602388166;7005516646;7005260816;7005516646;","Recombinant vaccinia viruses which express MHV-JHM proteins: Protective immune response and the influence of vaccination on coronavirus-induced encephalomyelitis",1994,"Advances in Experimental Medicine and Biology","342",,,"401","406",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028328622&partnerID=40&md5=0419960769a317e2e737c82182b4ca7f","Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany","Flory, E., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Stuhler, A., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Wege, H., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany, Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Siddell, S., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Wege, H., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany, Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany","Vaccinia-virus (VV) recombinants encoding either the nucleocapsid (N) or the spike (S) protein of MHV-JHM were constructed to study the role of the immune response against defined coronavirus antigens. For the S-protein, a fusogenic (Sfus+) or non fusogenic variant (Sfus-) of the gene was inserted into the VV genome. A strong protection against acute encephalomyelitis (AE) was mediated in Lewis rats which were immunized by VV-Sfus+ and challenged with an otherwise lethal dose of MHV-JHM before the induction of S-specific IgG antibodies. By contrast, a VV recombinant encoding a variant non fusogenic S-protein or the N-protein was not capable conferring protection. In addition, we demonstrated that MHV-JHM S-specific IgG antibodies elicited before MHV-JHM challenge modulated the disease process, changing it from an acute disease to subacute demyelinating encephalomyelitis (SDE).",,"capsid protein; vaccine; vitronectin; animal experiment; animal model; antibody production; conference paper; coronavirus; demyelinating disease; disease activity; humoral immunity; nonhuman; priority journal; rat; vaccination; vaccinia virus; virus encephalitis; virus nucleocapsid; virus recombinant; virus resistance; Acute Disease; Animal; Antibodies, Viral; Capsid; Cell Fusion; Chronic Disease; Demyelinating Diseases; Encephalomyelitis; Immunity, Cellular; Immunoglobulin G; Membrane Glycoproteins; Murine hepatitis virus; Rats; Rats, Inbred Lew; Recombination, Genetic; Support, Non-U.S. Gov't; T-Lymphocytes, Helper-Inducer; Vaccination; Vaccines, Synthetic; Vaccinia virus; Viral Core Proteins; Viral Envelope Proteins; Viral Vaccines; Virulence; Virus Latency",,"Flory, E.; Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany",,,00652598,,AEMBA,"8209761","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028328622
"Li X., Scott F.W.","57192492158;35611898900;","Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction",1994,"Veterinary Microbiology","42","1",,"65","77",,25,"10.1016/0378-1135(94)90078-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027997817&doi=10.1016%2f0378-1135%2894%2990078-7&partnerID=40&md5=b4b389ab8319895c749e1acb242f2dcf","Cornell Feline Health Center and Department of Microbiology, Immunology and Parasitology, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853USA, United States","Li, X., Cornell Feline Health Center and Department of Microbiology, Immunology and Parasitology, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853USA, United States; Scott, F.W., Cornell Feline Health Center and Department of Microbiology, Immunology and Parasitology, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853USA, United States","Feline coronavirus infections in cell cultures and in fresh and fixed feline tissues were detected using a polymerase chain reaction (PCR) test. Cell cultures were inoculated with feline infectious peritonitis virus (FIPV), feline enteric coronavirus (FECV)_or sham inoculum. The tissue samples of liver, kidney and spleen were taken from specific-pathogen-free (SPF) cats that were inoculated intranasally with 103 TCID50 of FIPV 79-1146 (n = 10), FIPV UCD1 (n = 3) or sham inoculum (n = 3), from clinical cats (n = 43), and from formalin-fixed archived feline tissues (n = 49), respectively. Additional tissue samples were taken from the FIPV-inoculated cats (n = 6) and were kept at 4°C, room temperatures (20-24°C) and 37°C respectively for 0, 6, 12, 24, 48, 72, and 96 hours before frozen (-70°C) for PCR to evaluate the effects of the ambient temperatures and post-mortem intervals on the test. The samples were also fixed in 10% neutrally buffered formalin, 95% ethanol, and Bouin's solution respectively to evaluate the effects of the fixatives on the test. Positive PCR results were obtained from the cell cultures that were inoculated with FIPV and FECV and from the FIPV-inoculated cats (13/13). Negative PCR results were obtained from the sham-inoculated cell cultures and cats (3/3). Of the 92 clinical cats, 7 of the 8 FIP-suspected cats (87.5%) and 51 of the 84 non-FIP-suspected cats (60.7%) were shown to be virus-positive in at least one of the tissue samples. There was no significant difference in the PCR results between the fresh and the formalin-fixed tissues of the clinical cats (P > 0.05). Of the FIPV inoculated cats, the virus was detectable equally well in fresh and formalin-, Bouin's solution- or ethanol-fixedtissues. However, the amounts of total RNA extracted from the fixed tissues were significantly less than those from fresh tissues (P < 0.01). In tissues that were kept at 4°C, the virus was detectable up to 96 h; at room temperatures, up to 48 h; and at 37°C, up to 24 h, respectively. © 1994.","Cat; Diagnosis; Feline coronavirus; feline coronavirus; PCR","animal cell; animal tissue; article; cat; controlled study; coronavirus; diagnostic value; nonhuman; polymerase chain reaction; virus detection; Animal; Base Sequence; Cat Diseases; Cats; Cells, Cultured; Coronavirus; Coronavirus Infections; DNA, Viral; Molecular Sequence Data; Nucleic Acid Hybridization; Polymerase Chain Reaction; RNA, Viral; Support, Non-U.S. Gov't; Animalia; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; Felis catus","Addie, Jarrett, Control of feline cononavirus infection in kittens (1990) Vet. Rec., 126, p. 164; Addie, Garde, A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; August, Feline infectious peritonitis: An immune-mediated coronaviral vasculitis (1984) Vet. Clin. North Am., 14, pp. 971-984; Barlough, Serodiagnostic aids and management practice for feline retrovirus infection (1984) Vet. Clin. North Am., 14, pp. 955-969; Barlough, Stoddart, Feline coronaviral infections (1990) Infectious diseases of the dog and cat, pp. 300-312. , C.E. Greene, W.B. Saunders Company, Philadelphia; Chomczynski, Sacchi, Single-step RNA isolation from cultured cells or tissues (1992) Current protocols in molecular biology, 1, pp. 4.2.4-8. , F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl, John Wiley and Sons, New York; De Groot, Maduro, Lenstra, Horzinek, Van Der Zeijst, Spaan, cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J. Gen. Virol., 68, pp. 2639-2646; De Groot, Andeweg, Horzinek, Spaan, Sequence analysis of the 3′end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virol., 167, pp. 370-376; Evermann, McKeirnan, Ott, Perspectives on the epizootiology of feline enteric coronavirus and pathogenesis of feline infectious peritonitis (1991) Vet. Microbiol., 28, pp. 243-255; Evermann, Heeney, Roelke, McKeirnan, O'Brien, Biological and pathological consequences of feline infectious peritonitis virus infection in the cheetah (1988) Arch. Virol., 102, pp. 155-171; Hok, Demonstration of feline infectious peritonitis virus in conjuctival epithelial cells from cats. A simple and reliable method for clinical veterinary virology screening (1989) APMIS, 97, pp. 820-824; Hok, Demonstration of feline corona virus (FCV)_antigen in organs of cats suspected of feline infectious peritonitis (FIP) disease (1990) APMIS, 98, pp. 659-664; Holzworth, Some important disorders of cats (1963) Cornell Vet., 53, pp. 157-160; Homberger, Smith, Barthold, Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Horzinek, Osterhaus, Feline infectious peritonitis: A worldwide serosurvey (1979) Am. J. Vet. Res., 40, pp. 1487-1492; Martinez, Weiss, Detection of feline infectious peritonitis virus infection in cell cultures and peripheral blood mononuclear leukocytes of experimentally infected cats using a biotinylated cDNA probe (1993) Vet. Microbiol., 34, pp. 259-271; McKeirnan, Evermann, Hargis, Miller, Ott, Isolation of feline coronaviruses from two cats with diverse disease manifestations (1981) Fel. Pract., 11, pp. 16-20; Olsen, Corapi, Ngichabe, Baines, Scott, Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enahancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Pedersen, Coronavirus diseases (coronavirus enteritis, feline infectious peritonitis) (1987) Diseases of the cats, pp. 193-214. , J. Holzworth, W.B. Saunders, Philadelphia; Pedersen, Boyle, Floyd, Fudge, Barker, An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, Evermann, McKeirnan, Ott, Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Rodgers, Baldwin, A serologic survey of Oklahoma cats for antibodies to feline immunodeficiency virus, coronavirus, and Toxoplasma gondii and for antigen to feline leukemia virus (1990) J. Vet. Diagn. Invest., 2, pp. 180-183; Sambrook, Fritsch, Maniatis, Slot hybridization of RNA (1989) Molecular Cloning: A Laboratory Manual, 2, pp. 7.54-55. , 2nd ed., Cold Spring Harbor Laboratory Press, New York; Sambrook, Fritsch, Maniatis, Analysis and cloning of eukaryotic genomic DNA (1989) Molecular Cloning: A laboratory Manual, 2, pp. 9.31-59. , 2nd ed., Cold Spring Harbor Laboratory Press, New York; Sambrook, Fritsch, Maniatics, Colony hybridization (1989) Molecular Cloning: A Laboratory Manual, 2, pp. 10.18-66. , 2nd ed., Cold Spring Harbor Laboratory Press, New York; Scott, Update of FIP (1989) Proc. 12th KalKan Symp., 12, pp. 43-47; Scott, Transmission and epidemiology (1991) New perspectives on prevention of feline infectious peritonitis, pp. 8-13. , Proc. symp. Orlando, Florida; Slatko, Albright, Tabor, DNA sequencing by the dideoxyl method (1992) Current protocols in molecular biology, 1, pp. 7.4.1-27. , F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl, John Wiley and Sons, New York; Sparkes, Gruffydd, Harbour, Feline infectious peritonitis: a review of clinicopathological changes in 65 cases, and a critical assessment of their diagnostic value (1991) Vet. Rec., 129, pp. 209-212; Tupper, Evermann, Russell, Thouless, Antigenic and biological diversity of feline coronaviruses: feline infectious peritonitis and feline enteritis virus (1987) Arch. Virol., 96, pp. 29-38; Vennema, Rossen, Wesseling, Horzinek, Rottier, Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virol., 191, pp. 134-140; Yamada, Imanishi, Detection of influenza B virus in throat swabs using the polymerase chain reaction (1992) Acta Virol., 36, pp. 320-325; Zook, King, Robinson, McCombs, Ultrastructural evidence for the viral etiology of feline infectious peritonitis (1968) Pathol. Vet., 5, pp. 91-95","Li, X.",,,03781135,,VMICD,"7839586","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0027997817
"Schultze B., Herrler G.","7006104520;7006339246;","Recognition of cellular receptors by bovine coronavirus.",1994,"Archives of virology. Supplementum","9",,,"451","459",,14,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028187750&partnerID=40&md5=3c2e28c983d4842aa2b11c3b90512054","Institut für Virologie, Philipps-Universität Marburg, Federal Republic of Germany., Germany","Schultze, B., Institut für Virologie, Philipps-Universität Marburg, Federal Republic of Germany., Germany; Herrler, G., Institut für Virologie, Philipps-Universität Marburg, Federal Republic of Germany., Germany","Bovine coronavirus (BCV) initiates infection by attachment to cell surface receptors the crucial component of which is N-acetyl-9-O-acetylneuraminic acid. Inactivation of receptors by neuraminidase treatment and restoration of receptors by enzymatic resialylation of asialo-cells is described as a method to determine (i) the type of sialic acid that is recognized; (ii) the linkage specificity of the viral binding activity; (iii) the minimal amount of sialic acid required for virus attachment. Evidence is presented that both glycoproteins and glycolipids can serve as receptors for BCV provided they contain 9-O-acetylated sialic acid. A model is introduced proposing that after initial binding to sialic acid-containing receptors, the S-protein of BCV interacts with a specific protein receptor. This interaction may result in a conformational change that exposes a fusogenic domain and thus induces the fusion between the viral and the cellular membrane.",,"coronavirus receptor; glycolipid; glycoprotein; membrane protein; sialic acid derivative; spike glycoprotein, coronavirus; virus envelope protein; virus receptor; article; carbohydrate analysis; chemistry; comparative study; Coronavirus; Influenza virus C; metabolism; molecular genetics; protein binding; Carbohydrate Sequence; Coronavirus, Bovine; Glycolipids; Glycoproteins; Influenzavirus C; Membrane Glycoproteins; Molecular Sequence Data; Protein Binding; Receptors, Virus; Sialic Acids; Viral Envelope Proteins",,"Schultze, B.",,,09391983,,,"8032275","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028187750
"Charley B., Lavenant L., Lefèvre F.","55246691600;57212990418;56974662200;","Coronavirus transmissible gastroenteritis virus-mediated induction of IFN alpha-mRNA in porcine leukocytes requires prior synthesis of soluble proteins.",1994,"Veterinary research","25","1",,"29","36",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028315428&partnerID=40&md5=71d0a64a9022bc5234f0f3e96528d8b5","INRA, Laboratorie de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France","Charley, B., INRA, Laboratorie de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France; Lavenant, L., INRA, Laboratorie de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France; Lefèvre, F., INRA, Laboratorie de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France","We studied the expression of interferon alpha (IFN alpha)-mRNA in porcine non-adherent peripheral blood mononuclear cells (PBMC) after induction by the coronavirus transmissible gastroenteritis virus (TGEV). We found that protein synthesis inhibition by cycloheximide (CHX) blocked IFN alpha-mRNA expression, except when PBMC were preincubated with a conditioned medium as a potential source of cytokines. These data indicate that IFN alpha-mRNA induction by TGEV requires de novo synthesis of proteins. Moreover, they suggest that IFN alpha-mRNA induction in porcine leukocytes by TGEV involves mechanisms identical to those described for the herpes simplex virus in humans. In addition, experiments performed with a TGEV mutant, dm 49-4, previously characterized for its low ability to induce IFN alpha, showed that addition of a conditioned medium could not normalize its IFN alpha-inducing ability. Therefore, the defect of the dm49-4 mutant may be at the level of the final triggering signal to PBMC.",,"actin; alpha interferon; cycloheximide; cytokine; messenger RNA; virus protein; animal; article; biosynthesis; cell culture; culture medium; drug antagonism; gene expression regulation; genetics; immunology; microbiology; mononuclear cell; Northern blotting; physiology; swine; Transmissible gastroenteritis virus; Actins; Animals; Blotting, Northern; Cells, Cultured; Culture Media, Conditioned; Cycloheximide; Cytokines; Gene Expression Regulation, Viral; Interferon-alpha; Leukocytes, Mononuclear; RNA, Messenger; Swine; Transmissible gastroenteritis virus; Viral Proteins",,"Charley, B.",,,09284249,,,"8142954","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028315428
"Stauber R., Pfleiderer M., Siddell S.","7005372065;6603844216;7005260816;","Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for its fusion activity",1994,"Advances in Experimental Medicine and Biology","342",,,"165","170",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028268358&partnerID=40&md5=8ac2c757e628f32714a84ad025e0d374","Institut fur Virologie, Universitat Wurzburg, Versbacherstr. 7, 8700 Wurzburg, Germany","Stauber, R., Institut fur Virologie, Universitat Wurzburg, Versbacherstr. 7, 8700 Wurzburg, Germany; Pfleiderer, M., Institut fur Virologie, Universitat Wurzburg, Versbacherstr. 7, 8700 Wurzburg, Germany; Siddell, S., Institut fur Virologie, Universitat Wurzburg, Versbacherstr. 7, 8700 Wurzburg, Germany","The surface glycoprotein (S) of the murine hepatitis coronavirus MHV normally undergoes proteolytic cleavage during transport to the cell surface. To determine whether the cleavage of the MHV-JHM S glycoprotein is required to activate its ability to fuse cellular membranes, the protease recognition sequence in a cDNA copy of the S gene was altered from Arg-Arg-Ala-Arg-Arg into Ser-Val-Ser-Gly-Gly by site directed mutagenesis. The mutated and wild type S genes were expressed by means of recombinant vaccinia viruses and it could be shown that the mutated S protein was not cleaved when it was expressed in mouse DBT cells, in contrast to the wild type S protein. Nevertheless, the non-cleaved S protein induced extensive syncytium formation in mouse DBT cells. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus, proteolytic cleavage is not an absolute requirement for its fusion function.",,"complementary dna; virus glycoprotein; virus rna; animal cell; cell fusion; conference paper; hela cell; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein transport; site directed mutagenesis; vaccinia virus; virus envelope; virus recombinant; Amino Acid Sequence; Animal; Astrocytoma; Cell Fusion; Cytopathogenic Effect, Viral; Endopeptidases; Hela Cells; Human; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Protein Processing, Post-Translational; Tumor Cells, Cultured; Viral Envelope Proteins",,"Stauber, R.; Institut fur Virologie, Universitat Wurzburg, Versbacherstr. 7, 8700 Wurzburg, Germany",,,00652598,,AEMBA,"8209724","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028268358
"Cornaglia E., Chrétien N., Charara S., Elazhary Y.","7003673251;6602989637;6505572124;7003751362;","Detection of porcine respiratory coronavirus and transmissible gastroenteritis virus by an enzyme-linked immunosorbent assay",1994,"Veterinary Microbiology","42","4",,"349","359",,1,"10.1016/0378-1135(94)90066-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028029928&doi=10.1016%2f0378-1135%2894%2990066-3&partnerID=40&md5=e9efca9ecdf482570998c401a891acd7","Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada","Cornaglia, E., Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada; Chrétien, N., Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada; Charara, S., Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada; Elazhary, Y., Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada","An enzyme-linked immunosorbent assay (ELISA) for the detection of transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) was developed. A bovine TGEV-specific polyclonal antibody was purified by affinity chromatography with the TRIO Bioprocessing System and was used as the capture antibody, at a concentration of 1.5 μg/well. The F5.39 monoclonal antibody was obtained by the fusion of spleen lymphocytes from TGEV immunized mice with NS-1 myeloma cells. This mAb was used as a second antibody for the ELISA to detect TGEV in field cases, 53 intestinal samples were taken from pigs exhibiting clinical signs of transmissible gastroenteritis. All the positive samples detected by the ELISA were confirmed as positive by immunofluorescence or cell culture immunofluorescence. To study the ability of this ELISA to detect PRCV in nasal swabs and lung samples, 20 seven-day-old piglets were inoculated with a Quebec strain of PRCV. The ELISA was able to detect PRCV in both kinds of samples. © 1994.","Diagnosis; ELISA; Pig; Porcine respiratory coronavirus; Porcine transmissible gastroenteritis virus; virus","animal experiment; article; controlled study; coronavirus; diagnostic accuracy; enzyme linked immunosorbent assay; nonhuman; swine; transmissible gastroenteritis virus; virus detection; Animal; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Feces; Gastroenteritis, Transmissible, of Swine; Lung; Lung Diseases; Mice; Mice, Inbred BALB C; Nasal Lavage Fluid; Sensitivity and Specificity; Swine; Swine Diseases; Transmissible gastroenteritis virus; Animalia; Bovinae; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Becker, Teufel, Mields, The immune-peroxidase method for detection of viral and chlamydial antigens. III. Demonstratio of TGE antigen in pig thyroid cell cultures (1974) Zentralbl. Veterinarmed. B., 21, pp. 59-65; Bernard, Lantier, Laude, Aynaud, Detection of transmissible gastroenteritis coronavirus antigens by a sandwich enzyme-linked immunosorbent assay technique (1986) Am. J. Vet. Res., 47, pp. 2441-2444; Bohac, Derbyshire, The demonstration of transmissible gastroenteritis viral antigens by immunoelectrophoresis and counterimmunoelectrophoresis (1975) Can. J. Microbiol., 21, pp. 750-753; Bohac, Derbyshire, Thorsen, The detection of transmissible gastroenteritis viral antigen by immunodiffusion (1975) Can. J. Comp. Med., 39, pp. 67-75; Bohl, Diagnosis of diarrhea in pigs due to transmissible gastroenteritis virus or rotavirus (1979) Viral Enteritis in Humans and Animals, 90, pp. 341-344. , F. Bricout, R. Scherrer, INSERM, Paris; Bourgueil, Hutet, Cariolet, Vannier, Experimental infection of pigs with the porcine respiratory coronavirus (PRCV): measure of viral excretion (1992) Vet. Microbiol., 31, pp. 11-18; Chu, Li, Glock, Ross, Applications of peroxidase-antiperoxidase staining technique for detection of transmissible gastroenteritis virus in pigs (1982) Am. J. Vet. Res., 43, pp. 77-81; Cornaglia, Elazhary, roy, Talbot, Monoclonal antibodies to Quebec strain (Q17) of bovine rotavirus (1990) Vet. Microbiol., 23, pp. 283-294; Correa, Jimenez, Suné, Bullido, Enjuanes, Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-94; Cox, Hooyberghs, Pensaert, Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Cox, Pensaert, Callebaut, van Deun, Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus (1990) Vet. Microbiol., 23, pp. 237-243; Cox, Pensaert, Callebaut, Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-272; Cubero, Leon, Contreras, Astorga, Lanza, Garcia, Transmissible gastroenteritis in pigs in south east Spain: prevalence and factors associated with infection (1993) Vet. Rec., 132, pp. 238-241; Doyle, Hutchings, A transmissible gastroenteritis in pigs. (1946) J Am Vet Med Assoc, 108, pp. 257-259; Duret, Brun, Guilmoto, Dauvergne, Isolement, identification et pothogène chez le porc d'un coronavirus apparenté au virus de la gastro-entérite transmissible (1988) Rec. Méd. Vét., 164, pp. 221-226; Egan, Harris, Hill, Prevalence of swine dysentery, transmissible gastroenteritis and pseudorabies in Iowa, Illinois and Missouri swine (1982) Proc. 86th Ann. Meet. United States Animal Health Association, pp. 497-502. , 7–12 november 1982, at Nashville, TN, USA; Elazhary, Jabrane, Talbot, Porcine respiratory coronavirus isolated from young piglets in Quebec (1992) Vet. Rec., 130, p. 500; Enjuanes, Suné, Gebauer, Smerdou, Camacho, Anton, Gonzalez, Sanchez, Antigen selection and presentation to protect against transmissible gastroenteritis coronavirus (1992) Vet. Microbiol., 33, pp. 249-262; Gebauer, Posthumus, Correa, Suné, Smerdou, Sanchez, Lenstra, Enjuanes, Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virology, 183, pp. 225-238; Halbur, Paul, Vaughn, Andrews, Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J. Vet. Diagn. Invest., 5, pp. 184-188; Jabrane, Elazhary, Pathogenicity of porcine respiratory coronavirus isolated in Quebec (1994) Can. Vet. J., 35, pp. 86-92; Lanza, Brown, Paton, Pathogenicity of concurrent infection of pigs with porcine respiratory coronavirus and swine influenza virus (1992) Research in Veterinary Science, 53, pp. 309-314; Laude, Van Reeth, Pensaert, Porcine respiratory coronavirus: molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Moxley, LeRoy, Davis, Experience with a planned exposure program for the control of enzootic transmissible gastroenteritis in swine (1993) J. Am. Vet. Med. Assoc., 202, pp. 1861-1864; O'Toole, Brown, Bridges, Cartwright, Pathogenicity of experimental infection with “pneumotropic” porcine respiratory coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, Haelterman, Burnstein, Transmissible gastroenteritis of swine: virus-intestinal cell interactions. I. Immunofluorescence, histopathology and virus production in the small intestine through the course of infection (1970) Archiv für Gesamte Virusforschung, 31, pp. 321-334; Pensaert, Callebaut, Vergote, Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Pensaert, Cox, van Deun, Callebaut, A sero-epizoobiological study of porcine respiratory coronavirus in belgian swine (1993) Vet. Q., 15, pp. 16-20; Saif, Heckert, (1990) Viral diarrhea of man and animals, pp. 190-204. , L.J. Saif, K.W. Theil, Boca Raton, Florida; Skalinskii, Mel'nikova, Kasyuk, Boiko, Diagnosis of procine transmissible gastroenteritis virus (1977) Veterinaria, 9, p. 104; Toma, Benet, A technique of research on microplates of the antibodies neutralizing transmissible gastroenteritis virus of swine (1976) Rec. Méd. Vét., 152, pp. 565-568; van Nieuwstadt, Pol, Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pigs (1989) Vet. Rec., 124, pp. 43-44; van Nieuwstadt, Cornelissen, Zetstra, Comparison of two methods for detection of transmissible gastroenteritis virus in feces of pigs with experimentally induced infection (1988) Am. J. Vet. Res., 49, pp. 1836-1843; van Nieuwstadt, Zetstra, Boonstra, Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet. Rec., 125, pp. 58-60; Vaughn, Paul, Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet. Microbiol., 36, pp. 333-347; Wesley, Woods, Immunization of pregnant gilts with PRCV induces lactogenic immunity for protection of nursing piglets from challenge with TGEV (1993) Vet. Microbiol., 38, pp. 31-40; Yolken, Enzyme immunoassays for the detection of infectious antigens in body fluids: current limitations and future prospects (1982) Rev. Infect. Dis., 4, pp. 35-68; Zola, (1988) Monoclonal antibodies: a manual of techniques, pp. 54-56. , CRC Press, Boca Raton, Florida","Cornaglia, E.; Virology Section, Faculty of Veterinary Medicine, University of Montreal, P.O. Box 5000, Saint Hyacinthe, Que. J2S 7C6, Canada",,,03781135,,VMICD,"9133060","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0028029928
"Martín M., Casal J., Lanza I., Rubio P., Cármenes P.","55387187500;7102107252;6701643399;7006722520;6603172896;","Porcine respiratory coronavirus spread in Catalunya, Spain, a previously infection-free area",1994,"Preventive Veterinary Medicine","21","1",,"65","74",,2,"10.1016/0167-5877(94)90032-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0008339684&doi=10.1016%2f0167-5877%2894%2990032-9&partnerID=40&md5=02c4776a9868006900bbf1708b1f4548","Patologia Infecciosa i Epidemiologia, Departament de Patologia i Producció Animals, U.A.B., 08193 Bellaterra, Spain; Enfermedades Infecciosas y Epizootiología, Departamento de Patología Animal (Sanidad Animal), Universidad de León, 24007 León, Spain","Martín, M., Patologia Infecciosa i Epidemiologia, Departament de Patologia i Producció Animals, U.A.B., 08193 Bellaterra, Spain; Casal, J., Patologia Infecciosa i Epidemiologia, Departament de Patologia i Producció Animals, U.A.B., 08193 Bellaterra, Spain; Lanza, I., Enfermedades Infecciosas y Epizootiología, Departamento de Patología Animal (Sanidad Animal), Universidad de León, 24007 León, Spain; Rubio, P., Enfermedades Infecciosas y Epizootiología, Departamento de Patología Animal (Sanidad Animal), Universidad de León, 24007 León, Spain; Cármenes, P., Enfermedades Infecciosas y Epizootiología, Departamento de Patología Animal (Sanidad Animal), Universidad de León, 24007 León, Spain","A retrospective study of sera from seven commercial pig herds was conducted from May 1985 to July 1989, showing that antibodies against Porcine Respiratory Coronavirus (PRCV) were first detected in Spain in September 1986. During 1991 a stratified sampling of breeding herds was conducted to establish prevalence to PRCV or Transmissible Gastroenteritis Virus (TGEV) infections in Catalunya (northeast Spain). An antibody-capture ELISA was used for PRCV- and/or TGEV-antibodies, while a competitive inhibition ELISA tested for TGEV-specific antibodies. This study revealed 91.1% positive sera and 96.7% positive farms to PRCV and/or TGEV with a gradual increase in prevalence during 1991, which was more noticeable in small herds. Of the total 569 herds tested, 65.2% were positive only to PRCV, 8.6% were positive to TGEV and 22.8% had mixed infections. The first appearance of antibodies coincided with large importation of feeder pigs from Belgium and Holland. This prevalence is much higher than previously reported in other regions of Spain. © 1994.",,,"Bereiter, Hasler, Keller, Transmissible Gastroenteritis (TGE) in der Schweiz: Antikorperpersistenz nach Infektion und seroepidemiologische Untersuchungen zur Bedeutung des TGE-Virus als Durchfallerreger (1988) Schweiz. Arch. Tierh., 130, pp. 237-248; Brown, Paton, Serological studies of transmissible gastroenteritis in Great Britain, using a competitive ELISA (1991) Vet. Rec., 128, pp. 500-503; Callebaut, Correa, Pensaert, Jiménez, Enjuanes, Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) Journal of General Virology, 69, pp. 1725-1730; Cox, Hooyberghs, Pensaert, Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Cubero, León, Contreras, Astorga, Epidemiological enquiry by serological survey (ELISA) of transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) in the region of Murcia (Spain) (1990) Proceedings of the 11th Congress IPVS, p. 264. , Scientific Committee of the 11th IPVS Congress, 1–5 July 1990, Lausanne, Crissier-Lausanne; Dean, Dean, Burton, Dicker, (1990) Epi Info, Version 5: a word processing database, and statistics program for epidemiology on micro-computers, , USD Inc, Stone Mountain, GA; Duret, Brun, Guilmoto, Dauvergne, Isolement, identification et pouvoir pathogène chez le porc d'un coronavirus apparenté au virus de la gastro-entérite transmissible (1988) Recl. Med. Vet., 164, pp. 221-226; Henningsen, Mousing, Aalund, Porcint corona virus (PCV) i Danmark. En epidemiologisk tvaersmitsanalyse baseret pa screening-omrade sporgeskema data (1988) Dansk Vet-tidssk., 71, pp. 1168-1177; Jabrane, Elazhary, Talbot, Ethier, Dubuc, Assaf, Porcine respiratory coronavirus in Quebec Serological studies using a competitive inhibition enzyme-linked immunosorbent assay (1992) Can Vet J, 33, pp. 727-733; Jestin, Leforban, Vannier, Madec, Gourreau, Un nouveau coronavirus porcin, Études séro-épidemiologiques rétrospectives dans les lélevages de Bretagne (1987) Recl. Med. Vet., 163, pp. 567-571; Jiménez, Correa, Melgosa, Bullido, Enjuanes, Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Lanza, Rubio, Muñoz, Callebaut, Cármenes, Epidemiology of TGEV and PRCV infections in Spain (1990) Proceedings of the 11th Congress IPVS, p. 199. , Scientific Committee of the 11th IPVS Congress, 1–5 July, Lausanne, Crissier-Lausanne; Lanza, Brown, Paton, Pathogenicity of concurrent infection in pigs with porcine respiratory coronavirus and swine influenza virus (1992) Res. Vet. Sci., 53, pp. 309-314; Lanza, Rubio, Muñoz, Cármenes, Comparison of a monoclonal antibody capture ELISA (MACELISa) to indirect ELISA and virus neutralization test for the serodiagnosis of transmissible gastroenteritis virus (1993) J. Vet. Diagn. Invest., 5, pp. 21-25; Larson, (1988) Introducción a la Teoría de Probabilidades e Inferencia Estadstica, , Limusa, México D.F., México; O'Toole, Brown, Bridges, Cartwright, Pathogenicity of experimental infection with “pneumotropic” porcine coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, Callebaut, Vergote, Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Pensaert, Callebaut, Hooyberghs, Transmissible Gastroenteritis Virus in Swine: Old and New (1987) Jornadas Técnicas Expoaviga-87, pp. 40-45. , Barcelona; Vannier, Disorders induced by the experimental infection of pigs with the porcine respiratory coronavirus (PRCV) (1990) J. Vet. Med., Series B, 37, pp. 177-180; Van, Pol, Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pigs (1989) Veterinary Record, 124, pp. 43-44; Wesley, Woods, Hill, Biwer, Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Yus, Laviada, Moreno, Castro, Escribano, Simarro, Prevalencia de anticuerpos frente a virus influenza y coronavirus respiratorio en cerdos de cebo en España (1989) J. Vet. Med., Series B, 36, pp. 551-556","Martín, M.; Patologia Infecciosa i Epidemiologia, Departament de Patologia i Producció Animals, U.A.B., 08193 Bellaterra, Spain",,,01675877,,PVMEE,,"English","Prev. Vet. Med.",Article,"Final",,Scopus,2-s2.0-0008339684
"Kapil S., Trent A.M., Goyal S.M.","7003293348;7004738499;7202441793;","Antibody responses in spiral colon, ileum, and jejunum of bovine coronavirus-infected neonatal calves",1994,"Comparative Immunology, Microbiology and Infectious Diseases","17","2",,"139","149",,4,"10.1016/0147-9571(94)90039-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028275354&doi=10.1016%2f0147-9571%2894%2990039-6&partnerID=40&md5=943c4e97982b04b0337aecea8bc05c8f","Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Department of Clinical and Population Sciences, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States","Kapil, S., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Trent, A.M., Department of Clinical and Population Sciences, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Goyal, S.M., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States","A preliminary study was conducted to compare the regional intestinal immune responses of neonatal calves inoculated with virulent or attenuated bovine coronavirus (BCV) to determine the cause of reported vaccine failures. A group of 9 newborn, colostrum-deprived calves was used; two calves were inoculated with attenuated virus, four calves were infected with virulent virus (including one naturally infected calf), and three calves were uninfected controls. Calves inoculated with virulent virus produced higher titers of BCV antibodies in the intestines than those inoculated with the attenuated virus. The failure of the calves to respond to the attenuated virus was apparently due to the inability of the virus to replicate to high titers. Spiral colon, ileum, and jejunum were found to be immunologically distinct; the highest anti-BCV antibody responses were detected in spiral colon, the primary site of infection, and involved all four isotypes of bovine immunoglobulins. The antibody response in ileum was lower than in spiral colon. The immune responses developed slowly in jejunum and were associated primarily with the IgG subtypes. © 1994.","Bovine coronavirus; calf scours; enteric disease; mucosal immunity; regional immunity","bovine immunoglobulin; immunoglobulin g; vaccine; animal experiment; antibody response; antibody titer; article; colon; coronavirus; diarrhea; ileum; jejunum; male; newborn; nonhuman; virus attenuation; virus infection; virus replication; virus virulence; Animal; Animals, Newborn; Antibodies, Viral; Cattle; Cattle Diseases; Colon; Coronavirus Infections; Coronavirus, Bovine; Ileum; Immunoglobulin G; Jejunum; Male; Support, Non-U.S. Gov't; Animalia; Bovinae; Bovine coronavirus; Coronavirus","Saif, Heckert, Enteric coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , L.J. Saif, K.W. Theil, CRC Press, Boca Raton, Fla; Kapil, Pomeroy, Goyal, Trent, Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J. Vet. Diagn. Invest., 3, pp. 88-89; Thurber, Bass, Bechenhauer, Field trial evaluation of a reo-coronavirus calf diarrhea vaccine (1977) Can. J. Comp. Med., 41, pp. 131-136; De Leeuw, Tiessink, Laboratory experiments on oral vaccination of calves against rotavirus or coronavirus induced diarrhea (1985) Zbl. Vet. Med., 32, pp. 55-64; Deregt, Gifford, Ijaz, Watts, Gilchrist, Haines, Babiuk, Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3 demonstration of in vivo virus neutralizing activity (1989) Journal of General Virology, 70, pp. 993-998; Offit, Clark, Protection against rotavirus-induced gastroenteritis in a murine model by passively acquired gastrointestinal but not circulating antibodies (1985) J. Virol., 54, pp. 58-64; Kapil, Trent, Goyal, Excretion and persistence of bovine coronavirus in neonatal calves (1990) Arch. Virol., 115, pp. 127-132; Saif, Redman, Moorhead, Theil, Experimentally induced infections in calves: viral replication in the respiratory and intestinal tracts (1986) Am. J. Vet. Res., 47, pp. 1426-1432; Heckert, Saif, Mengel, Myers, Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces, and mucosal secretions from experimentally challenge-exposed colostrum-deprived calves (1991) Am. J. Vet. Res., 52, pp. 692-699; Kapil, Secretory immune response to foot-and-mouth disease virus type Asia 1 vaccine (1985) MVSc Thesis, , Haryana Agricultural University, Hisar, India; Banks, (1993) Applied Veterinary Histology, pp. 277-297. , Williams & Wilkins, Baltimore, Maryland, U.S.A; Srikumaran, Goldsby, Guidry, Hague, Onisk, Srikumaran, Library of monoclonal bovine immunoglobulins and monoclonal antibodies to bovine immunoglobulins (1987) Hybridoma, 6, pp. 527-530; Kimman, Van Zaane, Isotype-specific ELISAs for the detection of antibodies to bovine respiratory syncytial virus (1987) Res. Vet. Sci., 43, pp. 180-187","Goyal, S.M.; Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States",,,01479571,,CIMID,"7924247","English","Comp. Immunol. Microbiol. Infect. Dis.",Article,"Final",,Scopus,2-s2.0-0028275354
"Kapil S., Goyal S.M., Trent A.M.","7003293348;7202441793;7004738499;","Cellular immune status of coronavirus-infected neonatal calves",1994,"Comparative Immunology, Microbiology and Infectious Diseases","17","2",,"133","138",,1,"10.1016/0147-9571(94)90038-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028237926&doi=10.1016%2f0147-9571%2894%2990038-8&partnerID=40&md5=8cff729fe0c08877d74c254c4de55e56","Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Department of Clinical and Population Sciences, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States","Kapil, S., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Goyal, S.M., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States; Trent, A.M., Department of Clinical and Population Sciences, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States","A preliminary study was conducted to determine the cellular immune status of neonatal, colostrum-deprived calves following inoculation with either attenuated or virulent bovine coronavirus (BCV). Uninfected calves served as controls. To determine the intestinal and systemic cellular immune status, we performed MHC-restricted cytotoxic lymphocyte (CTL) assay on mesenteric lymphocytes, enumerated T cell subsets in peripheral blood lymphocytes, and examined histopathological alterations in mesenteric lymph nodes and gut-associated lymphoid tissue. Target cells for the CTL assay were autologous testicular cells and effector cells were mesenteric lymphocytes from calves infected with BCV. No appreciable specific lysis was observed in any group of calves indicating the absence of demonstrable CTL responses. The TC/TS population was severely depressed in the calf inoculated with the virulent virus but not in those inoculated with either the attenuated virus or placebo. The mesenteric lymph nodes and Peyer's patches of calves inoculated with the virulent virus showed severe depletion of lymphocytes. These calves developed intestinal antibody responses in the acute phase of infection (1 week after infection) but were immunosuppressed in the later stage of infection. © 1994.","Bovine coronavirus; calf scours; cellular immunity; immunosuppression; T lymphocytes","animal experiment; antibody response; article; assay; cattle; cellular immunity; colostrum; controlled study; coronavirus; cytotoxic lymphocyte; effector cell; histopathology; immune response; immune status; inoculation; lymphocyte count; lymphoid tissue; lysis; major histocompatibility complex; male; mesentery lymph node; newborn; nonhuman; peripheral lymphocyte; peyer patch; t lymphocyte subpopulation; target cell; virus attenuation; virus infection; Animal; Animals, Newborn; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Cytotoxicity Tests, Immunologic; Immunity, Cellular; Male; Support, Non-U.S. Gov't; T-Lymphocyte Subsets; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus","Saif, Heckert, Enteric coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , L.J. Saif, K.W. Theil, CRC Press, Boca Raton, Fla; Torres-Medina, Schlafer, Mebus, Rotaviral and coronaviral diarrhea (1985) Vet. Clin. N. Am., Food Anim. Pract., 1, pp. 471-493; Saif, Development of nasal, fecal, and serum isotype-specific antibodies in calves challenged with bovine coronavirus or rotavirus (1987) Vet. Immunol. Immunopathol., 17, pp. 425-439; Kapil, Trent, Goyal, Antibody responses in spiral colon, ileum, and jejunum of bovine coronavirus infected calves (1994) Comp. Immunol. Microbial. Infect. Dis., 17, pp. 139-149; Kapil, Pomeroy, Goyal, Trent, Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J. Vet. Diagn. Invest., 3, pp. 88-89; Kapil, Trent, Goyal, Excretion and persistence of bovine coronavirus in neonatal calves (1990) Arch. Virol., 115, pp. 127-132; Baldwin, Teale, Naessens, Goddeeris, MacHugh, Morrison, Characterization of a subset of bovine T lymphocytes that express BoT4 by monoclonal antibodies and function: Similarity to lymphocytes defined by human T4 and murine L3T4 (1986) J. Immunol., 136, pp. 4385-4391; Ellis, Baldwin, MacHugh, Bensaid, Teale, Goddeeris, Morrison, Characterization by a monoclonal antibody and functional analysis of a subset of bovine T lymphocytes that express BoT8, a molecule analogous to human CD8 (1986) Immunology, 58, pp. 351-358; Rose, Friedman, (1980) Manual of Clinical Immunology, , American Society for Microbiology, Washington, D.C; Huegin, Cerny, Zinkernagel, Neftel, Suppressive effects of beta-lactam-antibiotics on in vitro generation of cytotoxic T cells (1986) Int. J. Immunopharmacol., 8, pp. 723-729; Campos, Rossi, In vitro induction of cytotoxic lymphocytes from infectious bovine rhinotracheitis virus hyperimmune cattle (1986) Am. J. Vet. Res., 47, pp. 2411-2414; Godson, Campos, Babiuk, Non-major histocompatibility complex-restricted cytotoxicity of bovine coronavirus-infected target cells mediated by bovine intestinal intraepithelial leukocytes (1991) J. Gen. Virol., 72, pp. 2457-2465; Shimizu, Shimizu, Demonstration of cytotoxic lymphocytes to virus-infected target cells in pigs inoculated with transmissible gastroenteritis virus (1979) Am. J. Vet. Res., 40, pp. 208-213; Carman, Ernst, Rosenthal, Clark, Befus, Bienenstock, Intraepithelial leukocytes contain a unique subpopulation of NK-like cytotoxic cells active in the defense of gut epithelium to enteric murine coronavirus (1986) J. Immunol., 136, pp. 1548-1553; Mebus, Stair, Rhodes, Twiehaus, Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet. Pathol., 10, pp. 45-64; Sharma, Dupuy, Lamontagnel, Immunosuppression by avian infectious bursal disease virus and mouse hepatitis virus (1990) Virus Induced Immunosuppression, pp. 201-216. , S. Spector, M. Bendinelli, H. Friedman, Plenum Press, New York","Goyal, S.M.; Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St Paul, MN 55108, United States",,,01479571,,CIMID,"7924246","English","Comp. Immunol. Microbiol. Infect. Dis.",Article,"Final",,Scopus,2-s2.0-0028237926
"Alexander L.K., Keene B.W., Small J.D., Yount Jr. B., Baric R.S.","36812461600;7006043632;7202783844;6603564156;7004350435;","Electrocardiographic changes following rabbit coronavirus-induced myocarditis and dilated cardiomyopathy",1994,"Advances in Experimental Medicine and Biology","342",,,"365","370",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028353255&partnerID=40&md5=5ea706774162ee22dd84e31037b1e1e9","Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Alexander, L.K., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Keene, B.W., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Small, J.D., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Yount Jr., B., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Baric, R.S., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Rabbit Coronavirus (RbCV) infection was divided into two phases based upon day of death and pathologic findings. During the acute phase (days 2-5) heart weights (HW) and heart weight-to-body weight (HW/BW) ratios were increased with striking dilation of the right ventricle. These changes as well as increased dilation of the left ventricle were especially pronounced during the subacute phase (days 6-12). Myocytolysis, pulmonary edema, and degeneration and necrosis of myocytes, were seen during both phases. Myocarditis, pleural effusion, calcification of myocytes, and congestion in the liver and lungs were seen in the subacute phase. Electrocardiograms (ECGs) exhibited low voltage, nonspecific ST-T wave changes, sinus tachycardia, occasional ventricular and supraventricular premature complexes and 2° AV block consistent with myocarditis and heart failure. Forty-one percent of the survivors exhibited increased HW and HW/BW ratios, biventricular dilation, interstitial and replacement fibrosis, myocyte hypertrophy and myocarditis. ECGs exhibited nonspecific ST-T wave changes, sinus arrhythmia, occasional ventricular and supraventricular premature complexes and 2° AV block. These data suggest that RbCV infection may result in viral myocarditis and heart failure with a proportion of survivors progressing into DCM.",,"animal model; animal tissue; atrioventricular block; conference paper; congestive cardiomyopathy; controlled study; coronavirus; electrocardiography; heart failure; heart ventricle extrasystole; heart ventricle hypertrophy; heart weight; male; nonhuman; priority journal; rabbit; sinus arrhythmia; st segment; supraventricular premature beat; t wave; virus myocarditis; Acute Disease; Animal; Arrhythmia; Body Weight; Cardiomyopathy, Congestive; Convalescence; Coronavirus Infections; Electroencephalography; Male; Myocarditis; Myocardium; Organ Weight; Pleural Effusion; Pulmonary Edema; Rabbits",,"Alexander, L.K.; Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States",,,00652598,,AEMBA,"8209755","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028353255
"Imrich H., Schwender S., Hein A., Dörries R.","6602841707;7003953447;8047618900;7003359298;","Cervical lymphoid tissue but not the central nervous system supports proliferation of virus-specific T lymphocytes during coronavirus-induced encephalitis in rats",1994,"Journal of Neuroimmunology","53","1",,"73","81",,14,"10.1016/0165-5728(94)90066-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027938639&doi=10.1016%2f0165-5728%2894%2990066-3&partnerID=40&md5=209a094e82c25d21be3d48af76f9aa88","Institut für Virologie, Immunbiologie der Universität Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Zentrallabor der Medizinischen Klinik der Universität Würzburg, Würzburg, Germany","Imrich, H., Institut für Virologie, Immunbiologie der Universität Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Schwender, S., Zentrallabor der Medizinischen Klinik der Universität Würzburg, Würzburg, Germany; Hein, A., Institut für Virologie, Immunbiologie der Universität Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Dörries, R., Institut für Virologie, Immunbiologie der Universität Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany","The CD4+ T lymphocyte response in the central nervous system (CNS) and cervical lymph nodes (CLNs) of rats with different susceptibility to coronavirus-induced encephalitis was investigated. The majority of CD4+ T lymphocytes entering the virus-infected CNS in the course of the infection are primed cells that neither proliferate ex vivo nor can be stimulated to proliferation by viral antigens or mitogen in vitro. In contrast, T lymphocytes taken from CLNs of the same animals revealed a strong proliferative response. Restimulation of CLN lymphocytes by viral antigens disclosed a striking difference between the disease-resistant rat strain Brown Norway (BN) and the susceptible Lewis (LEW) strain. Whereas BN lymphocytes responded as early as 5 days post infection, it took more than 11 days until a comparable proliferation was detectable in LEW lymphocytes. From these data we postulate that the majority of T lymphocytes entering the virus-infected brain after sensitisation and expansion in cervical lymph nodes is unresponsive to further proliferation signals and that the kinetics and magnitude of T lymphocyte stimulation in CLNs play an important role in the clinical course of the infection. © 1994.","Central nervous system; Cervical lymph nodes; Proliferation; T cells; Viral encephalitis","cd4 antigen; animal experiment; animal model; animal tissue; article; central nervous system; controlled study; coronavirus; encephalitis; lymphocyte proliferation; lymphoid tissue; nonhuman; priority journal; rat; Animal; Brain; CD4-Positive T-Lymphocytes; Coronavirus; Coronavirus Infections; Encephalitis; Lymph Nodes; Lymphocyte Activation; Rats; Rats, Inbred BN; Rats, Inbred Lew; Receptors, Antigen, T-Cell, alpha-beta; Support, Non-U.S. Gov't; T-Lymphocytes","Cross, Cannella, Brosnan, Raine, Hypothesis: Antigen-specific T cells prime central nervous system endothelium for recruitment of nonspecific inflammatory cells to effect autoimmune demyelination (1991) J. Neuroimmunol., 33, pp. 237-244; Cserr, Knopf, Cervical lymphatics, the blood-brain barrier and the immunoreactivity of the brain: a new view (1992) Immunol. Today, 13, pp. 507-512; Doherty, Allan, Lynch, Ceredig, Dissection of an inflammatory process induced by CD8+ T cells (1990) Immunol. Today, 11, pp. 55-59; Dörries, Watanabe, Wege, ter Meulen, Murine coronavirus induced encephalomyelitides in rats: Analysis of immunoglobulins and virus-specific antibodies in serum and cerebrospinal fluid (1986) J. Neuroimmunol., 12, pp. 131-142; Dörries, Schwender, Imrich, Harms, Population dynamics of lymphocyte subsets in the CNS of rats with different susceptibility to coronavirus-induced demyelinating encephalitis (1991) Immunology, 74, pp. 539-545; Frei, Siepl, Groscurth, Bodmer, Schwerdel, Fontana, Antigen presentation and tumor cytotoxicity by interferon-γ-treated microglial cells (1987) Eur. J. Immunol., 17, pp. 1271-1278; Griffin, Levine, Tyor, Irani, The immune response in viral encephalitis (1992) Semin. Immunol., 4, pp. 111-119; Harling-Berg, Knopf, Merriam, Cserr, Role of cervical lymph nodes in the systemic humoral immune response to human serum albumin microinfused into rat cerebrospinal fluid (1989) J. Neuroimmunol., 25, pp. 185-193; Hayes, Woodroofe, Cuzner, Microglia are the major cell type expressing MHC class II in human white matter (1987) J. Neurol. Sci., 80, pp. 25-37; Hickey, Kimura, Perivascular microglia cells of the CNS are bone marrow derived and present antigen in vivo (1988) Science, 239, pp. 290-292; Holt, Downregulation of immune responses in the lower respiratory tract: role of alveolar macrophages (1986) Clin. Exp. Immunol., 63, pp. 261-270; Hünig, Wallny, Hartley, Lawetzky, Tiefenthaler, A monoclonal antibody to a constant determinant of the rat T cell antigen receptor that induces T cell activation (1989) J. Exp. Med., 169, pp. 73-86; Lowe, MacLennan, Powe, Pound, Palmer, Microglial cells in human brain have phenotypic characteristics related to possible function as dendritic antigen presenting cells (1989) J. Pathol., 159, pp. 143-149; McCombe, Fordyce, de Jersey, Yoong, Pender, Expression of CD45RC and Ia antigen in the spinalcord in acute experimental allergic encephalomyelitis: an immunocytochemical and flow cytometric study (1992) J. Neurol. Sci., 113, pp. 177-186; Matsumoto, Hara, Tanaka, Fujiwara, Immunohistochemical analysis of the rat central nervous system during experimental allergic encephalomyelitis, with special reference to Ia-positive cells with dendritic morphology (1986) J. Immunol., 136, pp. 3668-3676; Matsumoto, Ohmori, Fujiwara, Immune regulation by brain cells in the central nervous system: microglia but not astrocytes present myelin basic protein to encephalitogenic T cellsv under in vivo-mimicking conditions (1992) Immunology, 76, pp. 209-216; Morimoto, Letvin, Boyd, Hagan, Brown, Kornacki, Schlossman, The isolation and characterization of the human helper inducer T cell subset (1985) J. Immunol., 134, pp. 3762-3769; Nelson, Strickland, Holt, Selective attrition of non-recirculating T cells during normal passage through the lung vascular bed (1990) Immunology, 69, pp. 476-481; Ohmori, Hong, Fujiwara, Matsumoto, In situ demonstration of proliferating cells in the rat central nervous system during experimental autoimmune encephalomyelitis. Evidence suggesting suggesting that most infiltrating T cells do not proliferate in the target organ (1992) J. Lab. Invest., 66, pp. 54-62; Paterson, Jefferies, Green, Brandon, Corthesy, Puklavec, Williams, Antigens of activated rat T lymphocytes including a molecule of 50 000 Fr detected only on CD4 positive T blasts (1987) Mol. Immunol., 24, pp. 1281-1290; Schmied, Breitschopf, Gold, Zischler, Rothe, Wekerle, Lassmann, Apoptosis of T lymphocytes in experimental autoimmune encephalomyelitis. Evidence for programmed cell death as a mechanism to control inflammation in the brain (1993) Am. J. Pathol., 143, pp. 446-452; Schwender, Imrich, Dörries, The pathogenic role of virus-specific antibody secreting cells in the central nervous system of rats with different susceptibility to coronavirus-induced demyelinating encephalitis (1991) Immunology, 74, pp. 533-538; Sedgwick, Dörries, The immune system response to viral infection of the CNS (1991) Sem. Neurosci., 3, pp. 93-100; Sedgwick, Schwender, Imrich, Dörries, Butcher, ter Meulen, Isolation and direct characterization of resident microglial cells from the normal and inflamed nervous system (1991) Proc. Natl. Acad. Sci., 88, pp. 7438-7442; Spickett, Brandon, Mason, Williams, Woollett, MRC OX-22, a monoclonal antibody that labels a new subset of T lymphocytes and reacts with the high molecular weight form of the leucocyte-common antigen (1983) J. Exp. Med., 158, pp. 795-810; Watanabe, Wege, ter Meulen, Comparative analysis of coronavirus JHM-induced demyelinating encephalomyelitis in Lewis and Brown Norway rats (1987) Lab. Invest., 57, pp. 375-384; Wege, Müller, ter Meulen, Genomic RNA of murine coronavirus JHM (1978) J. Gen. Virol., 41, pp. 217-227; Weinstein, Walker, Akiyama, McGeer, Herpes simplex virus type I infection of the CNS induces major histocompatibility complex antigen expression on rat microglia cell (1990) J. Neurosci. Res., 26, pp. 55-65; Wekerle, Linnington, Lassmann, Meyermann, Cellular immune reactivity within the CNS (1986) Trends Neurosci., 9, pp. 271-277; Wong, Bartlett, Clark-Lewis, McKimm-Breschkin, Schrader, Interferon-γ induces the expression of H-2 and I-a antigens on brain cells (1985) J. Neuroimmunol., 7, pp. 255-278; Williams, Galfre, Milstein, Analysis of cell surfaces by xenogenic myeloma-hybrid antibodies: differentiation antigens of rat lymphocytes (1977) Cell, 12, pp. 663-673; Williams, Bar-Or, Ulvestad, Olivier, Antel, Yong, Biology of adult human microglia in culture: comparisons with peripheral blood monocytes and astrocytes (1992) J. Neuropathol. Exp. Neurol., 51, pp. 538-549; Williamson, Virus-specific T cells in the central nervous system following infection with an avirulent neurotropic mouse hepatitis virus (1992) Reg. Immunol., 4, pp. 145-152","Imrich, H.; Institut für Virologie, Immunbiologie der Universität Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany",,,01655728,,JNRID,"7914212","English","J. Neuroimmunol.",Article,"Final",Open Access,Scopus,2-s2.0-0027938639
"Herold J., Raabe T., Siddell S.G.","7006838690;56250084700;7005260816;","Characterization of the human coronavirus 229E (HCV 229E) gene 1",1994,"Advances in Experimental Medicine and Biology","342",,,"75","79",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028265962&partnerID=40&md5=04259b4e83138cf0e2f0e782a3ad19b4","Institut fur Virologie, Universitat Wurzburg, Versbacherstr.7, 8700 Wurzburg, Germany","Herold, J., Institut fur Virologie, Universitat Wurzburg, Versbacherstr.7, 8700 Wurzburg, Germany; Raabe, T., Institut fur Virologie, Universitat Wurzburg, Versbacherstr.7, 8700 Wurzburg, Germany; Siddell, S.G., Institut fur Virologie, Universitat Wurzburg, Versbacherstr.7, 8700 Wurzburg, Germany","The sequence of the HCV 229E gene 1 has been determined and compared with the homologous sequences of the murine hepatitis virus and the avian infectious bronchitis virus. The coding sequence of gene 1 is 20 273 nucleotides in length. Within this coding region are two large open reading frames, ORF 1a (4 086 codons) and ORF 1b (2 687 codons) which overlap by 40 nucleotides. In the overlapping region, the genomic RNA can be folded into a pseudoknot structure, an element which is known to mediate -1 ribosomal frame-shifting in other coronaviruses. Assuming that -1 frame-shifting occurs at the HCV sequence UUUAAAC (nucleotides 12 514 - 12 520), the ORF 1a - ORF 1b product is predicted to be 6 758 amino acids in length. Our sequence analysis of the HCV 229E gene 1 has revealed a high degree of similarity within the ORF 1b of HCV, MHV and IBV, whereas ORF 1a is much less conserved. Elements which are believed to be necessary for specific (e.g. frame- shifting) and general (e.g. NTP-binding/helicase) transcriptional functions have been identified. This study completes the genomic sequence of HCV 229E which is 27.27 kb long and one of the largest known RNA genomes.",,"virus rna; animal cell; avian infectious bronchitis virus; conference paper; coronavirus; frameshift mutation; gene sequence; murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; rna structure; sequence homology; virus genome; Base Sequence; Comparative Study; Coronavirus; Coronavirus 229E, Human; DNA, Complementary; Genes, Structural, Viral; Infectious bronchitis virus; Molecular Sequence Data; Murine hepatitis virus; Open Reading Frames; Protein Processing, Post-Translational; RNA, Viral; Species Specificity; Viral Proteins",,"Herold, J.; Institut fur Virologie, Universitat Wurzburg, Versbacherstr.7, 8700 Wurzburg, Germany",,,00652598,,AEMBA,"8209774","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028265962
"De Diego M., Rodriguez F., Alcaraz C., Gomez N., Alonso C., Escribano J.M.","7004243972;56415175900;7003388538;57212697516;7201579122;55402647000;","Characterization of the IgA and subclass IgG responses to neutralizing epitopes after infection of pregnant sows with the transmissible gastroenteritis virus or the antigenically related porcine respiratory coronavirus",1994,"Journal of General Virology","75","10",,"2585","2593",,9,"10.1099/0022-1317-75-10-2585","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027935955&doi=10.1099%2f0022-1317-75-10-2585&partnerID=40&md5=b8246449d0c2c286267a456c0ab52236","CISA-INIA, Valdeolmos, 28130 Madrid, Spain","De Diego, M., CISA-INIA, Valdeolmos, 28130 Madrid, Spain; Rodriguez, F., CISA-INIA, Valdeolmos, 28130 Madrid, Spain; Alcaraz, C., CISA-INIA, Valdeolmos, 28130 Madrid, Spain; Gomez, N., CISA-INIA, Valdeolmos, 28130 Madrid, Spain; Alonso, C., CISA-INIA, Valdeolmos, 28130 Madrid, Spain; Escribano, J.M., CISA-INIA, Valdeolmos, 28130 Madrid, Spain","In this study, we have investigated the characteristics of secreted IgA and other classes of Ig induced after vaccination of sows with transmissible gastroenteritis virus (TGEV) or the antigenically related porcine respiratory coronavirus (PRCV). Both viruses induced the secretion of neutralizing antibodies of different classes in the sows' milk, but these protected suckling piglets against TGEV to different degrees. Quantitative differences in the induction of IgA by both viruses were found among the different viral antigenic sites and subsites of glycoprotein S. In TGEV-vaccinated sows, antigenic subsite A was the best inducer of IgA, followed by antigenic site D. After vaccination with PRCV, lower levels of IgA were detected on colostrum and milk, antigenic site D and subsite Ab being the immunodominant sites. This quantitative difference in epitope recognition could explain the differences in newborn piglet protection found using Ig classes purified from the milk of sows immunized with both viruses. Apparently only IgA recognizing at least antigenic sites A and D confers good protection in vivo, whereas any Ig class recognizing only one antigenic site may neutralize the virus in cell culture. These results indicate that the formulation of a subunit vaccine against TGEV has to consider the inclusion of more than one antigenic site involved in virus neutralization.",,"epitope; immunoglobulin; immunoglobulin A; immunoglobulin G; neutralizing antibody; vitronectin; animal cell; antibody combining site; antibody production; article; cell culture; colostrum; controlled study; Coronavirus; Enterovirus; immune response; milk; molecular recognition; nonhuman; pregnancy; priority journal; purification; vaccination; virus infection; virus neutralization; Animalia; Coronavirus; Enterovirus; Porcine respiratory coronavirus; Suidae; Transmissible gastroenteritis virus",,"De Diego, M.; CISA-INIA, Valdeolmos, 28130 Madrid, Spain",,"Microbiology Society",00221317,,JGVIA,"7523577","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0027935955
"Cabirac G.F., Soike K.F., Butunoi C., Hoel K., Johnson S., Cai G.-Y., Murray R.S.","6602498805;7006220553;6507828683;6602461039;57207906756;57199040369;7403022204;","Coronavirus JHM OMP1 pathogenesis in owl monkey CNS and coronavirus infection of owl monkey CNS via peripheral routes",1994,"Advances in Experimental Medicine and Biology","342",,,"347","352",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028328618&partnerID=40&md5=dbf5235a6afd91765000f2f73ef3cdc9","Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States","Cabirac, G.F., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Soike, K.F., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Butunoi, C., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Hoel, K., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Johnson, S., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Cai, G.-Y., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States; Murray, R.S., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States","Two separate studies are described in this report. First, 5 Owl monkeys were inoculated intracerebrally (IC) with coronavirus JHM OMP1; this virus isolate was cultured from the brain of an animal inoculated with uncloned MHV JHM. Two of the animals became neurological impaired and were sacrificed; these animals had developed severe encephalomyelitis as previously described. Two of the remaining 3 healthy animals were inoculated IC again at 90 days post-inoculation (DPI) and all 3 were sacrificed approximately 5 months after the first virus inoculation. Despite the lack of detectable infectious virus, viral RNA and antigen, all 3 animals had significant white matter inflammation and areas of demyelination in the spinal cord. In the second study 4 Owl monkeys were inoculated intranasally (IN) and ocularly and 4 inoculated intravenously (IV) with JHM OMP1. The animals were sacrificed between 16 and 215 DPI with 2 IN and 2 IV animals receiving a second IV inoculum at 152 DPI. Viral RNA and/or antigen was detected in the brains of all animals and the distribution corresponded to areas of inflammation and edema. One of the animals that received the second inoculum developed neurological impairment and subsequent analysis of tissues showed viral antigen in both brain and spinal cord. Viral products were predominantly found in blood vessels suggesting hematogenous spread with entry into the central nervous system (CNS) through endothelium.",,"virus antigen; virus rna; animal model; animal tissue; brain edema; central nervous system infection; conference paper; controlled study; coronavirus; demyelinating disease; encephalitis; immunohistochemistry; inoculation; monkey; nonhuman; priority journal; virus infection; white matter; Administration, Intranasal; Animal; Antigens, Viral; Aotinae; Astrocytes; Brain; Brain Edema; Cornea; Coronavirus; Coronavirus Infections; Demyelinating Diseases; Encephalomyelitis; Gliosis; Injections; Injections, Intravenous; Meningitis, Viral; RNA, Viral; Spinal Cord; Viremia",,"Cabirac, G.F.; Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, Englewood, CO 80150, United States",,,00652598,,AEMBA,"8209752","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028328618
"Taguchi F., Ikeda T., Saeki K., Kubo H., Kikuchi T.","7103209890;7404132888;36854828200;55183402000;7402098274;","Fusogenic properties of uncleaved spike protein of murine coronavirus JHMV",1994,"Advances in Experimental Medicine and Biology","342",,,"171","175",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028218973&partnerID=40&md5=ab3e7b28bbbe7f304c330a1d74e7a3e4","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Ikeda, T., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Saeki, K., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Kubo, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Kikuchi, T., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","We have tested the fusogenic properties of cleaved and uncleaved spike (S) protein of murine coronavirus (MCV) JHMV variant cl-2 by expressing the S protein by recombinant vaccinia viruses (RVVs). The amino acid sequence of the putative cleavage site of cl-2 S protein, Arg-Arg-Ala-Arg-Arg, was replaced by Arg-Thr-Ala-Leu-Glu by in vitro mutagenesis of cl-2 S gene. The RVVs having cl-2 S gene [RVV t(+)] or mutated cl-2 S gene [RVV t(-)] were tested for their ability to induce fusion as well as cleavability in DBT cells. After inoculation with RVV t(+) onto DBT cells, the fusion formation was first observed at 8 h postinoculation (p.i.) and spread throughout the whole culture by 24 h. In cells infected with RVV t(-), fusion appeared by 2 h and most of cells were fused by 30 h p.i. The S protein and its cleavage products were detected in DBT cells expressing wild type S protein. However, no cleavage products of the S protein were detected in RVV t(-) infected cells producing mutated S protein, even though fusion was clearly visible. These results suggest that the cleavage event of JHMV-S protein of MCV is not a prerequisite for fusion formation, but that it enhances fusion.",,"hybrid protein; virus protein; amino acid sequence; animal cell; conference paper; immunoblotting; immunoprecipitation; murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; Amino Acid Sequence; Animal; Astrocytoma; Base Sequence; Cell Fusion; Cytopathogenic Effect, Viral; Endopeptidases; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Support, Non-U.S. Gov't; Tumor Cells, Cultured; Viral Envelope Proteins",,"Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,00652598,,AEMBA,"8209726","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028218973
"Collins A.R.","24439435400;","Human coronavirus OC43 interacts with major histocompatibility complex class I molecules at the cell surface to establish infection",1994,"Immunological Investigations","23","4-5",,"313","321",,11,"10.3109/08820139409066826","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027992655&doi=10.3109%2f08820139409066826&partnerID=40&md5=8c91557dfeabc748cb608064409a38c4","Department of Microbiology School of Medicine, State University of New York, Buffalo, United States","Collins, A.R., Department of Microbiology School of Medicine, State University of New York, Buffalo, United States","Human coronaviruses have been associated with common colds, diarrhea and enterocolitis, and have been implicated in multiple sclerosis. HLA class I molecules may play a critical role as receptor for OC43 because monoclonal antibody (mAb)W6/32 to HLA-A, -B and -C specificities completely blocks infectivity in human rhabdomyosarcoma (RD) cells. The role of HLA class 1 antigen as the virus receptor was examined using HLA-A3.1 stably transfected human plasma cells and untransfected HMY.C1R cells which do not express HLA-A and -B molecules. When the cells (5x106) were infected at a multiplicity of one, the HLA.A3 transfected cells produced 108 PFU of virus whereas no replication occurred in the HMY.C1R cells mAb W6/32 reduced the virus yield by 99.9% Cell membranes from HMY.C1R, HMY.A3 cells and chicken erythrocytes were biotinylated as live cells. Immunoprecipitation with polyclonal antiviral antibody to detect binding of biotinylated cell membranes to virus revealed that biotinylated HMY.A3 membranes co-precipitated with virus-antibody complexes when the immunoprecipitates were electrophoresed on SDS-PAGE gel, electroblotted and stained with Avidin-horseradish peroxidase. The results provide direct evidence that OC43 virus can recognize HLA class I as receptor on the cell surface. © 1994 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.","HLA Class I receptor - OC43 virus Interaction","major histocompatibility antigen class 1; virus receptor; animal cell; article; cell surface; coronavirus; human; human cell; nonhuman; priority journal; virus cell interaction; virus infection; Coronavirus; Coronavirus Infections; Coronavirus OC43, Human; HLA-A3 Antigen; Human; Precipitin Tests; Receptors, Virus; Support, Non-U.S. Gov't; Transfection; Tumor Cells, Cultured; Virus Replication","Larson, H.E., Reed, S.A., Tyrrell, D.A.J., (1980) J. Med. Virol, 5, pp. 221-229; Gerna, G., Passarini, N., Cerida, P.M., Battaglia, M., (1984) J. Infect. Dis, 150, p. 618; Sureau, C., Amul-Tison, C., Mascovici, O., Lebon, P., Laporte, J., Chany, C., (1980) Bull. Acad. Nat. Med, 164, pp. 286-293; Murray, R.S., Brown, B., Brian, D., Caberac, G.F., (1992) Annals of Neurol, 31, pp. 525-533; Lai, M.M.C., (1990) Ann. Rev. Microb, 44, pp. 303-333; Kunkel, F., Herler, G., (1993) Virol, 195, pp. 195-202; Collins, A.R., (1993) Immunol. Invest, 22, pp. 95-103; Silver, M.L., Parker, K.C., Wiley, D.C., (1991) Nature, 350, pp. 619-622; Takashi, K., L-Dai, C., Fuerst, T.R., Biddison, W.E., Earl, P.L., Moss, B., Ennis, F.A., (1991) Proc. Natl. Acad. Sci, 88, pp. 10277-10281; Berger, A.E., Davis, J.E., Crosswell, P., (1982) Hybridoma, 1, pp. 89-90; Busch, G., Hoder, D., Reutter, W., Tauber, R., (1989) European J. Cell Biol, 50, pp. 257-262; Laemmli, U.K., (1970) Nature, 227, pp. 680-685; Towbin, H., Stalhelin, T., Gordon, J., (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354; Ausubel, F.M., (1987) Current Protocols in Molecular Biology, pp. 10-16. , Green Publishing Associates and Wiley Intersciences New York; Haywood, A.M., (1994) J. Virol, 68, pp. 1-5; Helenius, A., Morein, B., Fries, E., Simons, K., Robinson, P., Schirrmacher, V., Terhorst, C., Strominger, J.L., (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 3846-3850; Wykes, M.N., Shellam, G.R., McCluskey, J., Kast, W.M., Dallas, P.B., Price, P., (1993) J. Virol, 67, pp. 4182-4189; Compton, S.R., Stephenson, C.R., Snyder, S.W., Weismuller, D.G., Holmes, K.V., (1992) J. Virol, 66, pp. 7420-7428; Kuby, J., (1992) Immunology, p. 117. , W.H. Freeman & Co. New York","Collins, A.R.; Department of Microbiology School of Medicine, State University of New York, Buffalo, United States",,"Informa Healthcare",08820139,,IMINE,"7959963","English","Immunol. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0027992655
"Van Reeth K., Pensaert M.B.","57191565576;55905425400;","Porcine respiratory coronavirus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs.",1994,"American journal of veterinary research","55","9",,"1275","1281",,28,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028509383&partnerID=40&md5=6e87ff05d73ba953a2b6a579950ab47a","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Belgium","Van Reeth, K., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Belgium; Pensaert, M.B., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Belgium","Effect of prior porcine respiratory coronavirus (PRCV) infection on replication of H1N1-influenza virus in the respiratory tract of swine was studied. In an initial experiment, 3 groups of 5 feeder pigs were studied. Pigs of 2 groups were inoculated sequentially with PRCV, followed by H1N1-influenza virus at 2- and 3-day intervals. Pigs of the other group were inoculated with H1N1-influenza virus only. Pigs were monitored clinically and examined for nasal excretion of influenza virus. In the singly influenza virus-inoculated group, 83% of nasal swab specimens were influenza virus-positive over a period of 6 days after inoculation. In the dually virus-inoculated groups, only 27% (2-day interval) and 53% (3-day interval) of nasal swab specimens were virus-positive over the same postinoculation period. However, clinical signs of infection in these dually inoculated pigs were more severe than those in the singly influenza virus-inoculated pigs. There were no significant differences in antibody responses against influenza virus among the 3 groups of pigs. In a second experiment, 2 groups of pigs were studied. One group of pigs was inoculated sequentially with PRCV, followed by H1N1-influenza virus 2 days later; the other group was inoculated with H1N1-influenza virus only. Pigs of both groups were serially euthanatized on postinoculation days (PID) 1, 2, 3, and 4 (after influenza virus). At necropsy, influenza virus titer and immunofluorescence in lung tissue were determined and gross lung lesions were recorded.(ABSTRACT TRUNCATED AT 250 WORDS)",,"animal; article; body temperature; cell culture; Coronavirus; Influenza virus A; isolation and purification; lung; male; Orthomyxovirus infection; pathophysiology; physiology; respiratory system; swine; testis; virology; virus infection; virus replication; virus shedding; Animals; Body Temperature; Cells, Cultured; Coronavirus; Coronavirus Infections; Influenza A virus; Lung; Male; Orthomyxoviridae Infections; Respiratory System; Swine; Testis; Virus Replication; Virus Shedding",,"Van Reeth, K.",,,00029645,,,"7802396","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028509383
"Liao C.-L., Lai M.M.C.","7401957370;7401808497;","Requirement of the 5'-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription",1994,"Journal of Virology","68","8",,"4727","4737",,56,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028234463&partnerID=40&md5=18d20fe9c55c38ddc26f43cb6652912d","Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States","Liao, C.-L., Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States","We have developed a defective interfering (DI) RNA containing a chloramphenicol acetyltransferase reporter gene, placed behind an intergenic sequence, for studying subgenomic mRNA transcription of mouse hepatitis virus (MHV), a prototype coronavirus. Using this system, we have identified the sequence requirement for MHV subgenomic mRNA transcription. We show that this sequence requirement differs from that for RNA replication. In addition to the previously identified requirement for an intergenic (promoter) sequence, additional sequences from the 5' end of genomic RNA are required for subgenomic mRNA transcription. These upstream sequences include the leader RNA and a spacer sequence between the leader and intergenic sequence, which is derived from the 5' untranslated region and part of gene 1. The spacer sequence requirement is specific, since only the sequence derived from the 5' end of RNA genome, but not from other MHV genomic regions or heterologous sequences, could initiate subgenomic transcription from the intergenic sequence. These results strongly suggest that the wild-type viral subgenomic mRNAs (mRNA2 to mRNA7) and probably their counterpart subgenomic negative- sense RNAs cannot be utilized for mRNA amplification. Furthermore, we have demonstrated that a partial leader sequence present at the 5' end of genome, which lacks the leader-mRNA fusion sequence, could still support subgenomic mRNA transcription. In this case, the leader sequences of the subgenomic transcripts were derived exclusively from the wild-type helper virus, indicating that the MHV leader RNA initiates in trans subgenomic mRNA transcription. Thus, the leader sequence can enhance subgenomic transcription even when it cannot serve as a primer for mRNA synthesis. These results taken together suggest that the 5'-end leader sequence of MHV not only provides a trans-acting primer for mRNA initiation but also serves as a cis-acting element required for the transcription of subgenomic mRNAs. The identification of an upstream cis-acting element for MHV subgenomic mRNA synthesis defines a novel sequence requirement for regulating mRNA synthesis in RNA viruses.",,"chloramphenicol acetyltransferase; messenger rna; plasmid dna; virus rna; animal cell; article; genome; mouse; murine hepatitis coronavirus; nonhuman; nucleotide sequence; plasmid; polymerase chain reaction; priority journal; rna replication; rna transcription; transcription regulation; vaccinia virus; viral genetics; Animal; Base Sequence; Chloramphenicol O-Acetyltransferase; DNA, Viral; Introns; Mice; Molecular Sequence Data; Murine hepatitis virus; Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Tumor Cells, Cultured",,"Lai, M.M.C.; Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"8035475","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028234463
"Tobler K., Bridgen A., Ackermann M.","6701508835;6603799081;7102624625;","Sequence analysis of the nucleocapsid protein gene of porcine epidemic diarrhoea virus",1994,"Advances in Experimental Medicine and Biology","342",,,"49","54",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028353235&partnerID=40&md5=c794bb62122714bebeed15357f0d3a83","Institute for Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland","Tobler, K., Institute for Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland; Bridgen, A., Institute for Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland; Ackermann, M., Institute for Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland","The nucleotide (nt) sequence of 1.7 kbp cDNA representing the 3' end of the PEDV genome has been determined. Viral RNA was reverse transcribed and the cDNA was amplified by polymerase chain reaction using degenerate primers. The sequences of the primers were based on conserved regions of coronaviral genomes. A 1323 nt open reading frame (ORF) showed good homology to the nucleocapsid (N) gene of other coronaviruses. The greatest homologies at the amino acid and the nt levels were observed with Human Coronavirus 229E. A second 336 nt ORF, which might encode a leucine-rich protein, was found within the N gene. Between the 3' end of the N gene and the poly(A) tail was a sequence of eleven nt, which is conserved among the other sequenced coronaviruses. Finally, a seven base sequence similar to the conserved intergenic sequences was present 5' to the N gene. These results confirm the classification of PEDV as a coronavirus.",,"capsid protein; complementary dna; virus rna; amino acid sequence; conference paper; coronavirus; diarrhea; epidemic; nonhuman; nucleotide sequence; open reading frame; polymerase chain reaction; priority journal; sequence analysis; sequence homology; swine; taxonomy; virus genome; virus nucleocapsid; Base Sequence; Capsid; Comparative Study; Coronavirus; Coronavirus 229E, Human; DNA, Complementary; Genes, Structural, Viral; Molecular Sequence Data; Open Reading Frames; RNA, Viral; Species Specificity; Support, Non-U.S. Gov't; Viral Core Proteins",,"Tobler, K.; Institute for Virology, Veterinary Medical Faculty, University of Zurich, Winterthurerstrasse 266a, CH-8057 Zurich, Switzerland",,,00652598,,AEMBA,"8209770","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028353235
"Duarte M., Laude H.","57205792139;7006652624;","Sequence of the spike protein of the porcine epidemic diarrhoea virus",1994,"Journal of General Virology","75","5",,"1195","1200",,85,"10.1099/0022-1317-75-5-1195","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326371&doi=10.1099%2f0022-1317-75-5-1195&partnerID=40&md5=8678998048a48d6f229278fb2e07246d","INRA, Unite Virol et Immunol Moleculaires, CR de Jouy-en-Josas, 78350 Jouy-en-Josas, France","Duarte, M., INRA, Unite Virol et Immunol Moleculaires, CR de Jouy-en-Josas, 78350 Jouy-en-Josas, France; Laude, H., INRA, Unite Virol et Immunol Moleculaires, CR de Jouy-en-Josas, 78350 Jouy-en-Josas, France","The complete sequence of the spike (S) gene of the Br1/87 isolate of porcine epidemic diarrhoea virus (PEDV) was determined from cDNA clones. The predicted polypeptide was 1383 amino acids long, contained 29 potential N-linked glycosylation sites and showed structural features similar to those of the coronavirus spike protein. The PEDV S protein, like that of the members of the transmissible gastroenteritis virus (TGEV)-related subset, lacks a proteolytic site to yield cleaved amino and carboxy subunits S1 and S2. Viral polypeptide species of the expected M(r), i.e. 170K/190K, were observed in PEDV-infected cells. Sequence comparison confirmed that, within the subset, PEDV was most closely related to the human respiratory coronavirus HCV 229E. However, PEDV S protein has an additional 250 residue N-terminal domain which is absent from HCV 229E and porcine respiratory coronavirus, the respiratory variant of TGEV. Alignment of the S1 regions revealed a second domain of about 90 residues with increased sequence divergence which might possibly express virus-specific determinants.",,"complementary DNA; polypeptide; protein subunit; virus protein; vitronectin; amino acid sequence; amino terminal sequence; animal cell; article; carboxy terminal sequence; Coronavirus; diarrhea; enteric virus; gastroenteritis; gene sequence; nonhuman; priority journal; protein degradation; protein glycosylation; sequence homology; swine disease; viral genetics; Animalia; Coronavirus; Hepatitis C virus; Porcine epidemic diarrhea virus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus",,"Laude, H.; INRA, Unite Virol et Immunol Moleculaires, CR de Jouy-en-Josas, 78350 Jouy-en-Josas, France",,"Microbiology Society",00221317,,JGVIA,"8176382","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0028326371
"Nowotny N., Möstl K., Maderbacher R., Odörfer G., Schuh M.","7005482650;6603843340;6602401739;6505735598;7005535556;","Serological studies in Austrian fattening pigs with respiratory disorders.",1994,"Acta veterinaria Hungarica","42","2-3",,"377","379",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028713462&partnerID=40&md5=b587ec2d6f6b68a4a1a5d149f4dffa84","Institute of Virology, Veterinary University, Vienna, Austria","Nowotny, N., Institute of Virology, Veterinary University, Vienna, Austria; Möstl, K., Institute of Virology, Veterinary University, Vienna, Austria; Maderbacher, R., Institute of Virology, Veterinary University, Vienna, Austria; Odörfer, G., Institute of Virology, Veterinary University, Vienna, Austria; Schuh, M., Institute of Virology, Veterinary University, Vienna, Austria","Serum samples of 253 fattening pigs out of 44 different herds with respiratory signs were examined for antibodies to Aujeszky's disease virus by ELISA, swine influenza virus (HI test), porcine respiratory coronavirus (ELISA) and porcine reproductive and respiratory syndrome virus (IPMA). One single case of Aujeszky's disease was detected at slaughter. On the other hand 24.5% of the animals proved to be positive for swine influenza, although no vaccine is licensed in Austria, and 63.6% reacted positively to porcine respiratory coronavirus. None of the sera showed antibodies to porcine reproductive and respiratory syndrome virus, which has not as yet been identified in the Austrian swine population.",,"virus antibody; animal; animal disease; article; Austria; breathing disorder; Coronavirus; enzyme linked immunosorbent assay; immunology; Influenza virus A; meat; Pseudorabies herpetovirus; swine; swine disease; virology; virus infection; Animals; Antibodies, Viral; Austria; Coronavirus; Enzyme-Linked Immunosorbent Assay; Herpesvirus 1, Suid; Influenza A virus; Meat; Respiration Disorders; Swine; Swine Diseases; Virus Diseases",,"Nowotny, N.",,,02366290,,,"7810433","English","Acta Vet. Hung.",Article,"Final",,Scopus,2-s2.0-0028713462
"Taylor K., Copley C.G.","55574242728;36641398800;","Detection of rodent RNA viruses by polymerase chain reaction",1994,"Laboratory Animals","28","1",,"31","34",,8,"10.1258/002367794781065861","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028088846&doi=10.1258%2f002367794781065861&partnerID=40&md5=4601311075a50055e16e533155446430","ICI plc Central Toxicology Laboratory, Alderley Park, Macclesfield, Cheshire SK10 4TJ, United Kingdom; ICI Pharmaceuticals, Biotechnology Department, Alderley Park, Macclesfield, Cheshire SK10 4TJ, United Kingdom","Taylor, K., ICI plc Central Toxicology Laboratory, Alderley Park, Macclesfield, Cheshire SK10 4TJ, United Kingdom; Copley, C.G., ICI Pharmaceuticals, Biotechnology Department, Alderley Park, Macclesfield, Cheshire SK10 4TJ, United Kingdom","Assays for rodent coronaviruses (mouse hepatitis virus and rat corona/sialodacryoadenitis virus) and a rodent paramyxovirus (Sendai virus) based on the polymerase chain reaction are described. © 1994, Royal Society of Medicine Press. All rights reserved.","polymerase chain reaction; RNA-viruses","animal cell; animal tissue; article; bioassay; mouse; murine hepatitis coronavirus; nonhuman; paramyxovirus; polymerase chain reaction; rat; rna virus; Animal; Base Sequence; Cells, Cultured; Coronavirus, Rat; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Parainfluenza Virus 1, Human; Polymerase Chain Reaction; Rats; RNA Viruses; RNA, Viral; Rodentia","Collins, M.F., (1986) Prevalence of pathogenic murine viruses and mycoplasma that are currently a problem to research, pp. 1-9. , In Complications of viral and mycoplasma infections to toxicology research and testing (ed. TE Hamm). Washington: Hemisphere Publishing Corporation; Hidako, Y., Kanda, T., Iwasaki, K., Nucleotide sequence of a Sendai virus genome region covering the entire M gene and the 3′ proximal 1013 nucleotides of the F gene (1984) Nucleic Acid Research, 12, pp. 7965-7972; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus Mouse Hepatitis Virus suggest a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Shioda, T., Hidaka, Y., Kanda, T., Shibuta, H., Nomoto, A., Iwasaki, K., Sequence of 3,687 nucleotides from the 3′ end of Sendai virus genome RNA and the predicted amino acid sequences of viral NP, P and C proteins (1983) Nucleic Acid Research, 11, pp. 7317-7330; Shioda, T., Iwasaki, K., Shibuta, H., Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins (1986) Nucleic Acid Research, 14, pp. 1545-1563; Skinner, M.A., Siddell, S.G., Coronavirus JHM. Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acid Research, 11, pp. 5045-5054; Taylor, K., Copley, C.G., Diagnosis of Kilham rat virus using PCR (1994) Laboratory Animals, 28, pp. 26-30",,,,00236772,,,"8158966","English","Lab. Anim.",Article,"Final",,Scopus,2-s2.0-0028088846
"Quigley J.D., III, Martin K.R., Bemis D.A., Potgieter L.N.D., Reinemeyer C.R., Rohrbach B.W., Dowlen H.H., Lamar K.C.","7102715774;7402551079;7003378914;7004094951;7003482337;7004280369;6603670834;6602567951;","Effects of Housing and Colostrum Feeding on the Prevalence of Selected Infectious Organisms in Feces of Jersey Calves",1994,"Journal of Dairy Science","77","10",,"3124","3131",,30,"10.3168/jds.S0022-0302(94)77255-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028528071&doi=10.3168%2fjds.S0022-0302%2894%2977255-6&partnerID=40&md5=e0c153625f80fc6907bf7f5bd4ad776e","Institute of Agriculture, Department of Animal Science, University of Tennessee, Knoxville, 37901-1071, United States; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, 37901-1071, United States; Dairy Experiment Station, USDA-ARS, Lewisburg, Tennessee, 37091, United States","Quigley, J.D., III, Institute of Agriculture, Department of Animal Science, University of Tennessee, Knoxville, 37901-1071, United States; Martin, K.R., Institute of Agriculture, Department of Animal Science, University of Tennessee, Knoxville, 37901-1071, United States; Bemis, D.A., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, 37901-1071, United States; Potgieter, L.N.D., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, 37901-1071, United States; Reinemeyer, C.R., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, 37901-1071, United States; Rohrbach, B.W., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, 37901-1071, United States; Dowlen, H.H., Dairy Experiment Station, USDA-ARS, Lewisburg, Tennessee, 37091, United States; Lamar, K.C., Dairy Experiment Station, USDA-ARS, Lewisburg, Tennessee, 37091, United States","Neonatal Jersey calves (n = 96) were used to evaluate effects of housing (individual hutches or wooden pens in a barn) and colostrum feeding (calves were separated from the dam and fed 2 L of colostrum in nipple-bottles or allowed to nurse the dam for 3 d) on the prevalence of selected organisms in feces. Prevalence of Cryptosporidium and Eimeria were reduced, and prevalence of rotavirus tended to be reduced, when calves were housed in hutches. Prevalence of coronavirus was unaffected by treatment. Weekly prevalence of Giardia was increased when calves were left to nurse the dam for 3 d. Mean prevalence of Cryprosporidia (wk 1 to 4), Eimeria (wk 4 to 5), Giardia, rotavirus, and coronavirus (wk 1 to 5) were 34.7, 20.6, 27.1, 15.8, and 4.9%, respectively. Escherichia coli (K99 positive) were observed in 3 of 174 samples cultured. Methods of housing and colostrum feeding affected acquisition of enteropathogens in this study. © 1994, American Dairy Science Association. All rights reserved.","colostrum; housing; Jersey","animal; animal housing; article; cattle; clinical trial; colostrum; controlled clinical trial; controlled study; Coronavirus; Cryptosporidium; Eimeria; Escherichia coli; feces; female; Giardia; isolation and purification; male; newborn; parasitology; physiology; randomized controlled trial; Rotavirus; virology; Animals; Animals, Newborn; Cattle; Colostrum; Coronavirus; Cryptosporidium; Eimeria; Escherichia coli; Feces; Female; Giardia; Housing, Animal; Male; Rotavirus","Besser, T.E., Gay, C.C., McGuire, T.C., Everman, J.F., Passive immunity to bovine rotavirus infection associated with transfer into the intestinal lumen (1988) J. Virol., 62, p. 2238; Blouin, D.C., Saxton, A.M., (1990) General Linear Mixed Models (GLMM) User's Manual, , Agric. Exp. Stn., Louisiana State Univ, Baton Rouge; (1993) Dairy Herd Management Practices Focusing on Preweaned Heifers. USDA, Anim. Plant Health Inspect, , Serv., Vet. Serv, Fort Collins, CO; Cox, D.D., Todd, A.F., A survey of gastrointestinal parasitisms in Wisconsin dairy cattle (1962) J Am. Vet. Med. Assoc., 141, p. 706; Davis, L.R., Autrey, K.M., Herlich, J., Hawkins, G.E., Outdoor individual portable pens compared with conventional housing for raising dairy calves (1954) Journal of Dairy Science, 37, p. 562; Gay, C.C., Failure of passive transfer of colostral immunoglobulins and neonatal disease in calves: a review (1983) Proc. 4th Int. Symp. Neonatal Dis, p. 346. , Vet. Infect. Dis. Org., Saskatoon, SK, Can; Harp, J.A., Woodmansee, D.B., Moon, H.W., Effects of colostral antibody on susceptibility of calves to Cryptosporidium parvum infection (1989) Am. J. Vet. Res., 50, p. 2117; James, R.E., McGilliard, M.L., Hartman, D.A., Calf mortality in Virginia dairy herd improvement herds (1984) J. Dairy Sci., 67, p. 908; Jorgensen, L.J., Jorgensen, N.A., Schingoethe, D.J., Owens, M.J., Indoor versus outdoor calf rearing at three weaning ages (1970) Journal of Dairy Science, 53, p. 813; Lopez, J.W., Allen, S.D., Mitchell, J., Quinn, M., Rotavirus and Cryptosporidium shedding in dairy calf feces and its relationship to colostrum immune transfer (1988) J. Dairy Sci., 71, p. 1288; Lucchelli, A., Lance, S.E., Bartlett, P.B., Miller, G.Y., Saif, L.J., Prevalence of bovine group A rotavirus shedding among dairy calves in Ohio (1992) Am. J. Vet. Res., 53, p. 169; Martin, S.W., Schwabe, C.W., Franti, C.E., Dairy calf mortality rate: influence of management and housing factors on calf mortality rate in Tulare County (1975) California. Am. J. Vet. Res., 36, p. 1111; Ongerth, J.E., Stibbs, H.H., Prevalence of Cryptosporidium infection in dairy calves in western Washington (1989) Am. J. Vet. Res., 50, p. 1069; Pohlenz, J., Moon, H.W., Cheville, N.F., Bemrick, W.J., Cryptosporidiosis as a probable factor in neonatal diarrhea of calves (1978) J. Am. Vet. Med. Assoc., 172, p. 452; Quigley, J.D., III, Martin, K.R., Dowlen, H.H., Wallis, L.B., Lamar, K., Immunoglobulin concentration, specific gravity, and nitrogen fractions of colostrum from Jersey cattle (1994) J. Dairy Sci., 77, p. 264; Saif, L.J., Rotavirus (1992) Veterinary Diagnostic Immunology, p. 126. , A.E. Castro, W.P. Heuschele, Mosby Year Book, St. Louis, MO; Saif, L.J., Smith, K.L., Enteric viral infections of calves and passive immunity (1985) J. Dairy Sci., 68, p. 206; St. Jean, G., Conture, Y., Dubreuil, P., Frechette, J.L., Diagnosis of Giardia infection in 14 calves (1987) J. Am. Vet. Med. Assoc., 191, p. 831; Tzipori, S., Smith, M., Halpin, C., Experimental cryptosporidiosis in calves: clinical manifestations and pathological findings (1983) Vet. Rec., 112, p. 116; Waltner-Toews, D., Martin, S.W., Meek, A.H., Dairy calf management, morbidity and mortality in Ontario Holstein herds. III. Association of management with morbidity (1986) Prev. Vet. Med., 4, p. 137; Waltner-Toews, D., Martin, S.W., Meek, A.H., Dairy calf management, morbidity and mortality in Ontario Holstein herds. IV. Association of management with mortality (1986) Prev. Vet. Med., 4, p. 159; Wilson, J.B., McEwen, S.A., Clarke, R.C., Leslie, K.E., Waltner-Toews, D., Gyles, C.L., A case-control study of selected pathogens including verotoxigenic Escherichia coli in calf diarrhea on an Ontario veal farm (1992) Can. J. Vet. Res., 56, p. 184","Quigley, J.D.; Institute of Agriculture, Department of Animal Science, University of Tennessee, Knoxville, 37901-1071, United States",,,00220302,,,"7836601","English","J. Dairy Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0028528071
"Myint S.H.","35479862600;","Common Colds, Asthma and Indoor Air Quality",1994,"Indoor and Built Environment","3","5",,"274","277",,1,"10.1177/1420326X9400300505","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84964121124&doi=10.1177%2f1420326X9400300505&partnerID=40&md5=348aa6204b67fbf9f20f8d399fd04922","Department of Microbiology, University of Leicester, United Kingdom","Myint, S.H., Department of Microbiology, University of Leicester, United Kingdom","Most common colds are caused by rhinoviruses and coronaviruses. These viruses are now thought to provoke the majority of asthmatic attacks in children. This article summarises the role that these viruses play in inducing asthma and discusses the interaction between air pollution and virus-induced asthma. © 1994, Sage Publications. All rights reserved.","indoor Children Colds; Virus Asthma Pollution",,"(1985) Current estimates from the National Health Interview Survey, United States, 1982. Vital and Health Statistics Ser 10, No 150, pp. 85-1578. , National Center for Health Statistics: Washington US Department of Health and Human Services; (1983) Physician Visits, Volume and Interval since Last Visit, United States 1980. Ser 10, No 144, pp. 83-1572. , National Center for Health Statistics: Washington US Department of Health and Human Services; Noren, J., Frazier, T., Altman, I., Ambulatory medical care: A comparison of internists and general practitioners (1980) N Engl J Med, 302, pp. 11-16; Tompkins, R.K., Wood, R.W., Wolcroft, D.W., The effectiveness and cost of acute respiratory illness medical care provided by physicians and algorithm-assisted physicians assistants (1977) Med Care, 15, pp. 991-1003; Smith, A.P., Tyrrell, D.a.j., Al-Nakib, W., Barrow, I.G., Higgins, P.G., Leekam, S., Trickett, S., Effect and aftereffects of the common cold and influenza on human performance (1989) Neuropsychobiology, 21, pp. 90-93; Couch, R.B., Douglas, R.G., Jr., Lindgren, K.M., Gerone, P.J., Knight, V., Airborne transmission of respiratory infections with Coxsackie A type 21 (1970) Am J Epidemiol, 91, pp. 77-86; Kingston, D., Lidwell, O.M., Williams, R.e.o., The epidemiology of the common cold. III. The effect of ventilation, air disinfection and room use (1962) J Hyg Camb, 60, pp. 341-352; Minor, T.E., Dick, E.C., DeMeo, A.N., Ouellette, J.J., Cohen, M., Reed, C.E., Viruses as precipitants of asthmatic attacks in children (1974) JAMA, 227, pp. 292-298; Johnstone, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L., Symington, P., Holgate, S.T., The importance of virus infections in asthma-like exacerbations in 9- to 11-year-old children in a UK community BMJ, , in press; Kondo, S., Abe, K., The effects of influenza virus infection on FEV1 in asthmatic children (1991) Chest, 100, pp. 1235-1238; Laitinen, L.A., Heino, M., Laitenen, A., Kava, T., Haahtela, T., Damage of the airway epithelium and bronchial reactivity in patients with asthma (1985) Am Rev Respir Dis, 131, pp. 599-606; Welliver, R.C., Wong, D.T., Sun, M., The development of respiratory syncytial virus specific IgE and the release of histamine in nasopharyngeal secretions after infection (1981) N Engl J Med, 305, pp. 841-846; Warpinski, J.R., Busse, W.W., Effect of viral respiratory infections on airways responsiveness and late-phase asthmatic reactions in humans (1990) Semin Respir Med, 11, pp. 336-344; Makgoba, M.W., Sanders, M.E., Luce, G.e.g., ICAM-1, a ligand for LFA-1 dependent adhesion of B, T and myeloid cells (1988) Nature, 331, pp. 86-88; Empey, D.W., Laitenen, L.A., Jacobs, L., Gold, W.M., Nadel, J.A., Mechanisms of bronchial hyperreactivity in normal subjects after upper respiratory tract infection (1976) Am Rev Respir Dis, 133, pp. 131-139; McDonald, D.M., Respiratory tract infections increase susceptibility to neurogenic inflammation in the rat trachea (1988) Am Rev Respir Dis, 137, pp. 1432-1440; Douglas, J.w.b., Waller, R.E., Air pollution and respiratory infection in children (1966) Br J Prev Soc Med, 20, pp. 1-8; Jaakola, J.j.k., Paunio, M., Virtanen, M., Heinonen, O.P., Low level air pollution and upper respiratory infections in children (1991) Am J Public Health, 81, pp. 1060-1063; Goren, A.I., Hellmann, S., Prevalence of respiratory symptoms and diseases in schoolchildren living in a polluted and in a low polluted area in Israel (1988) Environ Res, 45, pp. 28-37; Pandey, M.R., Smith, K.R., Boleij, J.s.m., Wafula, E.M., Indoor air pollution in developing countries and acute respiratory infection in children (1989) Lancet, i, pp. 4277-4278","Myint, S.H.; Department of Microbiology, University of Leicester, Leicester LE1 9HN, United Kingdom",,,1420326X,,,,"English","Indoor Built Environ.",Article,"Final",,Scopus,2-s2.0-84964121124
"Hiscox J., Pocock D.H., Britton P.","7004565877;7005365522;57203302770;","Control of TGEV mRNA transcription",1994,"Advances in Experimental Medicine and Biology","342",,,"99","104",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326929&partnerID=40&md5=33e950ad824318ae24d5590917511d1b","Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom","Hiscox, J., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Pocock, D.H., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Britton, P., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom","Coronavirus proteins are translated from a nested set of subgenomic mRNAs which have common 3' termini with unique 5' extensions. Evidence suggests that coronavirus mRNAs are generated by a mechanism of leader primed transcription. Leader RNA binds to consensus sequences upstream of each gene on full length negative strand viral RNA and transcription proceeds to the 5' end of the negative strand to produce the nested set of mRNAs. Even though this gives rise to polycistronic mRNA species only the 5' extension of each mRNA is translated to give the viral proteins. The leader RNA for TGEV is about 90 nucleotides long and contains the sequence which recognises the leader binding sites on the negative strand RNA. Evidence suggests that the length of the leader binding sequence may be involved in transcriptional control of individual mRNAs. In order to investigate this a virus specific mRNA isolation method was developed to measure the relative amounts of mRNAs synthesized during an infection of LLC-PK1 cells with TGEV (strain FS772/70). Thus the relative quantity of each mRNA can be determined and correlated with the variation in size of the leader binding site.",,"virus messenger rna; virus protein; animal cell; binding site; conference paper; coronavirus; nonhuman; nucleotide sequence; priority journal; rna synthesis; rna transcription; swine disease; transcription regulation; Animal; Base Sequence; Cell Line; Gene Expression Regulation, Viral; Microspheres; Molecular Sequence Data; RNA, Messenger; RNA, Viral; Swine; Transcription, Genetic; Transmissible gastroenteritis virus",,"Hiscox, J.; Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom",,,00652598,,AEMBA,"8209778","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028326929
"Fleming J.O., Houtman J.J., Alaca H., Hinze H.C., McKenzie D., Aiken J., Bleasdale T., Baker S.","7401457370;6701855701;6505755018;7003795446;7202305081;7101788870;6507314644;57213308194;","Persistence of viral RNA in the central nervous system of mice inoculated with MHV-4",1994,"Advances in Experimental Medicine and Biology","342",,,"327","332",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028328616&partnerID=40&md5=4bbbe749c2aa85363e8ff27e12b7112a","University of Wisconsin, Madison, WI 53792, United States","Fleming, J.O., University of Wisconsin, Madison, WI 53792, United States; Houtman, J.J., University of Wisconsin, Madison, WI 53792, United States; Alaca, H., University of Wisconsin, Madison, WI 53792, United States; Hinze, H.C., University of Wisconsin, Madison, WI 53792, United States; McKenzie, D., University of Wisconsin, Madison, WI 53792, United States; Aiken, J., University of Wisconsin, Madison, WI 53792, United States; Bleasdale, T., University of Wisconsin, Madison, WI 53792, United States; Baker, S., University of Wisconsin, Madison, WI 53792, United States","In order to study the role that viral persistence may play in chronic central nervous system (CNS) disease induced by murine coronaviruses, we have used the reverse transcriptase-polymerase chain reaction (RT-PCR) to study viral RNA in the brains of mice after intracerebral inoculation of JHM virus (JHMV or MHV-4). Quantitative RT-PCR showed that JHMV RNA decreased from approximately 2 ng/ug total brain RNA at day 6 post-inoculation (PI) to 0.1 pg/ug total brain RNA at 360 days PI. Double-stranded viral RNA could be detected up to day 20 PI. By the selective use of upstream or downstream primers during the RT step, it was possible to measure negative sense and positive sense JHMV RNA respectively, and we found that there was a marked rise in the ratio of positive to negative sense JHMV RNA after day 13 PI. Analysis of amplified products by dideoxy DNA sequencing showed that the characteristic mutation of our input virus (at position 3340 of gene 3) is maintained to at least day 42 PI. Taken together, these results favor a model of JHMV persistence in vivo in which viral RNA is present as double stranded forms initially and predominantly as single stranded, positive sense forms at late timepoints. Further analysis of this model in quantitative terms may contribute to our understanding of the biological significance of coronavirus persistence in the CNS.",,"double stranded rna; rna directed dna polymerase; virus rna; animal model; animal tissue; central nervous system infection; conference paper; controlled study; inoculation; male; mouse; murine hepatitis coronavirus; nonhuman; persistent virus infection; polymerase chain reaction; priority journal; rna sequence; virus genome; virus replication; Animal; Brain; Injections; Male; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Polymerase Chain Reaction; RNA, Viral; RNA-Directed DNA Polymerase; Support, Non-U.S. Gov't; Virus Latency",,"Fleming, J.O.; University of Wisconsin, Madison, WI 53792, United States",,,00652598,,AEMBA,"7516107","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028328616
"Myint S.H.","35479862600;","Human coronaviruses: A brief review",1994,"Reviews in Medical Virology","4","1",,"35","46",,40,"10.1002/rmv.1980040108","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028556737&doi=10.1002%2frmv.1980040108&partnerID=40&md5=c27215b9b0ae0bc3f349154b4aa8df9d","Department of Clinical Virology, University of Leicester Medical School, Leicester, LE1 9HN, United Kingdom","Myint, S.H., Department of Clinical Virology, University of Leicester Medical School, Leicester, LE1 9HN, United Kingdom",[No abstract available],,"coronavirus; human; immune response; morphogenesis; nonhuman; review; virus morphology; virus replication","Dochez, A.R., Shibley, G.S., Mills, K.C., Studies in the common cold. IV. 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Child., 139, pp. 245-248; Hartley, J.W., Rowe, W.P., Bloom, H.H., Turner, H.C., Antibodies to mouse hepatitis virus in human sera (1964) Proc. Soc. Exp. Biol. Med., 115, pp. 414-418; Bradburne, A.F., Antigenic relationships amongst coronaviruses (1970) Arch. Ges. Virusforschung, 31, pp. 352-364; Gerdes, J.C., Jankovsky, L.D., Devald, B.L., Klein, I., Burks, J.S., Antigenic relationships of coronaviruses detectable by plaque neutralisation, competitive enzyme‐linked immunoabsorbent assay, and immunoprecipitation (1981) Adv. Exp. Med. Biol., 142, pp. 29-41; MacNaughton, M.R., Structural and antigenic relationships between human, murine and avian coronaviruses (1981) Adv. Exp. Med. Biol., 142, pp. 19-28; Small, J.D., Aurelian, L., Squirte, R.A., Rabbit cardiomyopathy. Associated with a virus antigenically related to human coronavirus strain 229E (1979) Am. J. Pathol., 95, pp. 709-729; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O‐glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Zhang, X.M., Kousoulas, K.G., Storz, J., The haemagglutinin/esterase gene of human coronavirus strain OC43: phylogenetic relationships to bovine and murine coronaviruses and influenza C virus (1992) Virology, 186, pp. 318-323; Schreiber, S.S., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleocapsid gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Myint, S., Harmsen, D., Raabe, T., Siddell, S.G., Characterisation of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) J. Med. Virol., 31, pp. 165-172; Raabe, T., Schelle‐Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Davies, H.A., MacNaughton, M.R., Comparison of the morphology of three coronaviruses (1979) Arch. Virol., 59, pp. 25-33; Lai, M.M.C., Coronavirus: organisation, replication and expression of genome (1990) Ann. Rev. Microbiol., 44, pp. 303-333; Schmidt, O.W., Kenny, G.E., Polypeptides and functions of antigens from human coronaviruses 229E and OC43 (1982) Infect. Immun., 35, pp. 515-522; Raabe, T., Siddell, S.G., Nucleotide sequence of the gene encoding the membrane protein of human coronavirus 229E (1989) Arch. Virol., 107, pp. 323-328; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M.C., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus 229E (1990) Virology, 174, pp. 608-612; Raabe, T., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E mRNA 4 and mRNA 5 unique regions (1989) Nucleic Acids Res., 17, p. 6387; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNA 4 and 5: evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Bucknall, R.A., King, L.M., Kapikian, A.Z., Chanock, R.M., Studies with human coronaviruses. II. Some properties of strains 229E and OC43 (1972) Proc. Soc. Exp. Biol. Med., 139, pp. 722-727; Lamarre, A., Talbot, P.J., Effect of pH and temperature on the infectivity of human coronavirus 229E (1989) Can. J. Microbiol., 35, pp. 972-974; Mental, R., Schmidt, J., Versuche zur Chemischen Inactivierung vo Rhinoviren und Coronaviren (1974) Z. Gesumte Hyg., 26, pp. 530-533; Hierholzer, J.C., Purification and biophysical properties of human coronavirus 229E (1976) Virology, 75, pp. 155-165; Kennedy, D.A., Johnson‐Lussenberg, C.M., Inhibition of coronavirus 229E replication by actinomycin D (1978) J. Virol., 29, pp. 401-404; Kaye, H.S., Dowdle, W.R., Some characteristics of haemagglutination of certain strains of ‘IBV‐like’ virus (1969) J. Infect. Dis., 120, pp. 576-581; Kaye, H.S., Ong, S.B., Dowdle, W.R., Detection of coronavirus 229E antibody by indirect haemagglutination (1972) Appl. Microbiol., 24, pp. 703-707; Patterson, S., MacNaughton, M.R., The distribution of human coronavirus strain 229E on the surface of human diploid cells (1981) J. Gen. Virol., 53, pp. 267-273; Sakaguchi, A.Y., Shows, T.B., Coronavirus 229E susceptibility in man‐mouse hybrids is located on human chromosome 15 (1982) Somatic Cell Genet., 8, pp. 83-94; Yeager, C.L., Ashmun, R.A., Williams, R.K., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognise sialic acidcontaining receptors similar to those of influenza C viruses (1988) Proc. Natl Acad. Sci. USA, 85, pp. 4526-4529; Martin, N.G., Oakeshott, J.G., Clark, P., Carr, A., Association between alpha‐1‐antitrypsin types and the common cold (1983) Hum. Hered., 33, pp. 265-269; Debiaggi, M., Luini, M., Cereda, P.M., Perduca, M., Romero, E., Serum inhibitor of coronaviruses OC43 and NCDCV: a study in vivo (1986) Microbiologica, 9, pp. 33-37; NacNaughton, M.R., Hasony, H.J., Madge, H., Reed, S.E., Antibody to virus components in volunteers experimentally infected with human coronavirus 229E group viruses (1981) Infect. Immun., 31, pp. 845-849; Callow, K.A., Effect of specific humoral immunity and some non‐specific factors on resistance of volunteers to respiratory coronavirus infection (1985) J. Hyg. Camb., 95, pp. 173-189; Callow, K.A., Tyrrell, D.A.J., Shaw, R.J., Fitzharris, P., Wardlaw, A.J., Kay, A.B., Influence of atopy on the clinical manifestations of coronavirus infection in adult volunteers (1988) Clin. Allergy, 18, pp. 119-129; Holmes, M.J., Callow, K.A., Childs, R.A., Tyrrell, D.A.J., Antibody dependent cellular cytotoxicity against coronavirus 229E‐infected cells (1986) Br. J. Exp. Pathol., 67, pp. 581-586; Leader, Splints don't stop colds—surprising! (1988) Lancet, 1, pp. 277-278; Ijaz, M.K., Brunner, A.H., Sattar, S.A., Nair, R.C., Johnson‐Lussenberg, C.M., Survival characteristics of airborne human coronavirus 229E (1985) J. Gen. Virol., 66, pp. 2743-2748; Gwaltney, J.M., Epidemiology of the common cold (1980) Ann. N. Y. Acad. Sci., 353, pp. 54-60; Hamre, D., Beem, M., Virologic studies of acute respiratory disease in young adults (1972) Am. J. Epidemiol., 96, pp. 94-106; Hendley, J.O., Fishburne, H.B., Gwaltney, J.M., Coronavirus infections in working adults. Eight year study with 229E and OC43 (1972) Am. Rev. Respir. Dis., 105, pp. 805-811; Isaacs, D., Flowers, D., Clarke, J.R., Valman, H.B., MacNaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch. Dis. Child., 58, pp. 500-503; Monto, A.S., Lim, S.K., The Tecumseh study of respiratory illness VI. Frequency of and relationship between outbreaks of coronavirus infection (1974) J. Infect. Dis., 129, pp. 271-276; McIntosh, K., Chad, R.K., Krause, H.E., Wasil, R., Mosega, H.E., Mufson, M.A., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J. Infect. Dis., 130, pp. 502-507; McIntosh, K., Kapikian, A.Z., Turner, H.C., Hartley, J.W., Parrott, R.H., Chanock, R.M., Seroepidemioloc studies of coronavirus infection in adults and children (1970) Am. J. Epidemiol., 91, pp. 585-592; Mufson, M.A., McIntosh, K., Chad, R.K., Krause, H.E., Mosega, H.E., Epidemiology of coronavirus infections in infants with acute lower respiratory disease (1972) Clin. Res., 20, p. 534; Wenzel Hendley, J.O., Davies, J.A., Gwaltney, J.M., Coronavirus infections in military recruits. Three year study with coronavirus strains OC43 and 229E (1974) Am. Rev. Resp. Dis., 109, pp. 621-624; Arnold, W., Klein, M., Wang, J.B., Scmidt, W.A.K., Trampisch, H.J., Coronavirus‐associated antibodies in nasopharyngeal carcinoma and infectious mononucleosis (1981) Arch. Otorhinolaryngol., 232, pp. 165-177; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J. Med. Virol., 6, pp. 259-265; Fazzini, E., Fleming, J., Fahn, S., Cerebrospinal fluid antibodies to coronavirus in patients with Parkinson's disease (1992) Mov. Disord., 7, pp. 153-158; Cunningham, A.L., Groham, G.S., Harkness, J., Gastrointestinal viral infections in homosexual men who were symptomatic and seropositive for human immunodeficiency virus (1988) J. Infect. Dis., 158, pp. 386-391; Schnagl, R.D., Greco, T., Morey, F., Antibody prevalence to human enteric coronavirus‐like particles and indications of antigenic differences between particles from different areas (1986) Arch. Virol., 87, pp. 331-337; Riordan, T., Curry, A., Bhattacharya, M.N., Enteric coronaviruses in symptomless homosexuals (1986) J. Clin. Pathol., 39, pp. 1159-1160; Kern, P., Muller, G., Schmitz, H., Detection of coronavirus‐like particles in homosexual men with acquired immunodeficiency and related lymphadenopathy syndrome (1983) Klin. Wochenstr., 63, pp. 68-72; Chany, C., Moscovici, O., Lebon, P., Rousset, S., Association of coronavirus infection with neonatal necrotising enterocolitis (1982) Paediatrics, 69, pp. 209-214; Baker, S.J., Mathan, M., Mathan, N.I., Jesudoss, S., Swaminathan, S.P., Chronic enterocyte infection with coronavirus. One possible cause of the syndrome of tropical sprue? (1982) Dig. Dis. Sci., 27, pp. 1039-1043; Tanaka, R., Iwasaki, Y., Koprowski, H., Intracisternal virus‐like particles in brain of a multiple sclerosis patients (1976) J. Neurol. Sci., 28, pp. 121-126; Burks, J.S., Devald, B.L., Jankovski, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Gerdes, J.C., Klein, I., DeVald, B.L., Burks, J.S., Coronavirus isolates SK and SD from multiple sclerosis patients are serologically related to murine coronaviruses A59 and JHM and human coronavirus OC43 but not to human coronavirus 229E (1981) J. Virol., 38, pp. 231-238; Salmi, A., Ziola, B., Hovi, T., Reunanem, M., Antibodies to coronaviruses OC43 and 229E in multiple sclerosis patients (1982) Neurology, 32, pp. 292-295; Murray, R.S., MacMillan, B., Burks, J.S., Detection of coronavirus genome in the CNS of MS patients and control patients (1987) Neurology, 37, p. 109; Pearson, J., Mims, C.A., Differential susceptibility of cultured neural cells to the human coronavirus OC43 (1985) J. Virol., 53, pp. 1016-1019; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Zuckerman, A.J., Taylor, P.E., Almeida, J.D., Presence of particles other than the Australian SH antigen in a case of chronic active hepatitis with cirrhosis (1970) Br. Med. J., 1, pp. 262-264; Apostolov, K., Spasic, P., Bojanic, N., Evidence of a viral aetiology in endemic (Balkan nephropathy) (1975) Lancet, 2, pp. 1271-1273; Myint, S., Tyrrell, D.A.J., Coronaviruses (1993) Diagnostic Procedures for Viral, Rickettsial and Chlamydial Infections, , ed. by, E. H. Lennette, American Public Health Association, Washington; Hierholzer, J.C., Tannock, G.A., The coronaviruses (1988) Laboratory Diagnosis of Infectious Diseases, , ed. by, E. H. Lennette, P. Halonen, F. A. Murphy, Springer‐Verlag, New York; Myint, S., Moffitt, J., Simpson, H., (1993), A nested PCR method for the detection of human respiratory coronaviruses 229E and OC43. In preparation; Higgins, P.G., Phillpotts, R.J., Scott, G.M., Wallace, J., Bernhardt, L.L., Tyrrell, D.A.J., Intranasal interferon as protection against experimental respiratory coronavirus infection in volunteers (1983) Antimicrob. Agents Chemother., 24, pp. 713-715; Tyrrell, D.A.J., Hot news on the Common Cold (1988) Ann. Rev. Microbiol., 42, pp. 35-47","Myint, S.H.; Department of Clinical Virology, University of Leicester Medical School, Leicester, LE1 9HN, United Kingdom",,,10529276,,,,"English","Rev. Med. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0028556737
"Coutelier J.‐P., Godfraind C., Dveksler G.S., Wysocka M., Cardellichio C.B., Noël H., Holmes K.V.","7003918786;56877631600;6603790777;7006341809;6602071538;7103299959;7201657724;","B lymphocyte and macrophage expression of carcinoembryonic antigen‐related adhesion molecules that serve as receptors for murine coronavirus",1994,"European Journal of Immunology","24","6",,"1383","1390",,62,"10.1002/eji.1830240622","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028364813&doi=10.1002%2feji.1830240622&partnerID=40&md5=6a177c42156de85fa4d82360d609733b","Unit of Experimental Medicine, International Institute of Cellular and Molecular Pathology, St-Luc Hospital, Catholic University of Louvain, Brussels, Belgium; Laboratory of Pathology, St-Luc Hospital, Catholic University of Louvain, Brussels, Belgium; Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, United States; Wistar Institute, Philadelphia, United States","Coutelier, J.‐P., Unit of Experimental Medicine, International Institute of Cellular and Molecular Pathology, St-Luc Hospital, Catholic University of Louvain, Brussels, Belgium; Godfraind, C., Laboratory of Pathology, St-Luc Hospital, Catholic University of Louvain, Brussels, Belgium; Dveksler, G.S., Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, United States; Wysocka, M., Wistar Institute, Philadelphia, United States; Cardellichio, C.B., Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, United States; Noël, H., Laboratory of Pathology, St-Luc Hospital, Catholic University of Louvain, Brussels, Belgium; Holmes, K.V., Department of Pathology, Uniformed Services University of the Health Sciences, Bethesda, United States","The expression of carcinoembryonic antigen (CEA)‐related glycoproteins that have been associated with intercellular adhesion and that serve as receptors for mouse hepatitis virus (MHV) was analyzed in cells from the immune system of BALB/c mice using immunolabeling and RNA polymerase chain reaction amplification of receptor transcripts. These glycoproteins, which are called biliary glycoproteins, were highly expressed in B lymphocytes, including cells of the B‐la (CD5+) lineage, and in macrophages, but were not detectable in resting T lymphocytes. Similarly, murine cell lines of B cell and macrophage origin expressed messenger RNA encoding CEA‐related molecules, while the corresponding mRNA was only slightly detectable in a T cell line. These CEA‐related cell adhesion glycoproteins were also expressed in endothelial cells. Therefore, their specific interaction with their so far unknown ligand may be of functional importance in cellular interactions in the immune response. Monoclonal antibody directed against these glycoproteins blocked MHV‐A59 infection of the B cell‐derived SP20 cell line. Thus, the functional receptors for MHV on B lymphocytes, like those on murine fibroblasts, are isoforms of CEA‐related glycoproteins. Treatment of B cells with anti‐receptor antibody also blocked B cell‐mediated cytotoxicity against MHV‐A59‐infected fibroblasts, indicating that this phenomenon is mediated by interaction of viral attachment protein on the infected target cells with specific CEA‐related receptor glycoproteins on the effector B cells. Copyright © 1994 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim","Adhesion molecule; B lymphocyte; Carcinoembryonic antigen; Mouse hepatitis virus receptor","carcinoembryonic antigen; cd5 antigen; glycoprotein; messenger rna; monoclonal antibody; rna polymerase; virus protein; virus receptor; animal cell; animal experiment; animal tissue; antibody labeling; antigen expression; article; b lymphocyte; controlled study; cytotoxicity; effector cell; endothelium cell; female; fibroblast; immune adherence; immune response; macrophage; mouse; murine hepatitis coronavirus; nonhuman; polymerase chain reaction; priority journal; t lymphocyte; target cell; Animal; Antibodies, Viral; B-Lymphocytes; Base Sequence; Cell Adhesion Molecules; Cell Line; Cytotoxicity, Immunologic; Female; Macrophages; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Receptors, Virus; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.","Springer, T.A., (1990) Nature, 346, p. 425; Turbide, C., Rojas, M., Stanners, C.P., Beauchemin, N., (1991) J. 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Immunol., 11, p. 767; White, J.M., Littman, D.R., (1989) Cell, 56, p. 725; Sattentau, Q.J., Weiss, R.A., (1988) Cell, 52, p. 631; Greve, J.M., Davis, G., Meyer, A.M., Forte, C.P., Connolly Yost, S., Marlor, C.W., Kamarck, M.E., McClelland, A., (1989) Cell, 56, p. 839; Staunton, D.E., Merluzzi, V.J., Rothlein, R., Barton, R., Marlin, S.D., Springer, T.A., (1989) Cell, 56, p. 849; Mendelsohn, C.L., Wimmer, E., Racaniello, V.R., (1989) Cell, 56, p. 855; Bang, F.B., Warwick, A., MOUSE MACROPHAGES AS HOST CELLS FOR THE MOUSE HEPATITIS VIRUS AND THE GENETIC BASIS OF THEIR SUSCEPTIBILITY (1960) Proceedings of the National Academy of Sciences, 46, p. 1065; Smith, A.L., Cardellichio, C.B., Winograd, D.F., de Souza, M.S., Barthold, S.W., Holmes, K.V., (1991) J. Infect. Dis., 163, p. 879; Boorman, G.A., Luster, M.I., Dean, J.H., Campbell, M.L., Lauer, L.A., Talley, F.A., Wilson, R.E., Collins, M.J., (1982) Am. J. Pathol., 106, p. 110; Dempsey, W.L., Smith, A.L., Morahan, P.S., (1986) J. Leuk. Biol., 39, p. 559; de Souza, M.S., Smith, A.L., (1991) Lab. Anim. Sci., 41, p. 112; Lamontagne, L., Descoteaux, J.‐P., Jolicoeur, P., (1989) J. Immunol., 142, p. 4458; Jolicoeur, P., Lamontagne, L., (1990) Adv. Exp. Med. Biol., 276, p. 543; Virelizier, J.‐L., Virelizier, A.‐M., Allison, A.C., (1976) J. Immunol., 117, p. 748; Coutelier, J.‐P., van der Logt, J.T.M., Heessen, F.W.A., Vink, A., van Snick, J., (1988) J. Exp. Med., 168, p. 2373; Coutelier, J.‐P., van der Logt, J.T.M., Heessen, F.W.A., (1991) J. Immunol., 147, p. 1383; Smith, A.L., Barthold, S.W., de Souza, M.S., Bottomly, K., (1991) Arch. Virol., 121, p. 89; Scalzo, A.A., Anders, E.M., (1985) J. Immunol., 135, p. 3524; Anders, E.M., Scalzo, A.A., Rogers, G.N., White, D.O., (1986) J. Virol., 60, p. 476","Coutelier, J.‐P.; Unit of Experimental Medicine, ICP, UCL, 7430, Av. Hippocrate, Bruxelles, B-1200, Belgium",,,00142980,,,"8206098","English","Eur. J. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0028364813
"Murray R.S., Cai G.-Y., Hoel K., Johnson S., Cabirac G.F.","7403022204;57199040369;6602461039;57207906756;6602498805;","Coronaviruses and multiple sclerosis",1994,"Advances in Experimental Medicine and Biology","342",,,"353","357",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028353254&partnerID=40&md5=2fcdf3c2a242edf7b9bdc45c4f5a0f1c","Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States","Murray, R.S., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States; Cai, G.-Y., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States; Hoel, K., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States; Johnson, S., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States; Cabirac, G.F., Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States",[No abstract available],,"complementary dna; virus antigen; virus rna; animal cell; cellular immunity; conference paper; controlled study; coronavirus; dna library; gene amplification; human; human cell; human tissue; immunohistochemistry; mouse; multiple sclerosis; nonhuman; polymerase chain reaction; priority journal; virus detection; virus infection; Animal; Astrocytes; Astrocytoma; Base Sequence; Brain; Cells, Cultured; Coronavirus; Human; Mice; Molecular Sequence Data; Multiple Sclerosis; Neurons; Polymerase Chain Reaction; RNA, Viral; Spinal Cord; Support, Non-U.S. Gov't; Tumor Cells, Cultured",,"Murray, R.S.; Rocky Mt. Multiple Sclerosis Center, Colorado Neurological Institute, Swedish Medical Center, 701 E. Hampden Ave., Englewood, CO 80150, United States",,,00652598,,AEMBA,"8209754","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028353254
"Wege H., Schliephake A., Korner H., Flory E., Wege H.","7005516646;6602329536;16166611800;7003965470;7005516646;","Coronavirus induced encephalomyelitis: An immunodominant CD4+ - T cell site on the nucleocapsid protein contributes to protection",1994,"Advances in Experimental Medicine and Biology","342",,,"413","418",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028349893&partnerID=40&md5=43a2412358aa39859fe16406c500c641","Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany","Wege, H., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany, Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Schliephake, A., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Korner, H., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Flory, E., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany; Wege, H., Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany, Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany","In this communication we present clear evidence, that the N-protein of MHV-JHM contains immunodominant CD4+ T-cell sites. These sites were recognized by the immune system of virus infected Lewis rats. In previous investigations we have shown, that CD4+ T-cell lines with specificity for defined viral proteins can be selected from diseased Lewis rats and mediate protection, if transferred to otherwise lethally infected animals. To define regions of the N-protein, which are immunodominant for the T-cell response, we employed bacterially expressed N-protein and truncated subfragments of N as an antigen. We demonstrate, that T-cells from MHV-JHM infected, diseased Lewis rats recognized with high prevalence the carboxyterminal subfragment C4-N (95 aa) and to some extent the adjacent C3-N protein. The same results were obtained with T-cells derived from rats immunized with bacterially expressed N-protein or from animals vaccinated by a stable N-protein expressing vaccinia recombinant. Finally, transfer of CD4+ line T-cells to MHV-JHM infected rats specific for C4-N mediated protection against acute disease.",,"capsid protein; cd4 antigen; guanine nucleotide binding protein; animal experiment; animal model; antigen specificity; carboxy terminal sequence; cellular immunity; conference paper; controlled study; coronavirus; disease course; encephalomyelitis; immunogenicity; lymphocyte subpopulation; lymphocyte transfer; lymphoid cell line; molecular recognition; mouse; murine encephalomyelitis virus; nonhuman; priority journal; protein domain; virus nucleocapsid; Animal; Capsid; CD4-Positive T-Lymphocytes; Coronavirus Infections; Encephalomyelitis; Immunodominant Epitopes; Immunotherapy, Adoptive; Murine hepatitis virus; Rats; Rats, Inbred Lew; Recombinant Fusion Proteins; Support, Non-U.S. Gov't; Vaccination; Viral Core Proteins; Viral Vaccines; Virulence",,"Wege, H.; Institute of Virology/Immunobiology, Versbacher Strasse 7, D-97078 Wurzburg, Germany",,,00652598,,AEMBA,"7911644","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028349893
"Schwender S., Hein A., Imrich H., Dorries R.","7003953447;8047618900;6602841707;7003359298;","On the role of different lymphocyte subpopulations in the course of coronavirus MHV IV (JHM)-induced encephalitis in Lewis rats",1994,"Advances in Experimental Medicine and Biology","342",,,"425","430",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028347610&partnerID=40&md5=4c96d6396338dd1cd90864fd27790753","Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany","Schwender, S., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Hein, A., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Imrich, H., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Dorries, R., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany",[No abstract available],,"animal experiment; animal model; animal tissue; b lymphocyte; cellular immunity; conference paper; disease course; humoral immunity; lymphocyte subpopulation; lymphocyte transfer; murine hepatitis coronavirus; nonhuman; priority journal; rat; t lymphocyte; virus encephalitis; virus neutralization; Animal; B-Lymphocytes; Brain; Coronavirus Infections; Encephalomyelitis; Immunity, Cellular; Immunosuppression; Immunotherapy, Adoptive; Lymphocyte Subsets; Murine hepatitis virus; Rats; Rats, Inbred Lew; Spinal Cord; Support, Non-U.S. Gov't; Whole-Body Irradiation",,"Schwender, S.; Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany",,,00652598,,AEMBA,"8209763","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028347610
"Martin Calvo M., Simarro I.","6507677556;6602938097;","Antigenicity of structural polypeptides from CVC: A trial with experimental animals [ANTIGENICIDAD DE LAS PROTEINAS ESTRUCTURALES DEL CORONAVIRUS CANINO (CVC): ENSAYO EN ANIMALES DE EXPERIMENTACION]",1994,"Medicina Veterinaria","11","1",,"36","40",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028343590&partnerID=40&md5=e09b662349888148059e0f15a1acf42a","Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, Avda. Puerta de Hierro, s/n, 28040 Madrid, Spain","Martin Calvo, M., Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, Avda. Puerta de Hierro, s/n, 28040 Madrid, Spain; Simarro, I., Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, Avda. Puerta de Hierro, s/n, 28040 Madrid, Spain","In this study was compared the antigenicity of structural polypeptides from CCV. Beagle pups were inoculated with whole virus or subviral preparations. Pups were challenged by oral administration of virulent CCV. Antibody titers in sera were analysed by neutralisation test, ELISA and immunoblotting. Results show good perspectives for the use of S glicoprotein as an effective immunogen for a subunit vaccine.","canine coronavirus; immunity; structural polypeptides","antibody; polypeptide; virus vaccine; animal model; article; coronavirus; dog; enzyme linked immunosorbent assay; immunoblotting; nonhuman; veterinary medicine",,"Martin Calvo, M.; Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, Avda. Puerta de Hierro, s/n, 28040 Madrid, Spain",,,02128292,,MDVEB,,"Spanish","MED. VET.",Article,"Final",,Scopus,2-s2.0-0028343590
"Barthold S.W., Smith A.L.","7103367422;57203012240;","Role of host age and genotype in murine enterotropic coronavirus infection",1994,"Advances in Experimental Medicine and Biology","342",,,"371","376",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028330826&partnerID=40&md5=29e8803cb9c38822c26312579be98357","Section of Comparative Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, United States","Barthold, S.W., Section of Comparative Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, United States; Smith, A.L., Section of Comparative Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, United States",[No abstract available],,"adolescent; age; aged; animal cell; animal model; animal tissue; conference paper; controlled study; disease severity; genotype; host; infection sensitivity; inoculation; intestine infection; mouse; murine hepatitis coronavirus; newborn; nonhuman; priority journal; virus cell interaction; virus infection; virus infectivity; virus replication; virus titration; Age Factors; Animal; Animals, Newborn; Animals, Suckling; Brain; Colon; Coronavirus Infections; Digestive System; Disease Susceptibility; Genotype; Mice; Mice, Inbred BALB C; Mice, Inbred Strains; Murine hepatitis virus; Organ Specificity; Support, U.S. Gov't, P.H.S.; Virulence",,"Barthold, S.W.; Section of Comparative Medicine, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06510, United States",,,00652598,,AEMBA,"8209756","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028330826
"Joo M., Makino S.","23008647300;7403067550;","Analysis of the CIS-acting elements of coronavirus transcription",1994,"Advances in Experimental Medicine and Biology","342",,,"91","97",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326927&partnerID=40&md5=6abdd984931868dbfde3665963a5d6ac","Department of Microbiology, University of Texas, Austin, TX 78712, United States","Joo, M., Department of Microbiology, University of Texas, Austin, TX 78712, United States; Makino, S., Department of Microbiology, University of Texas, Austin, TX 78712, United States",[No abstract available],,"animal cell; conference paper; mouse; murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; rna synthesis; rna transcription; virus genome; Base Sequence; Comparative Study; Consensus Sequence; Defective Viruses; Gene Expression Regulation, Viral; Genes, Structural, Viral; Molecular Sequence Data; Murine hepatitis virus; Nucleic Acid Conformation; Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; Sequence Homology, Nucleic Acid; Support, U.S. Gov't, P.H.S.; Transcription, Genetic",,"Joo, M.; Department of Microbiology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"8209777","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028326927
"Laude H., Vautherot J.-F.","7006652624;6701457086;","Coronaviruses: Molecular biology and virus-host interactions. Preface",1994,"Advances in Experimental Medicine and Biology","342",,,"v","vi",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028326920&partnerID=40&md5=973c7256179753c1bd44551f427a3134","INRA, Jouy-en-Josas, France","Laude, H., INRA, Jouy-en-Josas, France; Vautherot, J.-F., INRA, Jouy-en-Josas, France",[No abstract available],,"carcinoembryonic antigen; complementary dna; microsomal aminopeptidase; virus protein; central nervous system infection; coronavirus; editorial; gene expression; hepatitis virus; human; molecular cloning; nonhuman; priority journal; protein structure; torovirus; virus genome",,"Laude, H.; INRA, Jouy-en-Josas, France",,,00652598,,AEMBA,,"English","ADV. EXP. MED. BIOL.",Editorial,"Final",,Scopus,2-s2.0-0028326920
"Holmes K.V., Dveksler G., Gagneten S., Yeager C., Lin S.-H., Beauchemin N., Look A.T., Ashmun R., Dieffenbach C.","7201657724;6603790777;6602898805;7004844391;7407608684;7005461095;7102132660;7003934839;7004852757;","Coronavirus receptor specificity",1994,"Advances in Experimental Medicine and Biology","342",,,"261","266",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028299350&partnerID=40&md5=085488d68da6199769e4865c20e67737","Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States","Holmes, K.V., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Dveksler, G., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Gagneten, S., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Yeager, C., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Lin, S.-H., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Beauchemin, N., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Look, A.T., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Ashmun, R., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States; Dieffenbach, C., Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States",[No abstract available],,"virus receptor; conference paper; coronavirus; gene expression; infection sensitivity; murine hepatitis coronavirus; nonhuman; priority journal; virus adsorption; virus cell interaction; virus genome; virus infection; virus replication; Animal; Comparative Study; Coronavirus; Genetic Predisposition to Disease; Hamsters; Human; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Organ Specificity; Protein Binding; Rats; Receptors, Virus; Support, U.S. Gov't, P.H.S.; Viral Envelope Proteins",,"Holmes, K.V.; Department of Pathology, Uniformed Services Univ. Health Sci., Bethesda, MD 20814-4799, United States",,,00652598,,AEMBA,"8209740","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028299350
"Vennema H., Heijnen L., Rottier P.J.M., Horzinek M.C., Spaan W.J.M.","7003697291;7004331664;7006145490;7102624836;7007172944;","A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal",1994,"Advances in Experimental Medicine and Biology","342",,,"209","214",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028293998&partnerID=40&md5=e98d7a5348a9e67beb0ca1d9da9ff4ca","Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands","Vennema, H., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Heijnen, L., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Rottier, P.J.M., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Horzinek, M.C., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands; Spaan, W.J.M., Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands","A new protein of the feline infectious peritonitis virus (FIPV) was discovered in lysates of infected cells. Expression of the gene encoding open reading frame (ORF) 6b of FIPV in recombinant vaccinia virus infected cells was used to identify it as the 6b protein. It is a novel type of viral glycoprotein whose function is not clear. It is a soluble protein contained in microsomes; its slow export from the cell is caused by the presence of an ER-retention signal at the C-terminus. This amino acid sequence, KTEL, closely resembles the consensus KDEL-signal of soluble resident ER proteins. A mutant 6b protein with the C-terminal sequence KTEV became resistant to digestion by endo-β-N-acetylglucosaminidase H with a half-time that was reduced threefold. In contrast, a mutant with the sequence KDEL was completely retained in the ER. The FIPV 6 bp protein is the fist example of a viral protein with a functional KDEL-like ER-retention signal.",,"virus protein; amino acid sequence; animal cell; carboxy terminal sequence; conference paper; coronavirus; endoplasmic reticulum; nonhuman; open reading frame; priority journal; protein analysis; signal transduction; vaccinia virus; viral genetics; Amino Acid Sequence; Animal; Biological Transport; Cats; Cell Line; Coronavirus, Feline; Culture Media, Conditioned; Endoplasmic Reticulum; Hela Cells; Human; Kidney; Microsomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Open Reading Frames; Protein Processing, Post-Translational; Recombinant Fusion Proteins; Viral Nonstructural Proteins",,"Vennema, H.; Department of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3508 TD Utrecht, Netherlands",,,00652598,,AEMBA,"8209732","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028293998
"Kim Y.-N., Lai M.M.C., Makino S.","55699505200;7401808497;7403067550;","Site-specific sequence repair of coronavirus defective interfering RNA by RNA recombination and edited RNA",1994,"Advances in Experimental Medicine and Biology","342",,,"137","142",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028265963&partnerID=40&md5=c7fb8a013b663557dc63e0155e480f16","Department of Microbiology, University of Texas, Austin, TX 78712, United States","Kim, Y.-N., Department of Microbiology, University of Texas, Austin, TX 78712, United States; Lai, M.M.C., Department of Microbiology, University of Texas, Austin, TX 78712, United States; Makino, S., Department of Microbiology, University of Texas, Austin, TX 78712, United States",[No abstract available],,"recombinant rna; virus rna; animal cell; conference paper; mouse; murine hepatitis coronavirus; nonhuman; northern blotting; polymerase chain reaction; priority journal; rna analysis; rna sequence; rna structure; rna transcription; viral genetics; virus recombination; Amino Acid Sequence; Animal; Astrocytoma; Base Sequence; Cell Line; Comparative Study; Defective Viruses; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Open Reading Frames; Point Mutation; Polymerase Chain Reaction; Recombination, Genetic; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Proteins; Virus Replication",,"Kim, Y.-N.; Department of Microbiology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"8209720","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028265963
"Boireau P., Madelaine M.F., Saulnier D., Laporte J., Vautherot J.F.","6701747186;6603372900;56516574200;7201972588;6701457086;","Identification, expression in E. coli and insect cells of the non- structural protein NS2 encoded by mRNA2 of bovine coronavirus (BCV)",1994,"Advances in Experimental Medicine and Biology","342",,,"69","74",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028265961&partnerID=40&md5=9360cf1ed181b84b342fee9a58a406c7","CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France","Boireau, P., CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France; Madelaine, M.F., CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France; Saulnier, D., CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France; Laporte, J., CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France; Vautherot, J.F., CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France","The coding part of mRNA 2 (ORF2) of BCV (F15 strain) was cloned and sequenced. The comparison of our sequence data with the sequence of the same ORF of BCV Quebec strain previously published revealed a major difference in the length of the C-terminal part of the NS2 protein. In vitro transcription and translation of ORF2 resulted in the synthesis of a single protein migrating with a Mr of 31 kDa. The ORF2 was fused in frame with the glutathione S transferase gene (GSH) in the pGEX vector. The fusion protein was synthesized as inclusion bodies which were concentrated and used to raise a monospecific antiserum. Alternatively the fusion protein was solubilized, purified by affinity chromatography and cleaved with Factor Xa to yield pure recombinant NS2. The ORF2 was also expressed in the baculovirus system and the recombinant proteins expressed in pro- and eukaryotic systems were compared on the basis of their size and immunoreactivity. Immunoprecipitation performed with the monospecific antiserum allowed us to identify NS2 in HRT18 infected cells, to follow its kinetic of synthesis, and to ascertain that NS2 was not incorporated in the virion as a minor structural component.",,"blood clotting factor 10a; glutathione transferase; hybrid protein; recombinant protein; virus antibody; virus messenger rna; virus protein; animal cell; carboxy terminal sequence; conference paper; coronavirus; escherichia coli; immunoprecipitation; insect; molecular cloning; nonhuman; nucleotide sequence; open reading frame; priority journal; protein synthesis; rna transcription; rna translation; virus gene; Animal; Antibody Specificity; Base Sequence; Cell Line; Cloning, Molecular; Comparative Study; Coronavirus, Bovine; Escherichia coli; Factor Xa; Gene Expression; Genes, Structural, Viral; Genetic Vectors; Human; Immune Sera; Moths; Nucleopolyhedrovirus; Open Reading Frames; Rabbits; Recombinant Fusion Proteins; Rectal Neoplasms; RNA, Viral; Tumor Cells, Cultured; Viral Nonstructural Proteins",,"Boireau, P.; CNEVA-Lab. Central Recherches Vet., 22 rue P. Curie, 94703 Maisons-Alfort Cedex, France",,,00652598,,AEMBA,"8209773","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028265961
[No author name available],[No author id available],"Revision of the taxonomy of the Coronavirus, Torovirus and Arterivirus genera.",1994,"Archives of Virology","135","1-2",,"227","237",,58,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028252018&partnerID=40&md5=af60457b1178c67ed842e567ebfe357a",,"",[No abstract available],,"animal; Arterivirus; article; classification; comparative study; Coronavirus; physiology; Torovirus; ultrastructure; virion; virus genome; virus replication; Animal; Arterivirus; Comparative Study; Coronavirus; Genome, Viral; Torovirus; Virion; Virus Replication",,,,,03048608,,,"8198447","English","Arch Virol",Article,"Final",,Scopus,2-s2.0-0028252018
"Goncharuk E.I., Fuks P.P., Shevtsova Z.V.","7005858472;36885213700;7004158851;","Human and simian coronaviruses [Koronavirusy cheloveka i obez'ian.]",1994,"Voprosy Virusologii","39","1",,"2","6",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028251556&partnerID=40&md5=ad759e376b2884f8834da83aa0a47704",,"Goncharuk, E.I.; Fuks, P.P.; Shevtsova, Z.V.",[No abstract available],,"animal; animal disease; Coronavirus; gastrointestinal disease; Haplorhini; human; intestine; isolation and purification; microbiology; monkey disease; pathogenicity; review; virus infection; Animal; Coronavirus; Coronavirus Infections; Gastrointestinal Diseases; Haplorhini; Human; Intestines; Monkey Diseases",,"Goncharuk, E.I.",,,05074088,,,"8160442","Russian","Vopr Virusol",Review,"Final",,Scopus,2-s2.0-0028251556
"Weiss S.R., Hughes S.A., Bonilla P.J., Turner J.D., Leibowitz J.L., Denison M.R.","57203567044;22956252200;7004225518;7404250580;7006843902;7101971810;","Coronavirus polyprotein processing.",1994,"Archives of virology. Supplementum","9",,,"349","358",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028249434&partnerID=40&md5=9850944ebde2c913cc1a89ad8704cc4b","Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States","Weiss, S.R., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States; Hughes, S.A., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States; Bonilla, P.J., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States; Turner, J.D., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States; Leibowitz, J.L., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States; Denison, M.R., Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, United States","MHV gene 1 contains two ORFs in different reading frames. Translation proceeds through ORF 1a into ORF 1b via a translational frame-shift. ORF 1a potentially encodes three protease activities, two papain-like activities and one poliovirus 3C-like activity. Of the three predicted activities, only the more amino terminal papain-like domain has been demonstrated to have protease activity. ORF 1a polypeptides have been detected in infected cells by the use of antibodies. The order of polypeptides encoded from the 5' end of the ORF is p28, p65, p290. p290 is processed into p240 and p50. Processing of ORF1a polypeptides differs during cell free translation of genome RNA and in infected cells, suggesting that different proteases may be active under different conditions. Two RNA negative mutants of MHV-A59 express greatly reduced amounts of p28 and p65 at the non-permissive temperature. These mutants may have defects in one or more viral protease activities. ORF 1b, highly conserved between MHV and IBV, potentially contains polymerase, helicase and zinc finger domains. None of these activities have yet been demonstrated. ORF 1b polypeptides have yet been detected in infected cells.",,"gene 1 protein, Coronavirus; protein precursor; virus antibody; virus protein; animal; article; biological model; cell culture; cell free system; comparative study; genetics; immunology; metabolism; mouse; Murine hepatitis coronavirus; open reading frame; protein processing; protein synthesis; sequence analysis; species difference; virus gene; Animals; Antibodies, Viral; Cell-Free System; Cells, Cultured; Genes, Viral; Mice; Models, Genetic; Murine hepatitis virus; Open Reading Frames; Protein Biosynthesis; Protein Precursors; Protein Processing, Post-Translational; Sequence Analysis; Species Specificity; Viral Proteins",,"Weiss, S.R.",,,09391983,,,"8032266","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028249434
"Taguchi F., Ikeda T., Makino S., Yoshikura H.","7103209890;7404132888;7403067550;7005249195;","A Murine Coronavirus MHV-S Isolate from Persistently infected Cells Has a Leader and Two Consensus Sequences between the M and N Genes",1994,"Virology","198","1", 71041,"355","359",,6,"10.1006/viro.1994.1041","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028246512&doi=10.1006%2fviro.1994.1041&partnerID=40&md5=e79ea6976949db169f312989d9ae4a62","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigash, Kodaira, Tokyo 187, Japan; Department of Microbiology, University of Texas at Austin, Austin, TX,78212-1095;, United States; Department of Bacteriology, University of Tokyo, Hongo, Tokyo 113, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigash, Kodaira, Tokyo 187, Japan; Ikeda, T., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigash, Kodaira, Tokyo 187, Japan; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX,78212-1095;, United States; Yoshikura, H., Department of Bacteriology, University of Tokyo, Hongo, Tokyo 113, Japan","A plaque-cloned mouse hepatitis virus mutant, MHV-S No. 8, was isolated from Ki-BALB cells persistently infected with MHV-S. The mRNAs 1 to 6 were larger in the mutant, whereas there was no difference between the two viruses in the size of the smallest mRNA, mRNA 7. Sequence analyses of the genomic RNA, mRNA 6, and mRNA 7 of the two viruses revealed that an additional 111 nt were inserted just upstream of the intergenic consensus sequence preceding the N gene in MHV-S No. 8. The inserted region consisted of two different parts; the 3′-most 30 nt corresponded to nucleotides 28 to 57 of the leader sequence and the 5′-most 81 nt corresponded to nucleotides 58 to 138 of mRNA 7. This structure of No. 8 was most likely generated by RNA-RNA recombination between genomic RNA and subgenomic RNA species. The nucleotide insertion in the intergenic sequence between genes M and N resulted in two consensus sequences separated by 111 nt. Primer extension analysis revealed that the amount of a slightly larger, subgenomic mRNA resulting from initiation of synthesis at the upstream consensus sequence was only 5% of the usual sized mRNA 7 initiated from the downstream consensus sequence. © 1994 Academic Press. All rights reserved.",,"matrix protein; sialidase; signal peptide; animal cell; article; controlled study; mouse; murine hepatitis coronavirus; nonhuman; northern blotting; nucleotide sequence; persistent virus infection; priority journal; virus mutant; Animal; Base Sequence; Capsid; Cells, Cultured; Consensus Sequence; Coronavirus Infections; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Core Proteins; Viral Matrix Proteins","Lai, M.M.C., (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lee, H., Shieh, C., Gorbalenya, A.E., Loonin, R.V., Lamonica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., (1991) Virology, 180, pp. 567-582; Spaan, W., Cavanagh, D., Horznek, M.C.J., (1988) Gen. Virol, 69, pp. 2939-2952; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., (1983) J. Virol, 46, pp. 1027-1033; Siddell, S., Wege, H., Ter Meulen, V.J., (1983) Gen. Virol, 64, pp. 761-776; Shieh, C.-K., Soe, L.H., Makino, S., Chang, M.-F., Stohlman, S.A., Lai, M.M.C., (1987) Virology, 156, pp. 321-330; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., (1981) J. Virol, 39, pp. 823-834; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., (1984) Proc. Natl. Acad. Sci. Usa, 81, pp. 3626-3630; Sethna, P.B., Hung, S.-L., Brian, D.A., (1989) Proc. Natl. Acad.Sci. Usa, 86, pp. 5626-5630; Sawicki, S.G., Sawicki, D.L., (1990) J. Virol, 64, pp. 1050-1056; Sethna, P.B., Hofmann, A.M., Brian, D.A., (1991) J. Virol, 65, pp. 320-325; Hofmann, M.A., Brian, D.A., (1991) J. Virol, 65, pp. 6331-6333; Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K., Lai, M.M.C., Lauoe, H., Stddell, S.G., Talbot, P.J., (1990) Virology, 176, pp. 306-307; King, B.B., Potts, B.J., Brian, D.A., (1985) Virus Res, 2, pp. 53-59; Yoshikura, H., Tejima, S., (1981) Virology, 113, pp. 503-511; Taguchi, F., Siddell, S., Wege, H.H., Ter Meulen, V., (1985) J. Virol, 44, pp. 487-492; Skinner, M.A., Siddell, S., (1983) G. Nucleic Acid Res, 5, pp. 5045-5054; Yokomori, K., Lai, M.M.C., (1991) J. Virol, 65, pp. 5605-5608; Makino, S., Taguchi, F., Hayami, M., Fujiwara, K., (1983) Microbiol.Immunol, 27, pp. 445-454; Taguchi, F., Hayashi, T., Yamada, A., Fujiwara, K., (1978) Jpn. J.Exp. Med, 48, pp. 369-371; Gubler, U., Hofman, B.J., (1983) Gene, 25, pp. 263-269; Pfleiderer, M., Skinner, M.A., Siddell, S., (1986) G., Nucleic Acid Res, 14, p. 6338; Winship, P.R., (1989) Nucleic Acid Res, 17, p. 1266; Makino, S., Lai, M., (1989) M. C., Virology, 57, pp. 227-232; Sambrook, J., Fritsch, E.F., Maniatis, T., Molecularclon-Ing (1989) Cold Spring Harbor Laboratory, pp. 779-782. , 2nd Ed, Cold Spring Harbor, New York; Mounir, S., Talbot, P.J., (1993) Virology, 192, pp. 355-360; Makino, S., Joo, J., (1993) J. Virol, 67, pp. 3304-3311",,,,00426822,,,"8259671","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028246512
"Imrich H., Schwender S., Hein A., Dorries R.","6602841707;7003953447;8047618900;7003359298;","Phenotypic and functional characterization of CD4+ T-cells infiltrating the central nervous system of rats infected with coronavirus MHV IV",1994,"Advances in Experimental Medicine and Biology","342",,,"437","442",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028207360&partnerID=40&md5=c5e25ce03b4b23e0304144854d1a23dc","Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany","Imrich, H., Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Schwender, S., Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Hein, A., Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany; Dorries, R., Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany",[No abstract available],,"cd4 antigen; animal cell; animal experiment; animal model; conference paper; lymphocyte proliferation; lymphocyte subpopulation; lymphocytic infiltration; lymphoid tissue; murine hepatitis coronavirus; nonhuman; phenotype; priority journal; rat; strain difference; t lymphocyte; virus encephalitis; Animal; Brain; CD4-Positive T-Lymphocytes; Comparative Study; Coronavirus Infections; Demyelinating Diseases; Disease Susceptibility; Encephalomyelitis; Immunologic Memory; Immunophenotyping; Lymph Nodes; Lymphocyte Activation; Models, Biological; Murine hepatitis virus; Neck; Rats; Rats, Inbred BN; Rats, Inbred Lew; Species Specificity; Spinal Cord; Support, Non-U.S. Gov't",,"Imrich, H.; Inst. fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, Wurzburg 8700, Germany",,,00652598,,AEMBA,"7911645","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028207360
"Hein A., Imrich H., Schwender S., Dorries R.","8047618900;6602841707;7003953447;7003359298;","Functional characterization of CD8+ lymphocytes during coronavirus MHV IV induced encephalitides in rats",1994,"Advances in Experimental Medicine and Biology","342",,,"431","436",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028205756&partnerID=40&md5=d60bbfa7b1f2901aebdd6de30fc46bb4","Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany","Hein, A., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany; Imrich, H., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany; Schwender, S., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany; Dorries, R., Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany",[No abstract available],,"cd8 antigen; animal experiment; animal model; animal tissue; cell isolation; conference paper; cytotoxicity; demyelination; lymphocyte activation; lymphocyte subpopulation; lymphocytic infiltration; lymphoid cell; murine hepatitis coronavirus; nonhuman; priority journal; rat; virus encephalitis; Animal; Brain; Cell Line; Comparative Study; Coronavirus Infections; Cytotoxicity, Immunologic; Demyelinating Diseases; Disease Susceptibility; Encephalomyelitis; Hybridomas; Murine hepatitis virus; Paralysis; Rats; Rats, Inbred BN; Rats, Inbred Lew; Species Specificity; Spinal Cord; Support, Non-U.S. Gov't; T-Lymphocytes, Cytotoxic",,"Hein, A.; Institut fur Virologie/Immunbiologie, Universitat Wurzburg, Versbacher Str. 7, 8700 Wurzburg, Germany",,,00652598,,AEMBA,"8209765","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028205756
"Hofmann M.A., Senanayake S.D., Brian D.A.","57203181972;7004008817;7006460232;","An intraleader open reading frame is selected from a hypervariable 5' terminus during persistent infection by the bovine coronavirus",1994,"Advances in Experimental Medicine and Biology","342",,,"105","109",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028204245&partnerID=40&md5=c06414c219e2095c51360b1f80a44cf9","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Hofmann, M.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Senanayake, S.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States",[No abstract available],,"complementary dna; structural protein; virus messenger rna; amino acid substitution; animal cell; conference paper; coronavirus; molecular cloning; nonhuman; nucleotide sequence; open reading frame; persistent infection; priority journal; rna translation; sequence homology; virus replication; Amino Acid Sequence; Base Sequence; Coronavirus, Bovine; DNA, Complementary; Genes, Structural, Viral; Human; Molecular Sequence Data; Open Reading Frames; Point Mutation; Rectal Neoplasms; RNA, Messenger; RNA, Viral; Tumor Cells, Cultured; Virus Replication",,"Hofmann, M.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States",,,00652598,,AEMBA,"8209714","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028204245
"Saif L.J., van Cott J.L., Brim T.A.","7102226747;6506805561;6602281848;","Immunity to transmissible gastroenteritis virus and porcine respiratory coronavirus infections in swine",1994,"Veterinary Immunology and Immunopathology","43","1-3",,"89","97",,46,"10.1016/0165-2427(94)90124-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028151228&doi=10.1016%2f0165-2427%2894%2990124-4&partnerID=40&md5=a0188fd104ec2fc3ff6889998a31dea1","Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, United States","Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, United States; van Cott, J.L., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, United States; Brim, T.A., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, United States","Despite the pioneering efforts to identify correlates of passive immunity to transmissible gastroenteritis virus (TGEV), effective vaccines for the control of TGE in suckling pigs have remained elusive. The initial concept of an enteromammary immunologic axis in monogastrics originated from studies of lactogenic immunity to TGEV in swine. These studies revealed that infection of pregnant swine with virulent TGEV stimulated high titers of SIgA antibodies in milk which correlated with protection of suckling pigs against TGE; parenteral or oral inoculation with live attenuated or killed TGEV vaccines induced mainly IgG antibodies in milk which generally provided poor protection to suckling pigs. The recent appearance of PRCV infections in swine and continuing studies of TGEV infections, present a unique model for further studies of mucosal immunity. Research using these viruses has increased our understanding of the various components of the common mucosal immune system and their interactions. Although the most important consideration in designing an effective vaccine for TGEV is the stimulation of GALT through intestinal virus replication, studies addressing the contribution of BALT to immunity to TGEV and PRCV may provide insights for alternative vaccine approaches. The mechanism by which exposure to PRCV elicits a variable degree of immunity to TGEV challenge is unknown. Virus replication in the gut or respiratory tract is a major factor affecting the magnitude of the immune response at the respective site and may be necessary for the recruitment of specific immune cells from other mucosal inductive sites, i.e., GALT to BALT and BALT to GALT migration. Further studies on the induction and immune regulation of specific responses to TGEV and PRCV that affect the distribution patterns of IgM-, IgG- and IgA-antibody-secreting cells (ASC) and T lymphocytes should provide valuable insights for optimizing vaccine regimens to elicit the highest mucosal immune responses and optimal protection against TGEV challenge. © 1994.",,"vaccine; antibody response; coronavirus; gastroenteritis; immune response; immunoregulation; lactation; nonhuman; pregnancy; review; swine; virus replication; Animal; Antibodies, Viral; Coronavirus; Coronavirus Infections; Female; Gastroenteritis, Transmissible, of Swine; Immunity, Active; Immunity, Cellular; Immunization, Passive; Pregnancy; Respiratory Tract Infections; Swine; Swine Diseases; Transmissible gastroenteritis virus; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","(1991) National Swine Survey, , National Animal Health Monitoring System, USDA, APHIS, Veterinary Services, Anonymous; Aynaud, (1991) Vet. Microbiol., 26, p. 227; Bae, (1991) J. Clin. Microbiol., 29, p. 215; Bernard, Bottreau, Aynaud, Have, Szymansky, (1989) Vet. Microbiol., 21, p. 1; Berthon, Bernard, Salmon, Binns, (1990) J. Immunol. Methods, 131, p. 173; Bohl, Gupta, Olquin, Saif, (1972) Infect. Immun., 6, p. 289; Bohl, Saif, (1975) Infect. Immun., 11, p. 23; Brim, van Cott, Lunney, Saif, (1994) Am. J. Vet. Res., 55, p. 494; T.A. Brim, J.L. van Cott, J.K. Lunney and L.J. Saif (1994b), submitted; Callebaut, Correa, Pensaert, (1988) Journal of General Virology, 69, p. 1725; Callebaut, Cox, Pensaert, van Deun, (1990) Coronaviruses and Their Diseases, p. 421. , D. Cavenaugh, T.D.K. Brown, Plenum Press, New York; Cepica, Derbyshire, (1984) Can. J. Comp. Med., 48, p. 258; Cepica, Derbyshire, (1984) Can. J. Comp. Med., 48, p. 360; Charley, Laude, La Bonnardière, (1987) Ann. Inst. Pasteur/Virol., 138, p. 183; Cox, Pensaert, Callebaut, (1993) Vaccine, 11, p. 267; DeDiego, Laviada, Enjuanes, Escribano, (1992) J. Virol., 66, p. 6502; Enjuanes, (1990) Adv. Exp. Med. Biol., 276, p. 159; Frederick, Bohl, (1976) J. Immunol., 116, p. 1000; Furuuchi, Shimizu, Kumagai, (1979) Vet. Microbiol., 3, p. 169; Halbur, Paul, Vaughn, Andrews, (1993) J. Vet. Diagn. Invest., 5, p. 184; Hill, (1989) Vet. Med., 89, p. 432; Hooper, Haelterman, (1966) J. Am. Vet. Med. Assoc., 149, p. 1580; Kodama, Ogata, Shimizu, (1980) Am. J. Vet. Res., 40, p. 740; Koren, Herberman, (1983) Immunol. Today, 4, p. 97; La Bonnardiere, Lefevre, Charley, (1994) Vet. Immunol. Immunopathol., 43, p. xxx; Laude, (1990) Vet. Microbiol., 23, p. 147; Laude, Gelfi, Lavenant, Charley, (1992) J. Virol., 66, p. 743; Lenstra, Posthumus, Meloen, (1990) Adv. Exp. Med. Biol., 276, p. 159; Lesnick, Derbyshire, (1988) Vet. Immunol. Immunopathol., 18, p. 109; Mensik, Salajka, Stepanek, Ulmann, Prochazka, Dressler, (1978) Ann Rech Vet, 9, p. 255; Pensaert, Cox, (1989) Agri-Practice, 10, p. 17; Paton, Brown, (1990) Vet. Res. Comm., 14, p. 329; Rasschaert, Durate, Laude, (1990) J. Gen. Virol., 71, p. 2599; Saif, (1976) Ph.D. Thesis, , The Ohio State University; Saif, Bohl, Gupta, (1972) Infect Immun, 6, p. 289; Saif, Bohl, (1977) Infect. Immun., 16, p. 961; Saif, Bohl, (1982) Annals of the New York Academy of Sciences, 409, p. 708; Saif, Wesley, (1992) Diseases of Swine, pp. 362-386. , A.D. Leman et al., Iowa State University Press, Ames; Shimizu, Shimizu, (1979) Am. J. Vet. Res., 40, p. 208; Shimizu, Shimizu, (1979) Infect. Immun., 23, p. 239; Simkins, Weilnau, Bias, Saif, (1992) Am. J. Vet. Res., 53, p. 1253; Simkins, Weilnau, van Cott, Brim, Saif, (1993) Am. J. Vet. Res., 54, p. 254; Sprino, Ristic, (1982) Am. J. Vet. Res., 43, p. 255; Stone, Kemeny, Woods, Jensen, (1977) Am. J. Vet. Res., 38, p. 1285; Underdahl, Mebus, Torres-Medina, (1975) Am. J. Vet. Res., 36, p. 1473; van Cott, Brim, Simkins, Saif, (1993) J. Immunol., 150, p. 3990; van Cott, Brim, Lunney, Saif, (1994) J. Immunol., 152, p. 3980; van Nieuwstadt, Pol, (1989) Veterinary Record, 128, p. 43; van Nieuwstadt, Zetstra, Boonstra, (1989) Vet. Rec., 125, p. 58; Weisz-Carrington, Roux, McWilliams, Phillips-Quagliata, Lamm, (1978) Proc. Natl. Acad. Sci., 75, p. 2928; Welch, Saif, (1988) Arch. Virol., 101, p. 221; Welch, Saif, Ram, (1988) Am. J. Vet. Res., 49, p. 1228; Wesley, Wesley, Paul, Hall, Woods, (1986) Ann. N.Y. Acad. Sci., 463, p. 412; Wesley, Woods, Correa, Enjuanes, (1988) Vet. Microbiol., 18, p. 197; Wesley, Wesley, Woods, (1991) J. Vet. Diag. Invest., 3, p. 29; Wesley, Woods, Cheung, (1991) J. Virol., 65, p. 3369; Woods, (1977) Am. J. Vet. Res., 38, p. 1267; Woods, Wesley, (1992) Can. J. Vet. Res., 56, p. 170","Saif, L.J.; Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, United States",,,01652427,,VIIMD,"7856068","English","Vet. Immunol. Immunopathol.",Article,"Final",,Scopus,2-s2.0-0028151228
"Penzes Z., Tibbles K., Shaw K., Britton P., Brown T.D.K., Cavanagh D.","55761804900;6507790687;7202206256;57203302770;56248391000;26642890500;","Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus",1994,"Virology","203","2", 71486,"286","293",,54,"10.1006/viro.1994.1486","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027930161&doi=10.1006%2fviro.1994.1486&partnerID=40&md5=8282171c41bef506d36d02352bab2a46","Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom; Division of Virology, Department of Pathology, University of Cambridge, Cambridgeshire, Cambridge, CB2 1QP, United Kingdom; Veternity Medical Research, Institute Of the Hungarian Academy of Sciences, Budapest, Hungary","Penzes, Z., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom, Veternity Medical Research, Institute Of the Hungarian Academy of Sciences, Budapest, Hungary; Tibbles, K., Division of Virology, Department of Pathology, University of Cambridge, Cambridgeshire, Cambridge, CB2 1QP, United Kingdom; Shaw, K., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom; Britton, P., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Cambridgeshire, Cambridge, CB2 1QP, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom","The Beaudette strain of IBV was passaged 16 times in chick kidney cells. Total cellular RNA was analyzed by Northern hybridization and was probed with 32P-labeled cDNA probes corresponding to the first 2 kb of the 5' end of the genome, but excluding the leader, and to the last 1.8 kb of the 3' end of the genome. A new, defective IBV RNA species (CD-91) was detected at passage 6. The defective RNA, present in total cell extract RNA and In oligo-(dT)30-selected RNA from passage 15, was amplified by the reverse transcription-polymerase chain reaction (RT-PCR) to give four fragments. The oligonucleotides used were selected such that CD-91 RNA, but not the genomic RNA, would be amplified. Cloning and sequencing of the PCR products showed that CD-91 comprises 9.1 kb and has three regions of the genome. It contains 1133 nucleotides from the 5' end of the genome, 6322 from gene 1b corresponding to position 12,423 to 18,744 in the IBV genome, and 1626 from the 3' end of the genome. At position 749 one nucleotide, an adenine residue, was absent from CD-91 RNA. By Northern hybridization CD-91 RNA was detected in virions in higher amounts than the subgenomic mRNAs. © 1994 Academic Press, Inc.",,,"Alonso-Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., Replication and morphogenesis of avian corona virus in Vero cells and their inhibition by monensin (1984) Virus Res, 1, pp. 153-167; Baric, R.S., Stohlman, S.A., Razavi, M.K., Lai, M.M.C., Characterisation of leader related small RNAs in coronavirus infected cells. Further evidence for leader primed mechanism transcription (1985) Virus Res, 3, pp. 19-33; Baric, R.S., Shieh, C., Stohlman, S.A., Lai, M.M.C., (1987) Analysis of Intracellular Small Rnas of Mouse Hepatitis Virus: Evidence for Discontinuous Transcription. Virology, 156, pp. 342-354; Barrett, A.D.T., Dimmock, N.J., (1986) Defective Interfering Viruses and Infections in Animals. Curr. Top. Microb. Immunol, 128, pp. 55-84; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol, 68, pp. 57-77; Brown, T.D.K., Binns, M.M., Boursnell, M.E.G., A leader sequence is present on mRNA A of avian infectious bronchitis virus (1984) I Gen. Virol, 65, pp. 1437-1442; Cavanagh, D., Davis, P.J., Pappin, D.J.C., Binns, M.M., Boursnell, M.E.G., Brown, T., Coronavirus IBV: Partial amino terminal of the spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41 (1986) Virus Res, 4, pp. 133-143; Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K.V., Lai, M.M.C., Lauoe, H., Sipdell, S.G., Talbot, P.J., Recommendations of the Coronavirus Study Group for the nomenclature of the structural proteins, mRNAs, and genes of coro-naviruses (1990) Virology, 176, pp. 306-307; Cavanagh, D., Davis, P.J., Cook, J.K.A., Infectious bronchitis virus: Evidence for recombination within the Massachusetts serotype (1992) Avian Pathol, 21, pp. 401-408; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chlorophorm extraction (1987) Anal. Biochem, 162, pp. 156-159; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus Dl-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol, 66, pp. 5898-5905; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol, 66, pp. 3522-3530; Furuya, T., Macnaughton, T.B., La Monica, N., Lai, M., Natural evolution of coronavirus defective-interfering RNA involves RNA recombination (1993) Virology, 194, pp. 408-413; Hofmann, M.A., Sethna, P.B., Brian, D., Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture (1990) J. Virol, 64, pp. 4108-4114; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription; Duration of primary transcription initiation activity and effects of subgenomic RNA transcription on RNA replication (1992) J. Virol, 66, pp. 3339-3346; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Viroi, 68, pp. 2615-2623; Kang, C.Y., Allen, R., Host function-dependent induction of defective interfering particles of vesicular stomatitis virus (1978) J. Virol, 25, pp. 202-206; Kang, C.Y., Weide, L.G., Tischfield, J.A., Suppression of vesicular stomatitis virus defective interfering particle generation by a function(S) associated with human chromosome 16 (1981) J. Virol, 40, pp. 946-952; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stholman, S.A., Lai, M., (1988) In Vivo RNA-RNA Recombination of Coronavirus in Mouse Brain. J. Virol, 62, pp. 1810-1813; Kim, Y., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Kim, Y., Jeong, Y., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Kusters, J.G., Jager, E.J., Niesters, H.G.M., Van Der Zeijst, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M.C., Coronavirus; Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Viroi, 56, pp. 449-456; Lee, H., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lin, Y., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Viroi, 67, pp. 6110-6118; Makino, S., Taguchi, F., Fujiwara, K., Defective interfering particles of mouse hepatitis virus (1984) Virology, 133, pp. 9-17; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol, 54, pp. 329-336; Makino, S., Stohlman, S.A., Lai, M.M., Leader sequences of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA transcription (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 4204-4208; Makino, S., Shieh, C., Soe, L., Lai, M., Baker, S.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus; Localization of a possible RNA-packaging signal (1990) J. Virol, 64, pp. 6045-6053; Reed, L.J., Muench, H., A simple method of estimating fifty per cent endpoints (1938) Am. J. Hyg, 27, pp. 493-497; Sambrook, J., Fritsch, E.F., Maniatis, T., Molecular Cloning; A Laboratory Manual (1989) Cold Spring Harbor Laboratory, , Cold Spring Harbor, NY; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription; Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol, 64, pp. 1050-1056; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol, 65, pp. 320-325; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronavi ruses: Structure and genome expression (1988) J. Gen. Virol, 69, pp. 2939-2952; Staden, R., The current status and portability of our sequence handling software (1986) Nucleic Acids Res, 14, pp. 217-233; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3' end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol, 65, pp. 3219-3226; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Yokomori, K., Banner, L.R., Lai, M.M.C., Coronavirus mRNA transcription; UV light transcriptional mapping studies suggest an early requirement for genome-length template (1992) J. Viroi, 66, pp. 4671-4678; Zhao, X., Shaw, K., Cavanagh, D., Presence of subgenomic mRNAs in virions of coronavirus IBV (1993) Virology, 196, pp. 172-178","Cavanagh, D.; Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG16 ONN, United Kingdom",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0027930161
"Stuhler A., Flory E., Wege H., Wege H.","6602388166;7003965470;7005516646;7005516646;","Coronaviruses from persistent infected cell cultures and brain tissue: Molecular analysis of the S gene of an avirulent variant",1994,"Advances in Experimental Medicine and Biology","342",,,"393","394",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027793883&partnerID=40&md5=2f3acab92c2e9e98908dfbfc014dcdc8","Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany","Stuhler, A., Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany; Flory, E., Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany; Wege, H., Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany, Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany; Wege, H., Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany, Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany",[No abstract available],,"vitronectin; membrane protein; spike glycoprotein, coronavirus; virus envelope protein; amino acid substitution; animal tissue; conference paper; coronavirus; gene sequence; mouse; nonhuman; pathogenicity; priority journal; sequence homology; strain difference; virus encephalitis; virus gene; virus virulence; amino acid sequence; animal; article; brain; cell culture; chemistry; comparative study; genetics; microbiology; molecular genetics; Murine hepatitis coronavirus; nucleotide sequence; polymerase chain reaction; rat; virulence; virus latency; Amino Acid Sequence; Animal; Base Sequence; Brain; Cells, Cultured; Comparative Study; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Rats; Support, Non-U.S. Gov't; Viral Envelope Proteins; Virulence; Virus Latency",,"Stuhler, A.; Inst. of Virology and Immunobiology, Versbacher Strasse 7, W-8700 Wurzburg, Germany",,,00652598,,AEMBA,"8209759","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0027793883
[No author name available],[No author id available],"Proceedings of the 5th International Symposium on Coronaviruses. Chantilly, France, September 13-18, 1992.",1994,"Advances in experimental medicine and biology","342",,,"1","478",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027793581&partnerID=40&md5=5465ab580d30b831af168ec71f473f5a",,"",[No abstract available],,"virus protein; virus receptor; animal; conference paper; Coronavirus; genetics; human; pathogenicity; virus gene; virus infection; Animals; Coronaviridae; Coronavirus Infections; Genes, Viral; Humans; Receptors, Virus; Viral Proteins",,,,,00652598,,,"7911641","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0027793581
"Aymard M., Chomel J.J., Allard J.P., Thouvenot D., Honegger D., Floret D., Boissel J.-P., Collet J.-P., Dürr F., Gillet J., Bossard N., Lyon L.","55306003900;7005666484;16148849600;7005288678;6603906233;7101620621;35943986000;16552082100;7006546113;56660877700;56054941500;18536571100;","Epidemiology of viral infections and evaluation of the potential benefit of OM-85 BV on the virologic status of children attending day-care centers",1994,"Respiration","61",,,"24","31",,33,"10.1159/000196377","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028146215&doi=10.1159%2f000196377&partnerID=40&md5=e6312b9e7ae0e6a720feded40a9c3fab","Laboratoirede Virologie, Centre Hospitalo-Universitaire de Lyon, Lyon, France; DDASS, Lyon, France; Pavilion S, Hòpital Edouard Ilerriot, Lyon, France; Unité de Pharmacologie Clinique, Lyon, France","Aymard, M., Laboratoirede Virologie, Centre Hospitalo-Universitaire de Lyon, Lyon, France; Chomel, J.J., Laboratoirede Virologie, Centre Hospitalo-Universitaire de Lyon, Lyon, France; Allard, J.P., Laboratoirede Virologie, Centre Hospitalo-Universitaire de Lyon, Lyon, France; Thouvenot, D., Laboratoirede Virologie, Centre Hospitalo-Universitaire de Lyon, Lyon, France; Honegger, D., DDASS, Lyon, France; Floret, D., Pavilion S, Hòpital Edouard Ilerriot, Lyon, France; Boissel, J.-P., Unité de Pharmacologie Clinique, Lyon, France; Collet, J.-P., Unité de Pharmacologie Clinique, Lyon, France; Dürr, F., Unité de Pharmacologie Clinique, Lyon, France; Gillet, J., Unité de Pharmacologie Clinique, Lyon, France; Bossard, N., Unité de Pharmacologie Clinique, Lyon, France; Lyon, L., Unité de Pharmacologie Clinique, Lyon, France","Viral investigations were performed during 4 winter seasons (88/89, 89/90, 92/93, 93/94) in children attending day-care centers (DCCs) in the Rhône Département in eastern France. Over the total observation period of 4 winter seasons. 780 children were screened with a nasal swab for the presence of viruses. Of those. 230 (29.5%) had a positive viral culture. The viruses identified were respiratory syncytial virus (RSV). influenza A and B virus, parainfluenza virus, coronavirus, rhinovirus. adenovirus and enterovirus. During that time, 83 epidemic events in 47 DCC were recorded. A particular virus was judged to be causally related to an epidemic if the identical virus was isolated in ≥ 3 children during the same outbreak of respiratory diseases. Thus, in 51 cases (61.4%) of all epidemics, the following viruses were responsible for an epidemic: RSV (n = 23), coronavirus (n = 10) (only during the season of 1993-1994), influenza A virus (n = 6), rhinovirus (n = 4), enterovirus (n =4). adenovirus (n = 3) and parainfluenza virus (n = 1). Except for the somewhat surprising accumulation of coronavirus epidemics during the winter of 1993-1994, there were only minor seasonal variations from one year to another. As expected. RSV accounted for about one third of all respiratory' tract infections in children attending DCCs and was therefore the most important single causative agent. These results are compared with data from children who did not attend a DCC and were cared for in a private practice. During the winter of 1989-1990, the viral epidemiological survey was performed at the same time and in parallel to a double-blind, placebo-controlled clinical study investigating the efficacy of OM-85 BV. an immunoactivc bacterial extract. This study, enrolling 423 children attending DCCs demonstrated a protective effect of OM-85 BV in significantly reducing the risk of recurrent infections of the upper respiratory tract during the treatment period with the compound. 34% of all participating children (75 in the verum group. 70 in the placebo group) were enrolled in an additional virological study. In these patients. RSV was isolated 10 times in the placebo group, but only 5 times in the treated group (p < 0.05) and influenza A virus was present in 4 children in the placebo group, but only in 1 infant in the verum group giving a total of 14 positive virologic results in the placebo group versus 6 in the verum group (p < 0.05). Despite the small numbers of children investigated for their virologic status during respiratory infectious outbreaks, there was a statistically significant difference in the prevalence of virus carriers in favor of the children treated with OM-85 BV. These results corroborate the clinical findings. © 1994 S. Karger AG, Basel.","Children; Day-care centers; OM-85 BV; Respiratory viruses","bacterium lysate; immunostimulating agent; adenovirus; child care; childhood disease; clinical trial; conference paper; controlled clinical trial; controlled study; coronavirus; day care; double blind procedure; drug efficacy; enterovirus; epidemic; france; human; infant; influenza virus a; influenza virus b; major clinical study; nose smear; oral drug administration; parainfluenza virus; preschool child; priority journal; respiratory syncytial pneumovirus; respiratory tract infection; rhinovirus; seasonal variation; virus culture; virus infection; winter; Adjuvants, Immunologic; Bacteria; Cell Extracts; Child; Child Day Care Centers; Child, Preschool; Disease Outbreaks; France; Humans; Infant; Risk Factors; Seasons; Virus Diseases; Viruses","Collet, J.P., Burtin, P., Kramer, M.S., Floret, D., Bossard, N., Dueruet, T., Epicrèche Research Group, Type of day care setting and repeated infections Pediatrics, , Press; Wald, E.R., Dashefsky, B., Beyers, C., Guerra, N., Taylor, F., Frequency and severity of infections in daycare (1988) J Pediatr, 112, pp. 540-546; Wald, E.R., Guerra, N., Byers, C., Frequency and severity of infections in day care: Three-year follow-up (1991) J Pediatr, 118, pp. 509-514; Hurwitz, E.S., Gunn, W.J., Pinsky, P.F., Schonberger, L.B., Risk of respiratory illness associated with day-care attendance. A nationwide study (1991) Pediatrics, 87, pp. 62-69; Anderson, U., Parker, R.A., Strikas, R.A., Farrar, J.A., Gangarosa, E.J., Keyserling, H.L., Sikes, R.K., Day-care center and hospitalization for lower respiratory tract illness (1988) Pediatrics, 82, pp. 300-308; Collet, J.P., Burtin, P., Gillet, J., Bossard, N., Ducruet, T., Dürr, F., Risk of infectious diseases in children attending different ypes of day-care setting (1994) Respiration, 61, pp. 16-19. , Epicrèche Research Group; Parrot, R.H., Kim, H.W., Brandt, C.D., Chanock, R.W., Respiratory syncytial virus in infants and children (1974) Prcv Med, 3, pp. 473-480; Welliver, R.C., Detection, pathogenesis and therapy of respiratory syncytial virus infections (1988) Clin Microbiol Rev, 1, pp. 27-39; Hall, W.J., Hall, C.B., Alterations in pulmonary function following respiratory viral infection (1979) Chest, 76, pp. 458-465; Chomel, J.J., Thouvenot, D., Onno, M., Gourreau, J.M., Aymard, M., Rapid diagnosis of influenza infection by NP antigen using an immunocapture ELISA test (1989) J Virol Methods, 25, pp. 81-92; Chomel, J.J., Pardon, D., Thouvenot, D., Allard, J.P., Aymard, M., Comparison between three methods for direct diagnosis of influenza and the conventional isolation procedure (1991) Biologicals, 19, pp. 287-292; Lennette, E.H., Halonen, P., Murphy, F.A., Laboratory Diagnosis of Infectious Diseases (1988) Principles and practice. Viral, Rickettsial and Chlamydial Diseases, 2. , Berlin, Springer; Chomel, J.J., Collet, J.P., Floret, D., Dauvergne, B., Szymczyszyn, P., Aymard, M., Suivi des infections virales épidémiques dans les crêches lyonnaiscs de décembre 1988 à juin 1989 (1990) Pediatrie, 45, pp. 412-413; Collet, J.P., Dueruet, T., Kramer, M.S., Haggerty, J., Floret, D., Chomel, J.J., Dürr, F., Stimulation of nonspecific immunity to reduce the risk of recurrent infections in children attending day care centers (1993) Pediatr Infect DisJ, 12, pp. 648-652; Aymard, M., Chomel, J.J., Allard, J.P., Collet, J.P., Floret, D., (1992) Suivi virologique des epidemics en collectivité durant deux années consécutives, , Des résultats intéressants sur le virus respiratoire syncytial. Rencontres de Pédiatrie. L’Immunostimulation. Laboratoires Fournier Thylmer. Istanbul, sept; Aymard, M., Influenza and acute respiratory infections in winters 1989-1990, 1992-1993, 1993-1994 (1990) Informal WHO Meetings on Influenza Vaccines, February, , 1994; Loda, F.A., Glezen, W.P., Clyde, W.A., Respiratory disease in group day care (1972) Pediatrics, 49, pp. 428-437; Chomel, J.J., Thouvenot, D., Allard, J.P., Aymard, M., Prevalence of coronavirus in the respiratory infections during the winter 1990-1991 (1991) Poster 3rd Joint Meeting of the European Group for Rapid Viral Diagnosis and the European Society against Viral Diseases, , Strasbourg, August; Chomel, J.J., Thouvenot, D., Allard, J.P., Aymard, M., Prévalence des infections rcspiratoires à coronavirus pendant les hivers 1990-1991 et 1991-1992 (1992) Poster 3e Congrès de la Société Française de Microbiologie, , Lyon, avril; Collet, J.P., Boissel, J.P., OM-85 BV: Primary versus secondary prevention (1994) Respiration, 61, pp. 20-23; Orcel, B., Delelaux, B., Baud, M., Derenne, J.P., Oral immunisation with bacterial extracts for protection against acute bronchitis in elderly, institutionalized patients with chronic bronchitis (1994) Eur Respir J, 7, pp. 446-452; Mauël, J., Stimulation of immunoprotective mechanisms by OM-85 BV: A review of results from in vivo and in vitro studies (1994) Respiration, 61, pp. 8-15","Aymard, M.; Laboratoire de Virologie, Centre Hospitalo-Universitaire de Lyon, 8, avenue Rockefeller, Cedex 08, Lyon, F-69373, France",,,00257931,,,"7800968","English","Respiration",Article,"Final",,Scopus,2-s2.0-0028146215
"Schlesinger S., Makino S., Linial M.L.","7005337025;7403067550;7103138036;","Cis-acting genomic elements and trans-acting proteins involved in the assembly of rna viruses",1994,"Seminars in Virology","5","1",,"39","49",,23,"10.1006/smvy.1994.1005","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0002855593&doi=10.1006%2fsmvy.1994.1005&partnerID=40&md5=701fe2b6e57d0c90421fe3d4797024fd","Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110-1093, United States; Department of Microbiology, University of Texas, Austin, TX 78712, United States; Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, United States","Schlesinger, S., Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110-1093, United States; Makino, S., Department of Microbiology, University of Texas, Austin, TX 78712, United States; Linial, M.L., Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, United States","There is now considerable evidence that a specific site (or sites) in the genome of an RNA virus interacts with a viral protein to initiate the assembly of the virus ribonucleoprotein or nucleocapsid. We describe the progress that has been made in defining these elements for a number of different viruses: the togavirus, Sindbis virus; the coronavirus, mouse hepatitis virus; influenza A virus; several retroviruses; and the hepadnavirus, hepatitis B virus. The importance of cis-acting elements in packaging has been established for all of these viruses. For Sindbis virus, specificity in the binding of the RNA element to a region of the viral capsid protein in vitro has also been demonstrated. © 1994 Academic Press. All rights reserved.","Packaging signals; RNA structures; RNA-protein binding",,"Caspar, D., Klug, A., Physical principles in the construction of regular viruses (1962) Cold Spr Harb Symp Quant Biol, 27, pp. 1-24; Fox, J.M., Johnson, J.E., Young, M.Y., RNA/protein interactions in icosahedral virus assembly (1994) Semin Virol, 5, pp. 51-60; Dubois-Dalcq, M., Holmes, K.V., Rentier, B., (1984) Assembly of Enveloped RNA Viruses, , Springer, New York; Schlesinger, S., Schlesinger, M., Replication of Togaviridae and Flaviviridae (1990) Virology, 1, pp. 697-711. , Fields BN, Knipe DM, Raven Press, New York; Strauss, E.G., Strauss, J.H., Structure and replication of the alphavirus genome (1986) The Togaviridae and Flaviviridae, pp. 35-90. , Schlesinger S, Schlesinger MJ, Plenum Press, New York; Weiss, B., Nitschko, H., Ghattas, I., Wright, R., Schlesinger, S., Evidence for specificity in the encapsidation of Sindbis virus RNAs (1989) J Virol, 63, pp. 5310-5318; Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., Delius, H., The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino terminal region (1980) Proc Natl Acad Sci USA, 77, pp. 6376-6380; Rice, C.M., Strauss, J.H., Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins (1981) Proc Natl Acad Sci USA, 78, pp. 2062-2066; Hahn, C.S., Strauss, E.G., Strauss, J.H., Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease (1985) Proc Nat] Acad Sci USA, 82, pp. 4648-4652; Hahn, C.S., Strauss, J.H., Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease (1990) J Virol, 64, pp. 3069-3073; Choi, H.-K., Tong, L., Minor, W., Dumas, P., Boege, U., Rossmann, M.G., Wengler, G., Structure of Sindbis virus core protein reveals a chymotrypsin like serine protease and the organization of the virion (1991) Nature, 354, pp. 37-43; Geigenmiiller-Gnirke, U., Nitschko, H., Schlesinger, S., Deletion analysis of the capsid protein of Sindbis virus: Identification of the RNA binding region (1993) J Virol, 67, pp. 1620-1626; Wengler, G., Wurkner, D., Wengler, G., Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores (1992) Virology, 191, pp. 880-888; Singh, I., Helenius, A., Role of ribosomes in Semliki Forest virus nucleocapsid uncoating (1992) J Virol, 66, pp. 7049-7058; Boursnell, M., Brown, T., Foulds, I.J., Green, P.F., Tomley, F.M., Binnis, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J Gen Virol, 68, pp. 57-77; Lai, M., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J Virol, 26, pp. 236-242; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J Virol, 33, pp. 449-462; Lai, M., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J Virol, 39, pp. 823-834; Lai, M., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, cytoplasmic RNA virus (1984) Proc Natl Acad Sci USA, 81, pp. 3626-3630; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of noncontiguous sequences (1983) EMBO J, 2, pp. 1939-1944; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol, 65, pp. 320-325; Makino, S., Yokomori, K., Lai, M., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J Virol, 64, pp. 6045-6053; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J Virol, 54, pp. 329-336; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W., A domain at the 3’ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J Virol, 65, pp. 3219-3226; Fosmire, J.A., Hwan, K., Makino, S., Identification and characterization of a coronovirus packaging signal (1992) J Virol, 66, pp. 3522-3530; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interactions between coronavirus leader RNA and nucleocapsid protein (1988) J Virol, 62, pp. 4288-4295; Perfman, S., Ries, D., Bolger, E., Chang, L.-J., Stolzfus, C.M., MHV nucleocapsid synthesis in the presence of cycloheximide and accumulation of negative strand MHV RNA (1986) Virus Res, 6, pp. 261-272; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., RNA-binding proteins of MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Pons, M.W., Schulze, I.T., Hirst, G.K., Isolation and characterization of the ribonucleoprotein of influenza virus (1969) Virology, 39, pp. 250-259; Kingsbury, D.W., Webster, R.G., Some properties of influenza virus nucleocapsids (1969) J Virol, 4, pp. 219-225; Lamb, R.A., The influenza virus RNA segments and their encoded proteins (1983) Genetics of Influenza Viruses, pp. 21-69. , PaleseP, Kingsbury DW, Springer, Vienna; Luytjes, W., Krystal, M., Enami, M., Parvin, J.D., Palese, P., Amplification, expression, and packaging of a foreign gene by influenza virus (1989) Cell, 59, pp. 1107-1113; Hsu, M.-T., Parvin, J.D., Gupta, S., Krystal, M., Palese, P., Genomic RNAs of influenza viruses are held in a circular conformation in virions and in infected cells by a terminal panhandle (1987) Proc Natl Acad Sci USA, 84, pp. 8140-8144; Yamanaka, K., Ishibama, A., Nagata, K., Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores (1990) J Biol Chem, 265, pp. 11151-11155; Honda, A., Ueda, K., Nagata, K., Ishihama, A., Identification of the RNA polymerase-binding site on genome RNA of influenza virus (1987) J Biochem, 102, pp. 1241-1249; Smith, G.L., Hay, A.J., Replication of the influenza virus genome (1982) Virology, 89, pp. 506-516; Akkina, R.K., Chambers, T.M., Nayak, D.P., Mechanism of interference by defective interfering particles of influenza virus: Differentia] reduction of intracellular synthesis of specific polymerase proteins (1984) Virus Res, 1, pp. 687-702; Nakajima, K., Ueda, M., Sugiura, A., Origin of small RNA in von Magnus particles of influenza virus (1979) J Virol, 29, pp. 1142-1148; Hirst, G.K., Mechanism of influenza recombination. 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Factors influencing recombination rates between temperature-sensitive mutants of strain WSN and the classification of mutants into complementation-recombination groups (1973) Virology, 55, pp. 81-93; Lamb, R.A., Choppin, P.W., The gene structure and replication of influenza virus (1983) Annu Rev Biochem, pp. 467-506; Scholtissek, C., Rohde, W., Harms, E., Rott, R., Orlich, M., Boschek, D.B., A possible partial heterozygote of an influenza A virus (1978) Virology, 89, pp. 506-516; Enami, M., Sharma, G., Benham, C., Palese, P., An influenza virus containing nine different RNA segments (1991) Virology, 185, pp. 291-298; Linial, M., Creation of a processed pseudogene by retroviral infection (1987) Cell, 49, pp. 93-102; Dornburg, R., Temin, H.M., Retroviral vector system for the study of cDNA gene formation (1988) Mol Cell Biol, 8, pp. 2328-2334; Jacks, T., Translational suppression in gene expression in retroviruses and retrotransposons (1990) Retroviruses Strategies of Replication, pp. 93-124. , Swanstrom R, Vogt PK, Springer, Berlin; Oroszlan, S., Luftig, R.B., Retroviral proteinases (1990) Retroviruses Strategies of Replication, pp. 153-186. , Swanstrom R, Vogt PK, Springer, Berlin; Linial, M., Medeiros, E., Hayward, W.S., An avian oncovirus mutant (SE2IQlb) deficient in genomic RNA: Biological and biochemical characterization (1978) Cell, 15, pp. 1371-1381; Boeke, J.D., Sandmeyer, S.B., Yeast transposable elements (1991) The Molecular and Cellular Biology of the Yeast Saccharomyces: Genome Dynamics, Protein Synthesis and Energetics, pp. 193-261. , Pringle J, Jones E, Haber J, Cold Spring Harbor Press, New York; Mathias, S.L., Scott, A.F., Kazazian, H.H., Jr., Boeke, J.D., Gabriel, A., Reverse transcriptase encoded by a human transposable element (1991) Science, 254, pp. 1808-1810; Huang, M.J., Summers, J., Infection initiated by the RNA pregenome of a DNA virus (1991) J Virol, 65, pp. 5435-5439; Bartenschlager, R., Junker-Niepmann, M., Schaller, H., The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation (1990) J Virol, 64, pp. 5324-5332; Junker-Niepmann, M., Bartenschlager, R., Schaller, H., A short j-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA (1990) EMBO J, 9, pp. 3389-3396; Hirsch, R.C., Loeb, D.D., Pollack, J.R., Ganem, D., Exacting sequences required for encapsidation of duck hepatitis B virus pregenomic RNA (1991) J Virol, 65, pp. 3309-3316; Nassal, M., Schaller, H., Hepatitis B virus replication (1993) Trends Microbiol; Pollack, J.R., Ganem, D., An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation (1993) J Virol, 67, pp. 3254-3263; Wang, G.-H., Seeger, C., A novel mechanism for reverse transcription in hepatitis B viruses (1993) J Virol; Nassal, M., The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly (1993) J Virol, 66, pp. 4107-4116; Linial, M.L., Miller, A.D., Retroviral RNA packaging: Sequence requirements and implications (1990) Curr Top Microbiol Immunol, 157, pp. 125-152; Alford, R.L., Honda, S., Lawrence, C.B., Belmont, J.W., RNA secondary structure analysis of the packaging signal for moloney murine leukemia virus (1991) Virology, 183, pp. 611-619; Harrison, G.P., Lever, A., The human immunodeficiency virus type 1 packaging signal and major splice donor region have a conserved stable secondary structure (1992) J Virol, 66, pp. 4144-4153; Tounekti, N., Mougel, M., Roy, C., Marquet, R., Darlix, J.-L., Paoletti, J., Ehresmann, B., Ehresmann, C., Effect of dimerization on the conformation of the encapsidation Psi domain of Moloney murine leukemia virus RNA (1992) J Mol Biol, 223, pp. 205-220; Konings, D.A., Nash, M.A., Maizel, J.V., Arlinghaus, R.B., Novel GACG-hairpin pair motif in the 5’ untranslated region of type C retroviruses related to murine leukemia virus (1992) J Virol, 66, pp. 632-640; Aronoff, R., Hajjar, A.M., Linial, M.L., Avian retroviral RNA encapsidation: Reexamination of functional 5’ RNA sequences and the role of nucleocapsid cys-his motifs (1993) J Virol, 67, pp. 178-188; Marquet, R., Baudin, F., Gabus, C., Darlix, J.-L., Mougel, M., Ehresmann, C., Ehresmann, B., Dimerization of human immunodeficiency virus (Type 1) RNA: Stimulation by cations and possible mechanism (1991) Nucl Acids Res, 19, pp. 2349-2337; Sorge, J., Ricci, W., Hughes, S.H., M-acting RNA packaging locus in the 115-nucleotide direct repeat of Rous sarcoma vims (1983) J Virol, 48, pp. 667-675; Aronoff, R., Linial, M.L., Specificity of retroviral RNA packaging (1991) J Virol, 65, pp. 71-80; Mann, R., Baltimore, D., Varying the position of a retrovirus packaging sequence results in the encapsidation of both unspliced and spliced RNAs (1985) J Virol, 54, pp. 401-407; Lever, A., Gottlinger, H., Haseltine, W., Sodroski, J., Identification of a sequence required for efficient packaging of Human Immunodeficiency Virus type 1 RNA into virions (1989) J Virol, 63, pp. 4085-4087; Clavel, F., Orenstein, J.M., A mutant of Human Immunodeficiency Virus with reduced RNA packaging and abnormal particle morphology (1990) J. Virol, 64, pp. 5230-5234; Aldovini, A., Young, R.A., Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging results in production of noninfectious virus (1990) J Virol, 64, pp. 1920-1926; Hunter, E., Macromolecular interactions in the assembly of HIV and other retroviruses (1994) Semin Virol, 5, pp. 71-83; Luban, J., Goff, S.P., Binding of human immunodeficiency virus type 1 (HIV-1) RNA to recombinant HIV-1 gag polyprotein (1991) J Virol, 65, pp. 3203-3212; Hayashi, T., Shioda, T., Iwakura, Y., Shibuta, H., RNA packaging signal of human immunodeficiency virus type 1 (1992) Virology, 188, pp. 590-599; Fu, X., Katz, R.A., Skalka, A.M., Leis, J., Site-directed mutagenesis of the avian retrovirus nucleocapsid protein, pp 12 (1988) J Biol Chem, 263, pp. 2140-2145; Stewart, L., Schatz, G., Vogt, V.M., Properties of avian retrovirus particles defective in viral protease (1990) J Virol, 64, pp. 5076-5092; Oertle, S., Bowles, N., Spahr, P.F., Complementation studies with Rous sarcoma virus gag and gag-pol polyprotein mutants (1992) Virology, 66, pp. 3873-3878; Gorelick, R.J., Henderson, L.E., Hanser, J.P., Rein, A., Point mutants of Moloney murine leukemia virus that fail to package viral RNA: Evidence for specific RNA recognition by a ‘zinc finger-like’ protein sequence (1989) Proc Natl Acad Sci USA, 85, pp. 8420-8424; Gorelick, R.J., Nigida, S.M., Jr., Bess, J.W., Jr., Arthur, L.O., Henderson, L.E., Rein, A., Noninfectious Human Immunodeficiency Virus type 1 mutants deficient in genomic RNA (1990) J Virol, 64, pp. 3207-3211; Merit, C., Gouilloud, E., Spahr, P.-F., Mutations in Rous sarcoma virus nucleocapsid protein pl2 (NCV): Deletions of Cys-His boxes (1988) J Virol, 62, pp. 3328-3333; Meric, C., Goff, S.P., Characterization of Moloney murine leukemia virus mutants with single-am ino-acid substitutions in the Cys-His box of the nucleocapsid protein (1989) J Virol, 63, pp. 1558-1568; Levin, J.G., Grimley, P.M., Ramseur, J.M., Berezesky, I.K., Deficiency of 60 to 70S RNA in murine leukemia virus particles assembled in cells treated with Actinomycin D (1974) J Virol, 14, pp. 152-161; Oertle, S., Spahr, P.F., Role of the gag polyprotein precursor in packaging and maturation of Rous sarcoma virus genomic RNA (1990) J Virol, 64, pp. 5757-5763; Roy, S., Delling, U., Chen, C.-H., Rosen, C., Sonenberg, N., A bulge structure in HIV-1 TAR RNA is required for Tat binding and Tat-mediated iranj-activation (1990) Genes Dev, 4, pp. 1365-1373; Harrison, S.C., A structural taxonomy of DNA-binding domains (1991) Nature, 353, pp. 715-719; Bandziulis, R.J., Swanson, M.S., Dreyfuss, G., RNA-binding proteins as developmental regulators (1989) Genes Dev, 3, pp. 431-437; Kenan, D.J., Query, C.C., Keene, J.D., RNA recognition: Towards identifying determinants of specificity (1991) Trends Biochem Sci, 16, pp. 214-220; Calnan, B.J., Tidor, B., Biancalana, S., Hudson, D., Frankel, A.D., Arginine-mediated RNA recognition: The arginine fork (1991) Science, pp. 1167-1171; Tao, J., Frankel, A.D., Specific binding of arginine to TAR RNA (1992) Proc Natl Acad Sci USA, 89, pp. 2723-2726; Bartel, D.P., Zapp, M.L., Green, M.R., Szostak, J.W., HIV-1 Rev regulation involves recognition of non-Watson-Crick base pairs in viral RNA (1991) Cell, 67, pp. 529-536; Uhlenbeck, O.C., Wu, H.-N., Sampson, J.R., Recognition of RNA by proteins (1987) Molecular Biology of RNA: New Perspectives, pp. 285-294. , Inouye M, Dudock BS, Academic Press, San Diego; Turner, D.R., Joyce, L.E., Buder, P., The tobacco mosaic virus assembly origin RNA. Functional characteristics defined by directed mutagenesis (1988) J Mol Biol, 203, pp. 531-547; Zhong, W., Dasgupta, R., Rueckert, R., Evidence that the packaging signal for nodaviral RNA2 is a bulged stem-loop (1992) Proc Natl Acad Sci USA, 89, pp. 11146-11150",,,,10445773,,,,"English","Semin. Virol.",Article,"Final",,Scopus,2-s2.0-0002855593
"Cegielski J.P., Msengi A.E., Miller S.E.","7003393735;6701668025;7406289098;","Enteric viruses associated with HIV infection in Tanzanian children with chronic diarrhea",1994,"Pediatric AIDS and HIV Infection","5","5",,"296","299",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028149384&partnerID=40&md5=1772403bb7a797c631ebc30cf73f49f6","Department of Medicine, Duke University Medical Center, Durham, NC, United States","Cegielski, J.P., Department of Medicine, Duke University Medical Center, Durham, NC, United States; Msengi, A.E., Department of Medicine, Duke University Medical Center, Durham, NC, United States; Miller, S.E., Department of Medicine, Duke University Medical Center, Durham, NC, United States","Objective. To determine whether specific viruses are associated with HIV infection in Tanzanian children with chronic diarrhea. Design. Cross- sectional survey. Setting. Major national teaching hospital in Dar es Salaam, Tanzania. Patients. Consecutively admitted, human immunodeficiency virus (HIV)-infected and HIV-uninfected children with chronic diarrhea, and controls without diarrhea, aged 15 months to 5 years. Main outcome measure. Enteric viruses identified by electron microscopy (EM) of fecal specimens. Results. Small round structured viruses (SRSV) were more frequent in HIV- infected than HIV-uninfected children with chronic diarrhea (4 of 21 vs 1 of 32, prevalence ratio = 6.09, 90% confidence limits 1.03, 36.14). Rotavirus and coronavirus-like particles (CVLP) were not associated with HIV infection. Conclusion. SRSV may be associated with HIV infection in Tanzanian children with chronic diarrhea. Larger, confirmatory studies are needed.",,"article; child; chronic diarrhea; clinical feature; controlled study; coronavirus; disease association; electron microscopy; enteric virus; human; human immunodeficiency virus; human immunodeficiency virus infection; major clinical study; rotavirus; tanzania; AIDS-Related Opportunistic Infections; Chronic Disease; Coronavirus; Cross-Sectional Studies; Diarrhea; Feces; Gastroenteritis; Human; Norwalk virus; Rotavirus; Support, Non-U.S. Gov't; Tanzania; Virus Diseases",,"Cegielski, J.P.; Department of Medicine, Duke University Medical Center, Durham, NC, United States",,,10455418,,PAHIE,"11361370","English","PEDIATR. AIDS HIV INFECT.",Article,"Final",,Scopus,2-s2.0-0028149384
"Akhter J., Burdette J.M., Qadri S.M.H., Myint S.H.","7007117594;7003971352;16469657300;35479862600;","Aetiology of Gastroenteritis at a Major Referral Centre in Saudi Arabia",1994,"Journal of International Medical Research","22","1",,"47","54",,19,"10.1177/030006059402200106","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028298990&doi=10.1177%2f030006059402200106&partnerID=40&md5=74c9c8bab74935544fa5aec222fa471a","KFSH and RC, Riyadh, Saudi Arabia; Department of Microbiology, University of Leicester, Leicester, United Kingdom","Akhter, J., KFSH and RC, Riyadh, Saudi Arabia; Burdette, J.M., KFSH and RC, Riyadh, Saudi Arabia; Qadri, S.M.H., KFSH and RC, Riyadh, Saudi Arabia; Myint, S.H., Department of Microbiology, University of Leicester, Leicester, United Kingdom","To determine the causes of gastroenteritis at a major referral centre in Saudi Arabia, retrospective study was carried out on 58,110 fresh stools from 42,035 patients. Examination of stool specimens for pathogens was based on the clinical judgement of the physician responsible, so that all specimens were not tested for the presence of all pathogen groups. Bacterial enteropathogens were found in 7.7% of patients; Salmonella species (51.7%) were found to be the most frequent pathogens followed by Campylobacter jejuni (28%) and Shigella species (14.9%). Protozoan or metazoan parasites were detected in 27.8% of patients examined, the most common being Giardia lamblia and Hymenolepsis nana. Of the patients tested for viruses in stool, 14.1% had rotavirus, 5.3% adenovirus, 1.2% small round viruses and 0.3% coronavirus. Clostridium difficile toxin was also found in 9.5% of patients examined. © 1994, SAGE Publications. All rights reserved.","Diarrhoea; Enteropathogens; Gastroenteritis; Intestinal parasites","bacterial toxin; adenovirus; article; campylobacter jejuni; clostridium difficile; coronavirus; feces culture; gastroenteritis; giardia lamblia; human; hymenolepis nana; major clinical study; protozoon; retrospective study; rotavirus; salmonella; saudi arabia; shigella; Animal; Bacteria; Campylobacter jejuni; Comparative Study; Feces; Gastroenteritis; Hospitals, Special; Human; Parasites; Retrospective Studies; Salmonella; Saudi Arabia; Shigella; Viruses","Mitchell, J., Skelton, M.M., Diarrheal infections (1988) Am Fam Physician, pp. 195-207; Guerrant, R., Lohr, J., Williams, E., Acute infectious diarrhea. I. Epidemiology, etiology and pathogenesis (1986) Pediatric Infect Dis, 5, pp. 353-359; Kapikian, A.Z., Kim, H.W., Wyatt, R.G., Human REOVIRUS-like agent as the major pathogen associated with “winter” gastroenteritis in hospitalized infants and young children (1976) N Engl J Med, 294, pp. 965-972; Young, K.H., Bullock, S.L., Melvin, D.M., Ethyl acetate as a substitute for diethyl ether in the formalin – ether sedimentation technique (1979) J Clin Microbial, 10, pp. 852-853; Olarte, J., Papel de los agentes infecciosos (1988) Enfermedades Diarreias en el Nino ed 9, Ediciones Medical del Hospital Infantil de Mexico, pp. 21-27. , (Torregrosa FL, ed); Etheverria, P., Seriwatana, J., Taylor, D.N., A comparative study of enterotoxigenic Escherichia coli, Shigella, Aeromonas, and Vibrio as etiologies of diarrhoea in North East Thailand (1985) Am J Trop Med Hyg, 34, pp. 547-554; Georges, M.C., Wachsmuth, I.K., Meunier, D.M.V., Parasitic, bacterial, and viral enteric pathogens associated with diarrhoea in the Central African Republic (1984) J Clin Microbiol, 19, pp. 571-575; Guerrant, R.L., Kirchoff, L.V., Shields, D.S., Prospective study of diarrhoeal illness in north eastern Brazil: patterns of disease, nutritional impact, etiologies, and risk factors (1983) J Infect Dis, 148, pp. 986-997; Ashenafi, M., Gedebou, M., Salmonella and Shigella in adult diarrhoea in Addis Ababa – prevalence and antibiograms (1985) Trans R Soc Trop Med Hyg, 79, pp. 719-721; Jones, L.V., Rodriguez, R.S., Bacterial induced diarrhoea (1988) Drugs, 36, pp. 6-17. , suppl 4); Al-Bwardy, M.A., Ramia, S., Al-Frayh, A.R., Bacterial, parasitic, and viral enteropathogens associated with diarrhoea in Saudi children (1988) Ann Trop Paediatr, 8, pp. 26-30; Mahgoub, E.S., Chowdhury, N.H., Jamjoum, G., A preliminary survey of intestinal pathogenic bacteria and parasites in King Abdul Aziz Teaching Hospital, Riyadh (1980) Proceedings of the Fourth Saudi Medical Conference, pp. 272-274. , Dammam; Al-Saud, A.S.A., Fecal parasites in non-Saudi catering and domestic staff at the Riyadh Military Hospital (1983) Saudi Med J, 4, pp. 259-262; Bolbol, A.H.S., Mahmoud, A.A., Laboratory and clinical study of intestinal pathogenic parasites among the Riyadh population (1984) Saudi Med J, 5, pp. 159-166; Birch, C.J., Lewis, F.A., Kennett, A study of the prevalence of rotavirus infection in children with gastroenteritis admitted to an infectious disease hospital (1977) J Med Virol, 1, pp. 69-77; Arya, S.C., Parande, C.M., Rotavirus gastroenteritis in the Gizan area of Saudi Arabia, 6, pp. 468-472; Jamjoom, G.A., Ramia, S., Bakir, T., A two year survey of diagnostic virus laboratory services at King Saud University Hospital, Riyadh (1986) Saudi Med J, 7, pp. 166-174; Al-Ahdal, M.N., Qadri, S.M.H., Al-Dayel, F., Incidence of Rotaviral Gastroenteritis at a Referral Centre in Saudi Arabia (1991) Ann Saudi Med, 11, pp. 19-22; Akhter, J., Qadri, S.M.H., Incidence of rotaviral gastroenteritis at a 550-bed tertiary care hospital in Saudi Arabi (1992) Med Sci Res, 20, pp. 195-196; Carlson, J.A.K., Middleton, P.J., Szymanski, M.T., Fatal rotavirus gastroenteritis. An analysis of 21 cases (1978) Am J Dis Child, 132, pp. 477-479; Dutta, S.R., Khalfan, S.A., Baig, B.A., Epidemiology of Rotavirus diarrhoea in children under five years in Bahrain (1990) Int J Epidemiol, 19 (3), pp. 722-727; Uhnoo, I., Olding-Stenkvist, E., Kneuger, A., Clinical features of acute gastroenteritis associated with rotavirus, enteric adenoviruses and bacteria (1986) Arch Dis Child, 61, pp. 732-738; Leite, J.P.G., Pereira, H.G., Azeredo, R.S., Schatzmayr, H.G., Adenoviruses in faeces of children with acute gastroenteritis in Rio de Janeiro, Brazil (1985) J Med Virol, 15, pp. 203-209; Herrmann, J.E., Blacklow, N.R., Perron-Henry, D.M., Incidence of enteric adenoviruses among children in Thailand and the significance of these viruses in gastroenteritis (1988) J Clin Microbiol, 26, pp. 1783-1786; Kidd, A.H., Harley, E.H., Erasmus, M.J., Specific detection and typing of adenovirus types 40 and 41 in stool specimens by dot-blot hybridization (1985) J Clin Microbiol, 22, pp. 934-939; Tiemessen, C.T., Wegerhoff, F.O., Erasmus, M.J., Infection by enteric adenoviruses, rotaviruses and other agents in a rural African environment (1989) J Med Virol, 28, pp. 176-182; Puerto, F.I., Polanco, G.G., Gonzales, M.R., Role of rotavirus and enteric adenovirus in acute paediatric diarrhoea at an urban hospital in Mexico Trans R Soc Trop Med Hyg, 83, pp. 396-398","Qadri, S.M.H.MBC 10, KFSH & RC, PO Box 3354, Riyadh 11211, Saudi Arabia",,,03000605,,,"8187944","English","J. Int. Med. Res.",Article,"Final",,Scopus,2-s2.0-0028298990
"Rangel H.A., Verinaud L., Camargo I.J., Gilioli R., Sakurada J.K.","7003471453;6602378213;6603667046;7003488906;7004164464;","Murine virus contaminant of Trypanosoma cruzi experimental infection.",1994,"Revista do Instituto de Medicina Tropical de São Paulo","36","5",,"423","431",,5,"10.1590/S0036-46651994000500006","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028511170&doi=10.1590%2fS0036-46651994000500006&partnerID=40&md5=982bb98ad9c3680e52aac130d7777179","CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil","Rangel, H.A., CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil; Verinaud, L., CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil; Camargo, I.J., CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil; Gilioli, R., CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil; Sakurada, J.K., CEMIB-UNICAMP, Department of Microbiology and Immunology, Campinas, São Paulo, Brazil","The possibility that some virus contaminants could be altering host response to Trypanosoma cruzi experimental infection was investigated. Data obtained showed that CBA/J mice infected with stocks of parasite maintained in mice (YIUEC) presented higher level of parasitemia and shorter survival times than those infected with a stock (YITC) which was also maintained in mice but had been previously passaged in cell culture. Mouse antibody production tests, performed with the filtered plasma of mice infected with YIUEC, indicated the presence of mouse hepatitis virus (MHV) while no virus was detected when testing the plasma of YITC infected mice. Filtered plasma of YIEUC infected mice was shown to contain a factor able to enhance the level of parasitemia and to reduce the mean survival time of mice challenged with 10(5) YITC. This factor, that could be serially passaged to naïve mice was shown to be a coronavirus by neutralization tests.",,"virus antibody; animal; article; Bagg albino mouse; CBA mouse; Chagas disease; female; immunology; LD 50; male; mouse; Murine hepatitis coronavirus; parasitology; pathogenicity; Trypanosoma cruzi; virology; Animals; Antibodies, Viral; Chagas Disease; Female; Lethal Dose 50; Male; Mice; Mice, Inbred BALB C; Mice, Inbred CBA; Murine hepatitis virus; Trypanosoma cruzi",,"Rangel, H.A.",,,00364665,,,"7569609","English","Rev. Inst. Med. Trop. Sao Paulo",Article,"Final",Open Access,Scopus,2-s2.0-0028511170
"Rossi O.V.J., Kinnula V.L., Tuokko H., Huhti E.","56830754300;7006741070;18736596300;16137531200;","Respiratory viral and Mycoplasma infections in patients hospitalized for acute asthma",1994,"Monaldi Archives for Chest Disease","49","2",,"107","111",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028341274&partnerID=40&md5=a907a690397247933fa354c94501d8fd","Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland","Rossi, O.V.J., Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland; Kinnula, V.L., Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland; Tuokko, H., Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland; Huhti, E., Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland","We evaluated the involvement of viral and Mycoplasma infections in severe attacks of asthma in 112 adult patients admitted to Oulu University Central Hospital for an exacerbation of asthma, during a period of one year. The total number of admissions was 151, and specimens for viral identification were collected from 142 of these. Although the methods for diagnosis of rhinoviruses and coronaviruses were lacking, the diagnosis of a viral or Mycoplasma infection was confirmed in 41 patients (29%) by one or more of the three methods; viral serology, viral culture from a throat wash or viral antigen detection from a nasopharyngeal aspirate. Thirty six of these patients (88%) with confirmed infection also had symptoms suggestive of a viral infection. We conclude that viral and Mycoplasma infections are so often involved in severe asthma attacks of adults that they may play an important role in the induction of such attacks.","asthma; exacerbation of asthma; trigger of asthma; viral infection","Adenovirus; adult; aged; article; asthma; clinical trial; controlled clinical trial; controlled study; female; human; major clinical study; male; Mycoplasma pneumoniae; Parainfluenza virus; respiratory tract infection; virus detection; virus infection",,"Rossi, O.V.J.; Department of Internal Medicine, University of Oulu, Kajaanintie 50, SF-90220 Oulu, Finland",,"PI-ME Tipografia Editrice S.r.l.",11220643,,MACDE,"8049692","English","MONALDI ARCH. CHEST DIS.",Article,"Final",,Scopus,2-s2.0-0028341274
"Mainka S.A., Qiu X., He T., Appel M.J.","6602844349;7402545680;57203272115;7101857422;","Serologic survey of giant pandas (Ailuropoda melanoleuca), and domestic dogs and cats in the Wolong Reserve, China.",1994,"Journal of wildlife diseases","30","1",,"86","89",,34,"10.7589/0090-3558-30.1.86","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028186369&doi=10.7589%2f0090-3558-30.1.86&partnerID=40&md5=893fde386778d17863b525a66b91c149","World Wide Fund for Nature International, Gland, Switzerland","Mainka, S.A., World Wide Fund for Nature International, Gland, Switzerland; Qiu, X., World Wide Fund for Nature International, Gland, Switzerland; He, T., World Wide Fund for Nature International, Gland, Switzerland; Appel, M.J., World Wide Fund for Nature International, Gland, Switzerland","Sera from captive and recently rescued giant pandas (Ailuropoda melanoleuca) in the Wolong Reserve, China, were examined by serum neutralization or hemagglutination inhibition for antibodies to canine distemper virus (CDV), canine coronavirus (CCV), canine herpesvirus (CHV), pseudorabies virus (PRV), canine adenovirus type 2 (CAV), and canine parvovirus (CPV). Serum samples from village domestic dogs and cats, which run free throughout the reserve also were examined. Antibodies against CPV were detected in six of eight giant pandas and all dogs and cats tested. The origin of the virus was not determined. Two of eight giant pandas and two of seven dogs had CDV antibody titers. Three of eight pandas and three of seven dogs had CCV antibody titers. Four of eight pandas and two of seven dogs had CAV titers; the titers in dogs were very high. No pandas or dogs had evidence of exposure to CHV or PRV.",,"virus antibody; Adenovirus; animal; animal disease; article; blood; Canine distemper morbillivirus; Carnivora; cat; cat disease; China; Coronavirus; dog; dog disease; immunology; Parvovirus; Pseudorabies herpetovirus; Varicella zoster virus; virus infection; Adenoviruses, Canine; Animals; Antibodies, Viral; Carnivora; Cat Diseases; Cats; China; Coronavirus, Canine; Distemper Virus, Canine; Dog Diseases; Dogs; Herpesvirus 1, Canid; Herpesvirus 1, Suid; Parvovirus, Canine; Virus Diseases",,"Mainka, S.A.",,,00903558,,,"8151830","English","J. Wildl. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0028186369
"Barlough J.E., Shacklett B.L.","7004310846;6701589733;","Antiviral studies of feline infectious peritonitis virus in vitro",1994,"Veterinary Record","135","8",,"177","179",,12,"10.1136/vr.135.8.177","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028023354&doi=10.1136%2fvr.135.8.177&partnerID=40&md5=521b2608a566e54a791d30f1233cfa6f","Department of Medicine, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Barlough, J.E., Department of Medicine, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Shacklett, B.L., Department of Medicine, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Sixteen compounds were tested for their ability to inhibit the replication in vitro of feline infectious peritonitis virus (FIPV), a coronavirus that causes a lethal, immunologically mediated illness in domestic and exotic cats. Six of the compounds, when incubated with cells and titrations of the virus, were found to reduce the virus titres by 0-401 to 0-833 log10 (P&lt;0.05), using the cytopathic effect as endpoint. Further inhibition studies were performed to determine the 50 per cent effective dose (ED50) levels for these six compounds. Selectivity indices (50 per cent cytotoxic dose [CD50]/ED50) provided the following order of antiviral activity: pyrazofurin &gt; 6-azauridine &gt; 3-deazaguanosine &gt; hygromycin B &gt; fusidic acid &gt; dipyridamole. Compounds which had no statistically significant effect on FIPV in the same assay were caffeic acid, carbodine, 3-deazauridine, 5-fluoroorotic acid, 5-fluorouracil, D(+)glucosamine, indomethacin, D-penicillamine, rhodanine and taurine.",,"3 deazauridine; antivirus agent; azauridine; caffeic acid; carbodine; dipyridamole; fluoroorotic acid; fluorouracil; fusidic acid; glucosamine; guanosine derivative; hygromycin B; indometacin; penicillamine; pirazofurin; rhodanine; taurine; animal cell; antiviral activity; article; cell culture; Coronavirus; cytopathogenic effect; nonhuman; virus inhibition; virus titration; Animalia; Coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus",,"Barlough, J.E.; Department of Medicine, School of Veterinary Medicine, University of California, Davis, CA 95616, United States",,"British Veterinary Association",00424900,,VETRA,"7992474","English","VET. REC.",Article,"Final",,Scopus,2-s2.0-0028023354
"McDonough S.P., Stull C.L., Osburn B.I.","57213758216;7004571359;7005048548;","Enteric pathogens in intensively reared veal calves.",1994,"American journal of veterinary research","55","11",,"1516","1520",,37,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028537680&partnerID=40&md5=056f31d0c6c799e10c9e6f1f26b4949d","Department of Pathology, School of Veterinary Medicine, University of California, Davis, 95616., United States","McDonough, S.P., Department of Pathology, School of Veterinary Medicine, University of California, Davis, 95616., United States; Stull, C.L., Department of Pathology, School of Veterinary Medicine, University of California, Davis, 95616., United States; Osburn, B.I., Department of Pathology, School of Veterinary Medicine, University of California, Davis, 95616., United States","Observations were made on development of diarrhea in special-fed calves (n = 460) on 8 commercial facilities during 2 successive 16-week production cycles at weeks 0, 2, 4, 8, 12, and 16. A total of 23% were affected, with peak number of calves with diarrhea observed at week 0. Suspected enteropathogens were identified in 86% of these calves, most commonly cryptosporidia, coronavirus, and rotavirus. Identified potential zoonotic pathogens included Giardia and Salmonella spp and verotoxigenic Escherichia coli. Noncytopathic bovine viral diarrhea virus was isolated from 6 calves that had repeated bouts of illness. Only 22% of calves entering the veal facilities had adequate transfer of passive immunity. At week 0, serum IgG concentration in calves that subsequently died or had diarrhea was lower (P < 0.001) than that in healthy calves. All calves that died (n = 6) during the first 4 weeks of production had complete failure of transfer of passive immunity.",,"immunoglobulin G; analysis of variance; animal; animal food; article; blood; Bovine diarrhea virus; cattle; cattle disease; cell line; comparative study; Coronavirus; Cryptosporidium; Enterobacteriaceae; Escherichia coli; geography; Giardia; immunology; isolation and purification; kidney; meat; passive immunization; Rotavirus; Salmonella; standard; United States; Analysis of Variance; Animal Feed; Animals; Bovine Virus Diarrhea-Mucosal Disease; California; Cattle; Cell Line; Coronaviridae; Cryptosporidium; Diarrhea Viruses, Bovine Viral; Enterobacteriaceae; Escherichia coli; Geography; Giardia; Immunization, Passive; Immunoglobulin G; Kidney; Meat; Oregon; Rotavirus; Salmonella",,"McDonough, S.P.",,,00029645,,,"7879973","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028537680
"Atkins G.J., Balluz I.M., Glasgow G.M., Mabruk M.J.E., Natale V.A.I., Smyth J.M.B., Sheahan B.J.","7102660845;6505998861;7004413370;6701563578;7003390433;7201478123;7005814297;","Analysis of the molecular basis of neuropathogenesis of RNA viruses in experimental animals: Relevance for human disease?",1994,"Neuropathology and Applied Neurobiology","20","2",,"91","102",,20,"10.1111/j.1365-2990.1994.tb01167.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028323577&doi=10.1111%2fj.1365-2990.1994.tb01167.x&partnerID=40&md5=e8bf718eb322bb05342bb192c5d26177","Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland","Atkins, G.J., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Balluz, I.M., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Glasgow, G.M., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Mabruk, M.J.E., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Natale, V.A.I., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Smyth, J.M.B., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland; Sheahan, B.J., Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland","RNA viruses with segmented genomes were the first model used for molecular analysis of viral neuropathogenesis, since they could be analysed genetically by reassortment. Four viruses with non-segmented genomes have been used as models of neurovirulence and demyelinating disease: JHM coronavirus, Theiler's virus, Sindbis virus and Semliki Forest virus (SFV). Virus gene expression in the central nervous system of infected animals has been measured by in situ hybridization and immunocytochemistry. Cell tropism has been analysed by neural cell culture. Infectious clones have been constructed for Theiler's virus, Sindbis virus and SFV, and these allow analysis of the sequences involved in the determination of neuropathogenesis, through the construction of chimeric viruses and site-specific mutagenesis. Measles and rubella viruses have been studied in animal systems because of their importance for human disease. The importance of two recently discovered mechanisms of neuropathogenesis, antibody-induced modulation of virus multiplication, and persistence of virus in the absence of multiplication, remains to be assessed.","Encephalitis; Multiple sclerosis; Neuropathogenesis; RNA virus; Teratogenesis","chimera; clonogenesis; Coronavirus; demyelinating disease; disease model; experimental animal; gene expression; gene sequence; human; immunocytochemistry; in situ hybridization; Measles virus; molecular genetics; Murine encephalomyelitis virus; nerve cell culture; neuropathology; nonhuman; priority journal; review; RNA virus; Semliki Forest alphavirus; Sindbis virus; site directed mutagenesis; virogenesis; virus gene; virus genome",,"Atkins, G.J.; Department of Microbiology, Moyne Institute, Trinity College, Dublin 2, Ireland",,"Blackwell Publishing Ltd",03051846,,NANED,"8072672","English","NEUROPATHOL. APPL. NEUROBIOL.",Review,"Final",,Scopus,2-s2.0-0028323577
"Delmas B., Gelfi J., Kut E., Sjostrom H., Noren O., Laude H.","7003294168;8769591600;6603135299;7005649072;7006675786;7006652624;","Determinants essential for the transmissible gastroenteritis virus- receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site",1994,"Journal of Virology","68","8",,"5216","5224",,86,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028308336&partnerID=40&md5=d45a591bd1833ff90690a14ffcf0028f","Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France","Delmas, B., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France; Gelfi, J., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France; Kut, E., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France; Sjostrom, H., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France; Noren, O., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France; Laude, H., Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France","The swine-specific coronavirus transmissible gastroenteritis virus (TGEV) uses pig aminopeptidase-N (pAPN) as a cellular receptor. We showed that the human aminopeptidase-N (hAPN) cannot substitute for pAPN in this respect, although the two enzymes have 80% amino acid sequence identity. In order to map the TGEV binding site on pAPN, we constructed a series of APN cDNA chimeras between pAPN and hAPN and analyzed them for their capacity to confer infectivity. The region between residues 717 and 813 was found to be essential for infectivity. This region also contains the epitopes for three TGEV-blocking monoclonal antibodies directed against pAPN. These data support the view that the catalytic site and the TGEV receptor site are located in different domains. Moreover, APN inhibitors and mutations in the catalytic site had no obvious effect on permissiveness for virus, thus providing evidence that the APN enzymatic activity is not involved in the process of infection.",,"complementary dna; microsomal aminopeptidase; amino acid sequence; amino acid substitution; article; coronavirus; enzyme mechanism; enzyme specificity; human; nonhuman; priority journal; sequence homology; swine disease; virus infectivity; virus transmission; Amino Acid Sequence; Aminopeptidases; Animal; Antigens, CD13; Base Sequence; Binding Sites; Catalysis; Cloning, Molecular; DNA, Viral; Human; Molecular Sequence Data; Mutagenesis; Receptors, Virus; Species Specificity; Support, Non-U.S. Gov't; Swine; Transmissible gastroenteritis virus; Virus Replication",,"Laude, H.; Unite Virologie/Immunologie Molec., INRA, 78850 Jouy-en-Josas, France",,,0022538X,,JOVIA,"7913510","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028308336
"Meulenberg J.J., Hulst M.M., de Meijer E.J., Moonen P.L., den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.","7003598565;6603742346;57088574400;7004669246;7801315180;6602784924;7004683225;7006536560;","Lelystad virus belongs to a new virus family, comprising lactate dehydrogenase-elevating virus, equine arteritis virus, and simian hemorrhagic fever virus.",1994,"Archives of virology. Supplementum","9",,,"441","448",,55,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028253254&partnerID=40&md5=5d7574b8740edb1452536692df54e6eb","Central Veterinary Institute, Department of Virology, Lelystad, Netherlands","Meulenberg, J.J., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; Hulst, M.M., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; de Meijer, E.J., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; Moonen, P.L., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; den Besten, A., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; de Kluyver, E.P., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; Wensvoort, G., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands; Moormann, R.J., Central Veterinary Institute, Department of Virology, Lelystad, Netherlands","Lelystad virus (LV) is an enveloped positive-stranded RNA virus, which causes abortions and respiratory disease in pigs. The complete nucleotide sequence of the genome of LV has been determined. This sequence is 15.1 kb in length and contains a poly(A) tail at the 3' end. Open reading frames that might encode the viral replicases (ORFs 1a and 1b), membrane-associated proteins (ORFs 2 to 6) and the nucleocapsid protein (ORF7) have been identified. Sequence comparisons have indicated that LV is distantly related to the coronaviruses and toroviruses and closely related to lactate dehydrogenase-elevating virus (LDV) and equine arteritis virus (EAV). A 3' nested set of six subgenomic RNAs is produced in LV-infected alveolar lung macrophages. These subgenomic RNAs contain a leader sequence, which is derived from the 5' end of the viral genome. Altogether, these data show that LV is closely related evolutionarily to LDV and EAV, both members of a recently proposed family of positive-stranded RNA viruses, the Arteriviridae.",,"virus protein; virus RNA; animal; Arterivirus; article; classification; comparative study; Equine viral arteritis virus; gene expression; genetics; growth, development and aging; Lactic dehydrogenase togavirus; microbiology; RNA virus; sequence homology; swine; swine disease; virus genome; virus replication; Animals; Arteritis Virus, Equine; Arterivirus; Gene Expression; Genome, Viral; Lactate dehydrogenase-elevating virus; RNA Viruses; RNA, Viral; Sequence Homology, Amino Acid; Swine; Swine Diseases; Viral Proteins; Virus Replication",,"Meulenberg, J.J.",,,09391983,,,"8032274","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028253254
"Yokomori K., Lai M.M.","57206215028;7401808497;","Mouse hepatitis virus receptors: more than a single carcinoembryonic antigen.",1994,"Archives of virology. Supplementum","9",,,"461","471",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028187751&partnerID=40&md5=69add97374514afea0f99651cce5453f","Howard Hughes Medical Institute, University of Southern California School of Medicine, Los Angeles, United States","Yokomori, K., Howard Hughes Medical Institute, University of Southern California School of Medicine, Los Angeles, United States; Lai, M.M., Howard Hughes Medical Institute, University of Southern California School of Medicine, Los Angeles, United States","Mouse hepatitis virus (MHV), a murine coronavirus, has been shown to utilize carcinoembryonic antigen (CEA) as the receptor. We have demonstrated that MHV can utilize a different isoform of CEA, which is an alternatively spliced gene product that is expressed in different tissues, as a receptor. Furthermore, the CEA molecules from a resistant mouse strain (SJL) have different sequences and yet serve as functional viral receptors. Thus, MHV can use more than a single type of CEA molecule as the receptor. We have also shown that some mouse cell lines express functional CEA molecules and yet are resistant to infections by certain MHV strains. Biochemical studies of the infected cells indicate that MHV infections in these cell lines are blocked at the steps of virus entry. We conclude that MHV entry requires additional cellular factors other than CEA, the viral receptor. The significance of viral receptors and the additional cellular factors in regulating viral tropism is discussed.",,"carcinoembryonic antigen; coronavirus receptor; membrane protein; spike glycoprotein, coronavirus; virus envelope protein; virus receptor; animal; article; cell line; comparative study; growth, development and aging; innate immunity; metabolism; mouse; mouse strain; Murine hepatitis coronavirus; protein binding; species difference; tissue distribution; virus replication; Animals; Carcinoembryonic Antigen; Cell Line; Immunity, Natural; Membrane Glycoproteins; Mice; Mice, Inbred Strains; Murine hepatitis virus; Protein Binding; Receptors, Virus; Species Specificity; Tissue Distribution; Viral Envelope Proteins; Virus Replication",,"Yokomori, K.",,,09391983,,,"8032276","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028187751
"Hornberger F.R.","6508000786;","Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus",1994,"Virus Research","31","1",,"49","56",,17,"10.1016/0168-1702(94)90070-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028153860&doi=10.1016%2f0168-1702%2894%2990070-1&partnerID=40&md5=44af6b636b6dec50b6759d65cb0b63aa","Institute of Laboratory Animal Science, University of Zurich-Irchel, Winterthurerstrasse 190, 8057 Zurich, Switzerland","Hornberger, F.R., Institute of Laboratory Animal Science, University of Zurich-Irchel, Winterthurerstrasse 190, 8057 Zurich, Switzerland","The nucleotide sequences of the membrane (M) protein genes and their deduced amino acid sequences of three enterotropic strains of the coronavirus mouse hepatitis virus (MHV) -Y, -RI and -DVIM were determined and compared with the previously reported sequences of two respiratory MHV strains -A59 and -JHM. The five MHV strains shared extensive nucleotide (95.2-99.0%) as well as amino acid homology (95.6-98.7%). A variable region, including a 15 nucleotide deletion unique to MHV-RI, could be identified at the 5'-terminus of the gene. This region of the M protein may be immunogenic and may contribute to the antigenic diversity of the MHV strains. Sequence relationships between the strains showed no correspondence with the primary cell tropism. This may suggest that evolution of enterotropism was not a single occurrence among different MHV strains. No sequence unique to either tropism group could be identified, indicating that the M protein of MHV probably has no part in the determination of MHV tissue tropism. © 1994.","(Mouse); Coronavirus; Enterotropic; Membrane protein; MHV; Nucleotide sequence","membrane protein; article; controlled study; murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; virus strain; Amino Acid Sequence; Animal; Base Sequence; Coronavirus Infections; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Viral; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Support, Non-U.S. Gov't; Variation (Genetics); Viral Matrix Proteins; Coronavirus; Murinae; Murine hepatitis virus","Armstrong, Niemann, Smeekens, Rottier, Warren, Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Barthold, Mouse hepatitis virus: Biology and epidemiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents. Effect on Biomedical Research, pp. 571-601. , P.N. Bhatt, R.O. Jacoby, H.C. Morse III, A.E. New, Academic Press, Orlando, FL; Barthold, Smith, Lord, Jacoby, Main, Epizootic coronaviral typhlocolitis in suckling mice (1982) Lab. Anim. Sci., 32, pp. 376-383; Barthold, Smith, Povar, Enterotropic mouse hepatitis virus infection in nude mice (1985) Lab. Anim. Sci., 35, pp. 613-618; Budzilowicz, Wilczynski, Weiss, Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3' end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Cavanagh, Davis, Evolution of Avian Coronavirus IBV: Sequence of the Matrix Glycoprotein Gene and Intergenic Region of Several Serotypes (1988) Journal of General Virology, 69, pp. 621-629; Cheever, Daniels, Pappenheimer, Bailey, A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin. I. Isolation and biological properties of the virus (1949) J. Exp. Med., 90, pp. 181-194; Compton, Barthold, Smith, The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Fleming, Stohlman, Harmon, Lai, Frelinger, Weiner, Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Homberger, Smith, Barthold, Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Lai, Coronavirus: organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, Fleming, Stohlman, Fujiwara, Genetic heterogeneity of murine coronaviruses (1983) Arch. Virol., 78, pp. 167-175; Laude, Gelfi, Lavenant, Charley, Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by coronavirus transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 743-749; Pfleiderer, Skinner, Siddell, Coronavirus MHV-JHM: nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res., 14, p. 6338; Sambrook, Fritsch, Maniatis, (1989) Molecular Cloning: A Laboratory Manual, , 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY","Hornberger, F.R.; Institute of Laboratory Animal Science, University of Zurich-Irchel, Winterthurerstrasse 190, 8057 Zurich, Switzerland",,,01681702,,VIRED,"8165869","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0028153860
"Šplíchal I., Bonnneau M., Charley B.","6701407816;16165240100;55246691600;","Ontogeny of interferon alpha secreting cells in the porcine fetal hematopoietic organs",1994,"Immunology Letters","43","3",,"203","208",,19,"10.1016/0165-2478(94)90224-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028575668&doi=10.1016%2f0165-2478%2894%2990224-0&partnerID=40&md5=eac1fa7ff7c5eacadbd9ea83234950b9","Laboratoire de Virologie et d'Immunologie Moléculaires, INRA, 78350 Jouy-en-Josas, France; Centre de Recherche en Imagerie Interventionnelle, INRA, 78350 Jouy-en-Josas, France; Institute of Microbiology, Department of Immunology and Gnotobiology, 54922 Nový Hrádek, Czech Republic","Šplíchal, I., Institute of Microbiology, Department of Immunology and Gnotobiology, 54922 Nový Hrádek, Czech Republic; Bonnneau, M., Centre de Recherche en Imagerie Interventionnelle, INRA, 78350 Jouy-en-Josas, France, Institute of Microbiology, Department of Immunology and Gnotobiology, 54922 Nový Hrádek, Czech Republic; Charley, B., Laboratoire de Virologie et d'Immunologie Moléculaires, INRA, 78350 Jouy-en-Josas, France, Institute of Microbiology, Department of Immunology and Gnotobiology, 54922 Nový Hrádek, Czech Republic","We examined the ontogeny of IFN-α Secreting Cells (IFN-α SC) in different hematopoietic organs and blood of porcine fetuses at different stages of gestation. Cells were induced to produce IFN-α by incubation with the coronavirus TGEV and IFN-α SC were detected by ELISPOT. A striking finding was that IFN-α SC could be detected in the fetal liver as early as at 26 days of gestation, i.e., during the first quarter of gestation, a period at which T-cell markers could not be detected by flow cytometry. In addition, IFN-α SC could be detected in the cord blood, the spleen and the bone marrow of fetuses at later stages of gestation. These data indicate that IFN-α SC appear very early during the ontogeny of the immune system, long before the development of the specific immune system, and may therefore represent an early antiviral defence mechanism. IFN-α SC were found to be associated with hematopoietic organs, which argues for their hematopoietic lineage. © 1994.","Coronavirus; ELISPOT; Interferon; Leukocytes; Ontogeny; Porcine","alpha interferon; animal cell; article; coronavirus; enzyme immunoassay; fetus; flow cytometry; host resistance; nonhuman; ontogeny; priority journal; swine; Animal; Bone Marrow; Embryo and Fetal Development; Enzyme-Linked Immunosorbent Assay; Female; Fetal Blood; Flow Cytometry; Gestational Age; Hematopoietic Stem Cells; Interferon-alpha; Liver; Pregnancy; Spleen; Swine; Transmissible gastroenteritis virus","Joklik, (1990) Virology, pp. 383-410. , B.N. Fields, D.M. Knipe, Raven Press, New York; Sandberg, Matsson, Alm, (1990) J. Immunol., 145, p. 1015; Lebon, Commoy-Chevalier, Robert-Galliot, Chany, (1982) Virology, 119, p. 504; Capobianchi, Facchini, Di Marco, Antonelli, Dianzani, (1985) Proc. Soc. Exp. Biol. Med., 178, p. 551; Charley, Laude, (1992) Ann. Rech. Vet., 23, p. 318; Fitzgerald-Bocarsly, (1993) Pharmac. Ther., 60, p. 39; Lebon, (1985) J. Gen. Virol., 66, p. 2781; Capobianchi, Ankel, Ameglio, Paganelli, Pizzoli, Dianzani, (1992) AIDS Res. Retroviruses, 8, p. 575; Charley, Laude, (1988) J. Virol., 62, p. 8; Laude, Gelfi, Lavenant, Charley, (1992) J. Virol., 66, p. 743; Šterzl, Silverstein, (1967) Adv. Immunol., 6, p. 337; Kovářů, (1987) Thesis, , Inst. Microbiol, Prag; Nowacki, Charley, (1993) Res. Immunol., 144, p. 111; Lefèvre, L'Haridon, Borras-Cuesta, La Bonnardière, (1990) J. Gen. Virol., 71, p. 1057; De Arce, Artursson, L'Haridon, Perers, La Bonnardière, Alm, (1992) Vet. Immunol. Immunopathol., 30, p. 319; Lunney, (1993) Immunol. Today, 14, p. 147; Banatvala, Potter, Best, (1971) J. Gen. Virol., 13, p. 193; Cederblad, Riesenfeld, Alm, (1990) Pediatric Research, 27, p. 7; Trebichavský, Patriková, Mandel, Kovářů, Zahradníčková, (1988) Folia Microbiologica, 33, p. 329; Sandberg, Eloranta, Johanisson, Alm, (1991) Scand. J. Immunol., 34, p. 565; McCauley, Hartmann, (1984) Res. Vet. Sci., 37, p. 234; Nowacki, Cederblad, Renard, La Bonnardière, Charley, (1993) Vet. Immunol. Immunopathol., 37, p. 113; Šinkora, J., Řeháková, Z., Šinkora, M. and Trebichavský, I. (in press); Trebichavský, Reháková, Mandel, Němec, Zahradníčková, (1990) Folia Biologica, 36, p. 102; Janossy, Bofill, Poulter, Rawlings, Burford, Navarette, Ziegler, Kelemen, (1986) J. Immunol., 136, p. 4354","Charley, B.; Laboratoire de Virologie et d'Immunologie Moléculaires, INRA, 78350 Jouy-en-Josas, France",,,01652478,,IMLED,"7721334","English","Immunol. Lett.",Article,"Final",,Scopus,2-s2.0-0028575668
"Chinsangaram J., Akita G.Y., Osburn B.I.","6602148619;6602128491;7005048548;","Detection of bovine group B rotaviruses in feces by polymerase chain reaction",1994,"Journal of Veterinary Diagnostic Investigation","6","3",,"302","307",,14,"10.1177/104063879400600304","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028469297&doi=10.1177%2f104063879400600304&partnerID=40&md5=3da3c955cea21696b9d77c8247793481","Department of Veterinary Pathology, Microbiology and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Chinsangaram, J., Department of Veterinary Pathology, Microbiology and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Akita, G.Y., Department of Veterinary Pathology, Microbiology and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Osburn, B.I., Department of Veterinary Pathology, Microbiology and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","A pair of primers designed from the sequence of genome segment 9 of group B rat rotavirus (IDIR) were employed to amplify genome segment 9 of a group B bovine rotavirus in a polymerase chain reaction (PCR) and to sequence the derived PCR products. A new pair of primers were synthesized from the obtained sequence data and used in a PCR detection assay for group B bovine rotavirus in fecal samples. In addition, another pair of primers were designed to produce a PCR-derived internal probe. This probe was used in a chemiluminescent hybridization to confirm the specificity and to increase the sensitivity of the assay. This assay could detect 0.1 fg of target double-stranded RNA. It was specific to group B bovine rotavirus and did not detect group B rat (IDIR) and porcine rotaviruses, group A bovine (NCDV), simian (SA-11), equine (H-2), porcine (OSU), human (DS-1), deer, and avian rotaviruses, coronavirus, or other enteric organisms tested in this study. © 1994, American Association of Veterinary Laboratory Diagnosticians. All rights reserved.",,"primer DNA; animal; animal disease; article; cattle; cattle disease; feces; isolation and purification; methodology; microbiology; molecular genetics; nucleotide sequence; polymerase chain reaction; rat; Rotavirus; sensitivity and specificity; virology; virus infection; Animal; Base Sequence; Cattle; Cattle Diseases; DNA Primers; Feces; Molecular Sequence Data; Polymerase Chain Reaction; Rats; Rotavirus; Rotavirus Infections; Sensitivity and Specificity; Support, Non-U.S. Gov't","Bridger, J.C., Bock, G., Whelan, J., Novel rotaviruses in animals and man. In (1987) Novel diarrhoea viruses, ed., pp. 5-24. , John Wilev & Sons Chichester, UK; Chasey, D., Davies, P., Atypical rotaviruses in pigs and cattle (1984) Vet Rec, 114, pp. 16-17; Chen, G.M., Werner-Eckert, R., Tao, H., Mackow, E.R., Expression of the major inner capsid protein of the group B rotavirus ADRV: primary characterization of genome segment 5 (1991) Virology, 182, pp. 820-829; Chinsangaram, J., Akita, G.Y., Osburn, B.I., Castro, A.E., PCR detection of group A bovine rotaviruses in feces (1993) J Vet Diagn Invest, 5, pp. 516-521; Chinsangaram, J., Hammami, S., Osburn, B.I., Detection of bluetongue virus using a cDNA probe derived from genome segment 4 of bluetongue virus serotype 2 (1992) J Vet Diagn Invest, 4, pp. 8-12; Eiden, J.J., Allen, J.R., Identification of cognate genes among heterologous strains of group B rotavirus (1992) J Virol, 66, pp. 1232-1235; Eiden, J.J., Firoozmand, F., Sato, S., Detection of group B rotavirus in fecal specimens by dot hybridization with a cloned cDNA probe (1989) J Clin Microbiol, 27, pp. 422-426; Eiden, J.J., Nataro, J., Vonderfecht, S.L., Petric, M., Molecular cloning, sequence analysis, in vitro expression, and immunoprecipitation of the major inner capsid protein of the IDIR strain of group B rotavirus (GBR) (1992) Virology, 188, pp. 580-589; Eiden, J.J., Wilde, J., Firoozmand, F., Yolken, R.H., Detection of animal and human group B rotaviruses in fecal specimens by polymerase chain reaction (1991) J Clin Microbiol, 29, pp. 539-543; Fluett, T.H., Woode, G.N., The rotaviruses (1978) Arch Virol, 57, pp. 1-23; Gouvea, V., Allen, J.R., Glass, R.I., Detection of group B and C rotaviruses by polymerase chain reaction (1991) J Clin Microbiol, 29, pp. 519-523; Holland, R.E., Some infectious causes of diarrhea in young farm animals (1990) Clin Microbiol Rev, 3, pp. 345-375; McNulty, M.S., Rotaviruses (1978) J Gen Virol, 40, pp. 1-18; McNulty, M.S., Morphology and chemical composition of rotaviruses (1979) Colloq Inst Natl Sante Rech Med, 90, pp. 111-140; Mebus, C.A., Rhodes, M.B., Underdahl, N.R., Neonatal calf diarrhea caused by a virus that induced villous epithelial cell syncytia (1978) Am J Vet Res, 39, pp. 1223-1228; Petric, M., Mayur, K., Vonderfecht, S.L., Eiden, J.J., Comparison of group B rotavirus genes 9 and 11 (1991) J Gen Virol, 72, pp. 2801-2804; Saif, L.J., Saif, L.J., Theil, K.W., Nongroup A rotaviruses. In (1990) Viral diarrheas of man and animals, ed., pp. 73-95. , CRC Press Boca Raton, FL; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Squire, K.R.E., Chuang, R.Y., Osburn, B.I., Rapid methods for comparing the double-stranded RNA genome profiles of bluetongue virus (1983) Vet Microbiol, 8, pp. 543-553; Tsunemitsu, H., Saif, L.J., Jiang, B.M., Isolation, characterization, and serial propagation of a bovine group C rotavirus in a monkey kidney cell line (MA104) (1991) J Clin Microbiol, 29, pp. 2609-2613; Vonderfecht, S.L., Eiden, J.J., Torres, A., Identification of a bovine enteric syncytial virus as a nongroup A rotavirus (1986) Am J Vet Res, 47, pp. 1913-1918",,,,10406387,,,"7948199","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0028469297
"Paul-Murphy J., Work T., Hunter D., McFie E., Fjelline D.","7004153937;7004499516;36196628600;6504006936;6504471650;","Serologic survey and serum biochemical reference ranges of the free-ranging mountain lion (Felis concolor) in California.",1994,"Journal of wildlife diseases","30","2",,"205","215",,70,"10.7589/0090-3558-30.2.205","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028412037&doi=10.7589%2f0090-3558-30.2.205&partnerID=40&md5=1a5ede40653cf2a7e6470637fe0f509c","University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States","Paul-Murphy, J., University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States; Work, T., University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States; Hunter, D., University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States; McFie, E., University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States; Fjelline, D., University of Wisconsin-Madison, School of Veterinary Medicine 53706., United States","Serum samples from 58 mountain lions (Felis concolor) in California (USA) were collected between April 1987 and February 1990. Nineteen serum samples were used for serum biochemistry determinations; the ranges were similar to reference values in domestic cats, captive exotic felidae and free-ranging mountain lions. A serological survey was conducted to determine whether antibodies were present against selected infectious agents. Fifty-four (93%) of 58 sera had antibodies against feline panleukopenia virus. Fifteen (68%) of 22, 16 (28%) of 58, 11 (19%) of 58, and 10 (17%) of 58 had serum antibodies against feline reovirus, feline coronavirus, feline herpes virus, and feline calicivirus, respectively. Twenty-three (40%) of 58 and 21 (58%) of 36 had serum antibodies against Yersinia pestis and Toxoplasma gondii, respectively. Only one of 22 sera had antibodies against the somatic antigen of Dirofilaria immitis. Feline leukemia virus and feline immunodeficiency virus antigens were not detected in any mountain lion's sera. All 58 sera samples were negative for antibodies to feline immunodeficiency virus and Chlamydia psittaci.",,"antibody; bacterium antibody; helminth antibody; protozoon antibody; virus antibody; animal; animal disease; article; blood; blood analysis; Carnivora; communicable disease; female; male; prevalence; reference value; United States; Animals; Antibodies; Antibodies, Bacterial; Antibodies, Helminth; Antibodies, Protozoan; Antibodies, Viral; Blood Chemical Analysis; California; Carnivora; Communicable Diseases; Female; Male; Prevalence; Reference Values",,"Paul-Murphy, J.",,,00903558,,,"8028105","English","J. Wildl. Dis.",Article,"Final",,Scopus,2-s2.0-0028412037
"Mochizuki M., Nakatani H., Yoshida M.","7403050664;7102614005;57199290009;","Inhibitory effects of recombinant feline interferon on the replication of feline enteropathogenic viruses in vitro",1994,"Veterinary Microbiology","39","1-2",,"145","152",,44,"10.1016/0378-1135(94)90095-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028294515&doi=10.1016%2f0378-1135%2894%2990095-7&partnerID=40&md5=d636ce64698c99566d6e96f00883aa06","Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Korimoto 1-21-24, Kagoshima, 890, Japan","Mochizuki, M., Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Korimoto 1-21-24, Kagoshima, 890, Japan; Nakatani, H., Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Korimoto 1-21-24, Kagoshima, 890, Japan; Yoshida, M., Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Korimoto 1-21-24, Kagoshima, 890, Japan","Antiviral activities of a recombinant feline interferon (rFeIFN) KT-80 were evaluated against feline enteropathogenic viruses in feline and canine cell lines. Sensitivity to antiviral activities of the rFeIFN varied with cell types; Felis catus whole fetus (fcwf-4) cells were more sensitive than Crandell feline kidney cells, but no sensitivity was found for Madin-Darby canine kidney cells when vesicular stomatitis virus was used as a challenge virus. Reductions were generally IFN dose-dependent and were more consistent when the cells were continuously treated with the rFeIFN than when they were pretreated only before viral challenge. Compared with each virus control culture of fcwf-4 cells, yields of rotavirus, feline panleukopenia virus (FPLV), feline calicivirus and feline infectious peritonitis coronavirus were reduced by ranges of 1.3 to ≤3.1 log10, 0.6 log2, 0.8 to 3.7 log10 and 0.5 to 0.6 log10, respectively, in the cultures continuously treated with 10 to 10000 U of the rFeIFN. The yield reduction of FPLV was considered to be in part attributable to inhibition of cell growth by the rFeIFN supplemented in the medium. © 1994.",,"recombinant interferon; animal cell; antiviral activity; article; cat; enteric virus; in vitro study; nonhuman; virus infection; virus replication; Animal; Calicivirus, Feline; Cats; Cell Division; Cell Line; Coronavirus, Feline; Dogs; Dose-Response Relationship, Immunologic; Herpesviridae; Interferons; Parvovirus, Feline; Recombinant Proteins; Rotavirus; Vesicular stomatitis-Indiana virus; Virus Replication; Animalia; Caliciviridae; Catus; Coronavirus; Felidae; Feline calicivirus; feline infectious peritonitis coronavirus; Feline panleukopenia virus; Felis catus; Rotavirus; Vesicular stomatitis virus","Cocker, Howard, Harbour, Effect of human α-hybrid interferon on the course of feline viral rhinotracheitis (1987) Vet. Rec., 120, pp. 391-393; Cummins, Tompkins, Olsen, Tompkins, Lewis, Oral use of human alpha interferon in cats (1988) J. Biol. Response Modif., 7, pp. 513-523; Engelman, Fulton, Good, Day, Suppression of gamma interferon production by inactivated feline leukemia virus (1985) Science, 227, pp. 1368-1370; Fulton, Burge, Susceptibility of feline herpesvirus 1 and a feline calicivirus to feline interferon and recombinant human leukocyte interferons (1985) Antimicrob. Agents Chemother., 28, pp. 698-699; Horzinek, Lutz, Pedersen, Antigenic relationships among homologous structural polypeptides of porcine, feline and canine coronaviruses (1982) Infect. Immun., 37, pp. 1148-1155; Jamesen, Essex, Inhibition of feline leukemia virus replication by human leukocyte interferon (1983) Antiviral Res., 3, pp. 115-120; Mochizuki, Different stabilities to bile among feline calicivirus strains of respiratory and enteric origin (1992) Vet. Microbiol., 31, pp. 297-302; Mochizuki, Hashimoto, Growth of feline panleukopenia virus and canine parvovirus in vitro (1986) Jpn. J. Vet. Sci., 48, pp. 841-844; Mochizuki, Konishi, Ajiki, Akaboshi, Comparison of feline parvovirus subspecific strains using monoclonal antibodies against a feline panleukopenia virus (1989) Jpn. J. Vet. Sci., 51, pp. 264-272; Mochizuki, Konishi, Ogata, Studies on cytopathogenic viruses from cats with respiratory infections III. Isolation and certain properties of feline herpesviruses (1977) Jpn. J. Vet. Sci., 39, pp. 27-37; Mochizuki, Nakagomi, Shibata, Hemagglutinin activity of two distinct genogroups of feline and canine rotavirus strains (1992) Arch. Virol., 122, pp. 373-381; Mochizuki, Sameshima, Ata, Minami, Okabayashi, Harasawa, Characterization of canine rotavirus RS15 strain and comparison with other rotaviruses (1985) Jpn. J. Vet. Sci., 47, pp. 531-538; Mochizuki, Sugiura, Akuzawa, Micro-neutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Nakamura, Sudo, Matsuda, Yanai, Molecular cloning of feline interferon cDNA by direct expression (1992) Biosci. Biotech. Biochem., 56, pp. 211-214; Pedersen, Black, Boyle, Evermann, McKeirnan, Ott, Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Rodgers, Merigan, Hardy, Jr., Old, Kassel, Cat Interferon inhibits Feline Leukaemia Virus Infection in Cell Culture (1972) Nature New Biology, 237, pp. 270-271; Rollinson, Prospects for antiviral chemotherapy in veterinary medicine: 1. Feline virus diseases (1992) Antiviral Chem. Chemother., 3, pp. 249-262; Sen, Herz, Davatelis, Pestka, Antiviral and protein-inducing activities of recombinant human leukocyte interferons and their hybrids (1984) J. Virol., 50, pp. 445-450; Weiss, Synergistic antiviral activities of acyclovir and recombinant human leukocyte (alpha) interferon on feline herpesvirus replication (1989) Am. J. Vet. Res., 50, pp. 1672-1677; Weiss, Cox, Oostrom-Ram, Effect of interferon or Propionibacterium acnes on the course of experimentally induced feline infectious peritonitis in specific-pathogen-free and random-source cats (1990) Am. J. Vet. Res., 51, pp. 726-733; Weiss, Oostrom-Ram, Inhibitory effects of Ribavirin alone or combined with human alpha interferon on feline infectious peritonitis virus replication in vitro (1989) Vet. Microbiol., 20, pp. 255-265; Weiss, Toivio-Kinnucan, Inhibition of feline infectious peritonitis virus replication by recombinant human leukocyte (α) interferon and feline fibroblastic (β) interferon (1988) Am. J. Vet. Res., 49, pp. 1329-1335; Wiedbrauk, Bloom, Lodmell, Mink parvoviruses and interferons: in vitro studies (1986) J. Virol., 60, pp. 1179-1182; Yamamoto, Ho, Pedersen, A feline retrovirus induced T-lymphoblastoid cell-line that produces an atypical alpha type of interferon (1986) Vet. Immunol. Immunopathol., 11, pp. 1-19; Yanai, Nakamura, Matsuda, (1989) Synthetic plasmid, transformant, feline interferon gene and method for producing feline interferon, , European Patent Application., Publication number 322870; Yanai, Ueda, Sakurai, Satoh, (1991) Feline interferon and process for production thereof by a silkworm virus vector, , European Patent Application. Publication number 0 414 355 A1; Zeidner, Myles, Mathiason-DuBard, Dreitz, Mullins, Hoover, Alpha interferon (2b) in combination with Zidovudine for the treatment of presymptomatic feline leukemia virus-induced immunodeficiency syndrom (1990) Antimicrob. Agents Chemother., 34, pp. 1749-1756","Mochizuki, M.; Laboratory of Veterinary Microbiology, Department of Veterinary Medicine, Faculty of Agriculture, Korimoto 1-21-24, Kagoshima, 890, Japan",,,03781135,,VMICD,"7515537","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0028294515
"Le S.-Y., Sonenberg N., Maizel J.V., Jr.","7006184376;35370559100;35821615700;","Distinct structural elements and internal entry of ribosomes in mRNA3 encoded by infectious bronchitis virus",1994,"Virology","198","1", 71051,"405","411",,18,"10.1006/viro.1994.1051","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028341510&doi=10.1006%2fviro.1994.1051&partnerID=40&md5=d3eb2af5b63efcbcc1a3b5b01b0abf13","Laboratory of Mathematical Biology, Division of Cancer Biology, Diagnosis and Centers, National Cancer Institute, NIH, Building 469, Room 151, Frederick, MD 21702, United States; Department of Biochemistry and McGiil Cancer Center, McGill University, Montreal, QC, H3G 1Y6, Canada","Le, S.-Y., Laboratory of Mathematical Biology, Division of Cancer Biology, Diagnosis and Centers, National Cancer Institute, NIH, Building 469, Room 151, Frederick, MD 21702, United States; Sonenberg, N., Department of Biochemistry and McGiil Cancer Center, McGill University, Montreal, QC, H3G 1Y6, Canada; Maizel, J.V., Jr., Laboratory of Mathematical Biology, Division of Cancer Biology, Diagnosis and Centers, National Cancer Institute, NIH, Building 469, Room 151, Frederick, MD 21702, United States","Infectious bronchitis virus (IBV) mRNA3 encodes three small proteins, 3a, 3b, and 3c, at its 5' end. Recently, it was demonstrated that initiation of protein 3c is dependent on the upstream sequence. Monte Carlo simulations of RNA folding in this tricistronic mRNA3 indicate that a highly significant folding region occurs prior to the initiator AUG of 3c. The unusual folding region (UFR) of 265 nucleotides (nt) contains the coding sequences of proteins 3a and 3b. Details of the structural analyses show that five highly significant RNA stem-loops in the UFR can be modeled into a compact superstructure by the interaction of two predicted pseudoknot structures. The folded superstructure comprising nt 44 to 330, with additional 22 nt downstream from this UFR, is suggested to serve as a ribosome landing pad (or an internal ribosomal entry site) in the cap-independent translation of the 3c of IBV. Intriguingly, the proposed structural motif of this coronavirus shares structural features similar to those proposed in a number of picornavirus mRNAs. Based on the common structural features, a plausible base pairing model between mRNA3 and 18 S rRNA is suggested, which is consistent with a general mechanism for regulation of internal initiation described in many picornaviruses. © 1994 Academic Press, Inc.",,,"Liu, D.X., Cavanagh, D., Green, I.J., Inglis, S.C., (1991) Virology, 184, pp. 531-544; Liu, D.X., Inglis, S.C., (1992) J. Virol, 66, pp. 6143-6154; Kozak, M.J., (1989) Ceil Biol, 108, pp. 229-241; Kozak, M.J., (1991) Cell Biol, 115, pp. 887-903; Le, S.Y., Chen, J.-H., Sonenberg, N., Maizel, J.V., Jr., (1992) Virology W, pp. 858-866; Le, S.-Y., Chen, J.-H., Sonenberg, N., Maizel, J.V., Jr., (1993) Nucleic Acids Res, 21, pp. 2445-2451; Le, S.-Y., Chen, J.-H., Braun, M.J., Gonda, M.A., Maizel, J.V., Jr., (1988) Nucleic Acids Res, 16, pp. 5153-5268; Le, S.-Y., Chen, J.-H., Maizel, J.V., Jr., (1990) Structure & Methods: Human Genome Initiative and DNA Recombina-Tion, 1, pp. 127-136. , R. H. Sarma and M. H. Sarma, Eds, Adenine Press, Albany, NY; Le, S.-Y., Malim, M.H., Cullen, B.R., Maizel, J.V.J., (1990) Nucleic Acids Res, 18, pp. 1613-1623; Malim, M., Hauber, J., Le, S.-Y., Maizel, J.V., Jr., Cullen, B.R., (1989) Nature, 338, pp. 254-257; Fenrick, R., Malim, M., Hauber, J., Le, S.-Y., Maizel, J.V., Jr., Cullen, B.R., (1989) J. Virol, 63, pp. 5006-5012; Tiley, L.S., Brown, P.H., Le, S.-Y., Maizel, J.V., Jr., Clements, J.E., Cullen, B.R., (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 7497-7501; Freier, S.M., Kierzek, R., Jaeger, J.A., Sugimoto, N., Caruthers, M.H., Neilson, T., Turner, D.H., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 9373-9377; Jaeger, J.A., Turner, D.H., Zuker, M., (1990) Proc. Natl. Sci. USA, 86, pp. 7706-7710; Salser, W., (1977) Cold Spring Harbor Symp. Quant. Biol, 42, pp. 985-1002; Cech, T.R., Tanner, N.K., Tinoco, I., Jr., Weir, B.R., Zuker, M., Perlman, P.S., (1983) Proc. Natl. Acad. Sci. USA, 80, pp. 3903-3907; Le, S.-Y., Chen, J.-H., Maizel, J.V., Jr., (1993) Nucleic Acids Res, 21, pp. 2173-2178; Williams, A.L., Tinoco, I., Jr., (1993) Nucleic Acids Res, 14, pp. 299-315; Chen, J.-H., Le, S.-Y., Maizel, J.V., Jr., (1992) Comp. Appl. Biosci, 8, pp. 243-248; Le, S.-Y., Maizel, J.V., Jr., (1989) J. Theor. Biol, 138, pp. 495-510; Huysmans, E., Wachter, R., (1986) Nucleic Acids Res, 14, pp. 73-118; Rairkar, A., Rubino, H.M., Lockard, R.E., (1988) Biochemistry, 27, pp. 582-592; Shine, J., Dalgarno, L., (1974) Proc. Natl. Acad. Sci. USA, 71, pp. 1342-1346; Trono, D., Ino, R., Baltimore, D., (1988) J. Virol, 62, pp. 2291-2299; Pelletier, J., Sonenberg, N., (1988) Nature, 334, pp. 320-325; Bienkowska-Szewczyk, K.T., Ehrenfeld, E.J., (1988) Virol, 62, pp. 3068-3072; Brown, E.A., Day, S.P., Jansen, R.W., Lemon, S.M., (1991) J. Virol, 65, pp. 5828-5838; Duke, G.M., Hoffman, M.A., Palmenberg, A.C., (1992) J. Virol, 66, pp. 1602-1609; Borman, A., Jackson, R.J., (1992) Virology, 188, pp. 685-696; Kuhn, R., Luz, N., Beck, E., (1990) J. Virol, 64, pp. 4625-4631; Jang, S.K., Davies, M.V., Kaufman, R.J., Wimmer, E., (1989) J. Virol, 63, pp. 1651-1660; Pilipenko, E.V., Gmyl, A.P., Maslova, S.V., Svitkin, Y.V., Sinyakov, A.N., Agol, V.I., (1992) Cell, 68, pp. 119-131; Randyopadhyay, P.K., Wang, C.T., Lipton, H.L., (1992) J. Virol, 66, pp. 6249-6256; Nicholson, R., Pelletier, J., Le, S.-Y., Sonenberg, N., (1991) J. Virol, 65, pp. 5886-5894; Pestova, T.V., Hellen, C.U.T., Wimmer, E., (1991) J. Virol, 65, pp. 6194-6204; Brierley, I., Digard, P., Inglis, S.C., (1989) Cell, 57, pp. 537-547; Brierley, I., Rolley, N.J., Jenner, A.J., Inglis, S.C., (1991) J. Mol. Biol, 220, pp. 889-902; Tang, C.K., Draper, D.E., (1989) Ceil, 57, pp. 531-536; McPheeters, D.S., Stormo, G.D., Gold, L., (1988) J. Mol. Biol, 201, pp. 517-535; Meerovitch, K., Svitkin, Y.V., Lee, H.S., Lejbkowicz, F., Kenan, D.J., Chan, E.K.L., Agol, V.I., Sonenberg, N., (1993) J. Virol, 67, pp. 3798-3807; Scheper, G.C., Thomas, A., Voorma, H.O., (1991) Biochim. Biophys. Acta, 1089, pp. 220-226; Le, S.-Y., Zuker, M.J., (1990) Mol. Biol, 216, pp. 729-741; Feng, S., Holland, E.C., (1988) Nature, 334, pp. 165-167; Muesing, M.A., Smith, D., Capon, D., (1987) Ceil, 48, pp. 691-701; Esteban, R., Fujimura, T., Wickner, R.B., (1989) EMBOJ, 8, pp. 947-954; Jacks, T., Power, M.D., Masiarz, F.R., Luciw, P.A., Barr, P.J., Varmus, H.E., (1988) Nature, 331, pp. 280-283; Jacks, T., Madhani, H.D., Masiarz, F.R., Varmus, H.E., (1988) Cell, 55, pp. 447-458; Hanly, S.M., Rimsky, L.T., Malim, M.H., Kim, J.H., Hauber, J., Due Dodon, M., Le, S.-Y., Greene, W.C., (1989) Genes Dev, 3, pp. 1534-1544","Le, S.-Y.; Laboratory of Mathematical Biology, Division of Cancer Biology, Diagnosis and Centers, National Cancer Institute, NIH, Building 469, Room 151, Frederick, MD 21702, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",,Scopus,2-s2.0-0028341510
"Opstelten D.J., de Groote P., Horzinek M.C., Rottier P.J.","7003742658;7006255636;7102624836;7006145490;","Folding of the mouse hepatitis virus spike protein and its association with the membrane protein.",1994,"Archives of virology. Supplementum","9",,,"319","328",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028185397&partnerID=40&md5=e0bda438b75c7c74b8614aee2a742291","Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Netherlands","Opstelten, D.J., Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Netherlands; de Groote, P., Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Netherlands; Horzinek, M.C., Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Netherlands; Rottier, P.J., Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Netherlands","Coronaviruses are assembled by budding into pre-Golgi membranes. Using different approaches we have demonstrated that the spike (S) protein and the membrane (M) protein of mouse hepatitis virus (MHV) associate to form large complexes. Newly synthesized M was found in these complexes almost immediately after its synthesis, whereas the S protein started to appear in heterocomplexes after 10-20 min. This is consistent with the slow rate of folding of S and with the observation that folding of S preceeds its association with M. While the folding of S involves the formation of multiple disulfide bonds, folding of M is disulfide-independent. This contrast was reflected by the differential sensitivity of the two proteins to reduction with dithiothreitol (DTT). Addition of DTT to the culture medium of MHV-infected cells drastically impaired the folding of S, but not of M. Consequently, the S protein was unable to interact with M. Under these conditions, S stayed in the ER while M was transported efficiently beyond the site of budding to the Golgi complex. We conclude that the association of S with M is an essential step in the formation of the viral envelope and in the accumulation of both proteins at the site of virus assembly.",,"disulfide; dithiothreitol; M protein, Coronavirus; matrix protein; membrane protein; spike glycoprotein, coronavirus; virus envelope protein; article; drug effect; growth, development and aging; metabolism; Murine hepatitis coronavirus; oxidation reduction reaction; protein folding; transport at the cellular level; virus replication; Biological Transport; Disulfides; Dithiothreitol; Membrane Glycoproteins; Murine hepatitis virus; Oxidation-Reduction; Protein Folding; Viral Envelope Proteins; Viral Matrix Proteins; Virus Replication",,"Opstelten, D.J.",,,09391983,,,"8032264","English","Arch. Virol. Suppl.",Article,"Final",,Scopus,2-s2.0-0028185397
"Preston G.M., Jung J.S., Guggino W.B., Agre P.","35416035400;56073146800;35448882600;7102695643;","Membrane topology of aquaporin CHIP. Analysis of functional epitope- scanning mutants by vectorial proteolysis",1994,"Journal of Biological Chemistry","269","3",,"1668","1673",,139,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027976658&partnerID=40&md5=ff4d6bb04d10fadc2b2951adab481043","Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States","Preston, G.M., Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States; Jung, J.S., Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States; Guggino, W.B., Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States; Agre, P., Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States","CHIP is the archetypal member of the aquaporins, a widely expressed family of membrane water channels. The NH2- and COOH-terminal halves of CHIP are sequence-related, and hydropathy analysis predicted six membrane-spanning domains with five connecting loops (A-E). Here, we determined the membrane topology of CHIP expressed in Xenopus oocytes using biologically active recombinant channels. CHIP is glycosylated at Asn-42, indicating loop A is exofacial. An epitope from the coronavirus E1 glycoprotein was inserted into CHIP and localized to the outer or inner leaflet of the membrane by α- chymotrypsin digestion of intact oocytes or inside-out membrane vesicles. The E1 epitope at Thr-120 was protease-sensitive in intact oocytes, indicating that loop C is exofacial. The E1 epitope at Lys-6, Arg-162, or Lys-267 was protease-sensitive in inside-out membrane vesicles, confirming the cytoplasmic location of the NH2 and COOH termini and loop D. Insertions into loops B and E did not produce active water channels, but their cleavage patterns were consistent with inner (loop B) and outer (loop E) leaflet locations. This study indicates that the functional CHIP molecule is a unique structure with two internal repeats oriented 180° to each other within the membrane.",,"membrane protein; article; cellular distribution; membrane channel; nonhuman; priority journal; protein analysis; protein glycosylation; protein localization; xenopus laevis; Amino Acid Sequence; Animal; Cell Membrane; Chymotrypsin; Epitopes; Erythrocyte Membrane; Female; Glycosylation; Human; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Oocytes; Protein Structure, Secondary; Recombinant Proteins; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Xenopus laevis; Coronavirus",,"Preston, G.M.; Dept. of Biological Chemistry, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe St., Baltimore, MD 21205, United States",,,00219258,,JBCHA,"7507481","English","J. BIOL. CHEM.",Article,"Final",,Scopus,2-s2.0-0027976658
"Van Reeth K., Pensaert M.","57191565576;55905425400;","Prevalence of infections with enzootic respiratory and enteric viruses in feeder pigs entering fattening herds.",1994,"The Veterinary record","135","25",,"594","597",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028775899&partnerID=40&md5=7fb92e1b586b14d6c5e116c61831b6da","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Merelbeke, Belgium","Van Reeth, K., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Merelbeke, Belgium; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Merelbeke, Belgium","The prevalence of infections with H1N1- and H3N2-influenza viruses, porcine respiratory coronavirus (PRCV), transmissible gastroenteritis virus (TGEV) and porcine epidemic diarrhoea virus (PEDV) in feeder pigs shortly after their entry into fattening units was examined. Ten groups of pigs with acute respiratory disease during the months September to October 1991 and seven groups of pigs with acute diarrhoea during the months February to March 1992 were investigated. On arrival in the fattening herds, more of the pigs were negative for antibodies against H1N1-influenza virus and against PRCV during September to October (61 and 50 per cent, respectively) than in February to March (51 and 34 per cent, respectively). There was serological evidence of a triple infection with PRCV and both influenza viruses in seven of the 17 groups; dual infections with PRCV and H1N1-influenza virus occurred in nine groups and with H1N1- and H3N2-influenza viruses in one group. Seroconversion against TGEV was not detected in any of the 17 groups, but seven of them had seroconverted to PEDV. Multiple infections with PRCV and either one or both of the influenza viruses were thus very common shortly after the introduction of feeder pigs into the fattening herds. There was no association between the type and/or multiplicity of these infections and respiratory disease, but infections with PEDV were clearly associated with outbreaks of diarrhoea.",,"virus antibody; animal; animal disease; article; Belgium; epidemic; gastrointestinal disease; immunology; Influenza virus A; isolation and purification; Orthomyxovirus infection; prevalence; season; swine; swine disease; Transmissible gastroenteritis virus; virology; Animals; Antibodies, Viral; Belgium; Disease Outbreaks; Gastrointestinal Diseases; Influenza A virus; Orthomyxoviridae Infections; Prevalence; Seasons; Swine; Swine Diseases; Transmissible gastroenteritis virus",,"Van Reeth, K.",,,00424900,,,"7900243","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0028775899
"Chen Z., Faaberg K.S., Plagemann P.G.W.","7409486859;6701827490;7102193015;","Determination of the 5' end of the lactate dehydrogenase-elevating virus genome by two independent approaches",1994,"Journal of General Virology","75","4",,"925","930",,15,"10.1099/0022-1317-75-4-925","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028316666&doi=10.1099%2f0022-1317-75-4-925&partnerID=40&md5=314523b98f8938cf16a747806c15278a","Department of Microbiology, Medical School, University of Minnesota, Minneapolis, MN 55455, United States","Chen, Z., Department of Microbiology, Medical School, University of Minnesota, Minneapolis, MN 55455, United States; Faaberg, K.S., Department of Microbiology, Medical School, University of Minnesota, Minneapolis, MN 55455, United States; Plagemann, P.G.W., Department of Microbiology, Medical School, University of Minnesota, Minneapolis, MN 55455, United States","We have determined the 5' end of the lactate dehydrogenase-elevating virus (LDV) genome (strain LDV-P) using two independent approaches. In one approach, methylmercuric hydroxide-denatured genomic RNA was reverse-transcribed using as primer an oligonucleotide complementary to the 5' end of open reading frame (ORF) 1a. The first-strand cDNA was ligated with T4 RNA ligase to an oligonucleotide of which the 3' end was blocked. The ligated product was amplified by PCR, cloned and sequenced. In the second approach, untreated or decapped genomic RNA was ligated between the 3' and 5' ends, reverse-transcribed across the ligation junction and the product was amplified by PCR, cloned and sequenced. Both approaches yielded the same results, indicating that the 5' leader of LDV-P is 156 nucleotides long, inclusive of the 5' UAUAACC 3' sequence involved in the linkage of the 5' leader to the bodies of the seven subgenomic mRNAs of LDV. The 5' leader of LDV is about 50 nucleotides shorter than those of the related viruses, equine arteritis virus and Lelystad virus, but at least twice as long as the leaders of the coronaviruses. The finding that untreated LDV RNA was ligated 5' to 3' end as efficiently as RNA treated with decapping enzyme suggests that genomic LDV RNA may not possess a 5' cap but terminates with 5' phosphoryl-A.",,"complementary DNA; hydroxide; messenger RNA; methylmercury derivative; primer RNA; RNA ligase; article; Coronavirus; Equine viral arteritis virus; genetic linkage; Lactic dehydrogenase togavirus; nonhuman; nucleotide sequence; open reading frame; polymerase chain reaction; priority journal; RNA degradation; RNA transcription; virus genome; Coronavirus; Equidae; Equine arteritis virus; Lactate dehydrogenase-elevating virus; Lelystad virus; Togaviridae",,"Plagemann, P.G.W.; Department of Microbiology, Medical School, University of Minnesota, Minneapolis, MN 55455, United States",,"Microbiology Society",00221317,,JGVIA,"7512122","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0028316666
"Britton P., Kottier S., Chen C.-M., Pocock D.H., Salmon H., Aynaud J.M.","57203302770;6505850323;7501958673;7005365522;57214489289;7004089814;","The use of PCR genome mapping for the characterisation of TGEV strains",1994,"Advances in Experimental Medicine and Biology","342",,,"29","34",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028297069&partnerID=40&md5=c7193473a21dd99e8df8723897b0ad3e","Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom","Britton, P., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Kottier, S., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Chen, C.-M., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Pocock, D.H., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Salmon, H., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom; Aynaud, J.M., Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom","Previous studies on different transmissible gastroenteritis virus (TGEV) strains, including porcine respiratory coronavirus (PRCV), have identified regions within the genome that are polymorphic as regards insertions and deletions. For example the 672 base deletion within the S gene and multiple deletions 5', within and 3' of the ORF-3a gene were detected in strains of PRCV. The presence of deletions may be associated with a change in the virulence, attenuation or tissue tropism of the isolate. The Nouzilly (188- SG) TGEV vaccine strain was attenuated by passage of a cell culture adapted virulent isolate D-52 188 times through swine testis cells after treatment with gastric juice. PCR amplification with oligonucleotides, corresponding to known TGEV sequences, were used to analyze D-52 and 188-SG for genetic variation. Results with several pairs of oligonucleotides within the first 1565 nucleotides of the S gene did not identify a deletion within this region of the genome from either strain. However, oligonucleotides directed against the ORF-3a/3b region detected a deletion of about 250 nucleotides within the 188-SG genome but not in the D-52 genome. Since all the attenuated TGEV strains so far sequenced, PRCV, Miller SP and 188-SG, contained deletions within the ORF-3a/3b, it would suggest that this region of the TGEV genome is involved in regulating viral virulence.",,"oligonucleotide; conference paper; coronavirus; gene deletion; gene insertion; gene mapping; genetic polymorphism; nonhuman; polymerase chain reaction; priority journal; swine; virus genome; virus virulence; Amino Acid Sequence; Animal; Base Sequence; Cell Line; Comparative Study; Genome, Viral; Molecular Sequence Data; Open Reading Frames; Phenotype; Polymerase Chain Reaction; Sequence Alignment; Sequence Homology; Species Specificity; Swine; Transmissible gastroenteritis virus",,"Britton, P.; Division of Molecular Biology, A.F.R.C., Institute for Animal Health, Newbury, Berkshire RG16 0NN, United Kingdom",,,00652598,,AEMBA,"8209745","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028297069
"Welter M.W., Horstman M.P., Welter C.J., Welter L.M.","7004347897;6507248590;57196670411;36977509200;","An overview of successful TGEV vaccination strategies and discussion on the interrelationship between TGEV and PRCV",1994,"Advances in Experimental Medicine and Biology","342",,,"463","468",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028330832&partnerID=40&md5=0197af021d2b47a3a2be0a949ca7d3da","Ambico, Inc., Dallas Center, IA, United States","Welter, M.W., Ambico, Inc., Dallas Center, IA, United States; Horstman, M.P., Ambico, Inc., Dallas Center, IA, United States; Welter, C.J., Ambico, Inc., Dallas Center, IA, United States; Welter, L.M., Ambico, Inc., Dallas Center, IA, United States","Porcine respiratory coronavirus (PRCV) is a new variant of TGE with an altered pathogenesis. PRCV multiplies mainly in tonsilar tissues and the respiratory tract. There are no enteric symptoms and in experimentally infected pigs, even the respiratory tract infection is usually asymptomatic. PRCV is spread aerogenically through herds and the significance of PRCV as a pathogen in swine has yet to be determined. Despite the differences in pathogenesis and tissue tropism, the behavior of TGEV and PRCV are closely related antigenically. PRCV induces an antibody response in pigs that cannot be distinguished from TGEV-infected pigs by conventional serological assays. PRCV sensitized animals are not protected from TGEV challenge nor is the milk antibody provided to nursing piglets completely effective in prevention of TGEV infections; thus PRCV is not a good vaccine candidate for TGEV infections. PRCV subclinical infections have led to several reported cases of enzootic TGEV in herds that had been diagnosed as TGEV immune strictly on the basis of serum neutralizing titers which were later found to be due to exposure to PRCV. Vaccination studies conducted with the Ambico, oral modified live TGEV vaccine have led to some startling new results: (1) Use of Ambico TGEV modified live vaccine has been shown to provide complete protection against subsequent PRCV challenge and (2) the effectiveness of TGEV vaccination is actually enhanced by previous exposure to PRCV (3) Weanling pigs which have passively acquired circulating TGEV neutralizing antibodies are protected from subsequent PRCV infections.",,"vaccine; animal experiment; animal model; antibody production; conference paper; controlled study; coronavirus; immunogenicity; nonhuman; oral drug administration; pathogenesis; priority journal; respiratory tract disease; swine disease; vaccination; virus infection; virus inhibition; virus transmission; Administration, Intranasal; Administration, Oral; Animal; Animals, Newborn; Animals, Suckling; Antibodies, Viral; Coronavirus Infections; Female; Gastroenteritis, Transmissible, of Swine; Immunity, Maternally-Acquired; Milk; Pregnancy; Pregnancy Complications, Infectious; Respiratory Tract Infections; Swine; Swine Diseases; Transmissible gastroenteritis virus; Vaccination; Viral Vaccines",,"Welter, M.W.; Ambico, Inc., Dallas Center, IA, United States",,,00652598,,AEMBA,"8209768","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028330832
"Henrickson K.J.","7004132672;","Lower respiratory viral infections in immunocompetent children.",1994,"Advances in pediatric infectious diseases","9",,,"59","96",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028060896&partnerID=40&md5=bf7c4c89e844ff02f36e08bd200333ee","Department of Pediatrics, Medical College of Wisconsin, Milwaukee, United States","Henrickson, K.J., Department of Pediatrics, Medical College of Wisconsin, Milwaukee, United States","Viral lower respiratory disease causes a heavy burden on our society. Better understanding of the epidemiology of these viruses combined with new rapid diagnostic techniques will provide more rapid and more reliable diagnosis of these agents in the future. Two agents not commonly thought of as causes of LRI in children (rhinoviruses, coronaviruses) should now be added to an already long list. Effective drugs exist for prophylaxis against influenza virus type A and therapy for influenza virus type A, type B, and RSV. While no new antiviral drugs are near clinical use at this time, new antiviral agents are constantly being tested and developed. High-titer, specific antiviral IVIG appears promising for both therapy and prophylaxis. Over the next decade, improved influenza virus vaccines and safe and effective vaccines against HPIV and RSV are expected. Adenoviral vaccines for use in immunocompromised patients are possible, but a generally available vaccine for all children is less likely. Although the basic clinical epidemiology of these viruses has been well investigated over the last 30 years, new molecular techniques are greatly expanding our understanding of these agents. Antigenic and genetic variation is being found in many viruses previously thought homogeneous. The exact role and biologic significance of this variation is just beginning to be explored, but already there is evidence of differences in pathogenicity and immunogenicity in many of these substrains. All of this information will have an impact on future vaccine and antiviral drug development.",,"bronchus disease; child; cost; economics; female; human; infant; lung disease; male; microbiology; preschool child; review; United States; virus pneumonia; Bronchial Diseases; Child; Child, Preschool; Costs and Cost Analysis; Female; Humans; Infant; Lung Diseases; Male; Pneumonia, Viral; United States",,"Henrickson, K.J.",,,08849404,,,"8123226","English","Adv Pediatr Infect Dis",Review,"Final",,Scopus,2-s2.0-0028060896
"Li W., Junker D., Hock L., Ebiary E., Collisson E.W.","56113755300;6701370263;6701444235;6504820409;57194517102;","Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus",1994,"Virus Research","34","3",,"327","338",,79,"10.1016/0168-1702(94)90132-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028035270&doi=10.1016%2f0168-1702%2894%2990132-5&partnerID=40&md5=bfb066ec94b2573844d2069234724d95","Department of Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States; Research Laboratories, Syntro Corporation, San Diego, CA, United States","Li, W., Department of Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States; Junker, D., Research Laboratories, Syntro Corporation, San Diego, CA, United States; Hock, L., Research Laboratories, Syntro Corporation, San Diego, CA, United States; Ebiary, E., Department of Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States; Collisson, E.W., Department of Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States","The large number of phenotypically distinct strains of infectious bronchitis virus (IBV) provide a broad genetic background for examining naturally occurring coronavirus variation. Comparisons of the published nucleotide sequence of S1 genes of strains isolated in Europe, Japan and the USA and four additional American strains described in this report identified 4 genetically distinct groups. The Dutch group was the most divergent sharing only about 60% identity with the American, Mass and European groups which were about 80% homologous with each other. Whereas the strains within the Mass, European and Dutch strains were at least 95% homologous, the strains within the American group were most variable, sharing about 80% identity. The hypervariable region (HVR) which tended to correlate with serotype extended from amino acid residue 53 to 148. In addition to the previously described putative recombination events in the S1 gene of PP14 and SE17, we have now described similar shifts in homology in the corresponding gene of the Gray, Holte, 6/82 (European strain), and Iowa strains. Although minor cross-over sites were identified in the more conserved 3' end at approximately nt 1000 and 1400, a frequently used hot-spot for recombination extended from nt 25 to a region immediately upstream of, but not including, the hypervariable region (HVR). In addition to point mutations, deletions, and insertions, recombination often involving Mass-like and Ark-like sequences, is a commonly used mechanism responsible for the evolution of IBV. © 1994.","Evolution; IBV; Infectious bronchitis virus; Mutation; Recombination; S1 gene","article; avian infectious bronchitis virus; controlled study; evolution; genetic variability; mutation; nonhuman; nucleotide sequence; priority journal; united states; Amino Acid Sequence; Animal; Base Sequence; Databases, Factual; DNA Primers; Evolution; Genes, Viral; Infectious bronchitis virus; Molecular Sequence Data; Phenotype; Phylogeny; Recombination, Genetic; RNA, Viral; Sequence Analysis, RNA; Sequence Homology; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Variation (Genetics); Aves; Avian infectious bronchitis virus; Coronavirus","Banner, Lai, Random nature of Coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Beaudette, Hudson, Cultivation of the virus of infectious bronchitis (1937) J. Am. Vet. Med. Assoc., 90, pp. 51-60; Binns, Boursnell, Cavanagh, Pappin, Brown, Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) J. Gen Virol., 66, pp. 719-926; Butcher, Gelb, Collisson, Comparisons of the genomic RNA of Arkansas DPI embryonic passages 10 and 100, Australian T, and Massachusetts 41 strains of infectious bronchitis virus (1990) Avian Dis., 34, pp. 253-259; Cavanagh, Davis, Coronavirus IBV: Removal of Spike Glycopolypeptide S1 by Urea Abolishes Infectivity and Haemagglutination but Not Attachment to Cells (1986) Journal of General Virology, 67, pp. 1443-1448; Cavanagh, Davis, Cook, Li, Molecular basis of the variation exhibited by avian infectious bronchitis coronavirus (IBV) (1991) Coronaviruses and Their Diseases, pp. 369-372. , D. Cavanagh, T.D.K. Brown, Plenum Press, New York; Cavanagh, Davis, Mockett, Amino acids within hypervariable region 1 of avian coronavirus IBV (Massachusetts serotype) spike glycoprotein are associated with neutralization epitopes (1988) Virus Res, 11, pp. 141-150; Chomczynski, Sacchi, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analyt. Biochem., 162, pp. 156-159; Clewley, Morser, Avery, Lomniczi, Oligonucleotide fingerprinting of the RNA of different strains of infectious bronchitis virus (1981) Infect. Immun., 32, pp. 1227-1233; Cook, Isolation of a new serotype of infectious bronchitis-like virus from chickens in England (1983) Vet. Record, 112, pp. 104-105; Davelaar, Kouwenhoven, Burger, Occurrence and significance of infectious bronchitis virus variant strains in egg and broiler production in the Netherlands (1984) Vet. Q., 6, pp. 114-120; Field, Arkansas 99, a new infectious bronchitis serotype (1973) Avian Dis., 17, pp. 659-661; Gelb, Jr., nfectious bronchitis (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, pp. 124-127. , Purchase et al., 3rd ed., Dendall/Hunt; Hofstad, Antigentic differences among isolates of avian infectious bronchitis virus (1958) Am. J. Vet. Res., 19, pp. 740-743; Holland, Spindler, Horodyski, Grabau, Nichol, VandePol, Rapid evolution of RNA genomes (1982) Science, 215, pp. 1577-1585; Hopkins, Serologie and immunologie properties of a recent isolate of infectious bronchitis virus (1969) Avian Dis., 13, pp. 356-362; Jungherr, Chomiak, Luginbuhl, Immunologie differences in strains of infectious bronchitis virus (1956) Proc. 60th Annu. Meeting, pp. 203-209. , US Livestock San. Assoc; Koch, Cavanagh, Commentary on session two: IB virus (1991) Proceedings of II International Symposium on Infectious Bronchitis, pp. 191-194. , Rauischolzhausen, Germany. June 3–6; Koch, Kant, Nucleotide and amino acid sequence of the S1 subunit of the spike glycoprotein of avian infectious bronchitis virus, strain D3896 (1990) Nucleic Acids Res., 18, pp. 3063-3064; Küsters, Niesters, Lenstra, Horzinek, Van der Zeijst, Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Lai, RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Lai, Baric, Makino, Deck, Egbert, Leibowitz, Stohlman, The recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Liao, Lai, RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol., 66, pp. 6117-6124; Makino, Keck, Stohlman, Lai, High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Matthew, Binns, Boursnell, Brown, Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) J. Gen. Virol., 67, pp. 2825-2831; Niesters, Lenstra, Spaan, Zijderveld, Bleumink-Pluym, Hong, Van Scharrenburg, Van de Zeijst, The peplomer protein sequence of the M41 strain of coronavirus IBV and its comparison with Beaudette strains (1986) Virus Res., 5, pp. 253-263; Parr, Collisson, Epitopes on the spike protein of a nephropathogenic strain of infectious bronchitis virus (1993) Arch. Virology, 133, pp. 369-383; Sambrook, Fritsch, Maniatis, (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Sneed, Butcher, Parr, Wang, Collisson, Comparison of the structural proteins of avian infections bronchitis virus as determined by western blot analysis (1989) Virol. Immunol., 2, pp. 221-227; Sutou, Sato, Okabe, Nakai, Sasaki, Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Van Roekel, Clarke, Bullis, Olesiuk, Sperling, Infectious bronchitis (1951) Am. J. Vet. Res., 12, pp. 140-146; Wang, Junker, Collisson, Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Williams, Wang, Sneed, Collisson, Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Res., 25, pp. 213-222; Winterfield, Hitchner, Etiology of an infectious nephritis-nephrosis syndrome of chickens (1962) Am. J. Vet. Res., 23, pp. 1273-1279; Winterfield, Hitchner, Appleton, Immunological Characteristics of a Variant of Infectious Bronchitis Virus Isolated from Chickens (1964) Avian Diseases, 8 (1), pp. 40-47","Collisson, E.W.; Department of Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States",,,01681702,,VIRED,"7856318","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0028035270
"Oleszak E.L.","6603665574;","Molecular mimicry between Fc receptors and viral antigens.",1994,"Archivum immunologiae et therapiae experimentalis","42","2",,"83","88",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028678874&partnerID=40&md5=a0c2cfd1410bc3c6ed48344b2a009b3c","Department of Pathology, University of Texas Health Science Center, Medical School, Houston, 77030, United States","Oleszak, E.L., Department of Pathology, University of Texas Health Science Center, Medical School, Houston, 77030, United States","Molecular mimicry has been characterized as the presence of common epitopes, either linear or conformational, shared by host and microbial determinants. Such cross-reactivity may lead to an autoimmune disease. On the other hand molecular mimicry between certain viral proteins and host determinant may protect invading virus to be eliminated by immune system and may promote persistence. In this mini-review I discuss the molecular mimicry of S peplomer protein of mouse hepatitis virus, strain JHM (MHV-JHM) to the host Fc gamma receptor (Fc gamma R). MHV-JHM induces in rodents acute encephalomyelitis and surviving animals develop demyelinating disease with concomitant persistent infection. We have demonstrated that rabbit IgG, but not is F(ab')2 fragments, monoclonal rat and mouse IgG and the rat 2.4G2 anti-Fc gamma R mab immunoprecipitated natural and recombinant S peplomer protein of several strains of MHV. Furthermore, MHV-JHM infected cells formed rosettes with anti-sheep red blood cell (SRBC) - antibody coated SRBC. The 2.4G2 anti-Fc gamma R mab are able to neutralize several strains of MHV, presumably by binding to S peplomer protein. Therefore, the Fc binding site of S is present on the surface of MHV-infected cells. This molecular mimicry between S peplomer protein of MHV-JHM and Fc gamma R has been extended to other members of Coronaviridae, namely bovine coronavirus and transmissible gastroenteritis virus but not to infectious bronchitis virus. The molecular mimicry of viral antigens to Fc receptors has been described also for members of Herpesviridae, namely Herpes simplex, cytomegalovirus and Varicella zoster.(ABSTRACT TRUNCATED AT 250 WORDS)",,"epitope; Fc receptor; virus antigen; animal; cross reaction; human; immunology; review; Animals; Antigens, Viral; Cross Reactions; Epitopes; Humans; Receptors, Fc",,"Oleszak, E.L.",,,0004069X,,,"7503651","English","Arch. Immunol. Ther. Exp. (Warsz.)",Review,"Final",,Scopus,2-s2.0-0028678874
"Niyogi S.K., Saha M.R., De S.P.","7005034655;7102365247;7202304431;","Enteropathogens associated with acute diarrhoeal diseases.",1994,"Indian journal of public health","38","2",,"29","32",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028420770&partnerID=40&md5=9c8233074349d8102d2c438ee78d8afd","Division of Microbiology, National Institute of Cholera &amp; Enteric Diseases, Beliaghata, Calcutta, India","Niyogi, S.K., Division of Microbiology, National Institute of Cholera &amp; Enteric Diseases, Beliaghata, Calcutta, India; Saha, M.R., Division of Microbiology, National Institute of Cholera &amp; Enteric Diseases, Beliaghata, Calcutta, India; De, S.P., Division of Microbiology, National Institute of Cholera &amp; Enteric Diseases, Beliaghata, Calcutta, India","Five types of Escherichia coli are responsible for as much as 25% of all diarrheal diseases in developing countries. They tend to be transmitted via contaminated foods, particularly weaning foods, and water. They include enterotoxigenic, enteropathogenic, enteroadherent, enteroinvasive, and enterohemorrhagic E. coli. Shigella species are responsible for 10-15% of acute diarrheas in children less than 5 years old and the most common etiologic agents of childhood dysentery. Shigellosis is common in the warm season. An outbreak of shigella dysentery in West Bengal, India, had a high attack rate in children less than 5 years old and was resistant to many drugs. Nontyphoid Salmonella species cause watery diarrhea with nausea, cramps, and fever. Worldwide, various Salmonella strains exhibit resistance to ampicillin, chloramphenicol, and co-trimoxazole. Campylobacter jejuni produces watery diarrhea which, in 33% of cases and 1-2 days after onset, contains blood and mucus. Many normal healthy children in developing countries are carriers of C. jejuni. Vibrio cholerae O1 is endemic in parts of Africa and Asia (e.g., 5-10% of hospitalized diarrhea patients). The ElTor cholera biotype is responsible for the 7th pandemic. Other bacterial enteropathogens are Aeromonas species, Bacteroides fragilis, and Providencia alcalifaciens. Rotavirus is a major cause of sporadic and epidemic diarrhea among 6-23 month olds. Its incidence peaks in cold or dry seasons. Other viral enteropathogens are Norwalk virus, adenoviruses, astroviruses, and coronaviruses. In India, the prevalence of Entamoeba histolytica varies from 3.6% to 47.4%. It occurs equally in high and low socioeconomic classes. Giardia lamblia usually infects 1-5 year old children. Its transmission routes are food, water, and the fecal-oral route. Cryptosporidia produce acute watery diarrhea, especially in children less than 2 years old. Cryptosporidia diarrhea is common among AIDS patients. Oral rehydration therapy and proper feeding during and after diarrhea reduces deaths from diarrhea.",,"acute disease; Asia; Bacterial And Fungal Diseases--transmission; Case Fatality Rate; Demographic Factors; developing country; diarrhea; Diarrhea, Infantile--etiology; Diarrhea--etiology; Diseases; Enterobacter infection; fluid therapy; human; India; infant; Infections; intestine infection; microbiology; mortality; newborn; oral rehydration therapy; Parasitic Diseases--transmission; parasitology; population; population dynamics; preschool child; review; seasonal variation; Southern Asia; treatment; Viral Diseases--transmission; virus infection; Asia; Bacterial And Fungal Diseases--transmission; Case Fatality Rate; Death Rate; Demographic Factors; Developing Countries; Diarrhea, Infantile--etiology; Diarrhea--etiology; Diseases; India; Infections; Mortality; Oral Rehydration; Parasitic Diseases--transmission; Population; Population Dynamics; Seasonal Variation; Southern Asia; Treatment; Viral Diseases--transmission; Acute Disease; Child, Preschool; Developing Countries; Diarrhea; Enterobacteriaceae Infections; Fluid Therapy; Humans; India; Infant; Infant, Newborn; Intestinal Diseases, Parasitic; Rotavirus Infections",,"Niyogi, S.K.",,,0019557X,,,"7835992","English","Indian J Public Health",Review,"Final",,Scopus,2-s2.0-0028420770
"Krijnse-Locker J., Ericsson M., Rottier P.J.M., Griffiths G.","6602308258;7005269130;7006145490;56221617000;","Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step",1994,"Journal of Cell Biology","124","1-2",,"55","70",,188,"10.1083/jcb.124.1.55","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028069572&doi=10.1083%2fjcb.124.1.55&partnerID=40&md5=76f689beac819e8c8d49ec1327738862","Institute of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3584 CL Utrecht, Netherlands; EMBL, D-69012 Heidelberg, Germany; EMBL, Meyerhofstrasse 1, D-69012 Heidelberg, Germany","Krijnse-Locker, J., Institute of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3584 CL Utrecht, Netherlands; Ericsson, M., EMBL, D-69012 Heidelberg, Germany; Rottier, P.J.M., Institute of Virology, Faculty of Veterinary Medicine, University of Utrecht, Yalelaan 1, 3584 CL Utrecht, Netherlands; Griffiths, G., EMBL, D-69012 Heidelberg, Germany, EMBL, Meyerhofstrasse 1, D-69012 Heidelberg, Germany","Mouse hepatitis coronavirus (MHV) buds into pleomorphic membrane structures with features expected of the intermediate compartment between the ER and the Golgi complex. Here, we characterize the MHV budding compartment in more detail in mouse L cells using streptolysin O (SLO) permeabilization which allowed us to better visualize the membrane structures at the ER-Golgi boundary. The MHV budding compartment shares membrane continuities with the rough ER as well as with cisternal elements on one side of the Golgi stack. It also labeled with p58 and rab2, two markers of the intermediate compartment, and with PDI, usually considered to be a marker of the rough ER. The membranes of the budding compartment, as well as the budding virions themselves, but not the rough ER, labeled with the N-acetyl-galactosamine (GalNAc)-specific lectin Helix pomatia. When the SLO-permeabilized cells were treated with guanosine 5'-(3-O-thio)triphosphate (GTPγS), the budding compartment accumulated a large number of β-cop-containing buds and vesicular profiles. Complementary biochemical experiments were carried out to determine whether vesicular transport was required for the newly synthesized M protein, that contains only O-linked oligosaccharides, to acquire first, GalNAc and second, the Golgi modifications galactose and sialic acid. The results from both in vivo studies and from the use of SLO-permeabilized cells showed that, while GalNAc addition occurred under conditions which block vesicular transport, both cytosol and ATP were prerequisites for the M protein oligosaccharides to acquire Golgi modifications. Collectively, our data argue that transport from the rough ER to the Golgi complex requires only one vesicular transport step and that the intermediate compartment is a specialized domain of the endoplasmatic reticulum that extends to the first cisterna on the cis side of the Golgi stack.",,"adenosine triphosphate; guanosine 5' o (3 thiotriphosphate); M protein; n acetylgalactosamine; oligosaccharide; Ras protein; streptolysin O; virus protein; animal cell; article; controlled study; Golgi complex; membrane transport; membrane vesicle; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein determination; rough endoplasmic reticulum; virion; virus cell interaction; virus transmission; Animalia; Coronavirus; Helix pomatia; Mouse hepatitis coronavirus; Murinae; Murine hepatitis virus","Ahnert-Hilger, G., Mach, W., Föhr, K.J., Gratzl, M., Poration by α-toxin and streptolysin O: An approach to analyze intracellular processes (1989) Methods Cell Biol., 31, pp. 63-90; Beckers, C.J.M., Balch, W.E., Calcium and GTP: Essential components in vesicular trafficking between the endoplasmatic reticulum and Golgi apparatus (1989) J. 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USA, 87, pp. 6944-6948; Melançon, P., Sarafini, T., Gleason, M.L., Orci, L., Rothman, J.E., Involvement of GTP-binding ""G"" proteins in transport through the Golgi stack (1987) Cell, 51, pp. 1053-1062; Mellman, I., Simons, K., The Golgi complex: In vitro veritas? (1992) Cell, 68, pp. 829-840; Niemann, H., Geyer, R., Klenk, H.-D., Linder, D., Stirm, S., Wirth, M., The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein E1 (1984) EMBO (Eur. Mol. Biol. Organ.) J., 3, pp. 665-670; Oprins, A., Duden, R., Kreis, T.E., Geuze, H.J., Slot, J.W., COP localizes mainly to the cis-Golgi side in exocrine pancreas (1993) J. Cell Biol., 121, pp. 49-59; Orci, L., Palmer, D.J., Ravazzola, M., Perrelet, A., Amherdt, M., Rothman, J.E., Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins (1993) Nature (Lond.), 362, pp. 648-652; Pavelka, M., Ellinger, A., Localization of binding sites for concanavalin A, Ricinus communis I and Helix pomatia Lectin in the Golgi apparatus of rat small intestinal absorptive cells (1985) J. Histochem. Cytochem., 33, pp. 905-914; Pelham, H.R.B., Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment (1988) EMBO (Eur. Mol. Biol. Organ.) J., 7, pp. 913-918; Pelham, H.R.B., Control of protein exit from the endoplasmatic reticulum (1989) Annu. Rev. 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Cell Sci., 100, pp. 415-430; Schekman, R.W., Genetic and biochemical analysis of vesicular traffic in yeast (1992) Curr. Opin. Cell Biol., 4, pp. 587-592; Sodeik, B., Doms, R.W., Ericsson, M., Killer, G., Machamer, C.E., Van't Hof, W., Van Meer, G., Griffiths, G., Assembly of vaccinia virus: Role of the intermediate compartment between the endoplasmatic reticulum and the Golgi stacks (1993) J. Cell Biol., 121, pp. 521-541; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Tooze, J., Tooze, S.A., Infection of AtT-20 murine putuitary tumour cells by mouse hepatitis virus strain A59: Virus budding is restricted to the Golgi region (1985) Eur. J. 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USA, 90, pp. 1681-1685","Griffiths, G.; EMBL, Meyerhofstrasse 1, D-69012 Heidelberg, Germany",,"Rockefeller University Press",00219525,,JCLBA,"8294506","English","J. CELL BIOL.",Article,"Final",Open Access,Scopus,2-s2.0-0028069572
"Koopmans M., Horzinek M.C.","7006736989;7102624836;","Toroviruses of Animals And Humans: A Review",1994,"Advances in Virus Research","43","C",,"233","273",,32,"10.1016/S0065-3527(08)60050-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028119091&doi=10.1016%2fS0065-3527%2808%2960050-0&partnerID=40&md5=4b79371827d0407cb8d9802e6a23cec5","Viral Exanthems and Herpesvirus Branch, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, United States; Department of Infectious Diseases and Immunology, Virology Division, Veterinary Faculty, Utrecht University, Utrecht, Netherlands","Koopmans, M., Viral Exanthems and Herpesvirus Branch, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30333, United States; Horzinek, M.C., Department of Infectious Diseases and Immunology, Virology Division, Veterinary Faculty, Utrecht University, Utrecht, Netherlands","Toroviruses are a group of enveloped positive-stranded RNA viruses that cause enteric, respiratory, and perhaps generalized infections in animals and humans. Their name refers to their unique morphological features: an elongated bacilliform core with two rounded ends is surrounded by a membrane that may either tightly adhere to or “shrink-wrap” it, without respecting the capsid's rod shape; in the first instance, straight or curved rhabdovirus-like particles are formed, whereas in the latter a biconcave disk results. Torovirus history is brief: the first representative, Berne virus (BEV), was isolated in Berne, Switzerland, in 1972 from a rectal swab taken from a horse with diarrhea 1 week before it died. BEV is the only equine torovirus isolate that replicates in cell culture; since most molecular data have been obtained with this isolate, BEV has been acknowledged as the torovirus prototype. Recognition of toroviruses as a new group of potentially pathogenic viruses came seven years after the discovery of BEV, when morphologically similar particles were discovered by electron microscopy (EM) in stool specimens from calves with severe diarrhea in a dairy herd in Breda, Iowa. Despite repeated attempts, BRV has not been adapted to the growth in cell or tissue culture, a problem which has hampered its biochemical, bio-physical, and molecular characterization. However, its pathogenesis and pathology have been studied in the experimentally infected gnotobiotic calves, showing that BRV infections may cause gastroenteritis. Recently, Vanopdenbosch et al. reported the isolation of a torovirus-like virus from the respiratory tract of calves with pneumonia, suggesting that both enterotropic and pneumotropic bovine toroviruses exist. Besides the established toroviruses of horses and cattle, torovirus-like particles (TVLPs) have been found by EM in different animal species; torovirus antibodies appear to be widespread in higher vertebrates, indicating that these viruses infect a broad range of animal hosts. The possibility of a torovirus infecting humans was first reported in 1984 and has become more likely in view of the recent data. This chapter is intended to update the information about toroviruses, and to describe the similarities and differences with the related coronaviruses. © 1994, Academic Press Inc.",,,"Akashi, H., Inaba, Y., Miura, Y., Tokuhisa, S., Sato, K., Satoda, K., (1980) Vet. Microbiol., 5, pp. 265-276; Bachmann, P.A., Hess, R.G., (1983) Ann. Rech. Vet., 14, pp. 502-506; Beards, G.M., Green, J., Hall, C., Flewett, T.H., Lamouliatte, F., Du Pasquier, P., (1984) Lancet, 2, pp. 1050-1052; Beards, G.M., Brown, D.W.G., Green, J., Flewett, T.H., (1986) J. Med. 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Microbiol., 7, pp. 221-240; Woode, G.N., Mohammed, K.A., Saif, L.J., Winand, N.J., Quesada, M., Kelso, N.E., Pohlenz, J.F., (1983), pp. 533-538. , Proc. Int. Symp. World Assoc. Vet. Lab. Diagnost., 3rd; Woode, G.N., Pohlenz, J.F., Kelso-Gourley, N.E., Fagerland, J., (1984) J. Clin. Microbiol., 19, pp. 623-630; Woode, G.N., Saif, L.J., Quesada, M., Winand, N.J., Pohlenz, J.F., Kelso Gourley, N., (1985) Am. J. Vet. Res., 46, pp. 1003-1010; Zanoni, R., Weiss, M., Peterhans, E., (1986) J. Gen. Virol., 67, pp. 2485-2488",,,,00653527,,,"8191955","English","Adv. Virus Res.",Article,"Final",,Scopus,2-s2.0-0028119091
"Bonilla P.J., Gorbalenya A.E., Weiss S.R.","7004225518;7005626044;57203567044;","Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains",1994,"Virology","198","2", 71088,"736","740",,65,"10.1006/viro.1994.1088","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028241850&doi=10.1006%2fviro.1994.1088&partnerID=40&md5=8359170f956827a15f05b640cf1444f2","Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States; Institute of Poliomyelitis and Viral Encephatitides, Russian Academy of Medical Sciences, 142782 Moscow region, Russian Federation","Bonilla, P.J., Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States; Gorbalenya, A.E., Institute of Poliomyelitis and Viral Encephatitides, Russian Academy of Medical Sciences, 142782 Moscow region, Russian Federation; Weiss, S.R., Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States","Gene 1, the putative RNA replicase gene of coronaviruses, is expressed via two large overlapping open reading frames (ORF 1a and ORF 1b). We have determined the nucleotide sequence of ORF 1a, encoded within the first 13.7 kb of gene 1, for the coronavirus mouse hepatitis virus strain A59 (MHV- A59). Putative papain-like protease domains, a picornavirus 3C-like protease domain, two hydrophobic domains, and a domain 'X' of unknown function, previously identified in other coronaviruses (1-3), are also present in ORF 1a of MHV-A59. Comparison between the ORF 1a sequence of MHV-A59 and the published sequence of the JHM strain of MHV (2) showed a high degree of similarity with the exception of several short regions. We sequenced one region of MHV-JHM that contained an 18 amino acid insertion relative to A59 and four other regions in which the sequences of the two strains differed. The MHV-2 and MHV-3 strains were also sequenced in some of these regions. Our analysis confirmed the presence of only one heterogeneous region in ORF 1a of MHV-A59 and MHV-JHM which is also present in MHV-2. Our findings indicate the need to modify the published sequence of MHV-JHM. © 1994 Academic Press, Inc.",,,"Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., (1989) Nucleic Acids Res, 17, pp. 4847-4861; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La-Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., (1991) Virology, 180, pp. 567-582; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., (1993) Virology, 195, pp. 680-691; Spaan, W., Cavanagh, D., Horzinek, M.C., (1990) Immuno-Chemistry of Viruses. II. the Basis for Serodiagnosis and Vaccines, pp. 359-379. , M. H. van Regenmortel and A. R. Neurath, Eds.), Elseviers Science Publishers, New York; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., (1989) Virology, 171, pp. 141-148; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.H., (1990) Nucleic Acids Res, 18, pp. 1825-1832; Koonin, E.V., Gorbalenya, A.E., Purdy, M.A., Rozanov, M.N., Reyes, G.R., Bradley, D.W., (1989) Proc. Natl. Acad. Sci. USA, 89, pp. 8259-8263; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., (1991) FEBS Lett, 288, pp. 201-205; Baker, S.C., Shieh, C.K., Chang, M.F., Vannier, D.M., Lai, M.M., (1989) C.J. Virol, 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., (1993) J. Virol, 67, pp. 6056-6063; Domingo, E., (1992) Curr. Opin. Genet Dev, 2, pp. 61-63; Garcia-Barreno, B., Portela, A., Delgado, T., Lopez, J.A., Melero, J.A., (1990) EMBOJ, 9, pp. 4181-4187; Sambrook, J., Fritsch, E.F., Maniatis, T., Molecular Cloning: A Laboratory Manual, pp. 712-715. , J. Sambrook etal., Eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Kawasaki, E.S., (1990) PCR Protocols: A Guide to Methods and Applications, pp. 21-27. , M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White, Eds., Academic Press, San Diego; Kong, H., Kucera, R.B., Jack, W.E., (1993) J. Biol. Chem, 268, pp. 1965-1975; Gombold, J.L., Hingley, S.T., Weiss, S.R., (1993) J. Virol, 67, pp. 4504-4512; Parker, M.M., Masters, P.S., (1990) Virology, 179, pp. 463-468; Luytjes, W., Sturman, L., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., (1987) Virology, 161, pp. 479-487; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., (1989) Virology, 173, pp. 664-673; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., (1992) Virology, 189, pp. 274-284; Hughes, S.A., Dension, M.L., Bonilla, P.J., Leibowitz, J.L., Weiss, S.R., Proceeding of the Fifth International Cor-Onavirus Symposium","Weiss, S.R.; Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",,Scopus,2-s2.0-0028241850
"Duarte M., Tobler K., Bridgen A., Rasschaert D., Ackermann M., Laude H.","57205792139;6701508835;6603799081;7004067163;7102624625;7006652624;","Sequence Analysis of the Porcine Epidemic Diarrhea Virus Genome between the Nucleocapsid and Spike Protein Genes Reveals a Polymorphic ORF",1994,"Virology","198","2", 71058,"466","476",,72,"10.1006/viro.1994.1058","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028227851&doi=10.1006%2fviro.1994.1058&partnerID=40&md5=9f4b9dafc77cce8841dea6186873d5e7","I.N.R.A., Unité de Virologie et Immunologie Moléculaires, CR de Jouy-en-Josas, 78350 Jouy-endosas, France; IInstitut für Virologie, Vet. Med. Fak. der Universit?t Z?rich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland","Duarte, M., I.N.R.A., Unité de Virologie et Immunologie Moléculaires, CR de Jouy-en-Josas, 78350 Jouy-endosas, France; Tobler, K., IInstitut für Virologie, Vet. Med. Fak. der Universit?t Z?rich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland; Bridgen, A., IInstitut für Virologie, Vet. Med. Fak. der Universit?t Z?rich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland; Rasschaert, D., I.N.R.A., Unité de Virologie et Immunologie Moléculaires, CR de Jouy-en-Josas, 78350 Jouy-endosas, France; Ackermann, M., IInstitut für Virologie, Vet. Med. Fak. der Universit?t Z?rich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland; Laude, H., I.N.R.A., Unité de Virologie et Immunologie Moléculaires, CR de Jouy-en-Josas, 78350 Jouy-endosas, France","In order to investigate the genome organization of the porcine epidemic diarrhea virus (PEDV) further, cDNA clones covering the region between the nucleocapsid and the spike (S) protein genes were independently constructed and sequenced for the two virulent isolates Br1/87 and CV777. Of the three major ORFs identified, two were found to encode the major and minor coronavirus membrane proteins M and sM. A potentially single ORF, designated ORF3 according to the pattern of the viral subgenomic mRNAs, could be identified between the S and sM genes. A striking variability, essentially generated by short deletions clustered in a few loci, was observed in the ORF3 of both isolates. The largest predicted polypeptide of 223 amino acids showed homology with polypeptides potentially encoded by other members of the same genetic subset, including two shorter polypeptides of human respiratory virus HCV 229E and one of transmissible gastroenteritis virus TGEV. This homology suggests that the two HCV ORFs may have originated from a single precursor. The function of these polypeptides is not known, but the predicted products of the PEDV ORF3 and related ORFs share features suggestive of a membrane-associated protein. © 1994 Academic Press. All rights reserved.",,"virus protein; article; controlled study; enterovirus; genetic polymorphism; nonhuman; open reading frame; priority journal; sequence analysis; spike; virus genome; virus nucleocapsid; Amino Acid Sequence; Base Sequence; Capsid; Cloning, Molecular; Comparative Study; DNA, Complementary; Genome, Viral; Molecular Sequence Data; Open Reading Frames; Polymorphism (Genetics); RNA, Messenger; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Transmissible gastroenteritis virus; Viral Core Proteins; Viral Envelope Proteins; Viral Matrix Proteins; Viral Proteins","Boursnell, M.E.G., Brown, T.D.K., Binns, M., Sequence of the membrane protein gene from avian coronavirus IBV (1984) Virus Res, 1, pp. 303-313; Bridgen, A., Duarte, M., Tobler, K., Laude, H.P., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen. Virol, 74, pp. 1795-1804; Bridgen, A., Tobler, K., Ackermann, M., Identification of coronaviral conserved sequences and application to viral genome amplification (1993) Coronaviruses: Molecular Biology and Virus-Host Interactions, , H. Laude and J. V. Vautherot, EdsPlenum, New York, in press; Britton, P., Kottier, S., Chen, C.-M., Pockok, D.H., Salmon, H., Aynaud, J.M., The use of PCR genome mapping for the characterisation of TGEV strains (1993) Coronaviruses: Molecular Biology and Virus-Host Interactions”, , H. Laude and J, V. Vautherot, EdsPlenum, New York, in press; Debouck, P., Pensaert, M., Experimental infection of pigs with a new porcine enteric coronavirus, CV 777 (1980) Am. J. Vet. Res, 41, pp. 219-223; Debouck, P., Pensaert, M., Coussement, W., The pathogenesis of an enteric infection in pigs, experimentally induced by the coronavirus-like agent, CV 777. Vet (1981) Microbiol, 6, pp. 157-167; Debouck, P., Prevalence of the porcine epidemic diarrhea (PED) virus in the pig population of different countries, Proc. 7th Int. Congr (1982) Pig Vet. Soc, , Mexico City; Delmas, B., Gelfi, J., L’Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Lujude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Dessen, P., Fondrat, C., Valencien, C., Mugnier, C., BISANCE A french service for access to biomolecular sequence databases (1990) Comput. Appl. Biosci, 6, pp. 355-356; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Res, 12, pp. 387-395; Duarte, M., Gelfi, J., Lambert, P., Rasschaert, D., Laude, H., Genomic organization of porcine epidemic diarrhoea virus (PEDV) (1993) Coronaviruses: Molecular Biology and Virus-Host Interactions, , H. Laude and J. V. Vautherot, EdsPlenum, New York, in press; Egberink, H.F., Ederveen, J., Callebaut, P., Horzinek, M.C., Characterization of the structural proteins of porcine epi-zootic diarrhea virus, strain CV 111 (1988) Am. J. Vet. Res, 49, pp. 1320-1324; Felsenstein, J., (1991) Phylip: Phylogenetic Inference Package, Version 3.4.”, , University of Washington, Seattle, WA; Godet, M., L’Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Hamilton, B., Palazzolo, M., Meyerowitz, M., Rapid isolation of long cDNA clones from existing libraries (1991) Nucleic Acids Res, 18, p. 1951; Have, P., Moving, V., Svansson, V., Uttenthal, A., Bloch, B., Coronavirus infection in mink (Mustela vison). Serological evidence of infection with a coronavirus related to transmissible gastroenteritis virus and porcine epidemic diarrhea virus. Vet (1992) Microbiol, 31, pp. 1-10; Higgins, D., Sharp, P., Fast and sensitive multiple sequence alignments on a micro computer. Comput (1989) Appl. Biosci, 5, pp. 151-153; Hofmann, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell culture (1988) J. Clin. Microbiol, 26, pp. 2235-2239; Horsburgh, B.C., Brierley, I., Brown, T., Analysis of a 9.6 kb sequence from the 3' end of canine coronavirus genomic RNA, j. Gen (1992) Virol, 73, pp. 2849-2862; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol, 66, pp. 6330-6337; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus 229E (1990) Virology, 174, pp. 608-612; Jouvenne, P., Mounir, S., Steward, J., Richardson, C.D., Talbot, P., Sequence analysis of human coronavirus 229E mRNA4 and 5: Evidence for polymorphism and homology with myelin basis protein (1992) Virus Res, 22, pp. 125-141; Kapke, P.A., Tung, F.Y.T., Brian, D.A., Nucleotide sequence between the peplomer and matrix protein genes of the porcine transmissible gastroenteritis coronavirus identifies three largeopen reading frames (1988) Virus Genes, 2, pp. 293-294; Knuchel, M., Ackermann, M., Muller, H., Kihm, U., An ELISA for detection of antibodies against porcine epidemic diarrhoea virus (PEDV) based on the specific solubility of the viral surface glycoprotein (1992) Vet. Microbiol, 32, pp. 117-134; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome. Annu (1990) Rev. Microbiol, 44, pp. 303-333; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Laude, H., Rasschaert, D., Huet, J.C., Sequence and N-terminal processing of the transmembrane proteine E1 of the coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol, 68, pp. 1687-1693; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol, 73, pp. 2731-2736; Pensaert, M.B., Debouck, P., A new coronavirus-like particle associated with diarrhea in swine. Arch (1978) Virol, 58, pp. 243-247; Pensaert, M.B., Debouck, P., Reynolds, D.J., An im-munoelectron microscopic and immunofluorescent study on the antigenic relationship between the coronavirus-like agent, CV 777, and several coronaviruses. Arch (1981) Virol, 68, pp. 45-52; Pfleiderer, M., Skinner, M.A., Siddell, S.G., Coronavirus MHV-JHM: Nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res, 14, p. 6338; Raabe, T., Siddell, S., Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 and mRNA 5 unique regions (1989) Nucleic Acids Res, 17, p. 6387; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochimie, 69, pp. 591-600; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol, 71, pp. 2599-2607; Saitou, N., Nei, M., The neighbor-joining method: A new method for reconstructing phylogenetic trees (1987) Mol. Biol. Evol, 4, pp. 406-425; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; Schmidt, M.F., Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses (1982) Virology, 1 (16), pp. 327-338; Short, J., Fernandez, J., Sorge, J., Huse, W., 1ZAP: A bacteriophage 1 expression vector with in vivo excision properties (1988) Nucleic Acids Res, 16, pp. 7583-7599; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol, 69, pp. 2939-2952; Utiger, A., Rosskopf, M., Guscetti, F., Ackermann, M., Preliminary characterization of a monoclonal antibody specific for a viral 27 kD glycoprotein family synthesized in porcine epidemic diarrhoea virus infected cells (1993) “Coronaviruses: Molecular Biology and Virus-Host Interactions, , H. Laude and J. V. Vautherot, EdsPlenum, New York, in press; Vaquero, C., Sanceau, J., Catinot, L., Reu, G., Falcoff, E., Falcoff, R., Translation of mRNA from phytohemagglu-linin-stimulated human lymphocytes: Characterization of interferon mRNAs (1982) J. Interf. Res, 2, pp. 217-218; Vennema, H., De Groot, R., Harbour, D., Horzinek, M., Spaan, W., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunoge-nicity of recombinant vaccinia virus in kittens (1991) Virology, 131, pp. 327-335; Wesley, R., Woods, R., Cheung, A., Genetic basis forthe pathogenesis of transmissible gastroenteritis virus (1990) J. Virol, 64, pp. 4761-4766; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns4gene of mouse hepatitis virus (MHV), strain A59 contains two ORFs and thus differs from ns4 of the JHM and S strains. Arch (1993) Virol, 129, pp. 301-309; Wood, W., Gitschier, J., Lasky, L., Uwvn, R., Base composition-independent hybridization in tetramethylammonium chloride: A method for oligonucleotide screening of highly complex gene libraries (1985) Proc. Natl. Acad. Sci. USA, 82 (1), pp. 585-1588; Yaling, Z., Ederveen, J., Egberink, H., Pensaert, M., Porcine epidemic diarrhoea virus (CV777) and feline infectious peritonitis virus (FIPV) are antigenically related. Arch (1988) Virol, 102, pp. 63-71; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-423; Yokomori, K.T., Lai, M.C.C., Mouse hepatitis virus S RNA sequence reveals That nonstructural proteins ns4 and ns5a are not essential for murine coronaviruses replication (1991) J. Virol, 65, pp. 5605-5608; Young, R., Bloom, B., Grosskinsky, C., Ivanyi, J., Thomas, D., Davis, R., Dissection of Mycobacterium tuberculosis antigens using recombinant DNA (1985) Proc. Nati. Acad. Sci. USA, 82, pp. 2583-2587",,,,00426822,,,"8291230","English","Virology",Article,"Final",,Scopus,2-s2.0-0028227851
"Callebaut P., Pensaert M., Enjuanes L.","6603634162;55905425400;7006565392;","Construction of a recombinant adenovirus for the expression of the glycoprotein S antigen of porcine respiratory coronavirus",1994,"Advances in Experimental Medicine and Biology","342",,,"469","470",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028328625&partnerID=40&md5=ce2e20413648c1ef2c57f84a58b55a1a","Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium","Callebaut, P., Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium; Pensaert, M., Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium; Enjuanes, L., Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium",[No abstract available],,"virus vector; vitronectin; antigen expression; conference paper; Coronavirus; gene sequence; priority journal; virus gene; virus recombinant; Adenoviruses, Human; Animal; Antibodies, Viral; Antigens, Viral; Coronavirus Infections; Genetic Vectors; Membrane Glycoproteins; Respiratory Tract Infections; Support, Non-U.S. Gov't; Swine; Swine Diseases; Tonsillitis; Vaccination; Vaccines, Synthetic; Viral Envelope Proteins; Viral Vaccines; Adenoviridae; Coronavirus; Porcine respiratory coronavirus; Suidae",,"Callebaut, P.; Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium",,,00652598,,AEMBA,"8209769","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028328625
"Smerdou C., Torres J.M., Sanchez C.M., Sune C., Anton I.M., Medina M., Castilla J., Graham F.L., Enjuanes L.","6602856664;35516513600;57193985365;6701660310;57198264385;57214510018;8851950500;35821642700;7006565392;","Induction of an immune response to transmissible gastroenteritis coronavirus using vectors with enteric tropism",1994,"Advances in Experimental Medicine and Biology","342",,,"455","462",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028266967&partnerID=40&md5=c5371351e6677c6bdb98fe6c311fba04","Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain","Smerdou, C., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Torres, J.M., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Sanchez, C.M., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Sune, C., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Anton, I.M., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Medina, M., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Castilla, J., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Graham, F.L., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Enjuanes, L., Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain",[No abstract available],,"virus vector; animal cell; antibody production; conference paper; Coronavirus; immunogenicity; intestine lymphatic tissue; molecular cloning; nonhuman; priority journal; virus neutralization; Adenoviruses, Human; Amino Acid Sequence; Animal; Antibodies, Viral; Antigens, Viral; Cloning, Molecular; Coronavirus Infections; Epitopes; Genetic Vectors; Hamsters; Intestines; Membrane Glycoproteins; Molecular Sequence Data; Organ Specificity; Peyer's Patches; Recombinant Fusion Proteins; Salmonella typhimurium; Support, Non-U.S. Gov't; Transmissible gastroenteritis virus; Vaccination; Vaccines, Synthetic; Viral Envelope Proteins; Viral Vaccines; Animalia; Coronavirus",,"Smerdou, C.; Centro Nacional de Biotecnologia, CSIC - Universidad Autonoma, Canto Blanco, Madrid 28049, Spain",,,00652598,,AEMBA,"7516110","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028266967
"Masters P.S., Koetzner C.A., Peng D., Parker M.M., Ricard C.S., Sturman L.S.","7006234572;6602982748;7202530662;7403672668;7004706818;7003697107;","Site-directed mutagenesis of the genome of mouse hepatitis virus by targeted RNA recombination",1994,"Advances in Experimental Medicine and Biology","342",,,"143","148",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028330814&partnerID=40&md5=dff7f747620e0d2aa9a879562bc61aed","Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States","Masters, P.S., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States; Koetzner, C.A., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States; Peng, D., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States; Parker, M.M., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States; Ricard, C.S., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States; Sturman, L.S., Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States","We have genetically characterized a nucleocapsid (N) protein mutant of the coronavirus mouse hepatitis virus (MHV). This mutant, designated Alb4, is both temperature-sensitive and thermolabile, and its N protein is smaller than wild-type N. Sequence analysis of the Alb4 N gene revealed that it contains an internal deletion of 87 nucleotides, producing an in-frame deletion of 29 amino acids. All of these properties of Alb4 made it ideal for use as a recipient in a targeted RNA recombination experiment in which the deletion in Alb4 was repaired by recombination with synthetic RNA7, the smallest MHV subgenomic mRNA. Progeny from a cotransfection of Alb4 genomic RNA and synthetic RNA7 were selected for thermal stability. PCR analysis of candidate recombinants showed that they had regained the material that is deleted in the Alb4 mutant. They also had acquired a five nucleotide insertion in the 3' untranslated region, which had been incorporated into the synthetic RNA7 as a molecular tag. The presence of the tag was directly verified, as well, by sequencing the genomic RNA of purified recombinant viruses. This provided a clear genetic proof that the Alb4 phenotype was due to the observed deletion in the N gene. In addition, these results demonstrated that it is possible to obtain stable, independently replicating progeny from recombination between coronaviral genomic RNA and a tailored, synthetic RNA species. To date, we have constructed three additional mutants by this procedure. For two of these, a second-site point mutation that reverts the Alb4 phenotype has been transduced into a wild type background, which does not contain the Alb4 deletion. In the third, a portion of the region deleted in Alb4 has been replaced by its counterpart from the N protein of bovine coronavirus (BCV).",,"recombinant RNA; unclassified drug; animal cell; conference paper; mouse; Murine hepatitis coronavirus; nonhuman; point mutation; polymerase chain reaction; priority journal; progeny; rna transfection; site directed mutagenesis; temperature sensitive mutant; thermostability; viral genetics; virus genome; virus mutant; virus mutation; virus recombination; Amino Acid Sequence; Capsid; Genes, Structural, Viral; Genome, Viral; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Point Mutation; Polymerase Chain Reaction; Recombination, Genetic; RNA, Viral; Support, U.S. Gov't, P.H.S.; Viral Core Proteins; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Murinae; Murine hepatitis virus",,"Masters, P.S.; Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-0509, United States",,,00652598,,AEMBA,"8209721","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028330814
"Jeong Y.S., Makino S.","57198837031;7403067550;","Evidence for coronavirus discontinuous transcription",1994,"Journal of Virology","68","4",,"2615","2623",,28,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0039547024&partnerID=40&md5=dfab1ac586cf410b2b93cadb2b6aa7cb","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Microbiology, University of Texas at Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States","Jeong, Y.S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Microbiology, University of Texas at Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States","Coronavirus subgenomic mRNA possesses a 5'-end leader sequence which is derived from the 5' end of genomic RNA and is linked to the mRNA body sequence. This study examined whether coronavirus transcription involves a discontinuous transcription step; the possibility that a leader sequence from mouse hepatitis virus (MHV) genomic RNA could be used for MHV subgenomic defective interfering (DI) RNA transcription was examined. This was tested by using helper viruses and DI RNAs that were easily distinguishable. MHV JHM variant JHM(2), which synthesizes a subgenomic mRNA encoding the HE gene, and variant JHM(3-9), which does not synthesize this mRNA, were used. An MHV DI RNA, DI(J3-9), was constructed to contain a JHM(3-9)-derived leader sequence and an inserted intergenic region derived from the region preceding the MHV JHM HE gene. DI(J3-9) replicated efficiently in JHM(2)- or JHM(3-9)-infected cells, whereas synthesis of subgenomic DI RNAs was observed only in JHM(2)- infected cells. Sequence analyses demonstrated that the 5' regions of both helper virus genomic RNAs and genomic DI RNAs maintained their original sequences in DI RNA-replicating cells, indicating that the genomic leader sequences derived from JHM(2) functioned for subgenomic DI RNA transcription. Replication and transcription of DI(J3-9) were observed in cells infected with an MHV A59 strain whose leader sequence was similar to that of JHM(2), except for one nucleotide substitution within the leader sequence. The 5' region of the helper virus genomic RNA and that of the DI RNA were the same as their original structures in virus-infected cells, and the leader sequence of DI(J3-9) subgenomic DI RNA contained the MHV A59-derived leader sequence. The leader sequence of subgenomic DI RNA was derived from that of helper virus; therefore, the genomic leader sequence had a trans-acting property indicative of a discontinuous step in coronavirus transcription.",,"complementary dna; virus rna; animal cell; article; coronavirus; dna replication; genome; mouse; nonhuman; northern blotting; nucleotide sequence; plasmid; polymerase chain reaction; priority journal; rna synthesis; viral genetics; virus transcription; Animal; Base Sequence; Blotting, Northern; Defective Viruses; Helper Viruses; Mice; Molecular Sequence Data; Murine hepatitis virus; Plasmids; Polymerase Chain Reaction; Regulatory Sequences, Nucleic Acid; Sequence Analysis, RNA; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Transfection",,"Makino, S.; Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"8139040","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0039547024
"Afzelius B.A.","7005020315;","Ultrastructure of human nasal epithelium during an episode of coronavirus infection",1994,"Virchows Archiv","424","3",,"295","300",,20,"10.1007/BF00194614","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028242798&doi=10.1007%2fBF00194614&partnerID=40&md5=d3008108fcf80f9917bad3ed1b5954ba","Department of Ultrastructure Research, Stockholm University, Biology Building E4, Stockholm, S-10691, Sweden","Afzelius, B.A., Department of Ultrastructure Research, Stockholm University, Biology Building E4, Stockholm, S-10691, Sweden","The nasal epithelium from a young girl was examined by electron microscopy and found to be infected by coronavirus. Virions are seen within and outside the ciliated cells, but not outside or within the goblet cells or other cells of the nasal mucosa. Some virions are located near the microvilli, others in pockets in the apical cell membrane. The cytoplasm contains many small vesicles with a single virion, large apical vesicles containing hundreds of virions, and lysosome-like cytosomes with a moderate number of virions. Some viruslike particles devoid of an electron-dense interior are seen both in the cytosomes and extracellularly. Virus budding was observed in the Golgi apparatus but nowhere else in the cell. The ciliated cells seem not to be destroyed by the viruses, although in many cases the cilia are withdrawn into the cell body. The loss of cilia is likely to cause rhinorrhoea. © 1994 Springer-Verlag.","Coronavirus; Nasal cilia; Nasal epithelium; Virus budding","article; case report; cell membrane; cell ultrastructure; cell vacuole; ciliated epithelium; coronavirus; cytoplasm; electron microscopy; female; goblet cell; golgi complex; human; human tissue; microvillus; nose mucosa; preschool child; priority journal; rhinorrhea; virion; virus infection; virus particle; Case Report; Child, Preschool; Cilia; Coronaviridae Infections; Epithelium; Female; Human; Nasal Cavity; Nose Diseases","Afzelius, B.A., The immotile-cilia syndrome and other ciliary diseases (1979) Int Rev Exp Pathol, 19, pp. 1-43; Afzelius, B.A., Glycocalyx and glycocalyceal bodies in the respiratory epithelium of nose and bronchi (1984) Ultrastruct Pathol, 7, pp. 1-8; Becker, W.B., McIntosh, K., Dees, J.H., Chanock, R.M., Morphogenesis of avian infectious bronchitis virus and a related human virus (strain 229 E) (1967) J Virol, 1, pp. 1019-1027; Beesley, J.E., Hitchcock, L.M., The ultrastructure of feline infectious peritonitis virus in feline embryonic lung cells (1982) J Gen Virol, 59, pp. 23-28; Blaskovic, P., Rhodes, A.J., Doane, F.W., Labzoffsky, N.A., Infection of chick embryo tracheal organ cultures with influenza A2 (Hong-Kong) virus (1972) Arch Ges Virusforsch, 38, pp. 250-268; Carson, J.L., Collier, A.M., Hu, D.C.S., Acquired ciliary defects in nasal epithelium of children with acute viral upper respiratory infections (1985) N Engl J Med, 312, pp. 463-468; Chasey, J.L., Alexander, D.J., Morphogenesis of avian infectious bronchitis virus in primary chick kidney cells (1976) Arch Virol, 52, pp. 101-111; Cornille, F.J., Lauweryns, J.M., Corbeel, L., Atypical bronchial cilia in children with recurrent respiratory tract infections — a comparative ultrastructural study (1984) Pathology - Research and Practice, 178, pp. 595-604; David-Ferreira, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) J Cell Biol, 24, pp. 57-78; Dourmashkin, R.R., Tyrrell, D.A.J., Attachment of two myxoviruses to ciliated epithelial cells (1970) J Gen Virol, 9, pp. 77-88; Everman, J.F., Heeney, J.L., McKeirnan, A.J., O'Brien, S.J.O., Comparative features of a coronavirus isolated from a cheetah with feline infectious peritonitis (1989) Virus Research, 13, pp. 15-28; Giorgi, P.L., Oggiano, N., Braga, P.C., Catassi, C., Gabrielli, O., Goppa, G.V., Kantar, A., Cilia in children with recurrent upper respiratory tract infections: ultrastructural observations (1992) Pediatr Pulmonol, 14, pp. 201-205; Gwaltney, J.M., Virology and immunology of the common cold (1985) Rhinology, 23, pp. 265-271; Hae, D., Kindig, D., Mann, J., Growth and intracellular development of a new respiratory virus (1967) J Virol, 1, pp. 810-816; Hoorn, B., Tyrrell, D.A.J., Organ cultures in virology (1969) Prog Med Virol, 11, pp. 408-450; Konradova, V., Vávrová, V., Hlousvová, Z., Copová, M., Tománek, A., Houstek, J., Ultrastructure of bronchial epithelium in children with chronic and recurrent respiratory diseases (1982) Eur J Respir Dis, 63, pp. 516-525; Larson, H.E., Reed, S.E., Tyrrell, D.A.J., Isolation of rhinovirus and coronavirus from 38 colds in adults (1980) J Med Virol, 5, pp. 221-229; Lungarella, G., Fonzi, L., Ermini, G., Abnormalities of bronchial cilia in patients with chronic bronchitis. An ultrastructural and quantitative analysis (1983) Lung, 161, pp. 147-156; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Chanok, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc Natl Acad Sci USA, 57, pp. 933-940; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, M.A., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Oshiro, L.S., Schieble, J.H., Lennette, E.H., Electron microscopic studies of coronavirus (1971) J Gen Virol, 12, pp. 161-168; Ramphal, R., Fischlscheiger, W., Shands, J.W., Small, P.A., Murine influenzal tracheitis: a model for the study of influenza and tracheal epithelial repair (1979) Am Rev Respir Dis, 120, pp. 1313-1324; Rautiainen, M., Kiukaanniemi, H., Nuutinen, J., Collan, Y., Ultrastructural changes in human nasal cilia caused by the common cold and recovery of ciliated epithelium (1992) Ann Otol Rhinol Laryngol, 101, pp. 982-987; Rutland, J., Cole, P.J., Non-invasive sampling of nasal cilia for the measurement of beat frequency and study of ultrastructure (1980) Lancet, 2, pp. 564-565; Stott, E.J., Garwes, D.J., Rhinoviruses adenoviruses and coronaviruses: Their role in respiratory disease (1990) Principles in bacteriology, virology, and immunity, vol 4, pp. 243-272. , W.W.C., Topley, G.S., Wilsons, Arnold, London; Takeuchi, A., Binn, L.N., Jervis, H.R., Keenan, K.P., Hildebrandt, P.K., Valas, R.B., Bland, F.F., Electron microscope study of experimental enteric infection in neonatal dogs with a canine coronavirus (1976) Lab Invest, 34, pp. 539-549; Turner, R.B., Hendley, J.O., Gwaltney, J.M., Shedding of infected ciliated epithelial cells in rhinovirus colds (1982) J Infect Dis, 145, pp. 849-853; Winther, B., Brofeldt, S., Christensen, B., Mygind, N., Light and scanning electron microscopy of nasal biopsy material from patients with naturally acquired colds (1984) Acta Otolaryngol (Stockh), 97, pp. 309-318","Afzelius, B.A.; Department of Ultrastructure Research, Stockholm University, Biology Building E4, Stockholm, S-10691, Sweden",,"Springer-Verlag",09456317,,VARCE,"8186894","English","Vichows Archiv A Pathol Anat",Article,"Final",Open Access,Scopus,2-s2.0-0028242798
"Vancott J.L., Brim T.A., Lunney J.K., Saif L.J.","6603878315;6602281848;7005634527;7102226747;","Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge",1994,"Journal of Immunology","152","8",,"3980","3990",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028206508&partnerID=40&md5=66cd6f42be87cb3f5fbb861b9e888629","Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; U.S. Department of Agriculture, Helminthic Diseases Laboratory, Agricultural Research Service, Beltsville, MD 20705, United States; Department of Microbiology, Immunobiology Vaccine Center, Univ. Alabama Birmingham Med. Ctr., 845 19th Street South, Birmingham, AL 35294-2170, United States; Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States","Vancott, J.L., Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Department of Microbiology, Immunobiology Vaccine Center, Univ. Alabama Birmingham Med. Ctr., 845 19th Street South, Birmingham, AL 35294-2170, United States; Brim, T.A., Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Lunney, J.K., U.S. Department of Agriculture, Helminthic Diseases Laboratory, Agricultural Research Service, Beltsville, MD 20705, United States; Saif, L.J., Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Ohio Agric. R. and D. Center, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States","Two antigenically related porcine coronaviruses, transmissible gastroenteritis virus (TGEV) which infects primarily the intestinal tract and causes severe diarrhea, and porcine respiratory coronavirus (PRCV) which infects the respiratory tract and causes subclinical or mild respiratory infections, presented a unique opportunity to study the interrelationship of gut-(GALT) and bronchus-associated lymphoid tissues (BALT) and their contribution to protective immunity against TGEV infection. Pigs were inoculated oral-nasally with TGEV or with PRCV at eleven days of age and challenged 24 days later with TGEV. All pigs initially given TGEV developed diarrhea and were completely protected against disease upon challenge. In contrast, pigs given PRCV had no clinical disease and shed virus in nasal secretions only; after challenge, 5 of 12 pigs developed diarrhea. Virus- specific IgG and IgA Ab-secreting cells (ASC) were enumerated by ELISPOT in the mesenteric and bronchial lymph nodes, spleens, and gut lamina propria at challenge and various post challenge days. Before challenge, in pigs exposed to TGEV, IgA-ASC in the duodenum and jejunum constituted the major ASC response. Conversely, PRCV-exposed pigs had mainly IgG-ASC in bronchial lymph nodes, with low ASC responses in the gut. After challenge, numbers of IgG- ASC increased rapidly in the gut lamina propria and mesenteric lymph nodes of only PRCV-primed pigs. Our results suggest that virus-specific IgG-ASC precursors derived in BALT of PRCV-primed pigs may migrate to the gut in response to TGEV challenge and contribute to the partial protection observed. The presence of IgA-ASC in the gut lamina propria of TGEV-primed pigs at the time of challenge correlated with complete protection against TGEV challenge. Thus a dichotomy exists in the BALT and GALT ASC responses; immunization via BALT induced a systemic type of response (IgG-ASC) and provided imperfect protection against an enteric pathogen, whereas immunization via GALT induced IgA-ASC and provided complete protection.",,"immunoglobulin a; immunoglobulin m; animal cell; animal experiment; animal model; antibody producing cell; article; coronavirus; diarrhea; immunization; immunoglobulin production; intestine lymphatic tissue; nonhuman; priority journal; provocation test; virus immunity; virus infection; Animals; Antibodies, Viral; Antibody-Producing Cells; Coronavirus; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Intestinal Mucosa; Lymphoid Tissue; Neutralization Tests; Swine; Transmissible gastroenteritis virus","Binns, R.M., Pabst, R., Lymphoid cell migration and homing in the young pig: Alternative immune mechanisms in action (1988) Migration and Homing of Lymphoid Cells, 2, p. 137. , A. J. Husband, ed. CRC Press, Inc., Boca Raton; VanCott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, p. 3990; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., p. 362. , A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor, eds. Iowa State University Press, Ames; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Quarterly, 8, p. 257; Hill, H., Biwer, J., Woods, R., Wesley, R., Porcine respiratory coronavirus isolated from two U. S. swine herds (1990) Proc. Am. Assoc. Swine Practitioners, 21, p. 333; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diag. Invest., 2, p. 312; Cox, E., Pensaert, M., Hooyberghs, J., Van Deun, K., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Coronaviruses and Their Diseases, p. 429. , D. Cavanagh and T. D. K. Brown eds. Plenum press, New York; Callebaut, P., Correa, I., Pensaert, M., Jimenez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J. Gen. Virol., 69, p. 1725; Garwes, D.J., Stewart, F., Cartwright, S.F., Brown, I., Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet. Rec., 122, p. 86; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am. J. Vet. Res., 53, p. 1253; Welch, S.K.W., Saif, L.J., Ram, S., Cell-mediated immune responses of suckling pigs inoculated with attenuated or virulent transmissible gastroenteritis virus (1988) Am. J. Vet. Res., 49, p. 1228; Furuuchi, S., Shimizu, Y., Kumagai, T., Multiplication of low and high cell culture passaged strains of transmissible gastroenteritis virus in organs of newborn piglets (1979) Vet. Microbiol, 3, p. 169; Callebaut, P., Cox, E., Pensaert, M., Van Deun, K., Induction of milk IgA antibodies by porcine respiratory coronavirus infection (1990) Coronaviruses and Their Diseases, p. 421. , D. Cavanagh and T. D. K. Brown, eds. Plenum Press, New York; Bernard, S., Bottreau, E., Aynaud, J.M., Have, P., Szymansky, J., Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis virus (1989) Vet. Microbiol., 21, p. 1; Paton, D.J., Brown, I.H., Sows infected in pregnancy with porcine respiratory coronavirus show no evidence of protecting their suckling piglets against transmissible gastroenteritis (1990) Vet. Res. Commun., 14, p. 329; Wesley, R.D., Woods, R.D., Active and passive immunity to transmissible gastroenteritis virus induced by porcine respiratory coronavirus (1992) Proceedings of the 12th Congress of the International Pig and Veterinary Society, p. 95. , The Hague, The Netherlands; Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, p. 267; Sminia, M.Z., Structure and function of bronchus-associated lymphoid tissue (BALT) (1989) Critical Reviews in Immunology, 9, p. 118. , CRC Press, Inc., Boca Raton; Bohl, E.H., Kumagai, T., The use of cell cultures for the study of TGE virus of swine (1965) Proc. US Livestock Sanitary Assoc., 69, p. 343; Welch, S.K.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity with virulent and attenuated virus (1988) Arch. Virol., 101, p. 221; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am. J. Vet. Res., 38, p. 13; Bohl, E.H., Gupta, R.K.P., Olquin, M.V.F., Saif, L.J., Antibody responses in serum, colostrum, and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect. Immun., 6, p. 289; Van Der Heijden, P.J., Stok, W., Improved procedure for the isolation of functionally active Iymphoid cells from the murine intestine (1987) J. Immunol. Methods, 103, p. 161; Wilson, A.D., Stokes, C.R., Bourne, F.J., Responses of intraepithelial lymphocytes to T-cell mitogens: A comparison between murine and porcine responses (1986) Immunology, 58, p. 621; Paul, P.S., Mengeling, W.L., Malstrom, C.E., Van Deusen, R.A., Production and characterization of monoclonal antibodies to porcine immunoglobulin γ, α, and light chains (1989) Am. J. Vet. 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CRC Press, Inc., Boco Raton; McGhee, J.R., Mestecky, J.M., Dertzbaugh, M.T., Eldridge, J.H., Hirasawa, M., Kiyono, H., The mucosal immune system: Fundamental concepts to vaccine development (1992) Vaccine, 10, p. 75; Merchant, A.A., Groene, W.S., Cheng, E.H., Shaw, R.D., Murine intestinal antibody response to heterologous rotavirus infection (1991) J. Clin. Microbiol., 29, p. 1693; Morgan, K.L., Hussein, A.M., Newby, T.J., Bourne, F.J., Quantification and origin of the immunoglobulins in porcine respiratory tract secretions (1980) Immunology, 41, p. 729; Bradley, P.A., Brown, P.J., Bourne, F.J., The respiratory tract immune system of the pig (1976) Vet. Pathol., 31, p. 81; Messier, S., Ross, R.F., Paul, P.S., Humoral and cellular immune responses of pigs inoculated with Mycoplasma hyopneumoniae (1990) Am. J. Vet. Res., 51, p. 52; Pierce, N.F., Cray, W.C., Cellular dissemination of priming for a mucosal immune response to cholera toxin in rats (1981) J. 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Med., 148, p. 1146; Mazanec, M.B., Kaetzel, C.S., Lamm, M.E., Fletcher, D., Intracellular neutralization of virus by immunoglobulin A antibodies (1992) Proc. Natl. Acad. Sci. USA, 89, p. 6901; Brandtzaeg, P., Humoral immune response patterns of human mucosae: Induction and relation to bacterial respiratory tract infections (1992) J. Infect. Dis., 165, pp. S167; Nagura, H., Mucosal defense mechanism in health and disease: Role of the mucosal immune system (1992) Acta Pathol. Jpn., 42, p. 387; Brim, T.A., VanCott, J.L., Lunney, J.K., Saif, L.J., Lymphocyte proliferative responses of pigs inoculated with transmissible gastroenteritis virus or porcine respiratory coronavirus (1994) Am. J. Vet. Res., , In press; McQueen, C.E., Boedeker, E.C., Le, M., Hamada, Y., Brown, W.R., Mucosal immune response to RDEC-1 infection: Study of lamina propria antibody-producing cells and biliary antibody (1992) Infect. Immun., 60, p. 206; Halbur, P., Paul, P., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J. Vet. Diag. Invest., 5, p. 184; Weisz-Carrington, P.W., Grimes, S.R., Lamm, M.E., Gut-associated lymphoid tissue as source of an IgA immune response in respiratory tissues after oral immunization and intrabronchial challenge (1987) Cell. Immunol., 106, p. 132; Scicchitano, R., Husband, A.J., Clancy, R.L., Contribution of gut immunization to the local immune response in the respiratory tract (1984) Immunology, 53, p. 375; Chen, K.-S., Active synthesis of hemagglutinin-specific immunoglobulin a by lung cells of mice that were immunized intragastrically with inactivated influenza virus vaccine (1987) J. Virol., 61, p. 2150","VanCott, J.L.; Department of Microbiology, Immunology Vaccine Center, University of Alabama Medical Center, 845 19th Street South, Birmingham, AL 35294-2170, United States",,,00221767,,JOIMA,"8144965","English","J. IMMUNOL.",Article,"Final",,Scopus,2-s2.0-0028206508
"Sizun J., Soupre D., Legrand M., Giroux J., Rubio S., Chastel C., Alix D., de Parscau L.","35605340000;6602842875;7102317918;17934302900;7006260573;57197376300;7006494821;7006825420;","Coronavirus infection in 19 infants admitted to intensive care. A retrospective study using immunofluorescence [Rôle pathogéne des coronavirus en réanimation pédiatrique: analyse rétrospective de 19 prélèvements positifs en immunofluorescence indirecte]",1994,"Archives de pediatrie","1","5",,"477","480",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028432970&partnerID=40&md5=38ac549b951e58a53f7dadfa52f610f0","Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; Laboratoire de microbiologie, CHU, 29609 Brest, France","Sizun, J., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; Soupre, D., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; Legrand, M., Laboratoire de microbiologie, CHU, 29609 Brest, France; Giroux, J., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; Rubio, S., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; Chastel, C., Laboratoire de microbiologie, CHU, 29609 Brest, France; Alix, D., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France; de Parscau, L., Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France","Background. - Coronaviruses (CV) are ARN-containing agents that are responsible for mild upper respiratory tract infections in adults and children. Their pathogenicity in neonates is not wellknow. Population and methods. - Eighty five samples of tracheal or nasopharyngeal secretions were obtained from January to October 1991 from 53 children (29 less than 1 month of age; 19 from 1 month to 1 year; five older than 1 year). They were examined for respiratory syncytial virus, adenovirus, myxovirus influenza and parainfluenza and coronavirus by immunofluorescence (IF). Results. - Nineteen samples from nine newborns and three infants were positive for coronavirus. The mean birth weight of the nine neonates was 2100 ± 840 g; their mean gestational age was 34 ± 5 weeks and their mean age at diagnosis was 21 ± 9 days. Apnea and bradycardia were the main symptoms in this group. Blood C-reactive protein was not elevated and blood cultures were sterile. One infant was admitted for near-miss; the two others were admitted at birth because they suffered from chronic lung disease (pulmonary hypoplasia and bronchopulmonary dysplasia). An acute episode of pulmonary deterioration occurred at the time of coronavirus infection. Both died one at 4 months and the other at 10 months. Conclusion. - Coronaviruses seem to be responsible for respiratory tract infections in hospitalized neonates and chronically ventilated infants. © 1994.","coronavirus infections / apnea / bronchopulmonary dysplasia / infant; newborn","apnea; article; bradycardia; Coronavirus; fluorescent antibody technique; heterozygote; human; infant; intensive care; microbiology; newborn; pathogenicity; retrospective study; virus infection; coronavirus; major clinical study; newborn intensive care; respiratory tract infection; virus infection; Apnea; Bradycardia; Carrier State; Coronavirus; Coronavirus Infections; English Abstract; Fluorescent Antibody Technique; Human; Infant; Infant, Newborn; Intensive Care Units, Pediatric; Retrospective Studies",,"Sizun, J.; Service de réanimation pédiatrique et néonatologie, CHU, 29609 Brest, France",,,0929693X,,APEDE,"7951832","French","Arch. Pediatr.",Article,"Final",,Scopus,2-s2.0-0028432970
"Pasick J.M.M., Kalicharran K., Dales S.","6701444069;6602516345;7005597434;","Distribution and trafficking of JHM coronavirus structural proteins and virions in primary neurons and the OBL-21 neuronal cell line",1994,"Journal of Virology","68","5",,"2915","2928",,35,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028230836&partnerID=40&md5=b27570861bee3a32338a1de8b845c798","Cytobiology Group, Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada; Dept. of Microbiology and Immunology, Health Science Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada; Agriculture Canada, Sackville, NB E0A 3C0, Canada","Pasick, J.M.M., Cytobiology Group, Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada, Agriculture Canada, Sackville, NB E0A 3C0, Canada; Kalicharran, K., Cytobiology Group, Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada; Dales, S., Cytobiology Group, Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada, Dept. of Microbiology and Immunology, Health Science Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada","The neurotropic murine coronavirus JHM is capable of inducing various forms of neurologic diseases, including demyelination. Neurons have been shown to act as a repository site at the early stages of the disease process (O. Sorensen and S. Dales, J. Virol. 56:434-438, 1985). JHM virus (JHMV) replication and trafficking of viral proteins and virions in cultured rat hippocampal neurons and a neuronal cell line, OBL-21, were examined, with an emphasis placed on the role of the microtubular network. We show here that JHMV spread within the central nervous system occurs transneuronally and that virus protein trafficking was dependent upon microtubules. Viral trafficking occurred asymmetrically, involving both the somatodendritic and the axonal domains. Thus coronavirus can be disseminated from neurons at either the basolateral or the apical domains. A specific interaction between antibodies derived against the microtubule-associated protein tau and JHMV nucleocapsid protein (N) was observed, which can presumably be explained by an overall amino acid similarity of 44% and an identity of 20% between proteins N and tau, with optimal alignment at the microtubule binding domain of tau. Collectively, our data suggest an important role of the microtubule network in viral protein trafficking and distribution. They also draw attention to protein sequence mimicry of a cell component by this coronavirus as one strategy for making use of the host's functions on behalf of the virus.",,"capsid protein; guanine nucleotide binding protein; structural protein; tau protein; virus protein; animal cell; article; cellular distribution; controlled study; coronavirus; embryo; hippocampus; intracellular transport; microtubule; nerve cell culture; nonhuman; priority journal; protein localization; rat; virus assembly; virus cell interaction; virus nucleocapsid; Amino Acid Sequence; Animals; Astrocytes; Biological Transport; Capsid; Cell Compartmentation; Fluorescent Antibody Technique; Hippocampus; Microscopy, Electron; Microtubules; Molecular Sequence Data; Murine hepatitis virus; Neurites; Neurons; Rats; Sequence Homology, Amino Acid; tau Proteins; Vinblastine; Viral Core Proteins; Viral Proteins; Virion; Virus Replication","Banker, G., Goslin, K., Rat hippocampal neurons in low density culture (1991) Culturing Nerve Cells, pp. 251-281. , G. 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Virol., 70, pp. 2075-2085; Tyler, K.L., McPhee, D.A., Fields, B.N., Distinct pathways of viral spread in the host determined by reovirus S1 gene segment (1986) Science, 233, pp. 770-774; Ugolini, G., Kuypers, H.G.J.M., Strick, P.L., Transneuronal transfer of herpes simplex virus from peripheral nerves to cortex and brainstem (1989) Science, 243, pp. 89-91; Vallee, R.B., Bloom, G.S., Mechanisms of fast and slow axonal transport (1991) Annu. Rev. Neurosci., 14, pp. 59-92; Walsh, E., Ueda, Y., Nakanishi, H., Yoshida, K., Neuronal survival and neurite extension supported by astrocytes co-cultured in trans-wells (1992) Neurosci. Lett., 138, pp. 103-106; Wang, F.-I., Hinton, D.R., Gilmore, W., Trousdale, M.D., Flemming, J.O., Sequential infection of glial cells by the murine hepatitis virus JHM strain (MHV-4) leads to a characteristic distribution of demyelination (1992) Lab. Invest., 66, pp. 744-754; Wecelewicz, K., Kristensson, K., Orvell, C., Segregation of viral structural proteins in cultured neurons of rat spinal ganglia and cord (1990) Neuropathol. Appl. Neurobiol., 16, pp. 357-364","Dales, S.; Microbiology/Immunology Department, Health Science Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada",,,0022538X,,JOVIA,"8151762","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028230836
"Goncharuk E.I., Shevtsova Z.V., Krylova R.I., Rumel' N.B., Stetsenko V.I.","7005858472;7004158851;7003925235;6603552261;7003491543;","The experimental coronavirus infection of monkeys [Eksperimental'naia koronavirusnaia infektsiia obez'ian.]",1994,"Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993)","56","3",,"65","71",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028434608&partnerID=40&md5=69c6039c8dafed678993c6fc4d4db6fd",,"Goncharuk, E.I.; Shevtsova, Z.V.; Krylova, R.I.; Rumel', N.B.; Stetsenko, V.I.","The coronavirus (CV) infection has been reproduced on monkeys (Macaca mulatta) for the first time. The strain CVRM 281, obtained from rhesus monkey who died of the spontaneous CV injection, has been used for the infection. The experimental CV infection has a chronic current with periodical relapses and virus persistence. Gastrointestinal tract (enterocolitis) and respiratory tract (pneumonia) are damaged exhibiting characteristic histological lesions. The monkey model of the CV injection can be used to solve obscure questions of human one.",,"virus antibody; animal; article; blood; Coronavirus; disease model; feces; immunology; isolation and purification; Macaca; male; microbiology; monkey disease; pathogenicity; pathology; time; virology; virus culture; virus infection; Animal; Antibodies, Viral; Coronavirus; Coronavirus Infections; Disease Models, Animal; English Abstract; Feces; Macaca mulatta; Male; Monkey Diseases; Serial Passage; Time Factors",,"Goncharuk, E.I.",,,,,,"7952229","Russian","Mikrobiol Z",Article,"Final",,Scopus,2-s2.0-0028434608
"Castro R.F., Evans G.D., Jaszewski A., Perlman S.","7202082372;7403735309;16156813900;7102708317;","Coronavirus-induced demyelination occurs in the presence of virus-specific cytotoxic T cells",1994,"Virology","200","2", 71237,"733","743",,40,"10.1006/viro.1994.1237","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028297362&doi=10.1006%2fviro.1994.1237&partnerID=40&md5=24ed53c37cb86f4b5293145202303309","Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Castro, R.F., Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Evans, G.D., Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Jaszewski, A., Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","C57Bl/6, but not BALB/c, mice infected with mouse hepatitis virus strain JHM (MHV-JHM) develop a late onset, symptomatic demyelinating encephalomyelitis. In this report, we characterized anti-viral cytotoxic T cells in the central nervous system and spleen during the acute and chronic stages of the MHV infection. The data show that C57Bl/6 mice display a cytotoxic T cell (CTL) response to the surface (S) glycoprotein and this response can be demonstrated in lymphocytes isolated from the brains and spinal cords of mice both acutely and persistently infected with MHV-JHM. Thus, the anti-S CTL activity present in the central nervous system of chronically infected animals is not sufficient to prevent the demyelinating process. BALB/c mice have been shown previously to mount a CTL response against the nucleocapsid (N) protein (Stohlman et al., 1992). Since C57Bl/6 mice do not mount a response to the N protein, the role of the N-specific response in preventing the late onset disease was assessed using B10.A(18R) mice, recombinant in the H-2 locus. These mice contain the d alleles of the D and L loci and exhibit a CTL response against the N protein. However, unlike the BALB/c mice, these animals develop the late onset symptomatic disease. These results suggest that the N-specific response is partially protective against the development of the demyelinating disease, but that additional factors are also likely to be involved. © 1994 Academic Press, Inc.",,,"Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (Strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Bureau, J.-F., Montagutelli, X., Bihl, F., Lefebvre, S., Guenet, J.-U., Brahic, M., Mapping loci influencing the persistence of Theiler's virus in the murine central nervous system (1993) Nature Genet, 5, pp. 87-91; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin (1949) J. Exp. 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Neuroirnmunol, 30, pp. 31-41; Watanabe, R., Wege, H., Ter Meulen, V., Comparative analysis of coronavirus JHM-induced demyelinating encephalomyelitis in Lewis and Brown Norway rats. Lab (1987) Invest, 57, pp. 375-384; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus). Arch (1973) Neurol, 28, pp. 298-303; Welsh, C.J.R., Tonks, P., Nash, A.A., Blakemore, W.F., The effect of L3T4 T cells depletion on the pathogenesis of Theiler's murine encephalomyelitis virus infection in CBA mice (1987) J. Gen. Virol, 68, pp. 1659-1661; Welsh, R.M., Haspel, M.V., Parker, D.C., Holmes, K.V., Natural cytotoxicity against mouse hepatitis virus-infected cells. II. A cytotoxic effector cell with a B lymphocyte phenotype (1986) J. Immunol, 136, pp. 1454-1460; Williamson, J.S., Stohlman, S.A., Effective clearance of mouse hepatitis virus from the central nervous system requires both CD4+ and CD8+ T cells (1990) J. Virol, 64, pp. 4589-4592; Williamson, J.S., Sykes, K.C., Stohlman, S.A., Characterization of brain-infiltrating mononuclear cells during infection with mouse hepatitis virus strain JHM (1991) J. Neuroirnmunol, 32, pp. 199-201; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. Neuroirnmunol, 32, pp. 1-9","Perlman, S.; Department of Pediatrics, University of Iowa, ML207, Iowa City, IA 52242, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028297362
"Van Der Most R.G., De Groot R.J., Spaan W.J.M.","6701702352;7103077066;7007172944;","Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation",1994,"Journal of Virology","68","6",,"3656","3666",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028278092&partnerID=40&md5=663237149cebaca136f5c9c128144bed","Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Department of Virology, Institute of Medical Microbiology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Institute of Virology, Dept. of Infect. Dis. and Immunology, University of Utrecht, 3584 CL Utrecht, Netherlands","Van Der Most, R.G., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; De Groot, R.J., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands, Institute of Virology, Dept. of Infect. Dis. and Immunology, University of Utrecht, 3584 CL Utrecht, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands, Department of Virology, Institute of Medical Microbiology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands","We have used a full-length cDNA clone of a mouse hepatitis virus strain A59 defective interfering (DI) RNA, pMIDI-C, and cassette mutagenesis to study the mechanism of coronavirus subgenomic mRNA synthesis. Promoter sequences closely resembling those of subgenomic mRNAs 3 and 7 were inserted into MIDI-C. Both subgenomic RNA promoters gave rise to the synthesis of a subgenomic DI RNA in virus-infected and DI RNA-transfected cells. From a mutagenic analysis of the promoters we concluded the following. (i) The extent of base pairing between the leader RNA and the intergenic promoter sequence does not control subgenomic RNA abundance. (ii) Promoter recognition does not rely on base pairing only. Presumably, transcription initiation requires recognition of the promoter sequence by the transcriptase. (iii) Fusion of leader and body sequences takes place at multiple-possibly random- sites within the intergenic promoter sequence. A model is presented in which, prior to elongation, the leader RNA is trimmed by a processive 3'→5' nuclease.",,"transcriptase; antigen recognition; article; base pairing; coronavirus; gene insertion; molecular cloning; murine hepatitis coronavirus; mutagenesis; nonhuman; priority journal; promoter region; rna synthesis; transcription initiation; virus transcription; Animals; Base Composition; Base Sequence; Defective Viruses; DNA, Complementary; DNA, Viral; Mice; Models, Genetic; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Insertional; Promoter Regions (Genetics); RNA, Messenger; RNA, Viral; Transcription, Genetic","Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature (London), 308, pp. 751-752; Baker, S.C., Lai, M.M., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) EMBO J., 9, pp. 4173-4179; Baric, R.S., Stohlman, S.A., Razavi, M.K., Lai, M.M., Characterization of leader-related small RNAs in coronavirus-infected cells: Further evidence for leader-primed mechanism of transcription (1985) Virus Res., 3, pp. 19-33; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. 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Virol., 74, pp. 1697-1701; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; SantaLucia, J., Kierzek, R., Turner, D.H., Stabilities of consecutive A · C, C · C, G · G, and U · U mismatches in RNA internal loops: Evidence for stable hydrogen-bonded U · U and C · C+ pairs (1991) Biochemistry, 30, pp. 8242-8251; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. 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USA, 88, pp. 9056-9060; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Sequence relationships between the genome and the intracellular RNA species 1, 3, 6, and 7 of mouse hepatitis virus strain A59 (1982) J. Virol., 42, pp. 432-439; Sugimoto, N., Kierzek, R., Freier, S.M., Turner, D.H., Energetics of internal G · U mismatches in ribooligonucleotide helices (1986) Biochemistry, 25, pp. 5755-5759; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Yokomori, K., Banner, L.R., Lai, M.M., Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic-length template (1992) J. Virol., 66, pp. 4671-4678","Spaan, W.J.M.; Department of Virology, Institute of Medical Microbiology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands",,,0022538X,,JOVIA,"8189503","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028278092
"Nédellec P., Dveksler G.S., Daniels E., Turbide C., Chow B., Basile A.A., Holmes K.V., Beauchemin N.","7004379910;6603790777;7101961843;6603461883;7102826198;7101713440;7201657724;7005461095;","Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses",1994,"Journal of Virology","68","7",,"4525","4537",,95,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028335581&partnerID=40&md5=7f712a8fdd4feb0c658fd712dd8de2e7","McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Medicine, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Anatomy, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Biochemistry, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Oncology, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States","Nédellec, P., McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada, Department of Medicine, McGill University, Montreal, Que. H3G 1Y6, Canada; Dveksler, G.S., Department of Anatomy, McGill University, Montreal, Que. H3G 1Y6, Canada; Daniels, E., Department of Biochemistry, McGill University, Montreal, Que. H3G 1Y6, Canada; Turbide, C., McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada; Chow, B., McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada; Basile, A.A., Department of Anatomy, McGill University, Montreal, Que. H3G 1Y6, Canada; Holmes, K.V., Department of Anatomy, McGill University, Montreal, Que. H3G 1Y6, Canada; Beauchemin, N., McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada, Department of Medicine, McGill University, Montreal, Que. H3G 1Y6, Canada, Department of Oncology, McGill University, Montreal, Que. H3G 1Y6, Canada, Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States","Murine coronaviruses such as mouse hepatitis virus (MHV) infect mouse cells via cellular receptors that are isoforms of biliary glycoprotein (Bgp) of the carcinoembryonic antigen gene family (G. S. Dveksler, C. W. Dieffenbach, C. B. Cardellichio, K. McCuaig, M. N. Pensiero, G.-S. Jiang, N. Beauchemin, and K. V. Holmes, J. Virol. 67:1-8, 1993). The Bgp isoforms are generated through alternative splicing of the mouse Bgp1 gene that has two allelic forms called MHVR (or mmCGM1), expressed in MHV-susceptible mouse strains, and mmCGM2, expressed in SJL/J mice, which are resistant to MHV. We here report the cloning and characterization of a new Bgp-related gene designated Bgp2. The Bgp2 cDNA allowed the prediction of a 271-amino-acid glycoprotein with two immunoglobulin domains, a transmembrane, and a putative cytoplasmic tail. There is considerable divergence in the amino acid sequences of the N-terminal domains of the proteins coded by the Bgp1 gene from that of the Bgp2-encoded protein. RNase protection assays and RNA PCR showed that Bgp2 was expressed in BALB/c kidney, colon, and brain tissue, in SJL/J colon and liver tissue, in BALB/c and CD1 spleen tissue, in C3H macrophages, and in mouse rectal carcinoma CMT-93 cells. When Bgp2- transfected hamster cells were challenged with MHV-A59, MHV-JHM, or MHV-3, the Bgp2-encoded protein served as a functional MHV receptor, although with a lower efficiency than that of the MHVR glycoprotein. The Bgp2-mediated virus infection could not be inhibited by monoclonal antibody CC1 that is specific for the N-terminal domain of MHVR. Although CMT-93 cells express both MHVR and Bgp2, infection with the three strains of MHV was blocked by pretreatment with monoclonal antibody CC1, suggesting that MHVR was the only functional receptor in these cells. Thus, a novel murine Bgp gene has been identified that can be coexpressed in inbred mice with the Bgp1 glycoproteins and that can serve as a receptor for MHV strains when expressed in transfected hamster cells.",,"carcinoembryonic antigen; complementary dna; glycoprotein; messenger rna; monoclonal antibody; virus receptor; amino acid sequence; animal cell; animal tissue; article; cell strain 3t3; cell strain bhk; controlled study; dna sequence; gene expression; molecular cloning; mouse; mouse strain; murine hepatitis coronavirus; nonhuman; polymerase chain reaction; priority journal; tissue specificity; Amino Acid Sequence; Animals; Base Sequence; Carcinoembryonic Antigen; Cells, Cultured; Cloning, Molecular; Coronavirus Infections; Cricetinae; DNA, Complementary; Glycoproteins; Mice; Mice, Inbred Strains; Molecular Sequence Data; Murine hepatitis virus; Receptors, Virus; Sequence Homology, Amino Acid; Tumor Cells, Cultured","Afar, D.E.H., Stanners, C.P., Bell, J.C., Tyrosine phosphorylation of biliary glycoprotein, a cell adhesion molecule related to carcinoembryonic antigen (1992) Biochim. Biophys. Acta, 1134, pp. 46-52; Barnett, T., Kretschmer, A., Austen, D.A., Goebel, S.J., Hart, J.T., Elting, J.J., Kamarck, M.E., Carcinoembryonic antigens: Alternative splicing accounts for multiple mRNAs that code for novel members of the carcinoembryonic antigen family (1989) J. Cell Biol., 108, pp. 267-276; Barnett, T.R., Drake, L., Pickle II, W., Human biliary glycoprotein gene: Characterization of a family of novel alternatively spliced RNAs and their expressed proteins (1993) Mol. Cell. Biol., 13, pp. 1273-1282; Barthold, S.W., Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents. Effects on Biomedical Research, pp. 571-601. , P. N. Bhatt, R. O. Jacoby, H. C. Morse III, and A. E. New (ed.), Academic Press, Inc., Orlando, Fla; Beauchemin, N., Benchimol, S., Cournoyer, D., Fuks, A., Stanners, C.P., Isolation and characterization of full-length functional cDNA clones for human carcinoembryonic antigen (1987) Mol. Cell. Biol., 7, pp. 3221-3230; Beauchemin, N., Turbide, C., Huang, J.Q., Benchimol, S., Jothy, S., Shirota, K., Fuks, A., Stanners, C.P., Studies on the function of carcinoembryonic antigen (1989) The Carcinoembryonic Antigen Gene Family, pp. 49-64. , A. Yachi and J. E. Shively (ed.), Elsevier, Amsterdam; Boyle, J.F., Weismiller, G.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. 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Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elias, P.E., Holmes, K.V., Mouse coronavirus MHV-A59 and blocking anti-receptor monoclonal antibody bind to the N-terminal domain of cellular receptor MHVR (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Feinberg, A.P., Vogelstein, B., A technique for radiolabeling DNA restriction fragment endonuclease fragments to high specific activity (1983) Anal. Biochem., 132, pp. 6-13; Feracci, H., Connoly, T.P., Margolis, R.N., Hubbard, A.L., The establishment of hepatocyte cell surface polarity during fetal liver development (1987) Dev. Biol., 123, pp. 73-84; Hauck, W., Nédellec, P., Turbide, C., Stanners, C.P., Barnett, T.R., Beauchemin, N., Transcriptional Control of the Human Biliary Glycoprotein Gene, a CEA Gene Family Member Down-regulated in Colorectal Carcinomas, , Submitted for publication; Hauck, W., Stanners, C.P., Identification of Multiple Transcription Factors Regulating the Tissue-specific and Differentiation-dependent Expression of the Carcinoembryonic Gene, , Submitted for publication; Huang, J.Q., Turbide, C., Daniels, E., Jothy, S., Beauchemin, N., Spatiotemporal expression of murine carcinoembryonic antigen (CEA) gene family members during mouse embryogenesis (1990) Development, 110, pp. 573-588; Kuroki, M., Arakawa, F., Matsuo, Y., Oikawa, S., Nakazato, H., Matsuoka, Y., Three novel molecular forms of biliary glycoprotein deduced from cDNA clones from a human leukocyte library (1991) Biochem. Biophys. Res. Commun., 176, pp. 578-585; Leusch, H.G., Drzenick, Z., Markos-Pusztai, Z., Wagener, C., Binding of Escherichia coli and Salmonella strains to members of the carcinoembryonic antigen family: Differential binding inhibition by aromatic α-glycosides of mannose (1991) Infect. Immun., 59, pp. 2051-2057; Lin, S.H., Guidotti, G., Cloning and expression of a I cDNA coding for rat liver plasma membrane ecto-ATPase: The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein 1 (1989) J. Biol. Chem., 264, pp. 14408-14414; Margolis, R.N., Taylor, S.I., Seminara, D., Hubbard, A.L., Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain (1985) J. Biol. Chem., 85, pp. 7256-7259; McCuaig, K., Rosenberg, M., Nédellec, P., Turbide, C., Beauchemin, N., Expression of the Bgp gene and characterization of mouse colon biliary glycoprotein isoforms (1993) Gene, 127, pp. 173-183; McCuaig, K., Turbide, C., Beauchemin, N., mmCGM1a: A mouse carcinoembryonic antigen gene family member, generated by alternative splicing, functions as an adhesion molecule (1992) Cell Growth Differ., 3, pp. 165-174; Najjar, S.M., Accili, D., Neubert, P., Jernberg, J., Margolis, R.N., Taylor, S.I., pp120/EctoATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isoforms (1993) J. Biol. 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Chem., 266, pp. 7995-8001; Robbins, J., Robbing, P.F., Kozak, C.A., Callahan, R., The mouse biliary glycoprotein gene (Bgp): Partial nucleotide sequence, expression, and chromosomal assignment (1991) Genomics, 10, pp. 583-587; Rojas, M., Fuks, A., Stanners, C.P., Biliary glycoprotein, a member of the immunoglobulin supergene family, functions in vitro as a Ca2+-dependent intercellular adhesion molecule (1990) Cell Growth Differ., 1, pp. 527-533; Rosenberg, M., Nédellec, P., Jothy, S., Fleiszer, D., Turbide, C., Beauchemin, N., Expression of mouse biliary glycoprotein, a carcinoembryonic antigen-related gene, is downregulated in malignant mouse tissues (1993) Cancer Res., 53, pp. 4938-4945; Rudert, F., Saunders, A.M., Rebstock, S., Thompson, J.A., Zimmermann, W., Characterization of murine carcinoembryonic antigen gene family members (1992) Mamm. Genome, 3, pp. 262-273; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schrewe, H., Thompson, J., Bona, M., Hefta, L.J.F., Maruya, A., Hassauer, M., Shively, J.E., Zimmermann, W., Cloning of the complete gene for carcinoembryonic antigen: Analysis of its promoter indicates a region conveying cell type-specific expression (1990) Mol. Cell. Biol., 10, pp. 2738-2748; Sippel, C.J., Suchy, F.J., Ananthanarayanan, M., Perlmutter, D.H., The rat liver ecto-ATPase is also a canalicular bile acid transport protein (1993) J. Biol. Chem., 268, pp. 2083-2091; Smith, A.L., Cardellichio, C.B., Vinograd, D.F., DeSouza, M.S., Barthold, S.W., Holmes, K.V., Monoclonal antibody to the receptor for murine coronavirus MHV-A59 inhibits virus replication in vivo (1991) J. Infect. Dis., 163, pp. 879-882; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect. Immun., 6, pp. 501-507; Svalander, P.C., Odin, P., Nilsson, B.O., Obrink, B., Expression of CellCAM-105 in the apical surface of rat uterine epithelium is controlled by ovarian steroid hormones (1990) J. Reprod. Fert., 88, pp. 213-221; Thompson, J.A., Grunert, F., Zimmermann, W., Carcinoembryonic antigen gene family: Molecular biology and clinical perspectives (1991) J. Clin. Lab. Invest., 5, pp. 344-366; Turbide, C., Rojas, M., Stanners, C.P., Beauchemin, N., A mouse carcinoembryonic antigen gene family member is a calcium-dependent cell adhesion molecule (1991) J. Biol. Chem., 266, pp. 309-315; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Willcocks, T.C., Craig, I.W., Characterization of the genomic organization of human carcinoembryonic antigen (CEA): Comparison with other family members and sequence analysis of 5′ controlling region (1990) Genomics, 8, pp. 492-500; Williams, A.F., Barclay, A.N., The immunoglobulin superfamily: Domains for cell surface recognition (1988) Annu. Rev. Immunol., 6, pp. 381-405; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938; Zhou, H., Fuks, A., Alcaraz, G., Bolling, T.J., Stanners, C.P., Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds (1993) J. Cell Biol., 122, pp. 951-960","Beauchemin, N.; McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada",,,0022538X,,JOVIA,"8207827","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028335581
"Goncharuk E.I., Shevtsova Z.V., Rumel' N.B., Krylova R.I.","7005858472;7004158851;6603552261;7003925235;","Spontaneous coronavirus infection in monkeys [Spontannaia koronavirusnaia infektsiia obez'ian.]",1994,"Zhurnal Mikrobiologii Epidemiologii i Immunobiologii","Suppl 1",,,"109","114",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028492931&partnerID=40&md5=f813fa3e76af2cb72a61f5dca37d2cf4",,"Goncharuk, E.I.; Shevtsova, Z.V.; Rumel', N.B.; Krylova, R.I.","A high level of the spread of coronavirus (CV) infection among hamadryas baboons and macaques of different species (about 50%), both resident in the animal house and imported, has been established. The tropism of CV to the gastrointestinal and respiratory tracts has been demonstrated. The course of spontaneous CV infection is accompanied by enterocolitis and/or pneumonia with periodic exacerbations, or takes the inapparent form. Cases of virus persistence have also been noted. Infected macaques exhibited an increase in the titers of antibodies to their own CV strain isolated from these animals, as well as to antigenically related human CV strain 0043. Spontaneous CV infection in monkeys may be used for solving some obscure problems of the pathogenesis and epidemiology of CV infection in humans.",,"virus antibody; animal; animal disease; article; baboon; blood; Cercopithecus; comparative study; Coronavirus; electron microscopy; immunology; isolation and purification; Macaca; monkey disease; pathology; ultrastructure; virology; virus infection; Animal; Antibodies, Viral; Cercopithecus aethiops; Comparative Study; Coronavirus; Coronavirus Infections; English Abstract; Macaca; Microscopy, Electron; Monkey Diseases; Papio",,"Goncharuk, E.I.",,,03729311,,,"7856336","Russian","Zh Mikrobiol Epidemiol Immunobiol",Article,"Final",,Scopus,2-s2.0-0028492931
"Zhang X., Liao C.-L., Lai M.M.C.","55715175900;7401957370;7401808497;","Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis",1994,"Journal of Virology","68","8",,"4738","4746",,59,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028284497&partnerID=40&md5=6a08ee57f9bb7cc33dfb9d48ed482428","Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Zhang, X., Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Liao, C.-L., Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Mouse hepatitis virus (MHV), a coronavirus, utilizes a discontinuous transcription mechanism for subgenomic mRNA synthesis. Previous studies (C.- L. Liao and M. C. C. Lai, J. Virol. 68:4727-4737, 1994) have demonstrated that an upstream cis-acting leader sequence serves as a transcriptional enhancer, but the mechanism of transcriptional regulation is not clear. In this study, we constructed a series of defective interfering (DI) RNAs containing the chloramphenicol acetyltransferase (CAT) gene behind a differentially expressed transcription initiation (intergenic) sequence (for mRNA2-1). These DI RNAs had different copy numbers of the UCUAA pentanucleotide sequence at the 3' end of the leader. Transfection of these DI RNA constructs into cells infected with a helper MHV, which contains either two or three UCUAA copies at the 3' end of the leader, resulted in differential expression of CAT activities. We demonstrated that the copy number of UCUAA repeats in the leaders of both helper viral and DI RNAs affected the level of CAT activity, suggesting that MHV leader RNA could regulate both in trans and in cis the transcription of subgenomic mRNAs. The leader RNA of subgenomic mRNAs was derived from either the trans- or the cis- acting leader. Furthermore, insertion of a UA-rich sequence (UUUAUAAAC) immediately downstream of the leader in DI RNA, to match the sequence of helper viral RNA, enhanced the CAT activity by threefold, suggesting that this nine-nucleotide sequence is a cis-acting element. Interestingly, when the nine-nucleotide sequence was absent in DI RNA, the leaders of subgenomic mRNAs were exclusively derived from the helper virus. In contrast, when the nine-nucleotide sequence was present in DI RNA, the leaders were derived from both helper viral and DI RNAs. These results suggest that the nine-nucleotide sequence either is required for the leader RNA to initiate mRNA synthesis or, alternatively, serves as a transcription terminator for the leader RNA synthesis. However, when a constitutively expressed intergenic sequence (for mRNA7) was used, no difference in transcription efficiency was noted, regardless of the copy number of UCUAA in the DI RNA and helper virus. This study thus indicates that MHV subgenomic RNA transcription requires the interaction among the intergenic (promoter) sequence, a trans-acting leader, and a cis-acting leader sequence. A novel model of transcriptional regulation of coronavirus subgenomic mRNAs is presented.",,"chloramphenicol acetyltransferase; complementary dna; messenger rna; virus rna; animal cell; article; enzyme activity; genome; helper virus; mouse; murine hepatitis coronavirus; nonhuman; nucleotide sequence; plasmid; polymerase chain reaction; priority journal; rna synthesis; transcription initiation; transcription regulation; viral genetics; Cell Line; Chloramphenicol O-Acetyltransferase; Cloning, Molecular; DNA, Viral; Gene Expression Regulation, Viral; Helper Viruses; Introns; Molecular Sequence Data; Murine hepatitis virus; Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Transfection",,"Lai, M.M.C.; Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"8035476","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028284497
"Daniel C., Lacroix M., Talbot P.J.","11439494900;11839399600;7102670281;","Mapping of Linear Antigenic Sites on the S Glycoprotein of a Neurotropic Murine Coronavirus with Synthetic Peptides: A Combination of Nine Prediction Algorithms Fails To Identify Relevant Epitopes and Peptide Immunogenicity Is Drastically Influenced by the Nature of the Protein Carrier",1994,"Virology","202","2", 71376,"540","549",,14,"10.1006/viro.1994.1376","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028030443&doi=10.1006%2fviro.1994.1376&partnerID=40&md5=8a6e2a07fdc0f862838d387fdc7532c2","Virology Research Center, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Québec, H7N 4Z3, Canada; BioChem Immuno Systems, Inc., 10900 Hamon, Montréal, Québec, H3M 3A2, Canada","Daniel, C., Virology Research Center, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Québec, H7N 4Z3, Canada; Lacroix, M., BioChem Immuno Systems, Inc., 10900 Hamon, Montréal, Québec, H3M 3A2, Canada; Talbot, P.J., Virology Research Center, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Québec, H7N 4Z3, Canada","The elucidation of the antigenic structure of the S glycoprotein of murine coronaviruses will provide further understanding of the Complex pathogenicity of these viruses. In order to identify linear antigenic determinants, the primary structure of the S glycoprotein of murine hepatitis virus strain A59 was analyzed with a combination of nine epitope prediction algorithms. Fifteen potential epitopes were synthesized chemically and injected into BALB/c mice to study their biological relevance. This approach failed to identify novel important epitopes. Furthermore, the algorithms were unable to identify as antigenic the previously mapped immunodominant epitope A [C Daniel, R. Anderson, M. J. Buchmeier, J. O. Fleming, W. J. M. Spaan, H. Wege, and Talbot, P. J. (1993) J. Virol. 67, 1185-1194]. Interestingly, peptide A coupled to KLH induced an immune response that stimulated the immune response induced by the corresponding region of the protein much more accurately than when the same peptide was coupled to BSA. This included drastically enhanced competition with monoclonal antibodies and protection from virus challenge. These findings emphasize the shortcomings of amino acid sequence-based epitope prediction algorithms and demonstrate the critical importance of the carrier when synthetic peptides are considered as potential vaccines. © 1994 Academic Press. All rights reserved.",,"bovine serum albumin; carrier protein; epitope; monoclonal antibody; neutralizing antibody; synthetic peptide; virus glycoprotein; algorithm; amino acid sequence; animal experiment; antibody titer; antigen detection; article; controlled study; enzyme linked immunosorbent assay; female; immunization; immunoblotting; immunogenicity; intraperitoneal drug administration; mouse; murine hepatitis coronavirus; nonhuman; peptide synthesis; priority journal; virus pathogenesis; Amino Acid Sequence; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Hemocyanin; Membrane Glycoproteins; Molecular Sequence Data; Murine hepatitis virus; Peptides; Serum Albumin, Bovine; Support, Non-U.S. Gov't; Viral Envelope Proteins","Buchmeier, M.I., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (Strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Burks, J.S., Devald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissues of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Collins, A.F., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Daniel, C., Erson, R., Buchmeier, M.J., Fleming, J.O., Spaan, W.J.M., Wege, H., Talbot, P.J., Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of a complex tridimensional structure (1993) J. Virol, 67, pp. 1185-1194; Daniel, C., Talbot, P.J., Physico-chemical properties of murine hepatitis virus, strain A59 (1987) Arch. Virol, 96, pp. 241-248; Daniel, C., Talbot, P.J., Protection from lethal coronavirus infection by affinity-purified spike glycoprotein of murine hepatitis virus, strain A59 (1990) Virology, 174, pp. 87-94; Emini, E.A., Hughes, J.V., Perlow, D.S., Boger, J., Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide (1985) J. Virol, 55, pp. 836-839; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pFi dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. 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Experimental demyelination produced by the A59 strain of mouse hepatitis virus Neurology, 34, pp. 597-603; Lowenadler, B., Lycke, N., Svanholm, C., Svennerholm, A.M., Krook, K., Gidlund, M., T and B cell responses to chimeric proteins containing heterologous T helper epitopes inserted at different positions (1992) Mol. Immunol, 29, pp. 1185-1190; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Vander Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Luytjes, W., Geerts, D., Posthumus, W., Meloen, R., Spaan, W., Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses (1989) J. Virol, 63, pp. 1408-1412; Makel, A.M.J., Salmi, A.A., Norrby, E., Wild, T.F., Monoclonal antibodies against measles virus haemagglutinin react with synthetic peptides (1989) Scand. J. Immunol, 30, pp. 225-231; Mosmann, T.R., Coffman, R.L., Heterogeneity of cytokine secretion patterns and functions of helper T cells (1989) Adv. Immunol, 46, pp. 111-147; Murray, B.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann. Neurol, 31, pp. 525-533; Murray, R.S., Cai, G.Y., Hoel, K., Zhang, J.Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primate central nervous system (1992) Virology, 188, pp. 274-284; Parker, J., Guo, D., Hodges, R.S., New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray derived accessible sites (1986) Biochemistry, 25, pp. 5425-5432; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Pellequer, J.L., Westhof, E., Van Regenmortel, M.H.V., Overview of methods for predicting the location of continuous epitopes in proteins from their primary structures (1991) Methods Enzymol, 203, pp. 176-201; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Rose, G.D., Geselowitz, A.R., Lesser, G.J., Lee, R.H., Zehfus, M.H., Hydrophobicity of amino acid residues in globular proteins (1985) Science, 229, pp. 834-838; Salmi, A., Ziola, B., Hovi, T., Reunanen, M., Antibodies to coronaviruses OC43 and 229E in multiple sclerosis patients (1982) Neurology, 32, pp. 292-295; Scott, P., Kaufmann, S.H., The role of T-cell subsets and cytokines in the regulation of infection (1991) Immunol. Today, 12, pp. 346-348; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses (1990) Immunochemistry of Viruses, 2, pp. 359-379. , The Basis for Serodiagnosis and Vaccines"" (M. H. V. van Regenmortel and A. R. Neurath, Eds.), Elsevier, New York; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Stuhler, A., Wege, H., Siddell, S.G., Localization of antigenic sites on the surface glycoprotein of mouse hepatitis virus (1991) J. Gen. Virol, 72, pp. 1655-1658; Takase-Yoden, S., Kikuchi, T., Sid'dell, S.G., Taguchi, F., Localization of major neutralizing epitopes on the S1 polypeptide of the murine coronavirus peplomer glycoprotein (1991) Virus Res, 18, pp. 99-107; Talbot, P.J., Salmi, A.A., Knobler, R.L., Buchmeier, M.J., Topographical mapping of epitopes on the glycoproteins of murine hepatitis virus-4 (Strain JHM): Correlation with biological activities (1984) Virology, 132, pp. 250-260; Talbot, P.J., Dionne, G., Lacroix, M., Vaccination against lethal coronavirus-induced encephalitis with a synthetic decapeptide homologous to a domain in the predicted peplomer stalk (1988) J. 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Lett, 17, pp. 95-108; Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J Virol, 64, pp. 339-346; Wang, F.I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, H., Dorries, R., Wege, H., Hybridoma antibodies to the murine coronavirus JHM: Characterization of epitopes on the pepiomer protein (E2) (1984) J Gen. Virol, 65, pp. 1931-1942; Welling, G.W., Weijer, W.J., Van Der Zee, R., Welling-Wester, S., Prediction ot sequential antigenic regions in proteins FEBS Lett, 188, pp. 215-218; Wiersma, E.J., Enhancement of the antibody response to protein antigens by specific IgG under different experimental conditions (1992) Scand. J. Immunol, 36, pp. 193-200; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcirtoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536","Talbot, P.J.; Virology Research Center, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Québec, H7N 4Z3, Canada",,,00426822,,,"8030220","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028030443
"Tahara S.M., Dietlin T.A., Bergmann C.C., Nelson G.W., Kyuwa S., Anthony R.P., Stohlman S.A.","7103354164;6602911334;35449739000;7402779709;7006444820;7101632810;35502534500;","Coronavirus Translational Regulation: Leader Affects mRNA Efficiency",1994,"Virology","202","2", 71383,"621","630",,59,"10.1006/viro.1994.1383","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028022039&doi=10.1006%2fviro.1994.1383&partnerID=40&md5=5eb628efb61f94f8a33b89bde17e8333","Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Departments of Neurology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Department of Animal Pathology, Institute for Medical Science, University of Tokyo, Tokyo, Japan","Tahara, S.M., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States, Departments of Neurology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Dietlin, T.A., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Bergmann, C.C., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States, Departments of Neurology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Nelson, G.W., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Kyuwa, S., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States, Department of Animal Pathology, Institute for Medical Science, University of Tokyo, Tokyo, Japan; Anthony, R.P., Departments of Neurology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States; Stohlman, S.A., Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States, Departments of Neurology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States","Cells infected with the murine coronavirus, mouse hepatitis virus (MHV), show decreased host protein synthesis concomitant with an increase in viral protein synthesis. We examined the in vitro translation property of the conserved MHV 5′leader RNA sequence by constructing chimeric mRNAs in which the 72-nt 5′-leader of M protein mRNA (A59 strain) was positioned upstream of the human α-globin coding region in a T7 expression vector. Synthetic 5′-capped transcripts of these mRNA constructs were translated in cell-free extracts prepared from uninfected and MHV-infected murine DBT cells. Nonviral mRNAs translated readily in both uninfected and infected cell-free extracts. By contrast, replacement of the human α-globin 5′-untranslated region (UR) with the MHV 5′-leader increased translation ca. three- to fourfold in cell-free extracts from MHV-infected cells versus translation in extracts from uninfected cells. Chimeric globin mRNA containing the reverse complementary sequence of the viral leader RNA in the 5′-UR showed no such increase in translation, indicating sequence specificity for the effect. A 13-nt region (-UCUAAUCCAAACA-) immediately proximal to the start codon was found to be important for the increased translation of the MHV leader-containing mRNAs. These data indicate that the apparent down-regulation of host translation is not primarily due to an inhibition of host translation but also involves a significant stimulation of viral translation in cis by a structural feature of the MHV 5′-leader RNA sequence in conjunction with a virus-specified or virus-induced factor. © 1994 Academic Press. All rights reserved.",,"alpha globin; complementary dna; m protein; polyadenylated rna; signal peptide; virus messenger rna; animal cell; article; autoradiography; controlled study; culture medium; mouse; murine hepatitis coronavirus; nonhuman; northern blotting; plasmid; polymerase chain reaction; priority journal; rna analysis; rna sequence; rna transcription; rna translation; transcription regulation; tumor cell line; virus transcription; Animal; Base Sequence; Cell Line; Cell-Free System; Gene Expression Regulation, Viral; In Vitro; Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Translation, Genetic; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Chem, 257, pp. 5246-5252; Hann, S.R., King, M.W., Bentley, D.L., Erson, C.W., Eisen-Mann, R.N., A non-AUG translational initiation in c-myc exon 1 generates an N-termirtal!y distinct prctein whose synthesis is disrupted in Burkitt’s lymphomas (1988) Cell, 52, pp. 185-195; Hasan, N., Kim, S.C., Podhajska, A.J., Szybalski, W., A novel multistep method for generating precise unidirectional deletions using BspMI, a class IIS restriction enzyme (1986) Gene, 50, pp. 55-62; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol, 67, pp. 923-932; Huang, J.T., Schneider, R.J., Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein (1991) Cell, 65, pp. 271-280; Iackson, R.J., Cytoplasmic regulation of mRNA function: The importance of the 3’ untranslated region (1993) Ceil, 74, pp. 9-14; Katze, M.G., Detjen, B.M., Safer, B., Krug, R.M., Translational control by influenza virus, suppression of the kinase that phos-phorylates the alpha subunit of initiation factor elF-2 and selective translation of influenza viral mRNAs (1986) Mol. Cell. Biol, 6, pp. 1741-1750; Kuhn, L.C., Hentze, M.W., Coordination of cellular iron metabolism by post-transcriptionai gene regulation (1992) J Inorg. Bio-Chem, 47, pp. 3-4; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lai, M.M., Coronaviruses: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lai, M.M., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus MHV-A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol, 39, pp. 823-834; Lai, M.M., Patton, C.D., Stohlman, S.A., Further characterization of mRNAs of mouse hepatitis virus: Presence of common 5’-end nucleotides (1982) J. Virol, 41, pp. 557-565; Lee, H.-J., Shieh, C.-S., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 240, pp. 567-582; Leibowitz, J., Perlman, S., Weinstock, G., Devries, J.R., Budzilowicz, C., Weissemann, J.M., Weiss, S.R., Detection of a murine coronavirus non structural protein encoded in a downstream open reading frame (1988) Virology, 164, pp. 156-164; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol, 66, pp. 6143-6154; Meerovitch, K., Svitkin, Y.V., Lee, H.S., Lejbkowicz, F., Kenan, D.J., Chan, E.K., Agol, V.I., Sonenberg, N., La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate (1993) J. Virol, 67, pp. 3798-3807; Mehdi, H., Ono, E., Gupta, K.C., Initiation of translation at CUG, GUG, and ACG codons in mammalian cells (1990) Gene, 91, pp. 173-178; Mizzen, L., Macintyre, G., Wong, F., Anderson, R., Translational regulation in mouse hepatitis virus infection is not mediated by altered intracellular ion concentrations (1987) J. Gen. Virol, 68, pp. 2143-2151; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Pelletier, J., Sonenberg, N., Insertion mutagenesis to increase secondary structure within the 5’ noncoding region of a eu-caryotic mRNA reduces translational efficiency (1985) Cell, 40, pp. 515-526; Pensiero, M.N., Lucas-Lenard, J.M., Evidence for the presence of an inhibitor on ribosomes in mouse L cells infected with mengovirus (1985) J. 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Chem, 256, pp. 7691-7694; Xiao, J.H., Davidson, I., Matthes, H., Garnier, J.-M., Chambon, P., Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1 (1991) Cell, 65, pp. 551-568; Yokomori, K., Baker, S.C., Stohlman, S.A., Lai, M.M., Hemagglutinin-Esterase (HE)-specific monoclonal antibodies alter the neuropathogenicity of mouse hepatitis virus (1992) J. Virol, 66, pp. 2865-2874; Zagursky, R.J., Baumeister, K., Lomax, N., Berman, M.L., Rapid and easy sequencing of large linear double-stranded DNA and supercoiled plasmid DNA (1985) Gene Anal. Tech, 2, pp. 89-94","Tahara, S.M.; Departments of Microbiology, University of Southern California School of Medicine, Los Angeles, CA 90033, United States",,,00426822,,,"8030227","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028022039
"Compton S.R.","7102893878;","Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors",1994,"Virology","203","1", 71475,"197","201",,15,"10.1006/viro.1994.1475","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028001582&doi=10.1006%2fviro.1994.1475&partnerID=40&md5=df7859fd5aabc28537a31179ef0ef3e9","Section of Comparative Medicine, Yale University, School of Medicine, New Haven, CT 06520-8016, United States","Compton, S.R., Section of Comparative Medicine, Yale University, School of Medicine, New Haven, CT 06520-8016, United States","Enterotropic mouse hepatitis virus strains (MHV-RI and MHV-Y) replicate in the intestine and rarely disseminate to other tissues, unlike respiratory MHV strains. Murine carcinoembryonic antigen-related glycoproteins (MHVR and mmCGM2) are expressed in many murine tissues and serve as receptors for respiratory MHV strains. To assess the role of receptors in the limited tissue tropism of enterotropic MHV strains, the permissiveness of MHVR- and mmCGM2-expressing cell lines and peritoneal exudate cells from BALB/c and SJL mice for MHV-RI and MHV-Y replication was determined. MHVR-transfected BHK cells were susceptible to infection with both MHV-RI and MHV-Y. Additionally, the anti-MHVR monoclonal antibody CC1 blocked MHV-RI and MHV-Y infection, mmCGM2-transfected BHK cells were susceptible to infection with MHV-Y, but not MHV-RI. Peritoneal exudate cells from BALB/c mice were susceptible to infection with MHV-Y and MHV-RI, whereas peritoneal exudate cells from SJL mice were susceptible to infection with MHV-Y but not MHV-RI. These results indicate that MHV-RI probably uses a different receptor than other MHV strains to infect SJL mice and that receptors are probably not the primary determinant of the limited tissue tropism of enterotropic MHV strains. © 1994 Academic Press, Inc.",,,"Asanaka, M., Lai, M.M.C., (1993) Virology, 197, pp. 732-741; Barthold, S.W., (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, pp. 571-601. , P. N. Bhatt and R. O. Jacoby, Eds.), Academic Press, New York; Barthold, S.W., (1987) Lab. Anim. Sci, 37, pp. 36-40; Barthold, S.W., Beck, D.S., Smith, A.L., (1993) Lab. Anim. Sci, 43, pp. 276-284; Barthold, S.W., Beck, D.S., Smith, A.L., (1986) Arch. Virol, 91, pp. 247-256; Barthold, S.W., Smith, A.L., (1984) Arch. Virol, 81, pp. 103-112; Barthold, S.W., Smith, A.L., (1987) Virus Res, 7, pp. 225-239; Barthold, S.W., Smith, A.L., Lord, P.F.S., Bhatt, P.N., Jacoby, R.O., Main, A.J., (1982) Lab. Anim. Sci, 32, pp. 376-383; Barthold, S.W., Smith, A.L., Povar, M.L., (1985) Lab. Anim. Sci, 35, pp. 613-618; Beauchemin, N., Turbide, C., Afar, D., Bell, J., Raymond, M., Stan-Ners, C.P., Fuks, A., (1989) Cancer Res, 49, pp. 2017-2021; Boyle, J.F., Weismiller, D.G., Holmes, K.V., (1987) J. Virol, 61, pp. 185-189; Compton, S.R., Barthold, S.W., Smith, A.L., (1993) Lab. Anim. Sci, 43, pp. 1-14; Compton, S.R., Stephensen, C.B., Snyder, S.W., Weismiller, D.G., Holmes, K., (1992) J. Viroi, 66, pp. 7420-7428; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.-S., Beauchemin, N., Holmes, K.V., (1993) J. Viroi, 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., (1991) J. Viroi, 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., (1993) J. Viroi, 90, pp. 1716-1720; Knobler, R.L., Haspel, M.V., Oldstone, M.B.A., (1981) J. Exp. Med, 153, pp. 832-843; Knorifr, R.L., Tunison, L.A., Oldstone, M.B.A., (1984) J. Gen. Viroi, 65, pp. 1543-1548; McCuaig, K., Rosenberg, M., Nedellec, P., Turbide, C., Beauchemin, N., (1993) Gene, 127, pp. 173-183; McCuaig, K., Turbide, C., Beauchemin, N., (1992) Cell Growth Differ, 3, pp. 165-174; Smith, A.L., Cardellichio, C.B., Winograd, D.F., Desouza, M., Barthold, S.W., Holmes, K.V., (1991) J. Infect. Dis, 163, pp. 879-882; Smith, M.S., Click, R.E., Plagemann, P.G.W., (1984) J. Immunol, 133, pp. 428-432; Stohlman, S.A., Frelinger, J.A., (1978) Immunogenetics, 6, pp. 277-281; Turbide, C., Rojas, M., Stanners, C.P., Beauchemin, N., (1991) J. Bioi. Chem, 266, pp. 309-315; Williams, R.K., Jiang, G.-S., Holmes, K.V., (1991) Proc. Nati. Acad. Sci. USA, 88, pp. 5533-5536; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., (1990) J. Viroi, 64, pp. 3817-3823; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., (1993) Virology, 196, pp. 45-56; Yokomori, K., Lai, M.M.C., (1992) J. Viroi, 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., (1992) J. Viroi, 66, pp. 6931-6938","Compton, S.R.; Section of Comparative Medicine, Yale University, School of Medicine, New Haven, CT 06520-8016, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028001582
"Zhang X., Herbst W., Kousoulas K.G., Storz J.","55715175900;16161781000;7003476092;7006694594;","Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses",1994,"Archives of Virology","134","3-4",,"421","426",,19,"10.1007/BF01310579","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027948714&doi=10.1007%2fBF01310579&partnerID=40&md5=34428e6de92f43aeae66ec4d17b0c9ff","Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig Universität Giessen, Giessen, Germany","Zhang, X., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Herbst, W., Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig Universität Giessen, Giessen, Germany; Kousoulas, K.G., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States; Storz, J., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States","The nucleotide sequence of the S gene of the bovine respiratory coronavirus (BRCV) strain G95, which was isolated from nasal swabs of a calf suffering from respiratory disorders, was determined and compared with the S gene of the enteropathogenic bovine coronavirus (BECV) strain LY138. Sequence analysis revealed 98.7% nucleotide and 98.3% deduced amino acid identities between the S genes of BRCV-G95 and BECV-LY138 without any deletions or insertions. Nucleotide substitutions were distributed randomly throughout the gene. Five monoclonal antibodies specific for the S protein distinguished BRCV-G95 from BECV-L9, but failed to differentiate it from BECV-LY138 in Western blots under denatured and native conditions. BRCV-G95 induced cytopathic changes in cell cultures that were similar to BECV-LY138 but different from BECV-L9. These results suggest that strain BRCV-G95 is more closely related to the virulent strain BECV-LY138 than to the avirulent, cell culture-adapted strain BECV-L9. © 1994 Springer-Verlag.",,"glycoprotein; monoclonal antibody; spike glycoprotein, coronavirus; virus DNA; virus envelope protein; agglutination test; amino acid sequence; animal; animal disease; article; cattle; cattle disease; cell line; chicken; comparative study; Coronavirus; cytopathogenic effect; enteritis; genetics; immunology; lung disease; microbiology; molecular genetics; mouse; nucleotide sequence; virus gene; virus infection; Agglutination Tests; Amino Acid Sequence; Animal; Antibodies, Monoclonal; Base Sequence; Cattle; Cattle Diseases; Cell Line; Chickens; Comparative Study; Coronavirus Infections; Coronavirus, Bovine; Cytopathogenic Effect, Viral; DNA, Viral; Enteritis; Genes, Viral; Glycoproteins; Lung Diseases; Mice; Molecular Sequence Data; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Envelope Proteins","Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K.V., Lai, M.M., Laude, H., Siddell, S.G., Talbot, P.J., Recommendations of the Corona-virus Study Group for the nomenclature of the structural proteins, mRNAs, and genes of coronaviruses (1990) Virology, 176, pp. 306-307; 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Möstl, K., Bürki, F., Ursächliche Beteiligung boviner Coronaviren an respiratorischen Krankheitsausbrüchen bei Kälbern und pathogenetisch-immunologische Überlegungen hierzu (1988) Dtsch Tierärztl Wochenschr, 95, pp. 19-22; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Rai, R.B., Singh, N.P., Isolation of coronavirus from neonatal calves with pneumoenteritis in India (1983) Vet Rec, 113, pp. 47-48; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc Natl Acad Sci USA, 74, pp. 5463-5467; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-0- acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; St Cyr-Coats, K., Storz, J., Bovine coronavirus induced cytopathic expression and plaque formation: host cell and virus strain determine trypsin dependence (1988) J Vet Med B, 35, pp. 48-56; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J Virol, 56, pp. 904-911; Tompkins, W.A.F., Watrach, A.M., Schmale, J.D., Schultz, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 904-911; Zhang, X.M., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Zhang, X.M., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852; Zhang, X.M., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase gene of human coronavirus strain OC43: phylogenetic relationships to bovine and murine coronaviruses and influenza C virus (1992) Virology, 186, pp. 318-323","Zhang, X.; Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana, United States",,"Springer-Verlag",03048608,,ARVID,"8129626","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0027948714
"Rekik M.R., Dea S.","57209722214;7006056287;","Comparative sequence analysis of a polymorphic region of the spike glycoprotein S1 subunit of enteric bovine coronavirus isolates",1994,"Archives of Virology","135","3-4",,"319","331",,25,"10.1007/BF01310017","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028086705&doi=10.1007%2fBF01310017&partnerID=40&md5=005b195352f06dc95d2369213b4aaab3","Centre de recherche en virologie, Institut Armand-Frappier, Université du Québec Laval, Canada","Rekik, M.R., Centre de recherche en virologie, Institut Armand-Frappier, Université du Québec Laval, Canada; Dea, S., Centre de recherche en virologie, Institut Armand-Frappier, Université du Québec Laval, Canada","Complementary oligonucleotide primers which flank a 1146-nucleotide gene fragment (S1B: nt 1185 to 2333) encompassing a polymorphic region (nt 1368 to 1776) of the S1 subunit of bovine coronavirus spike glycoprotein were used for enzymatic amplification by PCR. We chose four clinical isolates, recovered from cases of epidemic diarrhea in neonatal calves in Québec dairy herds between 1987-1990, to specifically amplify and analyze their sequences in the selected genomic area. Nucleotide sequence analysis of the four clinical isolates indicated that their S1B gene fragments were highly conserved. We also compared the S1B gene sequences of the Québec BCV isolates to the published corresponding sequences from BCV-L9 [37], BCV-MEB [1], and BCV-F15 [3] reference strains. A high degree of similarity was demonstrated for all viruses, no deletions or insertions were observed, and the only variations that were identified consisted of nucleotide substitutions. The differing nucleotides and amino acids (aa) were not distributed randomly over the entire sequence but rather were clustered in the polymorphic region. Of these, four sporadic aa changes were located in antigenic domain II (aa residues 517 to 720) of S1. This correlates with varied antigenicity observed among the BCV Québec isolates when reacting with MAbs directed against the S glycoprotein of the Mebus strain. The other mutations seem to be fixed in all Québec isolates. © 1994 Springer-Verlag.",,"complementary DNA; primer DNA; virus RNA; amino acid sequence; animal; article; cattle; comparative study; Coronavirus; diarrhea; genetic polymorphism; genetics; isolation and purification; kidney; methodology; molecular genetics; multigene family; nucleotide sequence; phylogeny; polymerase chain reaction; sequence homology; virology; virus gene; Amino Acid Sequence; Animal; Base Sequence; Cattle; Comparative Study; Conserved Sequence; Coronavirus, Bovine; Diarrhea; DNA Primers; DNA, Complementary; Genes, Viral; Kidney; Molecular Sequence Data; Multigene Family; Phylogeny; Polymerase Chain Reaction; Polymorphism (Genetics); RNA, Viral; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Support, Non-U.S. Gov't","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1991) Virology, 176, pp. 296-301; Benfield, D.A., Saif, L., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Boireau, P., Cruciere, C., Laporte, J., Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) J Gen Virol, 71, pp. 487-492; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform (1987) Anal Biochem, 162, pp. 156-159; Cyr-Coats, K., Storz, J., Hussain, K.A., Schnorr, K.L., Structural proteins of bovine coronavirus strain L9: Effects of the host cell and trypsin treatment (1988) Arch Virol, 103, pp. 35-45; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J Virol, 64, pp. 3112-3118; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation and cultivation in continuous cell lines (1980) Am J Vet Res, 41, pp. 30-38; Dea, S., Garzon, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (bluecomb) coronaviruses in a continuous human rectal adenocarcinoma cell line (1989) Am J Vet Rec, 50, pp. 1310-1318; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Parker, M.D., Cox, G.C., Babiuk, L.A., Mapping of neutralizing epitopes to fragments of the bovine coronavirus E2 protein by proteolysis of antigen-antibody complexes (1989) J Gen Virol, 70, pp. 647-658; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-2877; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of aneurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J Virol, 64, pp. 731-741; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J Virol, 51, pp. 384-388; Hsu, M-C, Scheid, A., Choppin, P.W., Protease activation mutants of Sendai viruses: sequence analysis of the mRNA of the fusion protein (F) gene and direct identification of the cleavage-activation site (1987) Virology, 156, pp. 84-90; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: monoclonal antibodies to the spike protein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; King, B., Potts, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Res, 2, pp. 53-59; Laporte, J., Bobulesco, P., Rossi, F., Une lignée particulièrement sensible à la réplication du coronavirus entéritique bovin: les cellules HRT-18 (1980) CR Acad Sci (III) Paris, 290 D, pp. 623-626; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhoea: propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Parker, M.D., Yoo, D., Cox, G.J., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) J Gen Virol, 71, pp. 263-270; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletion within E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Rott, R., Orlich, M., Klenk, H-D, Wang, M.L., Skehel, J.J., Wiley, D.C., Studies on the adaptation of influenza viruses to MDCK cells (1984) EMBO J, 3, pp. 3329-3332; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally-induced coronavirus infections in calves: viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc Natl Acad Sci USA, 74, pp. 5463-5467; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am J Vet Res, 37, pp. 1031-1041; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) J Gen Virol, 64, pp. 761-776; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 Glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J Virol, 56, pp. 904-911; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv Virus Res, 28, pp. 35-112; Tompkins, W.A.F., Watrach, A.W., Schmale, J.D., Schultz, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 101-106; Vautherot, J.F., Laporte, J., Madelaine, M.F., Bobulesco, P., Roseto, A., Antigenic and polypeptide structure of bovine enteric coronavirus as defined by monoconal antibodies (1984) Adv Exp Med Biol, 173, pp. 117-132; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: detailed antigenic analysis of S1, S2 and HE (1992) J Gen Virol, 73, pp. 1725-1737; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J Virol, 62, pp. 4686-4690; Yoo, D., Parker, M.D., Song, J., Cox, G.J., Deregt, D., Babiuk, L.A., Structural analysis of the conformational domains involved in neutralization of bovine coronavirus using deletion mutants of the spike glycoprotein S1 subunit expressed by recombinant baculoviruses (1991) Virology, 183, pp. 91-98; Zhang, X., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404","Rekik, M.R.; Centre de recherche en virologie, Institut Armand-Frappier, Université du Québec LavalCanada",,"Springer-Verlag",03048608,,ARVID,"7979970","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0028086705
"Kubo H., Yamada Y.K., Taguchi F.","55183402000;55471420900;7103209890;","Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein",1994,"Journal of Virology","68","9",,"5403","5410",,173,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028018126&partnerID=40&md5=50a5388e6e44cfc69f57b328fcc590f8","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 190-12, Japan","Kubo, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Yamada, Y.K., National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 190-12, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","To localize the epitopes recognized by monoclonal antibodies (MAbs) specific for the S1 subunit of the murine coronavirus JHMV spike protein, we have expressed S1 proteins with different deletions from the C terminus of S1. S1utt is composed of the entire 769-amino-acid (aa) S1 protein; S1NM, S1N, S1N(330), and S1N(220) are deletion mutants with 594, 453, 330, and 220 aa from the N terminus of the S1 protein. The expressed S1 deletion mutant proteins were examined for reactivities to a panel of MAbs. All MAbs classified in groups A and B, those reactive to most mouse hepatitis virus (MHV) strains and those specific for isolate JHMV, respectively, recognized S1N(330) and the larger S1 deletion mutants but failed to react with S1N(220). MAbs in group C, specific for the larger S protein of JHMV, reacted only with the S1utt protein without any deletion. These results indicated that the domain composed of the N-terminal 330 aa comprised the cluster of conformational epitopes recognized by MAbs in groups A and B. It was also shown that the epitopes of MAbs in group C were not restricted to the region missing in the smaller S protein. These results together with the fact that all MAbs in group B retained high neutralizing activity suggested the possibility that the N-terminal 330 aa are responsible for binding to the MHV-specific receptors. In investigate this possibility, we expressed the receptor protein and examined the binding of each S1 deletion mutant to the receptor. It was demonstrated that the S1N(330) protein as well as other S1 deletion mutants larger than S1N(330) bound to the receptor. These results indicated that a domain composed of 330 aa at the N terminus of the S1 protein is responsible for binding to the MHV-specific receptor.",,"epitope; monoclonal antibody; mutant protein; neutralizing antibody; virus protein; virus receptor; amino acid sequence; amino terminal sequence; animal cell; antibody specificity; article; binding site; immunoblotting; immunoreactivity; mouse; murine hepatitis coronavirus; nonhuman; priority journal; receptor binding; receptor gene; vaccinia virus; virus cell interaction; virus neutralization; virus recombinant; Antibodies, Monoclonal; Antibodies, Viral; Base Sequence; Blotting, Western; Coronaviridae; Epitopes; Membrane Glycoproteins; Molecular Sequence Data; Neutralization Tests; Oligonucleotide Probes; Protein Binding; Receptors, Virus; Sequence Deletion; Structure-Activity Relationship; Viral Envelope Proteins",,"Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,0022538X,,JOVIA,"7520090","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028018126
"Liu D.X., Brierley I., Tibbles K.W., Brown T.D.K.","8972667300;7004639098;6507790687;56248391000;","A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products",1994,"Journal of Virology","68","9",,"5772","5780",,50,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027991248&partnerID=40&md5=48d2dea05be9e6d4b6654bdfae4d581f","Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom","Liu, D.X., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom, Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom; Tibbles, K.W., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom","The genome-length mRNA (mRNA 1) of the coronavirus infectious bronchitis virus (IBV) contains two large open reading frames (ORFs), 1a and 1b, with the potential to encode polypeptides of 441 and 300 kDa, respectively. The downstream ORF, ORF 1b, is expressed by a ribosomal frameshifting mechanism. In an effort to detect viral polypeptides encoded by ORF 1b in virus-infected cells, immunoprecipitations were carried out with a panel of region-specific antisera. A polypeptide of approximately 100 kDa was precipitated from IBV- infected, but not mock-infected, Vero cells by one of these antisera (V58). Antiserum V58 was raised against a bacterially expressed fusion protein containing polypeptide sequences encoded by ORF 1b nucleotides 14492 to 15520; it recognizes specifically the corresponding in vitro-synthesized target protein. A polypeptide comigrating with the 100,000-molecular-weight protein (100K protein) identified in infected cells was also detected when the IBV sequence from nucleotides 8693 to 16980 was expressed in Vero cells by using a vaccinia virus-T7 expression system. Deletion analysis revealed that the sequence encoding the C terminus of the 100K polypeptide lies close to nucleotide 15120; it may therefore be generated by proteolysis at a potential QS cleavage site encoded by nucleotides 15129 to 15135. In contrast, expression of IBV sequences from nucleotides 10752 to 16980 generated two polypeptides of approximately 62 and 235 kDa, which represent the ORF 1a stop product and the 1a-1b fused product generated by a frameshifting mechanism, respectively, but no processed products were observed. Since the putative picornavirus 3C-like proteinase domain is located in ORF 1a between nucleotides 8937 and 9357, this observation suggests that deletion of the picornavirus 3C-like proteinase domain and surrounding regions abolishes processing of the 1b polyprotein. In addition, the in vitro translation and in vivo transfection studies also indicate that the ORF 1a region between nucleotides 8763 and 10720 contains elements that down-regulate the expression of ORF 1b.",,"virus protein; animal cell; article; avian infectious bronchitis virus; controlled study; gene expression regulation; immunoprecipitation; nonhuman; nucleotide sequence; open reading frame; polymerase chain reaction; priority journal; protein synthesis regulation; vero cell; Base Sequence; DNA Primers; Endopeptidases; Genes, Structural, Viral; Infectious bronchitis virus; Molecular Sequence Data; Open Reading Frames; Protein Processing, Post-Translational; Recombinant Proteins; Support, Non-U.S. Gov't; Viral Proteins",,"Liu, D.X.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom",,,0022538X,,JOVIA,"8057459","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0027991248
"Gilmore W., Correale J., Weiner L.P.","7004544895;7003887037;15023667100;","Coronavirus induction of class I major histocompatibility complex expression in murine astrocytes is virus strain specific",1994,"Journal of Experimental Medicine","180","3",,"1013","1023",,20,"10.1084/jem.180.3.1013","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028025071&doi=10.1084%2fjem.180.3.1013&partnerID=40&md5=13f614313b5fccb7a7eec02b3a27785a","Departments of Neurology, School of Medecine, Los Angeles, CA, 90033, United States; Departments of Microbiology, University of Southern California, School of Medecine, Los Angeles, CA, 90033, United States","Gilmore, W., Departments of Neurology, School of Medecine, Los Angeles, CA, 90033, United States; Correale, J., Departments of Neurology, School of Medecine, Los Angeles, CA, 90033, United States; Weiner, L.P., Departments of Neurology, School of Medecine, Los Angeles, CA, 90033, United States, Departments of Microbiology, University of Southern California, School of Medecine, Los Angeles, CA, 90033, United States","Neurotropic strains of mouse hepatitis viruses (MHV) such as MHV-A59 (A59) and MHV-4 (JHMV) cause acute and chronic encephalomyelitis and demyelination in susceptible strains of mice and rats. They are widely used as models of human demyelinating diseases such as multiple sclerosis (MS), in which immune mechanisms are thought to participate in the development of lesions in the central nervous system (CNS). The effects of MHV infection on target cell functions in the CNS are not well understood, but A59 has been shown to induce the expression of MHC class I molecules in glial cells after in vivo and in vitro infection. Changes in class I expression in infected cells may contribute to the immunopathogenesis of MHV infection in the CNS. In this communication, a large panel of MHV strains was tested for their ability to stimulate class I expression in primary astrocytes in vitro. The data show that the more hepatotropic strains, such as MHV-A59, MHV-1, MHV-2, MHV-3, MHV-D, MHV-K, and MHV-NuU, were potent inducers of class I expression in astrocytes during acute infection, measured by radioimmunoassay. The K b molecule was preferentially expressed over Db. By contrast, JHMV and several viral strains derived from it did not stimulate the expression of class I molecules. Assays of virus infectivity indicated that the class I-inducing activity did not correlate with the ability of the individual viral strain to replicate in astrocytes. However, exposure of the viruses or the supernatants from infected astrocytes to ultraviolet light abolished the class I-inducing activity, indicating that infectious virus is required for class I expression. These data also suggest that class I expression was induced directly by virus infection, and not by the secretion of a soluble substance into the medium by infected astrocytes. Finally, analyses of A59/JHMV recombinant viral strains suggest that class I-inducing activity resides in one of the A59 structural genes. © 1994, Rockefeller University Press., All rights reserved.",,"major histocompatibility antigen class 1; animal cell; antigen expression; article; astrocyte; demyelinating disease; immunopathogenesis; major histocompatibility complex; mouse; murine hepatitis coronavirus; newborn; nonhuman; priority journal; virus encephalitis; virus infectivity; virus replication; Animal; Astrocytes; Cells, Cultured; Coronavirus Infections; Genes, Viral; Histocompatibility Antigens Class I; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Murine hepatitis virus; Species Specificity; Support, U.S. Gov't, P.H.S.; Virus Replication","Bailey, O.T., Pappenheimer, A.M., Cheever, F.S., Daniels, J.B., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin (1949) J. Exp. 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Pathog., 3, p. 309; Fazakerley, J.K., Parker, S.E., Bloom, J., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, p. 178; Van Berio, M.F., Wolswijk, G., Calafat, J., Koolen, M.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Restricted repli cation of mouse hepatitis virus A59 in primary mouse brain astrocytes correlates with reduced pathogenicity (1986) J. Virol, 58, p. 426; Koolen, M.J., Love, S., Wouda, W., Calafat, J., Horzinek, M.C., Van Der Zeijst, B.A.M., Induction of demyelination by a temperature-sensitive mutant of the coronavirus MHV-A59 is associated with restriction of viral replication in the brain (1987) J. Gen. Virol., 68, p. 703; Fleming, J.O., Trousdale, M.D., Stohlman, S.A., Weiner, L.P., Pathogenic characteristics of neutralization-resistant variants of JHM coronavirus (MHV-4) (1987) Adv. Exp. Med. 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"Klumperman J., Locker J.K., Meijer A., Horzinek M.C., Geuze H.J., Rottier P.J.M.","7003474433;6602308258;57061899200;7102624836;7007186478;7006145490;","Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding",1994,"Journal of Virology","68","10",,"6523","6534",,158,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028133370&partnerID=40&md5=4c3206768542a5086a4294d490761daa","Department of Cell Biology, Center for Electronmicroscopy, Utrecht University, 3584 CX Utrecht, Netherlands; Grad. School Neurosciences Amsterdam, Vrije University, Faculty of Biology, Boelelaan 1087, 1081 HV Amsterdam, Netherlands; Dept. of Infect. Dis. and Immunology, Virology Division, Utrecht University, 3584 CL Utrecht, Netherlands","Klumperman, J., Department of Cell Biology, Center for Electronmicroscopy, Utrecht University, 3584 CX Utrecht, Netherlands, Grad. School Neurosciences Amsterdam, Vrije University, Faculty of Biology, Boelelaan 1087, 1081 HV Amsterdam, Netherlands; Locker, J.K., Dept. of Infect. Dis. and Immunology, Virology Division, Utrecht University, 3584 CL Utrecht, Netherlands; Meijer, A., Dept. of Infect. Dis. and Immunology, Virology Division, Utrecht University, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Dept. of Infect. Dis. and Immunology, Virology Division, Utrecht University, 3584 CL Utrecht, Netherlands; Geuze, H.J., Department of Cell Biology, Center for Electronmicroscopy, Utrecht University, 3584 CX Utrecht, Netherlands; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Virology Division, Utrecht University, 3584 CL Utrecht, Netherlands","The prevailing hypothesis is that the intracellular site of budding of coronaviruses is determined by the localization of its membrane protein M (previously called E1). We tested this by analyzing the site of budding of four different coronaviruses in relation to the intracellular localization of their M proteins. Mouse hepatitis virus (MHV) and infectious bronchitis virus (IBV) grown in Sac(-) cells, and feline infectious peritonitis virus (FIPV) and transmissible gastroenteritis virus (TGEV) grown in CrFK cells, all budded exclusively into smooth-walled, tubulovesicular membranes located intermediately between the rough endoplasmic reticulum and Golgi complex, identical to the so-called budding compartment previously identified for MHV. Indirect immunofluorescence staining of the infected cells showed that all four M proteins accumulated in a perinuclear region. Immunogold microscopy localized MHV M and IBV M in the budding compartment; in addition, a dense labeling in the Golgi complex occurred, MHV M predominantly in trans-Golgi cisternae and trans-Golgi reticulum and IBV M mainly in the cis and medial Golgi cisternae. The corresponding M proteins of the four viruses, when independently expressed in a recombinant vaccinia virus system, also accumulated in the perinuclear area. Quantitative pulse-chase analysis of metabolically labeled cells showed that in each case the majority of the M glycoproteins carried oligosaccharide side chains with Golgi-specific modifications within 4 h after synthesis. Immunoelectron microscopy localized recombinant MHV M and IBV M to the same membranes as the respective proteins in coronavirus-infected cells, with the same cis-trans distribution over the Golgi complex. Our results demonstrate that some of the M proteins of the four viruses are transported beyond the budding compartment and are differentially retained by intrinsic retention signals; in addition to M, other viral and/or cellular factors are probably required to determine the site of budding.",,"m protein; membrane protein; virus protein; article; coronavirus; endoplasmic reticulum; gene expression; golgi complex; immunoelectron microscopy; murine hepatitis coronavirus; priority journal; protein analysis; protein localization; signal transduction; transactivation; virion; virus culture; virus transmission; Animals; Cats; Cell Line; Coronaviridae; Coronavirus, Feline; Fetus; Golgi Apparatus; Humans; Infectious bronchitis virus; Kidney; Microscopy, Electron; Microscopy, Immunoelectron; Murine hepatitis virus; Recombination, Genetic; Swine; Transmissible gastroenteritis virus; Tumor Cells, Cultured; Viral Matrix Proteins","Armstrong, J., Patel, S., The Golgi sorting domain of coronavirus E1 protein (1991) J. 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"Kyuwa S., Cohen M., Nelson G., Tahara S.M., Stohlman S.A.","7006444820;56390144700;7402779709;7103354164;35502534500;","Modulation of cellular macromolecular synthesis by coronavirus: Implication for pathogenesis",1994,"Journal of Virology","68","10",,"6815","6819",,24,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027936372&partnerID=40&md5=1855f6197cf4e106a6b664ea4f52ae9c","Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108, Japan; Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; USC School of Medicine, MCH 142, 2025 Zonal Ave., Los Angeles, CA 90033, United States","Kyuwa, S., Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108, Japan; Cohen, M., Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Nelson, G., Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Tahara, S.M., Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Stohlman, S.A., Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, USC School of Medicine, MCH 142, 2025 Zonal Ave., Los Angeles, CA 90033, United States","Infection with the murine coronavirus strain JHM decreases cell surface expression of major histocompatibility complex class I antigens. Northern blots showed that JHM virus infection rapidly reduced the level of actin mRNA, whereas the levels of major histocompatibility complex class I and tubulin mRNAs were reduced only slightly. By contrast, the mRNA levels of interleukin 1β, colony-stimulating factor 1 receptor, and tumor necrosis factor alpha increased following infection.",,"colony stimulating factor 1; colony stimulating factor receptor; interleukin 1beta; major histocompatibility antigen class 1; tumor necrosis factor alpha; antigen expression; coronavirus; gene expression regulation; immunopathogenesis; major histocompatibility complex; northern blotting; note; priority journal; virus infection; Actins; Animals; Antibodies, Monoclonal; Antibody Specificity; Cell Line; Cell Membrane; Coronavirus; Histocompatibility Antigens Class I; Interleukin-1; Kinetics; L Cells (Cell Line); Mice; Receptor, Macrophage Colony-Stimulating Factor; RNA, Messenger; RNA, Viral; Time Factors; Tumor Necrosis Factor-alpha","Aharon, T., Schneider, R.J., Selective destabilization of short-lived mRNAs with the granulocyte-macrophage colony-stimulating factor AU-rich 3′ noncoding region is mediated by a cotranslational mechanism (1993) Mol. 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Virol., 59, pp. 463-471; Estess, P., Begovich, A.B., Koo, M., Jones, P.P., McDevitt, H.O., Sequence analysis and structure-function correlation of murine q,k,u,s and f haplotype I-A beta cDNA clones (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 3594-3598; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationship of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Fleming, J.O., Wang, F.-I., Trousdale, M.D., Hinton, D.R., Stohlman, S.A., Interaction of immune and central nervous system: Contribution of anti-viral Thy-1+ cells to demyelination induced by coronavirus JHM (1993) Reg. Immunol., 5, pp. 37-43; Gombold, J.L., Weiss, S.R., Mouse hepatitis virus A59 increases steady-state levels of MHC mRNAs in primary glial cell cultures and in the murine central nervous system (1992) Microb. Pathog., 13, pp. 493-505; Gray, P.W., Glaister, D., Chen, E., Goeddel, D.V., Pennica, D., Two interleukin 1 genes in the mouse: Cloning and expression of the cDNA for murine interleukin 1β (1986) J. Immunol., 137, pp. 3644-3648; Hauser, S.L., Doolittle, T.H., Lincoln, R., Brown, R.H., Dinarello, C.A., Cytokine accumulation in CSF of multiple sclerosis patients: Frequent detection of interleukin-1 and tumor necrosis factor but not interleukin-6 (1990) Neurology, 40, pp. 1735-1739; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol., 67, pp. 923-932; Joseph, J., Knobler, R.L., Lubin, F.D., Hart, M.N., Differential modulation of MHC class I antigen expression on mouse brain endothelial cells by MHV-4 infection (1989) J. Neuroimmunol., 22, pp. 241-253; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lavi, E., Suzumura, A., Murray, E.M., Silberberg, D.H., Weiss, S.R., Induction of MHC class I antigens on glial cells is dependent on persistent mouse hepatitis virus infection (1989) J. Neuroimmunol., 22, pp. 107-111; Lecomte, J., Cainelli-Gebara, V., Mercier, G., Mansour, S., Talbot, P.J., Lussier, G., Oth, D., Protection from mouse hepatitis virus type 3-induced acute disease by an anti-nucleoprotein monoclonal antibody (1987) Arch. Virol., 97, pp. 123-130; Lewis, S.A., Lee, M.G., Cowan, N.J., Five mouse tubulin isotypes and their regulated expression during development (1985) J. Cell Biol., 101, pp. 852-861; Malter, J.S., Hong, Y., A redox switch and phosphorylation are involved in the post-translational up-regulation of the adenosine-uridine binding factor by phorbol ester and ionophore (1991) J. Biol. Chem., 266, pp. 3167-3171; Mobley, J., Evans, G., Dailey, M.O., Perlman, S., Immune response to a murine coronavirus: Identification of a homing receptor-negative CD4+ T cell subset that responds to viral glycoproteins (1992) Virology, 187, pp. 443-452; Myers, M.J., Pullen, J.F., Ghildyal, N., Eustis-Turf, E., Schook, L.B., Regulation of IL-1 and TNF-α expression during the differentiation of bone marrow derived macrophage (1989) J. Immu Nol., 142, pp. 153-160; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of monoclonal antibodies on lethal mouse hepatitis virus infection in mice (1986) J. Virol., 59, pp. 168-171; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of the F(ab′)2 fragments of monoclonal antibodies to mouse hepatitis virus (1987) Adv. Exp. Med. Biol., 218, pp. 365-371; Pearce, B.D., Hobbs, M.V., Buckmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol., 68, pp. 5483-5495; Rotzschke, O., Falk, K., Deres, K., Schild, H., Norda, M., Metzger, J., Jung, G., Rammensee, H.-G., Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cells (1990) Nature (London), 348, pp. 252-254; Schneider, R.I., Shenk, T., Impact of virus infection on host cell protein synthesis (1987) Annu. Rev. Biochem., 56, pp. 317-332; Selmaj, K., Raine, C.S., Cross, A.H., Anti-tumor necrosis factor therapy abrogates autoimmune demyelination (1991) Ann. Neurol., 30, pp. 694-700; Steinmetz, M., Frelinger, J.G., Fisher, D., Hunkapiller, T., Pereira, D., Weissman, S.M., Uehara, H., Hood, L., Three cDNA clones encoding mouse transplantation antigens: Homology to immunoglobulin genes (1981) Cell, 24, pp. 125-134; Stohlman, S.A., Bergmann, C.B., Cua, D., Wege, H., Van Der Veen, R., Location of antibody epitopes within the mouse hepatitis virus nucleocapsid protein (1994) Virology, 202, pp. 146-153; Stohlman, S.A., Kyuwa, S., Cohen, M., Bergmann, C., Polo, J.M., Yeh, J., Anthony, R., Keck, J.G., Mouse hepatitis virus nucleocapsid protein-specific cytotoxic T lymphocytes are Ld restricted and specific for the carboxy terminus (1992) Virology, 189, pp. 217-224; Stohlman, S.A., Kyuwa, S., Polo, J.M., Brady, D., Lai, M.M.C., Bergmann, C.C., Characterization of mouse hepatitis virus-specific cytotoxic T cells derived from the central nervous system of mice infected with the JHM strain (1993) J. Virol., 67, pp. 7050-7059; Stoll, G., Jung, S., Jander, S., Van Der Meide, P., Hartung, H.P., Tumor necrosis factor-α in immune-mediated demyelination and Wallerian degeneration (1993) J. Neuroimmunol., 45, pp. 175-182; Suzumura, A., Lavi, E., Weiss, S.R., Silberberg, D.H., Coronavirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes (1986) Science, 232, pp. 991-993; Sussman, M.A., Fleming, J.O., Allen, H., Stohlman, S.A., T-cell-mediated clearance of mouse hepatitis virus strain JHM from the central nervous system (1989) J. Virol., 63, pp. 3051-3056; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Townsend, A., Bodmer, H., Antigen recognition by class I-restricted T lymphocytes (1989) Annu. Rev. Immunol., 7, pp. 601-624; Van Bleek, G.M., Nathenson, S.G., Isolation of an endogenously processed immunodominant viral peptide from the class I H-2kd molecule (1990) Nature (London), 348, pp. 213-216; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of Coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes variant analysis (1988) J. Gen. Virol., 69, pp. 87-98; Williamson, J.S.P., Stohlman, S.A., Effective clearance of mouse hepatitis virus from the central nervous system requires both CD4+ and CD8+ T cells (1990) J. Virol., 64, pp. 4589-4592; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. Neuroimmunol., 32, pp. 1-9; Yamaguchi, K., Kyuwa, K., Nakanaga, K., Hayami, M., Establishment of cytotoxic T-cell clones specific for cells infected with mouse hepatitis virus (1988) J. Virol., 62, pp. 2505-2507; Yamamura, M., Wang, X.-H., Ohmen, J.D., Uyemura, K., Rea, T.H., Bloom, B.R., Modlin, R.L., Cytokine patterns of immunologically mediated tissue damage (1992) J. Immunol., 149, pp. 1470-1475","Stohlman, S.A.; USC School of Medicine, 2025 Zonal Ave., Los Angeles, CA 90033, United States",,,0022538X,,JOVIA,"8084020","English","J. VIROL.",Note,"Final",,Scopus,2-s2.0-0027936372
"Zhang X., Lai M.M.C.","55715175900;7401808497;","Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination",1994,"Journal of Virology","68","10",,"6626","6633",,40,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028086070&partnerID=40&md5=199387180bb2ba4aace199b6970ba1f8","Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Zhang, X., Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, Department of Microbiology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Coronavirus mRNA transcription was thought to be regulated by the interaction between the leader RNA and the intergenic sequence (IS), probably involving direct RNA-RNA interactions between complementary sequences. In this study, we found that a particular strain of mouse hepatitis virus, JHM2c, which has a deletion of a 9-nucleotide (nt) sequence (UUUAUAAAC) immediately downstream of the leader RNA, transcribed subgenomic mRNA species containing a whole array of heterogeneous leader fusion sites. Using a transfected defective interfering RNA which contains an IS and a reporter (chloramphenicol acetyltransferase) gene and JHM2c as a helper virus, we demonstrated that subgenomic mRNAs transcribed from the defective interfering RNAs were extremely heterogeneous. The leader-mRNA fusion sites in this virus can be grouped into five types. In type I, the leader is fused with the consensus IS of the template RNA at a site within the UCUAA repeats, consistent with the classical model of discontinuous transcription. In type II, the leader is fused with the consensus IS as in type I, but the leader of mRNA contains some nucleotide substitutions within the UCUAA repeats. In type III, the leader is fused with mRNAs at a site either upstream or downstream of the consensus IS. The sequences around the fusion sites bear little or no homology to the leader. As a result, mRNAs contain sequences complementary to the template sequences upstream of the IS or have sequence deletions downstream of the IS. In type IV, the leader is fused to the IS at the 9-nt sequence immediately downstream of the UCUAA repeats. In type V, the leader- mRNA fusion site contains a duplication of a portion of the leader sequence or an insertion of nontemplated sequences which are not present in either leader or template RNA. These patterns of leader-mRNA fusion resemble the aberrant homologous recombination frequently seen in other RNA viruses. The degree of heterogeneity of leader fusion sites is dependent on the sequences of both the leader RNA and IS. These results suggest that leader-mRNA fusion in coronavirus transcription does not require direct RNA-RNA interaction between complementary sequences. A modified model of RNA transcription and recombination based on protein-RNA and protein-protein interactions is proposed. This study also provides a paradigm for aberrant homologous recombination.",,"chloramphenicol acetyltransferase; complementary dna; messenger rna; recombinant rna; article; consensus sequence; dna sequence; gene deletion; gene fusion; genetic heterogeneity; genetic polymorphism; murine hepatitis coronavirus; nonhuman; nucleic acid base substitution; priority journal; reporter gene; rna transcription; virus recombination; Animal; Base Sequence; Cell Line; Chloramphenicol O-Acetyltransferase; Cloning, Molecular; DNA Primers; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Polymorphism (Genetics); Recombination, Genetic; Repetitive Sequences, Nucleic Acid; Restriction Mapping; RNA, Messenger; RNA, Viral; Sequence Deletion; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Transfection",,"Lai, M.M.C.; Department of Microbiology, Howard Hughes Medical Institute, S. California Univ. Sch. of Medicine, Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"8083998","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028086070
"Bornkessel B.","7006439068;","Rhino- and coronaviruses. Important pathogens of the common cold [Rhino- und Coronaviren. Wichtige Erreger von Erkältungskrankheiten.]",1994,"Medizinische Monatsschrift fur Pharmazeuten","17","10",,"306","308",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028523547&partnerID=40&md5=36cff3784eda57077f011ea5f8e0bc19",,"Bornkessel, B.",[No abstract available],,"adolescent; adult; child; common cold; Coronavirus; disease transmission; female; human; infant; male; pathogenicity; Picornavirus infection; preschool child; review; Rhinovirus; risk factor; virology; virus infection; Adolescent; Adult; Child; Child, Preschool; Common Cold; Coronavirus; Coronavirus Infections; Female; Human; Infant; Male; Picornaviridae Infections; Rhinovirus; Risk Factors",,"Bornkessel, B.",,,03429601,,,"7990751","German","Med Monatsschr Pharm",Review,"Final",,Scopus,2-s2.0-0028523547
"Der Vartanian M., Méchin M.-C., Jaffeux B., Bertin Y., Félix I., Gaillard-Martinie B.","6602094816;57195160292;16156810200;7003333864;16156589100;6603381883;","Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences",1994,"Gene","148","1",,"23","32",,15,"10.1016/0378-1119(94)90229-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028046269&doi=10.1016%2f0378-1119%2894%2990229-1&partnerID=40&md5=eab3e279f63565c0ac2eb7f97944e7a5","Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France","Der Vartanian, M., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France; Méchin, M.-C., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France; Jaffeux, B., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France; Bertin, Y., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France; Félix, I., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France; Gaillard-Martinie, B., Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France","The clpG gene, expressing the Escherichia coli major CS31A fimbrial subunit ClpG, was subjected to random mutagenesis by insertion of an EcoRI linker and a kanamycin-resistance (KmR) cassette into the multiple newly generated EcoRI sites. The KmR gene was then excised by PstI, which left a 48-bp linker representing the heterologous sequence. The same procedure was followed to introduce a synthetic oligodeoxyribonucleotide (oligo) corresponding to epitope C from the spike protein S from the porcine transmissible gastroenteritis coronavirus (TGEV). Nine insertion/deletion mutants (indels) that contained long foreign peptides variously located around the ClpG signal peptide (SP) processing site were characterized. A striking feature of this study is the variety of amino acid (aa) insertions in the ClpG prepilin that have little or no effect on CS31A fimbria biogenesis. These 'permissive' sites tolerate inserts of 18 or 19 aa and accept sequences of different natures in view of their aa composition, charge and hydrophobicity. The results obtained here are also interesting in light of the high level of aa sequence conservation seen in the SP and N-terminal domains of the ClpG-related subunits. The structure-function relationship of the ClpG SP is discussed. The TGEV-C epitope fused to the N-terminal end of the mature ClpG protein was cell-surface exposed, as observed on immuno-electron microscopy. Therefore, the CS31A fimbria seems to be a potent tool for the presentation of foreign antigenic determinants or the production of heterologous polypeptides in E. coli. © 1994.","antigen display; chaperone; epitope; genetic fusions; hybrid protein secretion; pilin; random mutagenesis; Recombinant DNA; signal sequence; transmissible gastroenteritis virus","epitope; hybrid protein; peptide; pilin; signal peptide; unclassified drug; article; escherichia coli; fimbria; gene structure; mutagenesis; mutant; nonhuman; nucleotide sequence; priority journal; protein secretion; Amino Acid Sequence; Animal; Bacterial Outer Membrane Proteins; Bacterial Proteins; Base Sequence; Coronavirus; DNA Mutational Analysis; Epitopes; Escherichia coli; Fimbriae, Bacterial; Gene Expression Regulation, Bacterial; Membrane Glycoproteins; Molecular Sequence Data; Mutagenesis, Insertional; Plasmids; Protein Processing, Post-Translational; Protein Sorting Signals; Recombinant Fusion Proteins; Support, Non-U.S. Gov't; Swine; Viral Envelope Proteins; Coronavirus; Escherichia coli; Suidae; Transmissible gastroenteritis virus","Bakker, Studies on the K88 Fimbriae of Enteropathogenic Escherichia coli (1991) Thesis, , Vrije Universiteit, Amsterdam; Bertin, Girardeau, Der Vartanian, Martin, The ClpE protein involved in biogenesis of the CS31A capsule-like antigen is a member of a periplasmic chaperone family in Gram-negative bacteria (1993) FEMS Microbiol. Lett., 108, pp. 59-68; Betton, Martineau, Saurin, Hofnung, Location of tolerated insertions/deletions in the structure of the maltose binding protein (1993) FEBS Lett., 325, pp. 34-38; Birnboim, Doly, Rapid alkaline extraction procedure for screening recombinant plasmid DNA (1979) Nucleic Acids Res., 7, pp. 1513-1523; Casey, Moseley, Moon, Characterization of bovine septicemie, bovine diarrheal, and human enteroinvasive Escherichia coli that hybridize with K88 and F41 accessory gene probes but do not express these adhesins (1990) Microb. Pathog., 8, pp. 383-392; Cherifi, Contrepois, Picard, Goullet, De Rycke, Fairbrother, Barnouin, Factors and marker of virulence in Escherichia coli from human septicemia (1990) FEMS Microbiol. Lett., 70, pp. 279-284; Contrepois, Fairbrother, Kaura, Girardeau, Prevalence of CS31A and F16S surface antigens in Escherichia coli isolates from animals in France, Canada and India (1989) FEMS Microbiol. Lett., 59, pp. 319-324; Delmas, Rasschaert, Godet, Gelfi, Laude, Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the N-terminal half of spike glycoprotein S (1990) J. Gen. Virol., 71, pp. 1313-1323; Eisenberg, Schwartz, Kamarsmy, Wall, Analysis of membrane and surface protein sequences with hydrophobic moment plot (1984) J. Mol. Biol., 179, pp. 125-142; Fikes, Barkocy-Gallagher, Klapper, Bassford, Jr., Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo (1990) J. Biol. Chem., 265, pp. 3417-3423; Gibrat, Gamier, Rosbon, Further developments of proteins secondary structure prediction using information theory (1987) J. Mol. Biol., 198, pp. 425-443; Girardeau, Bertin, Martin, Der Vartanian, Boeuf, Sequence analysis of the clpG gene, which codes for surface antigen CS31A subunit: evidence of an evolutionary relationship between CS31A, K88 and F41 subunit genes (1991) J. Bacteriol., 173, pp. 7676-7683; Girardeau, Der Vartanian, Oilier, Contrepois, CS31A, a new K88 related fimbrial antigen on bovine enterotoxigenic and septicemie Escherichia coli strains (1988) Infect. Immun., 56, pp. 2180-2188; Guesdon, Bouges-Bocquet, Debarbouillé, Hofnung, In situ enzyme immunodetection of surface or intracellular bacterial antigens using nitrocellulose sheets (1985) J. Immunol. Methods, 84, pp. 53-63; Hemilä, Pakkanen, Heikinheimo, Palva, Palva, Expression of the Erwinia carotovora polygalacturonase-encoding gene in Bacillus subtilis: role of signal peptide fusions on production of a heterologous protein (1992) Gene, 116, pp. 27-33; Hobbs, Mattick, Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes (1993) Mol. Microbiol., 10, pp. 233-243; Hopp, Woods, Prediction of protein antigenic determinants from amino acid sequences (1981) Proc. Natl. Acad. Sci. USA, 78, pp. 3824-3828; Hultgren, Linberg, Magnusson, Kihlberg, Tennent, Normark, The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 4357-4361; Inouye, Halegoua, Secretion and membrane localization of proteins in Escherichia coli (1980) Crit. Rev. Biochem., 7, pp. 339-371; Korth, Apostol, Moseley, Functional expression of heterologous fimbrial subunits mediated by the F41, K88 and CS31A determinants of Escherichia coli (1992) Infect. Immun., 60, pp. 2500-2505; Korth, Schneider, Moseley, An F41-K88-related genetic determinant of bovine septicemie Escherichia coli mediates expression of CS31A fimbriae and adherence to epithelial cells (1991) Infect. Immun., 59, pp. 2333-2340; Lathe, Kieny, Skory, Lecocq, Laboratory methods linker tailing: unphospho-rylated linker oligonucleotides for joining DNA termini (1984) DNA, 3, pp. 173-182; Laude, Chapsal, Gelfi, Labiau, Grosclaude, Antigenic structure of transmissible gastroenteritis virus I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Lehnhardt, Pollitt, Inouye, The differential effect of two hybrid proteins of deletion mutations within the hydrophobic region of the Escherichia coli OmpA signal peptide (1987) J. Biol. Chem., 262, pp. 1716-1719; Martin, Boeuf, Bousquet, Escherichia coli CS31A fimbriac: molecular cloning, expression and homology with the K88 determinant (1991) Microb. Pathog., 10, p. 429 442; Pheiffer, Zimmerman, Polymer-stimulated ligation: enhanced blunt- or cohesive-end ligation of DNA or deoxyribooligonucleotides by T4 DNA ligase in polymer solutions (1983) Nucleic Acids Res., 11, p. 7853; Prickett, Amberg, Hopp, A calcium dependent antibody for identification and purification of recombinant proteins (1989) BioTechniques, 7, pp. 580-589; Pugsley, The complete general secretory pathway in Gramnegative bacteria (1993) Microbiol. Rev., 57, pp. 50-108; Smith, Crouse, Construction of linker-scanning mutations using a kanamycin-resistance cassette with multiple symmetric restriction sites (1989) Gene, 84, pp. 159-164; Strom, Lory, Amino acid substitutions in pilin of Pseudomonas aeruginosa (1991) J. Biol. Chem., 266, pp. 1656-1664; Towbin, Staehelin, Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354; Vieira, Messing, The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers (1982) Gene, 19, p. 259 268","Der Vartanian, M.; Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France",,,03781119,,GENED,"7523252","English","Gene",Article,"Final",,Scopus,2-s2.0-0028046269
"Dong S., Baker S.C.","7402016646;7403307881;","Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus",1994,"Virology","204","2", 71567,"541","549",,52,"10.1006/viro.1994.1567","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027995476&doi=10.1006%2fviro.1994.1567&partnerID=40&md5=69d175374f3833e8d8ed2860d0ffeb90","Molecular Biology Program and Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States","Dong, S., Molecular Biology Program and Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Baker, S.C., Molecular Biology Program and Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States, Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States","The murine coronavirus polymerase gene is 22 kb in length with the potential to encode a polyprotein of approximately 750 kDa. The polyprotein has been proposed to encode three proteinase domains which are responsible for the processing of the polyprotein into mature proteins. The proteolytic activity of the first proteinase domain has been characterized and resembles the papain family of cysteine proteinases. This proteinase domain acts autoproteolytically to cleave the amino terminal portion of the polymerase polyprotein, releasing a 28-kDa protein designated p28. To identify the cleavage site of this papain-like cysteine proteinase, we isolated the peptide adjacent to p28 and determined the amino terminus sequence by Edman degradation reaction. We report that proteolysis occurs between the Gly-247 and Val-248 dipeptide bond. To determine the role of the amino acid residues surrounding the cleavage site, we introduced a total of 42 site-specific mutations at the residues spanning the P5 to P3' positions and assessed the effects of the mutations on the processing of p28 in an in vitro transcription and translation system. The substitutions of Gly-247 at the P1 position or Arg-246 at the P2 position resulted in a dramatic decrease of proteolytic activity, and the mutations of Arg-243 at P5 position also led to considerable reduction in p28 cleavage. In contrast, the substitutions of amino acids Gly-244 (P4), Tyr-245 (P3), Val-248 (P1'), Lys-249 (P2'), and Pro-250 (P3') had little or no effect on the amount of p28 that was released. This work has identified Gly-247-Val-248 as the cleavage site for the release of p28, the amino;terminal protein of the murine coronavirus polymerase polyprotein. Additionally, we conclude that the Gly-247 and Arg-246 are the major determinants for the cleavage site recognition by the first papain-like cysteine proteinase of murine coronavirus. © 1994 Academic Press, Inc.",,,"Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. 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Natl. Acad. Sci. USA, 88, pp. 1167-1171; Choi, G.H., Pawlyk, D.M., Nuss, D.L., The autocatalytic proteinase p29 encoded by a hypovirulence-associated virus of the chestnut biight fungus resembles the potyvirus-encoded proteinase HC-Pro (1991) Virology, 183, pp. 747-752; De Groot, R., Hardy, W.R., Shirako, Y., Strauss, J.H., Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo (1990) EMBO J, 9, pp. 2631-2638; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol, 65, pp. 2910-2920; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. 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Rev, 57, pp. 781-822; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS Lett, 288, pp. 201-205; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4847-4861; Hardy, W.R., Strauss, J.H., Processing the nonstructural polyproteins of Sindbis virus: Nonstructural proteinase is in the C- terminal half of nsP2 and functions both in cis and in trans (1989) J. Virol, 63, pp. 4653-4664; Hellen, C.U.T., Lee, C.-K., Wimmer, E., Determinants of substrate recognition by poliovirus 2A proteinase (1992) J. Virol, 66; Hutchison, C.A., Phillips, S., Edgell, M.H., Gilliam, S., Jahnke, P., Smith, M., Mutagenesis at a specific position in a DNA sequence (1978) J. Biol Chem, 253, pp. 6551-6560; Krausslich, H.G., Wimmer, E., Viral proteinases (1988) Annu. Rev. Biochem, 57, pp. 701-754; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lai, M.M.C., Coronaviruses: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol, 46, pp. 1027-1033; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerases (1991) Virology, 180, pp. 567-582; Lewis, M.K., Thompson, D.V., Efficient site directed in vitro mutagenesis using ampicillin selection (1990) Nucleic Acids Res, 18; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High frequency RNA recombination of murine coronaviruses (1986) J. Virol, 57, pp. 729-737; Maniatis, T.E., Fritsch, E.F., Sambrook, J., (1982) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes (1987) J. Biol. Chem, 262, pp. 35-110; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Palmenberg, A.C., Proteolytic processing of picornaviral poly- protein (1990) Annu. Rev. Microbiol, 44, pp. 603-623; Schechter, I., Berger, A., On the active site of proteinases. III. Papain (1967) Biochem. Biophys. Res. Commun, 32, pp. 898-902; Shapira, R., Nuss, D.L., Gene expression by a hypovirulence- associated virus of the chestnut blight fungus involves two papainlike proteinase activities (1991) Biol. Chem, 266, pp. 19419-19426; Shirako, Y., Strauss, J.H., Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123 (1990) Virology, 177, pp. 54-64; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., The 5 end of the equine arteritis virus replicase gene encodes a papainlike cysteine pratease (1992) J. Virol, 66, pp. 7040-7048; Soe Shieh, L.H.C.-K., Baker, S.C., Chang, M.F., Lai, M.M.C., Sequence and translation of the murine coronavirus 5f-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase (1987) J. Virol, 61, pp. 3968-3976; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Corona viruses: Structure and genome expression (1988) J. Gen. Virol, 69, pp. 2939-2952; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J, 2, pp. 1839-1944; Strauss, E.G., Strauss, J.H., Alphavirus proteinases (1990) Sem. Virol, 1, pp. 347-356; Vieira, J., Messing, J., Production of single-stranded plasmid DNA (1987) Methods Enzymol, 153, pp. 3-11","Baker, S.C.; Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0027995476
"Weingartl H.M., Derbyshire J.B.","6602300880;7004580204;","Evidence for a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs",1994,"Journal of Virology","68","11",,"7253","7259",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028007201&partnerID=40&md5=08c238ea8488c9614dd60fabe1b7f2f0","Dept. Vet. Microbiol. and Immunol., University of Guelph, Guelph, Ont. N1G 2W1, Canada","Weingartl, H.M., Dept. Vet. Microbiol. and Immunol., University of Guelph, Guelph, Ont. N1G 2W1, Canada; Derbyshire, J.B., Dept. Vet. Microbiol. and Immunol., University of Guelph, Guelph, Ont. N1G 2W1, Canada","Aminopeptidase-N (APN) has been identified [B. Delmas, J. Gelfi, R. L'Haridon, L. K. Vogel, H. Sjostrom, O. Noren, and H. Laude, Nature (London) 357:417-420, 1992] as a major receptor for porcine transmissible gastroenteritis virus (TGEV). Binding of TGEV to villous enterocytes from the jejuna of newborn pigs is saturable and at a higher level than that of binding of virus to newborn cryptal enterocytes or to enterocytes from older piglets (H. M. Weingartl and J. B. Derbyshire, Vet. Microbiol. 35:23-32, 1993). The distribution of APN in enterocytes in the jejuna of neonatal and 3 week-old-piglets, as determined by the measurement of enzymatic activity and by labeling of the cells with an anti-APN monoclonal antibody, did not correspond with the reported distribution of saturable binding sites on enterocytes. Monoclonal antibodies, which were prepared against plasma membranes derived from enterocytes harvested from the upper villi of newborn pigs, blocked the replication of TGEV, but not the porcine respiratory coronavirus, in ST cells and immunoprecipitated a 200-kDa protein in ST cell lysates. This protein was demonstrated by immunohistochemistry and by fluorescence-activated cell scanning to be present on the villous enterocytes of newborn pigs but to be lacking on the cryptal enterocytes of newborn pigs and on the villous and cryptal enterocytes of 3-week-old piglets. Since this distribution of the protein corresponds to the previously demonstrated distribution of saturable binding sites, we conclude that the 200-kDa protein may be an additional receptor for TGEV which is restricted to the villous enterocytes of newborn pigs and which contributes to the age sensitivity of these animals to the virus.",,"microsomal aminopeptidase; virus receptor; animal cell; article; binding site; controlled study; coronavirus; enzyme activity; immunohistochemistry; intestine cell; jejunum; newborn; nonhuman; priority journal; receptor binding; swine; virus adsorption; Animal; Animals, Newborn; Antibodies, Monoclonal; Antigens, CD13; Enzyme-Linked Immunosorbent Assay; Immunohistochemistry; Intestines; Precipitin Tests; Receptors, Virus; Support, Non-U.S. Gov't; Swine; Transmissible gastroenteritis virus",,"Derbyshire, J.B.; Veterinary Microbiol./Immunol. Dept., University of Guelph, Guelph, Ont. N1G 2W1, Canada",,,0022538X,,JOVIA,"7933108","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028007201
"Ostermann A., Klueppelberg U., Wassermann K., Krueger G.R.F.","57198122323;57194678562;7006104903;7103029509;","Non-specific interstitial pneumonia (NIP): Immunohistologic screening of etiologic agents",1994,"In Vivo","8","4",,"613","619",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027974264&partnerID=40&md5=b3e5f97e3f17bb316029e424699b7d4b","Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany","Ostermann, A., Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany; Klueppelberg, U., Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany; Wassermann, K., Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany; Krueger, G.R.F., Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany","Non-specific interstitial pneumonia (NIP) occurs frequently in patients with HIV-infection. To elucidate the etiology of this pulmonary disorder, we searched for 13 different microorganisms in transbronchial biopsies from 15 patients with NIP, 15 patients with Pneumocystis carinii pneumonia (PCP) and 20 patients with lung diseases not related to HIV-infection using monoclonal antibodies and the APAAP-or PAP-technique for immunostaining. Chlamydia trachomatis and parainfluenza III were detected frequently and in great number. Adenovirus, influenza B, varicella zoster and cytomegalovirus were also found frequently, but not in great number. Measles virus, respiratory syncytial virus, influenza A and herpesviruses 1 and 2 were not found. Also not found were parainfluenza I, mycoplasma pneumoniae and coronavirus. In seven out of fifteen NIP patients at least one organism was shown, compared to nine out of fifteen patients with PCP and eight out of twenty patients in the control group.","Chlamydia; HIV infection; Non-specific interstitial pneumonia; Viral infections","Adenovirus; adult; article; Chlamydia trachomatis; clinical article; controlled study; Cytomegalovirus; female; human; Human immunodeficiency virus infection; human tissue; immunohistology; Influenza virus B; interstitial pneumonia; male; nonhuman; Parainfluenza virus 3; Pneumocystis pneumonia; transbronchial biopsy; Varicella zoster virus; Adenoviridae Infections; Adult; Aged; AIDS-Related Opportunistic Infections; Antibodies, Bacterial; Antibodies, Monoclonal; Antibodies, Viral; Biopsy; Chlamydia Infections; Chlamydia trachomatis; Comparative Study; Female; HIV Infections; HIV-1; Human; Lung Diseases, Interstitial; Male; Middle Age; Parainfluenza Virus 3, Human; Paramyxoviridae Infections; Pneumonia, Pneumocystis carinii; Pneumonia, Viral",,"Ostermann, A.; Immunopathology Laboratory, Institute of Pathology, 50924 Cologne, Germany",,,0258851X,,IVIVE,"7893990","English","IN VIVO",Article,"Final",,Scopus,2-s2.0-0027974264
"Chang R.-Y., Hofmann M.A., Sethna P.B., Brian D.A.","36725275000;57203181972;7003358474;7006460232;","A cis-acting function for the coronavirus leader in defective interfering RNA replication",1994,"Journal of Virology","68","12",,"8223","8231",,87,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027997834&partnerID=40&md5=d2ada45db56aa003563eb8d77e767ae2","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Inst. Virol. and Immunoprophylaxis, CH-3147 Mittelhausern, Switzerland; Div. Molec. Genet. and Molec. Biol., Burroughs Wellcome Co., Research Triangle Park, NC 27709, United States","Chang, R.-Y., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Hofmann, M.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Inst. Virol. and Immunoprophylaxis, CH-3147 Mittelhausern, Switzerland; Sethna, P.B., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Div. Molec. Genet. and Molec. Biol., Burroughs Wellcome Co., Research Triangle Park, NC 27709, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","To test the hypothesis that the 65-nucleotide (nt) leader on subgenomic mRNAs suffices as a 5'-terminal cis-acting signal for RNA replication, a corollary to the notion that coronavirus mRNAs behave as replicons, synthetic RNA transcripts of a cloned, reporter-containing N mRNA (mRNA 7) of the bovine coronavirus with a precise 5' terminus and a 3' poly(A) of 68 nt were tested for replication after being transfected into helper virus-infected cells. No replication was observed, but synthetic transcripts of a cloned reporter-containing defective interfering (DI) RNA differing from the N mRNA construct by 433 nt of continuous 5'-proximal genomic sequence between the leader and the N open reading frame did replicate and become packaged, indicating the insufficiency of the leader alone as a 5' signal for replication of transfected RNA molecules. The leader was shown to be a necessary part of the cis-acting signal for DI RNA replication, however, since removal of terminal bases that destroyed a predicted intraleader stem- loop also destroyed replicating ability. Surprisingly, when the same stem- loop was disrupted by base substitutions, replication appeared only minimally impaired and the leader was found to have rapidly reverted to wild type during DI RNA replication, a phenomenon reminiscent of high-frequency leader switching in the mouse hepatitis coronavirus. These results suggest that once a minimal structural requirement for leader is fulfilled for initiation of DI RNA replication, the wild-type leader is strongly preferred for subsequent replication. They also demonstrate that, in contrast to reported natural mouse hepatitis coronavirus DI RNAs, the DI RNA of the bovine coronavirus does not require sequence elements originating from discontinuous downstream regions within the polymerase gene for replication or for packaging.",,"complementary dna; polyadenylated rna; ribonuclease; signal peptide; virus messenger rna; article; cancer cell culture; coronavirus; genetic transfection; human; human cell; molecular cloning; nonhuman; northern blotting; nucleic acid base substitution; open reading frame; priority journal; reporter gene; rna replication; rna transcription; Amino Acid Sequence; Base Sequence; Calorimetry; Cell Line; Cloning, Molecular; Coronavirus, Bovine; Defective Viruses; DNA Primers; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Open Reading Frames; Polymerase Chain Reaction; Protein Sorting Signals; Rectal Neoplasms; Restriction Mapping; RNA, Messenger; RNA, Viral; Transcription, Genetic; Transfection; Tumor Cells, Cultured","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′ end of viral RNA (1993) EMBO J., 12, pp. 3587-3598; Baker, S.C., Lai, M.M.C., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) EMBO J., 9, pp. 4173-4179; Ball, L.A., Li, Y., cis-acting requirements for the replication of flock house virus RNA 2 (1993) J. 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Rev., 56, pp. 61-79; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Levis, R., Weiss, B.G., Tsiang, M., Huang, H., Schlesinger, S., Deletion mapping of Sindbis virus di RNAs derived from cDNAs defines the sequences essential for replication and packaging (1986) Cell, 44, pp. 137-145; Li, X., Palese, P., Mutational analysis of the promoter required for influenza virus virion RNA synthesis (1992) J. Virol., 66, pp. 4331-4338; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol., 66, pp. 6117-6124; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontinuous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Stohlman, S., Lai, M.M.C., Leader sequence of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA in transcription (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 4204-4208; Masters, P., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Rice, C.M., Grakoui, A., Galler, R., Chambers, T.J., Transcription of Yellow Fever RNA from full-length cDNA templates produced by in vitro ligation (1989) New Biol., 1, pp. 285-296; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in mRNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene of the bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Sethna, P.B., Brian, D.A., Unpublished data; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNA and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Tinoco, I., Borer, P.N., Dengler, B., Levine, M.D., Uhlenbeck, O.C., Crothers, D.M., Gralla, J., Improved estimation of secondary structure in ribonucleic acids (1973) Nature (London) New Biol., 246, pp. 40-41; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Vidal, S., Kolakofsky, D., Modified model for the switch from Sendai virus transcription to replication (1989) J. Virol., 63, pp. 1951-1958; Yokomori, K., Banner, L.R., Lai, M.M.C., Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic-length template (1992) J. Virol., 66, pp. 4671-4678","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States",,,0022538X,,JOVIA,"7966615","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0027997834
"Godet M., Grosclaude J., Delmas B., Laude H.","57206533441;7004095202;7003294168;7006652624;","Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein",1994,"Journal of Virology","68","12",,"8008","8016",,117,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027971620&partnerID=40&md5=7cf37c3ebc23e2d0c9642cdb70b5dc54","U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, Jouy-en-Josas, France; U. Virologie Immunol. Moleculaires, INRA, 78852 Jouy-en-Josas Cedex, France","Godet, M., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, Jouy-en-Josas, France; Grosclaude, J., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, Jouy-en-Josas, France; Delmas, B., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, Jouy-en-Josas, France; Laude, H., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, Jouy-en-Josas, France, U. Virologie Immunol. Moleculaires, INRA, 78852 Jouy-en-Josas Cedex, France","The spike glycoprotein (S) of coronavirus, the major target for virus- neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization- mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor- binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.",,"aminopeptidase; neutralizing antibody; virus enzyme; virus glycoprotein; amino acid sequence; antigen binding; article; carboxy terminal sequence; coronavirus; enzyme linked immunosorbent assay; gastroenteritis; immunization; immunofluorescence; nonhuman; polyacrylamide gel electrophoresis; priority journal; protein binding; virion; virus cell interaction; virus neutralization; virus transmission; Amino Acid Sequence; Animal; Antibodies, Monoclonal; Base Sequence; Binding Sites; Cell Line; DNA Primers; Epitopes; Fluorescent Antibody Technique; Genetic Vectors; Membrane Glycoproteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Neutralization Tests; Nucleopolyhedrovirus; Polymerase Chain Reaction; Receptors, Virus; Recombinant Proteins; Restriction Mapping; Spodoptera; Support, Non-U.S. Gov't; Swine; Transfection; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Laude, H.; Unite Virologie/Immunologie Molec., INRA, 78852 Jouy-en-Josas Cedex, France",,,0022538X,,JOVIA,"7525985","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0027971620
"Rossen J.W.A., Bekker C.P.J., Voorhout W.F., Strous G.J.A.M., Van Der Ende A., Rottier P.J.M.","7005977394;56403027300;7003796069;7004975908;7007055960;7006145490;","Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells",1994,"Journal of Virology","68","12",,"7966","7973",,30,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028114493&partnerID=40&md5=cf491f9b676d99b9bbb1a1497a24e652","Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Laboratory of Cell Biology, Medical School, Utrecht University, 3584 CX Utrecht, Netherlands; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands; Department of Medical Microbiology, University of Amsterdam, 1105 AZ Amsterdam, Netherlands","Rossen, J.W.A., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Bekker, C.P.J., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Voorhout, W.F., Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Strous, G.J.A.M., Laboratory of Cell Biology, Medical School, Utrecht University, 3584 CX Utrecht, Netherlands; Van Der Ende, A., Laboratory of Cell Biology, Medical School, Utrecht University, 3584 CX Utrecht, Netherlands, Department of Medical Microbiology, University of Amsterdam, 1105 AZ Amsterdam, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands","The transmissible gastroenteritis coronavirus (TGEV) infects the epithelial cells of the intestinal tract of pigs, resulting in a high mortality rate in piglets. This study shows the interaction of TGEV with a porcine epithelial cell line. To determine the site of viral entry, LLC-PK1 cells were grown on permeable filter supports and infected with TGEV from the apical or basolateral side. Initially after plating, the virus was found to enter the cells from both sides. During further development of cell polarity, however, the entry became restricted to the apical membrane. Viral entry could be blocked by a monoclonal antibody to the viral receptor aminopeptidase N. Confocal laser scanning microscopy showed that this receptor protein was present at both the apical and basolateral plasma membrane domains just after plating of the cells but that it became restricted to the apical plasma membrane during culture. To establish the site of viral release, the viral content of the apical and basolateral media of apically infected LLC-PK1 cells was measured by determining the amount of radioactively labelled viral proteins and infectious viral particles. We found that TGEV was preferentially released from the apical plasma membrane. This conclusion was confirmed by electron microscopy, which demonstrated that newly synthesized viral particles attached to the apical membrane. The results support the idea that the rapid lateral spread of TGEV infection over the intestinal epithelia occurs by the preferential release of virus from infected epithelial cells into the gut lumen followed by efficient infection of nearby cells through the apical domain.",,"monoclonal antibody; virus protein; virus receptor; animal tissue; article; coronavirus; electron microscopy; gastroenteritis; immunoprecipitation; intestine epithelium cell; isotope labeling; nonhuman; priority journal; protein synthesis; swine; virus cell interaction; virus particle; virus transmission; Animals; Antibodies, Monoclonal; Antigens, CD13; Cell Line; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Epithelium; Microscopy, Electron; Receptors, Virus; Swine; Transmissible gastroenteritis virus; Viral Proteins","Ambali, A.G., Jones, R.C., Early pathogenesis in chicks of infection with an enterotropic strain of infectious bronchitis virus (1990) Avian Dis., 34, pp. 809-817; Anderson, G.W., Smith, J.F., Immunoelectron microscopy of Rift Valley fever viral morphogenesis in primary rat hepatocytes (1987) Virology, 161, pp. 91-100; Baron, R., Neff, L., Brown, W., Courtoy, P.J., Louvard, D., Farquhar, M.G., Polarized secretion of lysosomal enzymes: Co-distribution of cation-independent mannose-6-phosphate receptors and lysosomal enzymes along the osteoclast exocytic pathway (1988) J. Cell Biol., 106, pp. 1863-1872; Caplan, M., Matlin, K.S., Sorting of membrane and secretory proteins in polarized epithelial cells (1989) Functional Epithelial Cells in Culture, pp. 71-127. , K. S. Matlin and J. D. Valentich (ed.), Alan R. Liss, New York; Cereijido, M., Contreras, R.G., Gonzalez-Mariscal, L., Development and alteration of polarity (1989) Annu. Rev. Physiol., 51, pp. 785-795; Cerneus, D.P., Strous, G.J., Van Der Ende, A., Bidirectional transcytosis determines the steady state distribution of the transferrin receptor at opposite plasma membrane domains of BeWo cells (1993) J. Cell Biol., 122, pp. 1223-1230; Chen, S.-Y., Matsuoka, Y., Compans, R.W., Assembly and polarized release of Punta Toro virus and effects of brefeldin A (1991) J. Virol., 65, pp. 1427-1439; Clayson, E.T., Compans, R.W., Entry of simian virus 40 is restricted to apical surfaces of polarized epithelial cells (1988) Mol. Cell. Biol., 8, pp. 3391-3396; Compans, R.W., Srinivas, R.V., Protein sorting in polarized epithelial cells (1991) Curr. Top. Microbiol. Immunol., 170, pp. 141-181; Condron, R.J., Marshall, A.T., Pathogenesis of infectious bronchitis nephritis 1. Morphometric analysis of kidney proximal tubular epithelium in chickens (1986) J. Comp. Pathol., 96, pp. 47-61; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-420; Doyle, L.P., Hutchings, L.M.A., A transmissible gastro-enteritis in pigs (1946) J. Am. Vet. Med. Assoc., 108, pp. 257-259; Fuller, S.D., Von Bonsdorff, C.-H., Simons, K., Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK (1984) Cell, 38, pp. 65-77; Fuller, S.D., Von Bonsdorff, C.-H., Simons, K., Cell surface influenza haemagglutinin can mediate infection by other animal viruses (1985) EMBO J., 4, pp. 2475-2485; Griffiths, G., Rottier, P., Cell biology of viruses that assemble along the biosynthetic pathway (1992) Semin. Cell Biol., 3, pp. 367-381; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; Gstraunthaler, G.J.A., Epithelial cells in tissue culture (1988) Renal Physiol. Biochem., 11, pp. 1-42; Hubbard, A.L., Stieger, B., Bartles, J.R., Biogenesis of endogenous plasma membrane proteins in epithelial cells (1989) Annu. Rev. Physiol., 51, pp. 555-570; Hull, R.N., Cherry, W.R., Weaver, G.W., The origin and characteristics of a pig kidney cell strain, LLC-PK1 (1976) In Vitro, 12, pp. 670-677; Kaerber, G., Beitrag zur kollektiven behandlung pharmakologischer Reihenversuche (1931) Arch. Exp. Pathol. Pharmakol., 162, p. 480; Klumperman, J., Krijnse-Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Krijnse-Locker, J., Ericsson, M., Rottier, P.J.M., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J. Cell Biol., 124, pp. 55-70; Meertens, J., Rottier, P., Unpublished data; Pensaert, M., Haelterman, E.O., Burnstein, T., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions. 1. Immunofluorescence, histopathology and virus production in the small intestine through the course of infection (1970) Arch. Gesamte Virusforsch., 31, pp. 321-334; Pensaert, M., Haelterman, E.O., Hinsman, E.J., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions. 2. Electron microscopy of the epithelium in isolated jejunal loops (1970) Arch. Ges. Virusforsch., 31, pp. 335-351; Pfeffer, S.R., Mannose 6-phosphate receptors and their role in targeting proteins to lysosomes (1988) J. Membr. Biol., 103, pp. 7-16; Rabito, C.A., Kreisberg, J.I., Wight, D., Alkaline phosphatase and γ-glutamyl transpeptidase as polarization markers during the organization of LLC-PK1 cells into an epithelial membrane (1984) J. Biol. Chem., 259, pp. 574-582; Reynolds, E.S., The use of lead citrate at high pH as an electron-opaque stain in electron microscopy (1963) J. Cell Biol., 17, pp. 208-212; Rodriguez-Boulan, E., Nelson, W.J., Morphogenesis of the polarized epithelial cell phenotype (1989) Science, 245, pp. 718-725; Rodriguez-Boulan, E., Paskiet, K.T., Sabatini, D.D., Assembly of enveloped viruses in Madin-Darby canine kidney cells: Polarized budding from single attached cells and from clusters of cells in suspension (1983) J. Cell Biol., 96, pp. 866-874; Rodriguez-Boulan, E., Sabatini, D.D., Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 5071-5075; Schalk, A.F., Hawn, M.C., An apparently new respiratory disease of baby chicks (1931) J. Am. Vet. Med. Assoc., 78, pp. 413-422; See, H., Reithmeier, R.A., Identification and characterization of the major stilbene-disulphonate- And concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N (1990) Biochem. J., 271, pp. 147-155; Simons, K., Van Meer, G., Lipid sorting in epithelial cells (1988) Biochemistry, 27, pp. 6197-6202; Simons, K., Wandinger-Ness, A., Polarized sorting in epithelia (1990) Cell, 62, pp. 207-210; Srinivas, R.V., Blachandran, N., Alonso-Caplen, F.V., Compans, R.W., Expression of herpes simplex virus glycoproteins in polarized epithelial cells (1986) J. Virol., 58, pp. 689-693; Tashiro, M., Pritzer, E., Khoshnan, M.A., Yamakawa, M., Kuroda, K., Klenk, H.-D., Rott, R., Seto, J.T., Characterization of a pantropic variant of Sendai virus derived from a host-range mutant (1988) Virology, 165, pp. 577-583; Tashiro, M., Yamakawa, M., Tobita, K., Seto, J.T., Klenk, H.-D., Rott, R., Altered budding site of a pantropic mutant of Sendai virus, F1-R, in polarized epithelial cells (1990) J. Virol., 64, pp. 4672-4677; Tooze, J., Tooze, S.A., Fuller, S.D., Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells (1987) J. Cell Biol., 105, pp. 1215-1226; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Tucker, S.P., Compans, R.W., Virus infection of polarized epithelial cells (1993) Adv. Virus Res., 42, pp. 187-247; Van Meer, G., Simons, K., Viruses budding from either the apical or basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions (1982) EMBO J., 1, pp. 847-852; Wessels, H.P., Hansen, G.H., Fuhrer, C., Look, A.T., Sjöström, H., Norén, O., Spiess, M., Aminopeptidase N is directly sorted to the apical domain in MDCK cells (1990) J. Cell Biol., 111, pp. 2923-2930; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823","Rottier, P.J.M.; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,0022538X,,JOVIA,"7966587","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028114493
"Lin Y.-J., Liao C.-L., Lai M.M.C.","7406589398;7401957370;7401808497;","Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription",1994,"Journal of Virology","68","12",,"8131","8140",,84,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028061645&partnerID=40&md5=76267d71bec4cce2855698d7c04e777c","Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Department of Microbiology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States","Lin, Y.-J., Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Liao, C.-L., Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Department of Microbiology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States","Minus-strand RNA is the first RNA species made by plus-strand RNA viruses, such as mouse hepatitis virus (MHV), and serves as a template for subsequent RNA replication and transcription. The regulation of minus-strand RNA synthesis has been difficult to study because of the paucity of minus-strand RNA. We have optimized a ribonuclease (RNase) protection assay which enabled the detection of minus-strand RNA synthesis from nonreplicating RNAs, thus clearly separating minus-strand from plus-strand RNA synthesis. We used an MHV defective interfering (DI) RNA containing a chloramphenicol acetyltransferase gene as a reporter to determine the cis-acting signal for MHV minus-strand RNA synthesis. It was found that minus-strand RNAs existed in double-stranded RNA form in the cell. By using various deletion clones, we demonstrated that the cis-acting signal for minus-strand RNA synthesis resides in the 55 nucleotides from the 3' end plus poly(A) tail of the MHV genome. This is much shorter than the 436 nucleotides previously reported for the 3'-end replication signal. No specific upstream MHV sequence was required for the initiation of minus-strand RNA synthesis. This finding suggests that the requirement for minus-strand RNA synthesis is much less stringent than that for genomic and subgenomic plus-strand RNA synthesis and that some of the minus-strand RNAs made may not be functional since they may lack the recognition signals for RNA replication or transcription. We further showed that the DI clones which actively transcribed a subgenomic mRNA from an internal intergenic sequence synthesized much less minus-strand RNA than those clones which did not transcribe subgenomic mRNAs, indicating that minus-strand RNA synthesis was inhibited by transcription from an internal promoter of the same DI RNA. This result also suggests that the regulation of the quantities of subgenomic mRNAs is not at the point of minus-strand RNA synthesis but rather at plus-strand RNA synthesis. Furthermore, the finding that the leader sequence was not required for minus-strand RNA synthesis suggests that the leader RNA regulates mRNA transcription during plus-strand RNA synthesis.",,"chloramphenicol acetyltransferase; double stranded rna; minus strand rna; polyadenylated rna; ribonuclease; signal peptide; unclassified drug; virus rna; animal cell; article; astrocytoma cell; defective virus; mouse; murine hepatitis coronavirus; nonhuman; priority journal; rna replication; rna synthesis; rna transcription; Animal; Astrocytoma; Base Sequence; Cell Line; Chloramphenicol O-Acetyltransferase; Cytoplasm; DNA Primers; Genome, Viral; Kinetics; Mice; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Recombinant Fusion Proteins; Restriction Mapping; Ribonucleases; RNA, Double-Stranded; RNA, Viral; Signal Transduction; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Templates, Genetic; Transcription, Genetic; Transfection; Tumor Cells, Cultured",,"Lai, M.M.C.; Department of Microbiology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"7966604","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028061645
"Hart K.C., Xu Y.-F., Meyer A.N., Lee B.A., Donoghue D.J.","35611512800;16141131400;7401840204;16072667800;7005937300;","The v-sis oncoprotein loses transforming activity when targeted to the early Golgi complex",1994,"Journal of Cell Biology","127","6 II",,"1843","1857",,4,"10.1083/jcb.127.6.1843","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028604432&doi=10.1083%2fjcb.127.6.1843&partnerID=40&md5=88948e654b22f38de6e0028cc557b6c3","Dept. of Chemistry and Biochemistry, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Center for Molecular Genetics, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Department of Biology, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Molecular Pathology Program, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Ligand Pharmaceuticals, Inc., San Diego, CA 92121, United States; IXSYS, Inc., San Diego, CA 92121, United States; Dept. of Chemistry/Biochemistry, UCSD/Center for Molecular Genetics, San Diego, CA 92093-0322, United States","Hart, K.C., Molecular Pathology Program, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Xu, Y.-F., Dept. of Chemistry and Biochemistry, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States, Ligand Pharmaceuticals, Inc., San Diego, CA 92121, United States; Meyer, A.N., Dept. of Chemistry and Biochemistry, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States; Lee, B.A., Department of Biology, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States, IXSYS, Inc., San Diego, CA 92121, United States; Donoghue, D.J., Dept. of Chemistry and Biochemistry, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States, Center for Molecular Genetics, School of Medicine, University of California, San Diego, San Diego, CA 92093-0322, United States, Dept. of Chemistry/Biochemistry, UCSD/Center for Molecular Genetics, San Diego, CA 92093-0322, United States","The location of autocrine interactions between the v-sis protein and PDGF receptors remains uncertain and controversial. To examine whether receptor- ligand interactions can occur intracellularly, we have constructed fusion proteins that anchor v-sis to specific intracellular membranes. Fusion of a cis-Golgi retention signal from a coronavirus E1 glycoprotein to v-sis protein completely abolished its transforming ability when transfected into NIH3T3 cells. Fusion proteins incorporating mutations in this retention signal were not retained within the Golgi complex but instead were transported to the cell surface, resulting in efficient transformation. All chimeric proteins were shown to dimerize properly. Derivatives of some of these constructs were also constructed bearing the cytoplasmic tail from the glycoprotein of vesicular stomatitis virus (VSV-G). These constructs allowed examination of subcellular localization by double-label immunofluorescence, using antibodies that distinguish between the extracellular PDGF-related domain and the VSV-G cytoplasmic tail. Colocalization of sis-E1-G with Golgi markers confirmed its targeting to the early Golgi complex. The sis-E1 constructs, targeted to the early Golgi complex, exhibited no proteolytic processing whereas the mutant forms of sis-E1 exhibited normal proteolytic processing. Treatment with suramin, a polyanionic compound that disrupts ligand/receptor interactions at the cell surface, was able to revert the transformed phenotype induced by the mutant sis-E1 constructs described here. Our results demonstrate that autocrine interactions between the v-sis oncoprotein and PDGF receptors within the early Golgi complex do not result in functional signal transduction. Another v-sis fusion protein was constructed by attaching the transmembrane domain and COOH-terminus of TGN38, a protein that localizes to the trans-Golgi network (TGN). This construct was primarily retained intracellularly, although some of the fusion protein reached the surface. Deletion of the COOH-terminal region of the TGN38 retention signal abrogated the TGN-localization, as evidenced by very prominent cell surface localization, and resulted in increased transforming activity. The behavior of the sis-TGN38 derivatives is discussed within the context of the properties of TGN38 itself, which is known to recycle from the cell surface to the TGN.",,"hybrid protein; oncoprotein; platelet derived growth factor receptor; animal cell; article; golgi complex; nonhuman; priority journal; protein localization; protein protein interaction; structure activity relation; vesicular stomatitis virus; 3T3 Cells; Amino Acid Sequence; Animal; Base Sequence; Biological Markers; Biological Transport; Cell Compartmentation; Cell Membrane; Cell Transformation, Neoplastic; Fluorescent Antibody Technique; Golgi Apparatus; Membrane Glycoproteins; Mice; Molecular Sequence Data; Oncogene Proteins v-sis; Protein Sorting Signals; Receptor, Platelet-Derived-Growth Factor beta; Receptors, Platelet-Derived Growth Factor; Recombinant Fusion Proteins; Retroviridae Proteins, Oncogenic; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Suramin; Viral Envelope Proteins; Animalia; Coronavirus; Vesicular stomatitis virus",,"Donoghue, D.J.; Dept. of Chemistry/Biochemistry, UCSD/Center for Molecular Genetics, San Diego, CA 92093-0322, United States",,,00219525,,JCLBA,"7806564","English","J. CELL BIOL.",Article,"Final",Open Access,Scopus,2-s2.0-0028604432
"Pohl-Koppe A., Raabe T., Siddell S.G., ter Meulen V.","6701475179;56250084700;7005260816;7102867070;","Detection of human coronavirus 229E-specific antibodies using recombinant fusion proteins",1995,"Journal of Virological Methods","55","2",,"175","183",,10,"10.1016/0166-0934(95)00041-R","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028832731&doi=10.1016%2f0166-0934%2895%2900041-R&partnerID=40&md5=c1cba92462ab6df05c3f85a0c9c1a149","Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","Pohl-Koppe, A., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Raabe, T., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; ter Meulen, V., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","Human coronaviruses are known to be a common cause of respiratory infections in man. However, the diagnosis of human coronavirus infections is not carried out routinely, primarily because the isolation and propagation of these viruses in tissue culture is difficult and time consuming. The aim of this study was to evaluate the use of recombinant, bacterial expressed proteins in the serodiagnosis of coronavirus infections. Two proteins were examined: the human coronavirus 229E nucleocapsid protein (N), expressed as a fusion protein in the vector pUR and the coronavirus 229E surface glycoprotein (S), expressed as a fusion protein in the vector pROS. The recombinant proteins were used as antigens in Western blot (WB) assays to detect the 229E-specific IgG antibodies and the results were compared with a standard serological method, indirect immunofluorescence. Serum samples of 51 paediatric patients, suffering from acute respiratory illness, and 10 adults, voluntarily infected with human coronavirus, were tested. The serum samples of the adult group had coronavirus-specific IgG antibodies in both test systems. In contrast, only 8 51 sera of the paediatric group were positive for coronavirus-specific IgG by both WB and IF and 20 51 sera were positive by WB, but not by IF. The overall incidence of human coronavirus infections in the paediatric age group was 55% evaluated by WB analysis and 16% evaluated by IF. This study shows that recombinant human coronavirus 229E proteins are suitable reagents for the epidemiological screening of coronavirus 229E infections. © 1995.","229E; Antibody detection; Bacterial fusion protein; Coronavirus","hybrid protein; recombinant protein; adult; antibody detection; article; child; clinical article; clinical trial; controlled clinical trial; controlled study; Coronavirus; diagnostic value; human; priority journal; serodiagnosis; virus detection; virus infection; Bacteria (microorganisms); Coronavirus; human coronavirus; Human coronavirus 229E","Ellinger, Glockshuber, Jahn, Plückthun, Cleavage of procaryotically expressed human immunodeficiency virus fusion proteins by factor Xa and application in western blot (immunoblot) assays (1989) J. Clin. Microbiol., 27, pp. 971-976; Harlow, Lane, (1988) Antibodies. A Laboratory Manual, , Cold Spring Harbor Press, Cold Spring Harbor, NY; Henle, Henle, Horowitz, Epstein-Barr virus specific diagnostic tests in infectious mononucleosis (1974) Hum. Pathol., 5, pp. 551-555; Herold, Raabe, Siddell, Molecular analysis of the human coronavirus (strain 229E) genome (1993) Arch. Virol., 7, pp. 63-74. , (suppl.); Hierholzer, Tannock, Coronaviridae: the coronaviruses (1988) Viral, Rickettsial and Chlamydial Diseases, 2, pp. 451-483. , E.H. Lennette, F. Halonen, F.A. Murphy, Laboratory Diagnoses of Infectious Diseases. Principles and Practices, Springer Verlag, New York; Kraaijeveld, Reed, Macnaughton, Enzyme-linked immunosorbent assay for detection of antibody in volunteers experimentally infected with human coronavirus strain 229E (1980) J. Clin. Microbiol., 12, pp. 493-497; Macnaughton, Occurrence and frequency of coronavirus infections in humans as determined by enzyme-linked immunosorbent assay (1982) Infect. Immun., 28, pp. 419-423; Macnaughton, Madge, Reed, Two antigenic groups of human coronaviruses detected by using enzyme linked immunoabsorbent assay (1981) Infect. Immun., 33, pp. 734-737; McIntosh, McQuillin, Reed, Gardner, Diagnosis of human coronavirus infection by immunofluorescence: method and application to respiratory disease in hospitalised children (1978) J. Med. Virol., 2, pp. 341-346; Matsumoto, Kawana, Virological surveillance of acute respiratory tract illness in children in Morioka, Japan. III. Human respiratory coronavirus (1992) Kansenshogaku Zasshi, 66, pp. 319-326; Monto, Rhodes, Detection of coronavirus infection of man by immunofluorescence (1977) Proc. Soc. Exp. Biol. Med., 155, pp. 143-148; Myint, Siddell, Tyrell, The detection of human coronavirus 229E in nasal washings using RNA-RNA hybridisation (1989) J. Med. Virol., 19, pp. 70-73; Myint, Harnsen, Raabe, Siddell, Characterisation of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) J. Med. Virol., 31, pp. 165-172; Myint, Johnston, Sanderson, Simpson, Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell Probes, 8, pp. 357-364; Pattemore, Johnston, Bardin, Viruses as precipitants of asthma symptoms. I. Epidemiology (1992) Clin. Exp. Allergy, 22, pp. 325-336; Raabe, Siddell, Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 and mRNA 5 unique regions (1989) Nucleic Acids Res., 17, p. 6387; Raabe, Siddell, Nucleotide sequence encoding the membrane protein of human coronavirus 229E (1989) Arch. Virol., 107, pp. 323-328; Raabe, Schelle-Prinz, Siddell, Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Rüther, Müller-Hill, Easy identification of cDNA clones (1983) EMBO J, 2, pp. 1791-1794; Schreiber, Kamahora, Lai, Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Schmidt, Kenny, Immunogenicity and antigenicity of human coronaviruses HCV 229E and OC 43 (1982) Infect. Immun., 32, pp. 1000-1006; Strebel, Beck, Strohmaier, Schaller, Characterization of foot-and-mouth disease virus gene products with antisera against bacterially sythesized fusion proteins (1986) J. Virol., 57, pp. 983-991","Pohl-Koppe, A.; Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany",,,01660934,,JVMED,"8537456","English","J. Virol. Methods",Article,"Final",,Scopus,2-s2.0-0028832731
"Tsunemitsu H., El-Kanawati Z.R., Smith D.R., Reed H.H., Saif L.J.","7004628959;6505831008;7410366749;7005362314;7102226747;","Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea",1995,"Journal of Clinical Microbiology","33","12",,"3264","3269",,53,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028818061&partnerID=40&md5=879c1c052a3dc031068d5f26624e7bf0","Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States","Tsunemitsu, H., Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States; El-Kanawati, Z.R., Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States; Smith, D.R., Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States; Reed, H.H., Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States","Diarrheal feces from three sambar deer and one waterbuck in a wild animal habitat and one white-tailed deer on a wildlife farm in Ohio contained coronavirus particles which were agglutinated by antiserum to bovine coronavirus (BCV) in immune electron microscopy. Three coronavirus strains were isolated in human rectal tumor cells from the feces of the sambar and white-tailed deer and the waterbuck, respectively. Hemagglutination, receptor-destroying enzyme activity, indirect immunofluorescence, hemagglutination inhibition, virus neutralization, and Western blot (immunoblot) tests showed close biological and antigenic relationships among the isolates and with selected BCV strains, Gnotobiotic and colostrum- deprived calves inoculated with each of these isolates developed diarrhea and shed coronavirus in their feces and from their nasal passages. In a serological survey of coronavirus infections among wild deer, 8.7 and 6.6% of sera from mule deer in Wyoming and from white-tailed deer in Ohio, respectively, were seropositive against both of the isolates and selected BCV isolates by indirect immunofluorescence tests. These results confirm the existence of coronaviruses in wild ruminants and suggest that these species may harbor coronavirus strains transmissible to cattle.",,"virus antibody; animal experiment; antibody response; article; bovids; coronavirus; deer; diarrhea; enzyme activity; feces analysis; hemagglutination; immunoblotting; immunoelectron microscopy; immunofluorescence; nonhuman; priority journal; virus infection; virus isolation; virus neutralization; virus particle; Animal; Antibodies, Viral; Antigens, Viral; Cattle; Cattle Diseases; Cell Line; Chickens; Coronavirus; Coronavirus Infections; Coronavirus, Bovine; Deer; Diarrhea; Feces; Hemagglutination Tests; Human; Mice; Microscopy, Immunoelectron; Ruminants; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.",,"Saif, L.J.; Food Animal Health Research Program, Ohio Agricultural Research/Dev. Ctr., Ohio State University, Wooster, OH 44691, United States",,,00951137,,JCMID,"8586714","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0028818061
"Rossen J.W.A., Horzinek M.C., Rottler P.J.M.","7005977394;7102624836;25938717600;","Coronavirus infection of polarized epithelial cells",1995,"Trends in Microbiology","3","12",,"486","490",,13,"10.1016/S0966-842X(00)89018-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028866191&doi=10.1016%2fS0966-842X%2800%2989018-6&partnerID=40&md5=018a21d792dd659e83e42f444a99b41d","Virology Divn of the Dept of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Rossen, J.W.A., Virology Divn of the Dept of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Divn of the Dept of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottler, P.J.M., Virology Divn of the Dept of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Epithelial cells are the first host cells to be infected by incoming coronaviruses. Recent observations in vitro show that coronaviruses are released from a specific side of these polarized cells, and this polarized release might be important for the spread of the infection in vivo. Mechanisms for the directional sorting of coronaviruses might be similar to those governing the polar release of secretory proteins. © 1995.",,"cell polarity; coronavirus; epithelium cell; human; in vitro study; nonhuman; priority journal; short survey; ultrastructure; virus cell interaction; Animal; Coronavirus; Epithelium; Human; Murine hepatitis virus; Virus Replication","Tucker, Compans, (1993) Adv. Virus Res., 42, pp. 187-247; Rodriguez-Boulan, Sabatini, Asymmetric budding of viruses in epithelial monlayers: a model system for study of epithelial polarity. (1978) Proceedings of the National Academy of Sciences, 75, pp. 5071-5075; Tashiro, (1990) J. Virol., 64, pp. 4672-4677; Holmes, (1990) Virology, 1, pp. 841-856. , B.N. Fields et al., Raven Press; Krijnse-Locker, (1994) J. Cell Biol., 124, pp. 55-70; Tooze, Tooze, Warren, (1984) Eur. J. Cell Biol., 33, pp. 281-293; Tooze, Tooze, Fuller, (1987) J. Cell Biol., 105, pp. 1215-1226; Doughri, Storz, (1977) Zentralbl. Veterinarmed. Reihe B, 24, pp. 367-385; Ishida, Fujiwara, (1979) Jpn. J. Exp. Med., 49, pp. 33-41; Reynolds, (1985) Arch. Virol., 85, pp. 71-83; Wojcinski, Percy, (1986) Vet. Pathol., 23, pp. 278-286; O'Toole, (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, Haelterman, Hinsman, (1970) Arch. Gesamte Virusforsch., 31, pp. 335-351; Barthold, Beck, Smith, (1993) Lab. Anim. Sci., 43, pp. 276-284; Weingartl, Derbyshire, (1994) J. Virol., 68, pp. 7253-7259; Barthold, (1987) Lab. Anim. Sci., 37, pp. 36-40; Compton, Barthold, Smith, (1993) Lab. Anim. Sci., 43, pp. 15-28; Wang, (1992) Lab. Anim. Sci., 66, pp. 744-754; Robbins, (1990) Lab. Invest., 62, pp. 417-426; Butcher, Winterfield, Shapiro, (1990) Avian Dis., 34, pp. 916-921; Condron, Marshall, (1986) J. Comp. Pathol., 96, pp. 47-61; Afzelius, (1994) Virchows Arch. A Pathol. Anat., 424, pp. 295-300; Rossen, (1995) Virology, 210, pp. 54-66; Rossen, (1994) J. Virol., 68, pp. 7966-7973; Halban, Irminger, (1994) Biochem. J., 299, pp. 1-18; Pfeffer, (1988) J. Membr. Biol., 103, pp. 7-16; Baron, Polarized secretion of lysosomal enzymes: co-distribution of cation- independent mannose-6-phosphate receptors and lysosomal enzymes along the osteoclast exocytic pathway (1988) The Journal of Cell Biology, 106, pp. 1863-1872","Rossen, J.W.A.; Virology Divn of the Dept of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,0966842X,,TRMIE,"8800844","English","Trends Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0028866191
"Sizun J., Soupre D., Legrand M., Giroux J., Rubio S., Cauvin J., Chastel C., Mix D., Parscau L.d.","35605340000;6602842875;7102317918;17934302900;7006260573;57191434614;57197376300;57191436257;6505562318;","Neonatal nosocomial respiratory infection with coronavirus: a prospective study in a neonatal intensive care unit",1995,"Acta Pædiatrica","84","6",,"617","620",,40,"10.1111/j.1651-2227.1995.tb13710.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029062540&doi=10.1111%2fj.1651-2227.1995.tb13710.x&partnerID=40&md5=2bfe2db6da13849acb4abe2e4d9a3126","Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Department of Microbiology, University Hospital, Brest, France; Medical Information Department, University Hospital, Brest, France","Sizun, J., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Soupre, D., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Legrand, M., Department of Microbiology, University Hospital, Brest, France; Giroux, J., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Rubio, S., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Cauvin, J., Medical Information Department, University Hospital, Brest, France; Chastel, C., Department of Microbiology, University Hospital, Brest, France; Mix, D., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France; Parscau, L.d., Department of Pediatric and Neonatal Intensive Care Unit, University Hospital, Brest, France","The aim of this prospective study was to evaluate the incidence of viral respiratory infection in hospitalized premature newborn infants and to assess the role of coronaviruses. All hospitalized premature infants with a gestational age less than or equal to 32 weeks were included. Tracheal or nasopharyngal specimens were studied by immunofluorescence for coronaviruses, respiratory syncytial virus, adenoviruses, influenza and parainfluenza viruses. Forty premature infants were included; 13 samples were positive in 10 newborns (coronaviruses n = 10; influenza 1 n= 2; adenovirus n= 1). None was positive at admission. All premature infants infected with coronaviruses had symptoms of bradycardia, apnea, hypoxemia, fever or abdominal distension. Chest X‐ray revealed diffuse infiltrates in two cases. However, no significant difference was observed between infected and non‐infected premature infants for gestational age, birth weight, duration of ventilation, age at discharge, incidence of apnea or bradycardia. Nosocomial respiratory tract infection with coronaviruses appears to be frequent. The clinical consequences should be evaluated in a larger population. Copyright © 1995, Wiley Blackwell. All rights reserved","Coronavirus infections; prematurity; viral infections","article; clinical article; coronavirus; hospital infection; human; incidence; newborn; newborn intensive care; prematurity; priority journal; prospective study; respiratory tract infection; thorax radiography; virus infection; Body Fluids; Coronavirus; Coronavirus Infections; Cross Infection; Female; Human; Incidence; Infant, Newborn; Infant, Premature; Infant, Premature, Diseases; Intensive Care Units, Pediatric; Male; Prospective Studies; Respiratory Tract Infections","Abzug, MJ, Beam, AC, Gyorkos, EA, Viral pneumonia in the first month of life (1990) Pediatr Infect Dis J, 9, pp. 881-885; Gouyon, JB, Fantino, M, Couillault, G, Infections a virus respiratoire syncitial du nouveau‐ne (1986) Arch Fr Pediatr, 43, pp. 93-97; Hall, CB, Kopelman, AE, Douglas, G, Neonatal respiratory syncitial virus infection (1979) N Engl J Med, 300, pp. 393-396; Abzug, MJ, Levin, MJ, Neonatal adenovirus infection (1991) Pediatrics, 87, pp. 890-896; Jenista, JA, Powell, KR, Menegus, MA, Epidemiology of neonatal enterovirus infection (1984) J Pediatr, 104, pp. 685-690; Sizun, J, Soupre, D, Giroux, JD, Nasal colonization with coronavirus and apnea of the premature newborn (1993) Acta Paediatr, 82, p. 238; Bradburne, AF, Tyrell, DAJ., Coronaviruses of man (1971) Prog Med Virol, 13, pp. 373-403; Bradburne, AF, Bynoe, ML, Tyrrell, DAJ., (1967), pp. 767-769. , Effects of a “new” human respiratory virus in volunteers. BMJ, ;23 Septem‐ber; Riski, H, Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J Med Virol, 6, pp. 259-265; Mcintosh, K, Chao, RK, Krause, HE, Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Mcintosh, K, McQuillin, J, Reed, SE, Gardner, PS, Diagnosis of human coronavirus infection by immunofluorescence : method and application to respiratory disease in hospitalized children (1978) J Med Virol, 2, pp. 341-346; Ray, CG, Holberg, CJ, Minnich, LL, Acute lower respiratory illnesses during the first three years of life: potential roles for various etiologic agents (1993) Pediatr Infect Dis J, 12, pp. 10-14; Monto, AS, Coronaviruses (1991) Viral infections of humans‐‐‐epidemiology and control, , 3rd ed., New York:, AS Evans; Chany, C, Moscovici, O, Lebon, P, Association of coronavirus infection with neonatal necrotizing enterocolitis (1982) Pediatrics, 69, pp. 209-214; Sizun, J, Soupre, D, Giroux, JD, Rôle pathogene des coronavirus en reanimation pédiatrique: analyse retrospective de 19 prelevements positifs en immunofluorescence indirecte (1994) Arch Fr Pediatr, 1, pp. 477-480; Homberger, FR, Smith, AL, Barthold, SW, Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J Clin Microbiol, 29, pp. 2789-2793","Sizun, J.; Department of Pediatrics and Neonatal Intensive Care Unit, University Hospital, Brest, 29609, France",,,08035253,,,"7670241","English","Acta Paediatr. Int. J. Paediatr.",Article,"Final",Open Access,Scopus,2-s2.0-0029062540
"Tahir R.A., Pomeroy K.A., Goyal S.M.","55987643500;7003520694;7202441793;","Evaluation of shell vial cell culture technique for the detection of bovine coronavirus",1995,"Journal of Veterinary Diagnostic Investigation","7","3",,"301","304",,5,"10.1177/104063879500700301","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029337638&doi=10.1177%2f104063879500700301&partnerID=40&md5=de3d3a3089ac6b8dcda5f86620936753","Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States","Tahir, R.A., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States; Pomeroy, K.A., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States; Goyal, S.M., Department of Veterinary Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States","The effect of blind passage and centrifugation on the isolation of bovine coronavirus in human rectal tumor cells cultured in shell vials was investigated. A total of 68 fecal samples known to be positive for bovine coronavirus by transmission electron microscopic (TEM) examination were used. The samples were centrifuged onto human rectal tumor cell monolayers and incubated in the presence of trypsin. The growth of bovine coronavirus in infected cells was demonstrated by fluorescent antibody staining, and the extracellular virus was detected and confirmed by hemagglutination and hemagglutination-inhibition tests, respectively. Of the 68 TEM-positive samples, 51 (75%), 58 (85%), and 61 (90%) grew in shell vial cell cultures at first, second, and third passages, respectively. Of the 51 cultures positive on first passage, 19 were examined by TEM; 18 of these were positive for bovine coronavirus. The shell vial technique was also compared with direct detection of bovine coronavirus by staining cryostat sections of infected tissues in a direct fluorescent antibody assay. The results of direct fluorescent antibody assay were available for 54 of the 68 samples, of which 53 (98%) and 43 (80%) were positive by shell vial technique and direct fluorescent antibody assay, respectively. For identification of bovine coronavirus, shell vials using human rectal tumor cells in the presence of trypsin is more sensitive than direct fluorescent antibody assay but is relatively less sensitive than transmission electron microscopy. © 1995, American Association of Veterinary Laboratory Diagnosticians. All rights reserved.",,"animal; animal disease; article; cattle; cattle disease; cell culture; cell line; Coronavirus; electron microscopy; feces; gastroenteritis; growth, development and aging; hemagglutination inhibition test; hemagglutination test; human; isolation and purification; methodology; rectum tumor; tissue culture; virology; virus infection; Animal; Cattle; Cattle Diseases; Cell Line; Coronavirus Infections; Coronavirus, Bovine; Feces; Gastroenteritis; Hemagglutination Inhibition Tests; Hemagglutination Tests; Human; Microscopy, Electron; Rectal Neoplasms; Tissue Culture; Tumor Cells, Cultured","Akashi, H., Inaba, Y., Miura, Y., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet Microbiol, 5, pp. 265-276; Bonville, C.A., Forbes, B.A., Bartholoma, N., Rapid detection of herpes simplex virus in MRC-5 cells using low-speed centrifugation enhancement and immunoperoxidase staining, 16 h post-inoculation (1987) Diagn Microbial Infect Dis, 8, pp. 251-254; Bridger, J.C., Wood, G.N., Meling, A., Isolation of coronavirus from neonatal calf diarrhea in Britain and Denmark (1978) Vet Microbial, 3, pp. 101-113; Buxton, A., Fraser, G., Isolation, cultivation and identification procedures in diagnostic virology (1977) Anim Microbiol, 2, pp. 475-509; Cyr-Coats, K., Cyr-Coats, S.T., Storz, J., Bovine coronavirus-induced cytopathic expression and plaque formation: Host cell and virus strain determine trypsin dependence (1988) J Vet Med, 35, pp. 48-56; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation and cultivation in continuous cell lines (1979) Am J Vet Res, 41, pp. 30-38; Gleaves, C.A., Smith, T.F., Shuster, E.A., Pearson, G.R., Rapid detection of cytomegalovirus in MRC-5 cells inoculated with urine specimens by using low-speed centrifugation and monoclonal antibody to an early antigen (1984) J Clin Microbiol, 19, pp. 917-919; Goyal, S.M., Rademacher, R.A., Pomeroy, K.A., Comparison of electron microscopy with three commercial tests for the detection of rotavirus in animal feces (1987) Diagn Microbiol Infect Dis, 6, pp. 249-254; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet Microbiol, 22, pp. 187-201; House, J.A., Economics of the rotavirus and other neonatal disease agents of animals (1978) J Am Vet Med Assoc, 173, pp. 573-576; Inaba, Y., Sato, K., Kurogi, H., Replication of bovine coronavirus in cell line BEK-1 culture (1976) Arch Virol, 50, pp. 339-342; Kapil, S., Pomeroy, K.A., Goyal, S.M., Trent, A.M., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J Vet Diagn Invest, 3, pp. 88-89; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am J Vet Res, 40, pp. 1476-1478; Laporte, J., Haridon, R.L., Bobulesco, P., In vitro culture of bovine enteric coronavirus (BEC) (1979) Colloq I'INSERM Enterites Virales/Viral Enteritis, 90, pp. 99-102; Matthey, S., Nicholson, D., Ruhs, S., Rapid detection of respiratory viruses by shell vial culture and direct staining by using pooled and individual monoclonal antibodies (1992) J Clin Microbiol, 30, pp. 540-544; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-434; Naeem, K., Goyal, S.M., Comparison of virus isolation, immunofluorescence and electron microscopy for the diagnosis of animal viruses (1988) Microbiologica, 11, pp. 355-362; Osorio, F.A., Moxley, R.A., Arevalo, A., Srikumaran, S., Enhanced infectivity assays which are compatible with rapid viral diagnosis (1986) Proc Annu Meet Am Assoc Vet Lab Diagn, 29, pp. 303-316; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet Rec, 123, pp. 300-301; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Stair, L.E., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am J Vet Res, 33, pp. 1147-1156; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J Virol, 56, pp. 904-911; Tahir, R.A., Goyal, S.M., Rapid detection of pseudorabies virus by shell vial technique (1995) J Vet Diagn Invest, 7, pp. 173-176; Takahashi, E., Inaba, Y., Sato, K., Epizootic diarrhoea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbial, 5, pp. 151-154; Tompkins, W.A.F., Watrach, A.M., Schmale, J.D., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 1101-1110; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Vautherot, J.F., Laporte, J., Utilization of monoclonal antibodies for antigenic characterization of coronaviruses (1983) Ann Rech Vet, 14, pp. 437-1144",,,,10406387,,,"7578442","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0029337638
"Peng D., Koetzner C.A., McMahon T., Zhu Y., Masters P.S.","7202530662;6602982748;57198331629;57212262773;7006234572;","Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins",1995,"Journal of Virology","69","9",,"5475","5484",,55,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029117953&partnerID=40&md5=1bd4fa325913ea952e178b50fec46b74","New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States","Peng, D., New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States; Koetzner, C.A., New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States; McMahon, T., New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States; Zhu, Y., New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States; Masters, P.S., New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States","Targeted RNA recombination was used to construct mouse hepatitis virus (MHV) mutants containing chimeric nucleocapsid (N) protein genes in which segments of the bovine coronavirus N gene were substituted in place of their corresponding MHV sequences. This defined portions of the two N proteins that, despite evolutionary divergence, have remained functionally equivalent. These regions included most of the centrally located RNA-binding domain and two putative spacers that link the three domains of the N protein. By contrast, the amino terminus of N, the acidic carboxy-terminal domain, and a serine- and arginine-rich segment of the central domain could not be transferred from bovine coronavirus to MHV, presumably because these parts of the molecule participate in protein-protein interactions that are specific for each virus (or, possibly, each host). Our results demonstrate that targeted recombination can be used to make extensive substitutions in the coronavirus genome and can generate recombinants that could not otherwise be made between two viruses separated by a species barrier. The implications of these findings for N protein structure and function as well as for coronavirus RNA recombination are discussed.",,"methionine; sulfur 35; virus protein; virus rna; amino acid substitution; animal cell; article; genetic recombination; molecular cloning; mouse; murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; protein protein interaction; sequence homology; virus mutant; virus nucleocapsid; virus recombinant; Amino Acid Sequence; Animal; Base Sequence; Capsid; Cell Line; Chimeric Proteins; Coronavirus, Bovine; Crossing Over (Genetics); DNA, Ribosomal; Evolution; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Oligodeoxyribonucleotides; Plasmids; Recombination, Genetic; Repetitive Sequences, Nucleic Acid; Restriction Mapping; RNA, Viral; Species Specificity; Support, U.S. Gov't, P.H.S.; Variation (Genetics); Viral Core Proteins",,"Masters, P.S.; New York State Department of Health, Wadsworth Center, New Scotland Ave., Albany, NY 12201-2002, United States",,,0022538X,,JOVIA,"7636993","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029117953
"Krempl C., Schultze B., Herrler G.","6602462665;7006104520;7006339246;","Analysis of cellular receptors for human coronavirus OC43",1995,"Advances in Experimental Medicine and Biology","380",,,"371","374",,28,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028820443&partnerID=40&md5=34fdc3a3c59db66d2b582315f78414be","Institut for Virologie, Philipps-Universitat Marburg, Marburg, Germany","Krempl, C., Institut for Virologie, Philipps-Universitat Marburg, Marburg, Germany; Schultze, B., Institut for Virologie, Philipps-Universitat Marburg, Marburg, Germany; Herrler, G., Institut for Virologie, Philipps-Universitat Marburg, Marburg, Germany","Bovine coronavirus (BCV), human coronavirus OC43 (HCV-OC43) and hemagglutinating encephalomyelitis virus (HEV) are serologically related viruses that all have hemagglutinating activity. The receptor determinant for attachment to erythrocytes has been shown to be N-acetyl-9-O-acetylneuraminic acid (Neu5,9Ac2). We compared the ability of the three coronaviruses to recognize 9-O-acetylated sialic acid and found that they all bind to Neu5.9Ac2 attached to galactose in either A2,3 or A2,6-linkage. There are, however, some differences in the minimum amount of sialic acid that is required on the cell surface for agglutination by these viruses. Evidence is presented that HCV-OC43 uses Neu5,9Ac2 as a receptor determinant not only for agglutination of erythrocytes but also for attachment to and infection of a cultured cell line, MDCK I cells.",,"cell receptor; n acetylneuraminic acid; sialic acid; animal cell; conference paper; coronavirus; dog; erythrocyte; hemagglutination; nonhuman; priority journal; Animal; Carbohydrate Conformation; Carbohydrate Sequence; Cattle; Cell Line; Comparative Study; Coronavirus; Coronavirus OC43, Human; Coronavirus, Bovine; Erythrocytes; Hemagglutination; Human; Molecular Sequence Data; Receptors, Virus; Sialic Acids",,"Krempl, C.; Institut for Virologie, Philipps-Universitat Marburg, Marburg, Germany",,,00652598,,AEMBA,"8830510","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028820443
"Hogue B.G.","7003393593;","Bovine coronavirus nucleocapsid protein processing and assembly",1995,"Advances in Experimental Medicine and Biology","380",,,"259","263",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028810792&partnerID=40&md5=bbd2d551c41b28d9c2f71f5c5d0dd5b5","Division of Molecular Virology, Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX, United States","Hogue, B.G., Division of Molecular Virology, Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX, United States","The coronavirus nucleocapsid protein (N) encapsidates the genomic RNA to form a helical nucleocapsid. The requirements for coronavirus nucleocapsid assembly are being studied. Two forms (~50 kDa and 55 kDa) of the bovine coronavirus (BCV) N protein were detected in infected cells. However, only one form, a 50 kDa species, was detected in extracellular virions. After treatment with calf intestinal alkaline phosphatase (CIAP), the 55 kDa intracellular form increased in mobility to comigrate with the 50 kDa form; whereas, the 50 kDa intracellular species and N from extracellular virions was not sensitive to CIAP treatment. The data indicate that specificity exists with regard to assembly of N into the mature virion. The data suggests that processing of N may take place during assembly of either nucleocapsids or virions and that the processing may be a dephosphorylation event.",,"alkaline phosphatase; virus protein; animal cell; cell strain bhk; conference paper; coronavirus; dephosphorylation; nonhuman; priority journal; protein assembly; protein processing; protein transport; virion; virus nucleocapsid; Alkaline Phosphatase; Animal; Capsid; Cattle; Cell Line; Comparative Study; Coronavirus, Bovine; Hamsters; Intestines; Kidney; Molecular Weight; Protein Processing, Post-Translational; Protein Structure, Secondary; RNA, Viral; Viral Core Proteins; Virion",,"Hogue, B.G.; Division of Molecular Virology, Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX, United States",,,00652598,,AEMBA,"8830489","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028810792
"Zhang X.M., Lai M.M.C.","55715175900;7401808497;","Regulation of coronavirus RNA transcription is likely mediated by protein- RNA interactions",1995,"Advances in Experimental Medicine and Biology","380",,,"515","521",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028820448&partnerID=40&md5=455e2efa4b5ebba7aec339290292b035","Department of Neurology, So. California Univ. School of Med., Los Angeles, CA, United States","Zhang, X.M., Department of Neurology, So. California Univ. School of Med., Los Angeles, CA, United States; Lai, M.M.C., Department of Neurology, So. California Univ. School of Med., Los Angeles, CA, United States","Coronavirus mRNA transcription was thought to be regulated by the interaction between the leader RNA and the intergenic (IG) sequence, probably involving direct RNA-RNA interactions between complementary sequences. In this study, we found that a 9-nucleotide sequence immediately downstream of the leader RNA up-regulated mRNA transcription and that a particular strain of mouse hepatitis virus (MHV) lacking this 9-nucleotide transcribed subgenomic mRNA species containing unusually heterogeneous leader-fusion sites. These results suggest that the sequence complementarity between the leader and IG is not necessarily required for mRNA transcription. UV cross- linking experiments using cytoplasmic extracts of uninfected cells and the IG sequence showed that three different cellular proteins bound to IG of the template RNA. Deletion analyses and site-directed mutagenesis of IG further demonstrated a correlation between protein-binding and transcription efficiency, suggesting that these RNA-binding proteins are involved in the regulation of coronavirus mRNA transcription. We propose that coronavirus transcription is regulated by RNA-protein and protein-protein interactions.",,"messenger rna; rna binding protein; transcription factor; virus rna; animal cell; conference paper; controlled study; coronavirus; messenger rna synthesis; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein protein interaction; rna sequence; transcription regulation; virus transcription; Animal; Base Sequence; Gene Expression Regulation, Viral; Introns; Mice; Molecular Sequence Data; Murine hepatitis virus; Repetitive Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; RNA-Binding Proteins; Sequence Deletion; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Transfection",,"Zhang, X.M.; Department of Neurology, So. California Univ. School of Med., Los Angeles, CA, United States",,,00652598,,AEMBA,"8830534","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028820448
"Theil K.W., Mccloskey C.M.","7007118952;6701570972;","Rotavirus Shedding in Feces of Gnotobiotic Calves Orally Inoculated with a Commercial Rotavirus-Coronavirus Vaccine",1995,"Journal of Veterinary Diagnostic Investigation","7","4",,"427","432",,10,"10.1177/104063879500700401","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029382506&doi=10.1177%2f104063879500700401&partnerID=40&md5=4835c702b13f1134dae694a56993569d","Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States","Theil, K.W., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States; Mccloskey, C.M., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States","The purpose of this study was to monitor by negative stain electron microscopy the shedding of rotavirus in the feces of gnotobiotic calves orally inoculated with a commercial modified live bovine rotavirus-bovine coronavirus vaccine. Negative stain electron microscopic examination detected vaccine rotavirus in only 1 of 41 daily fecal specimens collected from 3 gnotobiotic calves during the 2 weeks following oral inoculation with a US Department of Agriculture-licensed modified live bovine rotavirus-bovine coronavirus vaccine. In contrast, rotavirus was demonstrable by the same negative stain electron microscopic examination procedure in 17 of 19 fecal specimens collected from diarrheic gnotobiotic or colostrum-deprived calves during the first 8 days after inoculation with virulent bovine rotavirus field strains. Rotavirus was also detected by this procedure in 4 enzyme-linked immunosorbent assay positive fecal specimens collected from naturally-infected diarrheic dairy calves. These results suggest that fecal shedding of vaccine rotavirus demonstrable by electron microscopic examination is uncommon following oral inoculation of calves with the bovine rotavirus-bovine coronavirus vaccine. © 1995, American Association of Veterinary Laboratory Diagnosticians. All rights reserved.",,"immunoglobulin G; immunoglobulin M; virus antibody; virus vaccine; animal; article; blood; cattle; colostrum; comparative study; Coronavirus; electron microscopy; feces; germfree animal; immunization; immunodiffusion; immunology; isolation and purification; Rotavirus; ultrastructure; virology; virus shedding; Animals; Antibodies, Viral; Cattle; Colostrum; Coronavirus; Feces; Germ-Free Life; Immunization; Immunodiffusion; Immunoglobulin G; Immunoglobulin M; Microscopy, Electron; Rotavirus; Viral Vaccines; Virus Shedding","Acres, S.D., Radostits, O.M., The efficacy of a modified live reo-like virus vaccine and an E. coli (1976) Can Vet J, 17, p. 1977. , bacterin for prevention of acute undifferentiated neonatal diarrhea of beef calves; Benfield, D.A., Stotz, I.J., Nelson, E.A., Groon, K.S., Comparison of a commercial enzyme-linked immunosorbent assay with electron microscopy, fluorescent antibody, and virus isolation for the detection of bovine and porcine rotavirus (1984) Am J Vet Res, 45, pp. 1998-2002; Blackmer, P.E., A practioner's experience with experimental reo-coronavirus calf diarrhea vaccine (1976) Vet Med Sm Anim Clin, 71, pp. 351-354; De Leeuw, P.W., Ellens, D.J., Talmon, F.P., Rotavirus infections in calves: Efficacy of oral vaccination in endemically infected herds (1980) Res Vet Sci, 29, pp. 142-147; England, J.J., Frye, C.S., Enright, E.A., Negative contrast electron microscopic diagnosis of viruses of neonatal calf diarrhea (1976) Cornell Vet, 66, pp. 172-182; Fernelius, A.L., Ritchie, A.E., Classick, L.G., Cell culture adaption and propagation of a reovirus-like agent of calf diarrhea from a field outbreak in Nebraska (1972) Arch Ges Virusforsch, 37, pp. 114-130; Goyal, S.M., Rademacher, R.A., Pomeroy, I.S.A., Comparison of electron microscopy with three commercial tests for the detection of rotavirus in animal feces (1987) Diagn Microbiol Infect Dis, 6, pp. 249-254; Hancock, D.D., (1983) Studies on the epidemiology of mortality and diarrheal morbidity in heifer calves in northeastern Ohio dairy herds, , PhD Thesis, The Ohio State University Columbus, OH; Mebus, C.A., Kono, K., Underdahl, N.R., Twiehaus, M.J., Cell culture propagation of neonatal calf diarrhea (scours) virus (1971) Can Vet J, 12, pp. 69-72; Mebus, C.A., Rhodes, M.B., Stair, E.L., (1972) Laboratory techniques for demonstrating Nebraska calf diarrhea virus, pp. 599-600. , Proc 75th Ann Mtg US Anim Health Assoc; Mebus, C.A., Stair, E.L., Underdahl, N.R., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a reo-like virus (1971) Vet Pathol, 8, pp. 490-505; Mebus, C.A., Underdahl, N.R., Rhodes, M.B., Twiehaus, M.J., Calf diarrhea (scours): Reproduced with a virus from a field outbreak (1969) U of Neb Ag Exp Station Res Bull, 233, pp. 1-16; Mebus, C.A., White, R.G., Bass, E.P., Twiehaus, M.J., Immunity to neonatal calf diarrhea virus (1973) J Am Vet Med Assoc, 163, pp. 880-883; Newman, F.S., Myers, L.L., Firehammer, B.D., Catlin, J.E., (1974) Licensing and use of the calf scours vaccine. Part II. An analysis of Scourvax-Reo, pp. 59-64. , Proc 75th Ann Mtg US Anim Health Assoc; Smith, A.B., Economic implications of a calf scours prevention program (1974) Vet Econ, 15, pp. 38-44; Stear, R.L., Calf scours: Questions most frequently asked (1975) Norden News, 50, pp. 4-6; Theil, K.W., Group A Rotaviruses (1990) Viral diarrheas of man and animals, ed., pp. 35-77. , Saif LJ Theil KW, CRC Press, Inc. Boca Raton, FL; Theil, K.W., McCloskey, C.M., Partial characterization of a bovine group A rotavirus with a short genome electropherotype (1988) J Clin Microbiol, 26, pp. 1094-1099; Theil, K.W., McCloskey, C.M., Molecular epidemiology and subgroup determination of bovine group A rotaviruses associated with diarrhea in dairy and beef calves (1989) J Clin Microbiol, 27, pp. 126-131; Theil, K.W., McCloskey, C.M., Nonreactivity of American avian group A rotaviruses with subgroup-specific monoclonal antibodies (1989) J Clin Microbiol, 27, pp. 2846-2848; Theil, K.W., Reynolds, D.L., Saif, Y.M., Comparison of immune electron microscopy and genome electropherotyping techniques for detection of turkey rotaviruses and rotaviruslike viruses in intestinal contents (1986) J Clin Microbiol, 23, pp. 695-699; Theil, K.W., Reynolds, D.L., Saif, Y.M., Isolation and serial propagation of turkey rotaviruses in a fetal rhesus monkey kidney (MA104) cell line (1986) Avian Dis, 30, pp. 93-103; Thurber, E.T., Bass, E.P., Beckenhauer, W.H., Field trial evaluation of a reo-coronavirus calf diarrhea vaccine (1977) Can J Comp Pathol, 41, pp. 131-136; Twiehaus, M.J., Mebus, C.A., Bass, E.P., Survey of the field efficacy of reoviral calf diarrhea vaccine (1975) Vet Med Sm Anim Clin, 70, pp. 23-25; White, R.G., Mebus, C.A., Twiehaus, M.J., Incidence ofherds infected with a neonatal calf diarrhea virus (NCDV) (1970) Vet Med Sm Anim Clin, 65, pp. 487-490; Woode, G.N., Bew, M.E., Dennis, M.J., Studies on cross protection induced in calves by rotaviruses of calves, children and foals (1978) Vet Rec, 103, pp. 32-34",,,,10406387,,,"8580160","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0029382506
"Jackwood D.J., Kwon H.M., Saif L.J.","7005468303;7401838151;7102226747;","Molecular differentiation of transmissible gastroenteritis virus and porcine respiratory coronavirus strains: Correlation with antigenicity and pathogenicity",1995,"Advances in Experimental Medicine and Biology","380",,,"35","41",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028803423&partnerID=40&md5=66fff57516481ad29765fa29784ff421","Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH 44691, United States","Jackwood, D.J., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH 44691, United States; Kwon, H.M., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH 44691, United States","Transmissible gastroenteritis virus (TGEV) causes an economically important enteric disease of swine. Differences in the pathogenicity, antigenicity and tissue tropism have been observed among porcine coronaviruses. Although porcine respiratory coronavirus (PRCV) is antigenically similar but not identical to TGEV isolates, these respiratory coronaviruses differ markedly in pathogenicity and tissue tropism compared to TGEV isolates. Using a reverse transcriptase/polymerase chain reaction- restriction fragment length polymorphism (RT/PCR-RFLP)assay, TGEV and PRCV isolates were assigned to several distinct groups. By RFLP analysis of the 5' region of the S gene, TGEV strains were differentiated into 4 groups using the restriction enzyme Sau3AI. A fifth Sau3AI group contained the PRCV isolates. These 5 groups correlated with antigenic groups previously defined using monoclonal antibodies in our laboratory. Several restriction enzymes could be used to differentiate the TGEV strains into Miller and Purdue types. Analysis of a PCR amplified product in the 3 and 3-1 genes indicated the RT/PCR-RFLP assay results for TGEV Miller strains could be correlated with lower virulence created by passage in cell culture.",,"monoclonal antibody; animal cell; animal model; antigenicity; conference paper; coronavirus; gastroenteritis; nonhuman; priority journal; restriction fragment length polymorphism; reverse transcription polymerase chain reaction; strain difference; swine; upper respiratory tract; virus infection; virus isolation; virus pathogenesis; virus virulence; Animal; Antibodies, Monoclonal; Antigens, Viral; Coronavirus; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Respiratory Tract Infections; RNA, Viral; Swine; Swine Diseases; Transmissible gastroenteritis virus; Virulence",,"Jackwood, D.J.; Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH 44691, United States",,,00652598,,AEMBA,"8830506","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028803423
"van Marle G., van der Most R.G., van der Straaten T., Luytjes W., Spaan W.J.","6603893383;6701702352;56675761300;6701683324;7007172944;","Regulation of transcription of coronaviruses.",1995,"Advances in experimental medicine and biology","380",,,"507","510",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029447636&partnerID=40&md5=2b759d6adc208135b8d6ad282f794206","Department of Virology, Faculty of Medicine, Leiden University, Netherlands","van Marle, G., Department of Virology, Faculty of Medicine, Leiden University, Netherlands; van der Most, R.G., Department of Virology, Faculty of Medicine, Leiden University, Netherlands; van der Straaten, T., Department of Virology, Faculty of Medicine, Leiden University, Netherlands; Luytjes, W., Department of Virology, Faculty of Medicine, Leiden University, Netherlands; Spaan, W.J., Department of Virology, Faculty of Medicine, Leiden University, Netherlands","To study factors involved in regulation of transcription of coronaviruses, we constructed defective interfering (DI) RNAs containing sg RNA promoters at multiple positions. Analysis of the amounts of sg DI RNA produced by these DIs resulted in the following observations: (i) a downstream promoter downregulates an upstream promoter; (ii) an upstream promoter has little or no effect on the activity of a downstream promoter. Our data suggest that attenuation of upstream promoter activities by downstream promoter sequences plays an important role in regulating the amounts of sg RNAs produced by coronaviruses. Our observations are in accordance with the models proposed by Konings et al. and Sawicki and Sawicki.",,"messenger RNA; virus RNA; animal; biological model; biosynthesis; comparative study; Coronavirus; defective virus; gene expression regulation; genetic transcription; genetics; metabolism; molecular genetics; mouse; Murine hepatitis coronavirus; nucleotide sequence; promoter region; review; Animals; Base Sequence; Coronavirus; Defective Viruses; Gene Expression Regulation, Viral; Mice; Models, Genetic; Molecular Sequence Data; Murine hepatitis virus; Promoter Regions (Genetics); RNA, Messenger; RNA, Viral; Transcription, Genetic",,"van Marle, G.",,,00652598,,,"8830531","English","Adv. Exp. Med. Biol.",Review,"Final",,Scopus,2-s2.0-0029447636
"Barac-Latas V., Wege H., Lassmann H.","6506163291;7005516649;35420677900;","Apoptosis of T lymphocytes in coronavirus-induced encephalomyelitis",1995,"Regional Immunology","6","5-6",,"355","357",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029073368&partnerID=40&md5=a3863de5d1967d96c73b3d0e66454b3c","c/o Institute of Neurology, Res. Unit of Exptl. Neuropathology, Austrian Academy of Sciences, Schwarzspanierstrasse 17, A-1090 Vienna, Austria","Barac-Latas, V., c/o Institute of Neurology, Res. Unit of Exptl. Neuropathology, Austrian Academy of Sciences, Schwarzspanierstrasse 17, A-1090 Vienna, Austria; Wege, H., c/o Institute of Neurology, Res. Unit of Exptl. Neuropathology, Austrian Academy of Sciences, Schwarzspanierstrasse 17, A-1090 Vienna, Austria; Lassmann, H., c/o Institute of Neurology, Res. Unit of Exptl. Neuropathology, Austrian Academy of Sciences, Schwarzspanierstrasse 17, A-1090 Vienna, Austria","In order to examine the mechanisms by which inflammatory cells can be cleared from the brain lesions in coronavirus-induced encephalomyelitis, immunohistochemical technique and in situ tailing were performed. Degenerating cells visualized by this technique were observed throughout the disease with maximum value in the last stage of disease. On average 42% of all apoptotic cells could be identified by immunocytochemistry as T lymphocytes. Morphological features reminiscent of apoptosis were not found in macrophages. Our results suggest that, similar to autoimmune encephalomyelitis, also in coronavirus-induced encephalomyelitis apoptosis of T cells may be a major mechanism to eliminate T lymphocytes from brain inflammatory lesions.",,"alkaline phosphatase; animal cell; animal experiment; animal model; animal tissue; apoptosis; autoimmunity; cell death; cell degeneration; conference paper; data analysis; encephalomyelitis; immunocytochemistry; immunohistochemistry; inflammatory cell; nonhuman; priority journal; rat",,"Lassmann, H.; c/o Institute of Neurology, Res. Unit of Exptl. Neuropathology, Austrian Academy of Sciences, Schwarzspanierstrasse 17, A-1090 Vienna, Austria",,,08960623,,REGIE,,"English","REG. IMMUNOL.",Conference Paper,"Final",,Scopus,2-s2.0-0029073368
"Compton S.R., Kunita S.","7102893878;6701719060;","Characterization of the S protein of enterotropic murine coronavirus strain-Y",1995,"Advances in Experimental Medicine and Biology","380",,,"23","28",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028805537&partnerID=40&md5=dbaa9885f21aca54f9ced67775cc9db4","Inst. of Laboratory Animal Research, School of Science, Kitasato University, Kanagawa, Japan","Compton, S.R., Inst. of Laboratory Animal Research, School of Science, Kitasato University, Kanagawa, Japan; Kunita, S., Inst. of Laboratory Animal Research, School of Science, Kitasato University, Kanagawa, Japan","The pathogenesis of enterotropic murine coronavirus strain MHV-Y differs extensively from that of prototypic respiratory strains of murine coronaviruses. The S protein of MHV-Y was characterized as a first step towards identifying viral determinants of enterotropism. Immunoblots of MHV- Y virions using anti-S protein specific antiserum revealed that the MHV-Y S protein was inefficiently cleaved. The MHV-Y S gene was cloned and sequenced. It encodes a protein predicted to be 1361 amino acids long. The presence of several amino acids changes within and surrounding the predicted cleavage site of the MHV-Y S protein may contribute to its inefficient cleavage.",,"antiserum; complementary dna; double stranded dna; plasmid dna; virus glycoprotein; virus rna; amino acid sequence; animal cell; conference paper; dna sequence; enteritis; immunoblotting; intestine cell; molecular cloning; mouse; murine hepatitis coronavirus; nonhuman; priority journal; strain difference; virion; virus hepatitis; virus infection; Amino Acid Sequence; Animal; Cell Line; Cloning, Molecular; Genes, Viral; Immunoblotting; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Recombinant Proteins; Support, U.S. Gov't, P.H.S.; Viral Envelope Proteins; Virion",,"Kunita, S.; Inst. of Laboratory Animal Research, School of Science, Kitasato University, Kanagawa, Japan",,,00652598,,AEMBA,"8830485","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028805537
"Horsburgh B.C., Brown T.D.K.","6603848032;56248391000;","Cloning, sequencing and expression of the S protein gene from two geographically distinct strains of canine coronavirus",1995,"Virus Research","39","1",,"63","74",,10,"10.1016/S0168-1702(95)00068-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028848534&doi=10.1016%2fS0168-1702%2895%2900068-2&partnerID=40&md5=26a2c38afdfd66c7dd3dfa5b5b1446bc","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","Horsburgh, B.C., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","The gene encoding the spike (S) protein from two geographically distinct strains (American and British) of canine coronavirus (CCV) was cloned and sequenced. The nucleotide sequence revealed open reading frames of 1443 or 1453 amino acids, respectively. Structural features include an N-terminal hydrophobic signal sequence, a hydrophilic cysteine-rich cluster near the C-terminus, two heptad repeats and 29 or 33 potential N-glycosylation sites. Pairwise comparisons of S amino acid sequences from these isolates with other CCV strains (Insavc1 and K378) revealed that heterogeneity, found mostly in the form of conservative substitutions, is distributed throughout the canine sequences. However, 5 variable regions could be identified. Similar analysis with feline, porcine, murine, chicken and human coronavirus sequences revealed that the canine sequences are much more closely related to the feline S protein sequence than to the porcine S protein sequences even though they are all from the same antigenic group. Moreover, the sequence similarity between CCV isolates and the feline coronavirus, feline infectious peritonitis virus (FIPV) was comparable. Expression of the CCV or the transmissible gastroenteritis virus (TGEV) S gene using the vaccinia virus system produced a protein of the expected size which could induce extensive syncytia formation in infected canine A72 cells. © 1995.","Coronavirus; S protein; Syncytium","vitronectin; article; cloning; coronavirus; gene expression; gene sequence; nonhuman; priority journal; virus strain; Amino Acid Sequence; Animal; Base Sequence; Cats; Cells, Cultured; Chickens; Cloning, Molecular; Comparative Study; Coronavirus, Canine; Dogs; Gene Expression; Genes, Viral; Human; Membrane Glycoproteins; Mice; Molecular Sequence Data; Recombinant Proteins; Sequence Alignment; Sequence Analysis; Support, Non-U.S. Gov't; Swine; Transfection; Viral Envelope Proteins; Viral Proteins; Canine coronavirus; Coronavirus; Felidae; Feline infectious peritonitis virus; Gallus gallus; human coronavirus; Murinae; Suidae; Transmissible gastroenteritis virus; Vaccinia; Vaccinia virus","Binns, Boursnell, Cavanagh, Pappin, Brown, Cloning and sequencing of the gene encoding the spike protein of coronavirus IBV (1985) J. Gen. Virol., 66, pp. 719-726; Brierley, Boursnell, Binns, Bilimoria, Blok, Brown, Inglis, An efficient ribosomal frameshifting signal in the polymerase encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Britton, Page, Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res., 18, pp. 71-80; Britton, Mawditt, Page, The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Cavanagh, Coronavirus IBV glycopeptides: size of their polypeptide moieties and nature of their oligosaccharides (1983) J. Gen. Virol., 64, pp. 1187-1191; Collins, Knobler, Powell, Buchmeier, Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Daya, Wong, Cervin, Evans, Vennema, Spaan, Anderson, Mutation of host cell determinants which discriminate between lytic and persistent mouse hepatitis virus infection results in a fusion-resistant phenotype (1989) J. Virol., 70, pp. 3335-3346; Delmas, Laude, Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5367-5375; Degroot, Maduro, Lenstra, Horzinek, Ziejst, van der Spaan, Spaan, cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) Journal of General Virology, 68, pp. 2639-2646; DeGroot, Andeweg, Horzinek, Spaan, Sequence analysis of the 3′ end of the feline coronavirus FIPV 79-1146 genome: comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Duatre, Laude, Sequence of the spike protein of the porcine epidemic diarrhoea virus (1994) J. Gen. Virol., 75, pp. 1195-1200; Enjuanes, Gebauer, Correa, Bullido, Sune, Smerdou, Sanchez, Meloen, Localization of antigenic sites of the S-glycoprotein of transmissible gastroenteritis virus and their conservation in coronaviruses (1990) Adv. Exp. Med. Biol., 276, pp. 159-172; Gallagher, Parker, Buchmeier, Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Garwes, Reynolds, The polypeptide structures of canine coronavirus and its relationship to porcine transmissible gastroenteritis virus (1981) J. Gen. Virol., 52, pp. 153-157; Godet, l'Haridon, Vautherot, Laude, TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Heijne, A new method for predicting signal sequence cleavage sites (1986) Nucleic Acids Res., 14, pp. 4683-4690; Higgins, Sharp, Fast and sensitive multiple sequence alignments on a microcomputer (1989) Cabios, 5, pp. 151-153; Holmes, Dolfer, Behnke, Analysis of the functions of coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin (1981) Adv. Exp. Med. Biol., 142, pp. 133-142; Horsburgh, Brierley, Brown, Analysis of a 9.6kb sequence from the 3′-end of canine coronavirus (1992) J. Gen. Virol., 73, pp. 2849-2862; Horzinek, Lutz, Pedersen, Antigenic relationships among coronavirus homologous structural polypeptides of porcine, feline and canine coronaviruses (1982) Infect. Immun., 37, pp. 1148-1155; Keck, Matsushima, Makino, Fleming, Vannier, Stohlman, Lai, In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Korner, Schliephake, Winter, Zimprich, Lassmann, Sedgwick, Siddell, Wege, Nucleocapsid or spike protein-specific CD4 + T lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CD8 + T cells (1991) J. Immunol., 147, pp. 2317-2323; Kusters, Jager, van der Zeijst, Sequence evidence for in vivo RNA recombination in avian coronavirus IBV (1989) Nucleic Acids Res., 17, pp. 6726-6729; Luytjes, Sturman, Bredenbeek, Charite, van der Zeijst, Horzinek, Spaan, Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Mackett, Smith, Vaccinia virus expression vectors (1986) Journal of General Virology, 67, pp. 2067-2082; Mounir, Talbot, Molecular characterization of the S protein gene of human coronavirux OC43 (1993) J. Gen. Virol., 74, pp. 1981-1987; Neimann, Boschek, Evans, Rosing, Tamura, Klenk, Post-translational glycosylation of coronavirus glycoprotein E1: inhibition by monensin (1982) EMBO J., 1, pp. 1499-1504; Parker, Gallagher, Buchmeier, Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Parker, Yoo, Cox, Babiuk, Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) J. Gen. Virol., 71, pp. 263-270; Pulford, Britton, Page, Garwes, Expression of TGEV structural genes in virus vectors (1990) Adv. Exp. Med. Biol., 276, pp. 223-231; Raabe, Schelle-Prinz, Siddell, Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Rasschaert, Laude, The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Rasschaert, Duarte, Laude, Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Sanchez, Jimenez, Laviada, Correa, Sune, Bullido, Gebaues, Enjuanes, Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Schmidt, Skinner, Siddell, Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Siddell, Wege, ter Meulen, The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Sodroski, Goh, Rosen, Dayton, Terwilligier, Haseltine, A second post-transcriptional trans activator gene required for HTLV-III replication (1986) Nature, 321, pp. 412-417; Spaan, Cavanagh, Horzinek, Coronaviruses: structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Staden, The current status and portability of our sequence handling software (1986) Nucleic Acids Res., 14, pp. 217-231; Stauber, Pfleiderer, Siddell, Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Sturman, Holmes, The novel glycoproteins of coronaviruses (1985) Trends Biochem. Sci., 10, pp. 17-20; Sturman, Ricard, Holmes, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Tomley, Binns, Boursnell, Mockett, Brown, Smith, Expression of IBV spike protein by a vaccinia virus recombinant (1987) Journal of General Virology, 68, pp. 2291-2298; Tyrrell, Almeida, Berry, Coronaviruses (1968) Nature, 220, p. 650; Vennema, Heijnen, Zijderveld, Horzinek, Spaan, Intracellular transport of recombinant coronavirus spike proteins: implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Wesseling, Vennema, Godeke, Horzinek, Rottier, Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794; Williams, Jiang, Holmes, Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536","Brown, T.D.K.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom",,,01681702,,VIRED,"8607285","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0028848534
"Labonte P., Mounir S., Talbot P.J.","6507854410;6603891523;7102670281;","Sequence and expression of the ns2 protein gene of human coronavirus OC43",1995,"Journal of General Virology","76","2",,"431","435",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028890366&partnerID=40&md5=1b732d307f4a5ae3d9f243e3cd35ce3d","Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Labonte, P., Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Mounir, S., Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Talbot, P.J., Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","The complete nucleotide sequence of the ns2 gene of human coronavirus OC43 (HCV-OC43) was determined. Sequence analysis revealed an open reading frame that could encode a protein of 278 amino acids, with an estimated molecular mass of 32.2 kDa. Six potential phosphorylation sites are present but no sites of N-glycosylation were found. The amino acid sequence of the HCV-OC43 ns2 protein shows 92% identity with that of the Mebus strain of bovine coronavirus (BCV). However, a stretch of nine consecutive amino acids near the C terminus is completely different, causing it to be very hydrophilic, which contrasts with the hydrophobic nature of this region in BCV. As shown by immunofluorescence with a monospecific antiserum, the ns2 protein was expressed in the cytoplasm of HCV-OC43-infected HRT-18 cells.",,"antiserum; virus protein; amino acid sequence; article; carboxy terminal sequence; cellular distribution; controlled study; coronavirus; cytoplasm; hydrophilicity; immunofluorescence test; molecular weight; nonhuman; nucleotide sequence; open reading frame; priority journal; protein phosphorylation; sequence homology; virus gene; virus infection; Amino Acid Sequence; Animal; Base Sequence; Coronavirus; Coronavirus OC43, Human; Coronavirus, Bovine; Escherichia coli; Genes, Viral; Mice; Molecular Sequence Data; Open Reading Frames; Rabbits; Recombinant Fusion Proteins; Support, Non-U.S. Gov't; Viral Nonstructural Proteins",,"Talbot, P.J.; Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada",,,00221317,,JGVIA,"7844564","English","J. GEN. VIROL.",Article,"Final",,Scopus,2-s2.0-0028890366
"Taguchi F.","7103209890;","The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding",1995,"Journal of Virology","69","11",,"7260","7263",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028818244&partnerID=40&md5=58e4917f295d0fff06a0a067e9a441ca","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","The receptor-binding capacity of the S2 subunit of the murine coronavirus S protein was examined by testing the inhibition of virus-receptor binding. Sp-4 virus and S1N(330), which consists of the N-terminal 330 amino acids of the S1 protein, both of which exhibited receptor-binding capacity, were able to prevent the binding of cl-2 virus to the receptor, while the mutant protein S1N(330)-159, which failed to bind to the receptor protein, and S2TM-, which lacks the transmembrane and cytoplasmic domains normally existing in the S2, were unable to prevent the binding of cl-2. By using cultured DBT cells, it was revealed that the infection of cells by cl-2 virus was significantly inhibited by S1N(330) but not by S2TM-. These results indicate that the S2 protein is not involved in the receptor binding of murine coronaviruses.",,"mutant protein; protein subunit; receptor protein; virus protein; virus receptor; amino acid sequence; animal cell; article; controlled study; mouse; murine hepatitis coronavirus; nonhuman; priority journal; receptor binding; virus infectivity; virus strain; Animal; Base Sequence; Binding Sites; Blotting, Western; Cell Membrane; Coronavirus; DNA Primers; Macromolecular Systems; Membrane Glycoproteins; Mice; Molecular Sequence Data; Mutagenesis; Receptors, Virus; Recombinant Proteins; Sequence Deletion; Support, Non-U.S. Gov't; Transfection; Viral Envelope Proteins",,"Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,0022538X,,JOVIA,"7474149","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028818244
"Ricard C.S., Koetzner C.A., Sturman L.S., Masters P.S.","7004706818;6602982748;7003697107;7006234572;","A conditional-lethal murine coronavirus mutant that fails to incorporate the spike glycoprotein into assembled virions",1995,"Virus Research","39","2-3",,"261","276",,14,"10.1016/0168-1702(95)00100-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029612190&doi=10.1016%2f0168-1702%2895%2900100-X&partnerID=40&md5=8c36c9bada0597e59c83612115709a57","Department of Microbiology, Immunology, and Molecular Genetics, Albany Medical College, Albany, NY 12208, United States; Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Department of Biomedical Sciences, State University of New York at Albany, Albany, NY 12237, United States","Ricard, C.S., Department of Microbiology, Immunology, and Molecular Genetics, Albany Medical College, Albany, NY 12208, United States; Koetzner, C.A., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Sturman, L.S., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States, Department of Biomedical Sciences, State University of New York at Albany, Albany, NY 12237, United States; Masters, P.S., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States, Department of Biomedical Sciences, State University of New York at Albany, Albany, NY 12237, United States","The coronavirus spike glycoprotein (S) mediates both the attachment of virus to the host cell receptor and membrane fusion. We describe here the characterization of a temperature-sensitive mutant of the coronavirus mouse hepatitis virus A59 (MHV-A59) having multiple S protein-related defects. The most remarkable of these was that the mutant, designated Albany 18 (Alb 18), assembled virions devoid of the S glycoprotein at the nonpermissive temperature. Alb18 also failed to bring about syncytia formation in cells infected at the nonpermissive temperature. Virions of the mutant assembled at the permissive temperature were much more thermolabile than wild type. Moreover, mutant S protein that was incorporated into virions at the permissive temperature showed enhanced pH-dependent thermolability in its ability to bind to the MHV receptor. Alb18 was found to have a single point mutation in S resulting in a change of serine 287 to isoleucine, and it was shown by revertant analysis that this was the lesion responsible for the phenotype of the mutant. © 1995.","Coronavirus; Spike glycoprotein; Temperature-sensitive mutant; Virus assembly","virus glycoprotein; animal cell; article; controlled study; coronavirus; nonhuman; priority journal; temperature sensitive mutant; virus assembly; virus mutant; Amino Acid Sequence; Animals; Cell Line; Genes, Viral; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Murine hepatitis virus; Mutation; Phenotype; Receptors, Virus; Sequence Analysis; Temperature; Viral Envelope Proteins; Virus Assembly","Boyle, Weismiller, Holmes, Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. Virol., 61, pp. 185-189; Cavanagh, Coronavirus IBV: structural characterization of the spike protein (1983) J. Gen. Virol., 64, pp. 2577-2583; Compton, Barthold, Smith, The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Dea, Garzon, Tijssen, Identification and location of the structural glycoproteins of a tissue culture-adapted turkey enteric coronavirus (1989) Arch. Virol., 106, pp. 221-237; Delmas, Laude, Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5367-5375; Frana, Behnke, Sturman, Holmes, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Fu, Baric, Map locations of mouse hepatitis virus temperature-sensitive mutants: confirmation of variable rates of recombination (1994) J. Virol., 68, pp. 7458-7466; Gallagher, Parker, Buchmeier, Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gallagher, Escarmis, Buchmeier, Alteration of the pH dependence of coronavirus-induced cell-fusion: effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Gallione, Rose, A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein (1985) J. Virol., 54, pp. 374-382; Gombold, Hingley, Weiss, Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gubler, Hoffman, A simple and very efficient method for generating cDNA libraries (1983) Gene, 25, pp. 263-269; Holmes, Doller, Sturman, Tunicamycin resistant glycosylation of a coronavirus glycoprotein: demonstration of a novel type of viral glycoprotein (1981) Virology, 115, pp. 334-344; Koetzner, Parker, Ricard, Sturman, Masters, Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Kubo, Yamada, Taguchi, Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Kusters, Niesters, Lenstra, Horzinek, van der Zeijst, Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Laemmli, Cleavage of structural proteins during the assembly of the head of bacterioshage T4 (1970) Nature, 227, pp. 680-685; La Monica, Banner, Morris, Lai, Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, pp. 883-888; Luytjes, Sturman, Bredenbeek, Charite, van der Zeijst, Horzinek, Spaan, Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Luytjes, Bredenbeek, Noten, Horzinek, Spaan, Sequence of mouse hepatitis virus A59 mRNA2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Masters, Koetzner, Kerr, Heo, Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Metsikkö, Simons, The budding mechanism of spikeless vesicular stomatitis virus particles (1986) EMBO J, 5, pp. 1913-1920; Mounir, Talbot, Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Opstelten, de Groote, Horzinek, Vennema, Rottier, Disulfide bonds in folding and transport of mouse hepatitis coronavirus glycoproteins (1993) J. Virol., 67, pp. 7394-7401; Parker, Gallagher, Buchmeier, Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Ricard, Sturman, Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite high performance liquid chromatography (1985) J. Chromatogr., 326, pp. 191-197; Rottier, Horzinek, van der Zeijst, Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: effects of tunicamycin (1981) J. Virol., 40, pp. 350-357; Sanger, Nicklen, Coulson, DNA sequencing with chain terminating inhbitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Sturman, Characterization of a coronavirus: I. Structural proteins: effect of preparative conditions on the migration of protein in polyacrylamide gels (1977) Virology, 77, pp. 637-649; Sturman, Holmes, The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-111; Sturman, Holmes, The novel glycoproteins of coronaviruses (1985) Trends Biochem. Sci., 10, pp. 17-20; Sturman, Holmes, Behnke, Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Sturman, Ricard, Holmes, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90 K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Sturman, Eastwood, Frana, Duchala, Baker, Ricard, Sawicki, Holmes, Temperature-sensitive mutants of MHV-A59 (1987) Coronaviruses, pp. 159-168. , M.M.C. Lai, S.A. Stohlman, Plenum Press, New York; Sturman, Ricard, Holmes, Conformational change of the coronavirus peplomer glycoprotein E2 at pH 8.0 correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Tooze, Tooze, Infection of AtT20 murine pituitary tumor cells by mouse hepatitis virus strain A59: virus budding is restricted to the Golgi region (1985) Eur. J. Cell Biol., 37, pp. 203-212; Tooze, Tooze, Warren, Replication of coronavirus MHV-A59 in Sac− cells: determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Vennema, Rottier, Heijnen, Godeke, Horzinek, Spaan, Biosynthesis and function of the coronavirus spike protein (1990) Coronaviruses and Their Diseases, pp. 9-19. , D. Cavanagh, T.D.K. Brown, Plenum Press, New York; Wang, Fleming, Lai, Sequence analysis of the spike protein gene of murine coronavirus variants: study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Williams, Jiang, Snyder, Frana, Holmes, Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Williams, Jiang, Holmes, Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yu, Bi, Weiss, Leibowitz, Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Masters, P.S.; Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States",,,01681702,,VIRED,"8837889","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0029612190
"Yoo D., Parker M.D., Cox G.J., Babiuk L.A.","7103242554;7403673276;7402494115;35427029400;","Zinc-binding of the cysteine-rich domain encoded in the open reading frame 1B of the RNA polymerase gene of coronavirus",1995,"Advances in Experimental Medicine and Biology","380",,,"437","442",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028784073&partnerID=40&md5=6b518dd9ffb44e0f5fd7479a718c6641","Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada","Yoo, D., Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada; Parker, M.D., Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada; Cox, G.J., Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada; Babiuk, L.A., Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada","We cloned and sequenced the second open reading frame of the RNA polymerase gene, ORF 1b, of bovine coronavirus. In the region representing nucleotide positions 49195677 upstream from the initiation codon of the 32K non-structural protein gene, we identified two putative functional domains. One of these domains contained four leucine residues repeated exactly in every seventh position, and the other domain represented a cluster of cysteine and histidine residues. The DNA sequence representing these domains was cloned and expressed in Escherichia coli as fusion proteins with glutathione S-transferase from Schistosoma japonicum. A high level expression of the cysteine-rich domain was achieved as a fusion protein when the bacterial culture was induced with IPTG. In a solid phase zinc binding assay using the recombinant fusion protein, we found that the protein containing the cysteine-rich domain was able to bind to radioactive zinc in vitro, demonstrating that the polypeptide encoded by the ORF1b of coronavirus is a zinc-binding protein.",,"binding protein; cysteine; dna; glutathione transferase; histidine; hybrid protein; nucleotide; rna polymerase; virus rna; zinc; conference paper; coronavirus; dna sequence; gene; immunoblotting; nonhuman; open reading frame; polyacrylamide gel electrophoresis; priority journal; Animal; Binding Sites; Cattle; Cloning, Molecular; Codon; Coronavirus, Bovine; Cysteine; DNA-Directed RNA Polymerases; Escherichia coli; Immunoblotting; Open Reading Frames; Recombinant Fusion Proteins; Recombinant Proteins; Support, Non-U.S. Gov't; Zinc",,"Yoo, D.; Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada",,,00652598,,AEMBA,"8830521","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028784073
"Williams G.D., Chang R.-Y., Brian D.A.","7406083594;36725275000;7006460232;","Evidence for a pseudoknot in the 3' untranslated region of the bovine coronavirus genome",1995,"Advances in Experimental Medicine and Biology","380",,,"511","514",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028786186&partnerID=40&md5=6e8158200d80f7545aa3624ce5be755f","Program in Biotechnology, University of Tennessee, Knoxville, TN 37996-0845, United States","Williams, G.D., Program in Biotechnology, University of Tennessee, Knoxville, TN 37996-0845, United States; Chang, R.-Y., Program in Biotechnology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Program in Biotechnology, University of Tennessee, Knoxville, TN 37996-0845, United States","A potential pseudoknot was found in the 3' untranslated region of the bovine coronavirus genome beginning 63 nt downstream from the stop codon of the N gene. Mutation analysis of the pseudoknot in a cloned defective interfering RNA indicated that this structural element is necessary for defective interfering RNA replication.",,"virus rna; cattle; conference paper; coronavirus; defective virus; molecular cloning; nonhuman; priority journal; rna synthesis; virus gene; virus mutant; virus replication; Animal; Base Sequence; Capsid; Cattle; Cloning, Molecular; Codon; Comparative Study; Coronavirus, Bovine; Defective Viruses; Genes, Viral; Genome, Viral; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Polymerase Chain Reaction; RNA, Viral; Sequence Homology, Nucleic Acid; Transcription, Genetic; Transmissible gastroenteritis virus; Viral Core Proteins",,"Williams, G.D.; Program in Biotechnology, University of Tennessee, Knoxville, TN 37996-0845, United States",,,00652598,,AEMBA,"8830533","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028786186
"Millane G., Michaud L., Dea S.","6508301204;57197459648;7006056287;","Biological and molecular differentiation between coronaviruses associated with neonatal calf diarrhoea and winter dysentery in adult cattle",1995,"Advances in Experimental Medicine and Biology","380",,,"29","33",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028858253&partnerID=40&md5=8f68ebcad46228219aa829e5210f58d1","Centre De Recherche en Virologie, Institut Armand Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada","Millane, G., Centre De Recherche en Virologie, Institut Armand Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada; Michaud, L., Centre De Recherche en Virologie, Institut Armand Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada; Dea, S., Centre De Recherche en Virologie, Institut Armand Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada","Cytopathic coronaviruses were isolated in HRT-18 cells from bloody faecal samples collected from cows in Quebec dairy herds with classical winter dysentery (WD). The formation of polykaryons in the infected cell cultures was found to be dependent on the presence of trypsin in the medium. Virus identification was confirmed by indirect immunofluorescence and indirect protein A-gold immunoelectron microscopy using rabbit hyperimmune serum, as well as monoclonal antibodies directed against the spike (S) and hemagglutinin-esterase (HE) glycoproteins of the prototype Mebus strain of bovine coronavirus (BCV-Meb). Four WD isolates differed from BCV-Meb by their ability to agglutinate rat erythrocytes at 4 and 37°C, their higher receptor destroying enzyme activity, but lower acetylesterase activity. The WD isolates were serologically indistinguishable from the reference BCV-Meb strain by virus neutralization and Western immunoblotting, but could be differentiated by hemagglutination-inhibition. Sequence analysis of the PCR- amplified HE gene of a plaque-purified WD isolate (BCQ-2590) revealed sufficient number of nucleotide and amino acid substitutions which may explain this antigenic variability.",,"acetylesterase; hemagglutinin; hyperimmune globulin; monoclonal antibody; amino acid substitution; animal cell; animal model; cattle; conference paper; coronavirus; cross reaction; diarrhea; dysentery; enzyme activity; feces analysis; immunoblotting; immunoelectron microscopy; newborn; newborn infection; nonhuman; nucleotide sequence; priority journal; rat; strain difference; virus characterization; virus infection; virus infectivity; virus neutralization; Animal; Animals, Newborn; Cattle; Cattle Diseases; Cell Line; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Dysentery; Hemagglutination; Rats",,"Millane, G.; Centre De Recherche en Virologie, Institut Armand Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada",,,00652598,,AEMBA,"8830495","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028858253
"Yu M., Talbot P.J.","16940438900;7102670281;","Induction of a protective immune response to murine coronavirus with non- internal image anti-idiotypic antibodies",1995,"Advances in Experimental Medicine and Biology","380",,,"165","172",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028846724&partnerID=40&md5=3e3c611e37f7da04d6a16f967ea20829","Virology Research Center, Institut Armand-Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada","Yu, M., Virology Research Center, Institut Armand-Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada; Talbot, P.J., Virology Research Center, Institut Armand-Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada","Neurotropic murine coronaviruses (MHV) provide an excellent animal model to study experimental modulation of the immune response to a vital pathogen with anti-idiotypic antibodies. It is known that among the various types of anti-idiotypic antibodies (anti-Id), those designated beta (β) or internal image can molecularly mimic the antigen and induce biological activities such as anti-viral protection and neutralization. We have recently shown that polyclonal non-internal image anti-idiotypic antibodies of the γ-type could induce protective anti-coronavirus immunity. In the present study, a polyclonal anti-Id (Ab2) was induced against a neutralizing murine monoclonal antibody (MAb1), designated 5B170.11. Mice immunized with this affinity- purified rabbit Ab2(α), a non-internal image antibody, were partially protected against lethal infection by the JHM strain of MHV. However, other polyclonal and monoclonal non-internal image Ab2 induced against another neutralizing MAb1, designated 4-11G.6, were not able to protect mice against lethal infection with the A59 strain of MHV. These results demonstrate that anti-viral protection by altering the idiotypic network with non-internal image-bearing anti-idiotype reagents can be achieved even with some anti-Id of the α-type.",,"idiotypic antibody; monoclonal antibody; neutralizing antibody; polyclonal antibody; animal experiment; animal tissue; antibody production; brain homogenate; conference paper; controlled study; coronavirus; enzyme linked immunosorbent assay; female; immune response; immunization; infection prevention; nonhuman; priority journal; rabbit; virus infection; virus inhibition; virus neutralization; virus plaque; virus strain; Animal; Antibodies; Antibodies, Anti-Idiotypic; Antibodies, Monoclonal; Antibody Formation; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Female; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Neutralization Tests; Plaque Assay; Rabbits; Support, Non-U.S. Gov't; Viral Envelope Proteins; Virus Replication",,"Yu, M.; Virology Research Center, Institut Armand-Frappier, Universite Du Quebec, Laval, Que. H7N 4Z3, Canada",,,00652598,,AEMBA,"8830474","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028846724
"Risco C., Anton I.M., Sune C., Pedregosa A.M., Martin-Alonso J.M., Parra F., Carrascosa J.L., Enjuanes L.","56251715300;57198264385;6701660310;6601944213;6701635642;7005551438;35481302900;7006565392;","Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion",1995,"Journal of Virology","69","9",,"5269","5277",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029112439&partnerID=40&md5=48416a3330efc9ad519e98ffcc97714c","Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Risco, C., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Anton, I.M., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sune, C., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Pedregosa, A.M., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Martin-Alonso, J.M., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Parra, F., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Carrascosa, J.L., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","The binding domains of four monoclonal antibodies (MAbs) specific for the M protein of the PUR46-MAD strain of transmissible gastroenteritis coronavirus (TGEV) have been located in the 46 carboxy-terminal amino acids of the protein by studying the binding of MAbs to recombinant M protein fragments. Immunoelectron microscopy using these MAbs demonstrated that in a significant proportion of the M protein molecules, the carboxy terminus is exposed on the external surface both in purified viruses and in nascent TGEV virions that recently exited infected swine testis cells. The same MAbs specifically neutralized the infectivity of the PUR46-MAD strain, indicating that the C-terminal domain of M protein is exposed on infectious viruses. This topology of TGEV M protein probably coexists with the structure currently described for the M protein of coronaviruses, which consists of an exposed amino terminus and an intravirion carboxy-terminal domain. The presence of a detectable number of M protein molecules with their carboxy termini exposed on the surface of the virion has relevance for vital function, since it has been shown that the carboxy terminus of M protein is immunodominant and that antibodies specific for this domain both neutralize TGEV and mediate the complement-dependent lysis of TGEV-infected cells.",,"m protein; membrane protein; monoclonal antibody; neutralizing antibody; virus protein; animal cell; antibody specificity; article; binding site; carboxy terminal sequence; complement dependent cytotoxicity; coronavirus; immunopathogenesis; mouse; nonhuman; priority journal; swine disease; transmissible gastroenteritis virus; virus morphology; virus neutralization; virus transmission; Animal; Antibodies, Monoclonal; Antigen-Antibody Reactions; Antigens, Viral; Cells, Cultured; Cloning, Molecular; Male; Mice; Microscopy, Immunoelectron; Models, Structural; Neutralization Tests; Protein Conformation; Recombinant Fusion Proteins; Support, Non-U.S. Gov't; Swine; Testis; Transmissible gastroenteritis virus; Viral Matrix Proteins; Virion",,"Enjuanes, L.; Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",,,0022538X,,JOVIA,"7636969","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029112439
"Joo M., Makino S.","23008647300;7403067550;","The effect of two closely inserted transcription consensus sequences on coronavirus transcription",1995,"Journal of Virology","69","1",,"272","280",,31,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028943212&partnerID=40&md5=56c2960d7641a24db85f7cfff430a757","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Microbiology, University of Texas at Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States","Joo, M., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Microbiology, University of Texas at Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States","Insertion of an intergenic region from the murine coronavirus mouse hepatitis virus into a mouse hepatitis virus defective interfering (DI) RNA led to transcription of subgenomic DI RNA in helper virus-infected cells. Using this system, we studied how two intergenic regions in close proximity affected subgenomic RNA synthesis. When two intergenic regions were separated by more than 100 nucleotides, slightly less of the larger subgenomic DI RNA (synthesized from the upstream intergenic region) was made; this difference was significant when the intergenic region separation was less than about 35 nucleotides. Deletion of sequences flanking the two intergenic regions inserted in close proximity did not affect transcription. No significant change in the ratio of the two subgenomic DI RNAs was observed when the sequence between the two intergenic regions was altered. Removal of the downstream intergenic region restored transcription of the larger subgenomic DI RNA. The UCUAAAC consensus sequence was needed for efficient suppression of the larger subgenomic DI RNA synthesis. These results demonstrated that the downstream intergenic sequence was suppressing subgenomic DI RNA synthesis from the upstream intergenic region. We discuss possible mechanisms to account for the regulation of this suppression of subgenomic DI RNA synthesis and the ways in which they relate to the general regulation of coronavirus transcription.",,"article; coronavirus; dna flanking region; gene insertion; priority journal; rna sequence; rna synthesis; rna transcription; virus transcription; Animal; Base Sequence; Cells, Cultured; Consensus Sequence; Coronavirus; Gene Expression Regulation, Viral; Mice; Molecular Sequence Data; RNA, Viral; Support, U.S. Gov't, P.H.S.; Transcription, Genetic",,"Makino, S.; Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"7983719","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028943212
"Herrewegh A.A.P.M., De Groot R.J., Cepica A., Egberink H.F., Horzinek M.C., Rottier P.J.M.","6602355430;7103077066;6602754809;7004767057;7102624836;7006145490;","Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR",1995,"Journal of Clinical Microbiology","33","3",,"684","689",,129,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028892966&partnerID=40&md5=bab8a0f964d4d1dcff03986f45bf7e5d","Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands","Herrewegh, A.A.P.M., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Groot, R.J., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands; Cepica, A., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands; Egberink, H.F., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands","A nested reverse transcriptase PCR (RT-nPCR) was developed for the detection of feline coronavirus (FCoV) RNA in the feces, tissues, and body fluids of infected cats. The RT-nPCR was targeted to the highly conserved 3'- untranslated region of the viral genome and will detect most, if not all, feline coronaviruses in the field. With the RT-nPCR, FCoV RNA was detected in plasma samples from experimentally infected cats as early as 2 days postinoculation. FCoV RNA was also detected in serum, plasma, or ascitic fluid samples from 14 of 18 cats (78%) with naturally occurring feline infectious peritonitis (FIP). The use of RT-PCR for FIP diagnosis is limited because of the occurrence of apparently healthy FCoV carriers. These asymptomatic cats shed the virus in the feces and, in a number of cases, also had detectable virus in the plasma. Because of the nature of FCoV infections, our RT-PCR assay with plasma or serum cannot be used to establish a definite diagnosis of FIP. However, this assay does provide a new means to identify asymptomatic FCoV carriers. As such, RT-nPCR will be of use to screen cats before their introduction into FCoV-free catteries. Moreover, this assay provides an important tool to study the epidemiology of FCoV.",,"antibody; nucleotide; virus rna; animal disease; antibody titer; article; ascites fluid; cat; controlled study; coronavirus; disease carrier; feces; nonhuman; nucleotide sequence; plasma; priority journal; reverse transcription polymerase chain reaction; tissue; virus genome; Animal; Base Sequence; Body Fluids; Carrier State; Cats; Cells, Cultured; Coronavirus, Feline; Feces; Feline Infectious Peritonitis; Molecular Sequence Data; Polymerase Chain Reaction; RNA, Viral; Sensitivity and Specificity; Support, Non-U.S. Gov't; Transcription, Genetic",,"Herrewegh, A.A.P.M.; Department of Infectious Diseases, Institute of Virology, Veterinary Faculty, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,00951137,,JCMID,"7751377","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0028892966
"Van Marle G., Luytjes W., Van der Most R.G., Van der Straaten T., Spaan W.J.M.","6603893383;6701683324;6701702352;56675761300;7007172944;","Regulation of coronavirus mRNA transcription",1995,"Journal of Virology","69","12",,"7851","7856",,50,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028883818&partnerID=40&md5=4b823598081c36cbdc0a0c6b1531a0de","Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands","Van Marle, G., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Luytjes, W., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Van der Most, R.G., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Van der Straaten, T., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands","Coronaviruses synthesize a nested set of six to eight subgenomic (sg) mRNAs in infected cells. These mRNAs are produced in different, but constant, molar ratios. It is unclear which factors control the different levels of sg mRNAs. To determine whether the intergenic sequence (IS) involved in sg mRNA synthesis could affect the transcription efficiencies of other ISs and in this way regulate transcription levels, we inserted multiple ISs at different positions into a mouse hepatitis virus defective interfering RNA. Quantitation of the sg RNAs produced by identical ISs in different sequence contexts led to the following conclusions: (i) transcription efficiency depends on the location of the IS in the defective interfering virus genome, (ii) downstream ISs have a negative effect on transcription levels from upstream ISs, and (iii) upstream ISs have little or no effect on downstream ISs. The observation that a downstream IS downregulates the amounts of sg RNA produced by an upstream IS explains why the smaller sg RNAs are, in general, produced in larger quantities than the larger sg RNAs. Our data are consistent with coronavirus transcription models in which ISs attenuate transcription. In these models, larger sg RNAs are synthesized in smaller amounts because they encounter more attenuating ISs during their synthesis.",,"messenger rna; virus rna; animal cell; article; controlled study; l cell; messenger rna synthesis; mouse; murine hepatitis coronavirus; nonhuman; priority journal; transcription regulation; virus genome; virus replication; virus transcription; Animal; Base Sequence; Comparative Study; Coronavirus; DNA Transposable Elements; Gene Expression Regulation, Viral; Kinetics; L Cells (Cell Line); Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Insertional; Oligodeoxyribonucleotides; Promoter Regions (Genetics); RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Transcription, Genetic; Transfection",,"Spaan, W.J.M.; Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands",,,0022538X,,JOVIA,"7494297","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028883818
"Kottier S.A., Cavanagh D., Britton P.","6505850323;26642890500;57203302770;","Experimental evidence of recombination in coronavirus infectious bronchitis virus",1995,"Virology","213","2",,"569","580",,93,"10.1006/viro.1995.0029","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028880390&doi=10.1006%2fviro.1995.0029&partnerID=40&md5=c0d65af47d65e185d4984f20a606bf53","Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire, RG20 7NN, United Kingdom","Kottier, S.A., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire, RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire, RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire, RG20 7NN, United Kingdom","Embryonated eggs were coinfected with two strains of the coronavirus avian infectious bronchitis virus (IBV), IBV-Beaudette and IBV-M41, to investigate whether recombination between the two strains would occur. Virions were isolated from the allantoic fluid of the coinfected eggs and putative hybrid RNAs were detected by polymerase chain reaction (PCR), using strain-specific oligonucleotides. PCR products, of the expected sizes, were obtained as predicted from potential recombination events between the nucleoprotein (N) gene and the 3'-untranslated region of the two IBV genomes. Sequencing confirmed that they corresponded to hybrid RNAs. Virus produced as a result of the mixed infection was treated with an M41-specific neutralizing monoclonal antibody and passaged in Vero cells, in which IBV-Beaudette, but not IBV-M41, replicated. Hybrid RNA was still detectable after three serial passages. Since no IBV-M41 was detectable this confirmed that infectious recombinant genomes had been produced in the embryonated eggs. These findings not only support the circumstantial evidence, from sequencing studies of IBV field strains, that recombination occurs during replication of IBV and contributes to the diversity of IBV, but also show that coronavirus RNA recombination is not limited to mouse hepatitis virus. © 1995 Academic Press, Inc.",,,"Baker, S.C., Lai, M.M.C., An in vitro system for the leader-primed transcription of coronavirus mRNA (1990) EMBO J, 9, pp. 4173-4179; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Baric, R.S., Shieh, C.K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol, 66, pp. 573-580; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol, 68, pp. 57-77; Boyer, J.C., Heanni, A., Infectious transcripts and cDNA clones of RNA viruses (1994) Virology, 198, pp. 415-426; Cavanagh, D., Davis, P.J., Evolution of avian coronavirus IBV: Sequence of the matrix glycoprotein gene and intergenic region of several serotypes (1988) J. Gen. Virol, 69, pp. 621-629; Cavanagh, D., Davis, P.J., Cook, J.K.A., Infectious bronchitis virus: Evidence for recombination within the Massachusetts serotype (1992) Avian Pathol, 21, pp. 401-408; Cavanagh, D., Davis, P.J., Pappin, D.J.C., Binns, M.M., Boursnell, M.E.G., Brown, T.D.K., Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41 (1986) Virus Res, 4, pp. 133-143; Cavanagh, D., Brian, D.A., Brinton, M., Enjuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Revision of the taxonomy of the Coronavirus, Torovirus and Arterivirus genera (1994) Arch. Virol, 135, pp. 227-237; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem, 162, pp. 156-159; Jarvis, T.C., Kirkegaard, K., Poliovirus RNA recombination: Mechanistic studies in the absence of selection (1992) EMBO J, 11, pp. 3135-3145; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol, 140, pp. 259-271; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol, 62, pp. 1810-1813; King, D.J., Cavanagh, D., Infectious bronchitis (1991) Diseases of Poultry, pp. 471-484. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoder, Eds.), Iowa State Univ. Press, Ames, IA; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol, 66, pp. 1841-1848; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Kusters, J.G., Jager, E.J., Niesters, H.G.M., Van Der Zeijst, A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Kwok, S., Kellogg, D.E., McKinney, N., Spasic, D., Goda, L., Levenson, L and Sninsky, J. J (1990) Nucleic Acids Res, 18, pp. 999-1005; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev, 56, pp. 61-79; Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J.L., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol, 56, pp. 449-456; Lambrechts, C., Pensaert, M., Ducatelle, R., Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus (1993) Avian Pathol, 22, pp. 577-590; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol, 66, pp. 6117-6124; Luo, G., Taylor, J., Template switching by reverse transcriptase during DNA synthesis (1990) J. Virol, 64, pp. 4321-4328; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol, 57, pp. 729-737; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleo-capsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol, 68, pp. 328-337; Meinkoth, J., Wahl, G., Hybridization of nucleic acids immobilized on solid supports (1984) Anal. Biochem, 138, pp. 267-284; Meyerhans, A., Vartanian, J.P., Wain-Hobson, S., DNA recombination during PCR (1990) Nucleic Acids Res, 18, pp. 1687-1691; Mockett, A.P.A., Cavanagh, D., Brown, T.D.K., Monoclonal antibodies to S1 spike and membrane proteins of avian infectious bronchitis coronavirus strain Massachusetts M41 (1984) J. Gen. Virol, 65, pp. 2281-2286; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co replicating RNAs (1992) Nucleic Acids Res, 20, pp. 3375-3381; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wang, L., Junker, D., Hock, L., Ebiary, E., Collisson, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Res, 34, pp. 327-338; Zhao, X., Shaw, K., Cavanagh, D., Presence of subgenomic mRNAs in virions of coronavirus IBV (1993) Virology, 196, pp. 172-178","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire, RG20 7NN, United Kingdom",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028880390
"Kunita S., Zhang L., Homberger F.R., Compton S.R.","6701719060;15039884400;7003348988;7102893878;","Molecular characterization of the S proteins of two enterotropic murine coronavirus strains",1995,"Virus Research","35","3",,"277","289",,15,"10.1016/0168-1702(94)00089-U","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028931605&doi=10.1016%2f0168-1702%2894%2900089-U&partnerID=40&md5=399549feb6520f19ebfdc3c5601c51ab","Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland","Kunita, S., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Zhang, L., Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland; Homberger, F.R., Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland; Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States","Enterotropic strains of murine coronaviruses (MHV-Y and MHV-RI) differ extensively in their pathogenesis from the prototypic respiratory strains of murine coronaviruses. In an effort to determine which viral proteins might be determinants of enterotropism, immunoblots of MHV-Y and MHV-RI virions using anti-S, -N and -M protein-specific antisera were performed. The uncleaved MHV-Y and MHV-RI S proteins migrated slightly faster than the MHV-A59 S protein. The MHV-Y S protein was inefficiently cleaved. The MHV-Y, MHV-RI and MHV-A59 N and M proteins showed only minor differences in their migration. The S genes of MHV-Y and MHV-RI were cloned, sequenced and found to encode 1361 and 1376 amino acid long proteins, respectively. The presence of several amino acids changes upstream from the predicted cleavage site of the MHV-Y S protein may contribute its inefficient cleavage. A high degree of homology was found between the MHV-RI and MHV-4 S proteins, whereas the homology between the MHV-Y S protein and the S proteins of other MHV strains was much lower. These results indicate that the enterotropism of MHV-RI and MHV-Y may be determined by different amino acid changes in the S protein and/or by changes in other viral proteins. © 1995.","Coronavirus; Mouse hepatitis virus; S glycoprotein","amino acid sequence; animal cell; article; controlled study; coronavirus; murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; virus strain; Amino Acid Sequence; Animal; Antibodies, Viral; Base Sequence; Capsid; Cell Line; Cloning, Molecular; DNA, Viral; Immunoblotting; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Core Proteins; Viral Envelope Proteins; Viral Matrix Proteins; Virion","Abraham, Kienzle, Lapps, Brian, Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Armstrong, Niemann, Smeekens, Rottier, Warren, Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Barthold, Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, pp. 571-601. , P.N. Bhatt, R.O. Jacoby, Academic Press, New York; Barthold, Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab. Anim. Sci., 37, pp. 36-40; Barthold, Smith, Response of genetically susceptible and resistant mice to intranasal inoculation with mouse hepatitis virus JHM (1987) Virus Res., 7, pp. 225-239; Barthold, Smith, Lord, Bhatt, Jacoby, Main, Epizootic coronaviral typhlocolitis in suckling mice (1982) Lab. Anim. Sci., 32, pp. 376-383; Barthold, Smith, Povar, Enterotropic mouse hepatitis virus infection in nude mice (1985) Lab. Anim. Sci., 35, pp. 613-618; Barthold, Beck, Smith, Enterotropic coronavirus (mouse hepatitis virus) in mice: influence of host age and strain on infection and disease (1993) Lab. Anim. Sci., 43, pp. 276-284; Binns, Boursnell, Cavanaugh, Pappin, Brown, Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) J. Gen. Virol., 66, pp. 719-726; Boireau, Crucière, LaPorte, Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) J. Gen. Virol., 71, pp. 487-492; Collins, Knobler, Powell, Buchmeier, Monoclonal antibodies to murine hepatitis virus 4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion (1982) Virology, 119, pp. 358-371; Compton, Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors (1994) Virology, 203, pp. 197-201; Compton, Barthold, Smith, The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Dalziel, Lampert, Talbot, Buchmeier, Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; De Groot, Maduro, Lenstra, Horzinek, van der Zeijst, Spaan, cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J. Gen. Virol., 68, pp. 2639-2646; Dveksler, Pensiero, Cardellichio, Williams, Jiang, Holmes, Dieffenbach, Cloning of the mouse hepatitis virus (MHV) receptor: expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Fazakerley, Parker, Bloom, Buchmeier, The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fleming, Trousdale, El-Zaatari, Stohlman, Weiner, Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Frana, Behnke, Sturman, Holmes, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Gallagher, Parker, Buchmeier, Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; (1991) Genetics Computer Group Sequence Analysis Software Package Version 7.0 Program Manual, , Genetics Computer Group, Inc, 575 Science Drive, Madison, WI 53711; Gombold, Hingley, Weiss, Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Hingley, Gombold, Lavi, Weiss, MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Homberger, Nucleotide sequence comparison of membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res., 31, pp. 49-56; Homberger, Smith, Barthold, Detection of rodent coronaviruses in tissues and cell culture by using polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Korner, Schliephake, Winter, Zimprich, Lassman, Sedgwick, Siddell, Wege, Nucleocapsid or spike protein-specific CD4+ T lymphocytes protect against coronavirus-induced encephalitis in the absence of CD8+ T cells (1991) J. Immunol., 147, pp. 2317-2323; Kunkel, Herrler, Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202; Lai, RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Luytjes, Sturman, Breedenbeek, Charite, van der Zeijst, Horzinek, Spaan, Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Mobley, Evans, Dailey, Perlman, Immune response to a murine coronavirus: identification of a homing receptor-negative CD4+ T cell subset that responds to viral glycoproteins (1992) Virology, 187, pp. 443-452; Parker, Gallagher, Buchmeier, Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Raabe, Schelle-Prinz, Siddell, Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Rasschaert, Laude, The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Robbins, Frana, McGowan, Boyle, Holmes, RNA-binding proteins of coronavirus MHV: detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Schmidt, Skinner, Siddell, Nucleotide sequence of the gene encoding the surface projection glycoprotein of the coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Spaan, Cavanaugh, Horzinek, Coronaviruses: structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stauber, Pfleiderer, Siddell, Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Stohlman, Lai, Phosphoproteins of murine hepatitis viruses (1979) J. Virol., 32, pp. 672-675; Sturman, Holmes, Behnke, Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Sturman, Ricard, Holmes, Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Taguchi, Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Tooze, Tooze, Warren, Replication of coronavirus MHV-A59 in sac-cells: determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Wang, Fleming, Lai, Sequence analysis of the spike protein gene of murine coronavirus variants: study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, Dorries, Hybridoma antibodies to the murine coronavirus JHM: characterization of epitopes on the peplomer protein (E2) (1984) J. Gen. Virol., 65, pp. 1931-1942; Wege, Winter, Meyermann, The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98; Williams, Jiang, Holmes, Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Zhang, Herbst, Kousoulas, Storz, Comparison of the S genes and biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch. Virol., 134, pp. 421-426","Compton, S.R.; Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States",,,01681702,,VIRED,"7785316","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0028931605
"Dea S., Michaud L., Milane G.","7006056287;57197459648;6508002405;","Comparison of bovine coronavirus isolates associated with neonatal calf diarrhoea and winter dysentery in adult dairy cattle in Quebec",1995,"Journal of General Virology","76","5",,"1263","1270",,19,"10.1099/0022-1317-76-5-1263","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029022181&doi=10.1099%2f0022-1317-76-5-1263&partnerID=40&md5=23d9adda0b1bd6ee106d913479737fa6","Centre de recherche en virologie, Institut Armand-Frappier, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Dea, S., Centre de recherche en virologie, Institut Armand-Frappier, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Michaud, L., Centre de recherche en virologie, Institut Armand-Frappier, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Milane, G., Centre de recherche en virologie, Institut Armand-Frappier, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Cytopathic coronaviruses were isolated in HRT-18 cells from bloody faecal samples collected from cows in Quebec dairy herds having experienced typical outbreaks of winter dysentery (WD). The formation of polykaryons in the infected cell cultures was found to be dependent on the presence of trypsin in the medium. The WD isolates differed from the prototype Mebus strain of bovine enteropathogenic coronavirus (BCV.Meb) in respect to haemagglutination inhibition (HI), haemagglutination patterns at 4°C and 37°C, and receptor destroying enzyme activity with rat erythrocytes. Other field strains of BCV associated with outbreaks of neonatal calf diarrhoea (NCD) also differed from the BCV.Meb strain by demonstrating differences in HI. In all cases, no differences were detected by virus neutralization and Western immunoblotting. Analysis and comparison of the nucleotide and deduced amino acid sequences of the PCR-amplified haemagglutinin esterase (HE) genes of one representative WD strain (BCQ.2590) and two highly cytopathic NCD strains (BCQ.3 and BCQ.571) revealed high degrees of similarities (nt and aa sequence homologies > 98%) with the BCV.Meb strain. The putative esterase active site FGDS was conserved among these four BCV strains, indicating that this domain is probably not a determinant for BCV virulence. Six amino acid substitutions occurred between the HE glycoproteins of BCV.Meb and BCQ.2590 strains; two proline substitutions occurred respectively in the signal peptide (at aa 5) and near the sequences of the putative esterase domain (at aa 53).",,"glycoprotein; trypsin; amino acid sequence; amino acid substitution; animal cell; article; Canada; cattle; Coronavirus; cytopathogenic effect; dairy industry; dysentery; erythrocyte; immunoblotting; infantile diarrhea; newborn; nonhuman; polymerase chain reaction; priority journal; rat; sequence homology; virus hemagglutination; virus virulence; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus",,"Dea, S.; Centre de recherche en virologie, Institut Armand-Frappier, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada",,"Microbiology Society",00221317,,JGVIA,"7730812","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029022181
"Bos E.C.W., Heijnen L., Spaan W.J.M.","7005778356;7004331664;7007172944;","Site directed mutagenesis of the murine coronavirus spike protein: Effects on fusion",1995,"Advances in Experimental Medicine and Biology","380",,,"283","286",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028785120&partnerID=40&md5=47a71855add3205d391f26ae08c97df8","Institute of Virology, Faculty of Medicine, University of Leiden, Leiden, Netherlands","Bos, E.C.W., Institute of Virology, Faculty of Medicine, University of Leiden, Leiden, Netherlands; Heijnen, L., Institute of Virology, Faculty of Medicine, University of Leiden, Leiden, Netherlands; Spaan, W.J.M., Institute of Virology, Faculty of Medicine, University of Leiden, Leiden, Netherlands","Mutations were introduced in the transmembrane region of the spike protein of the murine coronavirus A59. The maturation of these mutant S proteins was not affected, they were all expressed at the cell surface, and became acylated, however some mutant S proteins did not induce cell-to-cell fusion. An I→K change in the middle of the predicted transmembrane (TM) anchor and mutation of the first three cysteine residues of the TM domain resulted in a fusion-negative phenotype. We propose a model by which these data can be explained.",,"virus protein; acylation; cell fusion; cell surface; conference paper; coronavirus; gene expression; gene mutation; nonhuman; priority journal; site directed mutagenesis; Amino Acid Sequence; Animal; Cell Fusion; Comparative Study; Membrane Glycoproteins; Mice; Models, Biological; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Recombinant Proteins; Viral Envelope Proteins",,"Bos, E.C.W.; Institute of Virology, Faculty of Medicine, University of Leiden, Leiden, Netherlands",,,00652598,,AEMBA,"8830493","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028785120
"Ballesteros M.L., Sanchez C.M., Martin-Caballero J., Enjuanes L.","7006110601;57193985365;6602585656;7006565392;","Molecular bases of tropism in the PUR46 cluster of transmissible gastroenteritis coronaviruses",1995,"Advances in Experimental Medicine and Biology","380",,,"557","562",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028846735&partnerID=40&md5=35b49f87d685f835c6c2ddbbe92b7673","Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Ballesteros, M.L., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sanchez, C.M., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Martin-Caballero, J., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Transmissible gastroenteritis coronavirus (TGEV) infects both, the enteric and the respiratory tract of swine. S protein, that is recognized by the cellular receptor, has been proposed that plays an essential role in controlling the dominant tropism. The genetic relationship of S gene from different enteric strains and non-enteropathogenic porcine respiratory coronaviruses (PRCVs) was determined. A correlation between tropism and the genetic structure of the S gene was established. PRCVs, derived from enteric isolates have a large deletion at the N-terminus of the S protein. Interestingly, two respiratory isolates, attenuated Purdue type virus (PTV- ATT) and Toyarea (TOY56) have a full-length S gene. PTV-ATT has two specific amino acid differences with the S protein of the enteric viruses. One is located around position 219, within the deleted area, suggesting that alterations around this amino acid may result in the loss of enteric tropism. To study the role of different genes in tropism, a cluster of viruses closely related to PUR46 strain was analyzed. All of them have been originated by accumulating point mutations from a common, virulent isolate which infected the enteric tract. During their evolution these viruses have lost, virulence first, and then, enteric tropism. Sequencing analysis proved that enteric tropism could be lost without changes in ORFs 3a, 3b, 4, 6, and 7, and in 3'- end untranslated regions (3'-UTR). To study the role of the S protein in tropism recombinants were obtained between an enteric and a respiratory virus of this cluster. Analysis of the recombinants supported the hypothesis on the role in tropism of S protein domain around position 219.",,"cell receptor; vitronectin; animal cell; conference paper; coronavirus; intestine infection; nonhuman; point mutation; priority journal; protein domain; respiratory tract infection; sequence analysis; swine; virus gene; virus isolation; virus virulence; Animal; Cells, Cultured; Comparative Study; Genes, Viral; Male; Multigene Family; Open Reading Frames; Recombination, Genetic; RNA, Viral; Species Specificity; Support, Non-U.S. Gov't; Swine; Testis; Transmissible gastroenteritis virus; Viral Proteins; Virulence",,"Ballesteros, M.L.; Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"8830541","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028846735
"Lu Y., Lu X., Denison M.R.","47661483000;56137171400;7101971810;","Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59",1995,"Journal of Virology","69","6",,"3554","3559",,78,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029063624&partnerID=40&md5=b6fbda7d50c5e69ade1475ca6b0d43ba","Department of Pediatrics, Vanderbilt Medical School, Nashville, TN 37232-2581, United States","Lu, Y., Department of Pediatrics, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Lu, X., Department of Pediatrics, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Denison, M.R., Department of Pediatrics, Vanderbilt Medical School, Nashville, TN 37232-2581, United States","Gene 1 of the murine coronavirus, MHV-A59, encodes approximately 800 kDa of protein products within two overlapping open reading frames (ORFs 1a and 1b). The gene is expressed as a polyprotein that is processed into individual proteins, presumably by virus-encoded proteinases. ORF 1a has been predicted to encode proteins with similarity to viral and cellular proteinases, such as papain, and to the 3C proteinases of the picornaviruses (A. E. Gorbalenya, A. P. Donchenko, V. M. Blinov, and E. V. Koonin, FEBS Lett. 243:103-114, 1989; A. E. Gorbalenya, E. V. Koonin, A. P. Donchenko, and V. M. Blinov, Nucleic Acids Res. 17:4847-4861, 1989). We have cloned into a T7 transcription vector a cDNA fragment containing the putative 3C-like proteinase domain of MHV- A59, along with portions of the flanking hydrophobic domains. The construct was used to express a polypeptide in a combined in vitro transcription- translation system. Major polypeptides with molecular masses of 38 and 33 kDa were detected at early times, whereas polypeptides with molecular masses of 32 and 27 kDa were predominant after 30 to 45 min and appeared to be products of specific proteolysis of larger precursors. Mutations at the putative catalytic histidine and cysteine residues abolished the processing of the 27- kDa protein. Translation products of the pGpro construct were able to cleave the 27-kDa protein in trans from polypeptides expressed from the noncleaving histidine or cysteine mutants. The amino-terminal cleavage of the 27-kDa protein occurred at a glutamine-serine dipeptide as previously predicted. This study provides experimental confirmation that the coronaviruses express an active proteinase within the 3C-like proteinase domain of gene 1 ORF 1a and that this proteinase utilizes at least one canonical QS dipeptide as a cleavage site in vitro.",,"proteinase; article; coronavirus; enzyme analysis; molecular cloning; nonhuman; priority journal; protein degradation; rna translation; virus transcription; Amino Acid Sequence; Amino Acids; Base Sequence; Catalysis; DNA Primers; Hydrolysis; Molecular Sequence Data; Murine hepatitis virus; Protein Processing, Post-Translational; Serine Endopeptidases; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Translation, Genetic",,"Denison, M.R.; Department of Pediatrics, Vanderbilt Medical School, Nashville, TN 37232-2581, United States",,,0022538X,,JOVIA,"7745703","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029063624
"Collins A.R.","24439435400;","Interferon γ potentiates human coronavirus OC43 infection of neuronal cells by modulation of HLA class I expression",1995,"Immunological Investigations","24","6",,"977","986",,7,"10.3109/08820139509060722","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028818943&doi=10.3109%2f08820139509060722&partnerID=40&md5=6f5fd932b6fcbf58d56c6187973c3af2","Department of Microbiology, School of Medicine, State University of New York at Buffalo, Buffalo, NY, 14214, United States","Collins, A.R., Department of Microbiology, School of Medicine, State University of New York at Buffalo, Buffalo, NY, 14214, United States","HCN-1A, a human cerebral cortical neuron cell line, was examined for its susceptibility to human coronaviruses. The 229e strain replicated efficiently, but the OC43 strain did not replicate well, if at all. Treatment of the cells with interferonγ at 20U/ml for 48 hr markedly increased the susceptibility of the cells to infection with OC43 virus as shown by a 100-fold increase in secretion of infectious virus over a four day period as compared to untreated controls. The increased susceptibility was shown to be due to membrane expression of HLA class I by receptor-blockade with a monoclonal antibody specific for HLA molecules. © 1995 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.",,"HLA antibody; HLA antigen class 1; monoclonal antibody; recombinant gamma interferon; virus antibody; antigen binding; antigen expression; article; cell line; controlled study; coronavirus; human; human cell; immunofluorescence; infection prevention; infection sensitivity; inoculation; nerve cell; priority journal; virus infection; virus pathogenesis; virus replication; virus strain; Adjuvants, Immunologic; Cell Line; Cerebral Cortex; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Histocompatibility Antigens Class I; Human; Immunity, Natural; Interferon Type II; Neurons; Support, Non-U.S. Gov't; Virus Replication","McFarlin, D.E., McFarland, H., Multiple Sclerosis (1982) N. Eng. J. Med., 307, pp. 1183-1188; Sorenson, O., Dales, S., (1985) J. Virol., 56, pp. 434-445; Burks, J.S., Devald, B.L., Jankovski, L.D., Gerdes, J.C., (1980) Science, 209, pp. 933-934; Gerdes, J.C., Klein, I., Devald, B.L., Burks, J.S., (1981) J. Virol., 38, pp. 231-238; Weiss, S.R., (1983) Virol., 126, pp. 669-677; Murray, R.S., Cai, G.-Y., Holl, K., Johnson, S., Cabirac, G.F., (1993) Adv. Exptl. Biol. Med., 343, pp. 353-357; Stewart, J.N., Mounir, S., Talbot, P.J., (1992) Virol., 191, pp. 502-505; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M.C., Talbot, P.J., (1990) Virol., 174, pp. 608-612; Collins, A.R., Sorensen, O., (1986) Microbial Pathogen., 1, pp. 573-583; Pearson, J., Mim, C.A., (1985) J. Virol., 53, pp. 1016-1019; Vlasak, R., Luytes, W., Spaan, W., Palese, P., (1988) Proc. Natl. Acad. Sci., USA, 85, pp. 4526-4529; Collins, A.R., (1993) Immunol. Invest., 22, pp. 95-103; Elvin, J., Potter, C., Elliott, T., Cerundolo, V., Townsend, A., (1993) J. Immunol. Meth., 158, pp. 161-171; Mauerhoff, T., Pujol-Borrell, R., Mirakian, R., Bottazzo, G.F., (1988) J. Neuroimmunol., 18, pp. 271-289; Lampson, L.A., Fisher, C.A., (1984) PNAS, 81, pp. 6376-6480; Ronnett, G.V., Hester, L.D., Nye, J.S., Connors, K., Snyder, S.H., (1990) Science, 248, pp. 603-605; Holmes, K.V., Dveksler, G., Gagneten, S., Yeager, C., Lin, S.-H., Beauchemin, N., Look, A.T., Dieffenbach, C., (1993) Adv. Exptl. Med. Biol., 342, pp. 261-267; Steiner, I., Kennedy, P.G.E., (1995) J. Neurovirol., 1, pp. 19-29; Massa, P.T., Dorries, R., ter Meulen, V., (1986) Nature, 320, pp. 285-292; Collins, A.R., (1994) Immunol. Invest., 23, pp. 313-322; Joly, E., Oldstone, M.B.A., (1992) Neuron, 8, pp. 1185-1190; Doherty, P.C., (1995) ASM News, 61, pp. 68-71; Abbas, A.K., Lichtman, A.H., Pober, J.S., (1994) Cellular and Molecular Immunology, pp. 115-135. , editors. W.B. Saunders Co., Philadelphia Chapter 6 2nd Ed; Katze, M.G., (1993) Semin. Virol., 4, pp. 259-268; Herold, J., Siddell, S.G., (1993) Res., 21, pp. 5838-5842; Carrigan, D.R., Knox, K.K., (1990) J. Virol., 64, pp. 1606-1655","Collins, A.R.; Department of Microbiology, School of Medicine, State University of New York at Buffalo, Buffalo, NY, 14214, United States",,"Informa Healthcare",08820139,,IMINE,"8575842","English","Immunol. Invest.",Article,"Final",,Scopus,2-s2.0-0028818943
"Kai K., Kanoe M., Akagi Y., Soma T., Nomura K.","7005671795;7004595676;7102798173;7103108050;35576924100;","Biphasic immune responses of cats under controlled infection with a feline enteric coronavirus-79-1683 strain",1995,"Journal of Veterinary Medical Science","57","4",,"781","783",,1,"10.1292/jvms.57.781","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029349147&doi=10.1292%2fjvms.57.781&partnerID=40&md5=4a641e3c224c9bc94a49ad07c92188b3","Department of Veterinary Microbiology, Yamaguchi University, Yamaguchi 753, Japan; Veterinary Medicine, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753, Japan; Marupi Lifetech Co. Ltd., Ikeda, Osaka 563, Japan","Kai, K., Department of Veterinary Microbiology, Yamaguchi University, Yamaguchi 753, Japan; Kanoe, M., Department of Veterinary Microbiology, Yamaguchi University, Yamaguchi 753, Japan; Akagi, Y., Veterinary Medicine, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753, Japan; Soma, T., Marupi Lifetech Co. Ltd., Ikeda, Osaka 563, Japan; Nomura, K., Marupi Lifetech Co. Ltd., Ikeda, Osaka 563, Japan","Kittens inoculated orally with 102 PFU of feline enteric coronavirus developed no antibody to the virus despite the repeated challenges. However, they developed antibody for a long period with 5×103-1.6×105 (mean 3×104) and with 2.5×103-2×104 (mean 6×103) immunoperoxidase antibody titer when they were challenged with 105 and 103 PFU of virus following previous challenges, respectively. Viremia was found when kittens were inoculated with 105 PFU of virus, but not with 103 PFU of virus. The dose of 103 PFU of virus seemed to be a lower limit to establish infection. These results indicate that local infection induces a low antibody response and systemic infection induces a high antibody response. © 1995, JAPANESE SOCIETY OF VETERINARY SCIENCE. All rights reserved.","dose-dependent reaction; FECV","virus antibody; animal; antibody production; article; blood; cat; cat disease; classification; Coronavirus; enzyme immunoassay; immunology; pathophysiology; time; Animals; Antibodies, Viral; Antibody Formation; Cats; Coronavirus, Feline; Feline Infectious Peritonitis; Immunoenzyme Techniques; Time Factors","Boyle, J.F., Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Black, J.W., (1984) Adv. Exp. Med. Biol., 173, pp. 133-147; Kai, K., Yukimune, M., Murata, T., Uzuka, Y., Kanoe, M., Matsumoto, H., (1992) J. Vet. Med. Sci., 54, pp. 501-507; Kai, K., Kaneda, Y., Goto, N., Kanoe, M., (1987) Jpn. J. Vet. Sci., 49, pp. 1105-1111; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Pedersen, N.C., Boyle, J.F., Floyd, K., (1981) Am. J. Vet. Res., 42, pp. 363-367; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., (1984) Am. J. Vet. Res., 45, pp. 2580-2585",,,,09167250,,,"8519920","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0029349147
"Cabirac G.F., Murray R.S., McLaughlin L.B., Skolnick D.M., Hogue B., Dorovini- Zis K., Didier P.J.","6602498805;7403022204;7102364645;6603653737;7003393593;7003292809;57212824332;","In vitro interaction of coronaviruses with primate and human brain microvascular endothelial cells",1995,"Advances in Experimental Medicine and Biology","380",,,"79","88",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028785118&partnerID=40&md5=f293f2f43430285246e16fbd57164997","Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States","Cabirac, G.F., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Murray, R.S., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; McLaughlin, L.B., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Skolnick, D.M., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Hogue, B., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Dorovini- Zis, K., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Didier, P.J., Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States","Primary human and primate brain microvascular endothelial cells were tested for permissiveness to coronaviruses JHM and 229E. While sub-genomic viral RNAs could be detected up to 72 hours post-infection, primate cells were abortively infected and neither virus caused cytopathology. Human cells were non-permissive for JHM but permissive for 229E replication; peak production of progeny 229E and observable cytopathic effects occurred approximately 22 and 32 hour post-infection, respectively. Using the criterion of cytopathology induction in infected endothelial cells, 229E was compared to other human RNA and DNA viruses. In addition, virus induced modulation of intercellular adhesion molecule 1 (ICAM-1), vascular cell adhesion molecule 1 (VCAM-1) and HLA I was monitored by immunostaining of infected cells.",,"complementary dna; HLA antigen; intercellular adhesion molecule 1; vascular cell adhesion molecule 1; virus rna; animal cell; antigen expression; brain circulation; central nervous system infection; conference paper; coronavirus; cytopathogenic effect; human; human cell; immunohistochemistry; microvasculature; nonhuman; primate; priority journal; vascular endothelium; virus detection; virus replication; Animal; Antibodies, Monoclonal; Antigens, Viral; Brain; Cell Line; Cercopithecus aethiops; Comparative Study; Coronavirus; Coronavirus 229E, Human; Endothelium, Vascular; Gene Expression; Human; Immunohistochemistry; Intercellular Adhesion Molecule-1; Kinetics; Microcirculation; Primates; RNA, Viral; Species Specificity; Time Factors; Transcription, Genetic; Vascular Cell Adhesion Molecule-1; Vero Cells; Virus Replication",,"Cabirac, G.F.; Swedish Medical Center, RMMSC, Colorado Neurological Institute, Englewood, CO, United States",,,00652598,,AEMBA,"8830550","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028785118
"Hiscox J.A., Mawditt K.L., Cavanagh D., Britton P.","7004565877;6603252273;26642890500;57203302770;","Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts",1995,"Journal of Virology","69","10",,"6219","6227",,46,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029150543&partnerID=40&md5=75a823a2429ad630aba0fff437f44dce","Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom","Hiscox, J.A., Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom; Mawditt, K.L., Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom","The subgenomic mRNAs of the coronavirus transmissible gastroenteritis virus (TGEV) are not produced in equimolar amounts. We have developed a reporter gene system to investigate the control of this differential subgenomic mRNA synthesis. Transcription of mRNAs by the TGEV polymerase was obtained from negative sense RNA templates generated in situ from DNA containing a T7 promoter. A series of gene cassettes was produced; these cassettes comprised the reporter chloramphenicol acetyltransferase (CAT) gene downstream of transcription-associated sequences (TASs) (also referred to as intergenic sequences and promoters) believed to be Involved in the synthesis of TGEV subgenomic mRNAs 6 and 7. The gene cassettes were designed so that negative-sense RNA copies of the CAT gene with sequences complementary to the TGEV TASs, or modified versions, at the 3' end would be synthesized in situ by T7 RNA polymerase. Using this system, we have demonstrated that CAT was expressed from mRNAs derived from the T7-generated negative-sense RNA transcripts only in TGEV-infected cells and only from transcripts possessing a TGEV negative-sense TAS. Analysis of the CAT mRNAs showed the presence of the TGEV leader RNA sequence at the 5' end, in keeping with observations that all coronavirus mRNAs have a 5' leader sequence corresponding to the 5' end of the genomic RNA. Our results indicated that the CAT mRNAs were transcribed from the in situ-synthesized negative-sense RNA templates without the requirement of TGEV genomic 5' or 3' sequences on the T7, generated negative- sense transcripts (3'-TAS-CAT-5'). Modification of the TGEV TASs indicated (i) that the degree of potential base pairing between the 3' end of the leader RNA and the TGEV negative-sense TAS was not the sole determinant of the amount of subgenomic mRNA transcribed and (ii) that other factors, including nucleotides flanking the TAS, are involved in the regulation of transcription of TGEV subgenomic mRNAs.",,"chloramphenicol acetyltransferase; messenger rna; virus rna; amino acid sequence; article; coronavirus; gene expression regulation; messenger rna synthesis; nonhuman; priority journal; promoter region; reporter gene; sequence analysis; transcription regulation; virus transcription; Animal; Bacteriophage T7; Base Sequence; Cell Line; Chloramphenicol O-Acetyltransferase; DNA Primers; Gene Expression Regulation, Viral; Molecular Sequence Data; Mutagenesis, Insertional; Oligodeoxyribonucleotides; Polymerase Chain Reaction; Promoter Regions (Genetics); Recombinant Proteins; RNA, Messenger; Support, Non-U.S. Gov't; Templates, Genetic; Transcription, Genetic; Transfection; Transmissible gastroenteritis virus",,"Britton, P.; Division of Molecular Biology, Institute for Animal Health, Berkshire RG20 7NN, United Kingdom",,,0022538X,,JOVIA,"7666523","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029150543
"Rossen J.W.A., Bekker C.P.J., Voorhout W.F., Horzinek M.C., Van Der Ende A., Strous G.J.A.M., Rottier P.J.M.","7005977394;56403027300;7003796069;7102624836;7007055960;7004975908;7006145490;","Coronaviruses in polarized epithelial cells",1995,"Advances in Experimental Medicine and Biology","380",,,"135","138",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028839923&partnerID=40&md5=a361b5a798e061505a92fefadd51fa2a","Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands","Rossen, J.W.A., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Bekker, C.P.J., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Voorhout, W.F., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Horzinek, M.C., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Van Der Ende, A., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Strous, G.J.A.M., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands","Coronaviruses have a marked tropism for epithelial cells. In this paper the interactions of the porcine transmissible gastroenteritis virus (TGEV) and mouse hepatitis virus (MHV-A59) with epithelial cells are compared. Porcine (LLC-PK1) and murine (mTAL) epithelial cells were grown on permeable supports. By inoculation from the apical or basolateral side both TGEV and MHV-A59 were found to enter the polarized cells only through the apical membrane. The release of newly synthesized TGEV from LLC-PK1 cells occurred preferentially from the apical plasma membrane domain, as evidenced by the accumulation of viral proteins and infectivity in the apical culture fluid. In contrast, MHV was released preferentially from the basolateral membrane of mTAL cells. The apical release of TGEV and the basolateral release of MHV may explain the in vivo establishment of a local and systemic infection, respectively.",,"virus protein; animal cell; basolateral membrane; cell culture; cell line; cell membrane; conference paper; coronavirus; enterovirus; epithelium cell; inoculation; kidney proximal tubule; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virus cell interaction; virus infectivity; Animal; Autoradiography; Capsid; Cell Line; Coronavirus; Electrophoresis, Polyacrylamide Gel; Epithelium; Membrane Glycoproteins; Methionine; Mice; Murine hepatitis virus; RNA Viruses; Sulfur Radioisotopes; Swine; Viral Core Proteins; Viral Envelope Proteins; Viral Proteins; Virus Replication",,"Rossen, J.W.A.; Institute of Virology, Utrecht University, Yalelaan 1, 584 CL Utrecht, Netherlands",,,00652598,,AEMBA,"8830469","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028839923
"Schultze B., Herrler G.","7006104520;7006339246;","Polarized entry of bovine coronavirus in epithelial cells",1995,"Advances in Experimental Medicine and Biology","380",,,"375","378",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028818616&partnerID=40&md5=02f13010899db4caefc2d1655aa26be8","Institut fur Virologie, Philipps-Universitat Marburg, Marburg, Germany","Schultze, B., Institut fur Virologie, Philipps-Universitat Marburg, Marburg, Germany; Herrler, G., Institut fur Virologie, Philipps-Universitat Marburg, Marburg, Germany","Epithelial cells are highly polarized cells divided into an apical and a basolateral plasma membranae. The two domains are composed of a distinct set of proteins and lipids. Concerning virus infection of epithelial cells, the polarity of host cell receptor distribution defines the domain from which infection may be mediated. We were interested to analyze the infection of polarized cells by bovine coronavirus (BCV). The entry of BCV into MDCK I cells was investigated by growing the cells on a permeable support. Cell were infected with BCV from either the apical or basolateral domain. These efficiency of infection was determined my measuring the hemaglutinating activity of the virus released into the apical compartment. Virus replication was only detectable after inoculation from the apical surface. Therefore, infection of MDCK I cells with BCV is restricted to the apical side.",,"lipid; protein; receptor; animal cell; binding site; conference paper; coronavirus; dog; epithelium cell; filter; influenza virus c; nonhuman; priority journal; virus infection; Animal; Cattle; Cell Line; Cell Membrane; Chick Embryo; Comparative Study; Coronavirus, Bovine; Dogs; Epithelium; Hemagglutination; Influenzavirus C; Species Specificity",,"Schultze, B.; Institut fur Virologie, Philipps-Universitat Marburg, Marburg, Germany",,,00652598,,AEMBA,"8830511","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028818616
"Dales S.","7005597434;","Factors controlling coronavirus infections and disease of the central nervous system: A review",1995,"Advances in Experimental Medicine and Biology","380",,,"13","22",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028882527&partnerID=40&md5=646bf10b7ed805d39d7d568ea5edc647","Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada","Dales, S., Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada","There is a correlation between specificity of tropism of JHMV for O-2A lineage cells from the rat and demyelination of white mailer, associated with chronic disease. Susceptibility to infection, which can occur in O-2A cells before terminal differentiation may be influenced by cytokines. During the normal, age-related or rapidly induced maturation/differentiation of rat oligodendrocytes, suppression of JHMV replication is correlated with upregulation of the subunit R1 of the cAMP-dependent protein kinase. Virus inhibition occurs at a stage between penetration and initiation of genome expression. Regulation over coronavirus infection of oligodendroglia is strictly controlled by the host cell. There is evidence that induction of R1 subunit of protein kinase A influences uncoating, illustrated in Figure 9, by suppression of dephosphorylation during penetration. Our former working hypothesis, now borne out by recent data predicts that the infection in mature oligodendrocytes is blocked because specific dephosphorylation of the capsid protein N, required for uncoating, etc. is suppressed.",,"basic fibroblast growth factor; bucladesine; cyclic amp dependent protein kinase; platelet derived growth factor; virus rna; animal cell; animal model; central nervous system infection; chronic disease; conference paper; coronavirus; demyelinating disease; genetic variability; human; immune response; infection resistance; mouse; nerve cell culture; oligodendroglia; priority journal; virus cell interaction; virus infection; virus replication; Amino Acid Sequence; Animal; Brain; Capsid; Central Nervous System Diseases; Comparative Study; Coronavirus; Coronavirus Infections; Human; Mice; Mice, Inbred Strains; Molecular Sequence Data; Sequence Homology, Amino Acid; tau Proteins; Viral Core Proteins; Virus Replication",,"Dales, S.; Dept. of Microbiology and Immunology, University of Western Ontario, London, Ont. N6A 5C1, Canada",,,00652598,,AEMBA,"8830467","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028882527
"Joo M., Makino S.","23008647300;7403067550;","Analysis of coronavirus transcription regulation",1995,"Advances in Experimental Medicine and Biology","380",,,"473","478",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028784075&partnerID=40&md5=3c809dd126b67b325498b9ffd99ac59f","Department of Microbiology, University of Texas, Austin, TX, United States","Joo, M., Department of Microbiology, University of Texas, Austin, TX, United States; Makino, S., Department of Microbiology, University of Texas, Austin, TX, United States","Insertion of an intergenic region from murine coronavirus mouse hepatitis virus (MHV) into an MHV defective interfering (DI) RNA led to transcription of subgenomic DI RNA in helper virus-infected cells. Using this system we studied how two intergenic regions positioned in close proximity affected subgenomic RNA synthesis. When two intergenic regions were separated by more than 100 nt, slightly less of the larger subgenomic DI RNA (synthesized from the upstream intergenic region) was made; this difference was significant when the intergenic region separation was less than about 35 nucleotides. Deletion of sequences flanking the two intergenic regions inserted in close proximity did not affect transcription. No significant change in the ratio of the two subgenomic DI RNAs was observed when the sequence between the two intergenic regions was altered. Removal of the downstream intergenic region restored transcription of the larger subgenomic DI RNA. These results demonstrated the downstream intergenic sequence was suppressing subgenomic DI RNA synthesis from the upstream intergenic region.",,"rna; conference paper; coronavirus; nonhuman; priority journal; reverse transcription polymerase chain reaction; rna synthesis; rna transcription; Animal; Cell Line; DNA Primers; Gene Expression Regulation, Viral; Helper Viruses; Introns; Mice; Murine hepatitis virus; Polymerase Chain Reaction; RNA, Viral; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Transfection",,"Joo, M.; Department of Microbiology, University of Texas, Austin, TX, United States",,,00652598,,AEMBA,"8830526","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028784075
"Chen C.-M., Cavanagh D., Britton P.","7501958673;26642890500;57203302770;","Cloning and sequencing of a 8.4-kb region from the 3′-end of a Taiwanese virulent isolate of the coronavirus transmissible gastroenteritis virus",1995,"Virus Research","38","1",,"83","89",,17,"10.1016/0168-1702(95)00046-S","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029102841&doi=10.1016%2f0168-1702%2895%2900046-S&partnerID=40&md5=56cd8d16dec753f357a23a4af046c008","Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Chen, C.-M., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","The nucleotide sequence (8396 nucleotides) was determined, from the 3′-end of the putative polymerase gene to the poly(A) tail, for a Taiwanese virulent isolate, TFI, of transmissible gastroenteritis virus (TGEV). The TFI nucleotide sequence had very high identity to the British virulent field isolate FS772/70 (98.3%), the attenuated Purdue 115 (96.7%) and from the S gene to ORF-4 gene region, to the low passaged virulent Miller (98.3%) strains of TGEV. Comparison of the TFI S protein sequence with those determined from other TGEV strains and those of the TGEV variant, porcine respiratory coronavirus, isolated from Europe and North America showed that they had changed very little over a period of 4 decades. The two extra amino acids found to be present in the spike proteins of the virulent FS772/70 and Miller strains when compared to the avirulent Purdue strain were found to be present in the TFI strain. The genomic organisation of the TFI strain was the same as that of the other TGEV viruses. © 1995.","Coronavirus; Porcine; Swine; Transmissible gastroenteritis virus (TGEV)","article; controlled study; coronavirus; molecular cloning; nonhuman; nucleotide sequence; priority journal; taiwan; virus isolation; virus virulence; Animal; Base Sequence; Cloning, Molecular; DNA, Viral; Membrane Glycoproteins; Molecular Sequence Data; Open Reading Frames; Phylogeny; Support, Non-U.S. Gov't; Taiwan; Transmissible gastroenteritis virus; Viral Envelope Proteins; Virulence","Britton, Page, Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res., 18, pp. 71-80; Britton, Mawditt, Page, The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Britton, Kottier, Chen, Pocock, Salmon, Aynaud, The use of PCR genome mapping for the characterisation of TGEV strains (1993) Coronaviruses: Molecular Biology and Virus-Host Interactions, 342, pp. 29-34. , H. Laude, J.F. Vautherot, Adv. Exp. Med. Biol., Plenum Press, New York; Chen, Tien, Wu, Chu, The phenotype of Taiwan field isolated transmissible gastroenteritis virus (TGEV) is different from the other TGEV (1989) J. Chin. Soc. Vet. Sci., 15, pp. 11-18; Correa, Gebauer, Bullido, Sune, Baay, Zwaagstra, Posthumus, Enjuanes, Localisation of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis virus (1990) J. Gen. Virol., 71, pp. 271-279; Delmas, Rasschaert, Godet, Gelfi, Laude, Four Major Antigenic Sites of the Coronavirus Transmissible Gastroenteritis Virus Are Located on the Amino-Terminal Half of Spike Glycoprotein S (1990) J. Gen. Virol., 71, pp. 1313-1323; Devereux, Haeberli, Smithies, A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Res., 12, pp. 387-395; Eck, Dayhoff, (1966) Atlas of Protein Sequence and Structure 1966, , National Biomedical Research Foundation, Maryland, Silver Spring; Felsenstein, Phylogenies from molecular sequences: inferences and reliability (1988) Am. Rev. Genet., 22, pp. 512-565; Fitch, Margoliash, Construction of phylogenetic trees (1967) Science, 155, pp. 279-284; Higgins, Sharp, CLUSTAL: a package for performing multiple sequence alignment on a microcomputer (1988) Gene, 73, pp. 237-244; Page, Mawditt, Britton, Sequence comparison of the 5′ end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J. Gen. Virol., 72, pp. 579-587; Posthumus, Lenstra, Schaaper, van Nieuwstadt, Enjuanes, Meloen, Analysis and simulation of a neutralising epitope of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 3304-3309; Rasschaert, Laude, The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Rasschaert, Duarte, Laude, Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Sánchez, Gebauer, Suñé, Mendez, Dopazo, Enjuanes, Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virology, 190, pp. 92-105; Staden, Automation of the computer handling of gel reading data produced by the shotgun method of DNA sequencing (1982) Nucleic Acids Res., 10, pp. 4731-4751; Wang, Junker, Hock, Ebiary, Collisson, Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Res., 34, pp. 327-338; Wesley, Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain) (1990) Coronaviruses and their Diseases, 276, pp. 301-306. , D. Cavanagh, T.D.K. Brown, Adv. Exp. Med. Biol, Plenum Press, New York; Wesley, Woods, Cheung, Genetic-basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesley, Woods, Cheung, Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; email: Britton@BBSRC.AC.UK",,,01681702,,VIRED,"8546012","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0029102841
"Hein A., Schwender S., Imrich H., Sopper S., Czub M., Dörries R.","8047618900;7003953447;6602841707;6701733153;57200253688;7003359298;","Phenotypic and functional characterization of CD8+ T lymphocytes from the central nervous system of rats with coronavirus JHM induced demyelinating encephalomyelitis.",1995,"Journal of neurovirology","1","5-6",,"340","348",,7,"10.3109/13550289509111023","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029420053&doi=10.3109%2f13550289509111023&partnerID=40&md5=4f1865f70b8d2fdd89c2c74036054587","Institut für Virologie und Immunbiologie, University of Würzburg, Germany","Hein, A., Institut für Virologie und Immunbiologie, University of Würzburg, Germany; Schwender, S., Institut für Virologie und Immunbiologie, University of Würzburg, Germany; Imrich, H., Institut für Virologie und Immunbiologie, University of Würzburg, Germany; Sopper, S., Institut für Virologie und Immunbiologie, University of Würzburg, Germany; Czub, M., Institut für Virologie und Immunbiologie, University of Würzburg, Germany; Dörries, R., Institut für Virologie und Immunbiologie, University of Würzburg, Germany","Intracerebral infection of Lewis (LEW) inbred rats with the neurotropic strain of the murine coronavirus JHM (JHMV) frequently results in a monophasic paralytic disease. In contrast, infection of Brown Norway (BN) inbred rats does not lead to clinical disease. Previous findings indicated that in both rat strains brain-infiltrating leukocytes consisted mainly of CD8+ T lymphocytes. Here, we phenotypically as well as functionally characterised this T cell subset after isolation from the central nervous system (CNS). Using JHMV-infected target cells, MHC class I restricted, cytotoxic T lymphocytes were demonstrated to be present in the leukocyte fraction from the CNS of both, susceptible LEW and disease-resistant BN rats. However, compared to infected, but healthy BN rats, diseased LEW rats generated an enhanced cytotoxic immune response which became most prominent at the maximum of neurological disease. Recently published observations from our laboratory demonstrated a strong virus-specific antibody response in the CNS of BN rats. In LEW rats, however, the response was delayed and of low magnitude. This suggests, that consequences of cytotoxic T lymphocyte action in JHMV-infected CNS tissue largely depend on the efficacy of an accompanying virus-specific humoral immune response.",,"HLA antigen class 1; HLA antigen class 2; monoclonal antibody; virus antibody; animal; article; brain; CD8+ T lymphocyte; cell culture; cytology; cytotoxic T lymphocyte; demyelinating disease; flow cytometry; germfree animal; immunology; Lewis rat; multiple myeloma; Murine hepatitis coronavirus; phenotype; rat; spleen; virology; virus encephalitis; virus infection; Animals; Antibodies, Monoclonal; Antibodies, Viral; Brain; CD8-Positive T-Lymphocytes; Coronavirus Infections; Demyelinating Diseases; Encephalitis, Viral; Flow Cytometry; Histocompatibility Antigens Class I; Histocompatibility Antigens Class II; Multiple Myeloma; Murine hepatitis virus; Phenotype; Rats; Rats, Inbred Lew; Specific Pathogen-Free Organisms; Spleen; T-Lymphocytes, Cytotoxic; Tumor Cells, Cultured",,"Hein, A.",,,13550284,,,"9222376","English","J. Neurovirol.",Article,"Final",Open Access,Scopus,2-s2.0-0029420053
"Baca-Estrada M.E., Liang X., Babiuk L.A., Yoo D.","7004011163;57212902064;35427029400;7103242554;","Induction of mucosal immunity in cotton rats to haemagglutinin-esterase glycoprotein of bovine coronavirus by recombinant adenovirus",1995,"Immunology","86","1",,"134","140",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029082562&partnerID=40&md5=d016883be9883a535f5d73b5d8bf2ffc","Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada","Baca-Estrada, M.E., Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Liang, X., Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Babiuk, L.A., Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Yoo, D., Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada","An effective vaccine against enteric bovine coronavirus (BCV) must be able to induce mucosal immunity. We recently described the construction of recombinant human adenovirus type 5 (hAdS) carrying the BCV haemagglutinin-esterase (HE) gene in the early transcription region 3 of the adenovirus genome. In this study, we examined the induction of systemic and mucosal immune responses to the hAdS vector carrying the BCV HE gene (AdBcHE) following intranasal or enteric immunization of cotton rats. Regardless of the route of administration, mucosal immunization with AdBcHE induced significant levels of anti-HE IgG antibodies in serum. In addition, following intranasal immunization with AdBcHE, significant levels of anti-HE IgA antibodies were found in lung washes of immunized cotton rats. Furthermore, the specific anti-HE antibodies in sera and mucosal secretions efficiently neutralized BCV infectivity in vitro. T-cell proliferation and cell-mediated cytotoxic responses against the BCV HE were elicited in the spleen of intranasally immunized animals. The results demonstrate that mucosal immunization with AdBcHE is capable of inducing both systemic and mucosal immunity to the BCV HE. These immune responses may be important in protecting animals from BCV infection.",,"esterase; immunoglobulin g; virus hemagglutinin; virus vaccine; adenovirus; animal experiment; antibody response; article; controlled study; coronavirus; female; immunization; male; mucosa; nonhuman; priority journal; rat; virus recombinant; Adenoviridae; Administration, Intranasal; Administration, Topical; Animal; Antibodies; Coronavirus Infections; Coronavirus, Bovine; Duodenum; Genetic Vectors; Glycoproteins; Hemagglutinins, Viral; Hesperomyinae; Immunity, Cellular; Immunity, Mucosal; Immunization; Immunoglobulin G; Lung; Support, Non-U.S. Gov't; Vaccines, Synthetic; Viral Proteins",,"Baca-Estrada, M.E.; Vet. Infectious Dis. Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada",,,00192805,,IMMUA,"7590874","English","IMMUNOLOGY",Article,"Final",,Scopus,2-s2.0-0029082562
"Hiscox J.A., Cavanagh D., Britton P.","7004565877;26642890500;57203302770;","Quantification of individual subgenomic mRNA species during replication of the coronavirus transmissible gastroenteritis virus",1995,"Virus Research","36","2-3",,"119","130",,21,"10.1016/0168-1702(94)00108-O","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028915630&doi=10.1016%2f0168-1702%2894%2900108-O&partnerID=40&md5=05977b186d51ba9dd83864d5cc170d80","Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG16 0NN, United Kingdom","Hiscox, J.A., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG16 0NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG16 0NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG16 0NN, United Kingdom","A biotinylated-oligonucleotide-based method was used to isolate the subgenomic mRNAs of the coronavirus transmissible gastroenteritis virus (TGEV) to investigate the amounts of the mRNAs produced at early, middle and late times in the replication cycle. TGEV mRNA 6, which encodes the N protein, was observed to be the most abundant species throughout the replication cycle. The ratios of mRNA 6 to the other mRNAs were 1:0.11 (mRNA 2), 1:0.16 (mRNAs 3 and 4) and 1:0.37 (mRNA 5) at 12 h post-infection. All the mRNA species were differentially regulated throughout the replication cycle, although the rate of accumulation of mRNAs 4, 5, and 6, but not mRNA 3, increased markedly towards the end of the replication cycle. mRNA 7 was not detected in the system used. There was no observable correlation between the amounts of each mRNA synthesised and the potential degree of base pairing between the 3′ end of the leader sequence and the transcription associated sequences on the genomic RNA at any time during the replication cycle. This indicates that the extent of base pairing was not the only factor involved in the control of subgenomic mRNA synthesis. © 1995.","Coronavirus; Leader RNA; mRNA; Porcine; TGEV; Transcription","messenger rna; article; coronavirus; gastroenteritis; nonhuman; priority journal; quantitative assay; virus replication; Animal; Base Sequence; Conserved Sequence; Gastroenteritis, Transmissible, of Swine; Gene Expression Regulation, Viral; Molecular Sequence Data; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Swine; Virus Replication","Britton, Carmenes, Page, Garwes, Parra, Sequence of the nucleoprotein from a virulent British field isolate of transmissible gastroenteritis virus and its expression in Saccharomyces cerevisiae (1988) Mol. Microbiol., 2, pp. 89-99; Britton, Mawditt, Page, The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Britton, Page, Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res., 18, pp. 71-80; Budzilowicz, Wilcynski, Weiss, Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Chamberlain, Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate (1979) Anal. Biochem., 98, pp. 132-135; Chomczynski, Sacchi, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Compton, Rogers, Holmes, Fertsch, Remenick, McGowan, In vitro replication of mouse hepatitis virus strain A59 (1987) J. Virol., 61, pp. 1814-1820; de Groot, ter Haar, Horzinek, van der Zeijst, Intracellular RNAs of the feline infectious peritonitis coronavirus strain 791146 (1987) J. Gen. Virol., 68, pp. 995-1002; Ekenberg, McKormick, Smith, (1992) Promega Notes, 39, pp. 7-10; Godet, L'Haridon, Vautherot, Laude, TGEV coronavirus ORF-4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Hofmann, Sethna, Brian, Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture (1990) J. Virol., 64, pp. 4108-4114; Hofmann, Wyler, Propagation of the virus of porcine epidemic diarrhoea in cell culture (1988) J. Clin. Microbiol., 26, pp. 2235-2239; Horsburgh, Brierley, Brown, Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Jacobs, Van Der Zeijst, Horzinek, Characterization and translation of transmissible gastroenteritis virus mRNAs (1986) J. Virol., 57, pp. 1010-1015; Jeong, Makino, Mechanism of coronavirus transcription: duration of primary transcription initiation activity and effects of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Lai, Coronavirus—organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, Baric, Brayton, Stohlman, Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, Stohlman, The RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Page, Britton, Boursnell, Sequence analysis of the leader RNA of two porcine coronaviruses: transmissible gastroenteritis virus and porcine respiratory coronavirus (1990) Virus Genes, 4, pp. 289-301; Page, Mawditt, Britton, Sequence comparison of the 5′-end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J. Gen. Virol., 72, pp. 579-587; Sambrook, Fritsch, Maniatis, (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, New York; Sawicki, Sawicki, Coronavirus transcription—subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sethna, Hofmann, Brian, Minus-strand copies of replicating coronavirus mRNAs contain anti leaders (1991) J. Virol., 65, pp. 320-325; Sethna, Hung, Brian, Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shieh, Soe, Makino, Chang, Stohlman, Lai, The 5′-end sequence of the murine coronavirus genome—implications for mor multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; van der Most, de Groot, Spaan, Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: a study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Wesley, Cheung, Michael, Woods, Nucleotide sequence of coronavirus TGEV genomic RNA: evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Yokomori, Banner, Lai, Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic-lenght template (1992) J. Virol., 66, pp. 4671-4678","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG16 0NN, United Kingdom; email: Britton@BBSRC.AC.UK",,,01681702,,VIRED,"7653093","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0028915630
"Flori J., Mousing J., Gardner I., Willeberg P., Have P.","25934091000;56615752500;35401169500;7003580012;6603869973;","Risk factors associated with seropositivity to porcine respiratory coronavirus in Danish swine herds",1995,"Preventive Veterinary Medicine","25","1",,"51","62",,12,"10.1016/0167-5877(95)00498-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0040053300&doi=10.1016%2f0167-5877%2895%2900498-X&partnerID=40&md5=c2a3a0b6a4a9909aafd419726e218508","Federation of Danish Pig Producers and Slaughterhouses, Axelborg, Axeltorv 3, DK-1609 Copenhagen V, Denmark, Denmark; Department of Medicine and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Division of Ethology and Health, Royal Veterinary and Agricultural University, Bülowsvej 13, DK-1870 Frederiksberg C, Denmark; State Veterinary Institute for Virus Research, Lindholm, DK-4771 Kalvehave, Denmark, Denmark","Flori, J., Federation of Danish Pig Producers and Slaughterhouses, Axelborg, Axeltorv 3, DK-1609 Copenhagen V, Denmark, Denmark, Division of Ethology and Health, Royal Veterinary and Agricultural University, Bülowsvej 13, DK-1870 Frederiksberg C, Denmark; Mousing, J., Federation of Danish Pig Producers and Slaughterhouses, Axelborg, Axeltorv 3, DK-1609 Copenhagen V, Denmark, Denmark; Gardner, I., Department of Medicine and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Willeberg, P., Division of Ethology and Health, Royal Veterinary and Agricultural University, Bülowsvej 13, DK-1870 Frederiksberg C, Denmark; Have, P., State Veterinary Institute for Virus Research, Lindholm, DK-4771 Kalvehave, Denmark, Denmark","Serological screening of swine herds in 1984 indicated that porcine respiratory coronavirus (PRCV) had been introduced into Denmark. To determine risk factors associated with the introduction of PRCV, a cross-sectional study of 408 Danish swine herds was carried out between May 1985 and June 1986. The association between herd-PRCV serological status and possible risk factors, obtained from a field questionnaire, was assessed by unconditional maximum likelihood logistic regression. An increasing herd size, location in the Jutland peninsula (compared with location on the island of Funen) (OR = 7.9 in a multivariable logistic regression model not including interaction terms), the presence of a slurry system (i.e. pigs living on a slatted floor) (OR = 4.6) and purchase of pigs (OR= 1.7) were significantly (P < 0.05) associated with seropositivity. Two significant interactions, both involving herd size, were subsequently identified. The PRCV serological status of neighbouring herds was found to be related, and closeness of a seropositive herd was associated with an increased risk of a herd being serologically positive. The results of this study indicate that herd size may be an important determinant of airborne transmission of PRCV infection, and that herd size may modify the effect of other risk factors. © 1995.","Airborne infections; PRCV; Risk factors",,"Brown, Paton, Serological studies of TGE in Great Britain using a competitive ELISA (1991) Vet. Rec., 128, pp. 500-503; Callebaut, Correa, Pensaert, Jimenez, Enjuanes, Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) Journal of General Virology, 69, pp. 1725-1730; Callebaut, Pensaert, Hooyberghs, A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with the transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet. Microbiol., 20, pp. 9-19; Christensen, Mousing, Mortensen, Soerensen, Strandbygaard, Henriksen, Andersen, Evidence of long-distance airborne transmission of Aujeszky's disease (pseudorabies) virus (1990) Vet. Rec., 127, pp. 471-474; Cox, Hooyberghs, Pensaert, Sites of replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Garwes, Stewart, Cartwright, Differentiation of porcine respiratory coronavirus from transmissible gastroenteritis virus (1988) Vet. Rec., 122, pp. 86-87; Haberman, (1979) Analysis of Qualitative Data, pp. 519-532. , Academic Press, Chicago, IL; Henningsen, Mousing, Aalund, Porcine corona virus i Danmark. En epidemiologisk tværsnitsundersøgelse baseret på screening-område spørgeskema data (1989) Dansk Vet. Tidsskr., 71, pp. 1168-1177; Hosmer, Lemeshow, (1989) Applied Logistic Regression, p. 38. , Wiley, New York; Hosmer, Lemeshow, (1989) Applied Logistic Regression, p. 81. , Wiley, New York; Hosmer, Lemeshow, (1989) Applied Logistic Regression, pp. 82-134. , Wiley, New York; Kahn, Sempos, (1989) Statistical Methods in Epidemiology, pp. 137-167. , MacMahon, New York, Oxford; (1986) Landbrugsstatistik, , Denmarks Statistical Bureau; (1987) Landbrugsstatistik, , Denmarks Statistical Bureau; Laude, Gelfi, Rasschaert, Delmas, Caracterisation antigénique du coronavirus respiratoìre porcin à l'aide d'anticorps monoclonaux dirigés contre le virus de la gastroentérite transmissible (1988) J. Rech. Porcine France, 20, pp. 89-94; Martin, Meek, Willeberg, (1987) Veterinary Epidemiology. Principles and Methods, p. 45. , Iowa State University Press, Ames, Iowa; Onno, Jesti, Cariolet, Vannier, Rapid diagnosis of TGEV-like coronavirus in fattened pigs by indirect immunofluorescence labelling in nasal cells (1989) J. Vet. Med., Ser. B, 36, pp. 629-634; O'Toole, Brown, Bridges, Cartwright, Pathogenicity of experimental infection with ‘pneumotropic’ porcine coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, Cox, Porcine respiratory coronavirus related to transmissible gastroenteritis virus (1989) Agri-Practice, 10, pp. 17-21; Pensaert, Callebaut, Vergote, Isolation of a porcine respiratory, non-enteritic coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Pensaert, Cox, van Deun, Callebaut, A seroepizootiological study of porcine coronavirus in Belgian swine (1993) Vet. Q., 15, pp. 16-20; Sanchez, Jimenez, Laviada, Correa, Sune, Bullido, Gebauer, Enjuanes, Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Simkins, Weilnau, Bias, Saif, Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am. J. Vet. Res., 53, pp. 1253-1258; Statistical Analysis Systems Institute Inc., (1989) SAS User's Guide, 2, pp. 1071-1126. , 4th edn., SAS Institute Inc, Cary, NC, Version 6; Statistical Analysis Systems Institute Inc., (1990) SAS Procedures Guide, pp. 617-634. , 3rd edn., SAS Institute Inc, Cary, NC, Version 6; Straw, A look at the factors that contribute to the development of swine pneumonia (1986) Vet. Med., pp. 747-756. , August:; Strom, (1978) Heat loss from swine and poultry as a basis for design of environmental control systems in livestock buildings, pp. 46-47. , Statens Byggeforskningsinstitut, Denmark; Van Nieuwstadt, Boonstra, Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus, using monoclonal antibodies to antigenic sites A and X of the S glycoprotein (1992) Am. J. Vet. Res., 53, pp. 184-190; Van Nieuwstadt, Pol, Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pigs (1989) Vet. Rec., 124, pp. 43-44; Van Nieuwstadt, Zetstra, Boonstra, Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet. Rec., 125, pp. 58-60; Wesley, Woods, Hill, Biwer, Evidence of a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritidis virus in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Willeberg, Gardner, Mortensen, Mousing, Models of herd size effects in swine diseases (1994) Proc. 7th International Symposium on Veterinary Epidemiology and Economics, , Nairobi; Witte, Micro-color test for assay of transmissible gatroenteritis virus-neutralizing antibodies (1971) Arch. Gesamte Virusforsch., 33, pp. 171-176","Mousing, J.",,,01675877,,PVMEE,,"English","Prev. Vet. Med.",Article,"Final",,Scopus,2-s2.0-0040053300
"Callebaut P., Pensaert M.","6603634162;55905425400;","Expression and immunogenicity of the spike glycoprotein of porcine respiratory coronavirus encoded in the E3 region of adenovirus",1995,"Advances in Experimental Medicine and Biology","380",,,"265","270",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028884134&partnerID=40&md5=08e5df889ba8b6e1495f60c54d01d6f9","Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium","Callebaut, P., Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium; Pensaert, M., Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium","The full length spike (S) gene of porcine respiratory coronavirus (PRCV) was inserted into the genome of human adenovirus type 5 downstream of the early transcription region 3 promoter. The recombinant virus replicated in cultures of the swine testicle ST cell line and directed the synthesis ors antigen to an amount of approximately 33 μg per 106 cells, as determined by ELISA. The antigen was cell-associated except in the late phase of the infection, when a low amount (4 μg per 106 cells) was released in the culture supernatant. The cell-associated antigen consisted of 2 polypeptides of 160 K and 175 K, respectively. The 160 K polypeptide comigrated with the authentic S' precursor from PRCV-infected cells. The 175 K polypeptide had the same mobility as the authentic mature S protein from PRCV-infected cells and from PRCV released in the supernatant. The extracellular recombinant antigen corresponded with the 175 K mature protein. Immunofluorescent staining gave evidence that some recombinant S protein was exposed on the cell surface; it also showed that the protein was recognized by conformation- specific anti-S monoclonal antibodies. Piglets, immunized oronasally with the recombinant adenovirus vector developed PRCV-neutralizing serum antibodies and were partially protected against PRCV-challenge.",,"neutralizing antibody; spike protein; unclassified drug; virus glycoprotein; adenovirus; animal cell; animal model; antigen recognition; conference paper; controlled study; coronavirus; enzyme linked immunosorbent assay; gene expression; immunization; immunofluorescence; immunogenicity; nonhuman; priority journal; promoter region; protein synthesis; swine; testis; virus genome; virus recombinant; virus replication; Adenoviruses, Human; Animal; Base Sequence; Cells, Cultured; Coronavirus; Coronavirus Infections; DNA Primers; Gene Expression; Genetic Vectors; Human; Male; Membrane Glycoproteins; Molecular Sequence Data; Promoter Regions (Genetics); Recombination, Genetic; Respiratory Tract Infections; Support, Non-U.S. Gov't; Swine; Swine Diseases; Testis; Time Factors; Transcription, Genetic; Vaccines, Synthetic; Viral Envelope Proteins; Viral Vaccines; Virus Replication",,"Callebaut, P.; Laboratory of Virology, Faculty of Veterinary Medicine, University of Gent, Casinoplein 24, B-9000 Gent, Belgium",,,00652598,,AEMBA,"8830490","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028884134
"Houtman J.J., Hinze H.C., Fleming J.O.","6701855701;7003795446;7401457370;","Demyelination induced by murine coronavirus JHM infection of congenitally immunodeficient mice",1995,"Advances in Experimental Medicine and Biology","380",,,"159","163",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028864483&partnerID=40&md5=db712b927f640729d3407027d3d482a7","Department of Medical Microbiology, Wisconsin University School of Med., Madison, WI, United States","Houtman, J.J., Department of Medical Microbiology, Wisconsin University School of Med., Madison, WI, United States; Hinze, H.C., Department of Medical Microbiology, Wisconsin University School of Med., Madison, WI, United States; Fleming, J.O., Department of Medical Microbiology, Wisconsin University School of Med., Madison, WI, United States","Mouse hepatitis virus JHM (JHMV or MHV-4) induces demyelination in rodents and has been studied as a model for the human disease, multiple sclerosis (MS). As is proposed in MS, the mechanism of subacute demyelination induced by JHMV appears to be primarily immunopathological, since demyelination in JHMV-infected mice is abrogated by immunosuppressive doses of irradiation and restored by adoptive transfer of splenocytes. Thy-1+ cells play a critical role in transmitting disease to these recipient mice. To further characterize cells which may mediate JHMV-induced immunopathology, we inoculated congenitally immunodeficient mice with JHMV. By 12 days post-inoculation, both immunocompetent C57BL/6J controls and athymic nude C57BL/6 mice had severe paralysis and demyelination. In marked contrast, C57BL/6 mice with the severe combined immune deficiency (SCID) mutation had little or no paralysis or demyelination. Adoptive transfer of immune spleen cells from nude mice to infected SCID mice produced paralysis and demyelination. These findings suggest that a cell population present in immunocompetent C57BL/6J and nude mice but absent or non-functional in irradiated and SCID mice is essential for JHMV-induced demyelination. Identification of cells which mediate demyelination in this experimental system may have implications for our understanding of coronavirus pathogenesis and human demyelinating diseases.",,"adoptive transfer; animal experiment; combined immunodeficiency; conference paper; controlled study; demyelination; histopathology; immune deficiency; immunopathology; immunosuppressive treatment; inoculation; irradiation; male; mouse; murine hepatitis coronavirus; nonhuman; nude mouse; paralysis; priority journal; spleen cell; virus infection; virus pathogenesis; Animal; Antigens, Thy-1; Comparative Study; Coronavirus Infections; Demyelinating Diseases; Human; Immunotherapy, Adoptive; Male; Mice; Mice, Inbred C57BL; Mice, Nude; Mice, SCID; Murine hepatitis virus; Species Specificity; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Time Factors",,"Houtman, J.J.; Department of Medical Microbiology, Wisconsin University School of Med., Madison, WI, United States",,,00652598,,AEMBA,"8830473","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028864483
"Addie D.D., Toth S., Murray G.D., Jarrett O.","7003910352;57189707374;7202037224;7006845693;","Risk of feline infectious peritonitis in cats naturally infected with feline coronavirus.",1995,"American journal of veterinary research","56","4",,"429","434",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029287535&partnerID=40&md5=836a32843eb481519184ed20f51d4c81","Department of Veterinary Pathology, University of Glasgow, United Kingdom","Addie, D.D., Department of Veterinary Pathology, University of Glasgow, United Kingdom; Toth, S., Department of Veterinary Pathology, University of Glasgow, United Kingdom; Murray, G.D., Department of Veterinary Pathology, University of Glasgow, United Kingdom; Jarrett, O., Department of Veterinary Pathology, University of Glasgow, United Kingdom","A longitudinal survey of 820 cats in 73 households was conducted over a period of 6 years to establish the fate of pet cats that were seropositive after natural exposure to feline coronavirus (FCoV). In particular, their risk of developing feline infectious peritonitis (FIP) was determined. The seropositive cats were assigned to 1 of 3 groups: cats from households in which FIP had recently been diagnosed; cats from households in which FIP had not been diagnosed, but from which kittens had been relocated and subsequently died of FIP; and cats from households in which FIP had not been diagnosed. Cats in the first group were not at greater risk of developing FIP than were cats in the other 2 groups. Consequently, any household in which seropositive cats live must be considered a potential source of FCoV that can cause FIP. There was no evidence that the enhanced disease, which has been described after experimentally induced infection of seropositive cats, exists in nature. Thus, analysis of the survival of the seropositive cats over periods of up to 36 months indicated that their risk of developing FIP decreased with time, suggesting the development of immunity rather than increased susceptibility to disease. In addition, of 56 cats deemed to have been naturally reinfected because their anti-FCoV antibody titers decreased and subsequently increased, only 3 developed FIP.",,"animal; animal food; article; cat; cat disease; Coronavirus; disease transmission; domestic animal; follow up; isolation and purification; mortality; probability; risk factor; survival rate; time; virology; Animal Feed; Animals; Animals, Domestic; Cats; Coronavirus, Feline; Feline Acquired Immunodeficiency Syndrome; Feline Infectious Peritonitis; Follow-Up Studies; Probability; Risk Factors; Survival Rate; Time Factors",,"Addie, D.D.",,,00029645,,,"7785816","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029287535
"Torres J.M., Sánchez C., Suñé C., Smerdou C., Prevec L., Graham F., Enjuanes L.","35516513600;57193985365;6701660310;6602856664;7003455531;35821642700;7006565392;","Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein",1995,"Virology","213","2",,"503","516",,32,"10.1006/viro.1995.0023","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028864302&doi=10.1006%2fviro.1995.0023&partnerID=40&md5=7657e6ecc81e7a43d1a65795c93e0e28","Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain; Departments of Biology and Pathology, McMaster University, Hamilton, ON L8S 4K1, Canada","Torres, J.M., Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain; Sánchez, C., Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain; Suñé, C., Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain; Smerdou, C., Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain; Prevec, L., Departments of Biology and Pathology, McMaster University, Hamilton, ON L8S 4K1, Canada; Graham, F., Departments of Biology and Pathology, McMaster University, Hamilton, ON L8S 4K1, Canada; Enjuanes, L., Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain","Ten recombinant adenoviruses expressing either fragments of 1135, 1587, or 3329 nt or the full-length spike gene of transmissible gastroenteritis coronavirus (TGEV) have been constructed. These recombinants produce S polypeptides with apparent molecular masses of 68, 86, 135, and 200 kDa, respectively. Expression of the recombinant antigen driven by Ad5 promoters was inhibited by the insertion of an exogenous SV-40 promoter. Most of the recombinant antigens remain intracytoplasmic in infected cells. All the recombinant-directed expression products contain functional antigenic sites C and B (Gebauer et al., 1991, Virology 183, 225-238). The recombinant antigen of 135 kDa and that of 200 kDa, which represents the whole spike protein, also contain antigenic sites D and A, which have previously been shown to be the major inducers of TGEV-neutralizing antibodies. Interestingly, here we show that recombinant S protein fragments expressing only sites C and B also induced TGEV-neutralizing antibodies. The chimeric Ad5-TGEV recombinants elicited lactogenic immunity in hamsters, including the production of TGEV-neutralizing antibodies. The antisera induced in swine by the Ad5 recombinants expressing the amino-terminal 26% of the spike protein (containing sites C and B) or the full-length spike protein, when mixed with a lethal dose of virus prior to administration to susceptible piglets, delayed or completely prevented the induction of symptoms of disease, respectively. © 1995 Academic Press, Inc.",,,"Berkner, K.L., Development of adenovirus vectors for the expression of heterologous genes (1988) Biotechniques, 6, pp. 616-629; Bett, A.J., Prevec, L., Graham, F.L., Packaging capacity and stability of human adenovirus type 5 vectors (1993) J. Virol, 67, pp. 5911-5921; Birnboim, H.C., Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA (1979) Nucleic Acids Res, 7, pp. 1513-1517; Both, G.W., Lockett, L.J., Janardhana, V., Edwards, S.J., Bellamy, A.R., Graham, F.L., Prevec, L., Andrew, M.E., Protective immunity to rotavirus-induced diarrhea is passively transferred to newborn mice from naive dams vaccinated with a single dose of a recombinant adenovirus expressing rotavirus VP7sc (1993) Virology, 193, pp. 940-950; Bousquet, F., Martin, C., Girardeau, J.P., Mechin, M.C., Vartanian, M.D., Laude, H., Contrepois, M., CS31A capsule-like antigen as an exposure vector for heterologous antigenic determinants (1994) Infect. 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Virol, 64, pp. 6270-6273; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus (1992) J. Virol, 66, pp. 743-749; Lecomte, J., Cainelli-Cebera, V., Mercier, G., Mansour, S., Talbot, P., Lussier, G., Oth, D., Protection from mouse hepatitis virus type 3-induced acute disease by an anti-nucleoprotein monoclonal antibody (1987) Arch. Virol, 97, pp. 123-130; Lenstra, J.A., Erkens, J.H.F., Zwaagstra, K.A., Posthumus, W.P.A., Meloen, R.H., Gebauer, F., Enjuanes, L., Stanley, K.K., Selection of mimotopes from a random sequence expression library by monoclonal antibodies against transmissible gastroentritis coro-navirus (1991) J. Immunol. Methods, 152, pp. 149-157; Maniatis, T., Fritsh, E.F., Sambrook, J., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopatho-genic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci, 30, pp. 190-198; Mittal, S.K., McDermott, M.R., Johnson, D.C., Prevec, L., Graham, F.L., Monitoring foreign gene expression by a human adenovirus based vector using the firefly luciferase as a reporter gene (1993) Virus Res, 28, pp. 67-90; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of monoclonal antibodies on lethal mouse hepatitis virus infection in mice (1986) J. Virol, 59, pp. 168-171; Posthumus, W.P.A., Meloen, R.H., Enjuanes, L., Correa, I., Van Nieuwestadt, A., Koch, G., Linear neutralizing epitopes on the peplomer protein of coronaviruses (1990) Adv. Exp. Med. Biol, 276, pp. 181-188; Prevec, L., Campbell, J.B., Christie, B.S., Belbeck, L., Graham, F.L., A recombinant human adenovirus vaccine against rabies (1990) J. Infect. Dis, 161, pp. 227-230; Pulford, D.J., Britton, P., Intracellular processing of the porcine coronavirus transmissible gastroenteritis virus spike protein expressed by recombinant vaccinia virus (1991) Virology, 182, pp. 765-773; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , A. D. Leman, B. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor, Eds.), Iowa State Univ. Press, Ames; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Schneider, M., Graham, F.L., Preveck, L., Expression of the glycoprotein of VSV by infectious adenovirus vectors (1989) J. Gen. Virol, 70, pp. 417-427; Smerdou, C., Anton, I.M., Plana, J., Curtiss, R., Enjuanes, L., Expression of a continuous epitope from transmissible gastroenteritis coronavirus S protein fused to E. Coli heat-labile toxin B subunit in attenuated (1995) Salmonella, , for oral immunization. Submitted for publication; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses (1990) Immunochemistry of Viruses. II. the Basis for Serodiagnosis and Vaccines, pp. 359-375. , M. H. V. Regenmortel and A. R. Neurath, Eds, Elsevier, Amsterdam; Sune, C., Jimenez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Talbot, P.J., Salmi, A.A., Knobler, R.L., Buchmeier, M.J., Topographical mapping of epitopes on the glycoprotein of murine hepatitis virus-4 (Strain JHM): Correlation with biological activities (1984) Virology, 132, pp. 250-260; Torres, J.M., Alonso, C., Ortega, A., Graham, F.L., Enjuanes, L., Ad5 based vectors in swine and their use in protection against transmissible gastroenteritis virus (1995) Tropism of Human Adenovirus, , Submitted for publication; Tulboly, T., Nagy, E., Dennis, J.R., Derbyshire, J.B., Immuno-genicity of the S protein of transmissible gastroenteritis virus expressed in baculovirus (1994) Arch. Virol, 137, pp. 55-67; Welch, S.K.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity with virulent and attenuated virus (1988) Arch. Virol, 101, pp. 221-235; Wesseling, J.G., Godeke, G.J., Schijns, V.E.C.J., Prevec, L., Frank, F.L., Horzinek, M.C., Rotier, P.J.M., Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vector protect mice against a lethal infection (1993) J. Gen. Virol, 74, pp. 2061-2069; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56","Enjuanes, L.; Department of Molecular and Cell Biology, Centra Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049, Madrid, Spain",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028864302
"Taguchi F., Kubo H., Suzuki H., Yamada Y.K.","7103209890;55183402000;7407715967;55471420900;","Localization of neutralizing epitopes and receptor-binding site in murine coronavirus spike protein",1995,"Advances in Experimental Medicine and Biology","380",,,"359","365",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028787270&partnerID=40&md5=ac287d0e86bdaf7e832a1634c0bf5dc1","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Kubo, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Suzuki, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Yamada, Y.K., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","To identify the localization of the epitopes recognized by monoclonal antibodies (MAbs) against the S1 subunit of the murine coronavirus JHMV spike protein, we have expressed the S1 proteins with different deletions from the C terminus of the S1. All of MAbs in groups A and B recognized the S1 N(330) composed of 330 amino acids (aa) from the N terminus of the S1 and the larger S1 deletion mutants, but failed to react with the S1N(220) composed of 220 aa. MAbs in group C reacted only with the Slutt protein without any deletion. These results indicated that the S1 N330 comprised the cluster of epitopes recognized by MAbs in groups A and B. These results together with the fact that all the MAbs in group B retained the high neutralizing activity suggested that the N terminus 330 aa are responsible for binding to the MHV- specific receptors. In pursuit of this possibility, we have expressed the receptor protein and examined the binding of each S1 deletion mutants to the receptor. It was demonstrated that the S1N(330) protein as well as other S1 deletion mutants larger than S1N(330) bound to the receptor. These results indicated that a domain composed of 330 aa at the N terminus of the S1 protein is responsible for binding to the MHV-specific receptor.",,"epitope; monoclonal antibody; receptor; virus protein; amino terminal sequence; binding site; carboxy terminal sequence; conference paper; coronavirus; deletion mutant; gene expression; immunofluorescence; nonhuman; polyacrylamide gel electrophoresis; polymerase chain reaction; priority journal; virus neutralization; Animal; Antibodies, Monoclonal; Binding Sites; Epitopes; Glycoproteins; Liver; Macromolecular Systems; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Mutagenesis; Neutralization Tests; Receptors, Virus; Recombinant Proteins; Sequence Deletion; Viral Envelope Proteins",,"Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,00652598,,AEMBA,"8830508","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028787270
"Sawicki S.G., Sawicki D.L.","7004118344;7003804556;","Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands.",1995,"Advances in experimental medicine and biology","380",,,"499","506",,110,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029444973&partnerID=40&md5=07b6e93d1512c9679c966ffd576d247a","Department of Microbiology, Medical College of Ohio, Toledo, 43699, United States","Sawicki, S.G., Department of Microbiology, Medical College of Ohio, Toledo, 43699, United States; Sawicki, D.L., Department of Microbiology, Medical College of Ohio, Toledo, 43699, United States","We have developed a new model for coronavirus transcription, which we call discontinuous extension, to explain how subgenome-length negatives stands are derived directly from the genome. The current model called leader-primed transcription, which states that subgenomic mRNA is transcribed directly from genome-length negative-strands, cannot explain many of the recent experimental findings. For instance, subgenomic mRNAs are transcribed directly via transcription intermediates that contain subgenome-length negative-strand templates; however subgenomic mRNA does not appear to be copied directly into negative strands. In our model the subgenome-length negative strands would be derived using the genome as a template. After the polymerase had copied the 3'-end of the genome, it would detach at any one of the several intergenic sequences and reattach to the sequence immediately downstream of the leader sequence at the 5'-end of genome RNA. Base pairing between the 3'-end of the nascent subgenome-length negative strands, which would be complementary to the intergenic sequence at the end of the leader sequence at the 5'-end of genome, would serve to align the nascent negative strand to the genome and permit the completion of synthesis, i.e., discontinuous extension of the 3'-end of the negative strand. Thus, subgenome-length negative strands would arise by discontinuous synthesis, but of negative strands, not of positive strands as proposed originally by the leader-primed transcription model.",,"messenger RNA; primer DNA; virus RNA; animal; biosynthesis; Coronavirus; genetic transcription; genetics; isolation and purification; molecular genetics; mouse; nucleotide sequence; physiology; polymerase chain reaction; review; virus genome; virus replication; Animals; Base Sequence; Coronavirus; DNA Primers; Genome, Viral; Mice; Molecular Sequence Data; Polymerase Chain Reaction; RNA, Messenger; RNA, Viral; Transcription, Genetic; Virus Replication",,"Sawicki, S.G.",,,00652598,,,"8830530","English","Adv. Exp. Med. Biol.",Review,"Final",,Scopus,2-s2.0-0029444973
"Ziebuhr J., Herold J., Siddell S.G.","7003783935;7006838690;7005260816;","Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity",1995,"Journal of Virology","69","7",,"4331","4338",,80,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029017145&partnerID=40&md5=5ede5425e1d48b5e18ceed7a39a8089b","Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany","Ziebuhr, J., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; Herold, J., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; Siddell, S.G., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany","The RNA polymerase gene of human coronavirus (HCV) 229E encodes a large polyprotein that contains domains with motifs characteristic of both papain- like cysteine proteinases and proteinases with homology to the 3C proteinase of picornaviruses. In this study, we have, first, expressed the putative HCV 229E 3C-like proteinase domain as part of a β-galactosidase fusion protein in Escherichia coli and have shown that the expressed protein has proteolytic activity. The substitution of one amino acid within the predicted proteinase domain (His-3006→Asp-3006) abolishes, or at least significantly reduces, this activity. Amino-terminal sequence analysis of a purified, 34-kDa cleavage product shows that the bacterial fusion protein is cleaved at the dipeptide Gln-2965-Ala-2966, which is the predicted amino-terminal end of the putative 3C-like proteinase domain. Second, we have confirmed the proteolytic activity of a bacterially expressed polypeptide with the amino acid sequence of the predicted HCV 229E 3C-like proteinase by trans cleavage of an in vitro translated polypeptide encoded within open reading frame 1b of the RNA polymerase gene. Finally, using fusion protein-specific antiserum, we have identified a 34-kDa, 3C-like proteinase polypeptide in HCV 229E-infected MRC- 5 cells. This polypeptide can be detected as early as 3 to 5 h postinfection but is present in the infected cell in very low amounts. These data contribute to the characterization of the 3C-like proteinase activity of HCV 229E.",,"proteinase; amino acid substitution; article; coronavirus; enzyme activity; enzyme analysis; nonhuman; picornavirus; priority journal; protein degradation; sequence analysis; sequence homology; structure activity relation; Amino Acid Sequence; Animal; Base Sequence; Cells, Cultured; Coronavirus; Coronavirus 229E, Human; Cysteine Endopeptidases; Escherichia coli; Female; Human; Immune Sera; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Rabbits; Recombinant Fusion Proteins; Support, Non-U.S. Gov't; Viral Proteins",,"Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,,0022538X,,JOVIA,"7769694","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029017145
"Peng D., Koetzner C.A., Masters P.S.","7202530662;6602982748;7006234572;","Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination",1995,"Journal of Virology","69","6",,"3449","3457",,24,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029009852&partnerID=40&md5=2c38cfbaf83ee15471cf8224b5ba74ee","Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States","Peng, D., Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States; Koetzner, C.A., Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States; Masters, P.S., Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States","The Alb4 mutant of the coronavirus mouse hepatitis virus (MHV) is both temperature sensitive and thermolabile owing to a deletion in the gene encoding its nucleocapsid (N) protein. The deletion removes 29 amino acids that constitute a putative spacer region preceding the carboxyl-terminal domain of the protein. As a step toward understanding the structure and function of the MHV N protein, we isolated multiple independent revertants of Alb4 that totally or partially regained the ability to form large (wild- type-sized) plaques at the nonpermissive temperature. The N proteins of those revertant viruses concomitantly regained the ability to bind to RNA in vitro at a temperature that was restrictive for RNA binding by Alb4 N protein. Sequence analysis of the N genes of the revertants revealed that each contained a single second-site point mutation that compensated for the effects of the deletion. All reverting mutations were clustered within a stretch of 40 amino acids centered some 80 residues on the amino side of the Alb4 deletion, within a domain to which the RNA-binding activity of N had been previously mapped. By means of a targeted RNA recombination method that we have recently developed, two of the reverting mutations were introduced into a wild-type MHV genomic background. The resulting recombinants were stable and showed no gross phenotypic differences from the wild type. A detailed analysis of one, however, revealed that it was at a selective disadvantage with respect to the wild type.",,"capsid protein; virus protein; virus rna; animal cell; article; deletion mutant; gene mapping; genetic recombination; mouse; murine hepatitis coronavirus; nonhuman; priority journal; revertant; structure activity relation; temperature sensitivity; virus mutation; virus recombination; Amino Acid Sequence; Animal; Base Sequence; Capsid; Cell Line; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutation; Recombination, Genetic; RNA, Viral; Sequence Deletion; Support, U.S. Gov't, P.H.S.; Viral Core Proteins",,"Masters, P.S.; Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States",,,0022538X,,JOVIA,"7745691","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029009852
"Lamarre A., Talbot P.J.","7004646746;7102670281;","Protection from lethal coronavirus infection by immunoglobulin fragments",1995,"Journal of Immunology","154","8",,"3975","3984",,40,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028957940&partnerID=40&md5=c5d0aaf116ed0edc86acb343875f6c5c","Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Lamarre, A., Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada; Talbot, P.J., Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Molecular mechanisms of in vitro and in vivo virus neutralization by specific Ab remain largely undefined. Murine coronaviruses provide an excellent animal model for such studies. To determine the role of Ab bivalency and the contribution of its Fc portion in the neutralization of viral infectivity and passive protection of mice by an in vitro neutralizing and in vivo protective mAb (7-10A), F(ab')2 and Fab fragments were generated and their biologic properties were examined. The two fragments reacted in ELISA like the whole Ab against viral Ag or specific anti-idiotypic Abs. The affinity constants of the different Ab preparations were determined by surface plasmon resonance using immobilized anti-idiotypic Abs. The apparent affinity constant of the whole Ab molecule was 7.0 x 109 M-1 and was reduced 2-fold for F(ab')2 fragments and 14-fold for Fab molecules. Like whole Ab, both F(ab')2 and Fab fragments could neutralize virus in vitro and passively protect mice in vivo. However, the efficiency of in vivo neutralization by Fab fragments was reduced compared with the bivalent molecules, despite almost identical half-lives of both types of Ab fragments. These results demonstrate that in vitro and in vivo virus neutralization mechanisms by this Ab are independent of Fc-mediated functions and bivalency, but are probably influenced by Ab avidity. Also, this is the first report of in vivo protection against a vital infection by Fab fragments of antiviral Ab.",,"immunoglobulin f(ab')2 fragment; immunoglobulin f(ab) fragment; immunoglobulin fc fragment; immunoglobulin fragment; virus antibody; animal cell; animal model; antiviral activity; article; coronavirus; female; humoral immunity; male; mouse; nonhuman; priority journal; virus infection; virus inhibition; virus neutralization; Animal; Antibodies, Anti-Idiotypic; Antibodies, Monoclonal; Coronavirus Infections; Encephalitis, Viral; Female; Hepatitis Antibodies; Hepatitis, Viral, Animal; Immunization, Passive; Immunoglobulins, Fab; Male; Membrane Glycoproteins; Metabolic Clearance Rate; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Neutralization Tests; Support, Non-U.S. Gov't; Viral Envelope Proteins",,"Talbot, P.J.; Centre de Recherche en Virologie, Institut Armand-Frappier, Universite du Quebec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada",,,00221767,,JOIMA,"7706736","English","J. IMMUNOL.",Article,"Final",,Scopus,2-s2.0-0028957940
"Fulker R., Wasmoen T., Atchison R., Chu H.-J., Acree W.","6507290486;6602099285;36796830400;7202364837;7103180682;","Efficacy of an inactivated vaccine against clinical disease caused by canine coronavirus",1995,"Advances in Experimental Medicine and Biology","380",,,"229","234",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028826525&partnerID=40&md5=70866e81409da385add5a8dacaf18a58","Fort Dodge Laboratories, Fort Dodge, IA, United States","Fulker, R., Fort Dodge Laboratories, Fort Dodge, IA, United States; Wasmoen, T., Fort Dodge Laboratories, Fort Dodge, IA, United States; Atchison, R., Fort Dodge Laboratories, Fort Dodge, IA, United States; Chu, H.-J., Fort Dodge Laboratories, Fort Dodge, IA, United States; Acree, W., Fort Dodge Laboratories, Fort Dodge, IA, United States","Canine Coronavirus (CCV) is a causative agent of diarrhea in dogs. The reproduction of severe clinical disease with experimental CCV infection has been difficult. We have recently developed a CCV challenge model which reproduced clinical signs of disease in susceptible dogs. The following study was designed to determine whether immunization with an inactivated CCV vaccine would protect dogs from clinical disease induced using this model. Dogs (n=13) were vaccinated with an inactivated CCV vaccine. Vaccinates and controls (n=5) were orally inoculated with virulent CCV virus and treated with dexamethasone on days 0, 2, 4, and 6 after virus challenge. Control dogs developed clinical signs including diarrhea, dehydration, anorexia, depression, and nasal and ocular discharge. Diarrhea was noted in 80% of the controls and 60% progressed to a severe watery or bloody diarrhea that persisted for multiple days. Conversely, only 2/13 (15%) vaccinates developed mild diarrhea and none developed bloody diarrhea. The control dogs averaged 10.8 days of diarrhea compared to 1.4 days for vaccinates over the 21 day observation period. In addition to reduced clinical signs, the number of days of virus shedding and the level of CCV in feces was different for controls (100% shed virus) and vaccinates (38% shed virus). This study demonstrates that vaccination with an inactivated CCV vaccine can significantly reduce not only viral replication, but the occurrence of clinical disease following a virulent CCV infection.",,"corona virus vaccine; dexamethasone; duramune; inactivated virus vaccine; unclassified drug; animal experiment; clinical feature; conference paper; controlled study; coronavirus; diarrhea; dog; female; immunization; inoculation; intramuscular drug administration; male; nonhuman; priority journal; subcutaneous drug administration; virus infection; virus replication; virus shedding; virus virulence; Animal; Coronavirus; Coronavirus Infections; Diarrhea; Dog Diseases; Dogs; Female; Male; Time Factors; Vaccines, Inactivated; Viral Vaccines; Virus Shedding",,"Fulker, R.; Fort Dodge Laboratories, Fort Dodge, IA, United States",,,00652598,,AEMBA,"8830484","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028826525
"Spencer J.S., Cabirac G.F., Best C., McLaughlin L., Murray R.S.","55220571100;6602498805;56650074400;7102364645;7403022204;","Characterization of human T cell clones specific for coronavirus 229E",1995,"Advances in Experimental Medicine and Biology","380",,,"121","129",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028807196&partnerID=40&md5=36ba12894c2f9acb06e80161afcb1e31","RMMSC, Colorado Neurological Institute, Englewood, CO, United States","Spencer, J.S., RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Cabirac, G.F., RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Best, C., RMMSC, Colorado Neurological Institute, Englewood, CO, United States; McLaughlin, L., RMMSC, Colorado Neurological Institute, Englewood, CO, United States; Murray, R.S., RMMSC, Colorado Neurological Institute, Englewood, CO, United States","Coronaviruses (CV) are pleomorphic enveloped RNA viruses that are ubiquitous in nature, causing a variety of diseases in both man and domestic animals. In man, CV are generally associated with upper respiratory tract infections. The two prototype strains that are the best studied human CV isolates and which are thought to be responsible for most of the respiratory infections caused by CV are called 229E and OC43. Humoral responses consisting of neutralizing antibodies to CV are present in most individuals by six years of age. Although the cellular immune response to CV in man has not been characterized at all, it is known that the spike (S) and nucleocapsid (N) proteins elicit the major cell mediated immune responses in the mouse. This report describes the production and characterization of eleven independently isolated T cell clones that are specific for the human CV(HCV) 229E. The T cell clones are CD4+ and presumably recognize a processed viral peptide presented by class II molecules on the surface of antigen presenting cells. Of six 229E-specific T cell clones tested against purified vital proteins, three recognize the 180 kD spike glycoprotein while the other three recognize the 55 kD nucleocapsid phosphoprotein. Analysis of the human T cell mediated response to HCV will provide information regarding which viral proteins elicit the immunodominant response, what the fine specificity of these T cell clones are (immunodominant peptides), and what the T cell receptor (TCR) and cytokine usage is of these virus specific clones.",,"cd4 antigen; t lymphocyte receptor; virus glycoprotein; virus phosphoprotein; virus protein; animal cell; antigen presenting cell; antigen specificity; b lymphocyte; cell transformation; conference paper; controlled study; coronavirus; fibroblast culture; human; human cell; lymphocyte clone; lymphocyte proliferation; mouse; nonhuman; priority journal; protein purification; t lymphocyte; tumor cell culture; virus purification; Capsid; Cell Line; Cell Line, Transformed; Clone Cells; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Electrophoresis, Polyacrylamide Gel; Hemagglutinins, Viral; Herpesvirus 4, Human; Human; Lung; Lymphocyte Activation; Membrane Glycoproteins; Support, Non-U.S. Gov't; T-Lymphocytes; Viral Core Proteins; Viral Envelope Proteins",,"Spencer, J.S.; RMMSC, Colorado Neurological Institute, Englewood, CO, United States",,,00652598,,AEMBA,"8830466","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028807196
"Schunk M.K., Percy D.H., Rosendal S.","55572457800;16140219400;7005469090;","Effect of time of exposure to rat coronavirus and Mycoplasma pulmonis on respiratory tract lesions in the Wistar rat.",1995,"Canadian journal of veterinary research = Revue canadienne de recherche vétérinaire","59","1",,"60","66",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029193564&partnerID=40&md5=4adbb307256d06f07539f0a855697c59","Department of Pathology, Ontario Veterinary College, University of Guelph., Canada","Schunk, M.K., Department of Pathology, Ontario Veterinary College, University of Guelph., Canada; Percy, D.H., Department of Pathology, Ontario Veterinary College, University of Guelph., Canada; Rosendal, S., Department of Pathology, Ontario Veterinary College, University of Guelph., Canada","The effects of time of exposure on the progression of pulmonary lesions in rats inoculated with Mycoplasma pulmonis and the rat coronavirus, sialodacryoadenitis virus (SDAV) were studied, using six groups of 18 SPF Wistar rats (n = 108). Rats were inoculated intranasally as follows: Group 1, sterile medium only; Group 2, sterile medium followed one week later by 150 TCID50 SDAV; Group 3, sterile medium followed by 10(5.7) colony forming units of M. pulmonis; Group 4, SDAV followed one week later by M. pulmonis; Group 5, M. pulmonis followed one week later by SDAV; Group 6, M. pulmonis followed two weeks later by SDAV. Six rats from each group were euthanized at one, two and three weeks after the final inoculation. In a separate experiment, six additional animals were inoculated in each of groups 3, 5 and 6 (n = 18) and were sampled at five weeks after they had received M. pulmonis. Bronchoalveolar lavage and quantitative lung mycoplasma cultures were conducted on two-thirds of the rats. Histopathological examination and scoring of lesion severity were performed on all animals. Based on the prevalence and extent of histopathological lesions, bronchoalveolar lavage cell numbers, neutrophil differential cell counts and the isolation of M. pulmonis, the most severe disease occurred in the groups that received both agents. There was no significant difference in lesion severity between the groups receiving both agents other than in those examined during the acute stages of SDAV infection. Based on these results, it is evident that SDAV enhances lower respiratory tract disease in Wistar rats whether exposure occurs at one week prior to or at various intervals following M. pulmonis infections.",,"animal; animal disease; article; bacterial infection; Coronavirus; enzyme linked immunosorbent assay; male; microbiology; rat; respiratory tract infection; rodent disease; time; virology; virus infection; Wistar rat; Animals; Coronavirus Infections; Coronavirus, Rat; Enzyme-Linked Immunosorbent Assay; Male; Mycoplasma Infections; Rats; Rats, Wistar; Respiratory Tract Infections; Rodent Diseases; Time Factors",,"Schunk, M.K.",,,08309000,,,"7704844","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029193564
"Brim T.A., VanCott J.L., Lunney J.K., Saif L.J.","6602281848;6603878315;7005634527;7102226747;","Cellular immune responses of pigs after primary inoculation with porcine respiratory coronavirus or transmissible gastroenteritis virus and challenge with transmissible gastroenteritis virus",1995,"Veterinary Immunology and Immunopathology","48","1-2",,"35","54",,28,"10.1016/0165-2427(94)05416-P","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029092212&doi=10.1016%2f0165-2427%2894%2905416-P&partnerID=40&md5=2ba4ead80af1b282efbac1d78b732994","Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Wooster, OH 44691, United States; USDA, Helminthic Diseases Laboratory, Agricultural Research Service, Beltsville, MD 20705, United States","Brim, T.A., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Wooster, OH 44691, United States; VanCott, J.L., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Wooster, OH 44691, United States; Lunney, J.K., USDA, Helminthic Diseases Laboratory, Agricultural Research Service, Beltsville, MD 20705, United States; Saif, L.J., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Wooster, OH 44691, United States","The contribution of cell-mediated immunity to protective immunity against virulent transmissible gastroenteritis virus (TGEV) infection conferred by primary porcine respiratry coronavirus (PRCV) or TGEV exposure was assessed in pigs that were challenged with TGEV 24 days after a primary oronasal inoculation with PRCV or TGEV when 11 days old. PRCV exposure induced partial protection against TGEV challenge in suckling pigs based upon a decreased number of diarrhea cases (42% vs. 90% in age-matched control pigs), limited virus shedding in feces, and increases in virus-neutralizing serum antibody titers; in contrast, all 11-day-old pigs inoculated with TGEV were completely protected after challenge. Weaned pigs were also studied to eliminate any possibility that lactogenic immunity from contact PRCV-exposed sows contributed to protection against TGEV. Once weaned, none of the PRCV-exposed or age-matched control pigs had diarrhea after TGEV challenge; moreover, both groups exhibited less rectal virus shedding than suckling pigs. Vigorous lymphocyte proliferative responses (> 96 000 counts per minute (cpm)) were detected in mononuclear cells prepared from mesenteric (MLN) and bronchial (BLN) lymph nodes of TGEV-primed pigs. Analyses of these responses indicate that virus-specific cell-mediated immune responses correlated with protection against rectal and nasal virus shedding after TGEV challenge. Primary inoculation of 11-day-old pigs with PRCV induced moderate, transient virus-specific lymphocyte proliferation (> 47 000 cpm) in MLN from both suckling and weaned pigs after TGEV challenge. Substantial BLN proliferative responses (> 80 000 cpm) correlated with failure to detect TGEV in nasal secretions from these pigs. Virus-specific lymphocyte proliferation in spleens was delayed in onset and of lower magnitude than that observed in MLN and BLN. Virulent TGEV exposure resulted in increased percentages of T cell subsets, especially in the lamina propria and MLN, mucosaassociated lymphoid tissues in proximity to the primary replication site of TGEV in the small intestine. Our results confirm that PRCV infection primes anti-viral immune responses and, thus, contributes to partial immunity against virulent TGEV challenge. © 1995.","Cellular immunity; Lymphocyte proliferation; Lymphocyte subsets; Porcine respiratory coronavirus; T lymphocytes; Transmissible gastroenteritis virus","animal cell; animal experiment; article; cellular immunity; controlled study; coronavirus; diarrhea; intestine lymphatic tissue; lymphocyte proliferation; newborn; nonhuman; respiratory tract infection; swine; t lymphocyte; virulence; virus infection; Animal; Animals, Suckling; Antibodies, Viral; Coronavirus; Epitopes; Flow Cytometry; Immunization, Secondary; Immunophenotyping; Lymphocyte Activation; Neutralization Tests; Species Specificity; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Swine; T-Lymphocytes; Transmissible gastroenteritis virus; Viral Vaccines; Virus Shedding; Weaning; Animalia; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Akbar, Salmon, Janossy, The synergy between naive and memory T cells during activation (1991) Immunol. Today, 12, pp. 184-188; Bailey, Stevens, Bland, Stokes, A monoclonal antibody recognising an epitope associated with pig interleukin-2 receptors (1992) J. Immunol. Methods, 153, pp. 85-91; Bernard, Bottreau, Aynaud, Have, Szymansky, Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis virus (1989) Vet. Microbiol., 21, pp. 1-8; Binns, Organisation of the lymphoreticular system and lymphocyte markers in the pig (1982) Vet. Immunol. Immunopathol., 3, pp. 95-146; Binns, Duncan, Powis, Hutchings, Butcher, Subsets of null and γδ T-cell receptor+ T lymphocytes in the blood of young pigs identified by specific monoclonal antibodies (1992) Immunology, 77, pp. 219-227; Bohl, Kumagai, The use of cell cultures for the study of TGE virus of swine (1965) Proc. US Livest. Sanit. Assoc., 69, pp. 343-350; Bohl, Gupta, Olquin, Saif, Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect. Immun., 6, pp. 289-301; Brim, VanCott, Lunney, Saif, Lymphocyte proliferative responses of pigs inoculated with transmissible gastroenteritis virus or porcine respiratory coronavirus (1994) Am. J. Vet. Res., 55, pp. 494-501; Brown, Cartwright, New porcine coronavirus? (1986) Vet. Rec., 119, pp. 282-283; Callebaut, Correa, Pensaert, Jimenez, Enjuanes, Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) Journal of General Virology, 69, pp. 1725-1730; Callebaut, Cox, Pensaert, van Deun, Induction of milk IgA antibodies by porcine respiratory coronavirus infection (1990) Coronaviruses and Their Diseases, pp. 421-428. , D. Cavanagh, T.D.K. Brown, Plenum Press, New York; Cox, Hooyberghs, Pensaert, Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Cox, Pensaert, Callebaut, Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-272; De Diego, Laviada, Enjuanes, Escribano, Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 6502-6508; Dunkley, Husband, Distribution and functional characteristics of antigen-specific helper T cells arising after Peyer's patch immunization (1987) Immunology, 61, pp. 475-482; Furuuchi, Shimizu, Kumagai, Multiplication of low and high cell culture passaged strains of transmissible gastroenteritis virus in organs of newborn piglets (1978) Vet. Microbiol., 3, pp. 169-178; Garwes, Stewart, Cartwright, Brown, Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet. Rec., 122, pp. 86-87; Hall, Byrne, Effects of age and diet on small intestinal structure and function in gnotobiotic piglets (1989) Res. Vet. Sci., 47, pp. 387-392; Hein, Mackay, Prominence of γδ T cells in the ruminant immune system (1991) Immunol. Today, 12, pp. 30-34; Hill, Biwer, Wood, Wesley, Porcine respiratory coronavirus isolated from two U.S. swine herds (1990) Proceedings of the 21st Annual Meeting of the American Association of Swine Practitioners, pp. 333-335. , 4–6 March, Denver, CO; Hirt, Saalmuller, Reddehase, Distinct γ/δ T cell receptors define two subsets of circulating porcine CD2−CD4−CD8− T lymphocytes (1990) Eur. J. Immunol., 20, pp. 265-269; Kemeny, Wiltsey, Riley, Upper respiratory infection of lactating sows with transmissible gastroenteritis virus following contact exposure to infected piglets (1975) Cornell Vet., 65, pp. 352-362; Kimpen, Rich, Mohar, Ogra, Mucosal T cell distribution during infection with respiratory syncytial virus (1992) J. Med. Virol., 36, pp. 172-179; London, Cebra-Thomas, Rubin, Cebra, CD8 lymphocyte subpopulations in Peyer's patches induced by reovirus serotype I infection (1990) J. Immunol., 144, pp. 3187-3194; Lunney, Urban, Jr., Johnson, Protective immunity to Ascaris suum: analysis of swine peripheral blood cell subsets using monoclonal antibodies and flow cytometry (1986) Vet. Parasitol., 20, pp. 117-131; Lunney, Characterization of swine leukocyte differentiation antigens (1993) Immunol. Today, 14, pp. 147-148; Mestecky, McGhee, Immunoglobulin A (IgA): molecular and cellular interactions involved in IgA biosynthesis and immune response (1987) Adv. Immunol., 40, pp. 153-245; Moon, Norman, Lambert, Age dependent resistance to TGE of swine. I. Clinical signs and some mucosal dimensions in the small intestine (1973) Can. J. Comp. Med., 37, pp. 157-166; O'Toole, Brown, Bridges, Cartwright, Pathogenicity of experimental infection with ‘pneumotropic/’ porcine coronovirus (1989) Res. Vet. Sci., 47, pp. 23-29; Paton, Brown, Sows infected in pregnancy with porcine respiratory coronavirus show no evidence of protecting their sucking piglets against transmissible gastroenteritis (1990) Vet. Res. Commun., 14, pp. 329-337; Paul, Mengeling, Malstrom, van Deusen, Production and characterization of monoclonal antibodies to porcine immunoglobulin gamma, alpha, and light chains (1989) Am. J. Vet. Res., 50, pp. 471-479; Pensaert, Callebaut, Vergote, Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Pescovitz, Lunney, Sachs, Murine anti-swine T4 and T8 monoclonal antibodies; distribution and effects on proliferative and cytotoxic T cells (1985) J. Immunol., 134, pp. 37-44; Pescovitz, Sakopoulos, Gaddy, Hussman, Zuckermann, Porcine peripheral blood CD4+/CD8+ dual expressing T-cells (1994) Veterinary Immunology and Immunopathology, 43, pp. 53-62; Rothkotter, Pabst, Lymphocyte subsets in jejunal and ileal Peyer's pathches of normal and gnotobiotic minipigs (1989) Immunology, 67, pp. 103-108; Rothkotter, Ulbrich, Pabst, The postnatal development of gut lamina propria lymphocytes: number, proliferation, and T and B cell subsets in conventional and germ-free pigs (1991) Pediatr. Res., 29, pp. 237-242; Saalmuller, Reddehase, Buhring, Jonjic, Koszinowski, Simultaneous expression of CD4 and CD8 antigens by a substantial proportion of resting porcine T lymphocytes (1987) Eur. J. Immunol., 17, pp. 1297-1301; Saalmuller, Hirt, Reddehase, Phenotypic discrimination between thymic and extrathymic CD4−CD8− and CD4+CD8+ porcine T lymphocytes (1989) Eur. J. Immunol., 19, pp. 2011-2016; Saalmuller, Hirt, Reddehase, Porcine γ/δ T lymphocyte subsets differing in their propensity to home to lymphoid tissue (1990) Eur. J. Immunol., 20, pp. 2343-2346; Saif, Wesley, Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , A.D. Leman, B.E. Straw, W.L. Mengeling, S. D'Allaire, D.J. Taylor, 7th edn., Iowa State University Press, Ames; Saif, Bohl, Kohler, Hughes, Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am. J. Vet. Res., 38, pp. 13-20; Sanders, Makgoba, Shaw, Human naive and memory T cells: reinterpretation of helperinducer and suppressor-inducer subsets (1988) Immunol. Today, 9, pp. 195-199; Simkins, Weilnau, Bias, Saif, Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am. J. Vet. Res., 53, pp. 1253-1258; VanCott, Brim, Simkins, Saif, Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; VanCott, Brim, Lunney, Saif, Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J. Immunol., 152, pp. 3980-3990; Van Nieuwstadt, Boonstra, Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus, using monoclonal antibodies to antigenic sites A and X of the S glycoprotein (1992) Am. J. Vet. Res., 53, pp. 184-190; Van Nieuwstadt, Zetstra, Boonstra, Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet. Rec., 125, pp. 58-60; Welch, Saif, Ram, Cell-mediated immune responses of suckling pigs inoculated with attenuated or virulent transmissible gastroenteritis virus (1988) Am. J. Vet. Res., 49, pp. 1228-1234; Wesley, Woods, Active and passive immunity to transmissible gastroenteritis virus induced by porcine respiratory coronavirus (1992) Proceedings II of the 12th Congress of the International Pig Veterinary Society, p. 95. , 17–20 August 1992, The Hague, The Netherlands; Wesley, Woods, Hill, Biwer, Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Wilson, Stokes, Bourne, Responses of intraepithelial lymphocytes to T-cell mitogens: a comparison between murine and porcine responses (1986) Immunology, 58, pp. 621-625; Zeitz, Quinn, Graeff, James, Mucosal T cells provide helper function but do not proliferate when stimulated by specific antigen in lymphogranuloma venereum proctitis in nonhuman primates (1988) Gastroenterology, 94, pp. 353-366","Saif, L.J.; Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Wooster, OH 44691, United States",,,01652427,,VIIMD,"8533315","English","Vet. Immunol. Immunopathol.",Article,"Final",,Scopus,2-s2.0-0029092212
"Vaughn E.M., Halbur P.G., Paul P.S.","7007145803;7005935318;7202714004;","Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes",1995,"Journal of Virology","69","5",,"3176","3184",,65,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028958369&partnerID=40&md5=9366c64550862a99f418854ecc194c05","Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States","Vaughn, E.M., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States; Halbur, P.G., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States; Paul, P.S., Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States","Four new porcine respiratory coronavirus (PRCV) isolates were genetically characterized. Subgenomic mRNA patterns and the nucleotide sequences of the 5' ends of the S genes, the open reading frame (ORF) 3/3a genes, and the ORF 3-1/3b genes of these PRCV isolates were determined and compared with those of other PRCV and transmissible gastroenteritis virus (TGEV) isolates. The S, ORF 3/3a, and ORF 3-1/3b genes are under intense study because of their possible roles in determining tissue tropism and virulence. Northern (RNA) blot analysis of subgenomic mRNAs revealed that mRNA 2, which encodes for the S gene, of the PRCV isolates migrated faster than the mRNA 2 of TGEV. The PRCV isolates AR310 and LEPP produced eight subgenomic mRNA species, the same number as produced by the virulent Miller strain of TGEV. However, the PRCV isolates IA1894 and ISU-1 produced only seven subgenomic mRNA species. All four of the PRCV isolates were found to have a large in-frame deletion in the 5' end of the S gene; however, the size and location of the deletion varied. Analysis of the ORF 3/3a gene nucleotide sequences from the four PRCV isolates also showed a high degree of variability in this area. The ORF 3 gene of the PRCV isolates AR310 and LEPP was preceded by a CTAAAC leader RNA- binding site, and the ORF 3 gene was predicted to yield a protein of 72 amino acids, the same size as that of the virulent Miller strain of TGEV. The PRCV isolates AR310 and LEPP are the first PRCV isolates found to have an intact ORF 3 gene. The ORF 3a gene of the PRCV isolate IA1894 was preceded by a CTAAAC leader RNA-binding site and was predicted to yield a truncated protein of 54 amino acids due to a 23-nucleotide deletion. The CTAAAC leader RNA- binding site and ATG start codon of ORF 3 gene of the PRCV isolate ISU-1 were removed because of a 168-nucleotide deletion. Analysis of the ORF 3-1/3b gene nucleotide sequences from the four PRCV nucleotides isolates also showed variability.",,"article; codon; coronavirus; gene deletion; genetic analysis; nonhuman; nucleotide sequence; open reading frame; priority journal; sequence analysis; virus virulence; Amino Acid Sequence; Animal; Base Sequence; Cloning, Molecular; Comparative Study; Coronavirus; DNA, Complementary; DNA, Viral; Gene Deletion; Genes, Viral; Molecular Sequence Data; Open Reading Frames; Polymerase Chain Reaction; RNA, Messenger; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Support, Non-U.S. Gov't; Swine; Transmissible gastroenteritis virus; Variation (Genetics)",,"Paul, P.S.; Veterinary Medical Research Inst., Iowa State University, 1802 Elwood Dr., Ames, IA 50011, United States",,,0022538X,,JOVIA,"7707547","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028958369
"Lanza I., Shoup D.I., Saif L.J.","6701643399;7003909464;7102226747;","Lactogenic immunity and milk antibody isotypes to transmissible gastroenteritis virus in sows exposed to porcine respiratory coronavirus during pregnancy.",1995,"American journal of veterinary research","56","6",,"739","748",,36,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029315559&partnerID=40&md5=d46a877f032966d5341fceb8cdc5d2ee","Departamento de Sanidad Animal, Facultad de Veterinaria, Universidad de León, Spain","Lanza, I., Departamento de Sanidad Animal, Facultad de Veterinaria, Universidad de León, Spain; Shoup, D.I., Departamento de Sanidad Animal, Facultad de Veterinaria, Universidad de León, Spain; Saif, L.J., Departamento de Sanidad Animal, Facultad de Veterinaria, Universidad de León, Spain","Passive protection provided by sows inoculated with the virulent Miller strain of transmissible gastroenteritis virus (TGEV), or the ISU-1 strain of porcine respiratory coronavirus (PRCV), or both was evaluated in nursing pigs challenge exposed with virulent TGEV. Four sows (group B) were inoculated with PRCV oronasally twice at 4 and 2 weeks before parturition; 1 sow (group C) was inoculated similarly, but in 2 subsequent pregnancies; and 2 sows (group D) were oronasally primed with PRCV at 4 weeks before parturition, and 2 weeks later were administered a booster inoculation of virulent TGEV. Two additional sows (group E) remained uninoculated and served as seronegative controls, and 1 sow (group A) that had been naturally infected with TGEV served as a seropositive control. The degree of passive immunity transferred by these sows to their litters was assessed by challenge exposing the pigs of sows in groups B-E (only the second litter of group C) with virulent TGEV at 3 to 5 days of age. After challenge exposure, clinical signs of infection and mortality were noted and fecal and nasal shedding of virus was assessed by ELISA. The IgA, IgG, and IgM antibody titers to TGEV were quantified in colostrum and milk of the sows by use of an isotype-specific monoclonal antibody-capture ELISA, using biotinylated monoclonal antibodies against each porcine isotype as detecting reagents. A plaque-reduction assay was used to quantify neutralizing antibody titers in serum, colostrum, milk, and fractionated whey (IgG and IgA/IgM). In the sow naturally infected with TGEV (group A), there was a pronounced decrease in IgG antibody titers to TGEV in the transition from colostrum to milk, and IgA TGEV antibodies became predominant, with high titers maintained throughout lactation. The 4 group-B sows partially protected their pigs after TGEV challenge exposure; mean mortality was 67%, compared with 100% in pigs suckling the 2 TGEV seronegative control sows (group-E litters). Although IgA TGEV antibodies were detected in colostrum and milk of group-B sows, IgG TGEV antibodies were the most abundant. The sow of group C had a marked increase in IgA TGEV antibody titers in colostrum and milk after reinoculation with PRCV during the second pregnancy, before TGEV challenge exposure of the litter. Its pigs were passively protected to a high degree after TGEV challenge exposure (27% litter mortality). The sows in group D, primed with PRCV and boosted with TGEV, provided the best passive protection after TGEV challenge exposure of their pigs. Not only litter mortality (27%) but also morbidity was reduced, compared with those factors for the other challenge-exposed litters, and the sows did not become ill.(ABSTRACT TRUNCATED AT 400 WORDS)",,"immunoglobulin class; virus antibody; virus antigen; animal; animal disease; antibody production; article; biosynthesis; blood; breeding; cattle; Coronavirus; enzyme linked immunosorbent assay; female; immunology; methodology; milk; passive immunization; pregnancy; respiratory tract infection; swine; swine disease; Transmissible gastroenteritis virus; Animals; Antibodies, Viral; Antibody Formation; Antigens, Viral; Cattle; Coronavirus; Enzyme-Linked Immunosorbent Assay; Female; Gastroenteritis, Transmissible, of Swine; Immunity, Maternally-Acquired; Immunization, Passive; Immunoglobulin Isotypes; Milk; Pregnancy; Pregnancy, Animal; Respiratory Tract Infections; Swine; Swine Diseases; Transmissible gastroenteritis virus",,"Lanza, I.",,,00029645,,,"7653882","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029315559
"Vieler E., Herbst W.","6603650281;16161781000;","Electron microscopic demonstration of viruses in feces of dogs with diarrhea [Elektronenmikroskopischer Virusnachweis in Kotproben durchfallkranker Hunde.]",1995,"Tierärztliche Praxis","23","1",,"66","69",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029248116&partnerID=40&md5=595cf6aad82c1e23113fe0af30414f59","Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen., Germany","Vieler, E., Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen., Germany; Herbst, W., Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen., Germany","4044 stool samples of dogs with diarrhoea were examined by electron microscopy. The samples were sent for routine diagnostics in the years 1988-1993. Over the examination period virus was detected in 32% of the samples. Parvovirus was diagnosed in 17.2% and coronavirus in 12.4% of the cases. The number of parvovirus-positive samples was lower than in former years, whereas the number of coronavirus-positive samples was higher. Other virus particles (paramyxo-, picorna-, calici- and astrovirus or morphologically similar particles as well as rota- and adenovirus) were altogether detected in 2.5% of the samples. This detection rate corresponded to the results of former years. The majority of parvovirus-positive samples (80.7%) was found in animals aged between six weeks and six months. Of the coronavirus-positive samples 56.5% were detected in dogs older than six months of age and 42.5% in animals between six weeks and six months. In puppies up to six weeks viruses were only detected infrequently (parvovirus 4.7%, coronavirus 0.9%).",,"animal; animal disease; article; Coronavirus; diarrhea; dog; dog disease; electron microscopy; feces; isolation and purification; methodology; microbiology; Parvovirus; virology; virus infection; Animals; Coronavirus Infections; Coronavirus, Canine; Diarrhea; Dog Diseases; Dogs; Feces; Microscopy, Electron; Parvoviridae Infections; Parvovirus",,"Vieler, E.",,,03036286,,,"7792778","German","Tierarztl Prax",Article,"Final",,Scopus,2-s2.0-0029248116
"Finlaison D.S.","6507360587;","Faecal viruses of dogs - an electron microscope study",1995,"Veterinary Microbiology","46","1-3",,"295","305",,12,"10.1016/0378-1135(95)00094-Q","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029027941&doi=10.1016%2f0378-1135%2895%2900094-Q&partnerID=40&md5=2952671b666a98947d80519fd4d53cc6","Department of Veterinary Pathology, University of Sydney, Sydney, NSW 2006, Australia","Finlaison, D.S., Department of Veterinary Pathology, University of Sydney, Sydney, NSW 2006, Australia","Faecal samples from 112 dogs both with and without diarrhoea were screened for parvovirus by a haemagglutination titration test and then examined by electron microscopy for the presence of viruses and virus-like particles. On the basis of morphology eight distinct viruses or virus-like particles were identified. Particles identified were coronaviruses, coronavirus-like particles, rotavirus-like particles, papovavirus-like particles, torovirus-like particles, picornavirus-like particles, 27 nm virus-like particles with projections and parvovirus-like particles which did not cause haemagglutination. © 1995.","Coronavirus; Dogs; Faecal viruse","animal experiment; conference paper; controlled study; coronavirus; dog; electron microscopy; feces analysis; nonhuman; parvovirus; ultrastructure; virus characterization; virus detection; virus infection; Animal; Comparative Study; Coronavirus; Coronavirus Infections; Diarrhea; Dog Diseases; Dogs; Feces; Microscopy, Electron; Parvoviridae Infections; Parvovirus; Reference Values; Support, Non-U.S. Gov't; Viruses","Appel, Cooper, Greisen, Scott, Carmichael, Canine viral enteritis. I. Status report on corona-and parvo-like viral enteritides (1979) Cornell Vet., 69, pp. 123-133; Binn, Lazar, Keenan, Huxsoll, Marchwicki, Strano, Recovery and characterization of a coronavirus from military dogs with diarrhoea (1975) Proc. 78th Ann. Meeting U.S. Animal Hlth. Assoc., pp. 359-366; Carmichael, Infectious canine enteritis caused by a Corona like virus: current status and request for information (1978) Baker Fast. Lab. Rep. Series, 2 (9); Carmichael, Binn, New enteric viruses in the dog (1981) Adv. Vet. Sci. Comp. Med., 25, pp. 1-37; Doane, Anderson, Electron Microscopy in Diagnostic Virology (1987) A practical guide and atlas, , Cambridge University Press; England, Poston, Electron microscopic identification and subsequent isolation of a rotavirus from a dog with fatal neonatal diarrhea (1980) Am. J. Vet. Res., 41, pp. 782-783; Eugster, Sidwa, Rotaviruses in diarrheic feces of a dog (1979) Vet. Med. small Anim. Clin., 74, pp. 817-819; Evermann, McKeirnan, Smith, Skilling, Ott, Isolation and identification of caliciviruses from dogs with enteric infections (1985) Am. J. Vet. Res., 46, pp. 218-220; Fulton, Johnson, Pearson, Woode, Isolation of a rotavirus from a newborn dog with diarrhoea (1981) Am. J. Vet. Res., 42, pp. 841-843; Hamilton, Particles in canine faeces (1983) Aust. Vet. Practit., 13, p. 36; Hammond, Timoney, An electron microscopic study of viruses associated with canine gastroenteritis (1983) Cornell Vet., 73, pp. 82-97; Marshall, Healy, Studdert, Scott, Kennett, Ward, Gust, Viruses and virus like particles in the faeces of dogs with and without diarrhoea (1984) Aust. vet. J., 61, pp. 33-38; McGavin, (1985) PhD thesis, pp. 86-87; Mochizuki, Hsuan, Isolation of a rotavirus from canine diarrhoeal faeces (1984) Jpn. J. Vet. Sci., 46, pp. 905-908; Mochizuki, Kawanishi, Sakamoto, Tashiro, Fujimoto, Ohwaki, A calicivirus isolated from a dog with fatal diarrhoea (1993) Vet. Rec., 132, pp. 221-222; Schaffer, Soergel, Black, Skilling, Smith, Cubitt, Characterization of a new calicivirus isolated from feces of a dog (1985) Arch. Virol., 84, pp. 181-195; Schnagl, Brookes, Medvedec, Morey, Characteristics of Australian human enteric coronavirus-like particles: comparison with human respiratory coronavirus 229E and duodenal brush border vesicles (1987) Arch. Virol., 97, pp. 309-323; Schnagl, Holmes, Coronavirus-like particles in stools from dogs, from some country areas of Australia (1978) Vet. Rec., 102, pp. 528-529; Schroeder, Kalmakoff, Holdaway, Todd, The isolation of rotavirus from calves foals dogs and cats in New Zealand (1983) New Zealand Veterinary Journal, 31, pp. 114-116; Tzipori, Makin, Propagation of human rotavirus in young dogs (1978) Vet. Microbiol., 3, pp. 55-63; Williams, Astrovirus-like, coronavirus-like, and parvovirus-like particles detected in the diarrhoeal stools of beagle pups (1980) Arch. Virol., 66, pp. 215-226","Finlaison, D.S.; Department of Veterinary Pathology, University of Sydney, Sydney, NSW 2006, Australia",,,03781135,,VMICD,"8545969","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0029027941
"Levis R., Cardellichio C.B., Scanga C.A., Compton S.R., Holmes K.V.","7005215033;6602071538;6701713751;7102893878;7201657724;","Multiple receptor-dependent steps determine the species specificity of HCV-229E infection",1995,"Advances in Experimental Medicine and Biology","380",,,"337","343",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028787268&partnerID=40&md5=aea95b7158e5588a2e66442d3923a4c3","Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States","Levis, R., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States; Cardellichio, C.B., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States; Scanga, C.A., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States; Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States; Holmes, K.V., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States","Human coronavirus (HCV) -229E causes disease only in humans and grows in human cells and in cells of other species that express recombinant human aminopeptidase N (hAPN), the receptor for HCV-229E. We compared the species specificity of HCV-229E infection with the species specificity of virus binding using immunofluorescence, assay of virus yields, fluorescence activated cell sorting and a monoclonal antibody directed against hAPN that blocks infection. We found that HCV-229E binds to intestinal brush border membranes (BBM) and to membranes of cell lines from cats, dogs, pigs, and humans, however the virus only infects two of these species. HCV-229E will not bind to BBM or to membranes from cell lines derived from hamster or mice. Animal coronaviruses related to HCV-229E, including FIPV, CCV, and TGEV bind to cell membranes from cats, dogs, cows, pigs and humans (but not mice), while each virus infects cells from only a subset of these species. Infectious genomic HCV-229E RNA, can infect cells of all of these species. These data suggest that the species-specificity of infection for this serogroup of coronaviruses is determined at the levels of virus binding and penetration. Since binding of viral spike glycoprotein to cellular receptors is not the only limiting factor, we suggest that one or more steps associated with virus penetration may determine the species specificity of infection with the HCV-229E serogroup of coronaviruses.",,"microsomal aminopeptidase; virus receptor; animal cell; cat; conference paper; coronavirus; dog; fluorescence activated cell sorter; human; human cell; immunofluorescence; intestine brush border; mouse; nonhuman; priority journal; receptor binding; species difference; swine; virus infection; virus infectivity; Animal; Cats; Cell Line; Comparative Study; Coronavirus; Coronavirus 229E, Human; Dogs; Glycoproteins; Hamsters; Human; Intestines; Mice; Microvilli; Murine hepatitis virus; Receptors, Virus; Species Specificity; Support, U.S. Gov't, P.H.S.; Swine",,"Compton, S.R.; Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8019, United States",,,00652598,,AEMBA,"8830504","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028787268
"Kottier S.A., Cavanagh D., Britton P.","6505850323;26642890500;57203302770;","First experimental evidence of recombination in infectious bronchitis virus: Recombination in IBV",1995,"Advances in Experimental Medicine and Biology","380",,,"551","556",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028805545&partnerID=40&md5=ecbc327a1c5f3a9f0b39367651d3f247","Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom","Kottier, S.A., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom","A high frequency of recombination has been shown to occur during replication of the coronavirus mouse hepatitis virus (MHV) in vitro as well as in vivo. Although sequencing of field strains of coronavirus infectious bronchitis virus (IBV) has indicated that IBV strains also undergo recombination, there has been no experimental evidence to support this deduction. To investigate whether recombination occurs in IBV, embryonated eggs were coinfected with IBV-Beaudette and IBV-M41. Potential recombinants were detected by strain-specific polymerase chain reaction (PCR) amplifications, using oligonucleotides corresponding to regions in the 3' end of the genome. Sequencing of the PCR products confirmed that a number of recombinations had occurred between the two strains.",,"avian infectious bronchitis virus; conference paper; genetic recombination; murine hepatitis coronavirus; nonhuman; polymerase chain reaction; priority journal; virus replication; virus strain; Animal; Base Sequence; Chick Embryo; DNA Primers; Infectious bronchitis virus; Mice; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Recombination, Genetic; RNA, Viral; Support, Non-U.S. Gov't; Virus Replication",,"Kottier, S.A.; Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom",,,00652598,,AEMBA,"8830540","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028805545
"Gallagher T.M.","7202310503;","Overexpression of the MHV receptor: Effect on progeny virus secretion",1995,"Advances in Experimental Medicine and Biology","380",,,"331","336",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028807204&partnerID=40&md5=6deb4e8fff6f6933def8bc4968d0fe9b","Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","Gallagher, T.M., Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","The intracellular interaction of the coronavirus mouse hepatitis virus (MHV) with its cellular receptor (MHVR) was investigated. Overexpression of MHVR from vaccinia vectors during an ongoing MHV infection resulted in dramatic inhibition of virus production. Infectivity in both cytoplasmic extracts and supernatants was reduced by over three orders of magnitude relative to control cultures in which a truncated MHVR lacking virus binding activity was expressed. Complete MHV virions were not detectable in supernatants of MHVR expressing cells. In the presence of overexpressed MHVR, the coronavirus spike protein was not cleaved into posttranslation products S1 and S2, nor was it fully processed into a form resistant to endoglycosidase H digestion, indicating that intracellular engagement of spike with receptor prevented spike transport and consequent association with virions.",,"virus glycoprotein; virus receptor; animal cell; conference paper; gene expression; golgi complex; murine hepatitis coronavirus; nonhuman; priority journal; protein degradation; protein processing; protein transport; virion; virus infectivity; virus inhibition; Animal; Cell Line; Cells, Cultured; Genetic Vectors; Glycoproteins; Immunoblotting; Membrane Glycoproteins; Mice; Murine hepatitis virus; Protein Processing, Post-Translational; Receptors, Virus; Recombinant Proteins; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Vaccinia virus; Viral Envelope Proteins; Virion; Virus Replication",,"Gallagher, T.M.; Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States",,,00652598,,AEMBA,"8830503","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028807204
"Talbot P.","7102670281;","Implication of viruses in multiple sclerosis [IMPLICATION DES VIRUS DANS LA SCLEROSE EN PLAQUES]",1995,"Medecine/Sciences","11","6",,"837","843",,10,"10.4267/10608/2295","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029071024&doi=10.4267%2f10608%2f2295&partnerID=40&md5=f283eddcd466b8fb7165f42b98ac97c5","Laboratoire de Neuro-Immunologie, Centre de Recherche en Virologie, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Talbot, P., Laboratoire de Neuro-Immunologie, Centre de Recherche en Virologie, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada","Multiple sclerosis (MS) is an inflammatory neurological disease that results from an immune attack and destruction of the myelin sheath that normally surrounds nerve fibers. This chronic and recurrent demyelination perturbs the normal flow of nerve impulses and leads to a debilitating disease that affects about 0.2% of young adults in high-incidence areas such as Canada, making it the most prevalent neurological disease in this age group. Despite a still mysterious etiology, it is clear that the development of MS involves both genetic factors such as immune response genes HLA-DR2, and environmental factors, most likely infectious agents. About fifteen different viruses have been associated with MS over the years, but not a single agent has yet emerged as the strongest candidate. Coronaviruses are one of the most recent viral agents reported in association with MS, but more research is needed to strengthen their possible involvement. Unfortunately, coronaviruses have yet to attract the attention of the medical community, having been so far only implicated in relatively benign respiratory infections of the common cold type. On the other hand, coronaviruses in mice have provided for several years one of the best animal models of a viral disease that resembles human MS. The viral hypothesis for MS remains highly reasonable but is unlikely to involve only one virus but rather several viruses that could initiate by a common mechanism the immune disorders leading to the demyelination of MS. Hence, all viral possibilities and relevant animal models need to be explored in order to gain a better understanding of the mechanisms involved in disease initiation. In parallel, various promising treatments need to be scientifically validated to provide hope to patients while the elucidation of the exact causes of MS slowly proceeds, faster progress rendered possible by a close collaboration between virologists, immunologists and neurologists.",,"HLA DR2 antigen; animal model; common cold; Coronavirus; demyelination; environmental factor; human; immunogenetics; inflammatory disease; mouse; multiple sclerosis; nerve conduction; neurologic disease; nonhuman; respiratory tract infection; review; Animalia; Coronavirus",,"Talbot, P.; Laboratoire de Neuro-Immunologie, Centre de Recherche en Virologie, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada",,"Editions EDK",07670974,,MSMSE,,"French","MED. SCI.",Review,"Final",Open Access,Scopus,2-s2.0-0029071024
"Hirschberger J., Hartmann K., Wilhelm N., Frost J., Lutz H., Kraft W.","7004025795;7201407340;6603035089;7202439178;35480426400;7102138682;","Clinical symptoms and diagnosis of feline infectious peritonitis [Klinik und Diagnostik der Felinen Infektiösen Peritonitis.]",1995,"Tierärztliche Praxis","23","1",,"92","99",,28,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029245259&partnerID=40&md5=41476b213e6b239e8fbfa1445773a7e6","I. Medizinischen Tierklinik, Universität München., Germany","Hirschberger, J., I. Medizinischen Tierklinik, Universität München., Germany; Hartmann, K., I. Medizinischen Tierklinik, Universität München., Germany; Wilhelm, N., I. Medizinischen Tierklinik, Universität München., Germany; Frost, J., I. Medizinischen Tierklinik, Universität München., Germany; Lutz, H., I. Medizinischen Tierklinik, Universität München., Germany; Kraft, W., I. Medizinischen Tierklinik, Universität München., Germany","Body effusions from 197 cats and blood serum samples from 252 cats, where Feline Infectious Peritonitis (FIP) was part of the differential diagnosis, were analysed. The diagnoses were confirmed by clinical follow up or histopathology. The final diagnosis FIP was always confirmed by histopathology. The median age of cats with FIP was 1.6 years. FIP was responsible for 41% of the body effusions, whereas malignomas caused 24%, cardial insufficiencies 14% and purulent serositis 12% of the body effusions. The rivalta test was highly sensitive for FIP. Predictive value of a negative result was 100%, predictive value of a positive result was 84%. In half of the cases with purulent serositis and in 20% of malignomas rivalta reacted positive. The cardial insufficiencies were negative for rivalta. Coronavirus antigen could be demonstrated by immunofluorescence in 34 of 49 body effusions caused by FIP, whereas in the 50 body effusions caused by other diseases no coronavirus antigen was detected. An albumin globulin ratio of < 0.6 was highly diagnostic for an inflammatory process, nearly exclusively for FIP. An albumin globulin ratio of > or = 0.8 almost excluded FIP. Only a negative or very high (1:1600) FIP titer could contribute to confirm diagnosis. Low and medium titers, however, should not be interpreted.",,"serum albumin; serum globulin; aging; animal; article; blood; body fluid; cat; cat disease; comparative study; differential diagnosis; pathology; prediction and forecasting; sensitivity and specificity; virology; Aging; Animals; Body Fluids; Cats; Diagnosis, Differential; Feline Infectious Peritonitis; Predictive Value of Tests; Sensitivity and Specificity; Serum Albumin; Serum Globulins",,"Hirschberger, J.",,,03036286,,,"7792783","German","Tierarztl Prax",Article,"Final",,Scopus,2-s2.0-0029245259
"Masters P.S., Peng D., Fischer F.","7006234572;7202530662;7202883540;","Mutagenesis of the genome of mouse hepatitis virus by targeted RNA recombination",1995,"Advances in Experimental Medicine and Biology","380",,,"543","549",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028865889&partnerID=40&md5=dde0103959ffa74a0add6139c75a0e90","Wadsworth Ctr. for Laboratories/Res., New York State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, United States","Masters, P.S., Wadsworth Ctr. for Laboratories/Res., New York State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, United States; Peng, D., Wadsworth Ctr. for Laboratories/Res., New York State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, United States; Fischer, F., Wadsworth Ctr. for Laboratories/Res., New York State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, United States","Our laboratory has described a method for introducing site-specific mutations into the genome of the coronavirus mouse hepatitis virus (MHV) by RNA recombination between cotransfected genomic RNA and a synthetic subgenomic mRNA. By using a thermolabile N protein mutant of MHV as the recipient virus and synthetic RNA7 (the mRNA for the nucleocapsid protein N) as the donor, engineered recombinant viruses were selected as heat-stable progeny resulting from cotransfection. We have recently reported an optimization of the efficiency of targeted recombination in this process by using a synthetic defective interfering (Dl) RNA in place of RNA7. The frequency of recombination is sufficiently high that recombinants can often be directly identified without employing a thermal selection. We present here a progress report on our use of this system to map MHV mutants and to construct N gene mutants which include (1) a mutant in which the internal open reading frame within the N gene (the I gene) has been disrupted, and (2) a series of recombinants in which portions of the MHV N gene have been replaced by the homologous regions from the N gene of bovine coronavirus. We also report on some mutants we have not been able to construct.",,"capsid protein; messenger rna; recombinant rna; virus nucleoprotein; virus rna; conference paper; genetic recombination; murine hepatitis coronavirus; nonhuman; priority journal; rna sequence; virus capsid; virus gene; virus mutant; Amino Acid Sequence; Animal; Base Sequence; Capsid; Genetic Vectors; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Sorting Signals; Recombination, Genetic; Repetitive Sequences, Nucleic Acid; Restriction Mapping; RNA, Messenger; RNA, Viral; Support, U.S. Gov't, P.H.S.; Viral Core Proteins",,"Masters, P.S.; Wadsworth Ctr. for Laboratories/Res., New York State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, United States",,,00652598,,AEMBA,"8830539","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028865889
"Wasmoen T.L., Kadakia N.P., Unfer R.C., Fickbohm B.L., Cook C.P., Chu - H.J., Acree W.M.","6602099285;56926607200;57205001934;57192748108;7402436214;7202364837;7103180682;","Protection of cats from infectious peritonitis by vaccination with a recombinant raccoon poxvirus expressing the nucleocapsid gene of feline infectious peritonitis virus",1995,"Advances in Experimental Medicine and Biology","380",,,"221","228",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028802463&partnerID=40&md5=c9570d2f3536bb7c885f1731253760d7","Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States","Wasmoen, T.L., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Kadakia, N.P., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Unfer, R.C., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Fickbohm, B.L., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Cook, C.P., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Chu -, H.J., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States; Acree, W.M., Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States","Feline Infectious Peritonitis Virus (FIPV) is a coronavirus that induces an often fatal, systemic infection in cats. Various vaccines designed to prevent FIPV infection have been shown to exacerbate the disease, probably due to immune enhancement mediated by virus-specific immunoglobulins against the outer envelope (S) protein. An effective vaccine would be one that induces cell-mediated immunity without disease enhancing antibodies. In this report, we describe the use of a recombinant raccoon poxvirus that expresses the gene encoding the nucleocapsid protein of FIPV (rRCNV-FIPV N) as an effective vaccine against FIPV-induced disease. Cats were parenterally or orally vaccinated twice, three weeks apart. Cats were then orally challenged with Feline Enteric Coronavirus (FECV), which induces a subclinical infection that can cause enhancement of subsequent FIPV infection. Three weeks later, cats were orally challenged with FIPV. The FIPV challenge induced a fatal infection in 4/5 (80%) of the controls. On the other hand, all five cats vaccinated subcutaneously with rRCNV-FIPV N showed no signs of disease after challenge with FIPV. Four of the five subcutaneous vaccinates survived an additional FIPV challenge. Vaccination with rRCNV-FIPV N induced serum IgG antibody responses to FIPV nucleocapsid protein, but few, if any, FIPV neutralizing antibodies. In contrast to the controls, protected vaccinates maintained low FIPV serum neutralizing antibody titers after FIPV challenge. This suggests that the protective immune response involves a mechanism other than humoral immunity consisting of FIPV neutralizing antibodies.",,"immunoglobulin g antibody; neutralizing antibody; recombinant vaccine; virus protein; virus vaccine; animal experiment; antibody response; antibody titer; cat; conference paper; controlled study; coronavirus; nonhuman; oral drug administration; poxvirus; priority journal; subcutaneous drug administration; survival; vaccination; virus infection; virus nucleocapsid; Animal; Capsid; Cats; Cell Line; Cercopithecus aethiops; Cloning, Molecular; Coronavirus, Feline; Dose-Response Relationship, Drug; Feline Infectious Peritonitis; Genes, Viral; Poxviridae; Raccoons; Time Factors; Vaccination; Vaccines, Synthetic; Vero Cells; Viral Core Proteins; Viral Vaccines",,"Wasmoen, T.L.; Biological Research and Development, Fort Dodge Laboratories, 800 Fifth Street NW, Fort Dodge, IA 50501, United States",,,00652598,,AEMBA,"8830483","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028802463
"Ganaba R., Bélanger D., Dea S., Bigras-Poulin M.","57211662231;7102205107;7006056287;6602881462;","A seroepidemiological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from northwestern Quebec.",1995,"Canadian journal of veterinary research = Revue canadienne de recherche vétérinaire","59","1",,"26","33",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029191313&partnerID=40&md5=3bc0cf692c3b775487c0e11c99eb0768","Département de pathologie et microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada","Ganaba, R., Département de pathologie et microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada; Bélanger, D., Département de pathologie et microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada; Dea, S., Département de pathologie et microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada; Bigras-Poulin, M., Département de pathologie et microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada","Serum antibody analyses for bovine herpesvirus type 1 (BHV-1), bovine viral diarrhea virus (BVDV), bovine respiratory syncytial virus (BRSV), bovine coronavirus (BCV), and bovine rotavirus (BRV) were performed on 527 randomly selected cows, before calving, and on 407 three-week-old calves. In cows and calves, BCV and BRV were the most seroprevalent viruses (80% to 100% according to virus and vaccination status). Bovine respiratory syncytial virus was the least seroprevalent in the cows, independent of the vaccination status. In nonvaccinated cows the seroprevalence to BRSV was 36.7%, and 53.5% in cows vaccinated less than two weeks prior to collecting blood, and 67.6% in cows vaccinated two weeks or more prior to blood collection. In their calves, BHV-1 was the least seroprevalent, independent of the vaccination status. The serological status and antibody titers in calves were generally associated with those of the dam. The occurrence of respiratory diseases in the calves was associated with cow and calf serological profiles (BHV-1, BRSV and BCV in the nonvaccinated group, BHV-1, BVDV and BCV in the vaccinated group). The occurrence of diarrhea was not associated with cow and calf serological profiles but was negatively associated with high level calf serum IgG in the nonvaccinated group (odds ratio = 0.73). Bovine coronavirus and BRV were shed by 1.4% and 4.9% of calves in the nonvaccinated group, and by 0% and 9.9% of calves in the vaccinated group, respectively. Bovine rotavirus shedding was associated with fecal diarrheic consistency at the moment of fecal sampling but not with previous occurrence of diarrhea.",,"immunoglobulin G; virus antibody; animal; animal disease; article; blood; Canada; cattle; cattle disease; Coronavirus; epidemiology; feces; female; Herpes virus infection; immunology; Infectious bovine rhinotracheitis virus; microbiology; Respiratory syncytial pneumovirus; statistics; virology; virus infection; Animals; Antibodies, Viral; Bovine Virus Diarrhea-Mucosal Disease; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Feces; Female; Herpesviridae Infections; Herpesvirus 1, Bovine; Immunoglobulin G; Quebec; Respiratory Syncytial Virus Infections; Respiratory Syncytial Virus, Bovine; Rotavirus Infections; Seroepidemiologic Studies; Statistics; Virus Diseases",,"Ganaba, R.",,,08309000,,,"7704839","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029191313
"Gruffydd-Jones T., Harbour D.A., Jones B.R.","7005620906;7005502394;57191762527;","Coronavirus antibody titres in cats in New Zealand",1995,"New Zealand Veterinary Journal","43","4",,"166","167",,1,"10.1080/00480169.1995.35882","https://www.scopus.com/inward/record.uri?eid=2-s2.0-24644524687&doi=10.1080%2f00480169.1995.35882&partnerID=40&md5=7498bb2e5326024a17d5b843723013d9","The Feline Centre, Department of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol, United Kingdom; Department of Veterinary Clinical Sciences, Massey University, Palmerston North, New Zealand","Gruffydd-Jones, T., The Feline Centre, Department of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol, United Kingdom; Harbour, D.A., The Feline Centre, Department of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol, United Kingdom; Jones, B.R., Department of Veterinary Clinical Sciences, Massey University, Palmerston North, New Zealand",[No abstract available],,,"Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Gaskell, C.J., Virus shedding and immune responses in cats inoculated with cell culture adapted from feline infectious peritonitis virus (1988) Veterinary Microbiology, 16, pp. 145-158; Horzinek, M.C., Osterhaus, A., Feline infectious peritonitis: A worldwide serological survey (1979) American Journal of Veterinary Research, 40, pp. 1487-1492; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., Coronavirus serology in healthy pedigree cats (1992) Veterinary Record, 131, pp. 35-36; Loeffler, D.G., Ott, R.L., Evermann, J.F., Alexander, J.E., The incidence of naturally occurring antibodies against feline infectious peritonitis in selected cat populations (1978) Feline Practice, 8 (1), pp. 43-47; Horzinek, M.C., Lutz, H., Petersen, N.Z., Antigenic relationships among homologous structural polypeptides of porcine, feline and canine coronavirus (1979) Infection and Immunity, 37, pp. 1148-1155; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., Feline infectious peritonitis: A review of clinicopathological changes in 65 cases and a critical assessment of their diagnostic value (1992) Veterinary Record, 129, pp. 209-212; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus, FIP-UCD2, FIP-UCD3 and FIPUCD4 (1985) Compendium on Continuing Education for the Practising Veterinarian, 7, pp. 1101-1111","Gruffydd-Jones, T.; The Feline Centre, Department of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol, United Kingdom",,,00480169,,,,"English","New Zealand Vet. J.",Article,"Final",,Scopus,2-s2.0-24644524687
"Sizun J., Soupre D., Giroux J.D., Legrand M.C.","35605340000;6602842875;17934302900;7102317918;","Infection respiratoire nosocomiale par le coronavirus dars une unité de réanimation néonatále: évaluation prospective",1995,"Archives de pediatrie","2","10",,"1020","1021",,4,"10.1016/0929-693X(96)89905-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-16144367061&doi=10.1016%2f0929-693X%2896%2989905-2&partnerID=40&md5=6e390ba67bf51e1636cbff37ccbc4f8b","Service de réanimation pédiatrique et néonatologie CHU, 29609 Brest, France; département de microbiologie, CHU, 29609 Brest, France","Sizun, J., Service de réanimation pédiatrique et néonatologie CHU, 29609 Brest, France; Soupre, D., Service de réanimation pédiatrique et néonatologie CHU, 29609 Brest, France; Giroux, J.D., Service de réanimation pédiatrique et néonatologie CHU, 29609 Brest, France; Legrand, M.C., département de microbiologie, CHU, 29609 Brest, France",[No abstract available],,"cross infection; disease transmission; France; human; newborn; newborn intensive care; note; prospective study; respiratory tract infection; statistics; virus infection; Coronavirus Infections; Cross Infection; France; Humans; Infant, Newborn; Intensive Care Units, Neonatal; Prospective Studies; Respiratory Tract Infections","Chodicelli, Duboi, Thouvenot, Dutruge, Bellon, Infection à coronavirus du nourisson: atteinte des voies aériennes baises, apnée et mort subile? (Lettre) (1995) Arch Pédiatr, 2, p. 285; Sizun, Soupre, Legrand, Role pathogene des coronavirus en réanimation pédiarique: analyse rétrospective de 19 prélèvements positifs en immunofluorescence indirecte (1994) Arch Pédiatr, 1, pp. 477-480; Sizun, Soupre, Giroux, Nasal colonization with coronavirus and apnea of the premature newborn. (Letter) (1993) Acta Paediatr, 82, p. 238; Sizun, Soupre, Legrand, Neonatal nosocomial respiratory infection with coronavirus: a prospective study in a neonatal intensive care unit (1993) Acta Paediatr, , (sous presse)","Sizun, J.; Service de réanimation pédiatrique et néonatologie CHU, 29609 Brest, France",,,0929693X,,APEDE,"7496463","French","Arch. Pediatr.",Letter,"Final",,Scopus,2-s2.0-16144367061
"Talbot P., Levy G.","7102670281;35391580500;","State of the art: coronaviruses",1995,"Trends in Microbiology","3","4",,"127","129",,,"10.1016/S0966-842X(00)88899-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13444252807&doi=10.1016%2fS0966-842X%2800%2988899-X&partnerID=40&md5=c01fe46a4a0a37196e682fbe13cee487","the Virology Research Center, Institut Armand-Frappier, University of Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; the Dept of Medicine, University of Toronto, Ont. M5G 2C4, Canada","Talbot, P., the Virology Research Center, Institut Armand-Frappier, University of Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; Levy, G., the Dept of Medicine, University of Toronto, Ont. M5G 2C4, Canada",[No abstract available],,"virus vaccine; animal; conference paper; Coronavirus; genetic transcription; human; immunology; pathogenicity; physiology; virus replication; Animal; Coronavirus; Human; Transcription, Genetic; Viral Vaccines; Virus Replication","Cavanagh, Revision of the taxonomy of theCoronavirus, Torovirus andArterivirus genera (1994) Archives of Virology, 135, pp. 227-237; Wege, Siddell, ter Meulen, (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Myint, (1994) Rev. Med. Virol., 4, pp. 35-46; Lai, (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Talbot, P. and Levy, G., eds Proc. 6th Int. Symp. on Corona- and Related Viruses, Adv. Exp. Med. Biol., Plenum Press (in press)","Talbot, P.; the Virology Research Center, Institut Armand-Frappier, University of Quebec, 531 Boulevard des Prairies, Laval, Que. H7N 4Z3, Canada; email: pierre_talbot@iaf.uquebec.ca",,,0966842X,,TRMIE,"7613752","English","Trends Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-13444252807
"Tibbles K.W., Brierley I., Cavanagh D., Brown T.D.K.","6507790687;7004639098;26642890500;56248391000;","A region of the coronavirus infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate",1995,"Journal of General Virology","76","12",,"3059","3070",,13,"10.1099/0022-1317-76-12-3059","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029583636&doi=10.1099%2f0022-1317-76-12-3059&partnerID=40&md5=80736ae51611483bb0b2daffff72e1d7","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom","Tibbles, K.W., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Cavanagh, D., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom","In order to investigate the mechanisms involved in the processing of infectious bronchitis virus polyproteins, several candidate regions of the genome have been cloned and expressed in vitro. During these studies it was observed that the translation product encoded by one of these clones (pKT205) was poorly expressed. Biochemical and genetic analyses revealed that the basis for the poor expression was a post-translational event involving ubiquitination of the protein and degradation by an ATP-dependent system operating in the reticulocyte lysate used for the in vitro expression. Two independently acting regions which conferred instability were identified, one of which mapped to the predicted 3C protease domain, contained within the 5' end of the clone, while the other, more C-terminal region, was effective in conferring instability upon a heterologous protein to which it had been transferred. These regions may influence the stability of the authentic viral protein(s) in vivo and hence allow for the control of their expression and/or function at the level of proteolysis by cellular protease(s).",,"proteinase; ubiquitin; virus protein; amino acid sequence; animal cell; article; bronchitis; controlled study; Coronavirus; gene expression; molecular cloning; nonhuman; priority journal; protein degradation; protein domain; protein processing; protein stability; rabbit; reticulocyte lysate; structure activity relation; Animalia; Avian infectious bronchitis virus; Coronavirus; Oryctolagus cuniculus",,"Brown, T.D.K.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",,"Microbiology Society",00221317,,JGVIA,"8847511","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029583636
"Fleming J.O.","7401457370;","Coronaviruses.",1995,"Journal of neurovirology","1","5-6",,"323","325",,1,"10.3109/13550289509111019","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029420052&doi=10.3109%2f13550289509111019&partnerID=40&md5=fe33fc886c1a7f135421a8d4beca3604",,"Fleming, J.O.",[No abstract available],,"animal; Coronavirus; human; note; virology; virus infection; Animals; Coronavirus; Coronavirus Infections; Humans",,"Fleming, J.O.",,,13550284,,,"9222372","English","J. Neurovirol.",Note,"Final",,Scopus,2-s2.0-0029420052
"Kapil S., Chard-Bergstrom C., Bolin P., Landers D.","7003293348;6602711643;8617849200;7102066565;","Plaque Variations in Clinical Isolates of Bovine Coronavirus",1995,"Journal of Veterinary Diagnostic Investigation","7","4",,"538","539",,5,"10.1177/104063879500700420","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029383437&doi=10.1177%2f104063879500700420&partnerID=40&md5=278f07ebaa376cb2bdba55dbd9bf7f10","Department of Veterinary Diagnostic Investigation, College of Veterinary Medicine, Manhattan, KS 66506, United States; Wisconsin Animal Health Laboratory, Madison, WI 53705, United States","Kapil, S., Department of Veterinary Diagnostic Investigation, College of Veterinary Medicine, Manhattan, KS 66506, United States; Chard-Bergstrom, C., Department of Veterinary Diagnostic Investigation, College of Veterinary Medicine, Manhattan, KS 66506, United States; Bolin, P., Wisconsin Animal Health Laboratory, Madison, WI 53705, United States; Landers, D., Department of Veterinary Diagnostic Investigation, College of Veterinary Medicine, Manhattan, KS 66506, United States",[No abstract available],,"antivirus agent; hygromycin B; animal; article; cattle; cell culture; cell line; Coronavirus; drug effect; human; isolation and purification; microbiological examination; physiology; rectum tumor; virus culture; virus replication; Animals; Antiviral Agents; Cattle; Cell Line; Coronavirus, Bovine; Humans; Hygromycin B; Microbial Sensitivity Tests; Plaque Assay; Rectal Neoplasms; Tumor Cells, Cultured; Virus Replication","Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Cyr-Coats, K.S.t., Storz, J., Bovine coronavirus-induced cytopathic expression and plaque formation: Host cell and virus strain determine trypsin dependence (1988) J Vet Sci B, 35, pp. 48-56; Hirano, N., Sada, Y., Tuchiya, K., Plaque assay of bovine coronavirus in BEK-1 cells (1985) Jpn J Vet Sci, 47, pp. 679-681; Kapil, S., Pomeroy, K.A., Goyal, S.M., Trent, A.M., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J Vet Diagn Invest, 3, pp. 88-89; Kapil, S., Trent, A.M., Goyal, S.M., Excretion and persistence of bovine coronavirus in neonatal calves (1990) Arch Virol, 115, pp. 127-132; Macintyre, G., Curry, B., Wong, F., Hygromycin B therapy of a murine coronaviral hepatitis (1991) Antimicrob Agents Chemother, 35, pp. 2125-2170; Macintyre, G., Curry, B., Wong, F., Hygromycin B inhibits synthesis of murine coronavirus RNA (1991) Antimicrob Agents Chemother, 35, pp. 2630-2633; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, p. 12141; Vautherot, J.F., Plaque assay for titration of bovine enteric coronavirus (1981) J Gen Virol, 56, pp. 451-455",,,,10406387,,,"8580179","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0029383437
"Hirano N., Ono K., Nomura R., Tawara T.","7101604276;7403889877;7101883858;57196911575;","Isolation and Characterization of Sialodacryoadenitis Virus (Coronavirus) from Rats by Established Cell Line LBC",1995,"Journal of Veterinary Medicine, Series B","42","1-10",,"147","154",,1,"10.1111/j.1439-0450.1995.tb00695.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029296039&doi=10.1111%2fj.1439-0450.1995.tb00695.x&partnerID=40&md5=643d7d3f95e9f409856c66dce14c73c5","Department of Veterinary Microbiology, Iwate University, Morioka, Japan","Hirano, N., Department of Veterinary Microbiology, Iwate University, Morioka, Japan; Ono, K., Department of Veterinary Microbiology, Iwate University, Morioka, Japan; Nomura, R., Department of Veterinary Microbiology, Iwate University, Morioka, Japan; Tawara, T., Department of Veterinary Microbiology, Iwate University, Morioka, Japan","The outbreak of sialoadenitis occurred in a laboratory rat colony and the causative agent was isolated from the affected salivary glands of diseased rats using the established cell line LBC. The isolate readily multiplied, producing clear cytopathic effects with syncytium formation, and it was identified virologically and serologically as rat sialodacryoadenitis virus. In attempts to isolate the virus by primary rat kidney (PRK) cells and suckling mice as well as LBC cells, the LBC cells showed higher susceptibility for the virus growth as compared with PRK cells or the brain of suckling mice. The isolation rate of virus was 100 % (5/5) in LBC, 40 % (2/5) in PRK cells and 60 % (3/5) in suckling mice. After four passages in the LBC cells, the virus did not produce disease in adult rats, while the mouse brain‐passaged virus did. © 1995 Blackwell Verlag GmbH",,"animal; animal disease; article; cell line; Coronavirus; electron microscopy; epidemic; experimental animal; female; germfree animal; Institute for Cancer Research mouse; isolation and purification; male; mouse; rat; sialoadenitis; ultrastructure; virology; Wistar rat; Animals; Animals, Laboratory; Cell Line; Coronavirus; Disease Outbreaks; Female; Male; Mice; Mice, Inbred ICR; Microscopy, Electron; Rats; Rats, Wistar; Sialadenitis; Specific Pathogen-Free Organisms","Bhatt, P.N., Percy, D.H., Jonas, A.M., Characterization of the virus of sialodacryoadenitis of rats: a member of coronavirus group (1972) J. Infect. Dis., 126, pp. 123-130; Fujiwara, K., Tanishima, Y., Tanaka, M., Seromonitoring of laboratory mouse and rat colonies for common murine antigen (1980) Exp. Anim., 28, pp. 419-426; Hirano, N., Hino, S., Fujiwara, K., Physicochemical properties of mouse hepatitis virus (MHV‐2) grown on DBT cell culture (1978) Microbiol. Immunol., 22, pp. 377-390; Hirano, N., Ono, K., Plaque assay and propagation in rat cell line LBC cells of rat coronavirus and 5 strains of sialodacryoadenitis virus (1990) J. Vet. Med. B, 37, pp. 91-98; Hirano, N., Ono, K., Sada, Y., Inoue, A., Murakami, T., Replication of rat coronavirus in rat cell line, LBC (1985) Arch. Virol., 85, pp. 301-304; Hirano, N., Sato, R., Matsuda, Y., A survey of feline respiratory infections (1986) Jpn. J. Vet. Sci., 48, pp. 423-427; Hirano, N., Suzuki, Y., Ono, K., Murakami, T., Fujiwara, K., Growth of sialodacryoadenitis viruses in LBC cell cultures (1986) Jpn. J. Vet. Sci., 48, pp. 193-195; Hirano, N., Takamaru, H., Ono, K., Murakami, T., Fujiwara, K., Replication of sialodacryoadenitis virus of rat in LBC cell culture (1986) Arch. Virol., 88, pp. 383-387; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Pathogenesis of sialodacryoadenitis in gnotobiotic rats (1975) Vet. Pathol., 12, pp. 196-209; Kojima, A., Fujinami, F., Doi, K., Yososhima, A., Okaniwa, A., Isolation and properties of sialodacryoadenitis virus of rat (1980) Exp. Anim., 29, pp. 409-418; Machii, K., Iwai, H., Otsuka, Y., Ueda, K., Hirano, N., Reactivities of 4 murine coronavirus antigens with immunized or naturally infected rat sera by enzyme linked immunosorbent assay (1988) Exp. Anim., 37, pp. 251-255; Maru, M., Sato, K., Characterization of a coronavirus isolated from rats with sialoadenitis (1982) Arch. Virol., 73, pp. 33-43; Nakagawa, M., Saito, M., Suzuki, E., Nakayama, K., Matsubara, J., Muto, T., Ten years‐long survey on pathogen status of mouse and rat breeding colonies (1984) Exp. Anim., 33, pp. 115-120; Nunoya, T., Itabashi, M., Kudaou, S., Hayashi, K., Tajima, M., An epizootic sialodacryoadenitis of rats (1977) Jpn. J. Vet. Sci., 39, pp. 445-450; Parker, J.C., Cross, S.S., Rowe, W.P., Rat coronavirus: a prevalent naturally occurring pneumotropic virus of rat (1970) Arch. ges. Virusforsch., 31, pp. 293-302; Percy, D., Bond, S., Macinnes, J., Replication of sialodacryoadenitis virus in mouse L‐2 cells (1989) Arch. Virol., 104, pp. 323-333; Siddel, S.G., Anderson, R., Gabanagh, D., Fujiwara, K., Klenk, H.D., MacNaughton, M.R., Pensaert, M., van der Zeijst, B.A.M., Coronaviridae (1983) Intervirology, 20, pp. 181-189; Utsumi, K., Ishikawa, T., Maeda, T., Shimizu, S., Tatsumi, H., Fujiwara, K., Infectious sialodacryoadenitis and rat breeding (1980) Lab. Anim., 14, pp. 303-307; Utsumi, K., Maeda, T., Tatsumi, H., Fujiwara, K., Some clinical and epizootiological observations of infections sialoadenitis in rats (1978) Exp. Anim., 27, pp. 283-287; Yamaguchi, R., Taguchi, F., Yamada, A., Utsumi, K., Fujiwara, K., Pathogenicity of sialoadacryoadenitis virus for rats after brain passages in suckling mice (1982) Jpn. J. Exp. Med., 52, pp. 45-48","Hirano, N.; Department of Veterinary Microbiology, Iwate University, Morioka, Japan",,,09311793,,,"8553708","English","Zentralbl. Veterinarmed. Reihe B",Article,"Final",Open Access,Scopus,2-s2.0-0029296039
"Giudicelli J., Dubois F., Thouvenot D., Dutruge J., Bellon G.","57197180443;7103346291;7005288678;6603713664;7006333370;","Coronaviry, infections in infant lower respiratory tract diseases, apnea and sudden death? [Infection à coronavirus du nourrison: atteinte des voies aériennes basses, apnée et mort subite?]",1995,"Archives de pediatrie","2","2",,"185","",,1,"10.1016/0929-693X(95)90150-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029246709&doi=10.1016%2f0929-693X%2895%2990150-2&partnerID=40&md5=b7156bf03eb7197f7d23a67c8f331cbb","Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France; laboratoire de virologie des Hospices Civils de Lyon, 8, avenue Rockfelier, 69373 Lyon Cedex, France; centre de réference de la mort subite du nourrisson, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France","Giudicelli, J., Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France; Dubois, F., Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France; Thouvenot, D., laboratoire de virologie des Hospices Civils de Lyon, 8, avenue Rockfelier, 69373 Lyon Cedex, France; Dutruge, J., Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France, centre de réference de la mort subite du nourrisson, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France; Bellon, G., Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France",[No abstract available],,"apnea; human; infant; note; respiratory tract infection; sudden infant death syndrome; virology; virus infection; Apnea; Coronavirus Infections; Human; Infant; Respiratory Tract Infections; Sudden Infant Death","Sizun, Soupre, Legrand, Rôle pathogène des coronavirus en réanimation pédiatrique: analyse rétrospective de 19 prélèvements positifs en immunofluorescence indirecte (1994) Arch Pédiatr, 1, pp. 477-480; Isaacs, Flowers, Clarke, Epidemiology of coronavirus respiratory infections (1983) Archives of Disease in Childhood, 38, pp. 500-503; Mc Intosh, Chao, Krause, Coronavirus infection in acute lower respiratory tract diseases of infants (1974) Journal of Infectious Diseases, 130, pp. 502-507; Williams, Uren, Bretherton, Respiratory viruses and sudden infant death (1984) Br Med J, 288, pp. 1491-1493; Talbot, Jouvenne, Le potentiel neurotrope des coronavirus (1992) Med Sci, 8, pp. 119-125","Giudicelli, J.; Service de pédiatrie, centre hospitalier Lyon Sud, 69310 Pierre-Bénite, Lyon Cedex, France",,,0929693X,,APEDE,"7646659","French","Arch. Pediatr.",Letter,"Final",,Scopus,2-s2.0-0029246709
"Enjuanes L., Sánchez C., Méndez A., Ballesteros M.L.","7006565392;57193985365;7102774464;7006110601;","Tropism and immunoprotection in transmissible gastroenteritis coronaviruses.",1995,"Developments in biological standardization","84",,,"145","152",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029201281&partnerID=40&md5=aceee2080e75c3ccf4385c0f5ddd2fe8","Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain","Enjuanes, L., Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain; Sánchez, C., Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain; Méndez, A., Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain; Ballesteros, M.L., Centro Nacional de Biotecnología, Universidad Autónoma, Madrid, Spain",[No abstract available],,"live vaccine; virus antigen; virus vaccine; animal; animal disease; antibody specificity; article; genetic recombination; genetics; immunology; isolation and purification; pathogenicity; phenotype; standard; swine; swine disease; Transmissible gastroenteritis virus; vaccination; virulence; Animals; Antigens, Viral; Gastroenteritis, Transmissible, of Swine; Organ Specificity; Phenotype; Recombination, Genetic; Swine; Transmissible gastroenteritis virus; Vaccination; Vaccines, Attenuated; Viral Vaccines; Virulence",,"Enjuanes, L.",,,03015149,,,"7796947","English","Dev. Biol. Stand.",Article,"Final",,Scopus,2-s2.0-0029201281
"Enjuanes L., Smerdou C., Sanchez C.M., Sune C., Kelly S., Curtiss III R., Torres J.M.","7006565392;6602856664;57193985365;6701660310;57212985959;7006668153;35516513600;","Induction of transmissible gastroenteritis coronavirus specific immune responses using vectors with enteric tropism",1995,"Advances in Experimental Medicine and Biology","371","B",,"1535","1541",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029149154&partnerID=40&md5=e42a21de097c8e6db67832f30674102e","Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain","Enjuanes, L., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Smerdou, C., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Sanchez, C.M., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Sune, C., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Kelly, S., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Curtiss III, R., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; Torres, J.M., Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain",[No abstract available],,"animal cell; conference paper; coronavirus; gastroenteritis; immune response; immunostimulation; nonhuman; peyer patch; priority journal; virus transmission; Adenoviridae; Amino Acid Sequence; Animal; Antibodies, Viral; Antigens, Viral; Cloning, Molecular; Epitopes; Gastroenteritis, Transmissible, of Swine; Genes, Viral; Genetic Vectors; Hamsters; Immunity, Mucosal; Molecular Sequence Data; Peyer's Patches; Plasmids; Recombinant Proteins; Salmonella typhimurium; Support, Non-U.S. Gov't; Swine; Transmissible gastroenteritis virus; Viral Proteins",,"Enjuanes, L.; Centro Nacional de Biotecnologia, Centro de Biologia Molecular CSIC, Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"7502852","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0029149154
"Kim Y.-N., Makino S.","55699505200;7403067550;","Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal",1995,"Journal of Virology","69","8",,"4963","4971",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029040964&partnerID=40&md5=e86d31c0c0be85c36c79aace9394b776","Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States","Kim, Y.-N., Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States","The mouse hepatitis virus (MHV) sequences required for replication of the JHM strain of MHV defective interfering (DI) RNA consist of three discontinuous genomic regions: about 0.47 kb from both terminal sequences and a 0.13-kb internal region present at about 0.9 kb from the 5' end of the DI genome. In this study, we investigated the role of the internal 0.13-kb region in MHV RNA replication. Overall sequences of the 0.13-kb regions from various MHV strains were similar to each other, with nucleotide substitutions in some strains; MHV-A59 was exceptional, with three nucleotide deletions. Computer-based secondary-structure analysis of the 0.13-kb region in the positive strand revealed that most of the MHV strains formed the same or a similar main stem-loop structure, whereas only MHV-A59 formed a smaller main stem-loop structure. The RNA secondary structures in the negative strands were much less uniform among the MHV strains. A series of DI RNAs that contained MHV-JHM-derived 5'- and 3'-terminal sequences plus internal 0.13- kb regions derived from various MHV strains were constructed. Most of these DI RNAs replicated in MHV-infected cells, except that MRP-A59, with a 0.13- kb region derived from HV-A59, failed to replicate. Interestingly, replication of MRP-A59 was temperature dependent; it occurred at 39.5°C but ont at 37 or 35°C, whereas a DI RNA with an MHV-JHM-derived 0.13-kb region replicated at all three temperatures. At 37°C, synthesis of MRP-A59 negative-strand RNA was detected in MHV-infected and MRP-A59 RNA-transfected cells. Another DI RNA with the internal 0.13-kb region deleted also synthesized negative-strand RNA in MHV-infected cells. MRP-A59-transfected cells were shifted from 39.5 to 37°C at 5.5 h postinfection, a time when most MHV negative-strand RNAs have already accumulated; after the shift, MRP- A59 positive-strand RNA synthesis ceased. The minimum sequence required for maintenance of the positive-strand major stem-loop structure and biological function of the MHV-JHM 0.13-kb region was about 57 nucleotides. Function was lost in the 50-nucleotide sequence that formed a positive-strand stem-loop structure identical to that of MHV-A59. These studies suggested that the RNA structure made by the internal sequence was important for positive-strand MHV RNA synthesis.",,"article; murine hepatitis coronavirus; nonhuman; priority journal; rna replication; rna structure; rna synthesis; signal transduction; virus replication; Amino Acid Sequence; Animal; Base Sequence; Biological Transport; Cell Line; Coronavirus; Mice; Molecular Sequence Data; Nucleic Acid Conformation; RNA, Viral; Sequence Homology, Nucleic Acid; Support, U.S. Gov't, P.H.S.; Virus Replication",,"Makino, S.; Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"7609066","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029040964
"Van der Most R.G., Luytjes W., Rutjes S., Spaan W.J.M.","6701702352;6701683324;8936946300;7007172944;","Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus",1995,"Journal of Virology","69","6",,"3744","3751",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029013594&partnerID=40&md5=9ad6bdfbe81df1efa75536426b532ec7","Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands","Van der Most, R.G., Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands; Luytjes, W., Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands; Rutjes, S., Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands; Spaan, W.J.M., Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands","The defective interferieeeng (DI) RNA MIDI or mouse hepatitis virus strain A59 (MHV-A59) contains a large open reading frame (ORF) spanning almost its entire genome. This ORF consists of sequences derived from ORF1a, ORF1b, and the nucleocapsid gene. We have previously demonstrated that mutations that disrupt the ORF decrease the fitness of MIDI and its derivatives (R. J. de Groot, R. G. van der Most, and W. J. M. Spaan, J. Virol. 66:5898-5905, 1992). To determine whether translation of the ORF per se is required or whether the encoded polypeptide or a specific sequence is involved, we analyzed sets of related DI RNAs containing different ORFs. After partial deletion of ORF1b and nucleocapsid gene sequences, disruption of the remaining ORF is still lethal; translation of the entire ORF is not essential, however. When a large fragment of the MHV-A59 spike gene, which is not present in any of the MHV- A59 DI RNAs identified so far, was inserted in-frame into a MIDI derivative, translation across this sequence was vital to DI RNA survival. Thus, the translated sequence is irrelevant, indicating that translation per se plays a crucial role in DI virus propagation. Next, it was examined during which step of the vital life cycle translation plays its role. Since the requirement for translation also exists in DI RNA-transfected and MHV-infected cells, it follows that either the synthesis or degradation of DI RNAs is affected by translation.",,"virus rna; animal cell; article; gene sequence; mouse; murine hepatitis coronavirus; nonhuman; open reading frame; polyacrylamide gel electrophoresis; priority journal; reverse transcription polymerase chain reaction; rna synthesis; rna translation; virus gene; virus nucleocapsid; Base Sequence; Cell Line; Defective Viruses; Molecular Sequence Data; Murine hepatitis virus; Open Reading Frames; RNA, Viral; Support, Non-U.S. Gov't; Transfection; Translation, Genetic",,"Spaan, W.J.M.; Institute of Medical Microbiology, Faculty of Medicine, Leiden University, 2300 AH Leiden, Netherlands",,,0022538X,,JOVIA,"7745722","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029013594
"Flory E., Stuhler A., Barac-Latas V., Lassmann H., Wege H.","7003965470;6602388166;6506163291;35420677900;7005516649;","Coronavirus-induced encephalomyelitis: Balance between protection and immune pathology depends on the immunization schedule with spike protein S",1995,"Journal of General Virology","76","4",,"873","879",,8,"10.1099/0022-1317-76-4-873","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028965206&doi=10.1099%2f0022-1317-76-4-873&partnerID=40&md5=aa832efb08184b41dc4ebb043f95e852","Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany","Flory, E., Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany; Stuhler, A., Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany; Barac-Latas, V., Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany; Lassmann, H., Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany; Wege, H., Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany","The neurotropic mouse hepatitis virus MHV-JHM induces central nervous system (CNS) demyelination in Lewis rats that pathologically resembles CNS lesions in multiple sclerosis. The mechanisms of MHV-JHM-induced demyelination remain unclear and several studies have implicated the role of the immune response in this process. We have shown previously that protective immunity against MHV-JHM-induced encephalomyelitis was induced by immunization with a vaccinia virus (VV) recombinant expressing MHV-JHM S-protein (VV-S). Here, we present evidence that the time of MHV-JHM challenge after immunization with VV-S plays a critical role in protective immunity. The induction of virus-neutralizing S-protein-specific antibodies prior to the MHV-JHM challenge modulates the disease process and a subacute encephalomyelitis based on a persistent virus infection developed. Typical pathological alterations were lesions of inflammatory demyelination. In addition, the results indicate that after seroconversion, CD8+ T cells were no longer essential for virus elimination in contrast to their role in protection during acute encephalomyelitis.",,"neutralizing antibody; virus protein; animal cell; animal experiment; animal tissue; article; central nervous system infection; controlled study; demyelination; encephalomyelitis; female; immunity; immunization; multiple sclerosis; Murine hepatitis coronavirus; neurotropism; nonhuman; priority journal; rat; seroconversion; Vaccinia virus; virus recombinant; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus",,"Wege, H.; Fed. Res. Ctr. Virus Dis. Animals, Friedrich Loeffler Institutes, D-17498 Insel Riems, Germany",,"Microbiology Society",00221317,,JGVIA,"9049333","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0028965206
"Compton S.R., Winograd D.F., Gaertner D.J.","7102893878;6603149758;7004631465;","Optimization of in vitro growth conditions for enterotropic murine coronavirus strains",1995,"Journal of Virological Methods","52","3",,"301","307",,5,"10.1016/0166-0934(94)00161-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028920214&doi=10.1016%2f0166-0934%2894%2900161-9&partnerID=40&md5=a4b46ec796ddb547b652f3e359b271e5","Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8016, United States","Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8016, United States; Winograd, D.F., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8016, United States; Gaertner, D.J., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8016, United States","Enterotropic mouse hepatitis virus (MHV) strains have been difficult to grow in cell culture. In an attempt to develop an efficient in vitro cultivation system for enterotropic MHV strains (MHV-RI and MHV-Y), 8 murine cell lines were inoculated with MHV-RI- or MHV-Y-infected infant mouse intestinal homogenates and screened for the production of cytopathic effects. MHV-RI and MHV-Y consistently produced cytopathic effects only in J774A.1 cells. Both strains produced titers of 106 TCID50/ml in subsequent passages in J774.1 cells. MHV strains -1, -3, -A59, -JHM, -S and -DVIM also produced high-titer viral stocks in J774A.1 cells. Therefore J774A.1 cells are the first cells found that support the replication of these 8 enterotropic and respiratory MHV strains. After passage in J774A.1 cells, MHV-RI and MHV-Y could infect previously non-susceptible cell lines (17C1-1, CMT-93, N18 and NCTC 1469), though cytopathic effects were often negligible with MHV-RI. MHV-Y, but not MHV-RI, grew in L2(Percy) cells. Using L2(Percy) cells, an agarose overlay and Giemsa staining, MHV-Y could be quantified by plaque assay. Infant mouse bioassays, plaque assays and cell culture infections were compared for their sensitivity in detecting MHV-Y in infected intestinal homogenates and cell supernatants. © 1995.","Enterotropism; J774A.1 cell; Mouse hepatitis virus strain RI and Y; Murine coronavirus; Plaque assay","article; controlled study; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virus culture; virus replication; Animal; Cell Line; Coronavirus Infections; Cytopathogenic Effect, Viral; Enteritis; Intestines; Mice; Murine hepatitis virus; Support, U.S. Gov't, P.H.S.; Virus Cultivation; Coronavirus; Murinae; Murine hepatitis virus","Barthold, Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, pp. 571-601. , P.N. Bhatt, R.O. Jacoby, Academic Press, New York; Barthold, Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab. Anim. Sci., 37, pp. 36-40; Barthold, Smith, Lord, Bhatt, Jacoby, Main, Epizootic coronaviral typhlocolitis in suckling mice (1982) Lab. Anim. Sci., 32, pp. 376-383; Barthold, Smith, Povar, Enterotropic mouse hepatitis virus infection in nude mice (1985) Lab. Anim. Sci., 35, pp. 613-618; Barthold, Beck, Smith, Enterotropic coronavirus (mouse hepatitis virus) in mice: influence of host age and strain on infection and disease (1993) Lab. Anim. Sci., 43, pp. 276-284; Casebolt, Stephensen, Monoclonal antibody solution hybridization assay for detection of mouse hepatitis virus infection (1992) J. Clin. Microbiol., 30, pp. 608-612; Compton, Barthold, Smith, The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Gaertner, Winograd, Compton, Paturzo, Smith, Development and optimization of plaque assays for rat coronaviruses (1993) J. Virol. Methods, 43, pp. 53-64; Homberger, Smith, Barthold, Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Kunita, Terada, Goto, Kagiyama, Sequence analysis and molecular detection of mouse hepatitis virus using the polymerase chain reaction (1992) Lab. Anim. Sci., 42, pp. 593-598; Lucas, Flintoff, Anderson, Percy, Coulter, Dales, In vivo and in vitro models of demyelinating diseases: tropism of JHM strain of murine hepatitis virus for cells of glial origin (1977) Cell, 12, pp. 553-560; Reed, Muench, A simple method of estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Yamada, Yabe, Yamada, Taguchi, Detection of mouse hepatitis virus by the polymerase chain reaction and its application to the rapid diagnosis of infection (1993) Lab. Anim. Sci., 43, pp. 285-290","Compton, S.R.; Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT 06520-8016, United States",,,01660934,,JVMED,"7601904","English","J. Virol. Methods",Article,"Final",,Scopus,2-s2.0-0028920214
"Kyongmin Hwang Kim, Makino S.","7409773761;7403067550;","Two murine coronavirus genes suffice for viral RNA synthesis",1995,"Journal of Virology","69","4",,"2313","2321",,14,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028907967&partnerID=40&md5=8ed1630175fe551f520ee0c4c9bb4d41","Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States","Kyongmin Hwang Kim, Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States","We identified two mouse hepatitis virus (MHV) genes that suffice for MHV RNA synthesis by using an MHV-JHM-derived defective interfering (DI) RNA, DIssA. DIssA is a naturally occurring self-replicating DI RNA with nearly intact genes 1 and 7. DIssA interferes with most MHV-JHM-specific RNA synthesis, except for synthesis of mRNA 7, which encodes N protein; mRNA 7 synthesis is not inhibited by DIssA. Coinfection of MHV-JHM containing DIssA DI particles and an MHV-A59 RNA temperature-sensitive mutant followed by subsequent passage of virus at the permissive temperature resulted in elimination of most of the MHV-JHM helper virus. Analysis of intracellular RNAs at the nonpermissive temperature demonstrated efficient synthesis of DIssA and mRNA 7 but not of the helper virus mRNAs. Oligonucleotide fingerprinting analysis demonstrated that the structure of mRNA 7 was MHV- JHM specific and therefore must have been synthesized from the DIssA template RNA. Sequence analysis revealed that DIssA lacks a slightly heterogeneous sequence, which is found in wild-type MHV from the 3' one-third of gene 2-1 to the 3' end of gene 6. Northern (RNA) blot analysis of intracellular RNA species and virus-specific protein analysis confirmed the sequence data. Replication and transcription of another MHV DI RNA were supported in DIssA- replicating cells. Because the products of genes 2 and 2-1 are not essential for MHV replication, we concluded that expression of gene I proteins and N protein was sufficient for MHV RNA replication and transcription.",,"virus rna; animal cell; article; coronavirus; dna fingerprinting; gene expression regulation; helper virus; mouse; murine hepatitis coronavirus; nonhuman; priority journal; rna synthesis; sequence homology; temperature sensitive mutant; virus replication; Animal; Base Sequence; Cell Division; Cell Line; DNA, Complementary; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Neoplasm Proteins; RNA, Messenger; RNA, Viral; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Virus Replication",,"Makino, S.; Department of Microbiology, University of Texas, 24th at Speedway, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"7884877","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028907967
"Liu D.X., Tibbles K.W., Cavanagh D., Brown T.D.K., Brierley I.","8972667300;6507790687;26642890500;56248391000;7004639098;","Involvement of viral and cellular factors in processing of polyprotein encoded by ORF1a of the coronavirus IBV",1995,"Advances in Experimental Medicine and Biology","380",,,"413","421",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028880569&partnerID=40&md5=9d6ad0dc6dfd125a3aec2bd9636855a0","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom","Liu, D.X., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Tibbles, K.W., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Cavanagh, D., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",[No abstract available],,"gene product; messenger rna; protein; rna; animal cell; avian infectious bronchitis virus; conference paper; nonhuman; open reading frame; priority journal; vero cell; Animal; Cercopithecus aethiops; Genome, Viral; Infectious bronchitis virus; Molecular Weight; Open Reading Frames; Rabbits; Recombinant Fusion Proteins; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Translation, Genetic; Vero Cells; Viral Proteins",,"Liu, D.X.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",,,00652598,,AEMBA,"8830517","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028880569
"Liu D.X., Brierley I., Brown T.D.K.","8972667300;7004639098;56248391000;","Identification of a trypsin-like serine proteinase domain encoded by ORF 1a of the coronavirus IBV",1995,"Advances in Experimental Medicine and Biology","380",,,"405","411",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028872076&partnerID=40&md5=99685d348007f7e96956ccf892f521d7","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom","Liu, D.X., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",[No abstract available],,"polypeptide; serine proteinase; trypsin; animal cell; avian infectious bronchitis virus; conference paper; immunoprecipitation; mutation; nonhuman; open reading frame; picornavirus; priority journal; vero cell; Amino Acid Sequence; Animal; Cercopithecus aethiops; DNA Mutational Analysis; Electrophoresis, Polyacrylamide Gel; Gene Expression; Infectious bronchitis virus; Molecular Sequence Data; Molecular Weight; Open Reading Frames; Plasmids; Recombinant Proteins; Sequence Deletion; Serine Endopeptidases; Support, Non-U.S. Gov't; Transfection; Trypsin; Vero Cells; Viral Proteins",,"Liu, D.X.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",,,00652598,,AEMBA,"8830516","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028872076
"Denison M.R., Kim J.C., Ross T.","7101971810;7601384560;57212517856;","Inhibition of coronavirus MHV-A59 replication by proteinase inhibitors",1995,"Advances in Experimental Medicine and Biology","380",,,"391","397",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028865888&partnerID=40&md5=411d8f13a1bab9584b132c3636365734","Department of Pediatrics, E. B Lamb Pediatric Research Center, Vanderbilt University Medical School, Nashville, TN 37232-2581, United States","Denison, M.R., Department of Pediatrics, E. B Lamb Pediatric Research Center, Vanderbilt University Medical School, Nashville, TN 37232-2581, United States; Kim, J.C., Department of Pediatrics, E. B Lamb Pediatric Research Center, Vanderbilt University Medical School, Nashville, TN 37232-2581, United States; Ross, T., Department of Pediatrics, E. B Lamb Pediatric Research Center, Vanderbilt University Medical School, Nashville, TN 37232-2581, United States",[No abstract available],,"leupeptin; proteinase inhibitor; virus rna; animal cell; cell division; conference paper; controlled study; coronavirus; mouse; nonhuman; priority journal; protein degradation; rna synthesis; virus replication; Animal; Cell Line; Giant Cells; Kinetics; Leupeptins; Mice; Murine hepatitis virus; Plaque Assay; Protease Inhibitors; RNA Replicase; RNA, Viral; Support, U.S. Gov't, P.H.S.; Time Factors; Uridine; Virus Replication",,"Denison, M.R.; Department of Pediatrics, E. B Lamb Pediatric Research Center, Vanderbilt University Medical School, Nashville, TN 37232-2581, United States",,,00652598,,AEMBA,"8830514","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028865888
"Kyongmin Hwang Kim, Makino S.","7409773761;7403067550;","Expression of murine coronavirus genes 1 and 7 is sufficient for viral RNA synthesis",1995,"Advances in Experimental Medicine and Biology","380",,,"479","484",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028863331&partnerID=40&md5=a07c99ef28ce564d785795ac87c1e707","Department of Microbiology, University of Texas, Austin, TX, United States","Kyongmin Hwang Kim, Department of Microbiology, University of Texas, Austin, TX, United States; Makino, S., Department of Microbiology, University of Texas, Austin, TX, United States",[No abstract available],,"gene product; virus rna; agar gel electrophoresis; conference paper; coronavirus; gene expression; nonhuman; northern blotting; priority journal; reverse transcription polymerase chain reaction; rna replication; rna synthesis; rna transcription; virus gene; Animal; Base Sequence; Cell Line; Cloning, Molecular; Defective Viruses; DNA Primers; Electrophoresis, Agar Gel; Gene Expression; Genes, Viral; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Messenger; RNA, Viral; Support, U.S. Gov't, P.H.S.; Transcription, Genetic; Virus Replication",,"Kim, K.H.; Department of Microbiology, University of Texas, Austin, TX, United States",,,00652598,,AEMBA,"8830527","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028863331
"Sun N., Perlman S.","57214909902;7102708317;","Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes",1995,"Journal of Virology","69","2",,"633","641",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028852336&partnerID=40&md5=fe7755a65f4a54337da4b7925486eaf2","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Sun, N., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Mouse hepatitis virus strain JHM (MHV-JHM) causes a chronic encephalomyelitis in susceptible mice, with histological evidence of demyelination in the spinal cord. After intranasal inoculation, virus spreads retrogradely to several brain structures along neuroanatomic projections to the main olfactory bulb. In the absence of experimental intervention, mice become moribund before the spinal cord is infected. In this study, infusions of anti-MHV neutralizing monoclonal antibodies were administered to protect mice from the MHV-JHM-induced acute encephalitis and to allow survival until virus spread to the spinal cord. Under these conditions, virus was observed to enter specific layers (primarily laminae V to VII) in the gray matter of the upper spinal cord, consistent with transneuronal spread. While the brain structures which are the sources for virus spread to the spinal cord cannot be determined with certainty, the ventral reticular nucleus is likely to be important since it is consistently and extensively labeled in all mice and receives projections from subsequently infected areas of the spinal cord. After initial entry into the gray matter, virus rapidly spread to the white matter of the spinal cord. During the early stages of this process, extensive infection of astrocytes was noted, suggesting that cell-to-cell spread via these glial cells is an important part of this process. Reports from other laboratories using cultured cells strongly suggested that astrocytes serve as important regulators of oligodendrocyte function and, by extrapolation, have a major role in vivo in the processes of both demyelination and remyelination. Thus, our results not only outline the probable pathway used by MHV-JHM to infect the white matter of the spinal cord but also, with the assumption that infection of astrocytes leads to subsequent dysfunction, raise the possibility that infection of these cells contributes to the demyelinating process.",,"animal cell; article; astrocyte; coronavirus; demyelination; gray matter; lateral reticular nucleus; mouse; nerve cell; nonhuman; olfactory bulb; oligodendroglia; priority journal; remyelinization; spinal cord infection; virus transmission; white matter; Animal; Antibodies, Monoclonal; Astrocytes; Demyelinating Diseases; Mice; Murine hepatitis virus; Neurons; Spinal Cord; Support, U.S. Gov't, P.H.S.",,"Perlman, S.; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States",,,0022538X,,JOVIA,"7815526","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028852336
"Collins A.R.","24439435400;","Identification of 120 kD and 30 kD receptors for human coronavirus OC43 in cell membrane preparations from newborn mouse brain",1995,"Advances in Experimental Medicine and Biology","380",,,"387","390",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028845035&partnerID=40&md5=381d15b11f241fea0d5ba8ef9238d51b","Department of Microbiology, State University of New York, Buffalo, NY, United States","Collins, A.R., Department of Microbiology, State University of New York, Buffalo, NY, United States","A biotinylated virus overlay was used to identify a 120kD virus-binding molecule in dissociated newborn mouse brain (nmb) cell suspensions after separation of the proteins by polyacrylamide gel electrophoresis, electroblotting, and blockage of non-specific binding sites. The virus- binding molecule was not detected in adult mouse brain cell suspensions. Mannose- and glucose-rich glycoproteins from nmb cell membranes were selected by ConA-Sepharose (Pharmacia) chromatography. A 30kD virus-binding molecule was eluted by 0.2 M alpha-methyl-D-mannoside. O-linked sialic acid, a receptor component, was identified in the eluate.",,"alpha methyl mannoside; glucose; glycoprotein; mannose; receptor; sialic acid; animal cell; animal tissue; brain; cell membrane; chromatography; conference paper; coronavirus; immunoblotting; mouse; newborn; nonhuman; polyacrylamide gel electrophoresis; priority journal; Aging; Animal; Animals, Newborn; Brain; Cell Membrane; Chromatography, Affinity; Coronavirus; Coronavirus OC43, Human; Electrophoresis, Polyacrylamide Gel; Human; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Molecular Weight; Receptors, Virus",,"Collins, A.R.; Department of Microbiology, State University of New York, Buffalo, NY, United States",,,00652598,,AEMBA,"8830513","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028845035
"Lai M.M.C.","7401808497;","Transcription, replication, recombination, and engineering of coronavirus genes",1995,"Advances in Experimental Medicine and Biology","380",,,"463","471",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028826479&partnerID=40&md5=be15cab1db5e23362e94fb5e5f8c2cc9","Department of Molecular Microbiology, Howard Hughes Medical Institute, So. California Univ. School of Med., Los Angeles, CA 90033, United States","Lai, M.M.C., Department of Molecular Microbiology, Howard Hughes Medical Institute, So. California Univ. School of Med., Los Angeles, CA 90033, United States",[No abstract available],,"messenger rna; recombinant rna; rna polymerase; virus rna; conference paper; coronavirus; gene replication; genetic engineering; genetic recombination; genetic transcription; model; nonhuman; priority journal; rna replication; rna synthesis; rna transcription; virion; virus gene; Coronavirus; Genes, Viral; Genetic Engineering; Genome, Viral; Recombination, Genetic; Replicon; RNA, Messenger; RNA, Viral; Transcription, Genetic; Virus Replication",,"Lai, M.M.C.; Department of Molecular Microbiology, Howard Hughes Medical Institute, So. California Univ. School of Med., Los Angeles, CA 90033, United States",,,00652598,,AEMBA,"8830525","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028826479
"Sun N., Grzybicki D., Castro R.F., Murphy S., Perlman S.","57214909902;6701765174;7202082372;35514979400;7102708317;","Activation of Astrocytes in the Spinal Cord of Mice Chronically Infected with a Neurotropic Coronavirus",1995,"Virology","213","2", 70021,"482","493",,97,"10.1006/viro.1995.0021","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028826296&doi=10.1006%2fviro.1995.0021&partnerID=40&md5=194fa05eaeb37e449a843a68901d5bc7","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Pathology, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pharmacology, University of Iowa, Iowa City, IA 52242, United States","Sun, N., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Grzybicki, D., Department of Pathology, University of Iowa, Iowa City, IA 52242, United States; Castro, R.F., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Murphy, S., Department of Pharmacology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States","Mice infected with the neurotropic JHM strain of mouse hepatitis virus (MHV-JHM) develop a demyelinating encephalomyelitis several weeks after infection. Astrogliosis and infiltration of inflammatory cells are prominent findings in the brains and spinal cords of infected mice. In this report, astrocytes in infected spinal cords were analyzed for expression of three pleiotropic cytokines, TNF-α, IL-1β, and IL-6; Type 2 nitric oxide synthase (iNOS); and MHC class I and II antigen. The data show that all three cytokines and iNOS are expressed by astrocytes in chronically infected spinal cords. These activated astrocytes are localized to areas of virus infection and demyelination, although most of the astrocytes expressing these proteins are not MHV-infected. MHC class I and II antigen can be detected in these spinal cords as well, but not in cells with the typical morphology of astrocytes. TNF-α, IL-6, and iNOS are also evident in the brains of mice with MHV-induced acute encephalitis, but in marked contrast to the results obtained with the chronically infected mice, most of the cells expressing these cytokines or iNOS had the morphology of macrophages or other mononuclear cells and very few appeared to be astrocytes. Additionally, astrocytes and, most likely, oligodendrocytes are infected in the spinal cords of mice with chronic demyelination. These results are consistent with a role for both viral infection of glial cells and high localized levels of proinflammatory cytokines and nitric oxide in the demyelinating process in mice infected with MHV-JHM. They also show that analogously to the human demyelinating disease, multiple sclerosis, astrocytes are a major cellular source for these cytokines in mice with chronic, but not acute disease. © 1995 Academic Press, Inc.",,"cytokine; animal cell; animal experiment; article; astrocyte; cell activity; controlled study; coronavirus; demyelination; glia cell; mouse; nonhuman; priority journal; spinal cord; Acute Disease; Animal; Astrocytes; Brain; Chronic Disease; Coronavirus Infections; Cytokines; Demyelinating Diseases; Encephalomyelitis; Histocompatibility Antigens; Histocompatibility Antigens Class I; Histocompatibility Antigens Class II; Interleukin-1; Interleukin-6; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Nitric-Oxide Synthase; Oligodendroglia; Specific Pathogen-Free Organisms; Spinal Cord; Support, U.S. Gov't, P.H.S.; Tumor Necrosis Factor","Akira, S., Taga, T., Kishimoto, T., Interleukin-6 in biology and medicine (1993) Adv. Immunol, 54, pp. 1-78; Bo, L., Dawson, T., Wesselingh, S., Mork, S., Choi, S., Kong, P.A., Hanley, D., Trapp, B.D., Induction of nitric oxide synthase in demyelinating regions of multiple sclerosis brains (1994) Ann. Neurol, 36, pp. 778-786; Bo, L., Mork, S., Kong, P., Nyland, H., Pardo, C., Trapp, B.D., Detection of MHC class Il-antigens on macrophages and microglia, but not on astrocytes and endothelia in active multiple sclerosis lesions (1994) J. Neuroimmunol, 51, pp. 135-146; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (Strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Campbell, I., Samimi, A., Chiang, C.-S., Expression of the inducible nitric oxide synthase. Correlation with neuropathology and clinical features in mice with lymphocytic choriomeningitis (1994) J. Immunol, 153, pp. 3622-3629; Castro, R.F., Evans, G.D., Jaszewski, A., Perlman, S., Coro-navirus-induced demyelination occurs in the presence of virus-specific cytotoxic T cells (1994) Virology, 200, pp. 733-743; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol, 59, pp. 463-471; Eddleston, M., Mucke, L., Molecular profile of reactive astrocytes — Implications for their role in neurologic disease (1993) Neuroscience, 54, pp. 15-36; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., Monoclonal antibodies to the matrix (E1) glycoprotein of mouse hepatitis virus protect mice from encephalitis (1989) Virology, 168, pp. 162-167; Gard, A.L., Astrocyte-oligodendrocyte interactions (1993) Astrocytes: Pharmacology and Function, pp. 331-354. , S. 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USA, 75, pp. 4033-4036; Hatten, M., Liem, R., Shelanski, M., Mason, C., Astroglia in CNS injury (1991) Glia, 4, pp. 233-243; Hauser, S., Doolittle, T., Lincoln, R., Brown, R.H., Dinarello, C.A., Cytokine accumulations in CSF of multiple sclerosis patients: Frequent detection of interleukin-1 and tumor necrosis factor but not interleukin-6 (1990) Neurology, 40, pp. 1735-1739; Hofman, F.M., Hinton, D.R., Johnson, K., Merill, J.E., Tumor necrosis factor identified in multiple sclerosis brain (1989) J. Exp. Med, 170, pp. 607-612; Joseph, J., Knobler, R., Lublin, F., Hart, M., Regulation of MHC class I and II antigens on cerebral endothelial cells and astrocytes following MHV-4 infection (1990) Adv. Exp. Med. Biol, 279, pp. 579-591; Ken-Ichi, A., Lee, F., Miyajima, A., Shoichiro, M., Arai, N., Yokota, T., Cytokines: Coordinators of immune and inflammatory responses (1990) Annu. Rev. Biochem, 59, pp. 783-836; Knobler, R.L., Dubois-Dalcq, M., Haspel, M.V., Claysmith, A.P., Lamp-Ert, P.W., Oldstone, M.B.A., Selective localization of wild type and mutant mouse hepatitis (JHM strain) antigens in CNS tissue by fluorescence, light and electron microscopy (1981) J. Neuroimmunol, 1, pp. 81-92; Korner, H., Schliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S., Wege, H., Nucleocapsid or spike protein-specific CD4+ T lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CD8+ T cells (1991) J. Immunol, 147, pp. 2317-2323; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol, 1, pp. 273-280; Lampert, P.W., Sims, J.K., Kniazeff, A.J., Mechanism of demyelination in JHM virus encephalomyelitis (1973) Acta Neuropathol, 24, pp. 76-85; Lavi, E., Suzumura, A., Hirayama, M., Highkin, M.K., Dambach, D., Silberberg, D.H., Weiss, S.R., Coronavirus mouse hepatitis virus (MHV)-A59 causes a persistent productive infection in primary glial cell cultures (1987) Microb. Pathog, 3, pp. 79-86; Lee, S.C., Moore, G.R.W., Golenswsky, G., Raine, C.S., Multiple sclerosis: A role for astroglia in active demyelination suggested by class II MHC expression and ultrastructural study (1990) J. Neu-Ropathol. Exp. Neurol, 49, pp. 122-136; Lieberman, A.P., Pitha, P., Shin, H., Shin, M., Production of tumor necrosis factor and other cytokines by astrocytes stimulated with lipopolysaccaride or a neurotropic virus (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 6348-6352; Lipton, S.A., Gendelman, H.E., Dementia associated with the acquired immunodeficiency syndrome (1995) New Engl. J. Med, 332, pp. 934-940; Lipton, H.L., Twaddle, G., Jelachich, M.L., The predominant virus antigen burden is present in macrophages in Theiler's murine encephalomyelitis virus-induced demyelinating disease (1995) J. Virol, 69, pp. 2525-2533; Massa, P.T., Wege, H., Ter Meulen, V., Analysis of murine hepatitis virus (JHM strain) tropism toward Lewis rat glial cells (1986) In Vitro. Lab. Invest, 55, pp. 318-327; Matsumoto, Y., Fujiwara, M., In situ detection of class I and II major histocompatibility complex antigens in the rat central nervous system during experimental allergic encephalomyelitis. An immuno-histochemical study (1986) J. Neuroimmunol, 12, pp. 265-277; Merrill, J.E., Ignarro, L.J., Sherman, M.P., Melinek, J., Lane, T.E., Microglial cell cytotoxicity of oligodendrocytes is mediated through nitric oxide (1993) J. Immunol, 151, pp. 2132-2141; Morganti-Kossman, M.C., Kossman, T., Wahl, S.M., Cytokines and neuropathology (1992) Trends Neurosci, 13, pp. 286-291; Murphy, S., Simmons, M.L., Agullo, L., Garcia, A., Feinstin, D.L., Galea, E., Reis, D.J., Schwartz, J.P., Synthesis of nitric oxide in CNS glial cells (1993) Trends Neurosci, 16, pp. 323-328; Nagano, I., Nakamura, S., Yoshioka, M., Onodera, J., Kogure, K., Itoyama, Y., Expression of cytokines in brain lesions in subacute sclerosing panencephalitis (1994) Neurology, 44, pp. 710-715; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of monoclonal antibodies on lethal mouse hepatitis virus infection in mice (1986) J. Virol, 59, pp. 168-171; Pasick, J., Dales, S., Infection by coronavirus JHM of rat neurons and oligodendrocytes-Type-2 astrocyte lineage cells during distinct developmental stages (1991) J. Virol, 65, pp. 5013-5028; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol, 68, pp. 5483-5495; Perlman, S., Ries, D., The astrocyte is a target cell in mice persistently infected with mouse hepatitis virus, strain JHM (1987) Microb. Pathog, 3, pp. 309-314; Perlman, S., Evans, G., Afifi, A., Effect of olfactory bulb ablation on spread of a neurotropic coronavirus into the mouse brain (1990) J. Exp. Med, 172, pp. 1127-1132; Perlman, S., Jacobsen, G., Moore, S., Regional localization of virus in the central nervous system of mice persistently infected with murine coronavirus JHM (1988) Virology, 166, pp. 328-338; Perlman, S., Jacobsen, G., Olson, A.L., Afifi, A., Identification of the spinal cord as a major site of persistence during chronic infection with a murine coronavirus (1990) Virology, 175, pp. 418-426; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating encephalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog, 2, pp. 185-194; Powell, H.C., Lampert, P.W., Oligodendrocytes and their myelin-plasma membrane connections in JHM mouse hepatitis virus encephalomyelitis (1975) Lab. Invest, 33, pp. 440-445; Raine, C.S., Multiple sclerosis: Immune system molecule expression in the central nervous system (1994) J. Neuropathol. Exp. Neurol, 53, pp. 328-337; Renno, T., Krakowski, M., Piccirillo, C., Lin, J.-Y., Owens, T., TNF-a expression by resident microglia and infiltrating leukocytes in the central nervous system of mice with experimental allergic encephalomyelitis (1995) J. Immunol, 154, pp. 339-346; Selmaj, K., Raine, C.S., Tumor necrosis factor mediates myelin and oligodendrocyte damage in vitro (1988) Ann. Neurol, 23, pp. 339-346; Selmaj, K., Raine, C.S., Cannella, B., Brosnan, C., Identification of lymphotoxin and tumor necrosis factor in multiple sclerosis lesions (1991) J. Clin. Invest, 87, pp. 949-954; Simmons, M.L., Murphy, S., Induction of nitric oxide synthase in glial cells (1992) J. Neurochem, 59, pp. 897-905; Stohlman, S.A., Bergmann, C.C., Van Der Veen, R.C., Hinton, D.R., Mouse hepatitis virus-specific cytotoxic T lymphocytes protect from lethal infection without eliminating virus from the central nervous system (1995) J. Virol, 69, pp. 684-694; Stohlman, S.A., Hinton, D.R., Cua, D., Dimacali, E., Sensintaffar, J., Hofman, F.M., Tahara, S.M., Yao, Q., Tumor necrosis factor expression during mouse hepatitis virus-induced demyelinat-ing encephalomyelitis (1995) J. Virol, 69, pp. 5898-5903; Stohlman, S.A., Matsushima, G.K., Casteel, N., Weiner, L.P., In vivo effects of coronavirus-specific T cell clones: DTH inducer cells prevent a lethal infection but do not inhibit virus replication (1986) J. Immunol, 136, pp. 3052-3056; Sun, N., Perlman, S., Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes (1995) J. Virol, 69, pp. 633-641; Suzumura, A., Lavi, E., Weiss, S.R., Silberberg, D.H., Coro-navirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes (1986) Science, 232, pp. 991-993; Tracey, K.J., Cerami, A., Tumor necrosis factor, other cytokines and disease (1993) Annu. Rev. Cell Biol, 9, pp. 317-343; Van Berlo, M., Warringa, R., Wolswijk, G., Lopes-Cardozo, M., Vulnerability of rat and mouse brain cells in murine hepatitis virus (JHM-strain): Studies in vivo and in vitro (1989) Glia, 2, pp. 85-93; Vass, K., Lassmann, H., Wekerle, H., Wisnioski, H.M., The distribution of Ia antigen in the lesions of rat acute experimental allergic encephalomyelitis (1986) Acta Neurophathol. (Berlin), 70, pp. 149-160; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol, 30, pp. 31-41; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol, 28, pp. 298-303; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. Neuroimmunol, 32, pp. 1-9; Yong, V.W., Antel, J.P., Major histocompatibility complex molecules on glial cells (1992) Semin. Neurosci, 4, pp. 231-240; Zheng, Y., Schafer, M., Weihe, E., Sheng, H., Corisdeo, S., Fu, Z.F., Koprowski, H., Dietzschold, B., Severity of neurological signs and degree of inflammatory lesions in the brains of rats with Borna disease correlate with the induction of nitric oxide synthase (1993) J. Virol, 67, pp. 5786-5791","Perlman, S.; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States",,,00426822,,,"7491773","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028826296
"Castro R.F., Perlman S.","7202082372;7102708317;","CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity",1995,"Journal of Virology","69","12",,"8127","8131",,91,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028824901&partnerID=40&md5=b17daaf955f8ba9c24e26f5f87004cf6","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Castro, R.F., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","CD8+ T cells with cytotoxic activity against the surface glycoprotein (S) of mouse hepatitis virus, strain JHM, have been identified in the central nervous system (CNS) of both acutely and chronically infected C57BL/6 mice. In this report, two specific epitopes recognized by these CNS-derived cells were identified, using a panel of peptides chosen because they conformed to the allele-specific binding motif for MHC class I H-2Kb and H-2Db. The active peptides encompassed residues 510 to 518 (CSLWNGPHL, H-2Db) and 598 to 605 (RCQIFANI, H-2Kb). Both epitopes are located within the region of the S protein previously shown to be prone to deletion after passage in animals. These deleted strains are generally less neurovirulent than the wild-type virus but still are able to cause demyelination. Since C57BL/6 mice become persistently infected more commonly than many other strains of mice, these data are consistent with a role for CD8+ T-cell escape mutants in the pathogenesis of the demyelinating disease. This is the first report of CD8+ T-cell epitope localization within the S protein, the protein most strongly implicated thus far in pathogenesis in the host.",,"cd8 antigen; major histocompatibility antigen class 1; virus glycoprotein; animal cell; animal model; antigen expression; antigen recognition; article; cytotoxicity; demyelination; mouse; murine hepatitis coronavirus; neurotropism; nonhuman; priority journal; protein localization; strain difference; t lymphocyte; virus pathogenesis; Amino Acid Sequence; Animal; Base Sequence; Brain; CD8-Positive T-Lymphocytes; Coronavirus Infections; Cytotoxicity, Immunologic; DNA Primers; DNA, Viral; Epitopes; Genes, Viral; H-2 Antigens; Major Histocompatibility Complex; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Polymerase Chain Reaction; Sequence Deletion; Support, U.S. Gov't, P.H.S.; Viral Structural Proteins",,"Perlman, S.; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States",,,0022538X,,JOVIA,"7494335","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028824901
"Mendez A., Smerdou C., Gebauer F., Izeta A., Enjuanes L.","7102774464;6602856664;7004526580;6602523425;7006565392;","Structure and encapsidation of transmissible gastroenteritis coronavirus (TGEV) defective interfering genomes",1995,"Advances in Experimental Medicine and Biology","380",,,"583","589",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028822558&partnerID=40&md5=2bc77c05b64d7058227966b2de27eb6c","Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain","Mendez, A., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Smerdou, C., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Gebauer, F., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Izeta, A., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain; Enjuanes, L., Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain","Serial undiluted passages were performed with the PUR46 strain of TGEV in swine testis (ST) cells. Total cellular RNA was analyzed at different passages after orthophosphate metabolic labeling. Three new defective RNA species of 24, 10.5, and 9.5 kb (DI-A, DI-B, and DI-C respectively) were detected at passage 30, which were highly stable and significantly interfered with helper mRNA synthesis in subsequent passages. By Northern hybridization DIs A, B, and C were detected in purified virions at amounts similar to those of helper RNA. Standard and defective TGEV virions could be sorted in sucrose gradients, indicating that defective and full-length genomes are independently packaged. cDNA synthesis of DI-B and DI-C RNAs was performed by the reverse transcription-polymerase chain reaction (RT-PCR) to give four fragments in each case. Cloning and sequencing of the DI-C PCR products showed that the smallest DI particle comprises 9.5 kb and has 4 discontinuous regions of the genome. It contains 2.1 kb from the 5'-end of the genome, about 7 kb from gene 1b, the first 24 nucleotides of the S gene, 12 nucleotides of ORF 7, and the 0.4 kb of the UTR at the 3'-end.",,"virus rna; animal cell; conference paper; coronavirus; male; messenger rna synthesis; molecular cloning; nonhuman; priority journal; sequence analysis; swine; virus capsid; virus gene; virus purification; Animal; Capsid; Cells, Cultured; Defective Viruses; DNA, Complementary; Genome, Viral; Male; Polymerase Chain Reaction; RNA, Viral; Support, Non-U.S. Gov't; Swine; Testis; Transmissible gastroenteritis virus",,"Mendez, A.; Dept. of Molecular/Cellular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco, Madrid 28049, Spain",,,00652598,,AEMBA,"8830546","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028822558
"Baric R.S., Fu K., Chen W., Yount B.","7004350435;16189515400;55574216615;6603564156;","High recombination and mutation rates in mouse hepatitis virus suggest that coronaviruses may be potentially important emerging viruses",1995,"Advances in Experimental Medicine and Biology","380",,,"571","576",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028822557&partnerID=40&md5=4f50dbdc65361f936fe9e32d7d848e95","Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Baric, R.S., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Fu, K., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Chen, W., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Yount, B., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States",[No abstract available],,"allele; animal cell; common cold; conference paper; coronavirus; gastrointestinal infection; genetic recombination; hamster; lower respiratory tract infection; murine hepatitis coronavirus; mutation rate; nonhuman; priority journal; temperature sensitive mutant; virogenesis; virus gene; virus isolation; Alleles; Animal; Cell Line; Comparative Study; DNA-Directed RNA Polymerases; Genome, Viral; Hamsters; Kinetics; Mice; Murine hepatitis virus; Mutation; Recombination, Genetic; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Temperature; Virus Replication",,"Baric, R.S.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States",,,00652598,,AEMBA,"8830544","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028822557
"Hughes S.A., Bonilla P.J., Weiss S.R.","22956252200;7004225518;57203567044;","Identification of the murine coronavirus p28 cleavage site",1995,"Journal of Virology","69","2",,"809","813",,48,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028813105&partnerID=40&md5=c31e187cc325d29da8bd53d8d7ffc268","Department of Microbiology, 319 Johnson Pavilion, Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6076, United States","Hughes, S.A., Department of Microbiology, 319 Johnson Pavilion, Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6076, United States; Bonilla, P.J., Department of Microbiology, 319 Johnson Pavilion, Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, 319 Johnson Pavilion, Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6076, United States","Mouse hepatitis virus strain A59 encodes a papain-like cysteine proteinase (PLP-1) that, during translation of ORF1a, cleaves p28 from the amino terminus of the growing polypeptide chain. In order to determine the amino acid sequences surrounding the p28 cleavage site, the first 4.6 kb of murine hepatitis virus strain A59 ORF1a was expressed in a cell-free transcription- translation system. Amino-terminal radiosequencing of the resulting downstream cleavage product demonstrated that cleavage occurs between Gly- 247 and Val-248. Site-directed mutagenesis of amino acids surrounding the p28 cleavage site revealed that substitutions of Arg-246 (P2) and Gly-247 (P1) nearly eliminated cleavage of p28. Single-amino-acid substitutions of other residues between P7 and P2' were generally permissive for cleavage, although a few changes did greatly reduce proteolysis. The relationship between the p28 cleavage site and other viral and cellular papain proteinase cleavage sites is discussed.",,"amino acid substitution; article; binding site; cell free system; coronavirus; enzyme activity; nonhuman; priority journal; protein degradation; rna cleavage; site directed mutagenesis; translation regulation; virus genome; virus strain; Amino Acid Sequence; Animal; Mice; Molecular Sequence Data; Murine hepatitis virus; Papain; Sequence Alignment; Structure-Activity Relationship; Support, U.S. Gov't, P.H.S.; Viral Proteins",,"Weiss, S.R.; Department of Microbiology, 319 Johnson Pavilion, Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6076, United States",,,0022538X,,JOVIA,"7815547","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028813105
"Lavi E., Wang Q.","7006986911;16044062200;","The protective role of cytotoxic T cells and interferon against coronavirus invasion of the brain",1995,"Advances in Experimental Medicine and Biology","380",,,"145","149",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028803426&partnerID=40&md5=4bf5ad5efaa7a6f9a546848a19307778","Division of Neuropathology, Dept. of Pathology/Laboratory Med., Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6079, United States","Lavi, E., Division of Neuropathology, Dept. of Pathology/Laboratory Med., Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6079, United States; Wang, Q., Division of Neuropathology, Dept. of Pathology/Laboratory Med., Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6079, United States","MHV-A59 causes focal acute encephalitis, acute hepatitis, and chronic demyelination while MHV-2 causes acute hepatitis and no brain involvement. The difference in organ tropism between these two closely related MHVs is not related to the ability of these viruses to grow in brain cells since both viruses grow equally well in primary glial cell cultures derived from neonatal mouse brains. We postulated therefore that the ability of the virus to stimulate certain host immunological factors may be important for protection of the brain against invasion and replication of the virus. In this study we performed preliminary experiments to investigate the potential role of two host factors in protection of the brain against MHV invasion: cytotoxic T cells and interferon. Four week old β2M ((-/-)) mice, lacking β2 microglobulin, MHC class 1 expression and functional cytotoxic CD8+ T cells were inoculated intracerebrally (IC) with MHV-2 and analyzed at various intervals post infection for histopathology and vital titers in organs. Histology revealed both acute hepatitis and acute encephalitis. Acute encephalitis was observed in periventricular areas. Mononuclear lymphocytic infiltration involved the choroid plexus, the ependyma and in the surrounding brain parenchyma. There was no involvement of other areas of the brain including areas that are typically involved in A59 infection of C57B1/6 mice. By contrast, C57B1/6 mice infected with MHV-2 showed no involvement of the brain parenchyma and only slight inflammation of the choroid plexus was present. High titers of infectious virus was detected by plaque assay in both brains and livers of β2M ((-/-)) mice infected with MHV-2 in contrast to only liver titers in C57B1/6 mice infected with a similar dose of MHV-2. Polyclonal rabbit-anti mouse IFN α/β or anti IFN β (Lee Biomolecular Research LAb.) was given to groups of 4-week-old C57B1/6 mice at a dose of 10,000 U per one I.P. treatment, 24 hours prior to I.C. inoculation of 1LD50 of MHV-2 or MHV-A59. At various intervals post inoculation virus tilers from brains and livers were determined by plaque assay, and the histopathology of all the internal organs was analyzed by H and E staining. Treatment with preimmune serum from the same rabbit was used as control with no effect on disease outcome in either one of the viruses. While IFN antibodies had little or no effect on the outcome of disease in MHV-A59 infection, mice treated with either anti IFN α/β or anti IFN β had high titers of virus recovered from the brain and histopathological evidence of acute meningoencephalitis. Thus cytotoxic T cells and interferon may have a protective role against brain invasion of the virus in MHV-2 infection in mice.",,"beta 2 microglobulin; interferon; interferon antibody; major histocompatibility antigen class 1; polyclonal antibody; acute hepatitis; animal experiment; animal tissue; antigen expression; brain protection; conference paper; controlled study; coronavirus; cytotoxic t lymphocyte; histology; histopathology; inoculation; intraperitoneal drug administration; lymphocytic infiltration; mouse; nonhuman; priority journal; transgenic mouse; virus encephalitis; virus plaque; Animal; Antibodies; beta 2-Microglobulin; Brain; Brain Diseases; Coronavirus Infections; Interferon Type I; Interferon-beta; Mice; Mice, Knockout; Murine hepatitis virus; Rabbits; Support, Non-U.S. Gov't; T-Lymphocytes, Cytotoxic",,"Lavi, E.; Division of Neuropathology, Dept. of Pathology/Laboratory Med., Pennsylvania Univ. Sch. of Medicine, Philadelphia, PA 19104-6079, United States",,,00652598,,AEMBA,"8830471","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028803426
"Dea S., Michaud L., Rekik R.","7006056287;57197459648;6602928021;","Antigenic and genomic variations among cytopathic and non-cytopathic strains of bovine enteric coronavirus",1995,"Advances in Experimental Medicine and Biology","380",,,"99","101",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028802459&partnerID=40&md5=80c1dfe0d6ab621da0291447f4915166","Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada","Dea, S., Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada; Michaud, L., Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada; Rekik, R., Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada",[No abstract available],,"virus glycoprotein; animal cell; antigenicity; cattle; conference paper; coronavirus; cytopathogenic effect; dairy industry; diarrhea; enteritis; fetus; newborn infection; nonhuman; priority journal; strain difference; virus genome; virus infection; virus isolation; virus virulence; Animal; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Genome, Viral; Variation (Genetics)",,"Dea, S.; Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, Laval, Que. H7N 4Z3, Canada",,,00652598,,AEMBA,"8830553","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028802459
"Zhang X., Lai M.M.C.","55715175900;7401808497;","Erratum: Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: implications for the mechanism of RNA transcription and recombination (Journal of Virology 68:10 (6628))",1995,"Journal of Virology","69","2",,"1376","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028797418&partnerID=40&md5=d7cad37b53a48b22b3a133f24e6a832b","Howard Hughes Medical Institute, Department of Microbiology, So. California Univ. Sch. of Med., Los Angeles, CA 90033-1054, United States","Zhang, X., Howard Hughes Medical Institute, Department of Microbiology, So. California Univ. Sch. of Med., Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, Department of Microbiology, So. California Univ. Sch. of Med., Los Angeles, CA 90033-1054, United States",[No abstract available],,"erratum; error; priority journal",,"Zhang, X.; Howard Hughes Medical Institute, Department of Microbiology, So. California Univ. Sch. of Med., Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,,"English","J. VIROL.",Erratum,"Final",,Scopus,2-s2.0-0028797418
"Alexander L.K., Keene B.W., Baric R.S.","36812461600;7006043632;7004350435;","Echocardiographic changes following rabbit coronavirus infection",1995,"Advances in Experimental Medicine and Biology","380",,,"113","115",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028788326&partnerID=40&md5=f6ebb494e02966af629f51ff7c2ee331","Department of Epidemiology, University of North Carolina, Chapel Hill, NC, United States","Alexander, L.K., Department of Epidemiology, University of North Carolina, Chapel Hill, NC, United States; Keene, B.W., Department of Epidemiology, University of North Carolina, Chapel Hill, NC, United States; Baric, R.S., Department of Epidemiology, University of North Carolina, Chapel Hill, NC, United States",[No abstract available],,"animal model; cardiovascular infection; conference paper; controlled study; coronavirus; disease severity; echocardiography; heart left ventricle function; nonhuman; priority journal; rabbit; survival rate; virus infection; Animal; Coronavirus Infections; Echocardiography; Electrocardiography; Male; Myocarditis; Rabbits; Time Factors",,"Alexander, L.K.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC, United States",,,00652598,,AEMBA,"8830464","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028788326
"Kyuwa S., Machii K., Okumura A., Toyoda Y.","7006444820;7005995877;55844839600;7101966291;","Primary murine coronavirus infection in mice: A flow cytometric analysis",1995,"Advances in Experimental Medicine and Biology","380",,,"183","184",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028787266&partnerID=40&md5=6d7e6e8a98580f3b22adf6625c2fdf91","Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan","Kyuwa, S., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan; Machii, K., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan; Okumura, A., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan; Toyoda, Y., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan",[No abstract available],,"cd8 antigen; lymphocyte function associated antigen 1; t lymphocyte receptor; animal cell; animal experiment; cell line; conference paper; cytotoxicity; female; flow cytometry; mouse; murine hepatitis coronavirus; nonhuman; priority journal; spleen cell; t lymphocyte; virus infection; virus replication; Animal; Antigens, CD8; CD8-Positive T-Lymphocytes; Cell Line; Coronavirus Infections; Female; Flow Cytometry; Lymphocyte Function-Associated Antigen-1; Mice; Mice, Inbred C57BL; Murine hepatitis virus; T-Lymphocyte Subsets",,"Kyuwa, S.; Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo, Japan",,,00652598,,AEMBA,"8830477","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028787266
"Buschman E., Skamene E.","6603628629;7005192517;","Genetic resistance to coronavirus infection: A review",1995,"Advances in Experimental Medicine and Biology","380",,,"1","11",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028787262&partnerID=40&md5=5a5dfb2f47847340c9a6484d4f3e315d","MCSHR, Montreal General Hospital, Montreal, Que., Canada","Buschman, E., MCSHR, Montreal General Hospital, Montreal, Que., Canada; Skamene, E., MCSHR, Montreal General Hospital, Montreal, Que., Canada",[No abstract available],,"cell receptor; animal model; central nervous system infection; chromosome 7; chronic disease; conference paper; coronavirus; gene control; gene expression regulation; infection resistance; mouse; nonhuman; priority journal; swine; virus cell interaction; virus infection; virus replication; virus virulence; Animal; Coronavirus Infections; Human; Immunity, Natural; Macrophages; Mice; Murine hepatitis virus; Receptors, Virus",,"Buschman, E.; MCSHR, Montreal General Hospital, Montreal, Que., Canada",,,00652598,,AEMBA,"8830460","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028787262
"Penzes Z., Tibbles K.W., Shaw K., Britton P., Brown T.D.K., Cavanagh D.","55761804900;6507790687;7202206256;57203302770;56248391000;26642890500;","Generation of a defective RNA of avian coronavirus infectious bronchitis virus (IBV): Defective RNA of coronavirus IBV",1995,"Advances in Experimental Medicine and Biology","380",,,"563","569",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028785125&partnerID=40&md5=983ad4bd115ea5895678369b2c26f920","Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom","Penzes, Z., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Tibbles, K.W., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Brown, T.D.K., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom","The Beaudette strain of IBV was passaged 16 times in chick kidney (CK) cells. Total cellular RNA was analyzed by Northern hybridization and was probed with 32P-labeled cDNA probes corresponding to the first 2 kb of the 5' end of the genome, but excluding the leader, and to the last 1.8 kb of the 3' end of the genome. A new, defective IBV RNA species (CD-91) was detected at passage six. The defective RNA, present in total cell extract RNA and in oligo-(dT)30-selected RNA from passage 15, was amplified by the reverse transcription-polymerase chain reaction (RT-PCR) to give four fragments. The oligonucleotides used were selected such that CD-91 RNA, but not the genomic RNA, would be amplified. Cloning and sequencing of the PCR products showed that CD-91 comprises 9.1 kb and has three regions of the genome. It contains 1133 nucleotides from the 5' end of the genome, 6322 from gene 1b corresponding to position 12423 to 18744 in the IBV genome and 1626 from the 3' end of the genome. At position 749 one nucleotide, an adenine residue, was absent from CD-91 RNA. By Northern hybridization CD-91 RNA was detected in virions in higher amounts than the subgenomic mRNAs.",,"virus rna; animal cell; avian infectious bronchitis virus; chicken; conference paper; messenger rna synthesis; molecular cloning; nonhuman; priority journal; reverse transcription polymerase chain reaction; virus gene; virus replication; virus strain; Animal; Blotting, Northern; Cells, Cultured; Chickens; Defective Viruses; DNA Probes; DNA, Complementary; Infectious bronchitis virus; Kidney; Molecular Sequence Data; Open Reading Frames; Polymerase Chain Reaction; RNA, Messenger; RNA, Viral; Support, Non-U.S. Gov't; Virion",,"Cavanagh, D.; Division of Molecular Biology, Institute for Animal Health, Newbury, Berkshire RG16 ONN, United Kingdom",,,00652598,,AEMBA,"8830542","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028785125
"Zhang X., Lai M.M.C.","55715175900;7401808497;","Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed",1995,"Journal of Virology","69","3",,"1637","1644",,46,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028889896&partnerID=40&md5=a0766d2358902b4baa5d1de8a69e10a3","Department of Microbiology, Howard Hughes Medical Institute, S. California Univ. Sch. of Medicine, Los Angeles, CA 90033-1054, United States","Zhang, X., Department of Microbiology, Howard Hughes Medical Institute, S. California Univ. Sch. of Medicine, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Department of Microbiology, Howard Hughes Medical Institute, S. California Univ. Sch. of Medicine, Los Angeles, CA 90033-1054, United States","Previous studies suggested that coronavirus RNA transcription involves interaction between leader RNA and the intergenic (IG) sequences, probably via protein-RNA interactions (X. M. Zhang, C.-L. Liao, and M. M. C. Lai, J. Virol., 68:4738-4746, 1994; X. M. Zhang and M. M. C. Lai, J. Virol., 68:6626- 6633, 1994). To determine whether cellular proteins are involved in this process, we performed UV cross-linking experiments using cytoplasmic extracts of uninfected cells and the IG (promoter) sequence between genes 6 and 7 (IG7) and the 5' untranslational region of mouse hepatitis virus genomic RNA. We demonstrated that three different cellular proteins (p70, p48, and p35/38) bound to the promoter sequence of the template RNA. Deletion analyses of the template RNA mapped the binding site of p35/38 at the consensus transcription initiation signal. In contrast, the binding of p70 and p48 was less specific. p35/38 is the same protein as the one previously identified to bind to the complementary strand of the leader RNA; its binding affinity to the leader was approximately 15 times stronger than that to IG7. Site-directed mutagenesis of the IG sequence revealed that mutations in the consensus sequence of IG7 (UCUAAUCUAAAC to UCGAAAC and GCUAAAG), which resulted in reduced subgenomic mRNA transcription, also caused correspondingly reduced levels of p35/38 binding. These results demonstrated that the extent of protein binding to the IG sequences correlated with the amounts of subgenomic mRNAs transcribed from the IG site. These studies suggest that these RNA- binding proteins are involved in coronavirus RNA transcription and may represent transcription factors.",,"cytoplasm protein; virus rna; amino acid sequence; animal cell; article; binding site; gene deletion; gene mapping; hepatitis virus; mouse; nonhuman; priority journal; promoter region; protein protein interaction; rna transcription; Base Sequence; Binding Sites; Consensus Sequence; Cytoplasm; DNA Primers; Gene Expression Regulation, Viral; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Promoter Regions (Genetics); Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; RNA-Binding Proteins; Structure-Activity Relationship; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transcription, Genetic",,"Lai, M.M.C.; Department of Microbiology, Howard Hughes Medical Institute, S. California Univ. Sch. of Medicine, Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"7853499","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028889896
"Gagneten S., Gout O., Dubois-Dalcq M., Rottier P., Rossen J., Holmes K.V.","6602898805;7005177417;57204484178;7006145490;7005977394;7201657724;","Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein",1995,"Journal of Virology","69","2",,"889","895",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028813624&partnerID=40&md5=b6eda0841988f43e78e461e48fba121c","Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States","Gagneten, S., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States; Gout, O., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States; Dubois-Dalcq, M., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States; Rottier, P., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States; Rossen, J., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States; Holmes, K.V., Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States","In addition to the spike (S) glycoprotein that binds to carcinoembryonic antigen-related receptors on the host cell membrane, some strains of mouse coronavirus (mouse hepatitis virus [MHV]) express a hemagglutinin esterase (HE) glycoprotein with hemagglutinating and acetylesterase activity. Virions of strains that do not express HE, such as MHV-A59, can infect mouse fibroblasts in vitro, showing that the HE glycoprotein is not required for infection of these cells. The present work was done to study whether interaction of the HE glycoprotein with carbohydrate moieties could lead to virus entry and infection in the absence of interaction of the S glycoprotein with its receptor glycoprotein, MHVR. The DVIM strain of MHV expresses large amounts of HE glycoprotein, as shown by hemadsorption, acetylesterase activity, and immunoreactivity with antibodies directed against the HE glycoprotein of bovine coronavirus. A monoclonal anti-MHVR antibody, MAb- CC1, blocks binding of virus S glycoprotein to MHVR and blocks infection of MHV strains that do not express HE. MAb-CC1 also prevented MHV-DVIM infection of mouse DBT cells and primary mouse glial cell cultures. Although MDCK-I cells express O-acetylated sialic acid residues on their plasma membranes, these canine cells were resistant to infection with MHV-A59 and MHV-DVIM. Transfection of MDCK-I cells with MHVR cDNA made them susceptible to infection with MHV-A59 and MHV-DVIM. Thus, the HE glycoprotein of an MHV strain did not lead to infection of cultured murine neural cells or of nonmurine cells that express the carbohydrate ligand of the HE glycoprotein. Therefore, interaction of the spike glycoprotein of MHV with its carcinoembryonic antigen-related receptor glycoprotein is required for infectivity of MHV strains whether or not they express the HE glycoprotein.",,"esterase; membrane protein; virus glycoprotein; animal cell; article; dna transfection; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein binding; protein protein interaction; Animal; Cells, Cultured; Dogs; Hamsters; Hemagglutinins, Viral; Human; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Receptors, Virus; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Viral Proteins",,"Holmes, K.V.; Department of Pathology, Uniformed Svcs. Hlth. Sciences Univ., 4301 Jones Bridge Rd., Bethesda, MD 20814-4799, United States",,,0022538X,,JOVIA,"7815557","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028813624
"Bernard S., Laude H.","35607150100;7006652624;","Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity",1995,"Journal of General Virology","76","9",,"2235","2241",,32,"10.1099/0022-1317-76-9-2235","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029092240&doi=10.1099%2f0022-1317-76-9-2235&partnerID=40&md5=5a8595fba0077d9c059725675352e0a6","Virologie Immunologie Moleculaires, Inst. National Recherche Agronomique, Jouy-en-Josas, France","Bernard, S., Virologie Immunologie Moleculaires, Inst. National Recherche Agronomique, Jouy-en-Josas, France; Laude, H., Virologie Immunologie Moleculaires, Inst. National Recherche Agronomique, Jouy-en-Josas, France","The pathogenicity of neutralization-resistant mutants of the enteric coronavirus transmissible gastroenteritis virus (TGEV) was examined in the newborn piglet. The parental virus (Purdue-115 strain), as well as several mutants selected using monoclonal antibodies (MAbs) directed to antigenic sites A and B, caused an acute enteritis with 100% mortality. By contrast, most of the site D (MAb 40.1) mutants exhibited a strongly reduced enteropathogenicity, leading to the survival of animals inoculated with up to 1000-fold the 100% lethal dose of parental virus. Such a phenotypical change was correlated with point mutations or a small deletion, all located within the S gene sequence coding for the Pro-145 to Cys-155 segment of the mature polypeptide. These observations suggest that an N-terminal subregion of the S molecule is an essential determinant for pathogenesis in TGEV infection.",,"cysteine; epitope; monoclonal antibody; proline; virus protein; amino terminal sequence; animal cell; animal experiment; article; controlled study; deletion mutant; Enterovirus; gastroenteritis; lethal dose; mortality; newborn; nonhuman; pathogenicity; phenotype; point mutation; priority journal; swine disease; virus neutralization; virus transmission; Animalia; Enteric coronavirus; Enterovirus; Sus scrofa; Transmissible gastroenteritis virus",,"Laude, H.; Virologie Immunologie Moleculaires, Inst. National Recherche Agronomique, Jouy-en-Josas, France",,"Microbiology Society",00221317,,JGVIA,"7561760","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029092240
"Sueyoshi M., Tsuda T., Yamazaki K., Yoshida K., Nakazawa M., Sato K., Minami T., Iwashita K., Watanabe M., Suzuki Y., Mori M.","7004578788;7402162445;36124193100;57199926605;7402069719;7407875132;7402422738;36122947100;55493156200;57198662829;7404718176;","An immunohistochemical investigation of porcine epidemic diarrhoea",1995,"Journal of Comparative Pathology","113","1",,"59","67",,58,"10.1016/S0021-9975(05)80069-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029025790&doi=10.1016%2fS0021-9975%2805%2980069-6&partnerID=40&md5=46fdaf9036621f7cbaa4e0a61b748be2","Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan; Kagoshimachuo Livestock Hygiene Service Center, 5500 Kamifukumoto, Kagoshima, 891-01, Japan; Nansatsu Livestock Hygiene Service Center, 4210 Chiran, Kagoshima, 897-03, Japan; Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan","Sueyoshi, M., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Tsuda, T., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Yamazaki, K., Kagoshimachuo Livestock Hygiene Service Center, 5500 Kamifukumoto, Kagoshima, 891-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Yoshida, K., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Nakazawa, M., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Sato, K., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Minami, T., Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Iwashita, K., Kagoshimachuo Livestock Hygiene Service Center, 5500 Kamifukumoto, Kagoshima, 891-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Watanabe, M., Kagoshimachuo Livestock Hygiene Service Center, 5500 Kamifukumoto, Kagoshima, 891-01, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Suzuki, Y., Nansatsu Livestock Hygiene Service Center, 4210 Chiran, Kagoshima, 897-03, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan; Mori, M., Nansatsu Livestock Hygiene Service Center, 4210 Chiran, Kagoshima, 897-03, Japan, Chusei Livestock Hygiene Service Center, 3841 Takajayakomori, Tsu, Mie, 514, Japan","A sudden outbreak of epidemic diarrhoea of piglets occurred in Japan, the principal features being watery diarrhoea, dehydration and high mortality in newborn animals. The microscopical lesions were villous atrophy in the small intestine, the villous enterocytes being vacuolated and cuboidal in shape. The villus-crypt ratio was severely reduced, varying from 1:1 to 3:1. Transmission electron microscopy showed numerous coronaviruses within the cytoplasm of enterocytes and among microvilli. Specific antigens of porcine epidemic diarrhoea (PED) virus were detected in the cytoplasm of enterocytes by the streptavidin-biotin (SAB) technique. Infected cells, which were most abundant in the villous epithelia of the jejunum and ileum, were present in small numbers in the large intestine, the crypt epithelia, the lamina propria and Peyer's patches. The study suggests that the SAB technique is useful for the diagnosis of PED. © 1995 Academic Press Limited.",,"biotin; streptavidin; animal experiment; animal tissue; article; controlled study; crypt cell; cytoplasm; dehydration; diarrhea; epidemic; ileum; immunohistochemistry; intestine cell; intestine villus atrophy; japan; jejunum; lamina propria; large intestine; mortality; nonhuman; peyer patch; small intestine; swine; swine disease; transmission electron microscopy; Animal; Animals, Newborn; Diarrhea; Disease Outbreaks; Gastroenteritis, Transmissible, of Swine; Immunohistochemistry; Japan; Jejunum; Swine; Swine Diseases; Transmissible gastroenteritis virus; Animalia; Porcine epidemic diarrhea virus; Suidae; Sus scrofa","Chasey, Cartwright, Virus-like particles associated with porcine epidemic diarrhoea (1978) Research in Veterinary Science, 25, pp. 255-256; Cox, Hooyberghs, Pensaert, Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Research in Veterinary Science, 48, pp. 165-169; Debouck, Pensaert, Experimental infection of pigs with a new porcine enteric coronavirus CV 777 (1980) American Journal of Veterinary Research, 41, pp. 219-223; Debouck, Pensaert, Coussement, The pathogenesis of an enteric infection in pigs, experimentally induced by the coronavirus-like agent, CV 777 (1981) Veterinary Microbiology, 6, pp. 157-165; Ducatelle, Coussement, Charlier, Debouck, Hoorens, Three-dimensional sequential study of the intestinal surface in experimental porcine CV 777 coronavirus enteritis (1981) Zentralblatt für Veterinärmedizin, B, 28, pp. 483-493; Hooper, Haelterman, Growth of transmissible gastroenteritis virus in young pigs (1966) American Journal of Veterinary Research, 27, pp. 286-291; Horvath, Mocsari, Ultrastructural changes in the small intestinal epithelium of suckling pigs affected with a transmissible gastroenteritis (TGE)-like disease (1981) Archives of Virology, 68, pp. 103-113; Kusanagi, Kuwahara, Katoh, Nunoya, Ishikawa, Samejima, Tajima, Isolation and serial propagation of porcine epidemic diarrhoea virus in cell cultures and partial characterization of the isolate (1992) Journal of Veterinary Medical Science, 54, pp. 313-318; Kuwahara, Nunoya, Samejima, Tajima, Passage in piglets of a coronavirus associated with porcine epidemic diarrhoea (1988) Journal of the Japan Veterinary Medical Association, 41, pp. 169-173; Pensaert, Debouck, A new coronavirus-like particle associated with diarrhoea in swine (1978) Archives of Virology, 58, pp. 243-247; Pensaert, Debouck, Reynolds, An immunoelectron microscopic and immunofluorescent study on the antigenic relationship between the coronavirus-like agent, CV 777, and several coronaviruses (1981) Archives of Virology, 68, pp. 45-52; Pospischil, Hess, Bachmann, Light microscopy and ultrahistology of intestinal changes in pigs infected with epizootic diarrhoea virus (EVD): comparison with transmissible gastroenteritis (TGE) virus and porcine rotavirus infections (1981) Zentralblatt für Veterinärmedizin, B, 28, pp. 564-577; Takahashi, Okada, Ohshima, An outbreak of swine diarrhoea of a new type associated with coronavirus-like particles in Japan (1983) Japan Journal of Veterinary Science, 45, pp. 829-832; Turgeon, Morin, Jolette, Higgins, Marsolais, Difranco, Coronavirus-like particles associated with diarrhea in baby pigs in Quebec (1980) Canadian Veterinary Journal, 21, pp. 100-101; Wood, An apparently new syndrome of porcine epidemic diarrhoea (1977) Veterinary Record, 100, pp. 243-244","Sueyoshi, M.; Kyushu Branch Laboratory, National Institute of Animal Health, 2702 Chuzan, Kagoshima, 890-01, Japan",,,00219975,,JCVPA,"7490338","English","J. Comp. Pathol.",Article,"Final",,Scopus,2-s2.0-0029025790
"Heemskerk M.H.M., Schilham M.W., Schoemaker H.M., Spierenburg G., Spaan W.J.M., Boog C.J.P.","7004561258;7003459097;57191387504;6603503327;7007172944;7007043833;","Activation of virus‐specific major histocompatibility complex class II‐restricted CD8+ cytotoxic T cells in CD4‐deficient mice",1995,"European Journal of Immunology","25","4",,"1109","1112",,15,"10.1002/eji.1830250438","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028964360&doi=10.1002%2feji.1830250438&partnerID=40&md5=a81f0afb1633abaed795fa9c2907c24a","Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, Utrecht, Netherlands; Department of Immunology, University Hospital, Utrecht, Netherlands; Department of Virology, Faculty of Medicine, Leiden, Netherlands; Department of Transplantation Immunology, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Netherlands","Heemskerk, M.H.M., Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, Utrecht, Netherlands; Schilham, M.W., Department of Immunology, University Hospital, Utrecht, Netherlands; Schoemaker, H.M., Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, Utrecht, Netherlands; Spierenburg, G., Department of Immunology, University Hospital, Utrecht, Netherlands; Spaan, W.J.M., Department of Virology, Faculty of Medicine, Leiden, Netherlands; Boog, C.J.P., Institute of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, Utrecht, Netherlands, Department of Transplantation Immunology, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam, Netherlands","Acute enteritic or respiratory disease is a consequence of coronavirus infection in man and rodents. Mouse hepatitis virus, stain A59 (MHV‐A59) causes acute hepatitis in mice and rats and induces a response of major histocompatibility complex (MHC) class II‐restricted CD4+ cytotoxic T cells, protecting mice against acute infection. In the present study we show that MHV‐A59 infection of mice that lack a functional CD4 gene activates effector cells of the CD8+ phenotype. These cytotoxic T cells lyse virus‐infected target cells in a MHC class II‐restricted fashion. The results indicate that CD8+ T cells have the potential to utilize MHC class II as restriction element, illustrating that the immune system can effectively deal with evading microorganisms, such as viruses which down‐regulate MHC class I. Copyright © 1995 WILEY‐VCH Verlag GmbH &amp; Co. KGaA, Weinheim","CD8+ T cells; Major histocompatibility complex class II‐restricted; Mouse hepatitis virus","cd4 antigen; cd8 antigen; animal cell; animal experiment; article; cytolysis; cytotoxic t lymphocyte; effector cell; experimental infection; major histocompatibility complex; major histocompatibility complex restriction; mouse; murine hepatitis coronavirus; nonhuman; priority journal; t lymphocyte activation; virus hepatitis; Animal; Antigen Presentation; Antigens, CD4; CD8-Positive T-Lymphocytes; Coronavirus Infections; Histocompatibility Antigens Class II; Lymphocyte Activation; Mice; Mice, Inbred C57BL; Mice, Mutant Strains; Murine hepatitis virus; Support, Non-U.S. Gov't","Swain, S.L., (1994) Immunol. Rev., 74, p. 129; Kirberg, J., Baron, A., Jakob, S., Rolink, A., Karjalainen, K., Von Boehmer, H., (1994) J. Exp. Med., 180, p. 25; De Bueger, M., Bakker, A., Goulmy, E., (1992) Eur. J. Immunol., 22, p. 875; McKisic, M.D., Sant, A.J., Fitch, F.W., (1994) J. Immunol., 147, p. 2868; Vidovic, D., Juretic, A., Nagy, A., Klein, J., (1981) Eur. J. Immunol., 11, p. 499; Shinohara, N., Kojima, M., (1984) J. Immunol., 132, p. 578; Spits, H., Yssel, H., Thompson, A., De Vries, J.E., (1983) J. Immunol., 131, p. 678; Wege, H., Siddell, S., ter Meulen, V., (1982) Curr. Top. Microbiol. Immunol., 99, p. 164; Boog, C.J.P., Heemskerk, M.H.M., Schoemaker, H.M., Spaan, W.J.M., (1994) J. Cell. Biochem., 18, p. 351; Heemskerk, M.H.M., Schoemaker, H.M., Spaan, W.J.M., Boog, C.J.P., (1995), Immunology; Rahemtulla, A., Fung‐Leung, W.P., Schilham, M.W., Kündig, T.M., Sambhara, S.R., Narendran, A., Arabian, A., Mak, T.W., (1991) Nature, 353, p. 180; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., van der Zeijst, B.A.M., (1981) Virology, 108, p. 424; Koolen, M.J.M., Osterhaus, A.D.M.E., Steenis, G., Horzinek, M.C., van der Zeijst, B.A.M., (1982) Virology, 125, p. 393; de Waal, L.P., Kast, W.M., Melvold, R.W., Melief, C.J.M., (1983) J. Immunol., 130, p. 1090; Lorber, M.I., Loken, M.R., Stall, A.M., Fitch, F.W., (1982) J. Immunol., 128, p. 2798; Heemskerk, M.H.M., Schoemaker, H.M., Alphen, H.E., van der Zee, R., Joosten, I., Spaan, W.J.M., Boog, C.J.P., (1994) Adv. Exp. Med. Biol., 342, p. 407; Locksley, R.M., Reiner, S.L., Hatam, F., Littman, D.R., Killeen, N., (1993) Science, 261, p. 1448; Rahemtulla, A., Kündig, T.M., Narendran, A., Bachmann, M.F., Julius, M., Paige, C.J., Ohashi, P.S., Mak, T.W., Class II major histocompatibility complex-restricted T cell function in CD4-deficient mice (1994) European Journal of Immunology, 24, p. 2213; Bhattacharya, A., Dorf, M.E., Springer, T.A., (1981) J. Immunol., 127, p. 2488; Koch, S., Koch, H., Robinson, P., Hämmerling, G., (1983) Transplantation, 36, p. 177; Askonas, B.A., Taylor, P.M., Esquivel, F., (1988) Ann. NY Acad. Sci., 532, p. 230; Lehmann‐Grube, F., Moskophidis, D., Lohler, J., Recovery from Acute Virus Infection. (1988) Annals of the New York Academy of Sciences, 532, p. 238; Byre, J.A., Oldstone, M.B.A., (1984) J. Virol., 51, p. 682; Bergmann, C., McMillan, M., Stohlman, S., (1993) J. Virol., 67, p. 7041; Coutelier, J.P., Godfraind, C., Dveksler, G.S., Wysocka, M., Cardellichio, C.B., Noël, H., Holmes, K.V., (1994) Eur. J. Immunol., 24, p. 1383","Heemskerk, M.H.M.; Department of Immunology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam, NL-1066 CX, Netherlands",,,00142980,,,"7737281","English","Eur. J. Immunol.",Article,"Final",,Scopus,2-s2.0-0028964360
"Opstelten D.-J.E., Raamsman M.J.B., Wolfs K., Horzinek M.C., Rottier P.J.M.","7003742658;6603137050;6507471811;7102624836;7006145490;","Coexpression and association of the spike protein and the membrane protein of mouse hepatitis virus",1995,"Advances in Experimental Medicine and Biology","380",,,"291","297",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028856443&partnerID=40&md5=170000b0556e70b72c538a2297f3497d","Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands","Opstelten, D.-J.E., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Raamsman, M.J.B., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Wolfs, K., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands","The M and S envelope glycoproteins of mouse hepatitis virus associate in the process of virus assembly. We have studied the intrinsic properties of M/S heterocomplexes by coexpressing M and S in the absence of other coronaviral proteins. The formation of M/S complexes under these conditions indicates that M and S can interact independently of other coronaviral factors. Pulse-chase analysis revealed that M and S associate in a pre-Golgi compartment. M/S complexes are efficiently transported beyond the coronavirus budding compartment to the Golgi complex. The failure to detect complexes at the surface of coexpressing cells demonstrated that they are retained intracellularly. Thus, coexpression of the envelope glycoproteins drastically affects the intracellular transport of the S protein: instead of being transported to the cell surface, S is retained intracellularly by its association with M.",,"virus glycoprotein; animal cell; conference paper; gene expression; golgi complex; intracellular transport; murine hepatitis coronavirus; nonhuman; priority journal; protein assembly; protein transport; Animal; Antibodies, Monoclonal; Cell Line; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Gene Expression; Golgi Apparatus; Kinetics; Membrane Glycoproteins; Mice; Molecular Weight; Murine hepatitis virus; Recombinant Proteins; Sulfur Radioisotopes; Transfection; Viral Envelope Proteins; Viral Matrix Proteins",,"Opstelten, D.-J.E.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands",,,00652598,,AEMBA,"8830496","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028856443
"Norkin L.C.","7003826034;","Virus receptors: Implications for pathogenesis and the design of antiviral agents",1995,"Clinical Microbiology Reviews","8","2",,"293","315",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028930980&partnerID=40&md5=4441c9ce27f8f1722ed366211434b662","Department of Microbiology, University of Massachusetts, Amherst, MA 01003, United States","Norkin, L.C., Department of Microbiology, University of Massachusetts, Amherst, MA 01003, United States","A virus initiates infection by attaching to its specific receptor on the surface of a susceptible host cell. This prepares the way for the virus to enter the cell. Consequently, the expression of the receptor on specific cells and tissues of the host is a major determinant of the route of entry of the virus into the host and of the patterns of virus spread and pathogenesis in the host. This review emphasizes the virus-receptor interactions of human immunodeficiency virus, the rhinoviruses, the herpesviruses, and the coronaviruses. These interactions are often found to be complex and dynamic, involving multiple sites or factors on both the virus and the host cell. Also, the receptor may play an important role in virus entry per se in addition to its role in virus binding. In the cases of human immunodeficiency virus and the rhinoviruses, ingenious approaches to therapeutic strategies based on inhibiting virus attachment and entry are under development and in clinical trials.",,"antivirus agent; cd4 antigen; intercellular adhesion molecule 1; virus receptor; drug design; herpes virus; human immunodeficiency virus; human rhinovirus; nonhuman; pathogenesis; picornavirus; poliomyelitis virus; retrovirus; review; virus morphology; Antigens, CD4; Antiviral Agents; Coronavirus; Drug Design; Herpesviridae; HIV; Human; Intercellular Adhesion Molecule-1; Models, Molecular; Picornaviridae; Receptors, Virus; Retroviridae; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.",,"Norkin, L.C.; Department of Microbiology, University of Massachusetts, Amherst, MA 01003, United States",,,08938512,,CMIRE,"7621403","English","CLIN. MICROBIOL. REV.",Review,"Final",,Scopus,2-s2.0-0028930980
"Klepfer S., Reed A.P., Martinez M., Bhogal B., Jones E., Miller T.J.","6507963520;7202692665;37022351000;57197017709;7404237166;57198615518;","Cloning and expression of FECV spike gene in vaccinia virus: Immunization with FECV S causes early death after FIPV challenge",1995,"Advances in Experimental Medicine and Biology","380",,,"235","241",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028892119&partnerID=40&md5=629825061e681a8fe25807dc8492a136","Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States","Klepfer, S., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States; Reed, A.P., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States; Martinez, M., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States; Bhogal, B., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States; Jones, E., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States; Miller, T.J., Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States","The spike gene of the feline enteric coronavirus (FECV), strain FECV- 1683, was PCR amplified from total RNA extracted from FECV-infected cells and its sequence determined. A primary translation product of 1454 amino acids is predicted from the nucleotide sequence, containing a N-terminal signal sequence, a C-terminal transmembrane region and 33 potential N-glycosylation sites. The sequence shares 92% homology with the previously published feline infectious peritonitis virus, strain WSU-1146; however, several regions were identified that distinguished FECV from Feline Infectious Peritonitis virus, FIPV. The full length FECV S gene was cloned and expressed in vaccinia virus. Recombinants produced a 200 kD protein which was recognized by sera from cats infected with FIPV. When kittens were immunized with the vaccinia/FECV S recombinant, neutralizing antibodies to FIPV were induced. After challenge with a lethal dose of FIPV, the recombinant vaccinated animals died earlier than control animals immunized with vaccinia virus alone.",,"neutralizing antibody; recombinant vaccine; vaccinia vaccine; virus antibody; virus rna; animal experiment; cat; conference paper; controlled study; coronavirus; gene expression; immunization; molecular cloning; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; rna analysis; rna sequence; rna translation; sequence homology; subcutaneous drug administration; vaccinia virus; virus gene; virus infection; virus strain; Animal; Antibodies, Viral; Antibody Formation; Blotting, Western; Cats; Cell Line; Cloning, Molecular; Coronavirus, Feline; Enzyme-Linked Immunosorbent Assay; Feline Infectious Peritonitis; Genes, Viral; Immunization; Membrane Glycoproteins; Polymerase Chain Reaction; Protein Sorting Signals; RNA, Viral; Translation, Genetic; Vaccinia virus; Viral Envelope Proteins",,"Klepfer, S.; Department of Molecular Biology, Smithkline Beecham Animal Health, P.O. Box 1539, King of Prussia, PA, United States",,,00652598,,AEMBA,"8830486","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028892119
"Heemskerk M.H.M., Schoemaker H.M., Spaan W.J.M., Boog C.J.P.","7004561258;57191387504;7007172944;7007043833;","Predominance of MHC class II-restricted CD4+ cytotoxic T cells against mouse hepatitis virus A59",1995,"Immunology","84","4",,"521","527",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028953854&partnerID=40&md5=0847885646843fc4e7a54c92268d8eaa","Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands","Heemskerk, M.H.M., Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands; Schoemaker, H.M., Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands; Spaan, W.J.M., Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands; Boog, C.J.P., Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands","Coronavirus-induced acute hepatitis is a complex event and the role of different components of the immune system with regard to defined viral proteins and the course of the infection is not yet clear. We have analysed the cytotoxic T-lymphocyte (CTL) response in mouse hepatitis virus (MHV-A59) infection. Surprisingly, we detected only a very clear virus-specific major histocompatibility complex (MHC) class II-restricted cytotoxicity in mice infected with MHV-A59. We found no evidence of activation of the classical CD8+ MHC class I-restricted CTL. The virus-specific CD4+ CTL derived from two different mouse strains having different MHC haplotypes recognized the same immunodominant epitope. This epitope, comprising the amino acid residues 329-343 of the viral S-glycoprotein, was recognized both at the polyclonal level and by virus-specific CTL clones. Transfer studies using a MHV-A59-specific CD4+ CTL clone showed significant protection against a lethal challenge with MHV-A59, implicating that these CD4+ CTL play a pivotal role in the protection against MHV-A59 infections.",,"cd4 antigen; cd8 antigen; major histocompatibility antigen class 2; adoptive transfer; animal experiment; animal model; article; cell line; controlled study; cytotoxic t lymphocyte; major histocompatibility complex restriction; mouse; murine hepatitis coronavirus; nonhuman; priority journal; Animal; Antigens, Viral; CD4-Positive T-Lymphocytes; Cells, Cultured; Coronavirus Infections; Cytotoxicity, Immunologic; Histocompatibility Antigens Class II; Lymphocyte Transfusion; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Murine hepatitis virus; Peptide Fragments; Support, Non-U.S. Gov't; T-Lymphocytes, Cytotoxic",,"Boog, C.J.P.; Dept. of Transplantation Immunology, Central Laboratory, Red Cross Blood Transfusion Service, PO Box 9190, 1006 AD Amsterdam, Netherlands",,,00192805,,IMMUA,"7790024","English","IMMUNOLOGY",Article,"Final",,Scopus,2-s2.0-0028953854
"Evans E.W., Beach F.G., Moore K.M., Jackwood M.W., Glisson J.R., Harmon B.G.","7401610695;7003955256;35606774200;7003643324;7004067793;7101831921;","Antimicrobial activity of chicken and turkey heterophil peptides CHP1, CHP2, THP1, and THP3",1995,"Veterinary Microbiology","47","3-4",,"295","303",,81,"10.1016/0378-1135(95)00126-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028804058&doi=10.1016%2f0378-1135%2895%2900126-3&partnerID=40&md5=a24d571e8b63e8ba68981c6945e89649","Department of Veterinary Pathology, University of Georgia, Athens, GA, United States; Poultry Diagnostic and Research Center, University of Georgia, Athens, GA, United States","Evans, E.W., Department of Veterinary Pathology, University of Georgia, Athens, GA, United States; Beach, F.G., Department of Veterinary Pathology, University of Georgia, Athens, GA, United States; Moore, K.M., Poultry Diagnostic and Research Center, University of Georgia, Athens, GA, United States; Jackwood, M.W., Poultry Diagnostic and Research Center, University of Georgia, Athens, GA, United States; Glisson, J.R., Poultry Diagnostic and Research Center, University of Georgia, Athens, GA, United States; Harmon, B.G., Department of Veterinary Pathology, University of Georgia, Athens, GA, United States","Four avian heterophil antimicrobial cationic peptides (Chicken Heterophil Peptides 1 and 2, and Turkey Heterophil Peptides 1 and 3) were evaluated for in vitro microbicidal activity against selected avian pathogens and human pathogens which are harbored by birds. At concentrations of 16-2 μg/ml, all four avian peptides effected a greater than 90% reduction in the survival of Candida albicans, Salmonella enteriditis, and Campylobacter jejuni. None of the peptides, including the known antimicrobial peptide protamine (used as a positive control), were able to reduce the survival of Pasteurella multocida by 90% at the maximum peptide concentration (16 μg/ml) tested. At 16 μ/ml, the turkey peptide THP3 did not effect a 90% reduction in survival of Bordetella avium, Escherichia coli, or Salmonella typhimurium, while all of the other peptides tested were effective at this concentration or less. This peptide, THP3, does not share the same homologous amino acid sequence shared by the other three peptides. Under our experimental conditions, none of the peptides neutralized Infectious Bronchitis Virus, an enveloped coronavirus of chickens. © 1995.","Antimicrobial peptides; Avian heterophils; Beta-defensin; Chicken; Turkey","antiinfective agent; peptide; amino acid sequence; antimicrobial activity; article; campylobacter jejuni; candida albicans; chicken; controlled study; nonhuman; salmonella enteritidis; turkey (republic); veterinary medicine; Animal; Antibiotics, Peptide; Antifungal Agents; Bordetella; Campylobacter jejuni; Candida albicans; Chickens; Comparative Study; Escherichia coli; Microbial Sensitivity Tests; Proteins; Salmonella enteritidis; Salmonella typhimurium; Support, U.S. Gov't, Non-P.H.S.; Turkeys; Aves; Avian infectious bronchitis virus; Bordetella avium; Campylobacter jejuni; Candida albicans; Coronavirus; Enteritidis; Escherichia coli; Gallus gallus; Pasteurella multocida; Salmonella enteriditis; Salmonella enteritidis; Salmonella typhimurium; Typhimurium","Ahmad, Kleven, Avakian, Glisson, Sensitivity and specificity of Mycoplasma gallisepticum agglutination antigens prepared from medium with artificial liposomes substituting for serum (1988) Avian Dis., 32, pp. 519-526; Black, Levine, Clements, Hughes, Blaser, Experimental Campylobacter jejuni infection in humans (1988) J. Infect. Dis., 157, pp. 472-479; Breton-Gorius, Coquin, Guichard, Cytochemical distinction between azurophils and catalase-containing granules in leukocytes (1978) Lab. Invest., 38, pp. 21-31; Diamond, Zasloff, Eck, Brasseur, Maloy, Bevins, Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA (1991) Biochemistry, 88, pp. 3952-3956; Duvick, Rood, Rao, Marshak, Purification and characterization of a novel antimicrobial peptide from Maize (Zea mays L.) kernels (1992) J. Biol. Chem., 267, pp. 18814-18820; Eisenhauer, Harwig, Szklarek, Ganz, Selsted, Lehrer, Purification and antimicrobial properties of three defensins from rat neutrophils (1989) Infect. Immun., 57, pp. 2021-2027; Evans, Beach, Wunderlich, Harmon, Isolation of antimicrobial peptides from avian heterophils (1994) J. Leukoc. Biol., 56, pp. 661-665; Gelb, Jr., Perkins, Rosenberger, Allen, Serologic and cross-protection studies with several infectious bronchitis virus isolates from Delmarva-reared broiler chickens (1981) Avian Dis., 25, pp. 655-666; Harmon, Glisson, Nunnally, Turkey macrophage and heterophil bactericidal activity against Pasteurella multocida (1992) Avian Dis., 36, pp. 986-991; Harwig, Swiderek, Kokryakov, Tan, Lee, Panyutich, Aleshina, Lehrer, Gallinacins: Cysteine-rich antimicrobial peptides of chicken leukocytes (1994) FEBS Lett., 342, pp. 281-285; Jones, Bevins, Defensin-6 mRNA in human Paneth cells: implications for antimicrobial peptides in host defense of the human bowel (1993) FEBS Lett., 315, pp. 187-192; Kimbrell, Insect antibacterial proteins: not just for insects and against bacteria (1991) Bioessays, 13, pp. 657-663; King, Cavanagh, Infectious bronchitis (1991) Diseases of poultry, pp. 471-484. , B.W. Calnek, Ninth Edn., Iowa State University Press, Ames, IA; Lehrer, Lichtenstein, Ganz, Defensins: antimicrobial and cytotoxic peptides of mammalian cells (1993) Annu. Rev. Immunol., 11, pp. 105-128; Lockman, Curtiss, III, Virulence of non-type 1-fimbriated and nonfimbriated nonflagellated Salmonella typhimurium mutants in murine typhoid fever (1992) Infect. Immun., 60, pp. 491-496; MacRae, Powell, Cytochemical reaction for cationic proteins as a marker of primary granules during development in chick heterophils (1979) Histochemistry, 60, pp. 295-308; Muta, Fujimoto, Nakajima, Iwanaga, Tachyplesins isolated from hemocytes of southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor (1990) J. Biochem., 106, pp. 261-266; Ouelette, Greco, James, Frederick, Naftilan, Fallon, Developmental regulation of cryptdin a corticostatin/defensin precursor mRNA in mouse small intestinal crypt epithelium (1989) The Journal of Cell Biology, 108, pp. 1687-1695; Ozaki, Wada, Hase, Matsubara, Nakanishi, Yoshizumi, Amino acid sequence of a purothionin homolog from barley flour (1980) J. Biochem., 87, pp. 549-555; Peck, A one-plate assay for macrophage bactericidal activity (1985) J. Immunol. Methods, 82, pp. 131-140; Penniall, Spitznagel, Chicken neutrophils: oxidative metabolism in phagocytic cells devoid of myeloperoxidase (1975) Proc. Natl. Acad. Sci. USA, 72, pp. 5012-5015; Sabet, Hsia, Stanisz, El-domeiri, Van Alten, A simple method for obtaining peritoneal macrophages from chickens (1977) J. Immunol. Methods, 14, pp. 103-110; Schat, Purchase, Cell-culture methods (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, pp. 167-175. , H.G. Purchase, L.H. Arp, C.H. Domermuth, J.E. Pearson, Third Edition, Kendall/Hunt Publishing Company, Dubuque, IA; Selsted, Szklarek, Lehrer, Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes (1984) Infect. Immun., 45, pp. 150-154; Selsted, Szklarek, Ganz, Lehrer, Activity of rabbit leukocyte peptides against Candida albicans (1985) Infect. Immun., 49, pp. 202-206; Selsted, Tang, Morris, McGuire, Novotny, Smith, Henschen, Cullor, Purification, primary structure, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils (1993) J. Biol. Chem., 268, pp. 6641-6648; Stoscheck, Quantitation of Protein (1990) Guide to Protein Purification, pp. 50-68. , M.P. Deutscher, Academic Press, San Diego, CA; Yamashita, Saito, Purification, primary structure, and biological activity of guinea pig neutrophil cationic peptides (1989) Infect. Immun., 57, pp. 2405-2409; Zasloff, Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 5449-5453","Evans, E.W.; Department of Veterinary Pathology, University of Georgia, Athens, GA, United States; email: EvansE@svm.vetmed.wisc.edu",,,03781135,,VMICD,"8748545","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0028804058
"Laude H., Godet M., Bernard S., Gelfi J., Duarte M., Delmas B.","7006652624;57206533441;35607150100;8769591600;57205792139;7003294168;","Functional domains in the spike protein of transmissible gastroenteritis virus",1995,"Advances in Experimental Medicine and Biology","380",,,"299","304",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028880565&partnerID=40&md5=3a0069c42e2f9bfe6c2b7850a2eec42c","Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France","Laude, H., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France; Godet, M., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France; Bernard, S., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France; Gelfi, J., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France; Duarte, M., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France; Delmas, B., Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France","The coronavirus spike protein S is assumed to mediate essential biological functions, including recognition of target cells. Earlier studies from our and other groups identified two regions of the TGEV S (220K) protein possibly implicated in such functions. The first of these corresponds to the 224 amino acid N-terminal region which is deleted in PRCV, the respiratory variant of TGEV. We have examined the pathogenicity for the newborn piglet of a series of neutralization escape mutants encoding an S protein mutated in this region. Several amino acid changes were correlated with a dramatic loss of enterovirulence, thus indicating that crucial determinants are associated with this domain of S. The second region of potential relevance is the major neutralization domain. Baculovirus-vectored expression of 150 to 220 amino acid-long stretches encompassing this region, which is encoded by both TGEV and PRCV, was performed. The resultant recombinant proteins were shown to react with the cognate antibodies and to bind APN specifically, thus localizing the receptor-binding site on the S primary structure. Altogether these data lend support to the view that a domain of S protein structurally distinct from the receptor binding site is required for the virus to express its enteric tropism.",,"virus protein; amino terminal sequence; animal model; baculovirus; conference paper; coronavirus; newborn; nonhuman; priority journal; protein domain; receptor binding; swine; virus mutant; virus virulence; Amino Acid Sequence; Animal; Animals, Newborn; Antibodies, Monoclonal; Baculoviridae; Binding Sites; Cell Line; Gastroenteritis, Transmissible, of Swine; Membrane Glycoproteins; Molecular Sequence Data; Neutralization Tests; Receptors, Virus; Recombinant Proteins; Swine; Time Factors; Transfection; Transmissible gastroenteritis virus; Viral Envelope Proteins; Virulence",,"Laude, H.; Unite Virol. Immunol. Moleculaires, Jouy-en-Josas, France",,,00652598,,AEMBA,"8830497","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028880565
"Weingartl H.M., Derbyshire J.B.","6602300880;7004580204;","Cellular receptors for transmissible gastroenteritis virus on porcine enterocytes",1995,"Advances in Experimental Medicine and Biology","380",,,"325","329",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028825238&partnerID=40&md5=7ed283531540299b89466e676a9ac714","Veterinary Microbiol./Immunol. Dept., University of Guelph, Guelph, Ont. N1G 2W1, Canada","Weingartl, H.M., Veterinary Microbiol./Immunol. Dept., University of Guelph, Guelph, Ont. N1G 2W1, Canada; Derbyshire, J.B., Veterinary Microbiol./Immunol. Dept., University of Guelph, Guelph, Ont. N1G 2W1, Canada","The activity of aminopeptidase-N (APN), reported to be a major receptor for porcine transmissible gastroenteritis virus (TGEV), in enterocyte fractions harvested from the jejunal villi and crypts of newborn and weaned piglets, did not correspond with the levels of saturable virus binding previously demonstrated for the same fractions. Plasma membranes prepared from enterocytes harvested from the jejunal villi of a newborn piglet were used in the preparation of a monoclonal antibody (MAb) which blocked the binding of TGEV, but not that of the porcine respiratory coronavirus (PRCV), to ST cells. This MAb immunoprecipitated a 200 kDa non-glycosylated protein from lysates of ST cells, which was not precipitated by an anti-APN MAb. The 200 kDa protein was shown by immunostaining and fluorescence activated cell scanning to be present on ST cells and on villous enterocytes from newborn piglets, but not on MDBK cells or enterocytes from weaned piglets. APN was demonstrated by the same techniques to be present on villous enterocytes from both newborn and weaned piglets, as well as on ST cells. It was concluded that the 200 kDa protein may be a second receptor for TGEV, contributing to the high susceptibility of newborn piglets to the virus.",,"microsomal aminopeptidase; monoclonal antibody; virus receptor; animal cell; conference paper; controlled study; coronavirus; fluorescence activated cell sorter; intestine cell; intestine villus; jejunum; newborn; nonhuman; priority journal; swine; virus cell interaction; weaning; Aging; Animal; Animals, Newborn; Antibodies, Monoclonal; Antigens, CD13; Cell Line; Epithelium; Intestinal Mucosa; Jejunum; Molecular Weight; Receptors, Virus; Support, Non-U.S. Gov't; Swine; Transmissible gastroenteritis virus",,"Weingartl, H.M.; Veterinary Microbiol./Immunol. Dept., University of Guelph, Guelph, Ont. N1G 2W1, Canada",,,00652598,,AEMBA,"8830502","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028825238
"Den Boon J.A., Spaan W.J.M., Snijder E.J.","6701595706;7007172944;7006058325;","Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies",1995,"Virology","213","2",,"364","372",,18,"10.1006/viro.1995.0009","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028840838&doi=10.1006%2fviro.1995.0009&partnerID=40&md5=c9dac0489315ef3d06054787918c4a66","Department of Virology, Institute of Medical Microbiology, Leiden University, Netherlands","Den Boon, J.A., Department of Virology, Institute of Medical Microbiology, Leiden University, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, Netherlands; Snijder, E.J., Department of Virology, Institute of Medical Microbiology, Leiden University, Netherlands","The expression of the genetic information of equine arteritis virus (EAV), an arterivirus, involves the synthesis of six subgenomic (sg) mRNAs. These are 5' and 3' coterminal since they are composed of a leader and a body sequence, which are identical to the 5' and 3' ends of the genome, respectively. Previously, it has been suggested that cis-splicing of a genome-length precursor RNA is involved in their synthesis. This was reevaluated in a comparative analysis of the sg RNA synthesis of EAV, the coronavirus mouse hepatitis virus (MHV), and the alphavirus Sindbis virus. UV transcription mapping showed that the majority of the EAV sg RNAs made at later stages of infection is not derived from a genome-length precursor. However, complete independence of sg RNA synthesis from that of genomic RNA was never observed during the course of infection. The possibility that this resulted from UV irradiation-induced effects on the synthesis of the viral replicase was investigated by inhibiting translation using cycloheximide. For EAV, ongoing protein synthesis was found to be more important for the synthesis of sg RNA than for that of genomic RNA. In general, MHV transcription was extremely sensitive to translation inhibition, whereas EAV genomic RNA synthesis became independent of de novo protein synthesis late in infection. © 1995 Academic Press, Inc.",,,"Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Brzeski, H., Kennedy, S.I.T., Synthesis of alphavirus-speci- fied RNA (1978) J. Virol., 25, pp. 630-640; Chen, Z., Kuo, L., Rowland, R.R.R., Even, C., Faaberg, K.S., Plage-Mann, P.G.W., Sequence of 3’ end of genome and of 5’ end of ORF 1a of lactate dehydrogenase-elevating virus (LDV) and common junction motifs between 5’ leader and bodies of seven subgenomic mRNAs (1993) J. Gen. Virol., 74, pp. 643-660; Conzelmann, K.K., Visser, N., Woensel, P.V., Thiel, H.J., Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the arterivirus group (1993) Virology, 193, pp. 329-339; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol., 65, pp. 2910-2920; De Vries, A.A.F., Chirnside, E.D., Bredenbeek, P.J., Gravestein, L.A., Horzinek, M.C., Spaan, W.J.M., All subgenomic mRNAs of equine arteritis virus contain a common leader sequence (1990) Nucleic Acids Res., 18, pp. 3241-3247; De Vries, A.A.F., Chirnside, E.D., Horzinek, M.C., Rottier, P.J., Structural proteins of equine arteritis virus (1992) J. Virol., 66, pp. 6294-6303; Godeny, E.K., Chen, L., Kumar, S.N., Methven, S.L., Koonin, E.V., Brinton, M.A., Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (1993) Virology, 194, pp. 585-596; Godeny, E.K., Zeng, L., Smith, S.L., Brinton, M.A., Molecular characterization of the 3’ terminus of the simian hemorrhagic fever virus genome (1995) J. Virol., 69, pp. 2679-2683; Hofmann, M.A., Sethna, P.B., Brian, D.A., Bovine coronavi- rus mRNA replication continues throughout persistent infection in cell culture (1990) J. Virol., 64, pp. 4108-4114; Jacobs, L., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Synthesis of subgenomic mRNA’s of mouse hepatitis virus is initiated independently: Evidence from UV transcription mapping (1981) J. Virol., 39, pp. 401-406; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effects of subgenomic RNA transcription on RNA replication (1994) J. Virol., 66, pp. 3339-3346; Lai, M.M.C., Coronavirus Organization, replication and expression of genome. Annu (1990) Rev. MicroBiol., 44, pp. 303-333; Levis, R., Schlesinger, S., Huang, H.V., Promoter for Sindbis virus RNA-dependent subgenomic RNA transcription (1990) J. Virol., 64, pp. 1726-1733; Meulenberg, J.J.M., Hulst, M.M., De Meijer, E.J., Moonen, P.L.J.M., Den Besten, A., De Kluyver, E.P., Wensvoort, G., Moormann, R.J.M., Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS), is related to LDV and EAV (1993) Virology, 192, pp. 62-72; Meulenberg, J.J.M., De Meijer, E.J., Moormann, R.J.M., Subgenomic RNAs of Lelystad virus contain a conserved leader- bodyjunction sequence (1993) J. Gen. Virol., 74, pp. 1697-1701; Ou, J.H., Rice, C.M., Dalgarno, L., Strauss, E.G., Strauss, J.H., Sequence studies of several alphavirus genomic RNAs in the region containing the start of the subgenomic RNA (1982) Proc. Natl. Acad. Sci, 79, pp. 5235-5239. , USA; Plagemann, P.G.W., Moennig, V., Lactate dehydrogenase- elevating virus, equine arteritis virus and simian haemorrhagic fever virus, a new group of positive strand RNA viruses. Adv (1992) Virus Res., 41, pp. 99-192; Sauerbier, W., Hercules, K., Gene and transcription unit mapping by radiation effects. Annu (1978) Rev. Genet, 12, pp. 329-363; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Sethna, P.B., Hofmann, N.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain anti-leaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci, 86, pp. 5626-5630. , USA; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., Proteolytic processing of the replicase ORF1a protein of equine arteritis virus (1994) J. Virol., 68, pp. 5755-5764; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Spaan, W.J.M., Delius, H., Skinner, M., Armstrong, J., Rottier, P.J.M., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronavi- ruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stern, D.F., Sefton, B.M., Synthesis of coronavirus mRNAs: Kinetics of inactivation of infectious bronchitis virus RNA synthesis by UV light (1982) J. Virol., 42, pp. 755-759; Strauss, E.G., Rice, C.M., Strauss, J.H., Complete nucleotide sequence of the genomic RNA of Sindbis virus (1984) Virology, 133, pp. 92-110; Strauss, J.H., Strauss, E.G., The alphaviruses: Gene expression, replication, and evolution (1994) Microbiol. Rev, 58, pp. 491-562; Van Berlo, M.F., Horzinek, M.C., Van Der Zeijst, B.A.M., Equine arteritis virus-infected cells contain six polyadenylated virus- specific RNAs (1982) Virology, 118, pp. 345-352; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Yokomori, K., Banner, L.R., Lai, M.C., Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic-length template (1992) J. Virol., 66, pp. 4671-4678; Zeng, L., Godeny, E.K., Methven, S.L., Brinton, M.A., Analysis of simian hemorrhagic fever virus (SHFV) subgenomic RNAs, junction sequences, and 5’ leader (1995) Virology, 207, pp. 543-548","Snijder, E.J.; Department of Virology, Institute of Medical Microbiology, Leiden UniversityNetherlands",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028840838
"Truyen U., Parrish C.R., Harder T.C., Kaaden O.-R.","35300805300;7103173466;7102369501;7005855283;","There is nothing permanent except change. The emergence of new virus diseases",1995,"Veterinary Microbiology","43","2-3",,"103","122",,30,"10.1016/0378-1135(95)92531-F","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028799737&doi=10.1016%2f0378-1135%2895%2992531-F&partnerID=40&md5=b46f367d18929dc4920dac170db59521","Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig Maximilians University, Veterinaer Str. 13, D-80539 Munich, Germany; James A. Baker Institute for Animal Health, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Department of Virology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, Netherlands","Truyen, U., Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig Maximilians University, Veterinaer Str. 13, D-80539 Munich, Germany; Parrish, C.R., James A. Baker Institute for Animal Health, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Harder, T.C., Department of Virology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, Netherlands; Kaaden, O.-R., Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig Maximilians University, Veterinaer Str. 13, D-80539 Munich, Germany","The sudden appearance of apparently new viruses with pathogenic potential is of fundamental importance in medical microbiology and a constant threat to humans and animals. The emergence of a ""new"" pathogen is not an isolated event, as for instance the frequent appearance of new influenza virus strains demonstrates. Often the new virus strains co-circulate with the older strains in a susceptible population, but a replacement of the older strains has been also observed. In rare instances the new viruses can cause dramatic epidemics or pandemics, such as those observed with the human immunodeficiency virus, canine parvovirus, or most recently, with the agent of bovine spongiform encephalopathy in the United Kingdom. The mechanisms of the emergence are not always clearly understood, but an altered host range appears to be a common event. Whether a true change in host range occurs, or whether the virus adapted to the host and replicated more efficiently, is often unknown. This review tries to summarize the facts that are known about a wide variety of ""new"" viruses of mammals, such as the simian, human and feline lentiviruses, the feline coronaviruses, the feline parvoviruses, the carnivore morbilliviruses, the influenza A viruses, and the transmissible spongiform encephalopathies. A particular emphasis will be put on the genetic mechanisms that might have taken place and that might have been responsible for their sudden appearance. © 1995.","evolution; Virus","evolution; genetic analysis; nonhuman; review; virus classification; virus infection; Animal; Cats; Coronavirus; Evolution; Haplorhini; Human; Lentivirus; Morbillivirus; Orthomyxoviridae; Parvovirus, Feline; Prion Diseases; Animalia; Bovinae; Canine parvovirus; Felidae; Feline lentiviruses; Human immunodeficiency virus; Influenza A virus; Influenza virus; Mammalia; Morbillivirus; Parvovirus; Simiae","Allan, Viral evolution and AIDS (1992) J. NIH Res., 4, pp. 51-54; Appel, Scott, Carmichael, Isolation and immunization studies of a canine parvolike virus from dogs with haemorrhagic enteritis (1979) Vet. Rec., 105, pp. 156-159; Appel, Reggiardo, Summers, Pearce-Kelling, Mare, Noon, Redd, Örvell, Canine distemper virus infection and encephalitis in javelinas (collared peccaries) (1991) Arch. Virol., 119, pp. 147-152; Appel, Yates, Foley, Bernstein, Santinelli, Spelman, Miller, Summers, Canine distemper epizootic in lions, tigers, and leopards in North America (1994) J. Vet. Diagn. Invest., , submitted; Banner, Lai, Random nature of coronavirus RNA recombination in the absence of selection pressure (1988) Virology, 155, pp. 441-445; Barrett, Crowther, Osterhaus, Subbarao, Groen, Haas, Mamaev, Bostock, Molecular and serological studies on the recent seal epizootics in Europe and Siberia (1992) Sci. Total Environ., 115, pp. 117-132; Barrett, Visser, Mamaev, Goatley, van Bressem, Osterhaus, Dolphin and porpoise morbilliviruses are genetically distinct from phocine distemper virus (1993) Virology, 193, pp. 1010-1012; Bradley, Wilesmith, Epidemiology and control of bovine spongiform encephalopathy (BSE) (1993) British Med. Bull., 49, pp. 932-959; Chambers, Kawaoka, Webster, Protection of chickens from lethal influenza infection by vaccinia-expressed hemagglutinin (1988) Virology, 167, pp. 414-421; Chang, Sgro, Parrish, Multiple amino acids in the capsid structure of canine parvovirus coordinately determine the canine host range and specific antigenic and hemagglutination properties (1992) J. Virol., 66, pp. 6858-6867; Christianson, Ingersoll, Landon, Pfeiffer, Gerber, Characterization of a temperature sensitive feline infectious peritonitis coronavirus (1989) Arch. 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Microbiol., 16, pp. 219-230; Visser, Kumarev, Örvell, DeVries, Broeders, van de Bildt, Groen, Osterhaus, Comparison of two morbilliviruses isolated from seals during the outbreak of distemper in north western Europe and Siberia (1990) Arch. Virol., 111, pp. 149-164; Visser, van der Heijden, van de Bildt, Kenter, Örvell, Osterhaus, Fusion protein gene nucleotide sequence similarities, shared antigenic sites and genetic analysis suggest that phocid distemper virus type 2 and canine distemper virus belong to the same virus entity (1993) J. Gen. Virol., 74, pp. 1989-1994; Visser, van Bressem, de Swart, van de Bildt, Vos, van der Heijden, Saliki, Osterhaus, Characterization of morbilliviruses isolated from dolphins and porpoises in Europe (1993) J. Gen Virol., 74, pp. 631-641; Webster, Bean, Gorman, Chambers, Kawaoka, Evolution and ecology of influenza A viruses (1992) Microbiol. Rev., 56, pp. 152-179; Wilesmith, Wells, Cranwell, Ryan, Bovine spongiform encephalopathy: Epidemiological studies (1988) Vet. Rec., 123, pp. 638-644; Wyatt, Pearson, Smerdon, Gruffydd-Jones, Wells, Spongiform encephalopathy in a cat (1993) Vet. Rec., 126, p. 513","Truyen, U.; Institute for Medical Microbiology, Infectious and Epidemic Diseases, Ludwig Maximilians University, Veterinaer Str. 13, D-80539 Munich, Germany; email: u8a1102@sunmail.LRZ-Muenchen.DE",,,03781135,,VMICD,"7740750","English","Vet. Microbiol.",Review,"Final",,Scopus,2-s2.0-0028799737
"Bihun C.G., Percy D.H.","6506573763;16140219400;","Morphologic changes in the nasal cavity associated with sialodacryoadenitis virus infection in the Wistar rat.",1995,"Veterinary pathology","32","1",,"1","10",,16,"10.1177/030098589503200101","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029191320&doi=10.1177%2f030098589503200101&partnerID=40&md5=df26e8880836b4646b50cfa1b31d4e73","Department of Pathology, Ontario Veterinary College, University of Guelph, Canada","Bihun, C.G., Department of Pathology, Ontario Veterinary College, University of Guelph, Canada; Percy, D.H., Department of Pathology, Ontario Veterinary College, University of Guelph, Canada","A sequential study of lesions of the nasal cavity associated with sialodacryoadenitis virus (SDAV) infection was made in the laboratory rat. Wistar rats were intranasally inoculated with approximately 10(3) TCID50 of the coronavirus SDAV. Transverse sections of four regions of the nasal cavity from inoculated and control animals were examined by light microscopy and immunohistochemistry at 2, 4, 6, 8, 10, and 14 days postinoculation (PI). Lesions were observed in the following regions of the upper respiratory tract: respiratory epithelium, transitional epithelium, olfactory epithelium, nasolacrimal duct, vomeronasal organ, and the submucosal glands of the nasal passages. In general, in structures lined by ciliated epithelial cells, there was focal to segmental necrosis with exfoliation of affected cells and polymorphonuclear cell infiltration during the acute stages, progressing to squamous metaplasia during the reparative stages. Repair in these regions was essentially complete by 14 days PI. In the olfactory epithelium and the vomeronasal organ, there was interstitial edema with necrosis and exfoliation of epithelial cells and minimal to moderate inflammatory cell response during the acute stages. Residual reparative lesions were still evident in the olfactory epithelium, the columnar epithelium and neuroepithelium of the vomeronasal organ, and the nasolacrimal duct at 14 days PI. Viral antigen was demonstrated by immunohistochemistry in all regions during the acute stages of the disease, with the exception of the vomeronasal organ. In view of these findings, infections of the respiratory tract with viruses such as SDAV could have significant effects on functions such as olfaction and chemoreception for > or = 2 weeks postexposure in this species.",,"virus antigen; animal; animal disease; article; Coronavirus; epithelium; exocrine gland; germfree animal; immunohistochemistry; immunology; isolation and purification; lacrimal apparatus; male; necrosis; nose cavity; olfactory epithelium; pathology; pharynx; rat; rodent disease; time; virology; virus infection; Wistar rat; Animals; Antigens, Viral; Coronavirus Infections; Coronavirus, Rat; Epithelium; Exocrine Glands; Immunohistochemistry; Lacrimal Apparatus; Male; Nasal Cavity; Necrosis; Olfactory Mucosa; Pharynx; Rats; Rats, Wistar; Rodent Diseases; Specific Pathogen-Free Organisms; Time Factors",,"Bihun, C.G.",,,03009858,,,"7725592","English","Vet. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0029191320
"Smee D.F., Alaghamandan H.A., Ramasamy K., Revankar G.R.","7007104795;6603193216;15121544100;7102569995;","Broad-spectrum activity of 8-chloro-7-deazaguanosine against RNA virus infections in mice and rats",1995,"Antiviral Research","26","2",,"203","209",,23,"10.1016/0166-3542(94)00084-L","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028909886&doi=10.1016%2f0166-3542%2894%2900084-L&partnerID=40&md5=883efa19557d39ad306bd558b4910530","ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States","Smee, D.F., ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States; Alaghamandan, H.A., ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States; Ramasamy, K., ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States; Revankar, G.R., ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States","A novel nucleoside analog, 8-chloro-7-deazaguanosine (8-Cl-7-dzGuo), was evaluated for anti-RNA virus activity in rodents in parallel with the related compound 7-deaza-7-thia-8-oxoguanosine (7-dzTOGuo). Half-daily intraperitoneal (i.p.) doses of each substance administered 24 and 18 h prior to i.p. virus challenge protected the majority of mice infected with banzi, encephalomyocarditis, San Angelo, and Semliki Forest viruses at doses of 25, 50 and 100 mg/kg/day. These compounds at 100 mg/kg/day also protected most suckling rats infected intranasally with rat coronavirus. However, no survival benefit was afforded to treated mice infected intranasally with vesicular stomatitis virus. 8-Cl-7-dzguo was orally active against Semliki Forest virus in mice at 200 and 400 mg/kg/day, whereas 7-dzTOGuo is reported to not be effective orally. In uninfected mice, the two compounds induced similar amounts of interferon following i.p. injections. Interferon was induced by oral treatments with 8-Cl-7-dzGuo but not with 7-dzTOGuo. Fifty percent acute lethal doses to uninfected mice treated i.p. in half-daily doses for one day with 7-deazaguanosine (7-dzGuo), 7-dzTOGuo, and 8-Cl-7-dzGuo were 400, 600 and > 1600 (no mortality at this dose) mg/kg/day, respectively. Daily, i.p. treatments for 14 days with these substances (100 mg/kg/day) showed 7-dzGuo as 100% lethal and the other two substances at not toxic. By virtue of reduced toxicity and oral bioavailability, 8-Cl-7-dzGuo appears to have the greatest clinical potential as an interferon-inducing antiviral agent. © 1995.","7-Deazaguanosine; Alphavirus; Antiviral; Bunyavirus; Coronavirus; Flavivirus; Interferon inducer; Picornavirus","7 deaza 7 thia 8 oxoguanosine; 8 chloro 7 deazaguanosine; interferon; nucleoside analog; unclassified drug; alpha virus; animal experiment; animal model; antiviral activity; article; controlled study; intraperitoneal drug administration; mouse; nonhuman; oral drug administration; priority journal; rat; rna virus; virus infection; Animal; Antiviral Agents; Guanosine; Mice; Molecular Structure; Rats; RNA Viruses; Support, Non-U.S. Gov't; Virus Diseases; Alphavirus; Animalia; Coronavirus; Flavivirus; Orthobunyavirus; Picornaviridae; Rat coronavirus; RNA viruses; Rodentia; Semliki Forest virus; Thia; Vesicular stomatitis virus","Kunder, Kelly, Morahan, Biological response modifier-mediated resistance to herpesvirus infections requires induction of α/β interferon (1993) Antiviral Res., 21, pp. 129-139; Michael, Cottam, Smee, Robins, Kini, Alkylpurines as immunepotentiating agents (1993) Synthesis and antiviral activity of certain alkylguanines, 36, pp. 3431-3436. , J. Med. Chem; Morahan, Pinto, Stewart, Murasko, Brinton, Varying role of α/β interferon in the antiviral efficacy of synthetic immuno-modulators against Semliki Forest virus infection (1991) Antiviral Res., 15, pp. 241-254; Nagahara, Anderson, Kini, Dalley, Larson, Smee, Jin, Cottam, Thiazolo[45-d]pyrimidine nucleosides (1990) J Med Chem, 33, pp. 407-415. , J. Med. Chem; Ramasamy, Imamura, Robins, Revankar, A facile and improved synthesis of tubercidin and certain pyrrolo[2,3-d]pyrimidine nucleosides by the stereospecific sodium salt glycosylation procedure (1988) J. Heterocycl. Chem., 25, pp. 1893-1898; Sarzotti, Coppenhaver, Singh, Poast, Baron, The in vivo antiviral effect of CL246,738 is mediated by the independent induction of interferon-α and interferon-β (1989) J. Interferon Res., 9, pp. 265-274; Smee, Alaghamandan, Cottam, Sharma, Jolley, Robins, Broad-spectrum in vivo antiviral activity of 7-thia-8-oxoguanosine, a novel immunopotentiating agent (1989) Antimicrob. Agents Chemother., 33, pp. 1487-1492; Smee, Alaghamandan, Cottam, Jolley, Robins, Antiviral activity of the novel immune modulator 7-thia-8-oxoguanosine (1990) J. Biol. Response Modif., 9, pp. 24-32; Smee, Alaghamandan, Bartlett, Robins, Intranasal treatment of picornavirus and coronavirus respiratory infections in rodents using 7-thia-8-oxoguanosine (1990) Antiviral Chem. Chemother., 1, pp. 47-52; Smee, Alaghamandan, Jin, Sharma, Jolley, Roles of interferon and natural killer cells in the antiviral activity of 7-thia-8-oxoguanosine against Semliki Forest virus infections in mice (1990) Antiviral Res., 13, pp. 91-102; Smee, Alaghamandan, Gilbert, Burger, Jin, Sharma, Ramasamy, Robins, Immunoenhancing properties and antiviral activity of 7-deazaguanosine in mice (1991) Antimicrob. Agents Chemother., 35, pp. 152-157; Smee, Huffman, Gessaman, Huggins, Sidwell, Prophylactic and therapeutic activities of 7-thia-8-oxoguanosine against Punta Toro virus infections in mice (1991) Antiviral Res., 15, pp. 229-239; Smee, Cottam, Sharma, Kini, Revankar, Ojo-Amaize, Sidwell, Robins, Antiviral and immunoenhancing properties of 7-thia-8-oxoguanosine and related guanosine analogues (1992) Can. J. Infect. Dis., 3, pp. 41B-48B; Stringfellow, Kern, Kelsey, Glasgow, Suppressed response to interferon induction in mice infected with encephalomyocarditis virus, Semliki Forest virus, influenza A2 virus, Herpesvirus hominis type 2, or murnie cytomegalovirus (1977) J. Infect. Dis., 135, pp. 540-551","Smee, D.F.; ICN Nucleic Acid Research Institute, Costa Mesa, CA 92626, United States",,,01663542,,ARSRD,"7605116","English","Antiviral Res.",Article,"Final",,Scopus,2-s2.0-0028909886
"Falsey A.R., McCann R.M., Hall W.J., Tanner M.A., Criddle M.M., Formica M.A., Irvine C.S., Kolassa J.E., Barker W.H., Treanor J.J.","7003365074;7102761124;35416533700;7202127759;6603037162;7006308372;7006350076;7003722609;7201833309;35480003200;","Acute Respiratory Tract Infection in Daycare Centers for Older Persons",1995,"Journal of the American Geriatrics Society","43","1",,"30","36",,96,"10.1111/j.1532-5415.1995.tb06238.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028872298&doi=10.1111%2fj.1532-5415.1995.tb06238.x&partnerID=40&md5=12639ba6924b6b40c11b89c65a8b1a75","Department of Medicine, Rochester General Hospital, University of Rochester School of Medicine and Dentistry, United States; The Departments of Medicine, United States; The Departments Biostatistics; Community and Preventive Medicine, The University of Rochester School of Medicine and Dentistry, Rochester, New York, United States","Falsey, A.R., Department of Medicine, Rochester General Hospital, University of Rochester School of Medicine and Dentistry, United States; McCann, R.M., Department of Medicine, Rochester General Hospital, University of Rochester School of Medicine and Dentistry, United States; Hall, W.J., The Departments of Medicine, United States; Tanner, M.A., The Departments Biostatistics; Criddle, M.M., Department of Medicine, Rochester General Hospital, University of Rochester School of Medicine and Dentistry, United States; Formica, M.A., Department of Medicine, Rochester General Hospital, University of Rochester School of Medicine and Dentistry, United States; Irvine, C.S., The Departments Biostatistics; Kolassa, J.E., The Departments Biostatistics; Barker, W.H., Community and Preventive Medicine, The University of Rochester School of Medicine and Dentistry, Rochester, New York, United States; Treanor, J.J., The Departments Biostatistics","OBJECTIVE: To evaluate the rate of specific pathogens and clinical syndromes associated with acute respiratory tract infections (ARTI) in frail older persons attending daycare. DESIGN: Prospective descriptive study, without intervention. SETTING: Two sites of a senior daycare program providing all‐inclusive care for the older persons in Rochester, New York. PARTICIPANTS: Staff members and participants of the daycare. MEASUREMENTS: Demographic, medical, and physical findings were collected from older subjects at baseline and while ill with respiratory illnesses. Nasopharyngeal specimens for viral and Chlamydia culture and sputum for bacterial culture were obtained from subjects when ill. Acute and convalescent sera were also collected with each illness and examined for viral, chlamydial, and mycoplasma infection. MAIN RESULTS: One hundred sixty‐five illnesses were documented in 165 older daycare participants as well as 113 illnesses among 67 staff members during the 15‐month study. The rate of ARTI in the elderly group was 10.8 per 100 person months. The most common etiologies in both the staff and elderly participants were respiratory syncytial virus (RSV), Influenza A, and coronavirus. The etiologies of illnesses in the staff compared with those in elderly group were similar except that bacterial infections were significantly more common among the elderly (7% vs. 0, P = 0.05). Multiple pathogens were found to cocirculate within centers, and no clear outbreak of a predominant organism was noted. Cough and nasal congestion characterized most illnesses. The elderly experienced significantly more cough, dyspnea, and sputum production than did the staff. There were 10 hospitalizations related to respiratory infections and four deaths during the acute illness among the elderly group and none in staff. CONCLUSIONS: Acute respiratory infections are a common occurrence in both the staff and participants of a senior daycare center and are the cause of substantial morbidity in frail older persons. 1995 The American Geriatrics Society",,"acute respiratory tract disease; aged; article; bacterial infection; coronavirus; coughing; day care; dyspnea; elderly care; female; hospitalization; human; influenza virus a; major clinical study; male; morbidity; nose congestion; respiratory syncytial pneumovirus; respiratory tract infection; virus infection; Acute Disease; Aged; Aged, 80 and over; Allied Health Personnel; Chlamydophila pneumoniae; Comparative Study; Day Care; Enterovirus; Female; Frail Elderly; Human; Male; New York; Prospective Studies; Respiratory Tract Infections; Rhinovirus; Seasons; Support, U.S. Gov't, P.H.S.","Garibaldi, RA., Epidemiology of community‐acquired respiratory tract infections in adults: Incidence, etiology, and impact (1985) Am J Med, 78 (S6B), pp. 32-37; Falsey, AR., Non‐Influenza respiratory virus infection in long term care facilities (1991) Infect Control Hosp Epidemiol, 12, pp. 602-608; Goodman, RA, Orenstein, WA, Munro, TF, Impact of influenza A in a nursing home (1982) JAMA, 247, pp. 1451-1453; Monto, AS, Ullman, BM., Acute respiratory illness in an American community: The Tecumseh study (1974) JAMA, 227, pp. 164-169; Monto, AS, Cavallaro, JJ., The Tecumseh study of respiratory illness. II. Patterns of occurrence of infection with respiratory pathogens (1971) Am J Epidemiol, 94, pp. 280-289; Kane, RL, Illston, LH, Miller, NA., Qualitative analysis of the program of all‐inclusive care for the elderly (1992) Gerontologist, 32, pp. 771-780; Roblin, PM, Dumornay, W., Hammerschlag, MR., Use of HEp‐2 cells for improved isolation and passage of Chlamydia pneumoniae (1992) J Clin Microbiol, 30, pp. 1968-1971; Wang, SP, Kuo, CC, Grayston, JT., Formalized Chlamydia Trachomatis organisms as the antigen in the micro‐immunofluorescence (1979) J Clin Microbiol, 10, pp. 259-261; (1991) Center for Disease Control Vital and Health Statistics, 10 (184), p. 13; Reuben, FL, Dearwater, SR, Norden, CW, The Pittsburgh Good Health Study: Clinical infections in the non‐institutionalized geriatric age group; methods utilized and incidence of infection Am J Epidemiol; Loda, FA, Glezen, WP, Clyde, WA., Respiratory disease in group daycare (1972) Pediatrics, 49, pp. 428-437; Zaroukian, MH, Kashyap, GH, Wentworth, BB., Case report: Respiratory syncytial virus ‐ a cause of respiratory distress and pneumonia in adults (1988) Am J Med Sci, 295, pp. 218-227; Mathur, U., Bentley, DW, Hall, CB., Concurrent respiratory syncytial virus and influenza infections in the institutionalized elderly and chronically ill (1980) Ann Intern Med, 93, pp. 49-52; Sorvillo, FJ, Huie, SF, Strassburg, M., An outbreak of respiratory syncytial virus pneumonia in a nursing home for the elderly (1984) J Infect, 9, pp. 252-256; Falsey, AR, Treanor, JJ, Betts, RF, Viral respiratory infections in the institutionalized elderly: Clinical and epidemiologic findings (1992) J Am Geriatri Soc, 40, pp. 115-119; Fleming, DM, Cross, KW., Respiratory syncytial virus or influenza (1993) Lancet, 342, pp. 1507-1510; Larsen, HE, Reed, SE, Tyrrell, DA., Isolation of rhinoviruses and coronaviruses from 38 colds in adults (1980) Journal of Medical Virology, 5, pp. 221-229; Nicholson, KG, Baker, DJ, Farquhar, A., Acute respiratory tract viral illness and influenza immunization in homes for the elderly (1990) Epidemiol Infect, 105, pp. 609-618; Grayston, TJ., Infections caused by Chlamydia pneumoniae strain TWAR (1992) Clin Infect Dis, 15, pp. 757-763; Graman, PS, Hall, CB., Epidemiology and control of nosocomial viral infections (1989) Infect Dis Clin North Am, 3, pp. 815-841","Falsey, A.R.; Dept. of Medicine, Infectious Disease Unit, Rochester General Hospital, 1425 Portland Ave., Rochester, New York, 14621, United States",,,00028614,,,"7806736","English","J. Am. Geriatr. Soc.",Article,"Final",,Scopus,2-s2.0-0028872298
"Godfraind C., Langreth S.G., Cardellichio C.B., Knobler R., Coutelier - J.P., Dubois-Dalcq M., Holmes K.V.","56877631600;57190481052;6602071538;19735246800;7003918786;57204484178;7201657724;","Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus",1995,"Laboratory Investigation","73","5",,"615","627",,61,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028788246&partnerID=40&md5=e9365c4ae6a91476e554f796d3caf231","Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium","Godfraind, C., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Langreth, S.G., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Cardellichio, C.B., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Knobler, R., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Coutelier -, J.P., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Dubois-Dalcq, M., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium; Holmes, K.V., Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium","BACKGROUND: The receptor for the murine coronavirus mouse hepatitis virus (MHV)-A59, called MHVR or Bgp1a, is a glycoprotein in the carcinoembryonic antigen family of the Ig superfamily. Biliary glycoprotein (Bgp) isoforms play a role in cell adhesion, bile acid transport, and ecto-ATPase activity. MHV-resistant SJL/J mice express a different allele of Bgp1 called Bgp1b. Analysis of the tissue and cellular distribution of Bgp1 proteins can therefore provide new insight on both cellular functions and MHV-A59-induced pathogenesis. EXPERIMENTAL DESIGN: Bgp1 expression was analyzed in the digestive, respiratory, endocrine, urinary, and central nervous systems of adult BALB/c and SJL/J mice by immunocytochemistry and immunoelectron microscopy using a monoclonal Ab specific for the N-terminal domain of the Bgp1a proteins and polyclonal rabbit anti-Bgp1, which recognizes both the Bgp1a and Bgp1b proteins. The function of Bgp1 proteins as viral receptors was tested on tissue sections by a virus binding assay. MHV-A59 replication was analyzed by immunocytochemistry. RESULTS: Bgp1 expression was observed on membranes of epithelial cells (including hepatocytes, intestinal, endocrine, and respiratory epithelial cells), kidney proximal tubules, and endothelial cells in many tissues. It was usually localized at the apical pole of the cells and, when present, on the brush borders and the cilia. A new direct virus binding assay showed that MHV attachment onto cells correlates with Bgp1 expression. Viral infection was detected in hepatocytes, lymphoid tissue, and the exocrine pancreas but not in endocrine cells, enterocytes, kidney, or respiratory cells. In the central nervous system, no immunolabeling of neurons or glial cells was found with anti-Bgp1 Ab. CONCLUSIONS: Bgp1 proteins are present on BALB/c and SJL/J epithelia and endothelia. These glycoproteins might be involved in cell-to-cell contacts, for example between hepatocytes. On BALB/c mice, Bgp1a expression is consistent with the tropism of MHV-A59 for the liver. However, Bgp1a was also expressed on cells that were not infected by MHV-A59.","Adherence molecule; Immunocytochemistry; Immunoelectromicroscopy; Mouse hepatitis virus receptor","carcinoembryonic antigen; virus receptor; animal tissue; article; cell adhesion; cellular distribution; immunocytochemistry; mouse; nonhuman; priority journal; protein localization; receptor binding; tissue distribution; virus cell interaction; virus replication; Animal; Carcinoembryonic Antigen; Cell Adhesion Molecules; Cells, Cultured; Coronavirus Infections; Digestive System; Disease Susceptibility; Endocrine Glands; Glycoproteins; Immunohistochemistry; Kidney; Mice; Mice, Inbred BALB C; Microscopy, Immunoelectron; Murine hepatitis virus; Neuroglia; Receptors, Virus; Respiratory System; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.",,"Godfraind, C.; Pathology Laboratory, St. Luc Hospital, Catholic University of Louvain, Av. Hippocrate, 10, B-1200 Brussels, Belgium",,,00236837,,LAINA,"7474935","English","LAB. INVEST.",Article,"Final",,Scopus,2-s2.0-0028788246
"Sawicki S.G., Lu J.-H., Holmes K.V.","7004118344;55701377800;7201657724;","Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from the epigenetic expression of the MHV receptor",1995,"Journal of Virology","69","9",,"5535","5543",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029148439&partnerID=40&md5=3489d8f6f62fda98cf94506eb4546f2f","Department of Microbiology, Medical College of Ohio, Toledo, OH 43699-0008, United States","Sawicki, S.G., Department of Microbiology, Medical College of Ohio, Toledo, OH 43699-0008, United States; Lu, J.-H., Department of Microbiology, Medical College of Ohio, Toledo, OH 43699-0008, United States; Holmes, K.V., Department of Microbiology, Medical College of Ohio, Toledo, OH 43699-0008, United States","The A59 strain of taurine coronavirus mouse hepatitis virus (MHV) can cause persistent infection of 17C1-1 cells and other murine cell lines. Persistently infected cultures released large amounts of virus (107 to 108 PFU/ml) and were resistant to superinfection with MHV but not to infection with unrelated Semliki Forest and vesicular stomatitis viruses. The culture medium from persistently infected cultures did not contain a soluble inhibitor such as interferon that protected uninfected cells from infection by MHV or vesicular stomatitis virus. The persistent infection was cured if fewer than 100 cells were transferred during subculturing, and such cured cultures were susceptible to reinfection and the reestablishment of persistent infection. Cultures of 17C1-1 cells that had been newly cloned from single cells consisted of a mixture of MHV-resistant and -susceptible cells. 17C1-1/97 cells, which were cured by subcloning after 97 passages of a persistently infected culture over a 1-year period, contained 5 to 10% of their population as susceptible cells, while 17C1-1/402 cells, which were cured by subcloning after 402 passages over a 3-year period, had less than 1% susceptible cells. Susceptibility to infection correlated with the expression of MHV receptor glycoprotein (MHVR [Bgp1(a)]). Fluorescence-activated cell sorter analysis with antibody to MHVR showed that 17C1-1/97 cells contained a small fraction of MHVR-expressing cells. These MHVR-expressing cells were selectively eliminated within 24 h after challenge with MHV-A59, and pretreatment of 17C1-1/97 cells with monoclonal antibody CC1, which binds to the N-terminal domain of MHVR, blocked infection. We conclude that the subpopulation of MHVR-expressing cells were infected and killed in acutely or persistently infected cultures, while the subpopulation of MHVR-nonexpressing cells survived and proliferated. The subpopulation of MHVR-negative cells produced a small proportion of progeny cells that expressed MHVR and became infected, thereby maintaining the persistent infection as a steady-state carrier culture. Thus, in 17C1-1 cell cultures, the unstable or epigenetic expression of MHVR permitted the establishment of a persistent, chronic infection.",,"virus receptor; animal cell; article; cell strain 3t3; cell transfer; gene expression; infection sensitivity; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virus cell transformation; 3T3 Cells; Animal; Antibodies, Monoclonal; Clone Cells; Comparative Study; Disease Susceptibility; Flow Cytometry; Glycoproteins; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Receptors, Virus; Semliki forest virus; Species Specificity; Support, U.S. Gov't, P.H.S.; Vesicular stomatitis-Indiana virus; Virus Replication",,"Sawicki, S.G.; Department of Microbiology, Medical College of Ohio, Toledo, OH 43699-0008, United States",,,0022538X,,JOVIA,"7636998","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029148439
"Chen W., Baric R.S.","7409646434;7004350435;","Function of a 5'-end genomic rna mutation that evolves during persistent mouse hepatitis virus infection in vitro",1995,"Journal of Virology","69","12",,"7529","7540",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028838639&partnerID=40&md5=8f9d071ef535856f2d384bc6f1a18f05","Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Chen, W., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Baric, R.S., Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Persistently infected cultures of DBT cells were established with mouse hepatitis virus strain A59 (MHV-A59), and the evolution of the MHV leader RNA and 5' end of the genome was studied through 119 days postinfection. Sequence analysis of independent clones demonstrated an overall mutation frequency approaching 1.2 x 10-3 to 6.7 x 10-3. The rate of fixation of mutations was about 1.2 x 10-5 to 7.6 x 10-5 per nucleotide (nt) per day. In contrast to finding in bovine coronavirus, the MHV leader RNA sequences were extremely stable and did not evolve significantly during persistent infection. Rather, a 5' untranslated region (UTR) A-to-G mutation at nt 77 in the genomic RNA emerged by day 56 and accumulated until 50 to 80% of the genome-length molecules retained the mutation by 119 days postinfection. Although other 5'-end mutations were noted, only the nt 77 mutation was significantly associated with viral persistence in vitro. Mutations were also found in the 5' end of the p28 coding region, but no specific alterations accumulated in genome-length molecules through 119 days postinfection. The 5' UTR nt 77 mutation resulted in an 18-amino-acid open reading frame (ORF) upstream of the ORF 1a AUG start site. By in vitro translation assays, the small ORF was not translated into detectable product but the mutation significantly enhanced translation of the downstream p28 ORF about 2.5-fold. Variant viruses, containing either the nt 77 A-to-G mutation (V16-ATG+) or wild-type sequences at this locus (VI-ATG-), were isolated at 119 days postinfection. The variant viruses replicated more efficiently than wild- type virus and were extremely cytolytic in DBT cells, suggesting that the A- to-G mutation did not encode a nonlytic or attenuated phenotype. Consistent with the in vitro translation results, a significant increase (~3.5-fold) in p28 expression was also observed with the mutant virus (V16-ATG+) in DBT cells compared with that in wild-type controls. These data indicate that MHV persistence was significantly associated with mutation and evolution in the 5'-end UTR which enhanced the translation of the ORF 1a and potentially ORF 1b polyproteins which function in virus transcription and replication.",,"messenger rna; virus rna; animal cell; article; cattle; controlled study; evolution; gene mutation; mouse; murine hepatitis coronavirus; mutation rate; nonhuman; open reading frame; priority journal; rna sequence; rna translation; virus genome; virus infection; Amino Acid Sequence; Animal; Base Sequence; Cattle; Cell Line; Cloning, Molecular; Comparative Study; Coronavirus, Bovine; DNA Primers; Evolution; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Open Reading Frames; Polymerase Chain Reaction; Repetitive Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; Support, U.S. Gov't, P.H.S.",,"Baric, R.S.; Program in Infectious Diseases, Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States",,,0022538X,,JOVIA,"7494259","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028838639
"Yu W., Leibowitz J.L.","55473188900;7006843902;","Specific binding of host cellular proteins to multiple sites within the 3' end of mouse hepatitis virus genomic RNA",1995,"Journal of Virology","69","4",,"2016","2023",,49,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028965252&partnerID=40&md5=31b7f11e030f880ac82328de9df42374","Pathology/Laboratory Medicine Dept., Texas Univ. Health Sciences Center, P.O. Box 20708, Houston, TX 77225, United States","Yu, W., Pathology/Laboratory Medicine Dept., Texas Univ. Health Sciences Center, P.O. Box 20708, Houston, TX 77225, United States; Leibowitz, J.L., Pathology/Laboratory Medicine Dept., Texas Univ. Health Sciences Center, P.O. Box 20708, Houston, TX 77225, United States","The initial step in mouse hepatitis virus (MHV) RNA replication is the synthesis of negative-strand RNA from a positive-strand genomic RNA template. Our approach to begin studying MHV RNA replication is to identify the cis- acting signals for RNA synthesis and the proteins which recognize these signals at the 3' end of genomic RNA of MHV. To determine whether host cellular and/or viral proteins interact with the 3' end of the coronavirus genome, an RNase T1 protection/gel mobility shift electrophoresis assay was used to examine cytoplasmic extracts from mock- and MHV-JHM-infected 17Cl-1 murine cells for the ability to form complexes with defined regions of the genomic RNA. We demonstrated the specific binding of host cell proteins to multiple sites within the 3' end of MHV-JHM genomic RNA. By using a set of RNA probes with deletions at either the 5' or 3' end or both ends, two distinct binding sites were located. The first protein-binding element was mapped in the 3'-most 42 nucleotides of the genomic RNA [3' (+42) RNA], and the second element was mapped within an 86-nucleotide sequence encompassing nucleotides 171 to 85 from the 3' end of the genome (171-85 RNA). A single potential stem-loop structure is predicted for the 3' (+)42 RNA, and two stem-loop structures are predicted for the 171-85 RNA. Proteins interacting with these two elements were identified by UV-induced covalent cross-linking to labeled RNAs followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The RNA-protein complex formed with the 3'-most 42 nucleotides contains approximately five host polypeptides, a highly labeled protein of 120 kDa and four minor species with sizes of 103, 81, 70, and 55 kDa. The second protein-binding element, contained within a probe representing nucleotides 487 to 85 from the 3' end of the genome, also appears to bind five host polypeptides, 142, 120, 100, 55, and 33 kDa in size, with the 120-kDa protein being the most abundant. The RNA-protein complexes observed with MHV-infected cells in both RNase protection/gel mobility shift and UV cross-linking assays were identical to those observed with uninfected cells. The possible involvement of the interaction of host proteins with the viral genome during MHV replication is discussed.",,"cell protein; virus rna; animal cell; article; gene mapping; mouse; murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; protein cross linking; protein protein interaction; rna replication; virus cell interaction; virus replication; Animal; Base Sequence; Binding Sites; Cell Line; DNA Primers; Mice; Molecular Sequence Data; Murine hepatitis virus; Nucleic Acid Conformation; Protein Binding; RNA, Viral; RNA-Binding Proteins; Support, Non-U.S. Gov't; Ultraviolet Rays",,"Leibowitz, J.L.; Pathology/Laboratory Medicine Dept., Texas Univ. Health Sciences Center, P.O. Box 20708, Houston, TX 77225, United States",,,0022538X,,JOVIA,"7884846","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0028965252
"Van Heerden J., Mills M.G., Van Vuuren M.J., Kelly P.J., Dreyer M.J.","7201441435;7201488091;7004572625;8062615600;7101754016;","An investigation into the health status and diseases of wild dogs (Lycaon pictus) in the Kruger National Park.",1995,"Journal of the South African Veterinary Association","66","1",,"18","27",,59,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029265324&partnerID=40&md5=d6024db1298d27f463d1657953a7975d","Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.","Van Heerden, J., Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.; Mills, M.G., Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.; Van Vuuren, M.J., Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.; Kelly, P.J., Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.; Dreyer, M.J., Department of Infectious Diseases and Public Health, Faculty of Veterinary Science, Medical University of Southern Africa.","Many factors have been cited as possible reasons for the decline in the number of wild dogs (Lycaon pictus), but few studies have provided supportive data. Between 1990 and 1993, the dynamics of 10 wild dog packs in the southern district of the Kruger National Park in South Africa were monitored. Casual observations of the causes of disease and mortality in the entire population were also recorded. During the same period, 46 wild dogs were immobilised, weighed, and subjected to physical examination as well as the collection of blood and faecal specimens. External parasites were collected and blood smears were prepared. Serum specimens were subjected to routine blood chemistry analyses, hormone and serological assays and formalinised blood specimens and faeces were subjected to screening for endoparasites. The study population varied from 75 in 1990 to 123 in 1993 with a survival rate of 29.9% for pups, 64.3% for yearlings and 69% for adults. Eighty per cent or more of the population were under 4 years of age. The cause of death in all wild dogs in the Kruger National Park could be established only in a small number of cases. Lions were responsible for the death of 20/62 wild dogs and disease caused the death of 6/62 wild dogs. All immobilised dogs were in a good physical condition, but 85% of dogs had one or more skin lesions. Potential life-threatening lesions (bitewounds inflicted by other dogs and lesions inflicted by a snare) occurred in 4 dogs. One male dog had only one testicle in the scortum. Twenty-six (93%) blood smears were positive for gametocytes of Hepatozoon sp., presumably H. canis, and in 2 dogs trophozoites of Babesia canis were seen. Eighty-six per cent of the specimens were positive for Dipetalonema reconditum. All dogs were infested with ticks and Haemaphysalis leachi, Amblyomma hebraeum, A. marmoreum, Boophilus decoloratus, Rhipicephalus simus, R. evertsi, R. appendiculatus and R. zambesiensis were identified. Ctenocephalides sp. and Echidnophaga larina were also identified. Taenia sp., Toxascaris canis and Ancylostoma caninum were present in faecal specimens. Antibody titres to adenovirus (26/31), B. canis (6/15), canine para-influenza virus (21/31), coronavirus (20/31), Coxiella burnetti (8/29), reovirus Type 3 (9/31), Rickettsia conori/africae (27/29), rotavirus (16/31) and Toxoplasma gondii (16/16) were found. The average serum urea concentration was higher (16.4 mmol/e) than that described for captive wild dogs, but other biochemical parameters were generally in agreement with values reported for captive wild dogs.(ABSTRACT TRUNCATED AT 400 WORDS)",,"animal; animal disease; article; Carnivora; cause of death; enzyme linked immunosorbent assay; female; health status; male; physiology; skin disease; South Africa; Animals; Carnivora; Cause of Death; Enzyme-Linked Immunosorbent Assay; Female; Health Status; Male; Skin Diseases; South Africa",,"Van Heerden, J.",,,10199128,,,"7629782","English","J S Afr Vet Assoc",Article,"Final",,Scopus,2-s2.0-0029265324
"Eleouet J.-F., Rasschaert D., Lambert P., Levy L., Vende P., Laude H.","6602581440;7004067163;57213514921;7202296823;6601980639;7006652624;","Complete Sequence (20 Kilobases) of the Polyprotein-Encoding Gene 1 of Transmissible Gastroenteritis Virus",1995,"Virology","206","2", 71004,"817","822",,93,"10.1006/viro.1995.1004","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028897070&doi=10.1006%2fviro.1995.1004&partnerID=40&md5=a895374ff45f3c63dfbc31b33dd4f1f3","Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France","Eleouet, J.-F., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Rasschaert, D., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Lambert, P., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Levy, L., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Vende, P., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Laude, H., Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France","The entire nucleotide sequence of cloned cDNAs containing the 5′-untranslated region and gene 1 of Purdue-115 strain of transmissible gastroenteritis virus (TGEV) was determined. This completes the sequence of the TGEV genome, which is 28,579 nucleotides long. The gene 1 is composed of two large open reading frames, ORF1a and ORF1b, which contain 4017 and 2698 codons, respectively (stop excluded). A brief, three-codon-long ORF is present upstream of ORF1a. ORF1b overlaps ORF1a by 43 bases in the (-1) reading frame. In vitro experiments indicated that translation of the ORF1a/b polyprotein involves an efficient ribosomal frameshifting activity, as previously shown for other coronaviruses. Analysis of the predicted ORF1a and ORF1b translation products revealed that the putative functional domains identified in infectious bronchitis virus (IBV), mouse hepatitis virus (MHV) and human coronavirus 229E (HCV 229E) are all present in TGEV. The amino-terminal half of the ORFla product exhibits greater divergence then the carboxy-terminal half, including within the TGEV/HCV229E pair. The ORF1b protein is overall highly conserved among the above four coronaviruses, except a divergent region situated near the carboxy terminus. © 1995 Academic Press. All rights reserved.",,"protein; article; controlled study; gene sequence; nonhuman; open reading frame; priority journal; swine; Transmissible gastroenteritis virus; Avian infectious bronchitis virus; human coronavirus; Human coronavirus 229E; Murine hepatitis virus; Sus scrofa; Transmissible gastroenteritis virus","Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol, 67, pp. 6056-6063; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of thegenome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol, 68, pp. 57-77; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W.T., Weiss, S.R., Spaan, W., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59: A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res, 18, pp. 1825-1832; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Brown, J.D.K., Bcursnell, M.E.G., Binns, M.M., Tomley, F.M., Cloning and sequencing of the 5' terminal sequences from avian infectious bronchitis virus genomic RNA (1986) J. Gen. Virol, 67, pp. 221-228; Chomczynski, P., Sacchini, N., Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem, 162, pp. 156-159; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., Identification of polypeptides encoded in open reading frame 1 b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59 (1991) J. Virol, 65, pp. 3076-3082; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Weiss, S.R., Intracellular processing of the N-terminal ORF1 a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Dennis, D.E., Brian, D.A., RNA-dependent RNA polymerase activity in coronavirus-infected cells (1982) J. Virol, 42, pp. 153-164; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol, 65, pp. 2910-2920; Duarte, M., Gelfi, J., Lambert, P., Rasschaert, D., Laude, H., Genome organization of porcine epidemic diarrhea virus (1993) Coro-Naviruses, Molecular Biology and Virus-Host Interactions, 342, pp. 55-60. , H. Laude and J.-F. Vautherot, Eds.), Plenum, New York; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol, 66, pp. 3522-3530; Geballe, A.P., Morris, D.R., Initiation codons within 5'-leaders of mRNAs as regulators of translation (1994) Trends Biochem. Sci, 19, pp. 159-164; Godel, M., L’haridon, R., Vautherot, J.-F., Laude, H., TGEV coronavirus ORF-4 encodes a membrane protein that Is incorporated Into virions (1992) Virology, 188, pp. 666-675; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: P-edlction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4846-4861; Gorbalenya, A.E., Koonin, E.V., Viral proteins containing the purine NTP-binding sequence pattern (1989) Nucleic Acids Res, 17, pp. 8413-8440; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res, 21, pp. 5838-5842; Jacobs, L., Van Derzeijst, B.A.M., Horzinek, M.C., Characterization and translation of transmissible gastroenteritis virus mRNAs (1986) J. Virol, 57, pp. 1010-1015; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsld protein gene (1986) Virology, 151, pp. 41-49; Kozak, M., Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eucaryotic ribosomes (1986) Cell, 44, pp. 283-292; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Ann. Rev. Microbiol, 44, pp. 303-333; Laude, H., Chapsal, J.-M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol, 67, pp. 119-130; Laude, H., Rasschaert, D., Huet, J.C., Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol, 68, pp. 1687-1693; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brierley, I., Tibbies, K.W., Brown, T.D.K., A 100 kilodaltons polypeptide encoded by open reading frame (ORF) 1 b of the coronavirus infectious bronchitis virus is processed by ORF1a products (1994) J. Virol, 68, pp. 5772-5780; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Page, K.W., Britton, P., Boursnell, M.E.G., Sequence analysis of the leader RNA of two porcine coronaviruses: Transmissible gastroenteritis virus and porcine respiratory coronavirus (1990) Virus Genes, 4, pp. 289-301; Penzes, Z., Tibbies, K., Shaw, K., Britton, P., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Rasschaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol, 68, pp. 1883-1890; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organisation and expression (1987) Biochimie, 69, pp. 591-600; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol, 65, pp. 320-325; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J.M., Comparison of the genome organization of toro-and coronaviruses: Evidence for two nonhomologous RNA recombination events during Berne virus evolution (1991) Virology, 180, pp. 448-452; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M., Sequence and translation of the murine coronavirus 5'-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase (1987) J. Virol, 61, pp. 3968-3976; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.-L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3' end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res, 13, pp. 87-100; Wesley, R.D., Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain) (1990) Coronaviruses and Their Diseases, 276, pp. 301-306. , D. Cavanagh and T. D. K. Brown, Eds.), Plenum, New York","Laude, H.; IRNA, Laboratorie de Virologie et Immunologie Moléculaires, 78350 Jouy-en-Josas, France",,,00426822,,,"7856095","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028897070
"Jia W., Karaca K., Parrish C.R., Naqi S.A.","36851002600;6701729923;7103173466;7003290056;","A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains",1995,"Archives of Virology","140","2",,"259","271",,153,"10.1007/BF01309861","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029108556&doi=10.1007%2fBF01309861&partnerID=40&md5=c017c9b6a6a1bac0f92d1e0f69d2603a","Department of Avian and Aquatic Animal Medicine, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States; The James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States","Jia, W., Department of Avian and Aquatic Animal Medicine, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States; Karaca, K., Department of Avian and Aquatic Animal Medicine, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States; Parrish, C.R., The James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States; Naqi, S.A., Department of Avian and Aquatic Animal Medicine, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States","An antigenic variant of avian infectious bronchitis virus (IBV), a coronavirus, was isolated and characterized. This strain, CU-T2, possesses a number of unusual features, which have not been previously observed in IBV. The S1 glycoprotein of CU-T2 carries virus-neutralizing and serotype-specific epitopes of two IBV serotypes, Arkansas (Ark) and Massachusetts (Mass). Sequence analysis revealed that the virus, originally an Ark serotype, has acquired the Mass-specific epitope by mutation(s). This provides evidence that point mutations may lead to generation of IBV antigenic variants in the field. It was further observed that two independent recombination events involving three different IBV strains had occurred in the S2 glycoprotein gene and N protein gene of CU-T2, indicating that genomic RNA recombination in IBV may occur in multiple genes in nature. It was especially significant that a sequence of Holland 52 (a vaccine strain) had replaced half of the N gene of CU-T2. This proves that recombination among vaccine strains is contributing to the generation of IBV variants in the field. Based on these observations it is predicted that every IBV field isolate could have unique genetic nature. Therefore, several recently reported diagnostic and serotyping methods of IBV which are based on dot-blot hybridization, restriction fragment length polymorphism (RFLP), and polymerase chain reaction (PCR), may not reveal the true antigenic and/or genetic nature of IBV isolates, and may in fact yield misleading information. © 1995 Springer-Verlag.",,"complementary DNA; core protein; membrane protein; monoclonal antibody; spike glycoprotein, coronavirus; virus antigen; virus envelope protein; virus vaccine; animal; antigenic variation; article; Avian infectious bronchitis virus; chicken; classification; DNA sequence; genetic recombination; genetics; immunology; molecular genetics; nucleotide sequence; point mutation; sequence alignment; serotyping; virus capsid; virus gene; Animal; Antibodies, Monoclonal; Antigenic Variation; Antigens, Viral; Base Sequence; Capsid; Chickens; DNA, Complementary; Genes, Viral; Infectious bronchitis virus; Membrane Glycoproteins; Molecular Sequence Data; Point Mutation; Recombination, Genetic; Sequence Alignment; Sequence Analysis, DNA; Serotyping; Support, Non-U.S. Gov't; Viral Core Proteins; Viral Envelope Proteins; Viral Vaccines","Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Baric, R., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Binns, M.M., Boursnell, M.E.G., Cavanagh, D., Pappin, D.J.C., Brown, T.D.K., Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) J Gen Virol, 66, pp. 719-726; Binns, M.M., Boursnell, M.E.G., Tomley, F.M., Brown, T.D.K., Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) J Gen Virol, 67, pp. 2825-2831; Boots, A.M.H., Benaissa-Trouw, B.J., Hesselink, W., Rijke, E., Schrier, C., Hensen, E.J., Induction of anti-viral immune responses by immunization with recombination-DNA encoded avian coronavirus nucleocapsid protein (1992) Vaccine, 10, pp. 119-124; Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Sequencing of coronavirus IBV genomic RNA: three open reading frames in the 5′ ‘unique’ region of mRNA D (1985) J Gen Virol, 66, pp. 2253-2258; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequence of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J Gen Virol, 66, pp. 573-580; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J Gen Virol, 68, pp. 57-77; Cavanagh, D., Davis, P.J., Sequence analysis of strains of avian infectious bronchitis coronavirus isolated during the 1960s in the U.K. (1993) Arch Virol, 130, pp. 471-476; Cavanagh, D., Davis, P.J., Cook, J.K.A., Infectious bronchitis virus: evidence for recombination within the Massachusetts serotype (1992) Avian Pathology, 21, pp. 401-408; Cavanagh, D., Davis, P.J., Cook, J.K.A., Li, D., Kant, A., Koch, G., Location of the amino acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious bronchitis virus (1992) Avian Pathology, 21, pp. 33-43; Cavanagh, D., Davis, P.J., Pappin, D.J.C., Binns, M.M., Boursnell, M.E.G., Brown, T.D.K., Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor polypeptide of IBV strains Beaudette and M41 (1986) Virus Res, 4, pp. 133-143; Cavanagh, D., Davis, P.J., Darbyshire, J.H., Peter, R.W., Coronavirus IBV: virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or haemagglutination inhibiting antibody, or induce chicken tracheal protection (1986) J Gen Virol, 67, pp. 1435-1442; Cavanagh, D., Davis, P.J., Coronavirus IBV: removal of spike glycopolypeptide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells (1986) J Gen Virol, 67, pp. 1443-1448; Cowen, B.S., Hitcher, S.B., Serotyping of avian infectious bronchitis viruses by the virus-neutralization test (1975) Avian Dis, 19, pp. 583-595; Gelb, J., Jr, Wolff, J.B., Moran, C.A., Variant serotypes of infectious bronchitis virus isolated from commercial layer and broiler chickens (1991) Avian Dis, 35, pp. 82-87; Hopkins, S.R., Serological comparisons of strains of infectious bronchitis virus using plaque purified isolates (1974) Avian Dis, 18, pp. 231-239; Johnson, R.B., Marquardt, W.W., Newman, J.A., The neutralizing characteristics of strains of infectious bronchitis virus as measured by the constant-virus variable-serum method in chicken tracheal cultures (1973) Avian Dis, 17, pp. 518-523; Jungherr EL, Chomiak TW, Luginbuhl KH (1956) Immunologic differences in strains of infectious bronchitis. 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Assoc. 1956. pp 203–209; Karaca, K., Naqi, S.A., Gelb, J., Jr, Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Dis, 36, pp. 903-915; Keck, J.G., Matsushima, G.A., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J Virol, 62, pp. 1810-1813; Keck, J.G., Soe, L.H., Makino, S., Stolhlman, S.A., Lai, M.M.C., RNA recombination of murine coronaviruses: recombination between fusion-positive mouse hepatitis virus A59 and fusion-negative mouse hepatitis virus 2 (1988) J Virol, 62, pp. 1989-1998; King, D.J., Cavanagh, D., Avian infectious bronchitis (1991) Diseases of poultry, pp. 471-484. , B.W., Calnek, H.J., Barnes, C.W., Beard, W.M., Reid, H.W., Yoder, Jr, 9th edn., Iowa State University Press, Ames; Kusters, J.G., Jager, E.G., Niesters, H.G.M., van der Zeijst, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Kwon, H.M., Jackwood, M.W., Gelb, J., Jr, Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Dis, 37, pp. 194-202; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Lai, M.M.C., Baric, R.S., Makino, S., Kech, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J Virol, 56, pp. 449-456; Liao, C.L., Lai, M.M.C., RNA recombination in a coronavirus: recombination between viral genomic RNA and transfected RNA fragments (1992) J Virol, 66, pp. 6117-6124; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J Virol, 66, pp. 6143-6154; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J Virol, 57, pp. 729-737; Marquardt WW (1981) An overview of infectious bronchitis virus serotypes. 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Oct 20–21, Delmar, Maryland 1981; Nagano, H., Hashimoto, H., Tanaka, Y., Fujisaki, Y., Dot-blot hybridization using digoxigenin-labeled cDNA probe complementary to the S1 gene of avian infectious bronchitis virus permits discrimination between virus strains (1993) J Vet Med Sci, 55, pp. 735-738; Naqi, S.A., Karaca, K., Bauman, B., A monoclonal antibody-based antigen capture enzyme-linked immunosorbent assay for identification of infectious bronchitis virus serotypes (1993) Avian Pathology, 22, pp. 555-564; Siddell, S.G., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, H.D., MacNaughton, Pensaert, M., van der Zerjst, B.A.M., Coronaviridae (1983) Intervirology, 20, pp. 181-189; Stern, D.F., Sefton, B.M., Coronavirus proteins: structure and function of oligosaccharides of avian infectious bronchitis virus genome (1982) J Virol, 44, pp. 794-803; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Willia, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Analysis of a hypervariable region in the 3′ non-coding end of the infectious bronchitis virus genome (1993) Virus Res, 28, pp. 19-27; Zwaagstra, K.A., van der Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1992) J Clin Microbiol, 30, pp. 79-84","Jia, W.; Department of Avian and Aquatic Animal Medicine, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States",,"Springer-Verlag",03048608,,ARVID,"7710354","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0029108556
"Denison M.R., Hughes S.A., Weiss S.R.","7101971810;22956252200;57203567044;","Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59",1995,"Virology","207","1", 71085,"316","320",,45,"10.1006/viro.1995.1085","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028912686&doi=10.1006%2fviro.1995.1085&partnerID=40&md5=ab1ef3141551b5923208b136b47738fe","Department of Pediatrics and Microbiology and Immunology and the Elizabeth B. iamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232-2581, United States; Department of Microbiology, University of Pennsylvania Medical School, Philadelphia, PA, 19104, United States","Denison, M.R., Department of Pediatrics and Microbiology and Immunology and the Elizabeth B. iamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232-2581, United States; Hughes, S.A., Department of Microbiology, University of Pennsylvania Medical School, Philadelphia, PA, 19104, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania Medical School, Philadelphia, PA, 19104, United States","A 65-kDa protein has been detected in mouse hepatitis virus A59 (MHV-A59)-infected DBT cells using polyclonal antibodies directed against polypeptides encoded by the 5' 1.8 kb of gene 1. The presence of this 65-kDa protein (p65) was previously predicted from immunoprecipitation studies of gene 1 expression in MHV-A59-infected DBT cells with other antisera (1). p65 was rapidly labeled in virus-infected cells at late times of infection; however, its cleavage from the polyprotein was significantly delayed compared to the amino-terminal gene 1 polyprotein cleavage product, p28. Similar to p28, p65 was cleaved from the growing polyprotein without detectable intermediate precursors. Kinetic analysis of p65 with specific antibodies indicates that p65 is immediately adjacent to p28 in the gene 1 polyprotein. The proteolytic activity responsible for the carboxy-terminal cleavage of p65, as well as the function of the p65 protein, remains to be determined. © 1995 Academic Press, Inc.",,,"Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Oison, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., (1992) Virology, 189, pp. 274-284; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., (1993) J. Virol, 67, pp. 6056-6063; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., (1989) Nucleic Acids Res, 17, pp. 4847-4861; Breedenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charité, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., (1990) Nucleic Acids Res, 18, pp. 1825-1832; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadhzyan, A., Lai, M.M.C., (1991) Virology, 180, pp. 567-582; Bonilla, P., Gorbalenya, A., Weiss, S., (1994) Virology, 198, pp. 736-740; Leibowitz, J.L., Weiss, S.R., Paavola, E., Bond, C.W., (1982) J. Virol, 43, pp. 903-913; Denison, M.R., Perlman, S., (1986) J. Virol, 60, pp. 12-18; Denison, M., Perlman, S., (1987) Virology, 157, pp. 565-568; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., (1991) J. Virol, 65, pp. 3076-3082; Zoltick, P.W., Leibowitz, J.L., De Vries, J.R., Weinstock, G.M., Weiss, S.R., (1989) Gene, 85, pp. 413-420; Hughes, S.A., Denison, M.R., Bonilla, P.J., Leibowitz, J.L., Weiss, S.S., (1993) Coronaviruses; Molecular Biology and Virus- Host Interactions, 342, pp. 221-226. , H. Laude and J.-F. Vautherot, Eds, Plenum Press, New York; Pachuk, C.J., Breedenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., (1989) Virology, 171, pp. 141-148; Saborio, J.L., Pong, S.-S., Koch, G., (1974) J. Mol. Biol, 85, pp. 195-211; Weiss, S., Hughes, S., Bonilla, P., Turner, J., Leibowitz, J., Denison, M., (1994) Positive-Strand RNA Viruses, 9, pp. 349-358. , M. Brinton, C. Cal- isher, and R. Rueckert, Eds, Springer-Verlag, Vienna, Austria; Lawson, M.R., Semler, B., (1992) L, Virology, 191, pp. 309-320; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., (1989) J. Virol, 63, pp. 3693-3699; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M.M.C., (1987) J. Virol, 61, pp. 3968-3976; Lore, J., De Geus, B., Jackson, R., Pouwels, P., Enger-Valk, B., (1988) J. Gen. Virol, 69, pp. 1627-1636; Dougherty, W.G., Parks, T.D., Cary, S.M., Bazan, J.F., Fletterick, R.J., (1989) Virology, 172, pp. 302-310; Peters, S.A., Voorhorst, W.G.B., Wery, J., We Mink, J., Van Kämmen, A., (1992) Virology, 191, pp. 81-89","Denison, M.R.; Department of Pediatrics and Microbiology and Immunology and the Elizabeth B. iamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232-2581, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028912686
"Homberger F.R.","7003348988;","Sequence analysis of the nucleoprotein genes of three enterotropic strains of murine coronavirus",1995,"Archives of Virology","140","3",,"571","579",,13,"10.1007/BF01718432","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029111052&doi=10.1007%2fBF01718432&partnerID=40&md5=d22b41fa1e7a5936cea2605d26bb74a8","Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland","Homberger, F.R., Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland","The nucleotide sequences of the nucleoprotein genes of three enterotropic strains of the murine coronavirus mouse hepatitis virus (MHV-Y, MHV-RI and DVIM) were determined and compared with previously reported sequences of three polytropic (respiratory) strains (MHV-A59, MHV-JHM and MHV-S). Greater than 92% homology was found among the six strains by pair-wise comparison at the nucleotide level. The genes encoded proteins of 451 to 455 residues and the deduced amino acid sequences were more than 91% homologous. A unique deletion of twelve nucleotides was found at the carboxy terminus of MHV-Y and a three nucleotide deletion was found in MHV-RI, which corresponded to the one previously reported in MHV-A59 and MHV-S. Two internal open reading frames were found within the coding region of the nucleoprotein, the smaller one was specific for the enterotropic strains. It could potentially encode a truncated version of the hypothetical protein described for MHV-A59 and MHV-S. Sequence relationship of the N gene showed no correlation with tissue tropism and no sequence or even single amino acid change unique to either tropism group was found. This indicates that the nucleoprotein of MHV probably has no part in the determination of the primary tissue tropism of an MHV strain. The role of the potential internal protein warrants further investigation. © 1995 Springer-Verlag.",,"core protein; amino acid sequence; animal; article; chemistry; genetics; molecular genetics; mouse; Murine hepatitis coronavirus; nucleotide sequence; virus capsid; virus gene; Amino Acid Sequence; Animal; Base Sequence; Capsid; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Support, Non-U.S. Gov't; Viral Core Proteins","Artrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Barthold, S.W., Mouse hepatitis virus biology and epidemiology (1986) Viral and mycoplasmal infections of laboratory rodents: effect on biomedical research, pp. 571-601. , P.N., Bhatt, R.O., Jacoby, A.C., Morse, III, A.E., New, Academic Press, Orlando; Barthold, S.W., Smith, A.L., Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice (1987) Arch Virol, 81, pp. 103-112; Barthold, S.W., Smith, A.L., Duration of challenge immunity to coronavirus JHM in mice (1989) Arch Virol, 104, pp. 187-196; Barthold, S.W., Smith, A.L., Duration of mouse hepatitis virus infection: studies in immunocompetent and chemically immunosuppressed mice (1990) Lab Anim Sci, 40, pp. 133-137; Barthold, S.W., Smith, A.L., Lord, P.F.S., Bhatt, P.N., Jacoby, R.O., Main, A.J., Epizootic coronaviral typhlocolitis in suckling mice (1982) Lab Anim Sci, 32, pp. 376-383; Barthold, S.W., Smith, A.L., Povar, A.L., Enterotropic mouse hepatitis virus infection in nude mice (1985) Lab Anim Sci, 35, pp. 613-618; Barthold, S.W., Beck, D.S., Smith, A.L., Enterotropic coronavirus (mouse hepatitis virus) in mice: influence of host age and strain on infection and disease (1993) Lab Anim Sci, 43, pp. 276-284; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab Anim Sci, 43, pp. 15-28; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Hamm TE Jr, ed (1986) Complications of viral and mycoplasmal infections in rodent toxicology research and testing. Hemisphere Washington; Homberger, F.R., Maternally-derived passive immunity to enterotropic mouse hepatitis virus (1992) Arch Virol, 122, pp. 133-141; Homberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res, 31, pp. 49-56; Homberger, F.R., Barthold, S.W., Passively acquired challenge immunity to enterotropic coronavirus in mice (1992) Arch Virol, 126, pp. 35-43; Homberger, F.R., Smith, A.L., Barthold, S.W., Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J Clin Microbiol, 29, pp. 2789-2793; Homberger, F.R., Barthold, S.W., Smith, A.L., Duration and strain specificity of immunity to enterotropic mouse hepatitis virus (1992) Lab Anim Sci, 42, pp. 347-351; Kraft, V., Meyer, B., Seromonitoring in small laboratory animal colonies. A five year survey: 1984–1988 (1990) Z Versuchstierk, 33, pp. 29-35; Kunita, S., Tedara, E., Goto, K., Kagiyama, N., Sequence analysis and molecular detection of mouse hepatitis virus using the polymerase chain reaction (1992) Lab Anim Sci, 42, pp. 593-598; Kunita S, Zhang L, Homberger FR, Compton SR (1995) Characterization of two Enterotropic Murine Coronavirus Strain. Virus Res (in press); Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Lindsey, J.R., Prevalence of viral and mycoplasmal infections in laboratory rodents (1986) Viral and mycoplasmal infections of laboratory rodents: effect on biomedical research, pp. 801-808. , P.N., Bhatt, R.O., Jacoby, A.C., Morse, III, A.E., New, Academic Press, Orlando; Nelson, G.W., Stohlman, S.A., Localization of the RNA binding domain of MHV nucleocapsid protein (1993) J Gen Virol, 74, pp. 1975-1979; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Pfleiderer, M., Skinner, M.A., Siddell, S.G., Coronavirus MHV-JHM: nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res, 14, p. 6338; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., RNA-binding proteins of coronavirus MHV: detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning: a laboratory manual, , 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor; Skinner, M.A., Siddell, S.G., Coronavirus JHM: nucleotide sequence of the mRNA that encodes nuleocapsid protein (1983) Nucleic Acids Res, 11, pp. 5045-5054; Stohlman, S.A., Baric, R., Nelson, G.N., Soe, L.H., Welter, L.M., Dean, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid (1988) J Virol, 62, pp. 4288-4295; Stohlman, S.A., Bergmann, C., Cua, D., Wege, H., van der Veer, R., Location of antibody epitopes within the mouse hepatitis virus nucleocapsid protein (1994) Virology, 202, pp. 146-153; Sugiyama, K., Amano, Y., Hemagglutination and structural polypeptides of a new coronavirus associated with diarrhoea in infant mice (1980) Arch Virol, 66, pp. 95-105; Yie, Y., Wei, Z., Tien, P., A simplified and reliable protocol for plasmid DNA sequencing: fast miniprep and denaturation (1993) Nucleic Acids Res, 21, p. 361; Yokomori, K., Banner, L.R., Lai, M.M.C., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronavirus (1991) Virology, 183, pp. 647-657","Homberger, F.R.; Institute of Laboratory Animal Science, University of Zurich, Zurich, Switzerland",,"Springer-Verlag",03048608,,ARVID,"7733827","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0029111052
"Motokawa K., Hohdatsu T., Aizawa C., Koyama H., Hashimoto H.","7004136451;57197786893;7006086579;7402164528;55723256500;","Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I",1995,"Archives of Virology","140","3",,"469","480",,50,"10.1007/BF01718424","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029141098&doi=10.1007%2fBF01718424&partnerID=40&md5=3ace1815e276e83741edb61034f2faac","Department of Veterinary Infectious Diseases, School of Veterinary Medicine and Animal Sciences, Kitasato University, Japan; Department of Virology, Center of Basic Research, The Kitasato Institute, Tokyo, Japan","Motokawa, K., Department of Veterinary Infectious Diseases, School of Veterinary Medicine and Animal Sciences, Kitasato University, Japan; Hohdatsu, T., Department of Veterinary Infectious Diseases, School of Veterinary Medicine and Animal Sciences, Kitasato University, Japan; Aizawa, C., Department of Virology, Center of Basic Research, The Kitasato Institute, Tokyo, Japan; Koyama, H., Department of Veterinary Infectious Diseases, School of Veterinary Medicine and Animal Sciences, Kitasato University, Japan; Hashimoto, H., Department of Virology, Center of Basic Research, The Kitasato Institute, Tokyo, Japan","cDNA clones spanning the entire region of the peplomer (S) gene of feline infectious peritonitis virus (FIPV) type I strain KU-2 were obtained and their complete nucleotide sequences were determined. A long open reading frame (ORF) encoding 1464 amino acid residues was found in the gene, which was 12 residues longer than the ORF of the FIPV type II strain 79-1146. The sequences of FIPV type I and mainly FIPV type II were compared. The homologies at the N- (amino acid residues 1-693) and C- (residues 694-1464) terminal halves were 29.8 and 60.7%, respectively. This was much lower than that between FIPV type II and other antigenically related coronaviruses, such as transmissible gastroenteritis virus of swine and canine coronavirus. This supported the serological relatedness of the viruses and confirmed that the peplomer protein of FIPV type I has distinct structural features that differ from those of antigenically related viruses. © 1995 Springer-Verlag.",,"virus protein; virus vaccine; amino acid sequence; animal; article; cat; chemistry; Coronavirus; genetics; immunology; molecular cloning; molecular genetics; nucleotide sequence; sequence homology; virus gene; Amino Acid Sequence; Animal; Base Sequence; Cats; Cloning, Molecular; Coronavirus, Feline; Genes, Viral; Molecular Sequence Data; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Viral Proteins; Viral Vaccines","Cavanagh, D., Davis, P.J., Pappin, D.J., Binns, M.M., Boursnell, M.E., Brown, T.D., Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41 (1986) Virus Res, 4, pp. 133-143; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., van der Zeijst, B.A., Spaan, W.J., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J Gen Virol, 68, pp. 2639-2646; De Groot, R.J., ter Haar, R.J., Horzinek, M.C., van der Zeijst, B.A., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79–1146 (1987) J Gen Virol, 68, pp. 995-1002; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J., Sequence analysis of the 3′-end of the feline coronavirus FIPV 79–1146 genome: comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: evidence for markedly different peplomer glycoproteins (1987) J Virol, 61, pp. 2607-2613; Fiscus, S.A., Teramoto, Y.A., Functional differences in the peplomer glycoproteins of feline coronavirus isolates (1987) J Virol, 61, pp. 2655-2657; Hohdatsu, T., Nakamura, M., Ishizuka, Y., Yamada, H., Koyama, H., A study on the mechanism of antibody-dependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies (1991) Arch Virol, 120, pp. 207-217; Hohdatsu, T., Okada, S., Koyama, H., Characterization of mononoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch Virol, 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs); preparation of MAbs which discriminate between FIPV strain 79–1146 and FECV strain 79–1683 (1991) Vet Microbiol, 28, pp. 13-24; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J Vet Med Sci, 54, pp. 557-562; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J Gen Virol, 73, pp. 2849-2862; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect Immun, 37, pp. 1148-1155; Jacobs, L., De Groot, R.J., van der Zeijst, B.A., Horzinek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res, 8, pp. 363-371; Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein (1982) J Mol Biol, 157, pp. 105-132; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J Virol, 66, pp. 956-965; Olsen, C.W., A review of feline infectious peritonitis virus: molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet Microbiol, 36, pp. 1-37; Olsen, C.W., Corapi, W.V., Jacobson, R.H., Simkins, R.A., Saif, L.J., Scott, F.W., Identification of antigenic sites mediating antibody-dependent enhancement of feline infectious peretonitis virus infectivity (1993) J Gen Virol, 74, pp. 745-749; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infections peritonitis virus to coronaviruses of other species (1978) Arch Virol, 58, pp. 45-53; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am J Vet Res, 41, pp. 868-876; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv Exp Med Biol, 173, pp. 365-380; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79–1146 and 79–1683 (1984) Am J Vet Res, 45, pp. 2580-2585; Rasschaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J Gen Virol, 68, pp. 1883-1890; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M., Gebauer, F., Escribano, J.M., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Scott, F.W., Immunization against feline coronaviruses (1987) Adv Exp Med Biol, 218, pp. 569-576; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Vennema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd Jones, T., Horzinek, M.C., Spaan, W.J., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; von Heijne, G., Patterns of amino acids near signal-sequence cleavage sites (1983) Eur J Biochem, 133, pp. 17-21; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: comparisons with dengue hemorrhagic fever (1981) Comp Immunol Microbiol Infect Dis, 4, pp. 175-189; Wickner, W.T., Lodish, H.F., Multiple mechanisms of protein insertion into and across membranes (1985) Science, 230, pp. 400-407","Motokawa, K.; Department of Veterinary Infectious Diseases, School of Veterinary Medicine and Animal Sciences, Kitasato UniversityJapan",,"Springer-Verlag",03048608,,ARVID,"7733820","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0029141098
"Linden M., Greiff L., Andersson M., Svensson C., Akerlund A., Bende M., Andersson E., Persson C.G.A.","7202047803;7006426396;7402879512;7202512750;6701441885;7006668474;56763558000;35493943900;","Nasal cytokines in common cold and allergic rhinitis",1995,"Clinical and Experimental Allergy","25","2",,"166","172",,54,"10.1111/j.1365-2222.1995.tb01022.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028936931&doi=10.1111%2fj.1365-2222.1995.tb01022.x&partnerID=40&md5=7df1f0887b17318cdfb4acf6556ee5f5","Astra Draco AB, Box 34, S-221 00 Lund, Sweden","Linden, M., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Greiff, L., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Andersson, M., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Svensson, C., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Akerlund, A., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Bende, M., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Andersson, E., Astra Draco AB, Box 34, S-221 00 Lund, Sweden; Persson, C.G.A., Astra Draco AB, Box 34, S-221 00 Lund, Sweden","Coronavirus-induced common cold and allergen-induced rhinitis are characterized by nasal mucosal exudation of bulk blood plasma. The mucosal exudation process involves 'flooding' of the lamina propria with plasma-derived binding proteins and it is possible that subepithelial inflammatory cytokines and mediators may be moved by the exudate to the mucosal surface. In this study, we have analysed cytokine levels in nasal lavage (NAL) fluids from non-allergic subjects inoculated with coronavirus (n = 20) and from subjects with allergic (birch pollen) rhinitis subjected to additional allergen challenge (samples were obtained 35 min post challenge) in the laboratory (n = 10). Ten of the 20 inoculated subjects developed common cold and 10 remained healthy. Interferon-γ IFNγ), interleukin-1β (IL-1β), granulocyte-macrophage colony-stimulating factor (GM-CSF), IL-4, and IL-6 were analysed in unprocessed NAL fluids using immunoassays. The subjects who developed common cold had increased NAL fluid levels of IFNγ (P < 0.05) that correlated well with the symptoms (P < 0.001). IFNγ did not increase in subjects with allergic rhinitis. IL-1β levels were similar in NAL fluids obtained from all inoculated subjects. In the subjects with allergic rhinitis NAL fluid levels of both IL-1β and GM-CSF were increased (P < 0.05). GM-CSF was not detected in common cold. IL-4 and IL-6 were not detectable in any of the NAL fluids. The present cytokines may not only emanate from superficial mucosal cells. By aiding plasma exudation subepithelial cytokines may potentially also be retrieved on the mucosal surface. pur study provides original in vivo data supporting the notion that a TH-1 profile of cytokines, notably IFNγ, is present in viral infection and further supporting the view that GM-CSF is an important cytokine in allergic airways disease.",,"cytokine; gamma interferon; granulocyte macrophage colony stimulating factor; interleukin 1beta; interleukin 4; interleukin 6; adult; allergic rhinitis; article; clinical article; cold; controlled study; coronavirus; etiology; female; human; male; priority journal; virus infection; Adult; Comparative Study; Coronavirus; Coronavirus Infections; Cytokines; Hay Fever; Human; Male; Nasal Mucosa; Rhinitis; Support, Non-U.S. Gov't",,"Linden, M.; Astra Draco AB, Box 34, S-221 00 Lund, Sweden",,,09547894,,CLEAE,"7750009","English","CLIN. EXP. ALLERGY",Article,"Final",,Scopus,2-s2.0-0028936931
"Liao C.-L., Zhang X., Lai M.M.C.","7401957370;55715175900;7401808497;","Coronavirus Defective-Interfering RNA as an Expression Vector: The Generation of a Pseudorecombinant Mouse Hepatitis Virus Expressing Hemagglutinin-Esterase",1995,"Virology","208","1", 71155,"319","327",,30,"10.1006/viro.1995.1155","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028910967&doi=10.1006%2fviro.1995.1155&partnerID=40&md5=48352a012ec32ccb467d077d13284871","Howard Hughes Medical Institute, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States; Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States","Liao, C.-L., Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States; Zhang, X., Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States, Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States","We have developed an expression vector system using a defective-interfering (DI) RNA of mouse hepatitis virus (MHV), a prototype coronavirus, to deliver and express a foreign gene in MHV-infected cells. This vector contains an MHV intergenic sequence to promote the expression of foreign genes. In this study, we used this vector to introduce a hemagglutininesterase (HE) protein, an optional MHV structural protein, into the MHV-infected cells. The engineered HE protein could be efficiently incorporated into the virion which did not synthesize its own HE protein, thus generating a pseudorecombinant virus that expresses an exogenous HE protein. The engineered HE protein could be made distinguishable from the native protein by attaching an 8-amino-acid peptide tag at the carboxyl-terminus. Both the engineered and native HE proteins from the HE-producing virus train could be incorporated into the virion, thus generating phenotypically mixed virus parficles. We also showed that the HE-expressing DI RNA could be incorporated into viruses, and the engineered HE protein expressed in the infected cells for at least three serial virus passages. Furthermore, we have made two mutants, in which parts of the external domain of the HE protein have been deleted, to study the sequence requirements for the stable expression of HE and its incorporation into MHV virions. Although both of the mutant HE proteins could be expressed in the MHV-infected cells, they failed to be incorporated into virions, suggesting the importance of the extracellular domain of HE protein for its incorporation into virus particles. This vector system enabled the first successful incorporation of a selected coronaviral protein into virions and demonstrates its utility as an expression vector for studying the molecular biology of coronaviruses. © 1995 Academic Press. All rights reserved.",,"esterase; hemagglutinin; virus protein; animal cell; article; murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; rat; rna transcription; virion; virus expression; virus transcription; Animal; Defective Viruses; Genetic Vectors; Hemagglutinins, Viral; Mice; Murine hepatitis virus; Mutation; Reassortant Viruses; RNA, Viral; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Fusion Proteins; Animalia; Coronavirus; Hepatitis virus A; Murinae; Murine hepatitis virus","Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for the auto proteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol, 63, pp. 3693-3699; Bredenbeek, P.J., Frolov, I., Rice, C.M., Schlesinger, S., Sindbis virus expression vectors: Packaging of RNA replicons by using defective helper RNAs (1993) J. Virol, 67, pp. 6439-6446; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (Strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol, 66, pp. 3522-3530; Herrler, G., Durkop, I., Becht, H., Klenk, H.-D., The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor (1988) J. Gen. Virol, 69, pp. 839-846; Herrler, G., Rott, R., Klenk, H.-D., Mueller, H.-P., Shukla, A.K., Schauer, R., The receptor destroying enzyme of influenza C virus in neuraminate-O-acetylesterase (1985) EMBO. J, 4, pp. 1503-1506; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch, 44, pp. 298-302; Jang, S.K., Davies, M.V., Kaufman, R.J., Wimmer, E., Initiation of protein synthesis by internal entry of ribosomes into the 5' non-translated region of encephalomyocarditis virus RNA in vivo (1989) J. Virol, 63, pp. 1651-1660; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol, 66, pp. 1841-1848; La Monica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, pp. 883-888; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 585-680; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzyahdzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol, 66, pp. 6117-6124; Liao, C.-L., Lai, M.M.C., Requirement of the 5'-end genomic sequence as an upstream cis-acting element for coronavirus sub-genomic mRNA transcription (1994) J. Virol, 68, pp. 4727-4737; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective-interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol, 67, pp. 6110-6118; Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA2. Indications for RNA recombination between coronavirus and influenza C virus (1988) Virology, 166, pp. 415-422; Macnaughton, M.R., Davies, H.A., Nermut, M.V., Ribo-nucleoprotein-like structures from coronavirus particles (1978) J. Gen, Virol, 39, pp. 545-549; Makino, S., Ioo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. 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Virol, 68, pp. 328-337; Morris, V.L., Tieszer, C., Mackinnon, J., Percy, D., Characterization of coronavirus JHM variants isolated from Wistar Furth rats with a viral-induced demyelinating disease (1989) Virology, 169, pp. 127-136; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus strain A59 (1989) Virology, 171, pp. 141-148; Roger, G.N., Herder, G., Paulson, J.C., Klenk, H.-D., Influenza C virus uses 9-O-acetyl-W-neuraminic acid as high affinity receptor determinant for attachment to cells (1986) J. Biol. Chem, 261, pp. 5947-5951; Schultze, B., Herder, G., Bovine coronavirus uses J.V-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J. Gen. Virol, 73, pp. 901-906; Schultze, B., Wahn, K., Klenk, H.-D., Herder, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Shieh, C.-K., Lee, H.J., Yokomori, K., La Monica, N., Makino, S.P., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol, 63, pp. 3729-3736; Sturman, L., Holmes, K.V., The novel glycoproteins of coro-naviruses (1985) Trends Biochem. Sci, 10, pp. 17-20; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleo-capsid (1980) J. Virol, 33, pp. 449-462; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3'-end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. 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Virol, 68, pp. 4738-4746","Lai, M.M.C.; Department of Molecular Microbiology and Immunology, University of Southern California School of Medicine, Los Angeles, CA 90033-1054, United States",,,00426822,,,"11831714","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028910967
"Liu D.X., Tibbles K.W., Cavanagh D., Brown T.D.K., Brierley I.","8972667300;6507790687;26642890500;56248391000;7004639098;","Identification, Expression, and Processing of an 87-kDa Polypeptide Encoded by ORF 1a of the Coronavirus Infectious Bronchitis Virus",1995,"Virology","208","1", 71128,"48","57",,33,"10.1006/viro.1995.1128","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028968134&doi=10.1006%2fviro.1995.1128&partnerID=40&md5=c59141d80d65a2cd275d7a0c35ad120a","Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom; Institute for Animal Health, Compton Laboratory, Compton, Berkshire, Newbury, RG16 ONN, United Kingdom","Liu, D.X., Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom; Tibbles, K.W., Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Berkshire, Newbury, RG16 ONN, United Kingdom; Brown, T.D.K., Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom; Brierley, I., Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom","Nucleotide sequence analysis has shown previously that the genomic-length mRNA (mRNA1) of the coronavirus infectious bronchitis virus (IBV) contains two large open reading frames (ORFs), 1a and 1b, with the potential to encode polyproteins of approximately 441 and 300 kDa, respectively. We have characterized the specificity of a set of region-specific antisera raised against the 5′-portion of ORF 1a by immunoprecipitation of in vitro-synthesized, C-terminally truncated 1a polypeptides and used these antisera to detect virus-specific proteins in IBV-infected Vero cells. Two antisera, which had specificity for IBV sequences from nucleotides 710 to 2079 and 1355 to 2433, respectively, immunoprecipitated a polypeptide of approximately 87 kDa from IBV-infected Veto cells. In vitro translation of ORF 1a sequence terminating at nucleotide 5763 did not produce this protein unless the in vitro translation products were incubated with Vero cell S10 extracts prepared from either IBV-infected or mock-infected Vero cells. However, processing of the 87-kDa protein was also observed when the same region was expressed in Vero cells using the vaccinia virus/T7 expression system. This observation indicates that the 87-kDa polypeptide is encoded within the 5′-most 3000 nucleotides of mRNA 1 and that it might be cleaved from the 1a polyprotein by viral and cellular proteinases. © 1995 Academic Press. All rights reserved.",,"virus protein; animal cell; article; avian infectious bronchitis virus; coronavirus; nonhuman; open reading frame; polymerase chain reaction; priority journal; protein determination; protein processing; vero cell; virus expression; Animal; Cercopithecus aethiops; Genome, Viral; Infectious bronchitis virus; Open Reading Frames; Support, Non-U.S. Gov't; Vero Cells; Viral Proteins; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Vaccinia; Vaccinia virus","Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol, 63, pp. 3693-3699; Baker, S.C., Yolomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-tike cysteine proteinase of murine coronavirus (1993) J. Virol, 67, pp. 6056-6063; Blair, W.S., Li, X., Semler, B.L., A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor (1993) J. Virol, 67, pp. 2339-2343; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J Gen. Virol, 68, pp. 57-77; Briertey, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus (1987) IBV. EMBO. J, 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Rolley, N.J., Brown, T.D.K., Inglis, S.C., Products of the polymerase-encoding region of the coronavirus IBV (1990) Adv. Exp. Med. Biol, 276, pp. 275-278; Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K.V., Lai, M.M.C., Laude, H., Siddell, S.G., Talbot, P.J., Recommendations of the coronavirus study group for the nomenclature of the structural proteins, mRNAs, and genes of coro-naviruses (1990) Virology, 176, pp. 306-307; Chambers, T.J., Hahn, C.S., Galler, R., Rice, C.M., Flavivirus genome organization, expression, and replication (1990) Anno. Rev. Microbiol, 44, pp. 649-688; Contreras, R., Cheroutre, H., Degrave, W., Fiers, W., Simple efficient in vitro synthesis of capped RNA useful for direct expression of cloned DNA (1982) Nucleic Acids Res, 10, pp. 6353-6362; Denison, M.R., Zoltic, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Dorner, A., Semler, B.L., Jackson, R.J., Hanecak, R., Duprey, E., Wimmer, E., In vitro translation of poliovirus RNA: Utilization of internal initiation sites in reticulocyte lysate (1984) J. Virol, 50, pp. 507-514; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev, 57, pp. 781-822; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4847-4860; Herald, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Laemmli, U.K., Cleavage of structural proteins during the assembly of the bacteriophage T4 (1970) Nature, 227, pp. 680-685. , London; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycis-tronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Inglis, S.C., Identification of two new polypeptides encoded by mRNA5 of the coronavirus infectious bronchitis virus (1992) Virology, 186, pp. 342-347; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol, 66, pp. 6143-6154; Liu, D.X., Gompels, U.A., Nicholas, J., Lelliot, C., Identification and expression of the human herpesvirus 6 glycoprotein H and interaction with an accessory 40kDa glycoprotein (1993) J. Gen. Virol, 74, pp. 1847-1857; Liu, D.X., Brierley, I., Tibbies, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol, 68, pp. 5772-5780; Lomniczi, B., Biological properties of avian coronavirus RNA (1977) J. Gen. Virol, 36, pp. 531-533; Schochetman, G., Stevens, R.H., Simpson, R.W., Presence of infectious polyadenylated RNA in the coronavirus avian bronchitis virus (1977) Virology, 77, pp. 772-782; Smith, A.R., Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Inglis, S.C., Identification of a new membrane-associated polypeptide specified by the coronavirus infectious bronchitis virus (1990) J. Gen. Virol, 71, pp. 3-11; Smith, G.L., Vaccinia virus glycoproteins and immune evasion (1993) J. Gen. Virol, 74, pp. 1725-1740; Stern, D.F., Kennedy, S.I.T., Coronavirus multiplication strategy. Identification and characterisation of virus specified RNA species to the genome (1980) J. Virol, 34, pp. 665-674; Stern, D.F., Kennedy, S.I.T., Coronavirus multiplication strategy. II. Mapping the avian infectious bronchitis virus intracellular RNA species to the genome (1980) J. Virol, 36, pp. 440-449; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Location of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol, 50, pp. 22-29","Liu, D.X.; Department of Pathology, Division of Virology, University of Cambridge, Tennis Court Road, Cambridge, CB2 IQP, United Kingdom",,,00426822,,,"11831730","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028968134
"Taguchi F., Kubo H., Takahashi H., Suzuki H.","7103209890;55183402000;7405469520;7407715967;","Localization of neurovirulence determinant for rats on the S1 subunit of murine coronavirus JHMV",1995,"Virology","208","1", 71130,"67","74",,12,"10.1006/viro.1995.1130","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028955228&doi=10.1006%2fviro.1995.1130&partnerID=40&md5=f74a35f7b1384bb3d44196aceb691d60","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Kubo, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Takahashi, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Suzuki, H., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","A cloned virus of murine coronavirus JHMV, cl-2, was shown to be highly neurovirulent for rats in comparison with other JHMV variants. We have isolated cl-2-derived variant viruses resistant to neutralization by monoclonal antibodies (MAbs) specific for the spike (S) protein of cl-2. The variants MM6 and MM13, selected by the MAbs specific for the JHMV S protein, were revealed to have a point mutation located within the N-terminal 100 amino acids (aa) of the S1 protein. The variants MM56, MM85, and MM78, selected by MAbs specific for the larger S protein of JHMV, were shown to have a deletion composed of about 150 aa located in the middle of the S1 subunit (MM56 and MM85) or one amino acid deletion, aspartic acid at number 543 from the N-terminus of the S1 (MM78). These five MAb-resistant variants were not different from cl-2 in growth pattern on cultured DBT cells. MM6 and MM13 were shown to be highly neurovirulent for 4-week-old Lewis rats, growing to high titers in the brain and causing as high an incidence of neurological disease and death as the parental cl-2. In contrast, MM56 and MM85 were nonneurovirulent for rats. They did not cause any central nervous system disorders nor did they multiply in the rat brains. MM78 showed intermediate neurovirulence as well as intermediate growth potential in the rat brain. However, there was no apparent difference in neurovirulence between the parental and the MAb-resistant variants for mice; all of these viruses showed high neurovirulence for mice. These results suggest that the domain composed of about 150 aa in the middle of the S1 is critical for high neurovirulence of JHMV for rats. Furthermore, it is suggested that the neurovirulence of cl- 2 for mice is controlled by a different viral factor. © 1995 Academic Press, Inc.",,,"Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. 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Virol, 59, pp. 463-471; Evans, D.M.A., Minor, P.D., Schild, G.C., Almond, J.W., Critical role of an eight amino acid sequence of VP1 in neutralization of poliovirus type 3 (1983) Nature, 304, pp. 459-462. , London; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated and has a reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol, 58, pp. 869-875; Fleming, J.O., Trousdale, M.D., Bradbury, J., Stohlman, S.A., Weiner, L.P., Experimental demyelination induced by coronavirus JHM (MHV-4); Molecular identification of a viral determinant of paralytic disease (1987) Microb. 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Virol, 54, pp. 429-435; Taguchi, F., Yamada, A., Fujiwara, K., (1980) Resistance to Highly Virulent Mouse Hepatitis Virus Acquired by Mice after low-virulence infection; Enhanced Antiviral Activity of Macrophages, Infect Immun, 29, pp. 42-49; Wang, F.L., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants-. Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, H., Siddell, S.G., Ter Meulen, V., The biology and pathogenesis of coronavi ruses (1982) Curr. Top. Microbiol. Immunol, 99, pp. 185-200; Wege, H., Watanabe, R., Ter Meulen, V., Relapsing subacute demyelinating encephalomyelitis in rats during the course of coronavirus JHM infection (1984) J. NeuroImmunol, 6, pp. 325-336; Wege, H., Winter, J., Meyermann, R., The pepiomer protein E2 of coronavirus JHM as a determinant of neurovirulence; Definition of critical epitopes by variant analysis (1988) J. Gen. Virol, 69, pp. 87-98; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proa Waff. Acad. Sci, USA, 88, pp. 5533-6536; Winship, P.R., An improved method for directly sequencing PCR material using dimethyl sulfoxide (1989) Nucleic Acids Res, 17, pp. 12-66; Yamada, Y.K., Abe, M., Yamada, A., Taguchi, F., Detection of mouse hepatitis virus by the polymerase chain reaction and its application to the rapid diagnosis of infection (1993) Lab. Anim. Sci, 43, pp. 285-290; Yokomori, K., Stohlman, S.A., Lai, M.M.C., The detection and characterization of multiple hemagglutinin-esterase (HE)-defec-tive viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028955228
"Suiter B.T., Pfeiffer N.E., Jones E.V., Reed A.P., Klepfer S.R., Miller T.J., Srikumaran S.","6506647769;7005189966;7404237166;7202692665;6507963520;57198615518;7004307545;","Serological recognition of feline infectious peritonitis virus spike gene regions expressed as synthetic peptides and E. coli fusion protein",1995,"Archives of Virology","140","4",,"687","702",,2,"10.1007/BF01309958","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029139975&doi=10.1007%2fBF01309958&partnerID=40&md5=6eb1a83631a575e6e4d3ca9d34ad0801","Biological Research and Development, SmithKline Beecham Animal Health, Lincoln, Nebraska, United States; Department of Veterinary Science, University of Nebraska, Lincoln, Nebraska, United States; Molecular Genetics, SmithKline Beecham Animal Health, King of Prussia, Pennsylvania, United States","Suiter, B.T., Biological Research and Development, SmithKline Beecham Animal Health, Lincoln, Nebraska, United States, Department of Veterinary Science, University of Nebraska, Lincoln, Nebraska, United States; Pfeiffer, N.E., Biological Research and Development, SmithKline Beecham Animal Health, Lincoln, Nebraska, United States; Jones, E.V., Molecular Genetics, SmithKline Beecham Animal Health, King of Prussia, Pennsylvania, United States; Reed, A.P., Molecular Genetics, SmithKline Beecham Animal Health, King of Prussia, Pennsylvania, United States; Klepfer, S.R., Molecular Genetics, SmithKline Beecham Animal Health, King of Prussia, Pennsylvania, United States; Miller, T.J., Molecular Genetics, SmithKline Beecham Animal Health, King of Prussia, Pennsylvania, United States; Srikumaran, S., Department of Veterinary Science, University of Nebraska, Lincoln, Nebraska, United States","Cats exposed to feline infectious peritonitis virus (FIPV) or feline enteric coronavirus (FECV) cannot be differentiated by serological analysis. Three synthetic peptides and an E. coli recombinant fusion protein generated from FIPV 79-1146 spike gene sequence were produced. Coronavirus positive cat sera reacted to peptide aa 950-990 but were non-reactive to aa137-151 and aa 150-180 peptides as demonstrated by ELISA. Amino acid sequence 97-222 expressed as a galk fusion protein in E. coli was tested against coronavirus positive cat sera by western blot analysis. Only sera from cats exposed to the FIPV type-II strains DF-2 or 79-1146 that were exhibiting signs of FIP recognized the fusion protein. Sera from FECV exposed cats did not recognize the 97-222 fusion protein in western blot analysis. © 1995 Springer-Verlag.",,"hybrid protein; membrane protein; peptide; spike glycoprotein, coronavirus; virus envelope protein; virus hemagglutinin; animal; article; cat; cat disease; Coronavirus; cross reaction; enzyme linked immunosorbent assay; Escherichia coli; genetics; immunology; molecular cloning; rabbit; serology; synthesis; Western blotting; Animal; Blotting, Western; Cats; Cloning, Molecular; Coronavirus, Feline; Cross Reactions; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Feline Infectious Peritonitis; Hemagglutinins, Viral; Membrane Glycoproteins; Peptides; Rabbits; Recombinant Fusion Proteins; Serology; Viral Envelope Proteins","Birnboim, H.C., Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA (1979) Nucleic Acids Res, 7, p. 1513; Chou, P.Y., Fasman, G., Prediction of the secondary structure of proteins from their amino acid sequence (1978) Annu Rev Immunol, 2, pp. 67-101; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A., Spaan, M.J., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J Gen Virol, 68, pp. 2639-2646; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van der Zeijst, B.A., Spaan, W.J., Lenstra, J.A., Evidence for a coiled-coil structure in the spike proteins of coronaviruses (1987) J Mol Biol, 196, pp. 963-966; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis girus. II. domains in the peplomer glycoprotein (1986) J Gen Virol, 67, pp. 1405-1418; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the vax (1984) Nucleic Acids Res, 12, pp. 387-395; Emini, E.A., Hughes, J.V., Perlow, D.S., Boger, J., Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide (1983) J Virol, 55, pp. 836-83; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolated: evidence for markedly different peplomer glycoproteins (1987) J Virol, 61, pp. 2607-2613; Garnier, J., Osguthorpe, D.J., Robson, B., Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular protein (1978) J Mol Biol, 120, pp. 97-120; Gerber, J.D., Pfeiffer, N.E., Ingersoll, J.D., Chistianson, K.K., Landon, R.M., Selzer, N.L., Beckenhauer, W.H., Characterization of an attenuated temperature sensitive feline infectious peritonitis vaccine virus (1990) Coronaviruses and their diseases, pp. 481-489. , Plenum Press, New York; Gerber, J.D., Ingersoll, J.D., Gast, A.M., Christianson, K.K., Selzer, N.L., Landon, R.M., Pfeiffer, N.E., Beckenhauer, W.H., Protection against feline infectious peritonitis by intranasal inoculation of a temperature-sensitive FIPV vaccine (1990) Vaccine, 8, pp. 536-542; Hopp, T.P., Woods, K.R., Prediction of protein antigenic determinants from amino acid sequences (1981) Proc Natl Acad Sci USA, 78, pp. 3824-3828; Jacobs, L., Groot, R., Van der Zeijst, B.A., Horzinek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TEGV): comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res, 8, pp. 363-371; Jameson, B.A., Wolf, H., The antigenic index: a novel algorithm for predicting antigenic determinants (1988) Comput Appl Biosci, 4, pp. 181-186; Karplus, P.A., Schulz, G.E., Prediction of chain flexibility in proteins (1985) Naturwissenschafter, 72, pp. 212-213; Kusters, J.G., Jager, E.J., Lenstra, J.A., Koch, G., Posthumus, W.P., Meloen, R.H., Van der Zeijst, B.A., Analysis of an immunodominant region of infectious bronchitis virus (1989) J Immunol, 145, pp. 2692-2698; Kusters, J.G., Niesters, G.M., Lenstra, J.A., Horzinek, M.C., Van der Zeijst, B.A., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lerner, R.A., Chemically synthesized peptides from the nucleotide sequence of the hepatitus-B virus genome elicit antibodies reactive with the native envelope protein of dane particles (1981) Proc Natl Acad Sci USA, 78, pp. 3403-3407; Liu, F.T., New procedures for preparation and isolation of conjugates of proteins and a synthetic copolymer of D-amino acids and immunochemical characterization of such conjugates (1979) Biochemistry, 18, pp. 690-693; Luytjes, W., Geerts, D., Posthumus, W., Meloen, R., Spaan, W., Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses (1989) J Virol, 63, pp. 1408-1412; Merrifield, R.B., Solid phase peptide synthesis: the synthesis of a tetrapeptide (1963) J Am Chem Soc, 85, pp. 2149-2154; Maniatis, T., Sambrook, J., Fritsch, E.F., (1989) Molecular cloning, a laboratory manual, , 2nd edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor; Mitraki, A., King, J., Protein folding intermediates and inclusion body formation (1989) Biol Tech, 7, pp. 690-697; Pedersen, N.C., Boyle, J.F., Floyd Km Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1980) Am J Vet Res, 42, pp. 368-377; Pedersen NC, Floyd K (1985) Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4. In: Viral disease of small animals. 34th Annual Symposium, Continuing Education Article #5, Vol 7, No 12: pp 1001–1011; Posthumus, W.P., Lenstra, J.A., Schaaper, W.M., Nieuwstadt, A.P., Enjuanes, L., Meloen, R.H., Analysis and simulation of a neutralizing epitope of transmissible gastroenteritis virus (1990) J Virol, 64, pp. 3304-3309; Reed P, Klepfer S, Jones EV, Pfeiffer NE, Suiter BT, Miller TJ (1991) Recombinant feline coronavirus S proteins. WO 93US365; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc Natl Acad Sci USA, 74, pp. 5463-5467; Talbot, P.J., Buchmeier, M.J., Antigenic variation among murine coronaviruses: evidence for polymorphism on the peplomer glycoprotein, E2 (1985) Virus Res, 2, pp. 317-328; Talbot, P.J., Dionne, G., Lacroix, M., Vaccination against lethal coronavirus-induced encephalitis with a synthetic decapeptide homologous to a domain in the predicted peplomer stalk (1988) J Virol, 62, pp. 3032-3036; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose: procedure and some applications (1979) Proc Natl Acad Sci USA, 76, pp. 4350-4354; Vennema, H., Groot, R.J., Harbour, D.A., Dalderup, M., Jones, T.G., Horzinek, M.C., Spaan, W.J., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409","Suiter, B.T.; Biological Research and Development, SmithKline Beecham Animal Health, Lincoln, Nebraska, United States",,"Springer-Verlag",03048608,,ARVID,"7794112","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0029139975
"Xue S., Jaszewski A., Perlman S.","7202791284;16156813900;7102708317;","Identification of a CD4+ T cell epitope within the M protein of a neurotropic coronavirus",1995,"Virology","208","1", 71140,"173","179",,39,"10.1006/viro.1995.1140","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028966897&doi=10.1006%2fviro.1995.1140&partnerID=40&md5=ea0dd6450880958f8a6ca089fadd674f","Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Xue, S., Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Jaszewski, A., Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Departments of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","A significant CD4+ T cell response against the transmembrane (M) protein can be detected in the spleens of C57Bl/6 mice infected intraperitoneally with a sublethal injection of the neurotropic JHM strain of mouse hepatitis virus (MHV-JHM), but not in those of mice with the chronic demyelinating encephalomyelitis caused by this virus. With the ultimate goal of determining the role of the M-specific response in the pathogenesis of MHV-JHM-induced neurological diseases, CD4+ T cell epitopes within the M protein were identified using vaccinia virus recombinants expressing truncated forms of the protein and peptides spanning most of the M protein in cell proliferation assays. Peptides covering residues 128-147 contain at least one CD4+ T cell epitope for MHV-JHM. Within this region is a sequence (residues 135-143) which matches the recently described MHC class II I-Ab binding motif. Delineation of this epitope should facilitate analysis of the role of the M- specific CD4+ T cell response in the development of acute and chronic neurological infections caused by MHV-JHM. © 1995 Academic Press, Inc.",,,"Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (Strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Castro, R., Evans, G.D., Jaszewski, A., Perlman, S., Coronavi-rus-induced demyelination occurs in the presence of virus-specific cytotoxic T cells (1994) Virology, 200, pp. 733-743; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci, 43, pp. 15-28; Flory, E., Pfleiderer, M., Stuhler, A., Wege, H., Induction of protective immunity against coronavirus-induced encephalomyelitis: Evidence for an important role of CD8+ T cells in vivo (1993) Eur. J. Immunol, 23, pp. 1757-1761; Friedmann, A., Frankel, G., Lorch, Y., Steinman, L., Monoclonal anti-l-A antibody reverses chronic paralysis and demyelination in Theiler's virus-infected mice: Critical importance of timing of treatment (1987) J. Virol, 61, pp. 898-903; Gammon, G., Geysen, H.M., Apple, R.J., Pickett, E., Palmer, M., Amet-Ani, A., Sercarz, E., T cell determinant structure: Cores and determinant envelopes in three mouse major histocompatibility complex haplotypes (1991) J. Exp. Med, 173, pp. 609-617; Gerety, S., Rundell, M.K., Del Canto, M.C., Miller, S.D., Class ll-restricted T cell response in Theiler’s murine encephalomyelitis virus-induced demyelinating disease (1994) J. Immunol, 152, pp. 919-929; Haspel, M.V., Lampert, P.W., Oldstone, M.B.A., Temperature-sensitive mutants of mouse hepatitis virus produce a high incidence of demyelination (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 4033-4036; Imrich, H., Schwender, S., Hein, A., Dörries, R., Cervical lymphoid tissue but not the central nervous system supports proliferation of virus-specific T lymphocytes during coronavirus-induced encephalitis in rats (1994) J. Neuroimmunot, 53, pp. 73-81; Kono, D., Urban, I., Florvath, S., Ando, D., Saavedra, R., Flood, L., Two minor determinants of myelin basic protein induce experimental allergic encephalomyelitis in SJL/J mice (1988) J. Exp. Med, 168, pp. 213-227; Körner, H., Schliephaks, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S., Wege, H., Nucleocapsid or spike protein-specific CD4+ T lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CD8+ T cells (1991) J. Immunol, 147, pp. 2317-2323; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Sem. Virol, 1, pp. 273-280; Lampert, P.W., Sims, J.K., Kniazeff, A.J., Mechanism of demyelination in JHM virus encephalomyelitis (1973) Acta Neuropathoi, 24, pp. 76-85; Mobley, J., Evans, G., Dailey, M.O., Perlman, S., Immune response to a murine coronavirus: Identification of a homing receptor-negative CD4+ T cell subset that responds to viral glycoproteins (1992) Virology, 187, pp. 443-452; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol, 68, pp. 5483-5495; Perlman, S., Ries, D., The astrocyte is a target cell in mice persistently infected with mouse hepatitis virus, strain JHM (1987) Microb. Pathog, 3, pp. 309-314; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating encephalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog, 2, pp. 185-194; Pfleiderer, M., Skinner, M.A., Siddell, S.G., Coronavirus MHV-JHM: Nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res, 14, p. 6338; Rudensky, A., Preston-Hulbert, P., Al-Ramadi, B., Rothbard, J., Janeway, C., Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs (1992) Nature, 359, pp. 429-431; Stohlman, S.A., Kyuwa, S., Polo, J.M., Brady, D., Lai, M.M.C., Bergmann, C.C., Characterization of mouse hepatitis virus-specific cytotoxic T cells derived from the central nervous system of mice infected with the JHM strain (1993) J. Virol, 67, pp. 7050-7059; Stohlman, S.A., Matsushima, G.K., Casteel, N., Weiner, L.P., In vivo effects of coronavirus-specific T cell clones: DTH inducer cells prevent a lethal imection but do not inhibit virus replication (1986) J. Immunol, 136, pp. 3052-3056; Wahren, B., Rober, K.-H., Nordlund, S., Conditions for cytomegalovirus stimulation of lymphocytes. Scand (1981) J. Immunol, 13, pp. 581-586; Wall, K.A., Hu, J.-Y., Currier, P., Southwood, S., Sette, A., Infante, A., A disease-related epitope of Torpedo acetylcholine receptor: Residues involved in l-Ab binding, self-nonself discrimination, and TCR antagonism (1994) J. Immunol, 152, pp. 4526-4536; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologi-cally mediated (1990) J. NeuroImmunol, 30, pp. 31-41; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol, 28, pp. 298-303; Williamson, J.S., Sykes, K.C., Stohlman, S.A., Characterization of brain-infiltrating mononuclear cells during infection with mouse hepatitis virus strain JHM (1991) J. NeuroImmunol, 32, pp. 199-207; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. NeuroImmunol, 32, pp. 1-9","Perlman, S.; Departments of Microbiology, University of Iowa, Iowa City, IA 52242, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028966897
"Kim J.C., Spence R.A., Currier P.F., Lu X., Denison M.R.","7601384560;16168043100;36889539200;56137171400;7101971810;","Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d",1995,"Virology","208","1", 71123,"1","8",,73,"10.1006/viro.1995.1123","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028907271&doi=10.1006%2fviro.1995.1123&partnerID=40&md5=723cb058269556a32047b392b4c2b30c","Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States","Kim, J.C., Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Spence, R.A., Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Currier, P.F., Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Lu, X., Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States; Denison, M.R., Departments of Pediatrics, Microbiology, Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt Medical School, Nashville, TN 37232-2581, United States","Mouse hepatitis virus strain A59 (MHV-A59) encodes within the 22-kb gene 1 a large polyprotein containing three proteinase domains with proven or predicted cysteine catalytic residues E64d, a specific, irreversible inhibitor of cysteine (thiol) proteinases, inhibits the processing of the gene 1 polyprotein. Specifically, E64d blocks the carboxy-terminal cleavage of p65. E64d also inhibits replication of MHV-A59 in routine DBT cells in a dose-dependent manner, resulting in reduced virus titers and viral syncytia formation. This inhibition of replication is associated with a rapid shutoff of new viral RNA synthesis, in a manner similar to that seen in the presence of cycloheximide. The E64d-associated inhibition of RNA synthesis likely results from E64d-specific inhibition of processing of the gene 1 polyprotein, resulting in inactive proteinase or replicase proteins. These results indicate that processing of the MHV-A59 gene 1-encoded polyprotein is required throughout infection to sustain RNA synthesis and virus replication. © 1995 Academic Press, Inc.",,,"Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol, 67, pp. 6056-6063; Boursnell, M.F.G., Brown, T.D.K., Foulcs, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol, 68, pp. 57-77; Breedenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res, 18, pp. 1825-1832; Chomczynski, P., Solubilization informamide protects RNA from degradation (1992) Nucleic Acids Res, 20, pp. 3791-3792; Denison, M., Perlman, S., Identification of a putative polymerase gene product in cells infected with murine coronavirus A59 (1987) Virology, 157, pp. 565-568; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65 kilodalton protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. Virol, 60, pp. 12-18; Denison, M.R., Ross, T., Gombold, J., Inhibition of Mouse Hepatitis Virus A59 Replication by the Protease Inhibitor, Leupeptin (1992) Am. Soc. Virol, , Cornell University, Ithaca, NY; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF1a proteins of the coronavirus MHV- A59 requires multiple proteoiytic events (1992) Virology, 189, pp. 274-284; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59 (1991) J. Virol, 65, pp. 3076-3082; Furuya, T., Lai, M.M., Three different cellular proteins bind to complementary sites on the 5'-end positive and 3'-end negative strands of mouse hepatitis virus RNA (1993) J. Virol, 67, pp. 7215-7222; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural poiyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS Lett, 288, pp. 201-205; Hirano, N., Fujiwara, K., Matumoto, M., Mouse hepatitis virus (MHV-2); plaque assay and propagation in mouse cell line DBT cells (1976) Jpn. J. Microbiol, 20, pp. 219-225; Hughes, S.A., Denison, M.R., Bonilla, P.J., Leibowitz, J.L., Weiss, S.S., (1993) Coronaviruses: Molecular Biology and Virus-Host Interactions, pp. 221-226. , H. Laude and J.-F. Vautherot, Eds, Plenum, New York; Kleina, L.G., Grubman, M.J., Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus (1992) J. Virol, 66, pp. 7168-7175; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lee, H.J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadhzyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., Weiss, S.R., Paavola, E., Bond, C.W., Cell- free translation of murine coronavirus RNA (1982) J. Virol, 43, pp. 903-913; Mehdi, S., Cell-penetrating inhibitors of calpain (1991) Trends Biochem. Sci, 16, pp. 150-153; Rasband, W., NIH Image 1, 55 (1994) Internet via Anonymous Ftp at Zippy.Nimh.Nih.Gov; Sawicki, D.L., Sawicki, S.G., Coronavirus minus-strand RNA synthesis and effect of cyctoheximide on coronavirus RNA synthesis (1986) J. Viroi, 57, pp. 328-334; Weiss, S., Hughes, S., Bonilla, P., Turner, J., Leibowitz, J., Denison, M., (1994) Positive-Strand RNA Viruses, pp. 349-358. , M, Brinton, C. Calisher, and R. Rueckert, Eds, Springer-Verlag, Vienna","Denison, M.R.; Lamb Center for Pediatric Research, Vanderbilt Medical School, D7235 MCN, Nashville, TN 37232-2531, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028907271
"Shchetinina V.N., Panchenko L.A., Volianskiǐ I.L.","57193145347;7103100652;57215952720;","The structure and immunobiological properties of coronavirus proteins [Struktura i immunobiologicheskie svoǐstva belkov koronavirusov.]",1995,"Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993)","57","3",,"98","112",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029299189&partnerID=40&md5=6b26325fc3eab4d3de8beef3f0154256",,"Shchetinina, V.N.; Panchenko, L.A.; Volianskiǐ, I.L.","The survey includes data concerning structural proteins of coronaviruses obtained for the last ten years. It elucidates such problems as the proteins organization in the virion, heterogeneity of their composition, structure and biological properties, antigenic and immunobiological properties, prospects of creation of specific immunogenic anticoronavirus, prophylactic and diagnostic preparations.",,"virus antigen; virus protein; chemistry; Coronavirus; immunity; immunology; review; virion; Antigens, Viral; Coronavirus; English Abstract; Immunity; Viral Proteins; Virion",,"Shchetinina, V.N.",,,,,,"7655661","Russian","Mikrobiol Z",Review,"Final",,Scopus,2-s2.0-0029299189
"Liao C.-L., Lai M.M.C.","7401957370;7401808497;","A cis-Acting Viral Protein Is Not Required for the Replication of a Coronavirus Defective-Interfering RNA",1995,"Virology","209","2", 71275,"428","436",,21,"10.1006/viro.1995.1275","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029036798&doi=10.1006%2fviro.1995.1275&partnerID=40&md5=0f7f36b5797c3aed5228cee4d5433b6d","Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States; Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, CA 90033-1054, United States","Liao, C.-L., Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States, Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, CA 90033-1054, United States","Mouse hepatitis virus (MHV), a coronavirus, generates defective-interfering (DI) RNAs of different sizes during passages at high multiplicities of infection. All MHV DI RNAs characterized so far contain an open reading frame (ORF) encoding a fused viral protein; in addition, DI RNAs with a long ORF have a competitive advantage over those with a shorter ORF. These findings suggest that DI RNA replication may require an ORF encoding a cis-acting viral protein. In this study, we used a naturally occurring DI RNA and inserted a 12-nucleotide (nt) amber-mutation linker at various positions to truncate the ORF. Most of the mutants replicated as well as the wild-type DI RNA, irrespective of the presence or absence and the length of the ORF in the RNA. Sequence analysis showed that all of the mutants retained the insertional mutations even after two viral passages in tissue culture, establishing that the mutant DI RNAs replicated. We have further introduced two 3-nucleotide substitutions of the first two AUG codons of the ORF, thus completely closing the ORF. This DI RNA replicated as well as the wild-type DL but, after a single passage, the majority of the mutant RNAs was replaced by recombinant RNAs which contain a restored functional ORF. However, an additional insertion of a 12-nt amber-mutation linker downstream of the AUG substitutions prevented recombination, and the DI RNA still replicated. These data indicate that DI RNA replication does not require a DI-specific ORF encoding cis-acting viral proteins and that a 12-nucleotide insertion could prevent or delay the occurrence of RNA recombination, suggesting the importance of direct or indirect RNA alignment in homologous RNA recombination. © 1995 Academic Press. All rights reserved.",,"virus protein; amino acid substitution; animal cell; article; codon; gene deletion; gene sequence; genetic transcription; mouse; nonhuman; open reading frame; priority journal; rna sequence; virus activation; virus genome; virus replication; Animal; Astrocytoma; Base Sequence; Cell Line; Defective Viruses; DNA Primers; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Open Reading Frames; Plasmids; Polymerase Chain Reaction; Restriction Mapping; RNA, Viral; Sequence Deletion; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Transfection; Translation, Genetic; Tumor Cells, Cultured; Viral Proteins; Virus Replication; Animalia; Coronavirus; Hepatitis virus A; Murine hepatitis virus","Akklna, R.K., Chambers, T.M., Nayak, D.P., Expression of defective-interfering influenza virus-specific transcripts and polypeptides in infected cells (1984) J. Virol, 51, pp. 395-440; Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteoiytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol, 63, pp. 3693-3699; Collis, P.S., O’Donnell, B.J., Barton, D.J., Rogers, J.A., Flanegan, J.B., Replication of poliovirus RNA and subgenomic RNA transcripts in transfected cells (1992) J. Virol, 65, pp. 6480-6488; De Groot, R.J., Van Der Most, R.G., Spaan, W., The fitness of defective interfering murine coronavirus Dl-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol, 66, pp. 5898-5905; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. Virol, 60, pp. 12-18; Furuya, T., Macnaughton, T.B., La Monica, N., Lai, M.M.C., Natural evolution of coronavirus defective-interfering RNA involves RNA recombination (1993) Virology, 194, pp. 408-413; Hagino-Yamagishi, K., Nomoto, A., In vitro construction of poliovirus defective interfering particles (1989) J. Virol, 63, pp. 5386-5392; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virus Forsch, 44, pp. 298-302; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol, 68, pp. 2615-2623; Kamen, R.I., Structure and function of the Q (1975) RNA Phages, pp. 203-234. , N. D. Zinder, Ed, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; Kaplan, G., Racanlello, V.R., Construction and characterization of poliovirus subgenomic replicons (1988) J. Virol, 62, pp. 1687-1696; Keck, J.G., Matsushima, G.A., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol, 62, pp. 1810-1813; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M., RNA recomoination of murine coronaviruses: Recombination between fusion-positive mouse hepatitis virus A59 and fusion-negative mouse hepatitis virus 2 (1988) J. Virol, 62, pp. 1989-1998; Keck, J.G., Stohlman, S.A., Soe, L.H., Makino, S., Lai, M.M.C., Multiple recombination sites at 5'-end of the murine coronavirus RNA (1987) Virology, 156, pp. 331-341; Kim, Y.N., Jeong, Y.S., Makino, S., Analysis of c/s-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.-N., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant ot the coronavirus mouse hepatitis virus by targeted RNA-recombination (1992) J. Virol, 66, pp. 1841-1848; Kuge, S., Saito, I., Nomoto, A., Primary structure of poliovirus defective-interfering particle genomes and possible generation mechanisms of the particles (1986) J. Mol. Biol, 192, pp. 437-487; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome. Annu (1990) Rev. Microbiol, 44, pp. 303-333; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepato-tropic strain MHV-3 (1981) J. Virol, 39, pp. 823-834; Lai, M.M.C., Baric, R.S., Brayton, P.B., Stohiman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohiman, S.A., Recombination between nonseg-mented RNA genomes of murine coronavirus (1985) J. Virol, 56, pp. 449-456; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol, 66, pp. 6117-6124; Liao, C.-L., Lai, M.M.C., Requirement of the 5'-end genomic sequence as an upstream c/s-acting element for coronavirus sub-genomic transcription (1994) J. Virol, 68, pp. 4727-4737; Lin, Y.-L., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective-interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol, 67, pp. 6110-6118; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol, 63, pp. 5285-5292; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol, 54, pp. 329-336; Makino, S., Keck, J.G., Stohiman, S.A., Lai, M.M., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol, 57, pp. 729-737; Makino, S., Shieh, C.-K., Keck, J.G., Lai, M.M.C., Defective-interfering particles of murine coronaviruses; Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 1-11; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139, pp. 138-151; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus; Localization of a possible RNA-packaging signal (1990) J. Virol, 64, pp. 6045-6053; Manaker, R.A., Piczak, C.V., Miller, A.A., Stanton, M.F., A hepatitis virus complicating studies with mouse leukemia (1961) J. Natl. Cancer Inst, 27, pp. 29-51; Monroe, S.S., Schlesinger, S., Common and distinct regions of defective-interfering RNAs of Sindbis virus (1984) J. Virol, 49, pp. 865-872; Nayak, D.P., Chambers, T.M., Akkina, R.M., Structure of defective-interfering RNAs of influenza virus and their role in interference (1989) The Influenza Viruses, pp. 269-317. , R. M. Krug, Ed, Plenum Press, New York; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus strain A59 (1989) Virology, 171, pp. 141-148; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M.M.C., Sequence and translation of the murine coronavirus 5'-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase (1987) J. Virol, 61, pp. 3968-3976; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of noncontiguous sequences (1983) EMBO J, 2, pp. 1839-1844; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3' end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol, 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res, 20, pp. 3375-3381; Weber, F.H., Weissmann, C., Interaction of Q (1981) J. Mot. Biol, 153, pp. 631-660; White, K.A., Bancroft, J.B., Mackie, G.A., Defective RNAs of clover yellow mosaic virus encode nonstructural/coat protein fusion products (1991) Virology, 183, pp. 479-486; White, K.A., Bancroft, J.B., Mackie, G.A., Coding capacity determined in vivo accumulation of a defective RNA of clover yellow mosaic virus (1992) J. Virol, 66, pp. 3069-3076; Yokomori, K., Banner, L.R., Lai, M.M.C., Coronavirus mRNA transcription; UV fight transcriptional mapping studies suggest an early requirement for a genomic-length template (1992) J. Virol, 66, pp. 4671-4678; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates both in Vans and in cis subgenomic mRNA transcription (1994) J. Virol, 68, pp. 4738-4746","Lai, M.M.C.; Deparment of Molecular Microbiology and Immunology, University of Southern California, School of Medicine, 2011 Zonal Avenue, HMR-503C, Los Angeles, CA 90033-1054, United States",,,00426822,,,"7778278","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0029036798
"Adami C., Pooley J., Glomb J., Stecker E., Fazal F., Fleming J.O., Baker S.C.","57200804784;16167147600;16166180700;8614639500;57189021138;7401457370;7403307881;","Evolution of Mouse Hepatitis Virus (MHV) during Chronic Infection: Quasispecies Nature of the Persisting MHV RNA",1995,"Virology","209","2", 71265,"337","346",,77,"10.1006/viro.1995.1265","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028997972&doi=10.1006%2fviro.1995.1265&partnerID=40&md5=bf0d8a15d23940142a2327524a5c4664","Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States; Departments of Neurology and Medical Microbiology, University of Wisconsin and William S. Middleton Veterans Hospital, Madison, WI 53792, United States","Adami, C., Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States; Pooley, J., Departments of Neurology and Medical Microbiology, University of Wisconsin and William S. Middleton Veterans Hospital, Madison, WI 53792, United States; Glomb, J., Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States; Stecker, E., Departments of Neurology and Medical Microbiology, University of Wisconsin and William S. Middleton Veterans Hospital, Madison, WI 53792, United States; Fazal, F., Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States; Fleming, J.O., Departments of Neurology and Medical Microbiology, University of Wisconsin and William S. Middleton Veterans Hospital, Madison, WI 53792, United States; Baker, S.C., Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States","Coronavirus infection of mice has been used extensively as a model for the study of acute encephalitis and chronic demyelination. To examine the evolution of coronavirus RNA during chronic demyelinating infection, we isolated RNA from intracerebrally inoculated mice at 4, 6, 8, 13, 20, and 42 days postinfection and used reverse transcription-polymerase chain reaction amplification methods (RT-PCR) to detect viral sequences. RNA sequences from two viral structural genes, the spike gene and the nucleocapsid gene, were detected throughout the chronic infection. In contrast, infectious virus was not detectable from brain homongenates beyond 13 days postinfection. These results indicate that coronavirus RNA persists in the brain at times when infectious virus is not detected. To determine if genetic changes were occurring during viral replication in the host, we cloned and sequenced the RT-PCR products from the spike and nucleocapsid regions and analyzed the sequences for mutations. Sequencing of the cloned products revealed that a variety of mutant forms of viral RNA persisted in the CNS, including point mutants, deletion mutants, and termination mutants. The mutations accumulated during persistent infection in both the spike and the nucleocapsid sequences, with greater than 65% of the mutations encoding amino acid changes. These results show that a diverse population or quasispecies consisting of mutant and deletion variant viral RNAs (which may not be capable of producing infectious virus particles) persists in the central nervous system of mice during chronic demyelinating infection. The implications of these results for the role of persistent viral genetic information in the pathogenesis of chronic demyelination are discussed. © 1995 Academic Press. All rights reserved.",,"animal tissue; article; coronavirus; deletion mutant; demyelination; gene mutation; gene replication; male; murine hepatitis coronavirus; nonhuman; persistent virus infection; point mutation; priority journal; rna sequence; structural gene; virus nucleocapsid; Amino Acid Sequence; Animal; Base Sequence; Brain; Cell Line; Cloning, Molecular; Codon; DNA Primers; DNA, Complementary; Evolution; Hepatitis, Viral, Animal; Male; Mice; Mice, Inbred C57BL; Molecular Sequence Data; Murine hepatitis virus; Point Mutation; Polymerase Chain Reaction; RNA, Viral; Sequence Deletion; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Time Factors; Variation (Genetics); Animalia; Coronavirus; Murinae; Murine hepatitis virus","Baczko, K., Liebert, U.G., Billeter, M.A., Cattaneo, R.T., Budka, H., Ter Meulen, V., Expression of defective measles virus genes in brain tissues of patients with subacute sclerosing panencephalitis (1986) J.Virol, 59, pp. 472-478; Banner, L.R., Keck, G.K., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine corona virus (1990) Virology, 175, pp. 548-555; Bass, B.L., Weintraub, H., An unwinding activity that covalently modifies its double-stranded RNA substrate (1988) Cell, 55, pp. 1089-1098; Bass, B.L., Weintraub, H., Cattanec, R., Billeter, M.A., Biased hypermutation of viral RNA genomes could be due to unwindingJ. 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Virol, 1, pp. 273-280; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; La Monica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, pp. 883-888; Lee, C.-M., Bih, F.-Y., Chao, Y.C., Govindarajan, S., Lai, M.M.C., Evolution of hepatitis delta virus RNA during chronic Infection (1992) Virology, 188, pp. 265-273; Levine, B., Griffin, D., Persistence of viral RNA in mouse brains after recovery from acute alphavirus encephalitis (1992) J. Virol, 66, pp. 6429-6435; Madell, M., Esteban, J.I., Quer, J., Genesca, J., Weiner, A., Esteban, R., Guardia, J., Gomez, J., Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Guasispecies nature of HCV genome distribution (1992) J. Virol, 66, pp. 3225-3229; Morris, V.L., Tieszer, C., Mackinnon, J., Percy, D., Characterization of coronavirus JHM variants isolated from Wistar Furth rats with a viral-induced demyelinating disease (1989) Virology, 169, pp. 127-136; Oldstone, M.B.A., Viral persistence (1989) Cell, 56, pp. 517-520; Oldstone, M.B.A., Molecular anatomy of viral persistence (1991) J. Virol, 65, pp. 6381-6386; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 peplomer glycoprotein coding regions of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Parvin, J.D., Moscona, A., Pan, W.T., Leider, J.M., Palese, P., Measurement of the mutation rates of animal viruses: Influenza A virus and poliovirus type (1986) J. Virol, 59, pp. 377-383; Rataul, S.M., Htrano, A., Wong, T.C., Irreversible modification of measles virus RNA In vitro by nuclear RNA-unwirding activity in human neuroblastoma cells (1992) J. Virol, 66, pp. 1769-1773; Saiki, R.K., Gelfand, D.H., Stoffel, S., Scharf, S.J., Higuchi, R., Horn, G.T., Muims, K.B., Erlich, H.A., Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase (1988) Science, 239, pp. 487-491; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating Inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Spaan, W., Cavanagh, D., Horzinek, M.C., (1990) Immunochem-Istry of Viruses. II. the Basis for Serodiagnosis and Vaccines, pp. 359-379. , M. H. V. van Regenmortel and A. R. Neurath, Eds, Elsevier, New York; Steinhauer, D.A., Holland, J.J., Rapid evolution of RNA viruses (1987) Annu. Rev. Microbiol, 41, pp. 409-433; Wagner, R.W., Smith, J.E., Cooperman, B.S., Nishikuro, K., A double stranded RNA unwinding activity introduces structural alterations by means of adenosine to ¡nosine conversions in mammalian cells and Xenopus eggs (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 2647-2651; Wang, F.-L., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetics sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wong, T.C., Ayata, M., Ueda, S., Hirano, A., Role of biased hypermutation on evolution of subacute sclerosing panancephalitis virus from progenitor acute measles virus (1991) J. Virol, 65, pp. 2191-2199; Yokomori, K., Stohlman, S.A., Lai, M.M.C., The detection and characterization of multiple hemagglutinin-esterase (HE)-defec-tive viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178","Baker, S.C.; Department of Microbiology and Immunology, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153, United States",,,00426822,,,"7778268","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0028997972
"Utiger A., Tobler K., Bridgen A., Ackermann M.","6507172306;6701508835;6603799081;7102624625;","Identification of the membrane protein of porcine epidemic diarrhea virus",1995,"Virus Genes","10","2",,"137","148",,24,"10.1007/BF01702594","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029115631&doi=10.1007%2fBF01702594&partnerID=40&md5=44c992e7699d7d56e8dc59a19743c433","Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland","Utiger, A., Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland; Tobler, K., Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland; Bridgen, A., Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland; Ackermann, M., Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland","Sequence information on the genome of porcine epidemic diarrhea virus (PEDV) has only recently been determined. In contrast, very little is known about the viral proteins. In the present report we have identified the membrane glycoprotein (M) of PEDV by use of rabbit anti-peptide sera and transient expression of the cloned M gene in Vero cells and by expression in the baculovirus system. The native M protein of PEDV is incorporated into virions, is N-glycosylated, and migrates with a relative mobility (Mr) of 27 k in polyacrylamide gels. In contrast, the M protein synthesized by recombinant baculoviruses migrates with a Mr of 23 k, that is, with identical mobility as the deglycosylated product of PEDV. Thus, it appears that M protein specified by the recombinant baculovirus is poorly, if at all, glycosylated. Using monoclonal antibodies and rabbit antipeptide sera specific for the N and C termini of the M protein, we were able to show that a 19 k band detected in PEDV-infected cells but not in virions represented a fragment of M from which the C terminus had been cleaved off. Finally, by electron microscopy and immunogold labelling, the relative orientation of M within the virion envelope was determined as NexoCcyt. In conclusion, all of these data strongly support the hypothesis that PEDV should be classified with the group I coronaviruses. © 1995 Kluwer Academic Publishers.","coronavirus; membrane protein; PEDV; porcine epidemic diarrhea","antibody; monoclonal antibody; virus envelope protein; amino terminal sequence; animal cell; article; baculovirus; carboxy terminal sequence; controlled study; coronavirus; electron microscopy; electrophoretic mobility; immunogold staining; molecular cloning; nonhuman; priority journal; protein analysis; protein glycosylation; protein localization; rabbit; vero cell; virion; virus envelope; virus recombinant; Amino Acid Sequence; Animal; Antibodies, Monoclonal; Antibodies, Viral; Baculoviridae; Base Sequence; Cell Line; Cercopithecus aethiops; Comparative Study; Coronaviridae; DNA Primers; DNA, Viral; Glycosylation; Molecular Sequence Data; Recombinant Fusion Proteins; Spodoptera; Support, Non-U.S. Gov't; Vero Cells; Viral Matrix Proteins; Animalia; Coronavirus; Oryctolagus cuniculus; Porcine epidemic diarrhea virus; Suidae; unidentified baculovirus","Pensaert, M., Debouck, P., (1978) Arch Virol, 58, pp. 243-247; Hofmann, M., Wyler, R., (1988) J Clin Microbiol, 26, pp. 2235-2239; Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., (1993) J Gen Virol, 74, pp. 1795-1804; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., (1994) Virology, 198, pp. 466-476; Duarte, M., Laude, H., (1994) J Gen Virol, 75, pp. 1195-1200; Utiger A., Frei A.K., Carvajal A., and Ackermann M. in Talbot P.J. and Levy G.A. (eds.) Corona and Related Viruses. Advances in Experimental Biology and Medicine. Plenum Press, New York, pp. 131–133; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J.M., (1991) Virology, 181, pp. 327-335; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., (1989) Virology, 168, pp. 162-167; Holmes, K.V., Willia, R.K., (1990) Coronaviruses and their Diseases. Advances in Experimental Biology and Medicine, pp. 5-7. , D., Cavanagh, T.D.K., Brown, Plenum Press, New York; Rottier, P.J.M., (1990) Coronaviruses and their Diseases. Advances in Experimental Biology and Medicine, pp. 91-94. , D., Cavanagh, T.D.K., Brown, Plenum Press, New York; Mounir, S., Talbot, P.J., (1992) J Gen Virol, 73, pp. 2731-2736; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M., Talbot, P., (1990) Virology, 174, pp. 608-612; Jacobs, L., van der Zeijst, B.A.M., Horzinek, M.C., (1986) J Virol, 57, pp. 1010-1015; Utiger, A., Rosskopf, M., Guscetti, F., Ackermann, M., (1994) Coronaviruses: Molecular Biology and Virus-Host Interactions. Advances in Experimental Biology and Medicine, pp. 197-202. , H., Laude, J.F., Vautherot, Plenum Press, New York; Fraefel, C., Zeng, J., Choffat, Y., Engels, M., Schwyzer, M., Ackermann, M., (1994) J Virol, 68, pp. 3154-3162; Knuchel, M., Ackermann, M., Müller, H.K., Kihm, U., (1992) Vet Microbiol, 32, pp. 117-134; Sánchez-Martínez, D., Pellett, P.E., (1991) Virology, 182, pp. 229-238; Rusconi, S., Severne, Y., Georgiev, O., Galli, I., Wieland, S., (1990) Gene, 89, pp. 211-221; Laude, H., Rasschaert, D., Huet, J.C., (1987) J Gen Virol, 68, pp. 1687-1693; Raabe, T., Siddell, S.G., (1989) Arch Virol, 107, pp. 323-328; Godet, M., Rasschaert, D., Laude, H., (1991) Virology, 185, pp. 732-740; Kuroda, K., Veit, M., Klenk, H.D., (1991) Virology, 180, pp. 159-165; Locker, J.K., Rose, J.K., Horzinek, M.C., Rottier, P.J., (1992) J Biol Chem, 267, pp. 21911-21918; Artrong, J., McCrae, M., Colman, A., (1987) J Cell Biochem, 35, pp. 129-136; Machamer, C.E., Rose, J.K., (1987) J Cell Biol, 105, pp. 1205-1214","Ackermann, M.; Institute of Virology, Faculty of Veterinary Medicine, University of Zurich, Zurich, CH-8057, Switzerland",,"Kluwer Academic Publishers",09208569,,VIGEE,"8560773","English","Virus Genes",Article,"Final",,Scopus,2-s2.0-0029115631
"Liu D.X., Brown T.D.K.","8972667300;56248391000;","Characterisation and Mutational Analysis of an ORF 1a-Encoding Proteinase Domain Responsible for Proteolytic Processing of the Infectious Bronchitis Virus 1a/1b Polyprotein",1995,"Virology","209","2", 71274,"420","427",,57,"10.1006/viro.1995.1274","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029036797&doi=10.1006%2fviro.1995.1274&partnerID=40&md5=4e294edf8ac30ae4467b4c8e20b7f960","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","Liu, D.X., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","Coronavirus gene expression involves proteolytic processing of the mRNA 1-encoded polyproteins by viral and cellular proteinases. Recently, we have demonstrated that an ORF 1b-encoded 100-kDa protein is proteolytically cleaved from the 1a/1b fusion polyprotein by a viral-specific proteinase of the picornavirus 3C proteinase group (3C-like proteinase). In this report, the 3C-like proteinase has been further analysed by internal deletion of a 2.3-kb fragment between the 3C-like proteinase-encoding region and ORF 1b and by substitution mutations of its catalytic centre as well as the two predicted cleavage sites flanking the 100-kDa protein. The results show that internal deletion of ORF 1a sequences from nucleotide 9911 to 12227 does not influence the catalytic activity of the proteinase in processing of the 1a/1b polyprotein to the 100-kDa protein species. Site-directed mutagenesis studies have confirmed that the predicted nucleophilic cysteine residue (Cys2922) and a histidine residue encoded by ORF 1a from nucleotide 8985 to 8987 (His2820) are essential for the catalytic activity of the proteinase, and that the QS(G) dipeptide bonds are its target cleavage sites. Substitution mutations of the third component of the putative catalytic triad, the glutamic acid 2843 (Glu2843) residue, however, do not affect the processing to the 100-kDa protein. In addition, cotransfection experiment shows that the 3C-like proteinase is capable of trans-cleavage of the 1a/1b polyprotein. These studies have confirmed the involvement of the 3C-like proteinase domain in processing of the 1a/1b polyprotein, the predicted catalytic centre of the proteinase, and its cleavage sites. © 1995 Academic Press. All rights reserved.",,"animal cell; article; coronavirus; dna flanking region; gene expression; gene mutation; nonhuman; open reading frame; priority journal; protein degradation; protein domain; protein processing; site directed mutagenesis; virus expression; virus gene; virus morphology; Amino Acid Sequence; Animal; Base Sequence; Cercopithecus aethiops; Comparative Study; Coronaviridae; DNA Mutational Analysis; Endopeptidases; Gene Expression; Infectious bronchitis virus; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Open Reading Frames; Plasmids; Point Mutation; Protein Processing, Post-Translational; RNA, Messenger; Sequence Deletion; Support, Non-U.S. Gov't; Vero Cells; Viral Proteins; Animalia; Avian infectious bronchitis virus; Coronavirus; Picornaviridae","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N.G., Picornaviral 3C cysteine protéinases have a fold similar to chymo-trypsin-like serine protéinases (1994) Nature, 369, pp. 72-76; Bazan, J.F., Fletterick, R.J., Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 7872-7876; Blair, W.S., Li, X., Semler, B.L., A cellular cofactor facilitates efficient 3CD cleavage of the poliovirus P1 precursor (1993) J. Virol, 67, pp. 2339-2343; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol, 68, pp. 57-77; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J, 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Contreras, R., Cheroutre, H., Degrave, W., Fiers, W., Simple efficient in vitro synthesis of capped RNA useful for direct expression of cloned DNA (1982) Nucleic Acids Res, 10, pp. 6353-6362; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Blinov, V.M., Donchenko, A.P., Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular serine and cysteine proteinase families (1986) FEBS Lett, 194, pp. 253-257; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome; Prediction of putative functional domains in the non-structursl polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4847-4860; Kean, K.M., Howell, M.T., Grunert, S., Girard, M., Jackson, R.J., Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites (1993) Virology, 194, pp. 360-364; Laemmli, U.K., Cleavage of structural proteins during the assembly of the bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Lawson, M.A., Semler, B.L., Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 9919-9923; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3C protein with the virion envelope (1991) Virology, 185, pp. 911-917; Liu, D.X., Inglis, S.C., Identification of two new polypep-tides encoded by mRNA5 of the coronavirus infectious bronchitis virus (1992) Virology, 186, pp. 342-347; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol, 66, pp. 6143-6154; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycis-tronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Gompels, U.A., Nicholas, J., Lelliot, C., Identification and expression of the human herpesvirus 6 glycoprotein H and interaction with an accessory 40-kDa glycoprotein (1993) J. Gen. Virol, 74, pp. 1847-1857; Liu, D.X., Brierley, I., Tibbies, K.W., Brown, T.D.K., A 100-kiiodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol, 68, pp. 5772-5780; Liu, D.X., Tibbies, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression and processing of an 87-kDa polypeptide encoded by ORF1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Lomniczi, B., Biological properties of avian coronavirus RNA (1977) J. Gen. Virol, 36, pp. 531-533; Matthews, D.A., Smith, W.W., Ferre, R.A., Condon, B., Budahazi, G., Sisson, W., Viilafranca, J.E., Woriand, S., Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein (1994) Cell, 77, pp. 761-771; Palmenberg, A.C., Proteolytic processing of picornaviral polyprotein (1990) Annu. Rev. Microbiol, 44, pp. 603-623; Smith, A.R., Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Inglis, S.C., Identification of a new membrane-associated polypeptide specified by the coronavirus infectious bronchitis virus (1990) J.Gen. Virol, 71, pp. 3-11; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Location of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol, 50, pp. 22-29","Liu, D.X.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom",,,00426822,,,"7778277","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0029036797
"Rossen J.W.A., Voorhout W.F., Horzinek M.C., Van Der Ende A., Strous G.J.A.M., Rottier P.J.M.","7005977394;7003796069;7102624836;7007055960;7004975908;7006145490;","MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally",1995,"Virology","210","1", 71316,"54","66",,19,"10.1006/viro.1995.1316","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029026585&doi=10.1006%2fviro.1995.1316&partnerID=40&md5=76c433bca1bbada5968b5faddcf44d76","Institute of Virology, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Laboratory of Cell Biology, Medical School Utrecht University, Heidelberglaan 100, AZU-H02314, 3584 CX Utrecht, Netherlands; Department of Medical Microbiology, University of Amsterdam, AMC, Meibergdreef 15, 1105 AZ Amsterdam, Netherlands","Rossen, J.W.A., Institute of Virology, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Voorhout, W.F., Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Institute of Virology, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Van Der Ende, A., Laboratory of Cell Biology, Medical School Utrecht University, Heidelberglaan 100, AZU-H02314, 3584 CX Utrecht, Netherlands, Department of Medical Microbiology, University of Amsterdam, AMC, Meibergdreef 15, 1105 AZ Amsterdam, Netherlands; Strous, G.J.A.M., Laboratory of Cell Biology, Medical School Utrecht University, Heidelberglaan 100, AZU-H02314, 3584 CX Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Coronaviruses have a marked tropism for epithelial cells. Entry and release of the porcine transmissible gastroenteritis virus (TGEV) is restricted to apical surfaces of polarized epithelial cells, as we have recently shown (J. W. A. Rossen, C. P. J. Bekker, W. F. Voorhout, G. J. A. M. Strous, A. van der Ende, and P. J. M. Rottier, 1994, J. Virol. 68, 7966- 7973). In this paper we analyze the interactions of mouse hepatitis coronavirus A59 (MHV-A59) with polarized murine kidney cells (mTAL) grown on permeable supports. After inoculation from the apical or basolateral side, virus entry was found to take place only through the apical membrane. The virus utilized a protein of the carcinoembryonic antigen family as its receptor. In contrast to TGEV, MHV-A59 was released preferentially from the basolateral plasma membrane domain, as evidenced by the accumulation of vital proteins and infectivity in the basolateral culture fluid as well as by electron microscopical observations. In the mouse, MHV initially replicates in the nasal epithelium before being disseminated throughout the body; the basolateral release of MHV from epithelial cells into the animal's circulation may be the first step in the establishment of a systemic infection. © 1995 Academic Press, Inc.",,,"Baghdiguian, S., Verrier, B., Roccabianca, M., Pommier, G., Marvaldi, J., Fantini, J., Vectorial release of carcinoembryonic antigen induced by IFN-gamma in human colon cancer cells cultured in serum-free medium (1991) Eur. J. Cancer, 27, pp. 599-604; Barker, G., Simmons, N.L., Identification of two strains of cultured canine reral epithelial cells (MDCK cells) which displays entirely different physiological properties (1981) O. J. Exp. Physiol, 66, pp. 61-72; Cereijido, M., Robbins, E.S.-., Dolan, W.J., Rotunno, C.A., Sabatini, D.D., Polarized monolayers formed by epithelial cells on a permeable and translucent support (1978) J. Cell Biol, 77, pp. 853-880; Cereijido, M., Contreras, R.G., Gonzlaez-Mariscal, L., Development and alteration of polarity (1989) Annu. Rev. Physiol, 51, pp. 785-795; Cerneus, D.P., Strous, G.J., Van Der Ende, A., Bidirectional transcytosis determines the steady state distribution of the transferrin receptor at opposite plasma membrane domains of BeWo cells (1993) J. Cell Biol, 122, pp. 1223-1230; Clayson, E.T., Compans, R.W., Entry of simian virus 40 is restricted to apical surfaces of polarized epithelial celis (1988) Mol. Cell. Biol, 8, pp. 3391-3396; Clayson, E.T., Jones Brando, L.V., Compans, R.W., Release of simian virus 40 virions from epithelial cells is polarized and occurs without cell lysis (1989) J. Virol, 63, pp. 2278-2288; Compans, R.W., Srinivas, R.V., Protein sorting in polarized epithelial cells (1991) Cum Top. Microbiol. Immunol, 170, pp. 141-181; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coro navi ruses. Lab. Arum (1993) Science, 43, pp. 15-26; Delmas, B., Gelfi, J., L’Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Dottl, C.G., Sullivan, C.A., Banker, G., The establishment of polarity by hippocampal neurons in culture (1988) J. Neurosci, 8, pp. 1454-1468; Dotti, C.G., Simons, K., Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture (1990) Cell, 62, pp. 63-72; Doyle, L.P., Hutchings, L.M.A., A transmissible gastroenteritis in pigs (1946) J. Am. Vet. Med. Assoc, 108, pp. 257-259; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster ceil lines confers susceptibility to MHV (1991) J. Virol, 65, pp. 6881-6891; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus (1993) J. Virol, 67, pp. 1-8; Ecay, T.W., Valentich, J.D., Basal lamina formation by epithelial cell lines correlates with laminin A chain synthesis and secretion (1992) Exp. Ceil Res, 203, pp. 32-38; Fuller, S.D., Von Bonsdorff, C.-H., Simons, K., Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK (1984) Cell, 38, pp. 65-77; Fuller, S.D., Von Bonsdorff, C.-H., Simons, K., Cell surface influenza haemmagglutinin can mediate infection by other animal viruses (1985) EMBO J, 4, pp. 2475-2485; Gstraunthaler, G.J.A., Epithelial cells in tissue culture (1988) Renal Physiol. Biochem, 11, pp. 1-42; Herzlinger, D.A., Ojakian, G.K., Studies on the development and maintenance of epithelial cell surface polarity with monoclonal antibodies (1984) J. Ceil Biol, 98, pp. 1777-1787; Holmes, K.V., Coronaviridae and their replication (1990) Virology, pp. 841-856. , B. N. Fields, D. M. Knipe, R. M. Chanock, M. S. Hirsch, J. L. Melnick, T. P. Monath, and B. Roizman, EdsChap. 29, Raven Press, New York; Hubbard, A.L., Stieger, B., Bartles, J.R., Biogenesis of endogenous plasma membrane proteins in epithelial cells (1989) Annu. Rev. Physiol, 51, pp. 555-570; Kaerber, G., Beitrag zur kollektiven behandlung pharmakolog-ischer Reihenversuche (1931) Arch. Exp. Pathol Pharmakol, 162, p. 480; Klumperman, J., Krijnse-Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. 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Ceil Biol, 115, pp. 1009-1019; Van Meer, G., Simons, K., Viruses budding from either the apical or basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions (1982) EM BO L, 1, pp. 847-852; Weibel, E.R., (1979) Stereological Methods, 1. , Practical Methods for Biological Morphometry."" Academic Press, New York; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Flolmes, K., V, Purification of the 110-kilodalton glycoprotein receptor for Mouse Hepatitis Virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL7J mice (1990) J. Virol, 64, pp. 3817-3823; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Zurzolo, C.-., Rodriguez-Boulan, E., Delivery of Na, K-AT-Pase in polarized epithelial celis (1993) Science, 260, pp. 550-551","Rottier, P.J.M.; Institute of Virology, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0029026585
"Vieler E., Schlapp T., Anders C., Herbst W.","6603650281;6701808474;7004585426;16161781000;","Genomic relationship of porcine hemagglutinating encephalomyelitis virus to bovine coronavirus and human coronavirus OC43 as studied by the use of bovine coronavirus S gene-specific probes",1995,"Archives of Virology","140","7",,"1215","1223",,9,"10.1007/BF01322747","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028836932&doi=10.1007%2fBF01322747&partnerID=40&md5=f41a6c04254ad872deebfbf42b4009e8","Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany","Vieler, E., Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany; Schlapp, T., Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany; Anders, C., Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany; Herbst, W., Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany","The genomic relationship of porcine hemagglutinating encephalomyelitis virus (HEV) to bovine coronavirus (BCV) and human coronavirus (HCV) strain OC43 was examined by dot blot hybridization assays. Two BCV S gene-specific probes were generated by polymerase chain reaction from the avirulent L9-strain of BCV. Probes were located in the S1 and the S2 region of the peplomeric (S) glycoprotein gene. The S1 probe (726 bp) hybridized with BCV and HCV-OC43, but not with HEV under moderate stringency hybridization conditions (50 °C). Only slight signals were present with mouse hepatitis virus (MHV) and no signals were observed with feline infectious peritonitis virus (FIPV) or canine coronavirus (CCV). At high stringency conditions (60 °C) the S1 probe hybridized with BCV only. Using the S2 probe (680 bp) under moderate strin-gency conditions, hybridization signals were obtained with BCV, HCV-OC43 and HEV (strains 67N, NT9, VW572). The signals obtained by the three HEV strains were altogether weaker than with BCV and HCV-OC43. The S2 probe did not react with MHV, FIPV and CCV. At high stringency the S2-specific probe hybridized with BCV and HCV-OC43 but did not hybridize with HEV. Nucleotide sequence analysis of the region covering the S2 probe in HEV revealed 92.6% nucleotide sequence homology to BCV and 91.9% to HCV-OC43. In contrast, the region covering the S1 probe in HEV could not be amplified using the BCV S1-specific primers. The hybridization and sequencing results thus indicate a closer genomic relationship between BCV and HCV-OC43 than there is between HEV and BCV or HCV-OC43, respectively. © 1995 Springer-Verlag.",,"membrane protein; spike glycoprotein, coronavirus; virus DNA; virus envelope protein; animal; article; cat; cattle; cell culture; cell line; classification; comparative study; Coronavirus; cross reaction; DNA probe; dog; fluorescent antibody technique; genetics; human; molecular genetics; nucleotide sequence; sequence homology; swine; virus genome; Animal; Base Sequence; Cats; Cattle; Cell Line; Comparative Study; Coronavirus; Coronavirus OC43, Human; Coronavirus, Bovine; Cross Reactions; DNA Probes; DNA, Viral; Dogs; Fluorescent Antibody Technique; Genome, Viral; Human; Membrane Glycoproteins; Molecular Sequence Data; Sequence Homology, Nucleic Acid; Swine; Tumor Cells, Cultured; Viral Envelope Proteins","Boircau, P., Cruciere, C., Laporte, J., Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) Journal of General Virology, 71, pp. 487-492; Cyr-Coats, K.S., Storz, J., Bovine coronavirus-induced cytopathic expression and plaque formation: host cell and virus strain determine trypsin dependence (1988) J Vet Med B, 35, pp. 48-56; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-2877; Hajer, I., Storz, J., Antigens of bovine coronavirus strain LY-138 and their diagnostic properties (1978) Am J Vet Res, 39, pp. 441-444; Hess, R.G., Bachmann, P.A., Erbrechen und Kümmern der Ferkel: Vorkommen und Verbreitung in Süddeutschland (1978) TU, 33, pp. 571-574; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res, 12, pp. 1-9; Künkel, F., Herrler, G., Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Channock, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc Natl Acad Sci USA, 57, pp. 933-940; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J Gen Virol, 73, pp. 2731-2736; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus OC43 (1993) J Gen Virol, 74, pp. 1981-1987; Pensaert, M.B., Callebaut, P.E., Characteristics of a coronavirus causing vomiting and wasting in pigs (1974) Arch Ges Virusforschung, 44, pp. 35-50; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses (1990) Immunochemistry of viruses II. The basis for serodiagnosis and vaccines, pp. 359-379. , M.H.V., van Regenmortel, A.R., Neurath, Elsevier, Amsterdam; Tompkins, W.A.F., Watrach, A.M., Schmale, J.D., Schulza, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 101-106; Vautherot, J.F., Laporate, J., Utilization of monoclonal antibodies for antigenic characterization of coronaviruses (1983) Ann Rech Vet, 14, pp. 437-444; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: detailed antigenic analyses of S1, S2 and HE (1992) J Gen Virol, 73, pp. 1725-1737; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Yagami, K., Izumi, Y., Kajiwara, N., Sugiyama, F., Sugiyama, Y., Neurotropism of mouse-adapted hemagglutinating encephalomyelitis virus (1993) J Comp Pathol, 109, pp. 21-27; Zhang, X., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase gene of the human coronavirus strain OC43: phylogenetic relationships to bovine and murine coronaviruses and influenza C virus (1992) Virology, 186, pp. 318-323","Vieler, E.; Institut für Hygiene, und Infektionskrankheiten der Tiere der Justus-Liebig-Universität Giessen, Frankfurter Strasse 89-91, Giessen, D-35392, Germany",,"Springer-Verlag",03048608,,ARVID,"7646353","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0028836932
"Tsunemitsu H., Saif L.J.","7004628959;7102226747;","Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle",1995,"Archives of Virology","140","7",,"1303","1311",,39,"10.1007/BF01322757","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028851099&doi=10.1007%2fBF01322757&partnerID=40&md5=1f2d547f15bd7cd6e2c09f3c49e3e0f7","Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, Wooster, 44691, Ohio, United States","Tsunemitsu, H., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, Wooster, 44691, Ohio, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, Wooster, 44691, Ohio, United States","The antigenic and biological properties of 6 strains of bovine coronavirus (BCV) derived from neonatal calf diarrhea (CD) and 8 strains of BCV from winter dysentery (WD) of adult cattle, propagated in HRT-18 cells, were compared to determine if CD and WD strains belong to distinct serotypes or subtypes of BCV. All strains hemagglutinated both mouse and chicken erythrocytes at 4 °C, but the ratios of hemagglutination titers with mouse erythrocytes compared to chicken erythrocytes showed diversity for both CD and WD strains. Some CD and WD strains did not hemagglutinate chicken erythrocytes at 37 °C and showed receptor-destroying enzyme activity against chicken erythrocytes. Hyperimmune antisera were produced in guinea pigs against 3 and 7 strains of BCV from CD and WD, respectively. No significant differences in antibody titers against these strains were observed by indirect immunofluorescence tests. However, in virus neutralization tests, antisera to 1 CD and 2 WD strains had 16-fold or lower antibody titers against 3 WD and 1 CD strains than against the homologous strains, and this variation reflected low antigenic relatedness values (R=13-25%), suggesting the presence of different subtypes among BCV. In hemagglutination inhibition tests, some one-way antigenic variations among strains were also observed. These results suggest that some antigenic and biological diversity exists among BCV strains, but these variations were unrelated to the clinical source of the strains; i.e. CD or WD. © 1995 Springer-Verlag.",,"virus antibody; virus antigen; aging; animal; animal disease; antigenic variation; article; cattle; cattle disease; cell culture; classification; Coronavirus; diarrhea; dysentery; fluorescent antibody technique; guinea pig; hemagglutination test; human; immunology; isolation and purification; mouse; physiology; serodiagnosis; serotyping; virology; virus infection; Aging; Animal; Antibodies, Viral; Antigenic Variation; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus, Bovine; Diarrhea; Dysentery; Fluorescent Antibody Technique; Guinea Pigs; Hemagglutination Tests; Human; Mice; Neutralization Tests; Rotavirus Infections; Serotyping; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Tumor Cells, Cultured","Archetti, I., Horsfall, F.L., Persistent antigenic variation of influenza A viruses after incomplete neutralization in vivo with heterologous immune serum (1950) J Exp Med, 92, pp. 441-462; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Vet, 68, pp. 423-441; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Crouch, C.F., Raybould, T.J.G., Comparison of different antigen preparations as substrates for use in passive hemagglutination and enzyme-linked immunosorbent assays for detection of antibody against bovine enteric coronavirus (1983) J Clin Microbiol, 18, pp. 146-149; Dea, S., Roy, R.S., Elazhary, M.A.S.Y., Antigenic variations among calf diarrhea coronaviruses by immunodiffusion and counterimmuno-electrophoresis (1982) Ann Rech Vet, 13, pp. 351-356; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; El-Kanawati ZR, Tsunemitsu H, Smith DR, Saif LJ (1994) Infection and cross-protection studies of winter dysentery and calf bovine coronavirus strains in gnotobiotic calves. In: Proceedings of the 75th Annual Meeting of the Conference of Research Workers in Animal Diseases, Chicago, Illinois, Abstract No 77, p 10; Hohdatsu, T., Eiguchi, Y., Tsuchimoto, M., Ide, S., Yamagishi, H., Matsumoto, M., Antigenic variation of porcine transmissible gastroenteritis virus detected by monoclonal antibodies (1987) Vet Microbiol, 14, pp. 115-124; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: monoclonal antibodies to the spike protein distinguish between vaccine and wildtype strains (1991) Virology, 183, pp. 442-445; Jactel, B., Espinasse, J., Viso, M., Valiergue, H., an epidemiological study of winter dysentery in fifteen herds in France (1990) Vet Res Commun, 14, pp. 367-379; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.F., Neonatal calf diarrhea: propagation, attenuation, and characteristics of coronavirus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Saif, L.J., A review of evidence implicating bovine coronavirus in the ethiology of winter dysentery in cows: an enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., winter dysentery in dairy herds: electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Sato, K., Inaba, Y., Kurogi, H., Takahashi, E., Satado, K., Omori, T., Matsumoto, M., Hemagglutinationby calf diarrhea coronavirus (1977) Vet Microbiol, 2, pp. 83-87; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The Sprotein of bovine coronavirus is a hemagglutinin recognizing 9- O-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2956; Storz, J., Herrler, G., Snodgrass, D.R., Hussain, K.A., Zhang, X.M., Clark, M.A., Rott, R., Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine coronavirus (1991) J Gen Virol, 72, pp. 2817-2820; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Takahashi, E., Inaba, Y., Sato, K., Ito, Y., Kurogi, H., Akashi, H., Satoda, K., Omori, T., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Tsunemitsu, H., Yonemichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Van Kruiningen, H.J., Castellano, V.P., Torres, A., Sharpee, R.L., Serologic evidence of coronavirus infection in New York and New England dairy cattle with winter dysentery (1991) J Vet Diagn Invest, 3, pp. 293-296; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529","Tsunemitsu, H.; Food Animal Health Research Program, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, Wooster, 44691, Ohio, United States",,"Springer-Verlag",03048608,,ARVID,"7646362","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0028851099
"Wege H.","7005516649;","Immunopathological aspects of coronavirus infections",1995,"Springer Seminars in Immunopathology","17","2-3",,"133","148",,13,"10.1007/BF00196162","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029146911&doi=10.1007%2fBF00196162&partnerID=40&md5=6baa45d548916c630fd0771d2e9f23a4","Institute for Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, Insel Riems, D-17498, Germany","Wege, H., Institute for Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, Insel Riems, D-17498, Germany",[No abstract available],,"antibody; blood clotting factor 10a; glycoprotein; virus rna; autoimmunity; blood clotting disorder; central nervous system disease; coronavirus; demyelination; enteritis; human; immune complex deposition; immune response; immunopathology; inflammation; liver disease; macrophage; nonhuman; priority journal; review; t lymphocyte; virus infection; virus morphology; virus nucleocapsid; virus replication; Animal; Coronavirus; Coronavirus Infections; Support, Non-U.S. Gov't","Bergmann, C., McMillan, M., Stohlman, S., Characterization of the Ld-restricted cytotoxic T-lymphocyte epitope in the mouse hepatitis virus nucleocapsid protein (1993) J Virol, 67, p. 7041; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, p. 261; Burks, J.S., DeVald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from centralnervous system tissue of two multiple sclerosis patients (1980) Science, 209, p. 933; Cabirac, G.F., Soike, K.F., Zhang, J.Y., Hoel, K., Butunoi, C., Cai, G-Y, Johnson, S., Murray, S., Entry of coronavirus into primate CNS following peripheral inoculation (1994) Microb Pathog, 16, p. 349; Caseboldt, D.B., Spalding, D.M., Shoeb, T.R., Lindsey, J.R., Suppression of immune response induction in Peyer's patch lymphoid cells from mice infected with mouse hepatitis virus (1987) Cellular Immunology, 109, p. 97; 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"Goodwin M.A., Brown J., Player E.C., Steffens W.L., Hermes D., Dekich M.A.","57208456911;55724431000;6603362972;7005567469;7003733187;6603062422;","Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis complex/spiking mortality",1995,"Avian Pathology","24","3",,"497","505",,17,"10.1080/03079459508419089","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028814767&doi=10.1080%2f03079459508419089&partnerID=40&md5=3751d30e4832b74eb638172257b8de16","Department of Veterinary Pathology, United States; Medical Microbiology, United States; Georgia Poultry Laboratory, PO Box 20, Oakwood, GA 30566, United States; Anatomy and Radiology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Perdue Diagnostic Laboratory, Washington, IN 47501, United States; Perdue Farms, Inc., Salisbury, MD 28410, United States","Goodwin, M.A., Department of Veterinary Pathology, United States; Brown, J., Medical Microbiology, United States; Player, E.C., Georgia Poultry Laboratory, PO Box 20, Oakwood, GA 30566, United States; Steffens, W.L., Anatomy and Radiology, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Hermes, D., Perdue Diagnostic Laboratory, Washington, IN 47501, United States; Dekich, M.A., Perdue Farms, Inc., Salisbury, MD 28410, United States","The purpose of the present study was to use clinical epidemiologic tools to define the relationship between production performance data, virus particles, and intestinal fringed membranous particles (FMPs) in healthy turkey poults and in poults that were experiencing an outbreak of poult enteritis complex (PEC) and spiking mortality syndrome (SMS). Small and large intestines from flocks of healthy poults and poults with PEC/SMS were collected, processed, and examined for viruses. Production performance parameters were collected and analyzed. Flocks of turkeys with PEC/SMS in the present study had low survival expectancy (livability) and poor growth compared to their healthy turkey counterparts. The only significant association between sickness and intestinal virus was the presence of coronavirus. © 1995, Taylor & Francis Group, LLC. All rights reserved.",,,"Andral, B., Toquin, D., Observations au microscope electronique a partir de prelevements de dindes presentant des troubles pathologiques. Avian Pathology (1984), 13, pp. 389-417; Angel, C.R., Sell, J.L., Mallarino, E., Al-batshan, H., Piquer, J., Soto-salanova, M.F., Dietary effects of stunting syndrome in poults (1992) Poultry Science, 71, pp. 859-871; Barnes, H.J., Elias, G.M., Fernandez, D.V., Coleman, J.W., Jennings, R.S., Growth depression in tom turkey flocks produced on farms in continuous production (1994) Program of the 131st Annual Meeting of the American Veterinary Medical Association, p. 133. , San Francisco, CA; July 9–13; Brahem, A., Demarquez, D., Beyrie, M., Vulliaume, A., Fleury, H.J.A., A highly virulent togavirus-like agent associated with the fulminating disease of guinea fowl (1992) Avian Diseases, 36, pp. 143-148; Davis, J.F., Castro, A.E., De la torre, J.C., Goodwin, M.A., Player, E.C., Dorman, J.T., Teng, M., Fuchs, D., Arenavirus-like particles associated with enteritis and “spiking mortality syndrome” in Georgia chicks (1994) Proceedings of the 43rd Western Poultry Disease Conference, pp. 40-42. , Sacramento, CA, pp. Feb. 27-March 1; Dea, S., Tijssen, P., Viral agents associated with outbreaks of diarrhea in turkey flocks in Quebec (1988) Canadian Journal of Veterinary Research, 52, pp. 53-57; Doane, F.W., Anderson, N., Electron Microscopy in Diagnostic Virology—a practical guide and atlas, pp (1987), pp. 69-74. , Cambridge, MA, University Press; Ficken, M.D., Update on spiking mortality (1994) Proceedings of the Smith Kline Beecham Pacesetter Conference, pp. 7-12. , National Turkey Federation Annual Meeting, January 11, Reno, Nevada. pp; Fleury, H.J.A., Morere, G., Demarquez, N., Vuillaume, A., Unidentified viral particles could be associated with enteritis of various commercial bird species (1988) Annals Institute Pasteur (Paris), 139, pp. 449-453; Goodwin, M.A., Latimer, K.S., Nersessian, B.N., Fletcher, O.J., Quantitation of intestinal D-xylose absorption in normal and in reovirus inoculated turkey poults (1984) Avian Diseases, 28, pp. 959-967; Goodwin, M.A., Nersessian, B.N., Brown, J., Fletcher, O.J., Gastrointestinal transit times in normal and reovirus-inoculated turkeys. Avian Diseases (1985), 29, pp. 920-928; Goodwin, M.A., Steffens, W.L., Russell, I.D., Brown, J., Diarrhea associated with small-intestinal cryptosporidiosis in turkeys (1988) Avian Diseases, 32, pp. 63-67; Goodwin, M.A., Davis, J.F., Mcnulty, M.S., Brown, J., Player, E.C., Enteritis (so-called runting stunting syndrome) in Georgia broiler chicks (1993) Avian Diseases, 37, pp. 451-458; Goodwin, M.A., Player, E.C., Magee, D.L., Intralesional herpesvirus, reovirus-like particles, and bacteria in a flock of broiler chicks with spiking mortality, diarrhea, and enterotyphlitis (1994) Avian Diseases, 38. , in press; Gough, R.E., Collins, M.S., Alexander, D.J., Cox, W.J., Viruses and virus-like particles detected in samples from diseased game birds in Great Britain during 1988 (1990) Avian Pathology, 19, pp. 331-343; Hayat, M.A., Support films (1989) Principles and Techniques of Electron Microscopy, pp. 354-357. , 3rd Edn Boca Raton, FL, CRC Press; Hayhow, C.S., Saif, Y.M., Kerr, K.M., Whitmoyer, R.E., Further observations on enterovirus infection in specific-pathogen-free turkey poults (1993) Avian Diseases, 37, pp. 124-134; Kramer, M.S., Clinical Epidemiology and Biostatistics, a Primer for Clinical Investigators and Decision-makers. pp (1988), pp. 1-10. , Berlin, Springer-Veriag; Lozano, L.F., Bickford, A.A., Castro, A.E., Swartzman-andert, J., Chin, R., Meteyer, C., Cooper, G., Manalac, R.L., Association of reoviridae particles in an enteric syndrome of poults observed in turkey flocks during 1988 (1989) Journal of Veterinary Diagnostic Investigation, 1, pp. 254-259; Lukert, P.D., Virus identification and classification (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, pp. 182-185. , Dubuque, Iowa, Kendall/Hunt; Mcferran, J.B., Mcnulty, M.S., Curran, W.L., Diagnosis of avian viral diseases by electron microscopy (1978) American Journal of Veterinary Research, 39, pp. 505-508; Morishita, T.Y., Lam, K.M., Mccapes, R.H., Isolation of two filamentous bacteria associated with enteritis in turkey poults (1992) Poultry Science, 71, pp. 203-207; Naqi, S.A., Panigrahy, B., Hall, C.F., Purification and concentration of viruses associated with transmissible (coronaviral) enteritis of turkeys (bluecomb) (1975) American Journal of Veterinary Research, 36, pp. 548-552; Panigrahy, B., Naqi, S.A., Hall, C.F., Isolation and characterization of viruses associated with transmissible enteritis (bluecomb) of turkeys (1973) Avian Diseases, 17, pp. 430-438; Perry, R.W., Rowland, G.N., Gusson, J.G., Steffens, W.L., Quinn, J.A., Skeletal lesions associated with a naturally occurring poult enteritis (1991) Avian Diseases, 35, pp. 158-164; Reynolds, D.L., Jr, Viral enteric infections, Introduction (1991) Diseases of Poultry, pp. 619-620. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid & H. W. Yoder Jr Eds) 9th Edn Ames, Iowa State University Press; Reynolds, D.L., Saif, Y.M., Theil, K.W., Enteric viral infections of turkey poults: incidence of infection (1987) Avian Diseases, 31, pp. 272-276; Schnagel, R.D., Brokees, S., Medvedec, S., Morey, F., Characteristics of Australian human enteric coronavirus-like particles: comparison with human respiratory coronavirus 229E and duodenal brush border vesicles (1987) Archives of Virology, 97, pp. 309-323; Swayne, D.E., Radin, M.J., Saif, Y.M., Enteric disease in specific-pathogen-free turkey poults inoculated with a small round turkey-origin enteric virus (1990) Avian Diseases, 34, pp. 683-692",,,,03079457,,,,"English","Avian Pathol.",Article,"Final",,Scopus,2-s2.0-0028814767
"Herrewegh A.A.P.M., Vennema H., Horzinek M.C., Rottier P.J.M., De Groot R.J.","6602355430;7003697291;7102624836;7006145490;7103077066;","The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes",1995,"Virology","212","2", 71520,"622","631",,126,"10.1006/viro.1995.1520","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028863417&doi=10.1006%2fviro.1995.1520&partnerID=40&md5=f8e8b310813a6ffa7d881ac3c8f36247","Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Herrewegh, A.A.P.M., Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Vennema, H., Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Groot, R.J., Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Feline coronaviruses (FCoVs) have been subdivided into feline enteric coronaviruses (FECVs) and feline infectious peritonitis viruses (FIPVs) on the basis of pathogenic properties. Serologically, a distinction has been made between type I and II FCoVs, the latter of which more closely resemble canine coronavirus (CCV). To gain more insight into the genetic relationships between different FCoV biotypes, we determined the nucleotide sequences of the ORF7a/7b transcription unit of nine strains. The following observations were made: (i) The sequences are 87-100% identical. In this part of the genome, type I and II FCoVs are more closely related to each other than to CCV. To explain the genetic and antigenic differences between the spike genes of type I and II FCoVs, we postulate that type II FCoVs have arisen by an RNA recombination event between a type I FCoV and CCV. (ii) The avirulent 'FECV' strains UCD and 79-1683 are more similar to virulent 'FIPV' strains than to each other. Our findings thus support the notion that FECV and FIPV are not different species but merely virulence variants. (iii) In contrast to FECV 79-1683, FECV UCD contains an intact ORF7b, indicating that ORF7b deletions are not a universal distinguishing property of FECVs. (iv) ORF7b deletions readily occur in vitro, correlating with loss of virulence. By reverse transcription-polymerase chain reaction analysis, we show that in naturally occurring FCoVs ORF7b is maintained. Thus, ORF7b seems to provide a distinct selective advantage during natural infection. © 1995 Academic Press, Inc.",,,"Addie, D.D., Jarrett, J.O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet Rec, 130, pp. 133-137; Addie, D., Jarrett, J.O., Feline coronavirus antibodies in cats (1992) Vet Rec, 131, pp. 202-203; Barlough, J., Stoddart, C.A., Feline coronaviral infections (1990) Infectious Diseases of Dog and Cat, pp. 300-311. , C. E. Greene, Ed.), Saunders, Philadelphia; Black, J.W., Recovery and in vitro cultivation of a coronavirus from laboratory-induced cases of feline infectious peritonitis (FIP). VM/SAC Vet Med Small Anim (1980) Clin, 75, pp. 811-814; Boom, R., Sol, C.J., Salimans, M.M., Jansen, C.L., Wertheim-Van Dillen, P.M., Van Der Noordaa, J., A rapid and simple method for purification of nucleic acids (1990) J. Clin. MicroBiol, 28, pp. 495-503; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J., Characterization of a temperature sensitive feline infectious peritonitis coronavirus. Arch (1989) Virol, 109, pp. 185-196; De Groot, R.J., Eweg, A.C., Florzinek, M.C., Spaan, W.J., Sequence analysis of the 3’~end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; De Groot, R., Horzinek, M., Feline infectious peritonitis (1995) The Coronaviridae, , S, G. Siddell, Ed.). Plenum, New York. In press; Evermann, J.F., Baumgartner, L., Ott, R.L., Davis, E.V., McKeirnan, A.J., Characterization of a feline infectious peritonitis virus isolate (1981) Vet Pathol, 18, pp. 256-265; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol, 61, pp. 2607-2613; Garwes, D.J., Stewart, F., Britton, P., The polypeptide of Mr 14000 of porcine transmissible gastroenteritis virus: Gene assignment and intracellular location (1989) J. Gen. Virol, 70, pp. 2495-2499; Gerber, J.D., Pfeiffer, N.E., Ingersoll, J.D., Christianson, K., Landon, R.M., Selzer, N.L., Beckenbauer, W.F.I., Characterization of an attenuated temperature sensitive feline infectious peritonitis vaccine virus (1990) Adv. Exp. Med. Biol, 276, pp. 481-489; Gooding, L.R., Virus proteins that counteract host immune defenses (1992) Cell, 71, pp. 5-7; Flerrewegh, A.A., De Groot, R.J., Cepica, A., Egberink, H.F., Florzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in feces, tissue, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. MicroBiol, 33, pp. 684-689; Higgins, D., Sharp, P., Fast and sensitive multiple sequence alignments on a micro computer. Comput Appl (1989) Biosci, 5, pp. 151-153; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses. Arch (1991) Virol, 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs); Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683. Vet (1991) MicroBiol, 28, pp. 13-24; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H.P., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci, 54, pp. 557-562; Horsburgh, B., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3rd end of canine coronavirus genomic RNA (1992) J. Gen. Virol, 73, pp. 2849-2862; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenterits coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Lai, M.C., Genetic recombination in RNA viruses (1992) Curr. Top. Microbiol. Immunol, 176, pp. 21-32; Lipman, D.J., Pearson, W.R., Rapid and sensitive protein similarity searches (1985) Science, 227, pp. 1435-1441; Loeffler, D.G., Ott, R.L., Evermann, J.F.P., Alexander, J.E., The incidence of naturally occurring antibodies against feline infectious peritonitis in selected cat populations (1978) Feline Pract, 8, pp. 43-47; McKeirnan, A.J., Evermann, J.F., Hargis, A., Miller, L.M., Ott, R.L., Isolation of feline coronavirus from two cats with diverse disease manifestations (1981) Feline Pract, 11 (3), pp. 16-20; Motokawa, K.P., Hohdatsu, T.P., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch Virol, 140, pp. 469-480; O’Reilly, K.J., Fishman, L.M., Hitchcock, L.M., Feline infectious peritonitis: Isolation of a coronavirus. Vet (1979) Rec, 104, p. 348; Osterhaus, A.D., Horzinek, M.C., Wirahadiredja, R.M.S., Feline infectious peritonitis (FIP) virus. IV. Propagation in suckling rat and hamster brain. Zentralbi. Veterinaermed (1978) Reihe, 8 (25), p. 816; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res, 37, pp. 1449-1453; Pedersen, N.C., Feline infectious peritonitis: Something old, something new (1976) Feline Pract, 6, pp. 42-51; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens utilizing feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet Res, 42, pp. 363-367; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res, 42, pp. 368-377; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections, part V. Feline enteric coronaviruses (1983) Feline Pract, 13 (4), pp. 13-19; Pedersen, N.C., Black, J.W., Attempted immunization of cats against feline infectious peritonitis, using avirulent live virus or sublethal amounts of virulent virus (1983) Am. J. Vet. Res, 44, pp. 229-234; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Molecular Biology and Pathogenesis of Coronaviruses, pp. 356-380. , Plenum, New York; Pedersen, N.C., Evermann, J.F., Alison, J., McKeirnan, A.I., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res, 45, pp. 2580-2585; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of fetine infectious peritonitis virus; FIPV-UCD2, FIPV- UCD3, and FIPV-UCD4. Compend (1985) Contin. Educ. Pract. Vet, 7, pp. 1001-1011; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infections (1987) Coronaviruses, pp. 529-550. , M. M. C. Lai and S. Stohlman, Eds.), Plenum, New York; Reed, P.A., Klepfer, S., Miller, T., Jones, E., Cloning and sequence analysis of the spike gene from several feline coronaviruses (1993) Coronaviruses; Molecular Biology and Virus-Host Interactions, pp. 17-21. , H. Laude and J. F. Vautherot, Eds.), Plenum. New York; Smith, G.L., Vaccinia virus glycoproteins and immune evasion (1993) J. Gen. Virol, 74, pp. 1725-1740; Sneath, P.H., Sokal, R.R., (1973) In ""Numerical Taxonomy, pp. 230-234. , Freeman, San Francisco; Sparkes, A.F.I., Gruffydd Jones, T.J., Flarbour, D.A., Feline infectious peritonitis: A review of clinicopathological changes in 65 cases, and a critical assessment of their diagnostic value. Vet (1991) Rec, 129, pp. 209-212; Sparkes, A.F.I., Gruffydd-Jones, T.J., Ftoward, P.E.-., Harbour, D.A., Coronavirus serology in healthy pedigree cats. Vet (1992) Rec, 131, pp. 35-36; Tung, F.Y., Abraham, S., Sethna, M., Hung, S.-L., Sethna, P., Hogue, B.G., Brian, O., The 9-kDa hydrophobic protein encoded at the 3’ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Vennema, H., Heijnen, L., Rottier, P.J., Horzinek, M.C., Spaan, W.J., A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-iike endoplasmic reticulum retention signal (1992) J. Virol, 66, pp. 4951-4956; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3’ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-44; Wold, W.S., Gooding, L., Region E3 of adenovirus: A cassette of genes involved in host immunosurveillance and viruscell interactions (1991) Virology, 184, pp. 1-8","De Groot, R.J.; Virology Unit, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: Groot@velmie.dgk.ruu.nl",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028863417
"Opstelten D.-J.E., Raamsman M.J.B., Wolfs K., Horzinek M.C., Rottier P.J.M.","7003742658;6603137050;6507471811;7102624836;7006145490;","Envelope glycoprotein interactions in coronavirus assembly",1995,"Journal of Cell Biology","131","2",,"339","349",,85,"10.1083/jcb.131.2.339","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028826654&doi=10.1083%2fjcb.131.2.339&partnerID=40&md5=54cbb77a1c9c6e672a7a602a756c3c71","Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Center for Biotechnology, Karolinska Institute, Novum, S-141 57 Huddinge, Sweden; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands","Opstelten, D.-J.E., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands, Center for Biotechnology, Karolinska Institute, Novum, S-141 57 Huddinge, Sweden; Raamsman, M.J.B., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Wolfs, K., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands, Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands","Coronaviruses are assembled by budding into smooth membranes of the intermediate ER-to-Golgi compartment. We have studied the association of the viral membrane glycoproteins M and S in the formation of the virion envelope. Using coimmunoprecipitation analysis we demonstrated that the M and S proteins of mouse hepatitis virus (MHV) interact specifically forming heteromultimeric complexes in infected cells. These could be detected only when the detergents used for their solubilization from cells or virions were carefully chosen: a combination of nonionic (NP-40) and ionic (deoxycholic acid) detergents proved to be optimal. Pulse-chase experiments revealed that newly made M and S proteins engaged in complex formation with different kinetics. Whereas the M protein appeared in complexes immediately after its synthesis, newly synthesized S protein did so only after a lag phase of >20 min. Newly made M was incorporated into virus particles taster than S, which suggests that it associates with preexisting S molecules. Using the vaccinia virus T7-driven coexpression of M and S we also demonstrate formation of M/S complexes in the absence of other coronaviral proteins. Pulse-chase labelings and coimmunoprecipitation analyses revealed that M and S associate in pre- Golgi membranes because the unglycosylated form of M appeared in M/S complexes rapidly. Since no association of M and S was detected when protein export from the ER was blocked by brefeldin A, stable complexes most likely arise in the ER-to-Golgi intermediate compartment. Sucrose velocity gradient analysis showed the M/S complexes to be heterogeneous and of higher order, suggesting that they are maintained by homo- and heterotypic interactions. M/S complexes colocalized with α-mannosidase II, a resident Golgi protein. They acquired Golgi specific oligosaccharide modifications but were not detected at the cell surface. Thus, the S protein, which on itself was transported to the plasma membrane, was retained in the Golgi complex by its association with the M protein. Because coronaviruses bud at pre-Golgi membranes, this result implies that the envelope glycoprotein complexes do not determine the site of budding. Yet, the self-association of the MHV envelope glycoproteins into higher order complexes is indicative of its role in the sorting of the viral membrane proteins and in driving the formation of the viral lipoprotein coat in virus assembly.",,"alpha mannosidase; brefeldin a; deoxycholic acid; detergent; lipoprotein; virus envelope protein; virus glycoprotein; article; endoplasmic reticulum; golgi complex; immunofluorescence; immunoprecipitation; murine hepatitis coronavirus; nonhuman; priority journal; virion; virus assembly; virus envelope; Animal; Biological Transport; Cell Line; Coronavirus Infections; Endoplasmic Reticulum; Glycoproteins; Golgi Apparatus; Mice; Murine hepatitis virus; Viral Envelope Proteins; Virus Assembly; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus",,"Rottier, P.J.M.; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,00219525,,JCLBA,"7593163","English","J. CELL BIOL.",Article,"Final",Open Access,Scopus,2-s2.0-0028826654
"Antún I.M., Suñé C., Meloen R.H., Borrás-Cuesta F., Enjuanes L.","57195390354;6701660310;7005880851;7003805889;7006565392;","A transmissible gastroenteritis coronavirus nucleoprotein epitope elicits T helper cells that collaborate in the in vitro antibody synthesis to the three major structural viral proteins",1995,"Virology","212","2", 71535,"746","751",,23,"10.1006/viro.1995.1535","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028784165&doi=10.1006%2fviro.1995.1535&partnerID=40&md5=df9501f71ee130a281269646f5329dfc","Centro Nacional de Biotecnología, CSIC, Department of Molecular and Cell Biology, Campus Universidad Autónoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, Netherlands; Departamento de Medicina Interna, Universidad de Navarra, Pamplona, Spain","Antún, I.M., Centro Nacional de Biotecnología, CSIC, Department of Molecular and Cell Biology, Campus Universidad Autónoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Suñé, C., Centro Nacional de Biotecnología, CSIC, Department of Molecular and Cell Biology, Campus Universidad Autónoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Meloen, R.H., Central Veterinary Institute, P.O. Box 65, 8200 AB Lelystad, Netherlands; Borrás-Cuesta, F., Departamento de Medicina Interna, Universidad de Navarra, Pamplona, Spain; Enjuanes, L., Centro Nacional de Biotecnología, CSIC, Department of Molecular and Cell Biology, Campus Universidad Autónoma de Madrid, Canto Blanco, 28049 Madrid, Spain","Four strong T cell epitopes have been identified studying the blastogenic response of lymphocytes from haplotype-defined transmissible gastroenteritis virus (TGEV) immune miniswine to sixty-one 15-mer synthetic peptides. Three of these epitopes are located on the nucleoprotein (N46, amino acids 46 to 60; N272, amino acids 272 to 286; and N321, amino acids 321 to 335), and one on the membrane protein (M196, amino acids 196 to 210). N321 peptide induced the highest T cell response and was recognized by immune miniswine lymphocytes with haplotypes dd, aa, and cc. T lymphocytes from peptide N321 immune miniswine reconstituted the in vitro synthesis of TGEV-specific antibodies by complementing CD4- TGEV-immune cells. This response was directed at least against the three major structural proteins. The synthesized antibodies specific for S protein preferentially recognized discontinous epitopes and neutralized TGEV infectivity. These results show that peptide N321 defines a functional T helper epitope eliciting T cells capable of collaborating with B cells specific for different proteins of TGEV. © 1995 Academic Press, Inc.",,,"Saif, L.J., Wesley, R.D., (1992) Diseases of Swine, pp. 362-386. , A. D. Leman et al., Eds.), Iowa State Univ, Press, Ames; Spaan, W., Cavanagh, D., Hcrzinek, M.C., (1990) Immunochemistry of Viruses, II. the Basis for Serodtagnosis and Vaccines, pp. 359-375. , M. H. V, Regenmortel and A. R. Neurath, Eds.), Elsevier, Amsterdam; Enjuanes, L., Van Der Zeijst, B.A.M., (1995) Coronaviruses, pp. 337-376. , S, G. Siddell, Ed.), Plenum Press, New York; Godet, M., L’haridon, R., Vautherot, J.F., Laude, H., (1992) Virology, 188, pp. 666-675; Jimenez, G., Correa, L., Melgosa, M.P., Bullido, M.J., Enjuanes, L., (1986) J. Virol, 60, pp. 131-139; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., (1986) J. Gen. Virol, 67, pp. 119-130; Bohl, E.H., Saif, L.J., (1975) Infect. Immun, 11, pp. 23-32; Montgomery, P.C., Cohn, J., Lally, E.T., (1974) Adv. Exp. Med. Biol, 45, pp. 453-465; Strober, W., Jacobs, D., (1985) Mucosal Immunity, pp. 1-30. , J. I. Gallin, and A. S. Fauci, Eds.), Raven Press, New York; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., (1977) Am. J. Vet. Res, 38, pp. 1285-1288; De Diego, M., Laviada, M.D., Enjuanes, L., Escribano, J.M., (1992) J. Virol, 66, pp. 6502-6508; Bullido, M.J., Correa, I., Jimenez, G., Sune, C., Gebauer, F., Enjuanes, L., (1989) J. Gen. Virol, 70, pp. 659-672; Delmas, B., Gelfi, J., Laude, H., (1986) J. Gen. Virol, 67, pp. 1405-1418; Correa, I., Jimenez, G., Sune, C., Bullido, M.J., Enjuanes, L., (1988) Virus Res, 10, pp. 77-94; Correa, I., Gebauer, F., Bullido, M.J., Suho, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., (1990) Gen. Virol, 71, pp. 271-279; Schwartz, R., (1985) Anno. Rev, Immunol, 3, pp. 237-262; Delisi, C., Berzofsky, J.A., (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 7048-7052; Feller, D.C., De La Cruz, V.F., (1991) Nature, 349, pp. 720-721; Rothbard, J., Taylor, W., (1988) EMBO J, 7, pp. 93-100; Boots, A.M.H., Benaissatrouw, B.J., Hesselink, W., Rijke, E., Schrier, C., Anti Hensen, E.J., (1992) Vaccine, 10, pp. 119-124; Bergmann, G., McMillan, M., Stohlman, S., (1993) J. Virol, 67, pp. 7041-7049; Flory, E., Pfleiderer, M., Stuhler, A., Wege, F.I., (1993) Eur. J. Immunol, 23, pp. 1757-1761; Mobley, J., Evans, G., Dailey, M.O., Perlman, S., (1992) Virology, 187, pp. 443-452; Wege, F.I., Schliephake, A., Korner, F.I., Flory, E., Wege, F.I., (1993) J. Gen. Virol, 74, pp. 1287-1294; Lunney, J.K., Pescovitz, M.D., Sachs, D., (1986) Swine in Biomedical Research, pp. 1821-1836. , M. E. Tumbleson, Ed.), Plenum, New York; Sachs, D., Leight, G., Cone, J., Schwarz, S., Stuart, L., Rosem-Berg, S., (1976) Transplantation, 22, pp. 559-567; Anton, I.M., Gonzalez, S., Bullido, M.J., Enjuanes, L., (1995) Submitted for Publication; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, J., Sune, C., Bullido, M.J., Gebauer, F., Enjuanes, L., (1990) Virology, 174, pp. 410-417; Margalit, H., Spouge, J.L., Cornette, J.L., Cease, K.B., Delisi, C., Berzofsky, J.A., (1987) J. Immunol, 138, pp. 2213-2229; Rothschild, M.F., Hill, H.T., Christian, L.L., Lie, W.R., Warner, C.M., (1984) Am. J. Vet. Res, 45, pp. 1216-1218; Kumar, A., Arora, R., Kaur, P., Chauhan, V.S., Sharma, P., (1992) J. Immunol, 148, pp. 1499-1505; Panina-Sordignon, P.A., Tan, A., Termijtelen, A., Demotz, S., Cor-Radin, G.P., Lanzavecchia, A., (1989) Eur. J. Immunol, p. 2242; Casal, I., Vinuela, E., Enjuanes, L., (1987) Immunology, 62, pp. 207-213; Julius, M.H., Simpson, E., Plerzemberg, L.A., (1973) Eur. J. Immunol, 3, pp. 645-649; Laviada, M.D., V’degain, S.P., Moreno, L., Alonso, F., Enjuanes, L., Escribano, J.M., (1990) Virus Res, 16, pp. 247-254; Milich, D.R., (1989) Adv. Immunol, 45, pp. 195-281; Milich, D.R., McLachlan, A., Thornton, G.B., Hughes, J.L., (1987) Nature, 329, pp. 547-549; Gebauer, F., Posthumus, W.A.P., Correa, I., Sune, C., Sbnchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., (1991) Virology, 183, pp. 225-238; Pescovitz, M.D., Lunney, J.L., Sachs, D., (1984) J. Immunol, 133, pp. 368-375",,,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028784165
"Enjuanes L., Smerdou C., Castilla J., Anton I.M., Torres J.M., Sola I., Golvano J., Sanchez J.M., Pintado B.","7006565392;6602856664;8851950500;57198264385;35516513600;7003336781;6603190169;57212742351;6701776268;","Development of protection against coronavirus induced diseases: A review",1995,"Advances in Experimental Medicine and Biology","380",,,"197","211",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028875077&partnerID=40&md5=2f370d4fdf0ff321584e8e2199a49315","Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Enjuanes, L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Smerdou, C., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Castilla, J., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Anton, I.M., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Torres, J.M., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Golvano, J., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sanchez, J.M., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Pintado, B., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",[No abstract available],,"epitope; inactivated virus vaccine; live vaccine; recombinant protein; recombinant vaccine; virus envelope protein; virus glycoprotein; virus nucleoprotein; virus protein; virus vaccine; virus vector; cellular immunity; conference paper; Coronavirus; humoral immunity; immunization; immunogenicity; infection prevention; intraperitoneal drug administration; Murine hepatitis coronavirus; nonhuman; priority journal; subcutaneous drug administration; Vaccinia virus; virus infection; virus inhibition; virus neutralization; Animal; Antigens, Viral; B-Lymphocytes; Coronavirus; Coronavirus Infections; Drug Design; Epitopes; Human; Support, Non-U.S. Gov't; T-Lymphocytes; Vaccines, Synthetic; Viral Vaccines; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus",,"Enjuanes, L.; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"8830481","English","ADV. EXP. MED. BIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0028875077
"Lamarre A., Talbot P.J.","7004646746;7102670281;","Protection from lethal coronavirus infection by immunoglobulin fragments",1995,"Journal of Immunology","154","8",,"3985","3990",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-14844365503&partnerID=40&md5=834032a06f496fd37516f88dc99f8859","Virology Research Center, Armand-Frappier Institute, University of Quebec, Laval, Que., Canada; Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Lamarre, A., Virology Research Center, Armand-Frappier Institute, University of Quebec, Laval, Que., Canada; Talbot, P.J., Virology Research Center, Armand-Frappier Institute, University of Quebec, Laval, Que., Canada, Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Molecular mechanisms of in vitro and in vivo virus neutralization by specific Ab remain largely undefined. Murine coronaviruses provide an excellent animal model for such studies. To determine the role of Ab bivalency and the contribution of its Fc portion in the neutralization of viral infectivity and passive protection of mice by an in vitro neutralizing and in vivo protective mAb (7-10A), F(ab')2 and Fab fragments were generated and their biologic properties were examined. The two fragments reacted in ELISA like the whole Ab against viral Ag or specific anti-idiotypic Abs. The affinity constants of the different Ab preparations were determined by surface plasmon resonance using immobilized anti-idiotypic Abs. The apparent affinity constant of the whole Ab molecule was 7.0 × 109 M-1 and was reduced 2-fold for F(ab')2 fragments and 14-fold for Fab molecules. Like whole Ab, both F(ab')2 and Fab fragments could neutralize virus in vitro and passively protect mice in vivo. However, the efficiency of in vivo neutralization by Fab fragments was reduced compared with the bivalent molecules, despite almost identical half-lives of both types of Ab fragments. These results demonstrate that in vitro and in vivo virus neutralization mechanisms by this Ab are independent of Fc-mediated functions and bivalency, but are probably influenced by Ab avidity. Also, this is the first report of in vivo protection against a viral infection by Fab fragments of antiviral Ab. Copyright © 1995 by The American Association of Immunologists.",,,,"Talbot, P.J.; Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada",,,00221767,,JOIMA,,"English","J. Immunol.",Article,"Final",,Scopus,2-s2.0-14844365503
"Karaivanova G., Gomwalk N.E., Okunghae H.O.","6602923928;6603542998;6504148939;","Complement fixing antibodies to respiratory viruses in children in Jos, Nigeria",1995,"Journal of Tropical Pediatrics","41","6",,"325","327",,,"10.1093/tropej/41.6.325","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029564185&doi=10.1093%2ftropej%2f41.6.325&partnerID=40&md5=842c842d6ce230f98c7d5a6c5f17f1f9","Department of Medical Microbiology, University of Jos, Jos, Nigeria; Department of Virology, Institute of Infectious and Parasitic Diseases, Sofia, Bulgaria; Department of Paediatrics, University of Jos, Jos, Nigeria","Karaivanova, G., Department of Medical Microbiology, University of Jos, Jos, Nigeria; Gomwalk, N.E., Department of Medical Microbiology, University of Jos, Jos, Nigeria, Department of Virology, Institute of Infectious and Parasitic Diseases, Sofia, Bulgaria; Okunghae, H.O., Department of Paediatrics, University of Jos, Jos, Nigeria","Summary: One-hundred serum samples obtained from children in Jos were tested for the presence of complement fixing antibodies against several respiratory viruses. Sixty-two per cent of the samples were positive for adenoviruses, 53 per cent for para-influenza viruses, 47 and 41 per cent for influenza A and B, respectively, 31 per cent for respiratory syncytial virus, 29 per cent for coronaviruses, and 19 per cent for reoviruses. © 1995 Oxford University Press.",,"complement fixing antibody; Adenovirus; article; child; Coronavirus; human; infant; Influenza virus A; Influenza virus B; major clinical study; newborn; Nigeria; Parainfluenza virus; Reovirus; Respiratory syncytial pneumovirus; respiratory tract infection; virus infection","Bulla, H., Hitze, K., Acute respiratory infections: A review (1978) Bull Wld Hlth Org, 56, pp. 481-498; Pringle, C.R., Progress towards control of the acute respiratory viral diseases of childhood (1987) Bull Wld Hlth Org, 65, pp. 133-137; Global, W.H.O., Mortality from acute respiratory infec¬tions among children aged below 5 years (1987) Bull Wld Hlth Org, 65, pp. 112-116; Rankin, J.R., Analysis of medical admissions to University College Hospital, Ibadan— 1958 (1961) W Afr Med J, 10, pp. 3-31; Gans, B., Paediatric problems in Lagos (1961) W Afr Med J, 10, pp. 33-46; Obi, J.O., Analysis of paediatric medical cases admitted to children’s clinic, Benin City (1976) Nig Med J, 6, pp. 69-73; Odiase, G.I., The leading causes of death among inpatients of the University of Benin Teaching Hospital in the year 1974 (1978) Nig Med J, 8, pp. 242-248; Warrel, D.A., Respiratory tract infections in the tropics (1975) The Practitioner, 215, pp. 740-746; Osuhor, P.C., Etta, K.M., Morbidity patterns amongst children in a semi-urban community in Northern Nigeria (1980) J Trop Pediat, 26, pp. 99-103; Dobrev, I., Michailov, A., Karaivanova, G., The level of complement binding antibodies against some respiratory viruses (1978) Prob Infect Paras Dis, 6, pp. 20-27; Ogunbi, O., Bacteriological and viral aetiology of bron¬chiolitis and bronchopneumonia in Lagos children (1970) J Trop Med Hyg, 73, pp. 138-140; Olabode, A.O., Fagbami, A.H., Oyejide, C.O., Olaleye, O.D., Omilabu, S.A., Detection of adenovirus infection in children sufferingfrom acute respiratory infections (ARI) using complement fixation and immunofluorescent tech¬niques (1989) Nig J Immunol, 2, p. 63; Njoku-Obi, A.N., Ogunbi, O., Viral respiratory diseases in Nigeria: A serological survey II complement fixing antibody levels of adenoviruses, respiratory syncytial virus, psittacosis virus (1966) J Trop Med Hyg, 69, pp. 147-149; Dym, A.M., Schuit, K.E., Nwankwo, M.U., Omene JA. Respiratory syncytial virus and acute lower respiratory infections in Benin City (1986) Nigeria. Paediat Infect Dis, 5, pp. 717-718; Glezen, W.P., Denny, F.W., Epidemiology of acute lower respiratory diseases in children (1973) N Engl J Med, 288, pp. 498-505","Karaivanova, G.; Department of Medical Microbiology, University of Jos, JosNigeria",,,01426338,,JTRPA,"8606436","English","J. Trop. Pediatr.",Article,"Final",,Scopus,2-s2.0-0029564185
"Charley B., Nowacki W., Vaiman M.","55246691600;57198092280;7005079334;","Frequency of interferon-alpha-secreting blood leukocytes in irradiated and bone-marrow-grafted pigs",1995,"Veterinary Research","26","4",,"292","299",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028999486&partnerID=40&md5=d7ed60ef0fb3e80f6d481ba2573da8f8","INRA, virologie et immunologie moléculaires Jouy-en-Josas, France; Laboratoire mixte CEA-INRA de radiobiologie appliquée, 78350 Jouy-en-Josas, France","Charley, B., INRA, virologie et immunologie moléculaires Jouy-en-Josas, France; Nowacki, W., INRA, virologie et immunologie moléculaires Jouy-en-Josas, France; Vaiman, M., Laboratoire mixte CEA-INRA de radiobiologie appliquée, 78350 Jouy-en-Josas, France","The effects of irradiation were studied on porcine interferon-alpha (IFN-α) secreting cells (IFN-α SC). IFN-α SC were characterized by an ELISPOT assay on non-adherent PBMC following incubation with the transmissible gastroenteritis coronavirus. In vitro irradiation of PBMC was followed by a decrease in the number of IFN-α SC while IFN-γ production and cell viability were not affected. These data indicate that porcine IFN-α SC are relatively radiosensitive. Indeed, the frequency of blood IFN-α SC decreased markedly and rapidly after in vivo whole body or partial lympnoid irradiation. In addition, within several days of compatible bone-marrow engraftment in the irradiated animals, the number of blood IFN-α SC returned to normal values. These data demonstrate that circulating porcine IFN-α SC are derived from bone-marrow progenitors. © 1995.","interferon-alpha / leukocyte / bone marrow / irradiation / transmissible gastroenteritis virus / porcine","Animal; Bone Marrow; Bone Marrow Cells; Bone Marrow Transplantation; Enzyme-Linked Immunosorbent Assay; Interferon-alpha; Leukocyte Count; Leukocytes; Swine; Transmissible gastroenteritis virus",,"Charley, B.",,,09284249,,VEREE,"7550400","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0028999486
"Gonin P., Oualikene W., Fournier A., Soulier M., Audonnet J.-C., Riviere M., Eloit M.","6701502814;6507397088;7401993763;57213130114;6602099062;57197368772;55497906000;","Evaluation of a replication-defective adenovirus expressing the feline infectious peritonitis membrane protein as a vaccine in cats",1995,"Vaccine Research","4","4",,"217","227",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029620239&partnerID=40&md5=8c08bbab2cd89fbd69c6df5f8b085b2e","Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France","Gonin, P., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Oualikene, W., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Fournier, A., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Soulier, M., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Audonnet, J.-C., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Riviere, M., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France; Eloit, M., Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France","Feline infectious peritonitis (FIP) is a progressive and fatal systemic disease of domestic and wild felida that has continued to defy vaccination. It is induced by several closely related strains of coronavirus that produce a wide spectrum of multiorgan lesions due to the degree of cell-mediated immunity and the formation and deposition of vascular immune complexes. We describe the construction of a recombinant adenovirus type 5 that expresses the membrane glycoprotein (M) of FIP virus under the control of the major late promoter of adenovirus type 2 (MLP). This recombinant was used as an experimental vaccine in cats (six vaccinated and four controls) in a two injection regime at DO and D21. Cats developed no or only low amounts of anti-M antibodies. Nevertheless, a protection of 50% was recorded after a challenge that induced clinical signs, gross lesions, and mortality in control cats.",,"antibody; membrane protein; vaccine; adenovirus 2; adenovirus 5; animal cell; animal experiment; animal model; antibody production; article; cat; cellular immunity; controlled study; coronavirus; immune complex deposition; intramuscular drug administration; mortality; nonhuman; priority journal; promoter region; vaccination; virus infection; virus recombinant",,"Eloit, M.; Unite Genet. Moleculaire Virale, INRA, Ecole Nationale Veterinaire, 7 avenue du General de Gaulle, 94704 Maisons-Alfort Cedex, France",,,10567909,,VAREE,,"English","VACCINE RES.",Article,"Final",,Scopus,2-s2.0-0029620239
"McCutcheon A.R., Roberts T.E., Gibbons E., Ellis S.M., Babiuk L.A., Hancock R.E.W., Towers G.H.N.","7003513378;10138831200;7003880698;7402787602;35427029400;7201916259;7005453949;","Antiviral screening of British Columbian medicinal plants",1995,"Journal of Ethnopharmacology","49","2",,"101","110",,116,"10.1016/0378-8741(95)90037-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029592661&doi=10.1016%2f0378-8741%2895%2990037-3&partnerID=40&md5=c05883d3664c9544fae31dc86a4921db","Department of Botany, University of British Columbia, #3515- 6270 University Blvd, Vancouver, BC V6T 1Z4, Canada; Veterinary Infectious Disease Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Department of Microbiology, University of British Columbia, 232-6174 University Blvd, Vancouver, BC V6T 1Z4, Canada","McCutcheon, A.R., Department of Botany, University of British Columbia, #3515- 6270 University Blvd, Vancouver, BC V6T 1Z4, Canada; Roberts, T.E., Veterinary Infectious Disease Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Gibbons, E., Veterinary Infectious Disease Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Ellis, S.M., Department of Botany, University of British Columbia, #3515- 6270 University Blvd, Vancouver, BC V6T 1Z4, Canada; Babiuk, L.A., Veterinary Infectious Disease Organization, 124 Veterinary Road, Saskatoon, Sask. S7N 0W0, Canada; Hancock, R.E.W., Department of Microbiology, University of British Columbia, 232-6174 University Blvd, Vancouver, BC V6T 1Z4, Canada; Towers, G.H.N., Department of Botany, University of British Columbia, #3515- 6270 University Blvd, Vancouver, BC V6T 1Z4, Canada","One hundred methanolic plant extracts were screened for antiviral activity against seven viruses. Twelve extracts were found to have antiviral activity at the non-cytotoxic concentrations tested. The extracts of Rosa nutkana and Amelanchier alnifolia, both members of the Rosaceae, were very active against an enteric coronavirus. A root extract of another member of the Rosaceae, Potentilla arguta, completely inhibited respiratory syncytial virus. A Sambucus racemosa branch tip extract was also very active against respiratory syncytial virus while the inner bark extract of Oplopanax horridus partially inhibited this virus. An extract of Ipomopsis aggregata demonstrated very good activity against parainfluenza virus type 3. A Lomatium dissectum root extract completely inhibited the cytopathic effects of rotavirus. In addition to these, extracts prepared from the following plants exhibited antiviral activity against herpesvirus type 1: Cardamine angulata, Conocephalum conicum, Lysichiton americanum, Polypodium glycyrrhiza and Verbascum thapsus. © 1995.","Amelanchier alnifolia; Antiviral activity; Cardamine angulata; Conocephalum conicum; Ethnopharmacology (British Columbia); Ipomopsis aggregata; Lomatium dissectum; Lysichiton americanum; Oplopanax horridus; Polypodium glycyrrhiza; Potentilla arguta; Rosa nutkana; Sambucus racemosa; Traditional medicines (British Columbia); Verbascum thapsus","antivirus agent; plant extract; antiviral activity; article; canada; controlled study; coronavirus; cytopathogenic effect; drug screening; herpes simplex virus 1; herpes virus; parainfluenza virus 3; respiratory syncytial pneumovirus; rotavirus; traditional medicine; Animals; Antiviral Agents; British Columbia; Cell Line; Plant Extracts","Arisawa, Kinghorn, Cordell, Phoebe, Farnsworth, Plant anticancer agents VI. Schottenoi Glucoside from Baccharis cordifolia and Ipomopsis aggregata (1985) Planta Medica, 1985, pp. 544-545; Cardellina, Vanwagenen, Antifungal agents from Lomatium dissectum (1985) Abstracts of the International Research Congress on Natural Products, , University of North Carolina, Chapel Hill, N.C, Abstract 211; Chang, Cesarman, Pessin, Lee, Culpepper, Knowles, Moore, Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma (1994) Science, 266, pp. 1865-1869; Chang, Letters (1995) Science, 268, p. 1078; Cohen, AIDS mood upbeat — for a change (1995) Science, 267, pp. 959-960; Compton, Upper North Wakashan and Southern Tsimshian Ethnobotany (1993) Ph.D. Thesis, , University of British Columbia; De Clerq, Recent advances in the search for selective antiviral agents (1988) Advances in Drug Research, 17, pp. 1-59; De Clerq, Antiviral agents characteristic activity spectrum depending on the molecular target with which they interact (1993) Advances in Virus Research, 43, pp. 1-55; Densmore, Uses of plants by the Chippewa Indians (1928) Smithsonian Institution: B.A.E. Annual Report, 44, pp. 273-379; Galasso, Promises to keep: clinical use of antiviral drugs (1988) Clinical Use of Antiviral Drugs, p. 413. , E. De Clerq, Martinus Nijhoff Publishing, Boston; Girre, Amoros, Conan, Percehais, Yvin, Zerial, On the antiherpetic activity of extracts from marine and land plants and the standardization of the study of antiviral properties (1987) Fitoterapia, 58 (6), pp. 371-378; Gunther, (1973) Ethnobotany of Western Washington, p. 71. , University of Washington Press, Seattle; Hudson, (1990) Antiviral Compounds from Plants, p. 200. , CRC Press, Boca Raton, FL; Husson, Vilagines, Delaveau, Research into antiviral properties of a few natural extracts (1986) Annales Pharmaceutiques Francaises, 44 (1), pp. 41-48; Majak, McDiarmid, Hall, The cyanide potential of Saskatoon Serviceberry Amelanchier alnifolia and Chokecherry Prunus virginiana (1981) Canadian Journal of Animal Science, 61 (3), pp. 681-686; Majak, Bose, Quinton, Prunasin, the cyanogenic glycoside in Amelanchier alnifolia (1978) Phytochemistry, 17 (4), p. 803; McCutcheon, Ellis, Hancock, Towers, Antibiotic screening of medicinal plants of the British Columbian native peoples (1993) Journal of Ethnopharmacology, 37, pp. 213-223; McCutcheon, Ellis, Hancock, Towers, Antifungal screening of medicinal plants of the British Columbian native peoples (1994) Journal of Ethnopharmacology, 44, pp. 157-169; Mi, Li, Su, Wang, Zhao, Jiang, Studies on chemical constituents and antifungal activites of essential oil from Oplopanax elatus, Nakai (1987) Acta Pharmaceutica Sinica, 232 (7), pp. 549-552; Moerman, Medicinal Plants of Native America (1986) Research Reports in Ethnobotany, Contribution 2, p. 534. , University of Michigan Museum of Anthropology, Ann Arbor, MI, Technical Reports, Number 19; Palmer, (1975) Shuswap Indian Ethnobotany, , Dept. of Anthropology, University of Nevada, Las Vegas, NV, Cited in Moerman, 1986; Perry, Ethnobotany of the Indians of the interior of British Columbia (1952) Museum and Art Notes, 2 (2), pp. 36-43; Pojar, MacKinnon, (1994) Plants of Coastal British Columbia, , Lone Pine Publishing, Vancouver, B.C; Selenina, Zozulya, Yakovleva, Polyphenols of Potentilla erecta and their biological activity (1973) Rastit Resur, 9 (3), pp. 409-414; Smith, Materia medica of the Bella Coola and neighboring tribes of British Columbia (1928) National Museum of Canada Bulletin, 56, pp. 47-68; Steedman, The ethnobotany of the Thompson Indians of British Columbia. Based on the field notes of James A. Teit (1929) Smithsonian Institution: Bureau of American Ethnology Annual Report, 45, pp. 441-522; Turner, The ethnobotany of the Bella Coola Indians of British Columbia (1973) Syesis, 6, pp. 193-220; Turner, Food Plants of the British Columbian Indians: Coastal Peoples (1975) British Columbia Provincial Museum Handbook No. 34, p. 253. , Royal British Columbian Provincial Museum, Victoria, B.C; Turner, Food Plants of the British Columbian Indians: Interior Peoples (1978) British Columbia Provincial Museum Handbook No. 36, p. 241. , Royal British Columbian Provincial Museum, Victoria, B.C; Turner, Traditional use of Devil's Club (Oplopanax horridus; Araliaceae) by native peoples in western North America (1982) Journal of Ethnobiology, 2 (1), pp. 17-38; Turner, Bell, Ethnobotany of the Southern Kwakiutl Indians of British Columbia (1973) Economic Botany, 27, pp. 257-310; Turner, Hebda, Contemporary use of bark for medicine by two Salishan native elders of southeast Vancouver Island, Canada (1990) Journal of Ethnopharmacology, 29 (1), pp. 59-72; Turner, Bouchard, Kennedy, Ethnobotany of the Okanagan-Colville Indians of British Columbia and Washington (1980) British Columbia Provincial Museum No. 21. Occasional Papers Series, p. 156. , British Columbia Provincial Museum, Victoria, British Columbia; Turner, Thompson, Thompson, York, Thompson Ethnobotany: Knowledge and Uses of Plants by the Thompson Indians (1990) British Columbia Provincial Museum Memoir No. 25, p. 321. , British Columbia Provincial Museum, Victoria, British Columbia; Vanwagenen, Cardellina, Native American food and medicinal plants 7. Antimicrobial tetronic acids (1986) Tetrahedron, 42 (4), pp. 1117-1122; Vesikari, Isolauri, Ruuska, Delem, Andre, Rotavirus: new vaccine and vaccination (1988) Applied Antiviral Research (Volume 1): New Vaccines and Chemotherapy, p. 306. , E. Kurstak, R.G. Marusyk, F.A. Murphy, M.H.V. Van Regenmortel, Plenum Medical Book Co, New York","McCutcheon, A.R.; Department of Botany, University of British Columbia, #3515- 6270 University Blvd, Vancouver, BC V6T 1Z4, Canada",,,03788741,,JOETD,"8847882","English","J. Ethnopharmacol.",Article,"Final",,Scopus,2-s2.0-0029592661
"Yu W., Leibowitzt J.L.","55473188900;57195389432;","A conserved motif at the 3' end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication",1995,"Virology","214","1", 79947,"128","138",,43,"10.1006/viro.1995.9947","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028875939&doi=10.1006%2fviro.1995.9947&partnerID=40&md5=6aef969edab376ac2c5ff803d93ffbde","Department of Pathology and Laboratory Medicine, The University of Texas Medical School at Houston, Houston, Texas 77030, United States; Department of Pathology and Laboratory Medicine, Texas A and M University College of Medicine, 208 Reynolds Building, College Station, TX 77843-1114, United States; Department of Pathology and Laboratory Medicine, Texas A and M University College of Medicine, 208 Reynolds Building, College Station, TX 77843-1114, United States","Yu, W., Department of Pathology and Laboratory Medicine, The University of Texas Medical School at Houston, Houston, Texas 77030, United States, Department of Pathology and Laboratory Medicine, Texas A and M University College of Medicine, 208 Reynolds Building, College Station, TX 77843-1114, United States; Leibowitzt, J.L., Department of Pathology and Laboratory Medicine, Texas A and M University College of Medicine, 208 Reynolds Building, College Station, TX 77843-1114, United States","A conserved 11-nucleotide sequence, UGAAUGAAGUU, at the 3' end of the genomic RNA of coronavirus mouse hepatitis virus was required for host protein binding and viral RNA synthesis. An RNA probe containing this 11-nucleotide sequence bound four cellular proteins with a highly labeled protein of 120 kDa and three minor species with sizes of 103, 81, and 55 kDa. Mutation of the 11-nucleotide motif abolished cellular protein binding. The RNA-protein complexes observed with cytoplasmic extracts from MHV-JHM-infected cells in both RNase protection/gel mobility shift and UV cross-linking assays were indistinguishable from those observed with extracts from uninfected cells. Both negative-strand synthesis and positive-strand replication of viral defective interfering RNAs in the presence of helper virus were affected by mutations that disrupt RNA-protein complex formation, even though the 11 mutated nucleotides were converted to the wild-type sequence, presumably by recombination with helper virus. Kinetic analysis indicated that recombination between DI RNA and helper virus occurred relatively early in the MHV replicative cycle at 5.5 to 7.5 hr postinfection, a time when viral RNA synthesis and replication of positive-strand DI RNA were at barely detectable levels. A DI RNA with a mutation upstream of the protein binding element replicated as efficiently as wild type without undergoing recombination. Thus, the 11-nucleotide conserved host protein binding motif appears to play an important role in viral RNA replication. © 1995 Academic Press, Inc.",,,"Andino, R., Rieckhof, G.E., Baltimore, D., Afunctional ribo-nucleoprotein complex forms around the 5' end of poliovirus RNA (1990) Cell, 63, pp. 369-380; Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., Poliovirus RNA synthesis utilizes an RNP complex formed around the 5' end of viral RNA (1993) EMBO J, 12, pp. 3587-3598; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol, 48, pp. 633-640; Brian, D.A., Chang, R.Y., Hofmann, M.A., Sethna, P.B., Role of subgenomic minus-strand RNA in coronavirus replication (1994) Arch. 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Virol, 67, pp. 7215-7222; Kim, Y.N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepato-tropic strain MHV-3 (1981) J. 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Virol, 68, pp. 3656-3666; Yen, J.H., Chang, S.C., Hu, C.R., Chu, S.C., Lin, S.S., Hsieh, Y.S., Chang, M.F., Cellular proteins specifically bind to the 5'-noncoding region of hepatitis C virus RNA (1995) Virology, 208, pp. 723-733; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3' end of mouse hepatitis virus genomic RNA (1995) J. Virol, 69, pp. 2016-2023","Leibowitzt, J.L.; Department of Pathology and Laboratory Medicine, Texas A and M University College of Medicine, 208 Reynolds Building, College Station, TX 77843-1114, United States",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0028875939
"Chen D.S., Asanaka M., Yokomori K., Wang F.-I., Hwang S.B., Li H.-P., Lai M.M.C.","16165697600;6602256485;57206215028;7501310725;7404626445;9276641400;7401808497;","A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus",1995,"Proceedings of the National Academy of Sciences of the United States of America","92","26",,"12095","12099",,68,"10.1073/pnas.92.26.12095","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029608722&doi=10.1073%2fpnas.92.26.12095&partnerID=40&md5=d96b1dbb902d8186f42fc9b9d7d1ee8d","Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Tampa Bay Research Institute, St. Petersburg, FL 33716, United States; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, United States; School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Inst. of Environ. and Life Science, Hallym Academy of Sciences, Hallym University, Chuncheon, Kangwon-Do, 200-702, South Korea","Chen, D.S., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Asanaka, M., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States, Tampa Bay Research Institute, St. Petersburg, FL 33716, United States; Yokomori, K., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, United States; Wang, F.-I., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States, School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan; Hwang, S.B., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States, Inst. of Environ. and Life Science, Hallym Academy of Sciences, Hallym University, Chuncheon, Kangwon-Do, 200-702, South Korea; Li, H.-P., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Howard Hughes Medical Institute, School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States","Mouse hepatitis virus (MHV), a murine coronavirus known to cause encephalitis and demyelination, uses murine homologues of carcinoembryonic antigens as receptors. However, the expression of these receptors is extremely low in the brain. By low-stringency screening of a mouse brain cDNA library, we have identified a member of the pregnancy-specific glycoprotein (PSG) subgroup of the carcinoembryonic antigen gene family. Unlike other PSG that are expressed in the placenta, it is expressed predominantly in the brain. Transfection of the cDNA into COS-7 cells, which lack a functional MHV receptor, conferred susceptibility to infection by some MHV strains, including A59, MHV-2, and MHV-3, but not JHM. Thus, this is a virus strain- specific receptor. The detection of multiple receptors for MHV suggests the flexibility of this virus in receptor utilization. The identification of a PSG predominantly expressed in the brain also expands the potential functions of these molecules.","brain expression; carcinoembryonic antigen; coronavirus; virus receptor","brain protein; carcinoembryonic antigen; complementary dna; glycoprotein; virus receptor; animal cell; antigen specificity; article; female; gene expression regulation; mouse; murine hepatitis coronavirus; nonhuman; pregnancy; priority journal; protein determination; receptor binding; receptor occupancy; sequence homology; strain difference; Amino Acid Sequence; Animals; Base Sequence; Brain; Carcinoembryonic Antigen; Cell Line; Cercopithecus aethiops; Female; Gene Library; Kidney; Mice; Mice, Inbred C57BL; Molecular Sequence Data; Murine hepatitis virus; Organ Specificity; Placenta; Polymerase Chain Reaction; Pregnancy; Pregnancy Proteins; Receptors, Virus; Sequence Homology, Amino Acid; Transfection; Animalia; Coronavirus; Hepatitis virus A; Murinae; Murine hepatitis virus","Berberian, L., Goodglick, L., Kipps, T.J., Braun, J., (1993) Science, 261, pp. 1588-1591; Yokomori, K., Lai, M.M.C., (1992) J. Virol., 66, pp. 6194-6199; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G., Beauchemin, N., Holmes, K.V., (1993) J. Virol., 67, pp. 1-8; Robb, J.A., Bond, C.W., (1979) Comp. Virol., 14, pp. 193-247; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., (1982) Virology, 119, pp. 358-371; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., (1986) J. Virol., 59, pp. 463-471; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., (1986) J. Virol., 58, pp. 869-875; Williams, R.K., Jiang, G., Holmes, K.V., (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G., Holmes, K.V., Dieffenbach, C.W., (1991) J. Virol., 65, pp. 6881-6891; Yokomori, K., Lai, M.M.C., (1992) J. Virol., 66, pp. 6931-6938; Nedellec, P., Dveksler, G.A., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., (1994) J. 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USA, 85, pp. 4648-4652; Ellis, L., Clauser, E., Morgan, D.O., Edery, M., Roth, R.A., Rutter, W.J., (1986) Cell, 45, pp. 721-732","Lai, M.M.C.; Department of Microbiology, Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033-1054, United States",,,00278424,,PNASA,"8618851","English","PROC. NATL. ACAD. SCI. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0029608722
"Bos E.C.W., Heijnen L., Luytjes W., Spaan W.J.M.","7005778356;7004331664;6701683324;7007172944;","Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion",1995,"Virology","214","2", 70056,"453","463",,70,"10.1006/viro.1995.0056","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029592197&doi=10.1006%2fviro.1995.0056&partnerID=40&md5=bb28136e0b159e4a312dfa9b54994aca","Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands","Bos, E.C.W., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands; Heijnen, L., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands; Luytjes, W., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands","The spike (S) protein of murine coronavirus strain A59 (MHV-A59) is a type I membrane protein that induces membrane fusion. In this study we have analyzed the role of two domains in the S protein on fusion. The 180-kDa mature S protein is partially cleaved into two 90-kDa subunits during transport to the plasma membrane. We have identified several amino acids that are Important for cleavage of S, and we show that cleavage is not strictly required for fusion. However, the level of cleavage seems to influence the fusion kinetics. After introduction of an arginine at position P2 to mimick the MHV-JHM cleavage site, full cleavage of the spike protein was obtained. Further, we analyzed the effect of mutations in the trensmembrane (TM) domain of the S protein. Maturation and cell surface expression of the mutant proteins were not affected, and all proteins became acylated. The mutant in which the predicted transmembrane domain was shortened did not induce syncytia. From a group of mutants in which several conserved cysteines in the TM domain had been replaced by serines, one was unable to induce syncytia, another showed delayed syncytia formation, and the third mutant induced syncytia as did the wild-type protein. The potential role of the transmembrane domain in fusion is discussed. © 1995 Academic Press, Inc.",,,"Barr, P.J., Mammalian subtilisins: The long-sought dibasic processing endoproteases (1991) Cell, 66, pp. 1-3; Bonatti, S., Migliaccio, G., Simons, K., Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasma-tic reticulum (1989) J. Biol. Chem, 264, pp. 12590-12595; Boyd, D., Beckwith, J., The role of charged amino acids in the localization of secreted and membrane proteins (1990) Cell, 62, pp. 1031-1033; Cavanagh, D., Coronavirus IBV: Structural characterization of IBV glycoproteins (1983) J. Gen. Virol, 64, pp. 2577-2583; Daya, M., Wong, F., Cervin, M., Evans, G., Vennema, H., Spaan, W., Anderson, R., Mutation of host cell determinants which discriminate between lytic and persistent mouse hepatitis virus infection results in a fusion-resistant phenotype (1989) J. Gen. Virol, 70, pp. 3335-3346; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van Der Zeijst, B.A.M., Spaan, W., Lenstra, J.A., Evidence for a coiled-coil structure in the spike protein of coronaviruses (1987) J. Mol. Biol, 196, pp. 963-966; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol, 64, pp. 5367-5375; Doms, R.W., Lamb, R.A., Rose, J.K., Helenius, A., Folding and assembly of viral membrane proteins (1993) Virology, 193, pp. 545-562; Dubay, J.W., Roberts, S.J., Hahn, B.H., Hunter, E., Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity (1992) J. Virol, 66, pp. 6616-6625; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol, 56, pp. 912-920; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol, 65, pp. 1916-1928; Gilmore, W., Fleming, J.O., Stohlman, S.A., Weiner, L.P., Characterization of the structural proteins of the murine coronavirus strain A59 using monoclonal antibodies (1987) Proc. Natl. Acad. Sci. USA, 185, pp. 177-186; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol, 67, pp. 4504-4512; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Hammond, C., Braakman, I., Helenius, A., Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 913-917; Kawaoka, Y., Webster, R.G., Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalian cells (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 324-328; Kunkel, T.A., Roberts, J.D., Zakour, R., Rapid and efficient site-directed mutagenesis without phenotypic selection (1987) Methods En-Zymol, 154, pp. 367-382; Laemmli, U.K., Cleavage of structural proteins during assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lambrecht, B., Schmidt, M.F.G., Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids (1986) FEBS Lett, 202, pp. 127-132; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeijst, A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Marquardt, T., Helenius, A., Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum (1992) J. Cell. Biol, 117, pp. 505-513; Mizzen, L., Cheley, S., Rao, M., Wolf, R., Anderson, R., Fusion resistance and decreased infectability as major host cell determinants of coronavirus persistence (1983) Virology, 128, pp. 407-417; Molloy, S.S., Bresnahan, P.A., Leppla, S.H., Klimpel, K.R., Thomas, G., Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen (1992) J. Biol. Chem, 2679, pp. 16396-16402; Mulligan, M.J., Yamshchikov, G.V., Ritter, G.D., Gao, F., Jin, M.J., Nail, D., Spies, C.P., Compans, R.W., Cytoplasmic domain truncation enhances fusion activity by the exterior glycoprotein complex of human immunodeficiency virus type 2 in selected cell types (1992) J. Virol, 66, pp. 3971-3975; Naeve, C.W., Williams, D., Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion (1990) EMBO J, 9, pp. 3857-3866; Niemann, H., Klenk, H.-D., Coronavirus glycoprotein E1, a new type of viral glycoprotein (1981) J. Mol. Biol, 153, pp. 993-1010; Owens, R.J., Burke, C., Rose, J.K., Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity (1994) J. Virol, 68, pp. 570-574; Paterson, R.G., Shaughnessy, M.A., Lamb, R.A., Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide (1989) J. Virol, 63, pp. 1293-1301; Ragheb, J.A., Anderson, W.F., Uncoupled expression of moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry (1994) J. Virol, 68, pp. 3207-3219; Rasile, L., Ghosh, K., Raviprakash, K., Ghosh, H.P., Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring (1993) J. Virol, 67, pp. 4856-4866; Ricard, C.S., Sturman, L.S., Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite highperformance liquid chromatography (1985) J. Chromatogr, 326, pp. 191-197; Sefton, B.M., Buss, J.E., The covalent modification of eukaryotic proteins with lipid (1987) J. Cell Biol, 104, pp. 1449-1453; Schmidt, M.F.G., Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses (1982) Virology, 116, pp. 327-338; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol, 69, pp. 2939-2952; Stauber, R., Pfleiderera, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol, 74, pp. 183-191; Steinhauer, D.A., Wharton, S.A., Wiley, D.C., Skehel, J.J., Deacylation of the Hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties (1991) Virology, 184, pp. 445-448; Sturman, L.S., Holmes, K.V., The novel glycoproteins of coronaviruses (1985) Trends Biochem. Sci, 10, pp. 17-20; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol, 56, pp. 904-911; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol, 64, pp. 3042-3050; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol, 67, pp. 1195-1202; Van Berlo, M.F., Van Den Brink, W.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells: Brief report (1987) Arch. Virol, 95, pp. 123-128; Veit, M., Kretzschmar, E., Kuroda, K., Garten, W., Schmidt, M.F.G., Klenk, H.-D., Rott, R., Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin (1991) J. Virol, 65, pp. 2491-2500; Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J. Virol, 64, pp. 339-346; Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M.C., Spaan, W.J.M., Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system with encephalomyocarditis virus 5' untranslated region sequences (1991) Gene, 108, pp. 201-210; Vey, M., Orlich, M., Adler, S., Klenk, H.-D., Rott, R., Garten, W., Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R (1992) Virology, 188, pp. 408-413; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol, 99, pp. 164-200; Weismiller, D.G., Sturman, L.S., Buchmeier, M.J., Fleming, J.O., Holmes, K.V., Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify 2 subunits and detect a conformational change in the subunit released under mild alkaline conditions (1990) J. Virol, 64, pp. 3051-3055; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol, 52, pp. 675-679","Spaan, W.J.M.; Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH, Leiden, Netherlands; email: azruviro@rulcri.LeidenUniv.nl",,,00426822,,,,"English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0029592197
"Cristallo A., Gambaro F., Battaglia M., Cereda P.M.","6603250884;6506375719;7201908369;7003845258;","Main molecular aspects of human coronaviruses and homologies with animal coronavirus strains",1996,"Medecine Biologie Environnement","24","1",,"1","9",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029859567&partnerID=40&md5=9e2b76a583be9a4ea729542d3fa5a087","Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy","Cristallo, A., Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy; Gambaro, F., Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy; Battaglia, M., Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy; Cereda, P.M., Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy","Starting in 1965 after the discovery of several new human respiratory pathogens, a group of viruses, which had been known since 1937, although not by the name of coronavirus, began to emerge. Avian infectious bronchitis virus (IBV), mouse hepatitis virus (MHV), and some newly described human respiratory viruses, named OC43 and 229E were noted to have similar appearances. These viruses displayed a characteristic fringe of large, distinctive, petal-shaped peplomers or spikes which resembled a crown. They were called 'coronaviruses' after this feature. Shortly thereafter, several new viruses causing diseases in pigs, rats, turkeys, dogs, cats, and cattle were added to the coronavirus group. The range of animal species infected and the multiplicity of organ systems involved have made Coronaviridae one of the most important viral family in veterinary medicine. The two human coronaviruses (HCV) HCV-OC43 and HCV-229E belong to distinct antigenic groups. HCV-OC43 shares antigenic correlation with neonatal calf diarrhea coronavirus (NCDCV), hemagglutinating encephalomyelitis virus of swine (HEV) and MHV. HCV-229E is antigenically related to porcine transmissible gastroenteritis virus (TGEV) and canine coronavirus (CCV). Coronaviruses, as a group, contain a single-stranded, positive-sense RNA genome of 27 to 31 kb with an estimated molecular weight of 6 x 106 to 8 x 106 daltons. In infected cells, the viral RNA genome is first transcribed into a full-length negative-strand RNA, which, in turn, is transcribed into a positive-sense genomic RNA and six to eight subgenomic mRNAs by a mechanism of leader-primed transcription.","Genomic RNA; Human coronavirus 229E; Human coronavirus OC43; Neonatal calf diarrhea coronavirus NCDCV; Structural and nonstructural proteins; Subgenomic mRNAs","virus antigen; virus rna; animal disease; avian infectious bronchitis virus; coronavirus; murine hepatitis coronavirus; nonhuman; review; rna translation; virology; virus classification; virus genome",,"Cristallo, A.; Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy",,,03020800,,MBEND,,"English","MED. BIOL. ENVIRON.",Review,"Final",,Scopus,2-s2.0-0029859567
"Lai M.M.C.","7401808497;","Recombination in large RNA viruses: Coronaviruses",1996,"Seminars in Virology","7","6",,"381","388",,56,"10.1006/smvy.1996.0046","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030440990&doi=10.1006%2fsmvy.1996.0046&partnerID=40&md5=906f8e2189d7c5a03322003f83bcc75a","Howard Hughes Medical Institute, Dept. of Molec. Microbiol./Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Lai, M.M.C., Howard Hughes Medical Institute, Dept. of Molec. Microbiol./Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Coronaviruses contain a very large RNA genome, which undergoes recombination at a very high frequency of nearly 25% for the entire genome. Recombination has been demonstrated to occur between viral genomes and between defective-interfering (DI) RNAs and viral RNA. It provides an evolutionary tool for both viral RNAs and DI RNA and may account for the diversity in the genomic structure of coronaviruses. The capacity of coronaviruses to undergo recombination may be related to its mRNA transcription mechanism, which involves discontinuous RNA synthesis, suggesting the nonprocessive nature of the viral polymerase. Recombination is used as a tool for the mutagenesis of viral genomic RNA.","Defective-interfering RNA; Mouse hepatitis virus; RNA evolution; RNA recombination","messenger RNA; recombinant RNA; RNA polymerase; virus RNA; Coronavirus; nonhuman; review; RNA synthesis; RNA transcription; RNA virus; virus genome; virus recombination","Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J Virol, 56, pp. 449-456; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu Rev Microb, 44, pp. 303-333; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J Virol, 68, pp. 2615-2623; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis (1994) J Virol, 68, pp. 4738-4746; Keck, J.G., Stohlman, S.A., Soe, L.H., Makino, S., Lai, M.M.C., Multiple recombination sites at the 5′-end of murine coronavirus RNA (1987) Virology, 156, pp. 331-341; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J Virol, 62, pp. 1810-1813; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M.C., RNA recombination of murine coronaviruses: Recombination between fusion-positive MHV-A59 and fusion negative MHV-2 (1988) J Virol, 62, pp. 1989-1998; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J Virol, 57, pp. 729-737; Makino, S., Fleming, J.O., Keck, J.G., Stohlman, S.A., Lai, M.M.C., RNA recombination of coronaviruses: Localization of neutralizing epitopes and neuropathogenic determinants on the carboxyl terminus of peplomers (1987) Proc Natl Acad Sci USA, 84, pp. 6567-6571; Weiss, B.G., Schlesinger, S., Recombination between Sindbis virus RNA (1991) J Virol, 65, pp. 4017-4025; Bujarski, J.J., Dzianott, A.M., Generation and analysis of nonhomologous RNA-RNA recombinants in brome mosaic virus: Sequence complementarities at crossover sites (1991) J Virol, 65, pp. 4153-4259; Cascone, P.J., Carpenter, C.D., Li, X.H., Simon, A.E., Recombination between satellite RNAs of turnip crinkle virus (1990) EMBO J, 9, pp. 1709-1715; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Cooper, P.D., Genetics of picronaviruses (1977) Comprehensive Virology, pp. 133-208. , Fraenkel-Conrat H, Wagner RR, eds. Plenum Press, New York; Fu, K., Baric, R.S., Evidence for variable rates of recombination in the MHV genome (1992) Virology, 189, pp. 88-102; Fu, K., Baric, R.S., Map locations of mouse hepatitis virus temperature-sensitive mutants: Confirmation of variable rates of recombination (1994) J Virol, 68, pp. 7458-7466; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Cavanagh, D., Davis, P.J., Sequence analysis of strains of avian infectious bronchitis coronavirus isolated during the 1960s in the UK (1992) Arch Virol, 130, pp. 471-472; Wang, L., Junker, D., Collison, E.W., Evidence of natural recombination within the S1 gene of the infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wang, L., Junker, D., Hock, L., Ebiary, E., Collisson, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Res, 34, pp. 327-338; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch Virol, 140, pp. 259-271; Kotier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J Virol, 54, pp. 329-336; Furuya, T., Macnaughton, T.B., La Monica, N., Lai, M.M.C., Natural evolution of coronavirus defective-interfering RNA involves RNA recombination (1993) Virology, 194, pp. 408-413; Van Der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J Virol, 69, pp. 3744-3751; Liao, C.L., Lai, M.M.C., A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA (1995) Virology, 209, pp. 428-436; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J Virol, 66, pp. 5898-5905; Kim, Y.-N., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J Virol, 63, pp. 5285-5292; Chang, R.X., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J Virol, 70, pp. 2720-2729; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J Virol, 66, pp. 1841-1848; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J Virol, 66, pp. 6117-6124; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucl Acids Res, 20, pp. 3375-3381; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J Virol, 68, pp. 328-337; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J Virol, 69, pp. 3449-3457; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective-interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J Virol, 67, pp. 6110-6118; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J Virol, 69, pp. 5475-5484; Kusters, J.G., Jager, E.J., Niesters, H.G., Van Der Zeijst, B.A., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1991) Vaccine, 8, pp. 605-608; Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA-recombination between coronavirus and influenza C virus (1988) Virology, 166, pp. 415-422; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J.M., Comparison of the genome organization of toro-and coronaviruses: Evidence for two nonhomologous RNA recombination events during Berne virus evolution (1991) Virology, 180, pp. 448-452; Baric, R.S., Shieh, C.-K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Mills, D.R., Dobkin, C., Kramer, F.R., Template-determined, variable rate of RNA chain elongation (1978) Cell, 15, pp. 541-550; Banner, L.R., Keck, J.G., Lai, M.M.-C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Wang, D., Hawley, D.K., Identification of a 3′→5′ exonuclease activity associated with human RNA polymerase II (1993) Proc Natl Acad Sci USA, 90, pp. 843-847; Altmann, C.R., Solow-Cordero, D.E., Chamberlin, M.J., RNA cleavage and chain elongation by Escherichia coli DNA-dependent RNA polymerase in a binary enzyme-RNA complex (1994) Proc Natl Acad Sci USA, 91, pp. 3784-3788; Cascone, P.J., Haydar, T.F., Simon, A.E., Sequences and structures required for recombination between virus-associated RNAs (1993) Science, 260, pp. 801-805; White, K.A., Morris, T.J., RNA determinants of junction site selection in RNA virus recombinants and defective interfering RNAs (1995) RNA, 1, pp. 1029-1040","Lai, M.M.C.; Howard Hughes Medical Institute, Dept. Molecular Microbiol. Immunol., Univ. Southern CA School Medicine, Los Angeles, CA 90033-1054, United States",,"Academic Press Inc.",10445773,,SEVIE,,"English","SEMIN. VIROL.",Review,"Final",Open Access,Scopus,2-s2.0-0030440990
"Kamogawa O., Tomita Y., Kaneko M., Yamada S., Kubo M., Shimizu M.","7801578974;18036005400;17934749000;35494520900;7402198140;57199402584;","Isolation of porcine respiratory coronavirus from pigs affected with porcine reproductive and respiratory syndrome",1996,"Journal of Veterinary Medical Science","58","4",,"385","388",,8,"10.1292/jvms.58.385","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030113472&doi=10.1292%2fjvms.58.385&partnerID=40&md5=93042911aa104492b51aa94627ff0e80","Ibaraki Kenhoku Livestock Hyg. S., 966-1, Nakakawachi, Mito, Ibaraki 310, Japan; Tokyo Livestock Hyg. Service Center, 3-19-4, Fujimi, Tachikawa, Tokyo 190, Japan; Aichi Higaskimikawa Livestock H., Nishisaiwai, Toyohashi, Aichi 440, Japan; National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305, Japan","Kamogawa, O., Ibaraki Kenhoku Livestock Hyg. S., 966-1, Nakakawachi, Mito, Ibaraki 310, Japan; Tomita, Y., Tokyo Livestock Hyg. Service Center, 3-19-4, Fujimi, Tachikawa, Tokyo 190, Japan; Kaneko, M., Aichi Higaskimikawa Livestock H., Nishisaiwai, Toyohashi, Aichi 440, Japan; Yamada, S., National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305, Japan; Kubo, M., National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305, Japan; Shimizu, M., National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305, Japan","Four cytopathogenic viruses were isolated in CPK cells derived from porcine kidneys from tonsils and lungs of 3 of 15 pigs affected with porcine reproductive and respiratory syndrome virus. Physicochemically and morphologically, the isolates were similar to a coronavirus. The isolates were not distinguished from transmissible gastroenteritis virus (TGEV) by a neutralization test using polyclonal antibodies, but differentiated from TGEV by monoclonal antibodies capable of discriminating between TGEV and porcine respiratory coronavirus (PRCV), indicating that the isolates were PRCV. In a serological survey of 30 serum samples each collected from about 50 days old pigs in the 2 affected farms, 29 (97%) and 15 (50%) sera were positive for neutralizing antibody against the isolate with the titers ranging from 2 to 64, respectively.","Porcine reproductive and respiratory syndrome; Porcine respiratory coronavirus; PRCV","Coronavirus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Suidae; Transmissible gastroenteritis virus; monoclonal antibody; animal; animal disease; Arterivirus; article; cell culture; classification; electron microscopy; fluorescent antibody technique; isolation and purification; kidney; lung; pathology; respiratory tract disease; swine; swine disease; syndrome; tonsil; Transmissible gastroenteritis virus; ultrastructure; virology; virus infection; Animals; Antibodies, Monoclonal; Arterivirus; Arterivirus Infections; Cells, Cultured; Fluorescent Antibody Technique; Kidney; Lung; Microscopy, Electron; Respiratory Tract Diseases; Swine; Swine Diseases; Syndrome; Tonsil; Transmissible gastroenteritis virus","Britton, P., Mawditt, K.L., Page, K.W., (1991) Virus Res., 21, pp. 181-198; Brown, I., Cartwright, S., (1986) Vet. Rec., 119, pp. 282-283; Callebaut, P., Correa, I., Pensaert, M., Jiménez, G., Enjuanes, L., (1988) J. Gen. Virol., 69, pp. 1725-1730; Cox, E., Hooyberghs, J., Pensaert, M.B., (1990) Res. Vet. Sci., 48, pp. 165-169; Cox, E., Pensaen, M.B., Callebaut, P., Van Deun, K., (1990) Vet. Microbiol., 23, pp. 237-243; Fukusho, A., Ogawa, N., Yamamoto, H., Sawada, M., Sazawa, H., (1976) Infect. Immun., 14, pp. 332-336; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrew, J.J., (1993) J. Vet. Diagn. Invest., 5, pp. 184-188; Harada, K., Furuuchi, S., Kumagai, T., Sasahara, J., (1969) Natl. Ilnst. Anim. Health Q. (Jpn.), 9, pp. 185-192; Jabrane, A., Girard, C., Elazhary, Y., (1994) Can. Vet. J., 35, pp. 86-92; Komaniwa, H., Fukusyo, A., Shimizu, Y., (1981) Natl. Inst. Anim. Health Q. (Jpn.), 21, pp. 153-158; Lanza, I., Brown, I.H., Parton, D.J., (1992) Res. Vet. Sci., 53, pp. 309-314; Laude, H., Van Reeth, K., Pensaert, M.B., (1993) Vet. Res., 24, pp. 125-150; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, M., Callebaut, P., Vergote, J., (1986) Vet. Q., 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., (1990) J. Gen. Virol., 71, pp. 2599-2607; Saif, L.J., Bohl, E.H., (1986) Diseases of Swine, 6th Ed., pp. 255-274. , (Leman, A. D., Straw, B., Glock, R. D., Mengeling, W. L., Penny, R. H. C., and Scholl, E. eds.), Iowa State Univ. Press, Ames; Shimizu, M., Yamada, S., Murakami, Y., Morozumi, T., Kobayashi, H., Mitani, K., Ito, N., Watanabe, K., (1994) J. Vet. Med. Sci., 56, pp. 389-391; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., (1992) Am. J. Vet. Res., 53, pp. 1253-1258; Van Nieuwstadt, A.P., Boonstra, J., (1992) Am. J. Vet. Res., 53, pp. 184-190; Van Nieuwstadt, A.P., Pol, J.M.A., (1989) Vet. Rec., 124, pp. 43-44; Vaughn, E.M., Halbur, P.G., Paul, P.S., (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Cheung, A.K., (1991) J. Virol., 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., (1990) J. Vet. Diagn. Invest., 2, pp. 312-317","Shimizu, M.; National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305, Japan",,"Maruzen Co. Ltd.",09167250,,,"8741277","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0030113472
"Sirinarumitr T., Paul P.S., Kluge J.P., Halbur P.G.","6602842923;7202714004;7005760957;7005935318;","In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in formalin-fixed paraffin-embedded tissues",1996,"Journal of Virological Methods","56","2",,"149","160",,27,"10.1016/0166-0934(95)01901-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029867264&doi=10.1016%2f0166-0934%2895%2901901-4&partnerID=40&md5=3cd652cab527fc2c181cbd75a0b10343","Department of Veterinary Pathology, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Vet. Medical Research Institute, Dept. Microbiol. Immunol. Prev. Med., Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Veterinary Diagnostic Laboratory, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","Sirinarumitr, T., Department of Veterinary Pathology, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Paul, P.S., Vet. Medical Research Institute, Dept. Microbiol. Immunol. Prev. Med., Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Kluge, J.P., Department of Veterinary Pathology, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Halbur, P.G., Veterinary Diagnostic Laboratory, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","The in situ hybridization (ISH) technique was developed to detect the swine coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in cell culture and tissue sections from TGEV-or PRCV-infected pigs. The 35S-labeled RNA probes were generated from two plasmids pPSP.FP1 and pPSP.FP2 containing part of the S gene of TGEV. The procedure was first standardized in cell cultures. The radiolabeled pPSP.FP2 probe detected both TGEV and PRCV in virus-inoculated cell cultures, whereas pPSP.FP1 probe detected TGEV but not PRCV. The probe was then used to detect TGEV or PRCV in tissues of pigs experimentally infected with TGEV or PRCV or naturally infected with TGEV. Again, the probes detected TGEV in intestines of experimentally and naturally infected pigs and PRCV in the lungs of experimentally infected pigs. TGEV RNA was detected mainly within the enterocytes at the tips of villi and, less often, within some crypt epithelial cells. PRCV was shown to replicate mainly in the bronchiolar epithelial cells and in lesser amount in type II pneumocytes, type I pneumocytes, alveolar macrophages and bronchial epithelial cells, respectively. ISH has potential applications as a diagnostic test for the detection and differentiation of TGEV and PRCV in tissues and in studies to gain a better understanding of the mechanism of pathogenesis of enteric and respiratory coronavirus infections.","Coronavirus; In situ hybridization; Porcine respiratory coronavirus (PRCV); Single stranded RNA probe; Transmissible gastroenteritis virus (TGEV)","animal cell; article; controlled study; coronavirus; gastrointestinal infection; in situ hybridization; nonhuman; priority journal; respiratory tract infection; rna probe; swine; virus detection; virus infection; Animals; Cells, Cultured; Coronavirus; Coronavirus Infections; Formaldehyde; Gastroenteritis, Transmissible, of Swine; In Situ Hybridization; Male; Paraffin Embedding; Respiratory System; RNA, Viral; Swine; Testis; Tissue Fixation; Transmissible gastroenteritis virus","Angerer, L.M., Angerer, R.C., In situ hybridization to cellular RNA with radiolabeled RNA probe (1992) In Situ Hybridization: A Practical Approach, pp. 15-32. , D.G. Wilkinson (Ed), Oxford University Press, New York; Bohl, E.H., Pensaert, M.B., Transmissible gastroenteritis virus (classical enteric variant) and transmissible gastroenteritis virus (respiratory variant) (1989) Virus Infections of Porcines, pp. 139-265. , M.B. Pensaert (Ed), Elsevier Science Publishers B.N., Amsterdam; Brahic, M., Ozden, S., Simultaneous detection of cellular RNA and protein (1992) In Situ Hybridization: A Practical Approach, pp. 85-104. , D.G. Wilkinson (Ed), Oxford University Press, New York; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res, 21, pp. 181-198; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res., 18, pp. 71-80; Cox, E., Hooybergh, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Chu, R.M., Li, N., Glock, R.D., Ross, R.F., Applications of peroxidase-antiperoxidase staining technique for detection of transmissible gastroenteritis virus in pigs (1982) Am. J. Vet. Res., 43, pp. 77-81; Delmas, B., Gelfi, J., L'Haridon, R., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1990) Nature, 357, pp. 417-420; Frederick, G.I., Bohl, E.H., Cross, J.E., Pathogenicity of an attenuated strain of transmissible gastroenteritis virus for newborn pigs (1976) Am. J. Vet. Res., 42, pp. 1163-1169; Gibson, S.J., Polak, J.M., Principles and applications of complementary RNA probes (1990) In Situ Hybridization, Principles and Practice, pp. 81-94. , J.M. Polak and J.O. McGee (Eds), Oxford University Press, New York; Halbur, P.O., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J. Vet. Diagn. Invest., 5, pp. 184-188; Hill, H.T., Biwer, J.D., Wood, R.D., Wesley, R.D., Porcine respiratory coronavirus isolated from two US swine herds (1989) Proc. Am. Assoc. Swine Pract., pp. 333-335; Kohler, C.R., Nelsen, J.A., Technique for double-labelling virus infected cells (1990) Animal Virus Pathogenesis, A Practical Approach, pp. 67-86. , M.B. Oldstone (Ed), Oxford University Press, New York; Larochelle, R., Mogar, R., The application of immunogold silver staining (IGSS) for the detection of the transmissible gastroenteritis virus in fixed tissue (1993) J. Vet. Diagn. Invest., 5, pp. 16-20; Larson, D.J., Morehouse, L.G., Solorzano, R.F., Kinden, D.A., Transmissible gastroenteritis in neonatal dogs: Experimental intestinal infection with transmissible gastroenteritis virus (1979) Am. J. Vet. Res., 40, pp. 477-487; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Morin, M., Morehouse, L.G., Solorzano, R.F., Olsen, L.D., Transmissible gastroenteritis in feeder swine: Clinical, immunofluorescence and histopathological observations (1973) Can. J. Comp. Med., 37, pp. 239-248; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with pneumotropic porcine respiratory coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Paul, P.S., Halbur, P.G., Vaughn, E.M., Significance of porcine respiratory coronavirus infection (1994) Compend. Cont. Educ. Pract. Vet., 16, pp. 1223-1234; Paul, P.S., Vaughn, E.M., Halbur, P.G., Characterization and pathogenicity of a new porcine respiratory coronavirus strain AR310 (1992) Proc. Int. Pig. Vet. Soc. Congr., 12, p. 92; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Quart., 8, pp. 257-261; Rassachaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Rassachaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., pp. 362-386. , A.D. Leman, B.E. Strauss, W.L. Mengeling, S. D'Allaire, D.J. Taylor (Eds), Iowa State University Press, Ames, IA; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virol., 190, pp. 92-105; Shepherd, R.W., Butler, D.G., Cutz, E., Gall, D.G., The mucosal lesion in viral enteritis: Extent and dynamics of the epithelial response to virus invasion in transmissible gastroenteritis of piglets (1979) Gastroenterology, 76, pp. 770-777; Shockley, L.J., Kapke, P.A., Lapps, W., Brain, D.A., Potgieter, L.D., Woods, R.D., Diagnosis of porcine and bovine enteric coronavirus infections using cloned cDNA probes (1987) J. Clin. Micro., 25, pp. 1591-1596; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J. Virol., 69, pp. 3176-3184; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet. Microbiol., 36, pp. 333-347; Weingartl, H., Derbyshire, J.B., Evidence for a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs (1994) J. Virol., 68, pp. 7253-7259; Weingartl, H., Derbyshire, J.B., Binding of porcine transmissible gastroenteritis virus by enterocytes from newborn and weaned piglets (1993) Vet. Microbiol., 35, pp. 223-232; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a respiratory coronavirus antigenically similar to transmissible gastroenteritis in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1991) J. Virol., 64, pp. 4761-4768; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J. Vet. Diagn. Invest., 3, pp. 29-32; Wilcox, J.N., Fundamental principles of in situ hybridization (1993) J. Histochem. Cytochem., 41, pp. 1725-1733; Woods, R.D., Cheville, N.F., Gallagher, J.E., Lesions in the small intestine of newborn pigs inoculated with porcine, feline and canine coronavirus (1981) Am. J. Vet. Res., 42, pp. 1163-1169","Paul, P.S.; Vet. Medical Research Institute, Dept. Microbiol. Immunol. Prev. Med., Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; email: pspaul@iastate.edu",,"Elsevier",01660934,,JVMED,"8882645","English","J. Virol. Methods",Article,"Final",,Scopus,2-s2.0-0029867264
"Motokawa K., Hohdatsu T., Hashimoto H., Koyama H.","7004136451;57197786893;55723256500;7402164528;","Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses",1996,"Microbiology and Immunology","40","6",,"425","433",,73,"10.1111/j.1348-0421.1996.tb01089.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029945044&doi=10.1111%2fj.1348-0421.1996.tb01089.x&partnerID=40&md5=4e8114aae1a881f27906157fe2d3180e","Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Department of Virology, Center of Basic Research, Kitasato Institute, Minato-ku, Tokyo 108, Japan; Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, 23-35-1 Higashi, Towada, Aomori 034, Japan","Motokawa, K., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Hohdatsu, T., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan, Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, 23-35-1 Higashi, Towada, Aomori 034, Japan; Hashimoto, H., Department of Virology, Center of Basic Research, Kitasato Institute, Minato-ku, Tokyo 108, Japan; Koyama, H., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan","Complete nucleotide sequences were determined by cDNA cloning of peplomer (S), integral membrane (M) and nucleocapsid (N) genes of feline infectious peritonitis virus (FIPV) type I strain KU-2, UCD1 and Black, and feline enteric coronavirus (FECV) type II strain 79-1683. Only M and N genes were analyzed in strain KU-2 and strain 79-1683, which still had unknown nucleotide sequences. Deduced amino acid sequences of S, M and N proteins were compared in a total of 7 strains of coronaviruses, which included FIPV type II strain 79-1146, canine coronavirus (CCV) strain Insavc-1 and transmissible gastroenteritis virus of swine (TGEV) strain Purdue. Comparison of deduced amino acid sequences of M and N proteins revealed that both M and N proteins had an identity of at least 90% between FIPV type I and type II. The phylogenetic tree of the M and N protein-deduced amino acid sequences showed that FIPV type I and type II form a group with FECV type II, and that these viruses were evolutionarily distant from CCV and TGEV. On the other hand, when the S protein-deduced amino acid sequences was compared, identity of only about 45% was found between FIPV type I and type II. The phylogenetic tree of the S protein-deduced amino acid sequences indicated that three strains of FIPV type I form a group, and that it is a very long distance from the FIPV type II, FECV type II, CCV and TGEV groups.","Amino acid sequence; Feline enteric coronavirus; Feline infectious peritonitis virus","calnexin; virus protein; amino acid sequence; article; Coronavirus; nucleotide sequence; phylogeny; protein analysis; virus nucleocapsid; virus transmission; Canine coronavirus; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; gastroenteritis virus of swine; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Black, J.W., Recovery and in vitro cultivation of a coronavirus from laboratory-induced cases of feline infectious peritonitis (FIP) (1982) Vet. Med. [Small Anim Clin], 75, pp. 811-814; Dayhoff, M.O., Schwaryz, R.M., Orcutt, B.C., A model of evolutionary change in proteins (1987) Atlas of Protein Sequence and Structure, 5 (3 SUPPL.), pp. 345-352. , Dayhoff, M.O. (ed) National Biomedical Research Foundation, Washington, D.C; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A., Spaan, W.J., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J. Gen. Virol., 68, pp. 2639-2646; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J., Sequence analysis of the 3′-end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs): Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol., 28, pp. 13-24; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect. Immun., 37, pp. 1148-1155; Jacobs, L., De Groot, R.J., Van Der Zeijst, B.A., Horzinek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res., 8, pp. 363-371; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Kapke, P.A., Tung, F.Y., Brian, D.A., Woods, R.D., Wesley, R., Nucleotide sequence of the porcine transmissible gastroenteritis coronavirus matrix protein gene (1987) Adv. Exp. Med. Biol., 218, pp. 117-122; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; McKeirnan, A.J., Evermann, J.F., Hargis, A., Miller, L.M., Ott, R.L., Isolation of feline coronavirus from two cats with diverse disease manifestations (1981) Feline Pract., 11, pp. 16-20; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of the feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-37; Pedersen, N.C., Morphologic and physical characteristics of feline infectious peritonitis virus and its growth in autochthonous peritoneal cell cultures (1976) Am. J. Vet. Res., 37, pp. 567-572; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens, using feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 363-367; Pedersen, N.C., Black, J.W., Attempted immunization of cats against feline infectious peritonitis, using avirulent live virus or sublethal amounts of virulent virus (1983) Am. J. Vet. Res., 44, pp. 229-234; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Rasschaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Reed, A.P., Klepfer, S., Miller, T., Jones, E., Cloning and sequence analysis of the spike gene from several feline coronaviruses (1993) Adv. Exp. Med. Biol., 342, pp. 17-21; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M., Gebauer, F., Escribano, J.M., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sokal, R.R., Michener, C.D., A statistical method for evaluating systematic relationships (1958) Univ. Kansas Sci. Bull., 28, pp. 1409-1438; Takashi, K., Gotoh, P., Sequence relationship among various 4.5 S RNA species (1984) J. Biochem., 92, pp. 1173-1177; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenitity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Hohdatsu, T.; Veterinary Infectious Diseases Dept., Vet. Medicine/Animal Sciences School, Kitasato University, 23-35-1 Higashi, Towada, Aomori 034, Japan",,"Blackwell Publishing Asia",03855600,,MIIMD,"8839428","English","MICROBIOL. IMMUNOL.",Article,"Final",Open Access,Scopus,2-s2.0-0029945044
"Künkel F., Herrler G.","6602129906;7006339246;","Structural and functional analysis of the S proteins of two human coronavirus OC43 strains adapted to growth in different cells",1996,"Archives of Virology","141","6",,"1123","1131",,16,"10.1007/BF01718615","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029784875&doi=10.1007%2fBF01718615&partnerID=40&md5=c4e9ea553f5aec57c357e90db3e55162","Institut für Virologie, Philipps-Universität Marburg, Marburg, Germany; Maco Pharma International GmbH, Langen, Germany; Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Strasse 17, D-35037 Marburg, Germany","Künkel, F., Institut für Virologie, Philipps-Universität Marburg, Marburg, Germany, Maco Pharma International GmbH, Langen, Germany; Herrler, G., Institut für Virologie, Philipps-Universität Marburg, Marburg, Germany, Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Strasse 17, D-35037 Marburg, Germany","The receptor-binding activity of strain CU (grown in MDCK I cells) and of strain VA (adapted to Vero cells) of human coronavirus OC43 was analyzed and compared with the binding activity of bovine coronavirus (BCV) and of the OC43 strain provided by the American Type Culture Collection (AT). Results obtained with resialylated erythrocytes indicated that the ability of the viruses to recognize 9-O-acetylated sialic acid in an α2,6- linkage decreased in the following order: AT > CU > BCV > VA. Only minor differences were observed with respect to the α2,3-linkage. The amino acid sequence of the S protein of strain CU and VA was derived from the nucleotide sequence of the cloned gene. Strain VA differed from strain CU in 34 positions, 18 in the S1 and 16 in the S2 subunit.",,"Animalia; Bos taurus; Bovinae; Bovine coronavirus; Canis familiaris; Cercopithecus; Coronavirus; DNA viruses; human coronavirus","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Czerny, C.-P., (1986), doctoral thesis. Ludwigs-Maximilian-Universität, München; Hogue, B.G., Brian, D.A., Structural proteins of human coronavirus OC43 (1986) Virus Res, 5, pp. 131-144; Künkel, F., Herrler, G., Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202; McIntosh, K., Becker, W.B., Chanock, R.M., Growth in suckling-mouse brain of ""IBV-like"" viruses from patients with upper respiratory tract disease (1967) Proc Natl Acad Sci USA, 58, pp. 2268-2273; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus OC43 (1993) J Gen Virol, 74, pp. 1981-1987; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc Natl Acad Sci USA, 74, pp. 5463-5467; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Schultze, B., Gross, H.J., Brossmer, R., Klenk, H.-D., Herrler, G., Hemagglutinating encephalomyelitis virus attaches to N-acetyl-9-O-acetylneuraminic acid containing receptors on erythrocytes: Comparison with bovine coronavirus and influenza C virus (1990) Virus Res, 16, pp. 185-194; Schultze, B., Herrler, G., Recognition of cellular receptors by bovine coronavirus (1994) Positive-strand RNA Viruses, pp. 451-459. , Brinton MA, Calisher CH, Rueckert R (eds) Springer Wien New York, (Arch Virol [Suppl] 9); Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) J Gen Virol, 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529; Yoo, D., Parker, M.D., Song, J., Cox, G.J., Deregt, D., Babiuk, L.A., Structural analysis of the conformational domains involved in neutralization of bovine coronavirus using deletion mutants of the spike glycoprotein S1 subunit expressed by recombinant baculoviruses (1991) Virology, 183, pp. 91-98","Kunkel, F.; Maco Pharma International GmbH, Langen, Germany",,"Springer-Verlag Wien",03048608,,ARVID,"8712929","English","ARCH. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029784875
"Vieler E., Schlapp T., Herbst W.","6603650281;6701808474;16161781000;","The region between the M and S genes of porcine haemagglutinating encephalomyelitis virus is highly similar to human coronavirus OC43",1996,"Journal of General Virology","77","7",,"1443","1447",,6,"10.1099/0022-1317-77-7-1443","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029886824&doi=10.1099%2f0022-1317-77-7-1443&partnerID=40&md5=984e0a03dee78e6bbe6c1ad26211261c","Inst. F. Hyg. I., Justus-Liebig-Universität, Giessen, Germany; Retrovirus Laboratory, Division of Comparative Medicine, Johns Hopkins Univ. Sch. of Medicine, 720 Rutland Avenue/Traylor G-60, Baltimore, MD 21205, United States","Vieler, E., Inst. F. Hyg. I., Justus-Liebig-Universität, Giessen, Germany, Retrovirus Laboratory, Division of Comparative Medicine, Johns Hopkins Univ. Sch. of Medicine, 720 Rutland Avenue/Traylor G-60, Baltimore, MD 21205, United States; Schlapp, T., Inst. F. Hyg. I., Justus-Liebig-Universität, Giessen, Germany; Herbst, W., Inst. F. Hyg. I., Justus-Liebig-Universität, Giessen, Germany","The nucleotide sequences of the regions between the membrane and spike protein genes of three strains of porcine haemagglutinating encephalomyelitis virus (HEV) were determined. A total of 739 (HEV strain 67 N) and 751 (strains NT9 and VW572) nucleotides were sequenced. Two ORFs, potentially encoding proteins of 12.8 and 9.6 kDa, were identified. Pairwise comparisons with the corresponding ORFs in bovine coronavirus (BCV) and human coronavirus (HCV) OC43 revealed sequence similarities of greater than 88.5% at the nucleotide and 85.3% at the amino acid level for the 12.8 kDa ORF product. For the 9.6 kDa ORF product similarities were greater than 96.9% and 95.2%, respectively. An additional 12 nucleotide deletion upstream of the 12.8 kDa ORF start codon was found in HEV 67N compared to NT9 and VW572. These results reveal a genomic organization of HEV in the region analysed that is homologous to HCV OC43 but different from BCV.",,"amino acid sequence; article; Coronavirus; gene deletion; nonhuman; nucleotide sequence; open reading frame; priority journal; sequence homology; start codon; virus gene","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4·9, 4·8, 12·7 and 9·5 kDa encoded between the spike and the membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Boursnell, M.E.G., Brown, T.D.K., Sequencing of coronavirus IBV genomic RNA: A 195-base open reading frame encoded by mRNA B (1984) Gene, 29, pp. 87-92; Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Sequencing of coronavirus IBV genomic RNA: Three open reading frames in the 5′ 'unique' region of mRNA D (1985) Journal of General Virology, 66, pp. 2253-2258; Cox, G.J., Parker, M.D., Babiuk, L.A., The sequence of cDNA of bovine coronavirus 32K nonstructural gene (1989) Nucleic Acids Research, 17, p. 5847; Fenner, F.J., Gibbs, E.P.J., Murphy, F.A., Rott, R., Studdert, M.J., White, D.O., Coronaviridae (1993) Veterinary Virology, 2nd Edn, pp. 457-469. , San Diego: Academic Press; Hirano, N., Haga, S., Fujiwara, K., The route of transmission of hemagglutinating encephalomyelitis virus (HEV) 67N strain in 4-week-old rats (1993) Advances in Experimental and Medical Biology, 342, pp. 333-338; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fields Virology, 3rd Edn, pp. 1075-1093. , Edited by B. N. Fields, D. M. Knipe & P. M. Howley. Philadelphia: Lippincott-Raven; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Research, 12, pp. 1-9; Künkel, F., Herrler, G., Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202; Labonté, P., Mounir, S., Talbot, P.J., Sequence and expression of the ns2 protein gene of human coronavirus OC43 (1995) Journal of General Virology, 76, pp. 431-435; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein gene (1987) Virology, 157, pp. 47-57; Leibowitz, J.L., Perlman, S., Weinstock, G., Devries, J.R., Budzilowicz, C., Weissemann, J.M., Weiss, S.R., Detection of a murine coronavirus nonstructural protein encoded in a downstream open reading frame (1988) Virology, 164, pp. 156-164; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) Journal of General Virology, 73, pp. 2731-2736; Mounir, S., Talbot, P.J., Human coronavirus OC43 RNA 4 lacks two open reading frames located downstream of the S gene of bovine coronavirus (1993) Virology, 192, pp. 355-360; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus OC43 (1993) Journal of General Virology, 74, pp. 1981-1987; Skinner, M.A., Siddell, S.G., Coding sequence of coronavirus MHV-JHM mRNA 4 (1985) Journal of General Virology, 66, pp. 593-596; Skinner, M.A., Ebner, D., Siddell, S.G., Coronavirus MHV-JHM mRNA 5 has a sequence arrangement which potentially allows translation of a second, downstream open reading frame (1985) Journal of General Virology, 66, pp. 581-592; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2952; Vieler, E., Schlapp, T., Anders, C., Herbst, W., Genomic relationship of porcine hemagglutinating encephalomyelitis virus to bovine coronavirus and human coronavirus OC43 as studied by the use of bovine coronavirus S gene-specific probes (1995) Archives of Virology, 140, pp. 1215-1223; Yagami, K., Izumi, Y., Kajiwara, N., Sugiyama, F., Sugiyama, Y., Neurotropism of mouse-adapted hemagglutinating encephalomyelitis virus (1993) Journal of Comparative Pathology, 109, pp. 21-27; Zhang, X., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase gene of human coronavirus strain OC43: Phylogenetic relationships to bovine and murine coronavirus and influenza C virus (1992) Virology, 186, pp. 318-323","Vieler, E.; Retrovirus Laboratory, Division of Comparative Medicine, Johns Hopkins Univ. School Medicine, 720 Rutland Avenue, Baltimore, MD 21205, United States",,"Microbiology Society",00221317,,JGVIA,"8757985","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029886824
"Kalicharran K., Dales S.","6602516345;7005597434;","The murine coronavirus as a model of trafficking and assembly of viral proteins in neural tissue",1996,"Trends in Microbiology","4","7",,"264","269",,10,"10.1016/0966-842X(96)10045-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030200104&doi=10.1016%2f0966-842X%2896%2910045-7&partnerID=40&md5=e0775ac5276c964a853efb90e502203e","Dept. of Microbiology and Immunology, Health Sciences Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada","Kalicharran, K., Dept. of Microbiology and Immunology, Health Sciences Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada; Dales, S., Dept. of Microbiology and Immunology, Health Sciences Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada","The replication of JHM, a murine coronavirus, provides a useful model of the assembly and dissemination of viral components in neuronal cells. Involvement of microtubules in virus trafficking is an important feature which may explain dissemination of the infection from primary cell targets at olfactory, hippocampal and cerebellar sites within the central nervous system, resulting in severe neuropathies.",,"virus protein; animal cell; biological model; Coronavirus; mouse; nervous tissue; nonhuman; priority journal; protein assembly; protein determination; review; tissue distribution; virus replication; virus strain","Murray, R.S., (1992) Virology, 188, pp. 274-284; Dales, S.D., Anderson, R., (1995) The Coronaviridae, pp. 257-291. , (Siddell, S.G., ed.), Plenum Press; Sorensen, O., (1980) Arch. Neurol., 37, pp. 478-484; Sorensen, O., (1982) Infect. Immun., 37, pp. 1248-1260; Sorensen, O., (1987) Microb. Pathog., 2, pp. 79-90; Zimmer, M.J., Dales, S., (1989) Microb. Pathog., 6, pp. 7-16; Talbot, P.J., Buchmeier, M.J., (1985) Virus Res., 2, pp. 317-328; Dalziel, R.G., (1986) J. Virol., 59, pp. 463-471; Levine, S.M., Goldman, J.E., (1988) J. Comp. Neurol., 277, pp. 441-455; Barnett, E.M., Cassell, M.D., Perlman, S., (1993) Neuroscience, 57, pp. 1007-1025; Lavi, E., (1988) Lab. Invest., 58, pp. 31-36; Perlman, S., (1990) Virology, 175, pp. 418-426; Perlman, S., Jacobsen, G., Moore, S., (1988) Virology, 166, pp. 328-338; Fishman, P.S., (1985) Science, 229, pp. 877-879; Parham, D., (1986) Arch. Neurol., 43, pp. 702-708; Sorensen, O., Dales, S., (1985) J. Virol., 56, pp. 434-438; McCarthy, K.D., Vellis, D.J., (1980) J. Cell Biol., 85, pp. 890-902; Beushausen, S., Dales, S., (1985) Virology, 141, pp. 89-101; Wilson, G.A.R., Beushausen, S., Dales, S., (1986) Virology, 151, pp. 253-264; Bogler, O., Noble, M., (1994) Dev. Biol., 162, pp. 525-538; Beushausen, S., (1987) J. Virol., 61, pp. 3795-3803; Dotti, C.G., Simons, K., (1990) Cell, 62, pp. 63-72; Fuller, S.D., (1984) Cell, 38, pp. 65-77; Rodriguez-Boulan, E., Pendergast, M., (1980) Cell, 20, pp. 45-54; Tooze, J., Tooze, S.A., Fuller, S.D., (1987) J. Cell Biol., 105, pp. 1215-1226; Tooze, J., Tooze, S.A., Warren, G., (1984) Eur. J. Cell Biol., 33, pp. 281-293; Tooze, S.A., Tooze, J., Warren, G., (1988) J. Cell Biol., 106, pp. 1475-1487; Krijnse-Locker, J., (1994) J. Cell Biol., 124, pp. 55-70; Dubois-Dalcq, M., (1982) Virology, 119, pp. 317-331; Vallee, R.B., Bloom, G.S., (1991) Annu. Rev. Neurosci., 14, pp. 59-92; Rodriguez-Boulan, E., Powell, S.K., (1992) Annu. Rev. Cell Biol., 8, pp. 395-427; Penfold, M.E.T., Armati, P., Cunningham, A.L., (1994) Proc. Natl Acad. Sci. USA, 91, pp. 6529-6533; Kucera, P., (1985) J. Virol., 55, pp. 158-162; LaFay, F., (1991) Virology, 83, pp. 320-330; Flamand, A., (1991) J. Virol., 65, pp. 123-131; Morrison, L.A., Sidman, R.L., Fields, B.N., (1991) Proc. Natl Acad. Sci. USA, 88, pp. 3852-3856; Tyler, K.L., McPhee, D.A., Fields, B.N., (1986) Science, 233, pp. 770-774; Zemanick, M.C., Strick, P.L., Dix, R.D., (1991) Proc. Natl Acad. Sci. USA, 88, pp. 8048-8051; Card, J.P., (1993) J. Neuroscience, 13, pp. 2515-2539; Card, J.P., Enquist, L.W., (1995) Crit. Rev. Neurobiol., 9, pp. 137-162; Coulton, P., (1989) J. Virol., 63, pp. 3550-3554; Tsiang, H., (1989) J. Gen. Virol., 70, pp. 2075-2085; Ceccaldi, P.E., Gillet, J.P., Tsiang, H., (1989) J. Neuropath. Exp. Neurol., 48, pp. 620-630; Kristensson, K., (1986) J. Gen. Virol., 67, pp. 2023-2028; Pasick, J.M.M., Kalicharran, K., Dales, S., (1994) J. Virol., 68, pp. 2915-2928; Ren, R., Racaniello, V.R., (1992) J. Infect. Dis., 166, pp. 747-752; Van Pottelsberghe, C., (1979) Lab. Invest., 40, pp. 99-108; Carbone, K.M., (1987) J. Virol., 61, pp. 3431-3440; Gosztonyi, G., (1993) Lab. Invest., 68, pp. 285-295; Wang, F.-I., (1992) Lab. Invest., 66, pp. 103-106; Knobler, R.L., (1981) J. Neuroimmunol., 1, pp. 81-92; Pasick, J.M.M., Dales, S., (1991) J. Virol., 65, pp. 5013-5028; Dales, S., (1963) Proc. Natl Acad. Sci. USA, 50, pp. 268-275; Dales, S., Chardonnet, Y., (1973) Adv. Biosci., 11, pp. 29-40; Lee, G., Cowan, N., Kirschner, M., (1988) Science, 239, pp. 285-288; Lee, G., Neve, R.L., Kosik, K.S., (1989) Neuron, 2, pp. 1615-1624; Chapin, S.J., Bulinski, J.C., (1992) Cell Motil. Cytoskeleton, 23, pp. 236-243; Wecelewicz, K., Kristensson, K., Orvell, C., (1990) Appl. Neurobiol., 16, pp. 357-364","Kalicharran, K.; Dept of Microbiology and Immunology, Health Sciences Centre, University of Western Ontario, London, Ont. N6A 5C1, Canada",,"Elsevier Ltd",0966842X,,TRMIE,"8829334","English","TRENDS MICROBIOL.",Review,"Final",,Scopus,2-s2.0-0030200104
"Yu M.W.N., Lemieux S., Talbot P.J.","16940438900;7004556064;7102670281;","Genetic control of anti-idiotypic vaccination against coronavirus infection",1996,"European Journal of Immunology","26","12",,"3230","3233",,6,"10.1002/eji.1830261258","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029800148&doi=10.1002%2feji.1830261258&partnerID=40&md5=3e424a1bd8e66d3d99602e0094ad3a44","Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Lavai, Que., Canada; Immunology Research Center, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Centre de Recherche en Virologie, Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 boulevard des Prairies, Lavai, Que. H7N 4Z3, Canada","Yu, M.W.N., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Lavai, Que., Canada; Lemieux, S., Immunology Research Center, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Lavai, Que., Canada, Centre de Recherche en Virologie, Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 boulevard des Prairies, Lavai, Que. H7N 4Z3, Canada","The idiotypic network can be experimentally altered to induce protective immune responses against microbial pathogens. Both internal image and noninternal image anti-idiotypic (anti-Id) antibodies have been shown to trigger antigen (Ag)-specific immune responses. Therefore, mechanisms of anti-Id vaccination appear to go beyond structural mimicry of Ag, but remain undefined. Using the neurotropic murine coronavirus animal model, we have previously shown that a polyclonal noninternal image anti-Id (Ab2) could vaccinate BALB/c mice. To characterize its mode of action, we have examined the immune modulating capability of this Ab2 in vivo in strains of mice with different H-2 haplotypes. Even though only internal image anti-Id are expected to induce non-genetically restricted immunity, this noninternal image Ab2 induced protective immunity in four of eight genetically different strains of mice susceptible to coronavirus infection. These were BALB/c (H-2(d)), DBA/2 (H-2(d)), DBA/1 (H-2(q)), and SWR (H-2(q)) mice. Protection was generally correlated with the induction of specific antiviral Ab (Ab3) that showed biological properties, such as virus neutralization in vitro, similar to the initial Ab1. To evaluate the genetic implication of the H-2 haplotypes in protection, congenic mice were also tested. Vaccination profiles suggest that cooperation between background gene(s) of the BALB/c mouse with H-2(d) and H-2(q) loci is necessary for an optimal protective immune response, although the main genetic element(s) regulating the antiviral response to Ab2 inoculation appeared to be located outside the major histocompatibility complex. These results are consistent with the ability of Ab2 to induce protective antiviral antibodies in genetically different animals by biological mimicry.","Anti-idiotypic antibody; Infectious immunity virus; Rodent; Vaccination","idiotypic antibody; animal cell; animal experiment; animal model; antiviral activity; article; Coronavirus; immunogenetics; immunomodulation; major histocompatibility complex; mouse; neurotropism; nonhuman; priority journal; vaccination; virus infection; virus neutralization","Su, S., McNamara Ward, M., Apicella, M.A., Ward, R.E., (1992) J. Immunol., 148, p. 234; Billetta, R., Hollingdale, M.R., Zanetti, M., (1991) Proc. Natl. Acad. Sci. USA, 88, p. 4713; Fung, M.S.C., Sun, C.R.Y., Liou, R.S., Gordon, W., Chang, N.T., Chang, T.-W., Sun, N.-C., (1990) J. Immunol., 145, p. 2199; Fagerberg, J., Steinitz, M., Wigzell, H., Askelöf, P., Mellstedt, H., (1995) Proc. Natl. Acad. Sci. USA, 92, p. 4773; Kennedy, R.C., Eichberg, J.W., Dreesman, G.R., (1986) Virology, 148, p. 369; Pohl, C., Renner, C., Schwonzen, M., Sieber, M., Lorenz, P., Pfreundschuh, M., Diehl, V., (1992) Int. J. Cancer., 50, p. 958; Schick, M.R., Dreesman, G.R., Kennedy, R.C., (1987) J. Immunol., 138, p. 3419; Kang, C.-Y., Nara, P., Chamat, S., Caralli, V., Chen, A., Nguyen, M.-L., Yoshiyama, H., Köhler, H., (1992) Proc. Natl. Acad. Sci. USA, 89, p. 2546; Kraaijeveld, C.A., Oosterlaken, T.A.M., Snijders, A., Benaissa-Trouw, B.J., Ekstijn, G.L., Snippe, H., (1992) Antiviral Res., 19, p. 275; Zhou, E.-M., Lohman, K.L., Kennedy, R.C., (1990) Virology, 174, p. 9; Zhou, S.-R., Whitaker, J.N., (1993) J. Immunol., 150, p. 1629; Yang, Y.-F., Thanavala, Y., (1995) Clin. Immunol. Immunopathol., 75, p. 154; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., (1982) Virology, 119, p. 358; Körner, H., Schliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S., Wege, H., (1991) J. Immunol., 147, p. 2317; Flory, E., Pfleiderer, M., Stuher, A., Wege, H., (1993) Eur. J. Immunol., 23, p. 1757; Kubo, H., Yamada, Y.K., Taguchi, F., (1994) J. Virol., 68, p. 5403; Daniel, C., Anderson, R., Buchmeier, M.J., Fleming, J.O., Spaan, W.J.M., Wege, H., Talbot, P.J., (1993) J. Virol., 67, p. 1185; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., (1986) J. Virol., 59, p. 463; Taguchi, F., Kubo, H., Takahashi, H., Suzuki, H., (1995) Virology, 208, p. 67; Lamarre, A., Lecomte, J., Talbot, P.J., (1991) J. Immunol., 147, p. 4256; Daniel, C., Talbot, P.J., (1987) Arch. Virol., 96, p. 241; Armitage, P., Berry, G., (1987) Statistical Methods in Medical Research. 2nd Edn., , Blackwell Scientific Publications, Oxford; Yu, M., Talbot, P.J., (1995) Adv. Exp. Med. Biol., 380, p. 165; Kennedy, R.C., Adler-Strothz, K., Burns Sr., J.W., Henkel, R.D., Dreesman, G.R., (1984) J. Virol., 50, p. 951","Talbot, P.J.; Centre de recherche en virologie, Laboratoire de neuroimmunovirologie, Institut Armand Frappier, 531 boulevard des Prairies, Laval, Que. H7N 4Z3, Canada",,"Wiley-VCH Verlag",00142980,,EJIMA,"8977327","English","EUR. J. IMMUNOL.",Article,"Final",Open Access,Scopus,2-s2.0-0029800148
"El-Kanawati Z.R., Tsunemitsu H., Smith D.R., Saif L.J.","6505831008;7004628959;7410366749;7102226747;","Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves",1996,"American Journal of Veterinary Research","57","1",,"48","53",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029678924&partnerID=40&md5=77ecc65cfe9638262a24a2a00e96609c","Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States","El-Kanawati, Z.R., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Tsunemitsu, H., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Smith, D.R., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States","Objective - To investigate in vitro antigenic relations, in vivo cross-protection, and isotype antibody responses to a winter dysentery (WD) and calf diarrhea strain of bovine coronavirus (BCV). Design and Animals - Gnotobiotic and colostrum-deprived calves were inoculated oronasally with a WD (DBA) or a calf diarrhea (DB2) BCV, and were challenge exposed with the heterologous BCV. Procedure - Nasal swab and feces specimens and blood samples were collected. Fecal and nasal specimens were assayed for BCV shedding by antigen-capture ELISA or immune electron microscopy. Bovine coronavirus antigens were detected in nasal epithelial cells by immunofluorescence. Antibody titers to BCV in serum were assayed by virus neutralization (VN), and BCV antibody isotype titers in feces and sera were quantitated by ELISA. Results - All calves developed diarrhea and shed BCV nasally and in feces, then recovered and were protected from BCV-associated diarrhea after challenge exposure with the heterologous BCV. After challenge exposure with either strain, fecal shedding of DBA was detected in 1 of 4 calves and nasal shedding of DB2 was detected in 2 of 4 calves. Immunoglobulin M was the principal coproantibody to BCV early, followed predominantly by IgA Imunoglobulin G1 coproantibody titers to BCV were low, but increased after challenge exposure. Immunoglobulin G1 antibodies were predominant in serum After challenge exposure, all serum antibody isotype titers increased except IgG2. The VN antibody responses paralleled serum IgG1 antibody responses. Conclusions and Clinical Relevance - Immunoglobulin A coproantibodies at challenge exposure were associated with protection against diarrhea. Nasal shedding of BCV after challenge exposure confirmed field data documenting reinfection of the respiratory tract of cattle, suggesting that, in closed herds, respiratory tract infections constitute a source of BCV transmission to cows (WD) or young calves.",,"immunoglobulin class; virus antibody; animal; animal disease; antibody production; article; blood; cattle; cattle disease; classification; colostrum; Coronavirus; diarrhea; disease transmission; dysentery; enzyme linked immunosorbent assay; feces; female; germfree animal; hemagglutination test; immunology; isolation and purification; nose mucosa; serodiagnosis; virology; virus infection; Animals; Antibodies, Viral; Antibody Formation; Cattle; Cattle Diseases; Colostrum; Coronavirus; Coronavirus Infections; Diarrhea; Dysentery; Enzyme-Linked Immunosorbent Assay; Feces; Female; Germ-Free Life; Hemagglutination Tests; Immunoglobulin Isotypes; Nasal Mucosa; Neutralization Tests","Doughri, A.M., Storz, J., Light and ultrastructural pathologic changes in coronavirus infection of newborn calves (1977) Zentralbl Veterinarmed [B], 24, pp. 367-385; Mebus, C.A., Stair, E.L., Rhodes, M.B., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet Pathol, 10, pp. 45-64; Mebus, C.A., Stair, E.L., Rhodes, M.B., Neonatal calf diarrhea: Propagation, attenuation and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Vet, 68, pp. 423-441; Durham, P.J.K., Hasard, L.E., Armstrong, K.R., Coronavirus-associated diarrhea (winter dysentery) in adult cattle (1989) Can Vet J, 30, pp. 625-827; Espinasse, J., Viso, M., Laval, A., Winter dysentery. a coronavirus-like agent in the feces of beef and dairy cattle with diarrhea (1982) Vet Rec, 110, p. 385; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet Rec, 127, pp. 300-301; Takahashi, E., Inaba, Y., Sat, K., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Heckert, R.A., Saif, L.J., Hoblet, K.H., Longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet Microbiol, 22, pp. 187-201; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronavirus from the intestinal and the respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infection in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Zhang, X., Herbst, W., Kousoulas, K.G., Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 24, pp. 421-426; Cavanagh, D., Brain, D.A., Enjuanes, L., Recommendation of the coronavirus study group for the nomenclature of the structural proteins, mRNAs, and genes of coronaviruses (1990) Virology, 176, pp. 306-307; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Vlasak, R., Luytjes, W., Spaan, W., Human and bovine coronavirus recognize sialic acid-containing receptors similar to those of influenza C virus (1988) Proc Natl Acad Sci U S A, 85, pp. 4526-4529; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from calves with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Smith, K.L., Enteric viral infections of calves and passive immunity (1985) J Dairy Sci, 68, pp. 206-228; Saif, L.J., Development of nasal, fecal and serum isotype-specific antibodies in calves challenged with bovine coronavirus or rotavirus (1987) Vet Immunol Immunopathol, 17, pp. 425-439; Heckert, R.A., Saif, L.J., Mengel, J.P., Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces, and mucosal secretions from experimentally challenge-exposed colostrum-deprived calves (1991) Am J Vet Res, 52, pp. 692-699; El-Ghorr, P.J.K., Snodgrass, D.R., Scott, F.M.M., Serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variations among Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Rekik, M.R., Dea, S., Comparative sequence analysis of a polymorphic region of spike protein gene of bovine coronavirus isolates (1994) Arch Virol, 135, pp. 319-331; Van Kuiningen, H.J., Hiestand, L., Hill, D.L., Winter dysentery in dairy cattle recent findings (1985) Compend Contin Educ Pract Vet, 7, pp. S591-S599; Van Kruiningen, H.J., Khairallah, L.H., Sasseville, V.G., Calfhood coronavirus enterocolitis: A clue to the etiology of winter dysentery (1987) Vet Pathol, 24, pp. 564-567; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Crouch, C.F., Raybould, T.J.G., Comparison of different antigen preparation as substrates for use in passive hemagglutination and enzyme-linked immunosorbent assays for detection of antibody against bovine enteric coronavirus (1983) J Clin Microbiol, 18, pp. 146-149; Bohl, E.H., Saif, L.J., Theil, K.W., Porcine pararotavirus: Detection, differentiation from rotavirus and pathogenesis in gnotobiotic pigs (1982) J Clin Microbiol, 15, pp. 312-319; Saif, L.J., Bohl, E.H., Kohler, E.M., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (rotavirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Saif, L.J., Heckert, R.A., Miller, K.L., Cell culture propagation of bovine coronavirus (1988) J Tissue Cult Methods, 11, pp. 139-145; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swab of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Sato, K., Inaba, Y., Takaahashi, E., Hemagglutination by calf diarrhea coronavirus (1977) Vet Microbiol, 2, pp. 83-87; Storz, J., Herrler, G., Snodgrass, D.R., Monoclonal antibodies differentiate between the neutralizing and the receptor-destroying activities of BCV (1991) J Gen Virol, 72, pp. 2817-2820; Heckert, R.A., Saif, L.J., Myers, G., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am J Vet Res, 52, pp. 845-851; Heckert, R.A., Saif, L.J., Mengel, J., Mucosal and systemic antibody responses to bovine coronavirus structural proteins in experimentally challenged-exposed calves fed low or high amount of colostral antibodies (1991) Am J Vet Res, 52, pp. 700-708; Kimman, T.G., Westerbrink, F., Schreuder, B.E., Local and systemic antibody response to bovine respiratory syncytial virus infection and reinfection in calves with and without maternal antibodies (1987) J Clin Microbiol, 25, pp. 1097-1106; Akashi, H.Y., Inaba, Y., Miura, S., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet Microbiol, 5, pp. 265-276; Broes, A., Van Opdenbosch, E., Wellemans, G., Isolement d'un coronavirus chez des bovins atteints d'enterite hemoragiquechivernale (winter dysentery) en Belique (1984) Ann Med Vet, 128, pp. 299-303","Saif, L.J.; Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States",,,00029645,,AJVRA,"8720237","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029678924
"Wang Y., Burnier M., Detrick B., Hooks J.J.","56802808200;35751910100;7003911483;7006661655;","Genetic predisposition to coronavirus-induced retinal disease",1996,"Investigative Ophthalmology and Visual Science","37","1",,"250","254",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030043018&partnerID=40&md5=7987be1af1b25534650c4332e326bbac","Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States; Department of Ophthalmology, McGill University, Montreal, Que., Canada; Department of Pathology, George Washington University, Medical Center, Washington, DC, United States; National Eye Institute, National Institutes of Health, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States","Wang, Y., Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States; Burnier, M., Department of Ophthalmology, McGill University, Montreal, Que., Canada; Detrick, B., Department of Pathology, George Washington University, Medical Center, Washington, DC, United States; Hooks, J.J., Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States, National Eye Institute, National Institutes of Health, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States","Purpose. Retinal inflammatory and degenerative processes in humans and animals frequently are associated with genetic factors. The murine coronavirus, mouse hepatitis virus (MHV), JHM strain, induces a biphasic retinal disease in adult BALB/c mice. The genetic constitution of the host and the virus serotype can be critical factors in determining the outcome of a virus infection. The purpose of this study was to evaluate the possible role of host genetics in murine coronavirus-induced retinal disease. Methods. JHM virus was inoculated by the intravitreal route into BALB/c, CD-1, and A/J mice. At varying times after inoculation, eye tissues were evaluated histologically. Antibody responses to the virus were evaluated by neutralization assays. Results. JHM virus induces a biphasic retinal disease in BALB/c mice. In the early phase, 1 to 7 days after inoculation, retinal vasculitis is observed. The second phase, characterized by retinal degeneration in the absence of inflammation, is seen by day 10 and progresses for several months. There is a similar biphasic disease process in JHM virus- infected A/J mice. However, retinal changes are less severe than those seen in BALB/c mice. Retinal tissue damage induced by JHM virus in CD-1 mice is different. Only the early phase of the disease, consisting of retinal vasculitis, was observed. These CD-1 mice do not develop the retinal degenerative disease. In fact, after day 10, the retina has a normal appearance. These differences in retinal tissue damage are seen over a wide range of infectivity of the virus inocula. Virus concentrations ranging from 101.4 to 104.4 TCID50/5 μl were capable of inducing both inflammation and degeneration in BALB/c mice, whereas, the highest concentration of virus (104.4 TCID50/5 μl) in CD-1 mice resulted in only the early inflammatory changes. Conclusions. The authors show that the genetics of the host can profoundly affect the nature of retinal tissue damage. These studies substantiate the concept that a virus can indeed trigger retinal degenerative processes in genetically susceptible hosts.","coronavirus; genetic disease; retinal degeneration; retinal inflammation; viral infection","neutralizing antibody; virus antibody; animal model; animal tissue; antibody response; article; controlled study; coronavirus; disease predisposition; genetic predisposition; male; mouse; nonhuman; priority journal; retina degeneration; retina vasculitis; virus infection; virus infectivity; Animals; Antibodies, Viral; Coronavirus Infections; Eye Infections, Viral; Male; Mice; Mice, Inbred A; Mice, Inbred BALB C; Murine hepatitis virus; Neutralization Tests; Retinal Degeneration; Vasculitis","Robbins, S.G., Hamel, C.P., Detrick, B., Hooks, J.J., Murine coronavirus induces an acute and long-lasting disease of the retina (1990) Lab Invest., 62, pp. 417-426; Burnier, M., Wang, Y., Detrick, B., Hooks, J.J., Retinal manifestations of a murine coronavirus infection: A histopathological and ultrastructural study (1995) Exp Mol Pathol., , in press; Hooks, J.J., Percopo, C., Wang, Y., Detrick, B., Retina and retinal pigment epithelial cell autoantibodies are produced during murine coronavirus retinopathy (1993) J Immunol., 151, pp. 3381-3389; Roos, R.P., Genetically controlled resistance to virus infections of the central nervous system (1985) Prog Med Genet., 6, pp. 241-276; Barthold, S.W., Beck, D.S., Smith, A.L., Mouse hepatitis virus and host determinants of vertical transmission and maternally-derived passive immunity in mice (1988) Arch Virol., 100, pp. 171-183; Bang, F.B., Cody, T.S., Genetic resistance to mouse hepatitis virus (1980) Genetic Control of Natural Resistance to Infection and Malignancy, pp. 215-226. , Skamene E, Kongshavn PAL, Landy M, eds. New York: Academic Press; Wilson, G.A.R., Dales, S., In vivo and in vitro models of demyelinating disease: Efficiency of virus spread and formation of infectious centers among glial cells is genetically determined by the murine host (1988) J Virol., 62, pp. 3371-3377; Wang, Y., Detrick, B., Hooks, J.J., Coronavirus (JHM) replication with in the retina: Analysis of cell tropism in mouse retinal cell cultures (1993) Virology, 193, pp. 124-137; Oth, D., Lussier, G., Cainelli-Gebara, V.C.B., Dupuy, J.M., Susceptibility to murine hepatitis virus (type 3)-induced paralysis is influenced by class I genes of the MHC (1991) Eur J Immunogenet., 18, pp. 405-410","Hooks, J.J.; National Eye Institute, National Institutes of Health, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States",,,01460404,,IOVSD,"8550331","English","INVEST. OPHTHALMOL. VIS. SCI.",Article,"Final",,Scopus,2-s2.0-0030043018
"Ohsawa K., Watanabe Y., Takakura A., Itoh T., Sato H.","7102526100;7405447347;7003321513;7404747046;35354210200;","Replication of Rat Coronaviruses in Intestinal Cell Line, RCN-9, Derived from F344 Rats",1996,"Experimental Animals","45","4",,"389","393",,2,"10.1538/expanim.45.389","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030253245&doi=10.1538%2fexpanim.45.389&partnerID=40&md5=a007a2ce1cc9a4d24583236011b4edee","Lab. Anim. Ctr. for Biomed. Research, Nagasaki University, School of Medicine, 1-12-4 Sakamoto, Nagasaki 852, Japan; Ctrl. Inst. for Experimental Animals, 1430 Nogawa, Miyamae, Kawasaki 216, Japan","Ohsawa, K., Lab. Anim. Ctr. for Biomed. Research, Nagasaki University, School of Medicine, 1-12-4 Sakamoto, Nagasaki 852, Japan; Watanabe, Y., Lab. Anim. Ctr. for Biomed. Research, Nagasaki University, School of Medicine, 1-12-4 Sakamoto, Nagasaki 852, Japan; Takakura, A., Ctrl. Inst. for Experimental Animals, 1430 Nogawa, Miyamae, Kawasaki 216, Japan; Itoh, T., Ctrl. Inst. for Experimental Animals, 1430 Nogawa, Miyamae, Kawasaki 216, Japan; Sato, H., Lab. Anim. Ctr. for Biomed. Research, Nagasaki University, School of Medicine, 1-12-4 Sakamoto, Nagasaki 852, Japan","To examine the susceptibility of the epithelial cell line to rat coronavirus (RCV), we inoculated sialodacryoadenitis virus and Parker's RCV into five cell lines; JTC-19, rat L2, LLC, RCN-9 and LBC cells originating in the lungs, intestines and mammary tumors of rodents. Both RCVs were replicated in LBC and RCN-9 cells, but not in the others. The infectivity titers of both RCVs grown in RCN-9 cells were significantly higher than those in LBC cells in every passage (2.5-3.9 log rate). Both RCVs replicated in LBC cells showed higher tropism to RCN-9 cells than to LBC cells, suggesting that RCN-9 cells are more suitable for the replication of RCVs than LBC cells. The RCN-9 cell line would be useful for the investigation of RCV infection in rodents.","Rat coronavirus; Rcn-9 cell; SDAV","Coronavirus; Rat coronavirus; Rat sialodacryoadenitis coronavirus; Rodentia; animal; article; cell culture; cell line; Coronavirus; cytology; epithelium cell; Fischer 344 rat; giant cell; growth, development and aging; intestine; isolation and purification; mouse; pathogenicity; physiology; rat; rodent disease; virology; virus replication; Animals; Cell Line; Coronavirus, Rat; Epithelial Cells; Giant Cells; Intestines; Mice; Rats; Rats, Inbred F344; Rodent Diseases; Tumor Cells, Cultured; Virus Replication","Barthold, S.W., Souza, M.S., Smith, A.L., (1990) Lab. Anim. Sci., 40, pp. 481-485; Bhatt, P.N., Persy, D.H., Jonas, A.M., (1972) J. Infect. Dis., 126, pp. 123-130; Fujiwara, K., Wagner, J.E., (1994) Manual of Microbiologic Monitoring of Laboratory Animals, 2nd Ed., pp. 57-61. , (Waggie, K., Kagiyama, N., Allen, A. M., and Nomura, T., eds.) Public Health Service, Washington, D.C; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Jacoby, R.O., (1991) Arch. Virol., 118, pp. 57-66; Hajjar, A.M., DiGiacomo, R.F., Carpenter, J.K., Bingel, S.A., Moazed, T.C., (1991) Lab. Anim. Sci., 41, pp. 22-25; Hirano, N., Ono, K., Inoue, A., Murakami, T., Takamaru, H., (1985) Arch. Virol., 75, pp. 301-304; Hirano, N., Takamaru, H., Ono, K., Murakami, T., Fujiwara, K., (1986) Arch. Virol., 88, pp. 121-125; Inoue, Y., Kashima, Y., Aizawa, K., Hatakeyama, K., (1991) Jpn. J. Cancer Res., 82, pp. 90-97; Maeda, K., Ogura, Y., Fukagawa, S., Utsumi, K., Fujiwara, K., (1993) Exp. Anim., 42, pp. 221-224. , in Japanese; Maru, M., Sato, K., (1982) Arch. Virol., 73, pp. 33-43; Percy, D., Bond, S., MacInnes, J., (1989) Arch. Virol., 104, pp. 323-333; Percy, D.H., Williams, K.L., Bond, S.J., MacInnes, J.I., (1990) Arch. Virol., 112, pp. 195-202; Smith, A.L., DeSouza, M.S., Finzi, D., Barthold, S.W., (1992) Arch. Virol., 125, pp. 39-52; Taguchi, F., Yamada, A., Fujiwara, K., (1979) Arch. Virol., 59, pp. 275-279; Utsumi, K., Maeda, K., Yokota, Y., Fukagawa, S., Fujiwara, K., (1991) Exp. Anim., 40, pp. 361-365; Wagner, J.E., Besch-Williford, C.L., Steffen, E.K., (1991) Lab. Anim., 20, pp. 40-45; Weir, E.C., Jacoby, R.O., Paturzo, F.X., Johnson, E.A., Ardito, R.B., (1990) Lab. Anim. Sci., 40, pp. 138-143","Ohsawa, K.; Lab. Anim. Ctr. for Biomed. Research, Nagasaki University, School of Medicine, 1-12-4 Sakamoto, Nagasaki 852, Japan",,"International Press Editing Centre Incorporation",13411357,,JIDOA,"8902504","English","Exp. Anim.",Article,"Final",Open Access,Scopus,2-s2.0-0030253245
"Callebaut P., Enjuanes L., Pensaert M.","6603634162;7006565392;55905425400;","An adenovirus recombinant expressing the spike glycoprotein of porcine respiratory coronavirus is immunogenic in swine",1996,"Journal of General Virology","77","2",,"309","313",,27,"10.1099/0022-1317-77-2-309","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030088105&doi=10.1099%2f0022-1317-77-2-309&partnerID=40&md5=baad4552eea4c1e628534d24833bf5a2","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Canto Blanca, Madrid E-28049, Spain","Callebaut, P., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Enjuanes, L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Canto Blanca, Madrid E-28049, Spain; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Salisburylaan 133, B-9820 Merelbeke, Belgium","The full-length spike (S) gene of porcine respiratory coronavirus (PRCV) was inserted into the genome of human adenovirus type 5 downstream of the early transcription region 3 promoter. The recombinant virus replicated in cultures of the swine testicle ST cell line and directed the synthesis of S antigen with a maximum yield of approximately 26 μg per 106 cells. The antigen was cell-associated except in the late phase of the infection, when a small amount (3-5 μg per 106 cells) was released. The cell-associated antigen consisted of polypeptides of molecular mass 160 kDa and 175 kDa, comigrating with the authentic precursor S′ and the mature S protein of PRCV, respectively. The extra-cellular recombinant antigen corresponded to the 175 kDa mature protein. Some recombinant S protein was exposed on the cell surface and was recognized by neutralization-mediating anti-S monoclonal antibodies. Piglets, inoculated oronasally with the recombinant adenovirus vector developed PRCV-neutralizing serum antibodies and were partially protected against PRCV challenge, demonstrating the potential of live adenovirus as vaccine vector.",,"membrane antigen; monoclonal antibody; protein precursor; recombinant protein; virus antibody; virus antigen; virus glycoprotein; virus vaccine; membrane protein; recombinant vaccine; spike glycoprotein, coronavirus; virus envelope protein; virus vaccine; adenovirus; animal cell; animal experiment; article; controlled study; coronavirus; glycoprotein synthesis; immunization; immunogenicity; molecular weight; nonhuman; priority journal; promoter region; protein secretion; swine; virus recombinant; virus replication; animal; blood; Coronavirus; genetics; human; Human adenovirus; immunology; molecular genetics; nucleotide sequence; swine; virology; Adenoviruses, Human; Animals; Antibodies, Viral; Base Sequence; Coronavirus; Humans; Membrane Glycoproteins; Molecular Sequence Data; Swine; Vaccines, Synthetic; Viral Envelope Proteins; Viral Vaccines; Adenoviridae; Animalia; Coronavirus; Human adenovirus; Porcine respiratory coronavirus; Suidae; Sus scrofa","Andrew, M.E., Boyle, D.B., Whitefeld, P.L., Lockett, L.J., Anthony, I.D., Bellamy, A.R., Both, G.W., The immunogenicity of VP7, a rotavirus antigen resident in the endoplasmic reticulum is enhanced by cell-surface expression (1990) Journal of Virology, 64, pp. 4776-4783; Callebaut, P., Debouck, P., Pensaert, M., Enzyme-linked immunosorbent assay for the detection of the coronavirus-like agent and its antibodies in pigs with porcine epidemic diarrhea (1982) Veterinary Microbiology, 7, pp. 295-306; Callebaut, P., Correa, I., Pensaert, M., Jiménez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) Journal of General Virology, 69, pp. 1725-1730; Callebaut, P., Pensaert, M., Enjuanes, L., Construction of a recombinant adenovirus for the expression of the glycoprotein S antigen of porcine respiratory coronavirus (1994) Advances in Experimental Medicine and Biology, 342, pp. 469-470; Charltos, K.M., Artois, M., Prevec, L., Campbell, J.B., Casay, G.A., Wandeler, A.I., Armstrong, J., Oral rabies vaccination of skunks and foxes with a recombinant human adenovirus vaccine (1992) Archives of Virology, 123, pp. 169-179; Correa, I., Jiménez, G., Sune, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Research, 10, pp. 77-94; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. II Domains in the peplomer glycoprotein (1986) Journal of General Virology, 67, pp. 1405-1418; Godet, M., Raschaert, D., Laude, H., Processing and antigenicity of entire and anchor-free spike glycoprotein S of coronavirus TGEV expressed by recombinant baculovirus (1991) Virology, 185, pp. 732-740; Graham, F.L., Prevec, L., Manipulation of adenovirus vectors (1991) Methods in Molecular Biology, 7, pp. 109-128; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Veterinary Quarterly, 8, pp. 257-261; Pulford, D.J., Britton, P., Intracellular processing of the porcine coronavirus transmissible gastroenteritis virus spike protein expressed by recombinant vaccinia virus (1991) Virology, 182, pp. 765-773; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) Journal of General Virology, 71, pp. 2599-2607; Sanchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suné, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanchez, C.M., Gebauer, F., Suné, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; To, L.T., Bernard, S., Bottreau, E., Transmissible gastroenteritis corona virus: Surface antigens induced by virulent and attenuated strains (1992) Research in Virology, 143, pp. 241-248; Tuboly, T., Nagy, E., Derbyshire, J.B., Potential viral vectors for the stimulation of mucosal antibody responses against enteric antigens in pigs (1993) Research in Veterinary Science, 54, pp. 345-350; Van Reeth, K., Pensaert, M., Porcine respiratory corona-virus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) American Journal of Veterinary Research, 55, pp. 1275-1281; Wesseling, J.G., Godekle, G., Schijns, V.E.C.J., Prevec, L., Graham, F.L., Horzinek, M.C., Rottier, P.J.M., Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection (1993) Journal of General Virology, 74, pp. 2061-2069; Wold, W.S.M., Gooding, L.R., Region E3 of adenovirus: A cassette of genes involved in host immunosurveillance and virus-cell interactions (1991) Virology, 184, pp. 1-8","Callebaut, P.; Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, Salisburylaan 133, B-9820 Merelbeke, Belgium",,"Society for General Microbiology",00221317,,JGVIA,"8627235","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0030088105
"Kolb A.F., Maile J., Heister A., Siddell S.G.","7005622195;8048534500;57213128696;7005260816;","Characterization of functional domains in the human coronavirus HCV 229E receptor",1996,"Journal of General Virology","77","10",,"2515","2521",,34,"10.1099/0022-1317-77-10-2515","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029909263&doi=10.1099%2f0022-1317-77-10-2515&partnerID=40&md5=224cc53f7a141863ae63c41df81732e4","Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany","Kolb, A.F., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany; Maile, J., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany; Heister, A., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany","Human aminopeptidase N (hAPN or CD13) and porcine aminopeptidase N (pAPN) are functional receptors for human coronavirus (HCV) 229E and porcine transmissible gastroenteritis virus (TGEV), respectively. However, hAPN cannot function as a receptor for TGEV and pAPN cannot function as a receptor for HCV 229E. In this study, we constructed a series of chimeric hAPN/pAPN genes and expressed the corresponding proteins in transfected cells. Subsequently, we identified the chimeric proteins that can function as a receptor for HCV 229E. The results show that replacement of a small region of pAPN sequence (pAPN amino acids 255-348) with the corresponding hAPN sequence (hAPN amino acids 260-353) converts pAPN into a functional receptor for HCV 229E. The region of hAPN that we have defined in this way does not correspond to the region of pAPN that has been identified as essential for the TGEV-receptor interaction. We conclude that although both viruses use a homologous receptor protein, different regions of the protein are required to mediate susceptibility to infection with HCV 229E and TGEV.",,"chimeric protein; microsomal aminopeptidase; virus receptor; amino acid sequence; article; controlled study; Coronavirus; nonhuman; priority journal; protein domain; protein expression; recombinant gene; structure activity relation; swine; virus cell interaction; virus infection; Coronavirus; Hepatitis C virus; human coronavirus; Human coronavirus 229E; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Ashmun, R.A., Shapiro, L.H., Look, A.T., Deletion of the zinc-binding motif of CD13/aminopeptidase N molecules results in loss of epitopes that mediate binding of inhibitory antibodies (1992) Blood, 79, pp. 3344-3349; Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus binding activity on target tissues (1987) Journal of Virology, 61, pp. 185-189; Chen, C., Okoyama, H., High efficiency transformation of mammalian cells by plasmid DNA (1987) Molecular and Cellular Biology, 7, pp. 2745-2752; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) Journal of Virology, 68, pp. 5216-5224; Dimmock, N.J., Neutralization of animal viruses (1993) Current Topics in Microbiology and Immunology, 183, pp. 1-111; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Klumperman, J., Krijnse-Locker, J., Mijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) Journal of Virology, 68, pp. 6523-6534; Kumanishi, T., Brain tumors induced with Rous sarcoma virus, Schmidt-Ruppin strain. I. Induction of brain tumors in adult mice with Rous chicken sarcoma cells (1967) Japanese Journal of Experimental Medicine, 37, pp. 461-474; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) Journal of Clinical Investigation, 83, pp. 1299-1307; Olsen, J., Cowell, G.M., Konigshofer, E., Danielsen, E.M., Moller, J., Laustsen, L., Hansen, O.C., Noren, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Letters, 238, pp. 307-314; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) Journal of General Virology, 71, pp. 1065-1073; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Edited by S. G. Siddell. New York: Plenum Press; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Ziebuhr, J., (1995) Expression der 3-C-like-Proteinase des Humanen Coronavirus HCV 229E, , PhD thesis, University of Würzburg, Germany","Kolb, A.F.; Institute of Virology and Immunology, University of Wurzburg, Versbacherstr. 7, 97078 Wurzburg, Germany",,"Microbiology Society",00221317,,JGVIA,"8887485","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0029909263
"Houtman J.J.","6701855701;","Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM",1996,"Journal of NeuroVirology","2","2",,"101","110",,88,"10.3109/13550289609146543","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029920232&doi=10.3109%2f13550289609146543&partnerID=40&md5=24064cc403bb9190b161b1f41ebdf17e","Departments of Medical Microbiology and Immunology, University of Wisconsin, Madison, WI 53706, United States","Houtman, J.J., Departments of Medical Microbiology and Immunology, University of Wisconsin, Madison, WI 53706, United States","Infection of rodents with murine coronavirus JHM results in a subacute or chronic demyelinating disease which serves as a model for the human disease multiple sclerosis. Previous studies with JHMV have established a role for the immune system in both viral clearance and demyelination. To further clarify the role of the immune system in JHMV pathogenesis, several strains of congenitally immunodeficient mice were studied. Infection of immunocompetent C57BL/6 mice with JHMV resulted in severe paralysis and demyelination and complete clearance of infectious virus from the brain (C+D+ phenotype). In contrast, infected SCID mice showed little or no paralysis or demyelination and were unable to clear infectious virus (C-D- phenotype). Athymic nude mice and a proportion of mice lacking MHC Class I or II expression exhibited robust demyelination but did not completely clear infectious virus from the brain (C-D+ phenotype). These results are consistent with an immune-mediated mechanism for JHMV-induced demyelination, but indicate that the immune mechanisms which participate in demyelination and viral clearance are distinct. It may thus be possible to experimentally alter immunopathological responses without impairing antimicrobial immunity.","Immunopathology; Mouse hepatitis virus; Multiple sclerosis","major histocompatibility antigen class 1; major histocompatibility antigen class 2; animal experiment; animal model; animal tissue; article; controlled study; Coronavirus; demyelinating disease; demyelination; immune deficiency; immune system; immunocompetence; immunopathology; male; mouse; multiple sclerosis; nonhuman; paralysis; pathogenesis; phenotype; priority journal; virus infection; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Mus musculus; Rodentia","Bloemmen, J., Eyssen, H., Immunoglobulin levels of sera of genetically thymusless (nude) mice (1973) Eur J Immunol, 3, pp. 117-118; Bosma, G.C., Custer, R.P., Bosma, M.J., A severe combined immunodeficiency mutation in the mouse (1983) Nature, 301, pp. 527-530","Fleming, J.O.; Dept Medical Microbiology Immunology, University of Wisconsin, Madison, WI 53705, United States",,"Springer New York LLC",13550284,,JNVIF,"8799201","English","J. NEUROVIROL.",Article,"Final",,Scopus,2-s2.0-0029920232
"Schultze B., Zimmer G., Herrler G.","7006104520;7102982629;7006339246;","Virus entry into a polarized epithelial cell line (MDCK): Similarities and dissimilarities between influenza C virus and bovine coronavirus",1996,"Journal of General Virology","77","10",,"2507","2514",,15,"10.1099/0022-1317-77-10-2507","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030001570&doi=10.1099%2f0022-1317-77-10-2507&partnerID=40&md5=35f8acd45f5d6f3837f25df6ab710f22","Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str, 17, 35037 Marburg, Germany","Schultze, B., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str, 17, 35037 Marburg, Germany; Zimmer, G., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str, 17, 35037 Marburg, Germany; Herrler, G., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str, 17, 35037 Marburg, Germany","We have analysed the uptake of influenza C virus and bovine coronavirus (BCV) by a polarized epithelial cell line, Madin-Darby canine kidney (MDCK) cells. Both viruses use N-acetyl-9-O-acetylneuraminic acid as a receptor determinant for attachment to cells. Virus binding assays with immobilized proteins indicated that a glycoprotein of 40 kDa is the major surface protein containing the receptor determinant for the two viruses. MDCK cells grown on filters for permeable support were found to have differential sensitivity to infection by these viruses. Both viruses were able to initiate infection via the apical domain of the plasma membrane, but only influenza C virus also accomplished infection via the basolateral plasma membrane. The resistance of MDCK cells to BCV infection from the basal filter chamber was overcome when the cell polarity was abolished by maintaining the cells in calcium-free medium. This finding indicates that the resistance to basolateral infection by BCV is a property of the cell line and not due to a technical problem related to the use of filters. Our results indicate that two viruses which use the same receptor for attachment to cells may differ in their ability to enter polarized cells. The possible involvement of an accessory molecule in the entry of BCV is discussed.",,"glycoprotein; membrane protein; n acetylneuraminic acid; virus receptor; animal cell; article; basolateral membrane; cell polarity; controlled study; Coronavirus; epithelium cell; Influenza virus C; nonhuman; priority journal; virus cell interaction; virus infection; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Influenza C virus; Influenza virus","Basak, S., Turner, H., Compans, R.W., Expression of SV40 receptors on apical surfaces of polarized epithelial cells (1992) Virology, 190, pp. 393-402; Bhat, S., Spitalnik, S.L., Gonzalez-Scarano, F., Silberberg, D.H., Galactosyl ceramide or a derivative is an essential component of the neural receptor for human immunodeficiency virus type 1 envelope glycoprotein gp120 (1991) Proceedings of the National Academy of Sciences, USA, 88, pp. 7131-7134; Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) Journal of Virology, 61, pp. 185-189; Callebaut, C., Krust, B., Jacotot, E., Hovanessian, A.G., T cell activation antigen, CD26, as a cofactor for entry of HIV in CD4+ cells (1993) Science, 262, pp. 2045-2050; Clayson, E.T., Compans, R.W., Entry of simian virus 40 is restricted to apical surfaces of polarized epithelial cells (1988) Molecular and Cellular Biology, 8, pp. 3391-3396; Couceiro, J.N., Paulson, J.C., Baum, L.G., Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity (1993) Virus Research, 29, pp. 155-165; Dalgleish, A.G., Beverly, P.C.L., Clapham, P.R., Crawford, D.H., Graves, M.F., Weiss, R.A., The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus (1984) Nature, 312, pp. 763-766; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Dörig, R.E., Marcil, A., Chopra, A., Richardson, C.D., The human CD46 molecule is a receptor for measles virus (Edmonston strain) (1993) Cell, 75, pp. 295-305; Dunster, L.M., Schneider-Schaulies, J., Loffler, S., Lankes, W., Schwartz-Albiez, R., Lottspeich, F., Ter Meulen, V., Moesin: A cell membrane protein linked with susceptibility to measles virus infection (1994) Virology, 198, pp. 265-274; Hauri, H.P., Sterchi, E.E., Bienz, D., Fransen, J.A., Marxer, A., Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells (1985) Journal of Cell Biology, 101, pp. 838-851; Haverkamp, J., Veh, R.W., Sander, M., Schauer, R., Kamerling, J.P., Vliegenhart, G.F., Demonstration of 9-O-acetylneuraminic acid in brain gangliosides from various vertebrates including man (1977) Hoppe-Seyler's Zeitschrift für Physiologische Chemie, 358, pp. 1609-1612; Herrler, G., Klenk, H.-D., The surface receptor is a major determinant of the cell tropism of influenza C virus (1987) Virology, 159, pp. 102-108; Herrler, G., Klenk, H.-D., Structure and function of the HEF glycoprotein of influenza C virus (1991) Advances in Virus Research, 40, pp. 213-234; Herrler, G., Nagele, A., Meier-Ewert, H., Bhown, A.S., Compans, R.W., Isolation and structural analysis of influenza C virion glycoproteins (1981) Virology, 113, pp. 439-451; Herrler, G., Dürkop, I., Becht, H., Klenk, H.-D., The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor (1988) Journal of General Virology, 69, pp. 839-846; Klatzmann, D., Champagne, E., Chamaret, S., Gruest, J., Guetard, D., Hercend, T., Gluckman, J.C., Montagnier, L., T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV (1984) Nature, 312, pp. 767-768; Naniche, D., Varior-Krishnan, G., Cervoni, F., Wild, T.F., Rossi, B., Rabourdin-Combe, C., Gerlier, D., Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus (1993) Journal of Virology, 67, pp. 6025-6032; Payne, H.R., Storz, J., Analysis of cell fusion induced by bovine coronavirus infection (1988) Archives of Virology, 103, pp. 27-33; Richardson, J.C.W., Scalera, V., Simmons, N.L., Identification of two strains of MDCK cells which resemble separate nephron tubule segments (1981) Biochimica et Biophysica Acta, 673, pp. 26-36; Rogers, G.N., Pritchett, T.J., Lane, J.L., Paulson, J.C., Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: Selection of receptor specific variants (1983) Virology, 131, pp. 394-408; Rogers, G.N., Herrler, G., Paulson, J.C., Klenk, H.-D., Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells (1986) Journal of Biological Chemistry, 261, pp. 5947-5951; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells (1994) Journal of Virology, 68, pp. 7966-7973; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) Journal of General Virology, 73, pp. 901-906; Schultze, B., Herrler, G., Recognition of cellular receptors by bovine coronavirus (1994) Archives of Virology Supplement, 9, pp. 451-459; Schultze, B., Gross, H.J., Brossmer, R., Klenk, H.-D., Herrler, G., Hemagglutinating encephalomyelitis virus attaches to N-acetyl-9-O-acetylneuraminic acid-containing receptors on erythrocytes: Comparison with bovine coronavirus and influenza C virus (1990) Virus Research, 16, pp. 185-194; Schultze, B., Zimmer, G., Herrler, G., Viral lectins for the detection of 9-O-acetylated sialic acid on glycoproteins and glycolipids (1993) Lectins and Glycobiology, pp. 175-181. , Edited by H.-J. & S. Gabius. Wien: Springer Verlag; Shepley, M.P., Racaniello, V.R., A monoclonal antibody that blocks poliovirus attachment recognizes the lymphocyte homing receptor CD44 (1994) Journal of Virology, 68, pp. 1301-1308; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) Journal of General Virology, 64, pp. 761-776; Simmons, N.L., Ion transport in ""tight"" epithelial monolayers of MDCK cells (1981) Journal of Membrane Biology, 59, pp. 105-114; Simons, K., Wandinger-Ness, A., Polarized sorting in epithelia (1990) Cell, 62, pp. 207-210; Skehel, J.J., Baylay, P.M., Brown, E.B., Martin, S.R., Waterfield, M.D., White, J.M., Wilson, I.A., Wiley, D.C., Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion (1982) Proceedings of the National Academy of Sciences, USA, 79, pp. 968-972; Szepanski, S., Gross, H.J., Brossmer, R., Klenk, H.-D., Herrler, G., A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity (1992) Virology, 188, pp. 85-92; Tucker, S.P., Compans, R.W., Virus infection of polarized epithelial cells (1993) Advances in Virus Research, 42, pp. 187-247; Valentich, J.D., Morphological similarities between the dog kidney cell line MDCK and mammalian cortical collecting tubule (1981) Annals of the New York Academy of Sciences, 372, pp. 384-405; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proceedings of the National Academy of Sciences, USA, 85, pp. 4526-4529; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proceedings of the National Academy of Sciences, USA, 88, pp. 5533-5536; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Zimmer, G., Klenk, H.-D., Herrler, G., Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor (1995) Journal of Biological Chemistry, 270, pp. 17815-17822","Herrler, G.; Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany",,"Microbiology Society",00221317,,JGVIA,"8887484","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0030001570
"Gaertner D.J., Compton S.R., Winograd D.F., Smith A.L.","7004631465;7102893878;6603149758;57203012240;","Growth characteristics and protein profiles of prototype and wild-type rat coronavirus isolates grown in a cloned subline of mouse fibroblasts (L2p.176 cells)",1996,"Virus Research","41","1",,"55","68",,3,"10.1016/0168-1702(95)01274-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029865466&doi=10.1016%2f0168-1702%2895%2901274-5&partnerID=40&md5=01f33ddc8400710f936c948e469cada1","Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Institute for Animal Studies, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, United States","Gaertner, D.J., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States, Institute for Animal Studies, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, United States; Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Winograd, D.F., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Smith, A.L., Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States","Rat coronaviruses (RCVs) infect laboratory rats and confound biomedical research results. In vitro systems developed so far have limited the growth in knowledge about RCVs by not permitting generation of plaque-cloned virus stocks, reliable isolation of RCVs from rat tissues, or growth of high titered stocks of all isolates. Due to the fact that less than 20% of L2(Percy) cells were becoming infected, sublines were produced and selected for maximal growth of RCVs. Screening of 238 cell sublines yielded L2p.176 cells which were highly susceptible to all RCVs tested; however, susceptibility declined after 30 passages in vitro. Low-passaged L2p.176 cells were used to isolate virus from natural outbreaks and to propagate individual RCV plaques into high titered stocks. Proteins from six RCV isolates were immunoblotted using polyclonal rat and mouse antibodies to sialodacryoadenitis virus and polyclonal monospecific rabbit and goat antibodies against the peplomer (S) and nucleocapsid (N) proteins of mouse hepatitis virus (MHV). Proteins of two prototype, one Japanese and three wild type RCVs were examined and found to be similar to those of MHV, although the exact sizes and ratios of protein forms were unique for most RCV isolates. This study reports the development of a continuous cell line which reliably supports RCVs opening an opportunity for further in vivo studies of the biology of these agents. As a first step in the characterization of RCVs, we have shown that RCV proteins are very similar to those of MHV.","Cell culture; Cell line; Rat; Rat coronavirus; Sialodacryoadenitis virus; Virus strains","virus protein; animal cell; article; cell culture; cell line; controlled study; Coronavirus; fibroblast; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; rat; virogenesis; virus strain","Barker, M.G., Percy, D.H., Hovland, D.J., MacInnes, J.I., Preliminary characterization of the structural proteins of the coronaviruses, sialodacryoadenitis virus and Parker's rat coronavirus (1994) Can. J. Vet. Res., 58, pp. 99-103; Bhatt, P.N., Jacoby, R.O., Experimental infection of adult axenic rats with Parker's rat coronavirus (1977) Arch. Virol., 54, pp. 345-352; Bhatt, P.N., Jacoby, R.O., Jonas, A.M., Respiratory infection in mice with sialodacryoadenitis virus, a coronavirus of rats (1977) Infect. Immunol., 18, pp. 823-827; Boschert, K.R., Schoeb, T.R., Chandler, D.B., Dillehay, D.L., Inhibition of phagocytosis and interleukin-1 production in pulmonary macrophages from rats with sialodacryoadenitis virus infection (1988) J. Leukocyte Biol., 44, pp. 87-92; Freshney, R.I., Cloning and selection of specific cell types (1994) Culture of Animal Cells, pp. 161-178. , Wiley-Liss, New York; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Jacoby, R.O., Susceptibility of rodent cell lines to rat coronaviruses and differential enhancement by trypsin or DEAE-dextran (1991) Arch. Virol., 118, pp. 57-66; Gaertner, D.J., Winograd, D.F., Compton, S.R., Smith, A.L., Development and optimization of plaque assays for rat coronaviruses (1993) J. Virol. Methods, 43, pp. 53-64; Guberski, D.L., Thomas, V.A., Shek, W.R., Like, A.A., Handler, E.S., Rossini, A.A., Wallace, J.E., Welsh, R.M., Induction of type 1 diabetes by Kilham's rat virus in diabetes-resistant BB/Wor rats (1991) Science, 254, pp. 1010-1013; Huang, H.T., Haskell, A., McDonald, D.M., Changes in epithelial secretory cells and potentiation of neurogenic inflammation in the trachea of rats with respiratory infections (1989) Anat. Embryol., 180, pp. 325-341; Jacoby, R.O., Rat Coronavirus (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, pp. 625-638. , Bhatt, P.N., Jacoby, R.O., Morse, H.C. and New, A.E. (Eds.), Academic Press, Inc., New York; Kunita, S., Zhang, L., Homberger, F.R., Compton, S.R., Molecular characterization of the S proteins of two enterotropic murine coronavirus strains (1995) Virus Research, 35, pp. 277-289; Lorenz, R.J., Bogel, K., Calculation of titres and their significance (1973) Laboratory Techniques in Rabies, pp. 321-325. , M. Kaplan and H. Koprowski (Eds.), World Health Organization, Geneva; Maru, M., Sato, K., Characterization of a coronavirus isolated from rats with sialoadenitis (1982) Arch. Virol., 73, pp. 33-43; Parker, J.C., Cross, S.S., Rowe, W.P., Rat coronavirus (RCV): A prevalent naturally occurring pneumotropic virus of rats (1970) Arch fur Die Ges Virusforschg., 31, pp. 293-302; Paturzo, F.X., Letter to the Editor (1987) Lab. Anim. Sci., 37, p. 580; Percy, D., Bond, S., MacInnes, J., Replication of sialodacryoadenitis virus in mouse L-2 cells (1989) Arch. Virol., 104, pp. 323-333; Percy, D.H., Williams, K.L., Bond, S.J., MacInnes, J.I., Characteristics of Parker's rat coronavirus (PRC) replicated in L-2 cells (1990) Arch. Virol., 112, pp. 195-202; Percy, D.H., Scott, R.A.W., Coronavirus infection in the laboratory rat: Immunization trials using attenuated virus replicated in L-2 cells (1991) Can. J. Vet. Res., 55, pp. 60-66; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., RNA-binding proteins of coronavirus MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Smith, A.L., An immunofluorescence test for detection of serum antibody to rodent coronaviruses (1983) Lab. Anim. Sci., 33, pp. 157-160; Springer, T.A., Purification of proteins by precipitation (1994) Current Protocols in Molecular Biology, 2, pp. 10161-101611. , Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidmen, J.G., Smith, J.A., Struhl, K. (Eds.), Current Protocols, Greene Publishing Assoc, Inc. and Wiley, USA; Sturman, L.S., Holmes, D.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl. Acad. Sci., 76, pp. 4350-4354; Utsumi, K., Maeda, K., Yokota, Y., Fukagawa, S., Fujiwara, K., Reproductive disorders in female rats infected with sialodacryoadenitis virus (1991) Exp. Anim., 40, pp. 361-365; Weir, E.C., Jacoby, R.O., Paturzo, F.X., Johnson, E.A., Ardito, R.B., Persistence of sialodacryoadenitis virus in athymic rats (1990) Lab. Anim. Sci., 40, pp. 138-143","Gaertner, D.J.; Institute of Animal Studies, Albert Einstein College Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, United States",,"Elsevier B.V.",01681702,,VIRED,"8725102","English","VIRUS RES.",Article,"Final",,Scopus,2-s2.0-0029865466
"Gao H.-Q., Schiller J.J., Baker S.C.","34769957800;56354099200;7403307881;","Identification of the polymerase polyprotein products p72 and p65 of the murine coronavirus MHV-JHM",1996,"Virus Research","45","2",,"101","109",,14,"10.1016/S0168-1702(96)01368-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030560627&doi=10.1016%2fS0168-1702%2896%2901368-8&partnerID=40&md5=cf8164dfa1fa830a4ce592502a0a6482","Dept. of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States; ABL-Basic Research Program, National Cancer Institute, Cancer Res. and Development Center, Frederick, MD 21702, United States","Gao, H.-Q., Dept. of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States, ABL-Basic Research Program, National Cancer Institute, Cancer Res. and Development Center, Frederick, MD 21702, United States; Schiller, J.J., Dept. of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States; Baker, S.C., Dept. of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States","The RNA polymerase gene of murine coronavirus MHV-JHM encodes a polyprotein of greater than 750 kDa. This polyprotein is proposed to be processed by two papain-like cysteine proteinases, PCP-1 and PCP-2, and a poliovirus 3C-like proteinase domain, 3C-pro, to generate protein products. The amino-terminal product of the MHV polymerase polyprotein, p28, is generated by cleavage of the polyprotein by PCP-1. To identify the viral products downstream of p28, we generated a fusion-protein specific antiserum directed against the region adjacent to p28 and used the antiserum to detect virus-specific proteins from MHV-JHM infected cells. When this antiserum was used to immunoprecipitate radiolabeled proteins from MHV-JHM infected cell lysates, virus-specific proteins of 72 and 65 kDa were detected. Furthermore, pulse and chase experiments demonstrated that p72 is likely a precursor to the mature protein product, p65. To investigate which viral proteinase may be responsible for generating p72 and p65, we expressed the 5'-region of the MHV-JHM RNA polymerase gene including the two papain-like cysteine proteinase domains in an in vitro transcription/translation system and analyzed the translation products for proteolytic processing. We also cloned and expressed the 72 kDa region immediately downstream from p28, and tested the ability of in vitro translated PCP-1 and PCP-2 to cleave p72 to p65 in trans. Our results indicate that neither viral proteinase domain PCP-1 nor PCP-2 is capable of cleavage of p72 to produce p65 in vitro. The role of MHV proteinases in the processing of p72 and p65 is discussed.","Coronavirus; Polymerase polyprotein; Proteolytic processing","cysteine proteinase; RNA polymerase; virus protein; amino terminal sequence; Coronavirus; nonhuman; priority journal; protein degradation; protein processing; review; virus transcription; Coronavirus; Murinae; Murine hepatitis virus; Poliovirus","Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Piñon, J.D., Weiss, S.R., Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1932; Brierly, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Brierly, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65 kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. Virol., 60, pp. 12-18; Denison, M.R., Perlman, S., Identification of a putative polymerase gene product in cells infected with murine coronavirus A59 (1987) Virology, 157, pp. 565-568; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS Lett., 288, pp. 201-205; Guan, K., Dixon, J.E., Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase (1991) Anal. Biochem., 192, pp. 262-267; Hughes, S.A., Bonilla, P., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d (1995) Virology, 208, pp. 1-8; Krausslich, H.-G., Wimmer, E., Viral proteinases (1988) Annu. Rev. Biochem., 57, pp. 701-754; Lai, M.M.C., Liao, C.-L., Lin, Y.-J., Zhang, X., Coronavirus: How a large RNA viral genome is replicated and transcribed (1994) Infect. Agents Dis., 3, pp. 98-105; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierly, I., Identification, expression, and processing of an 87-kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Palmenberg, A.C., Proteolytic processing of picornaviral polyprotein (1990) Annu. Rev. Microbiol., 44, pp. 603-623; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A 59 (1989) Virology, 171, pp. 141-148; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M.M.C., Sequence and translation of the murine coronavirus 5′-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase (1987) J. Virol., 61, pp. 3968-3976; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Tibbles, K.W., Brierly, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S.G. Siddell (Ed.), Plenum Press, New York; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Baker, S.C.; Department of Microbiology, Layola University Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States",,"Elsevier B.V.",01681702,,VIRED,"8896245","English","VIRUS RES.",Article,"Final",Open Access,Scopus,2-s2.0-0030560627
"Van Reeth K., Nauwynck H., Pensaert M.","57191565576;7007141390;55905425400;","Dual infections of feeder pigs with porcine reproductive and respiratory syndrome virus followed by porcine respiratory coronavirus or swine influenza virus: A clinical and virological study",1996,"Veterinary Microbiology","48","3-4",,"325","335",,112,"10.1016/0378-1135(95)00145-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029873804&doi=10.1016%2f0378-1135%2895%2900145-X&partnerID=40&md5=b14722af5cff1d647607e3ccb69aac16","University of Gent, Faculty of Veterinary Medicine, Salisburylaan 133, 9820 Merelbeke, Belgium; Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium","Van Reeth, K., University of Gent, Faculty of Veterinary Medicine, Salisburylaan 133, 9820 Merelbeke, Belgium, Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Nauwynck, H., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium","Dual infections of pigs with porcine reproductive and respiratory syndrome virus (PRRSV) followed by a second common respiratory virus, either porcine respiratory coronavirus (PRCV) or swine influenza virus (SIV), were studied. The aim was to determine if dual infections, as compared to single virus infections, result in enhanced clinical manifestations. It was also examined if PRRSV replication affects replication of PRCV or SIV in the respiratory tract. Groups of conventional 10 week old pigs were inoculated with PRRSV-only (3 pigs), PRCV-only (4 pigs) or SIV-only (4 pigs). Dual inoculations with PRRSV-PRCV (4 pigs) and PRRSV-SIV (3 groups of 4, 4 and 5 pigs) were performed at a 3 day interval. A group of uninoculated control pigs (8 pigs) was included. The infection with PRRSV-only induced a transient fever (40.2°C) at 2 DPI, but no respiratory signs. The PRCV-only infection remained subclinical. The SIV-only infection resulted in a one day fever (40.1°C) with moderate tachypnoea and dyspnoea. Mean weight gain in the virus-inoculated groups was retarded compared with the control group. The PRRSV-PRCV infection induced a 9 day lasting fever (peak 40.9°C) with tachypnoea, dyspnoea and productive coughing. The PRRSV-SIV infection resulted in fever and respiratory signs in all 3 groups. Clinical signs, however, were more pronounced in group 1 than in groups 2 and 3. Pigs of group 1 showed fever during 10 days (peak 41.4°C), tachypnoea, marked dyspnoea with abdominal breathing, and a productive cough. Pigs of groups 2 and 3 had fever for 5 and 3 days (peaks 40.6 and 40.3°C) respectively and mild respiratory disorders. Mean weight gain during 14 DPI of the 2nd virus was 5.9 kg in the PRRSV-PRCV group and 4.0, 6.8 and 6.7 kg in PRRSV-SIV groups 1, 2 and 3 respectively. Mean weight gain during the corresponding period in the PRRSV-only group was 8.6 kg. It was concluded that dual infections with viruses causes more severe disease and growth retardation than single PRRSV infection. PRCV excretion curves-were similar in single and dual virus inoculated groups. Excretion of SIV was delayed by 2 days in the dual inoculated pigs. Thus, replication of the second virus is not (PRCV) or only slightly (SIV) affected by a prior infection with PRRSV.","Dual infections; Pigs; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Swine influenza virus","animal experiment; article; clinical feature; controlled study; Coronavirus; coughing; dyspnea; fever; lung infection; nonhuman; swine; Swine influenza virus; virus infection","Albina, E., Baron, T., Leforban, Y., Blue-eared pig disease in Brittany (1992) Vet. Rec., 130, p. 58; Boetner, A., Nielsen, J., Bille-Hansen, V., Porcine reproductive and respiratory syndrome in Denmark (1993) Progress Report AIR3-CT92-0939, PRRS; Epidemiology and Control; with Emphasis on Diagnosis, Viral Persistence, Extent of Viral Diversity, Anti-viral Immunity and Modes of Transmission, , Commission of the European Communities; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Edwards, S., Robertson, I., Wilesmith, J., Ryan, J., Kilner, C., Paton, D., Drew, T., Sands, J., PRRS (""blue-eared pig disease"") in Great Britain (1992) American Association of Swine Practitioners Newsletter, International PRRS Symposium Edition, 4, pp. 32-36; Feld, N.C., Qvist, P., Ahrens, P., Friis, N.F., Meyling, A., A monoclonal blocking ELISA detecting serum antibodies to Mycoplasma hyopneumoniae (1992) Vet. Microbiol., 30, pp. 35-46; Groschup, M.H., Brun, A., Haas, B., Serological studies on the potential synergism of porcine reproductive and respiratory syndrome virus and influenza-, corona-and paramyxoviruses in the induction of respiratory symptoms in swine (1993) J. Vet. Med. B, 40, pp. 681-689; Haesebrouck, F., Pensaert, M.B., Effect of intratracheal challenge of fattening pigs previously immunised with an inactivated influenza H1N1 vaccine (1986) Vet. Microbiol., 11, pp. 239-249; Houben, S., Van Reeth, K., Pensaert, M.B., Pattern of infection with the porcine reproductive and respiratory syndrome virus on swine farms in Belgium (1995) J. Vet. Med. B, 42, pp. 209-215; Ohlinger, V.F., Weiland, F., Haas, B., Visser, N., Ahl, R., Mettenleiter, T.C., Weiland, E., Straub, O.C., Porcine reproductive and respiratory syndrome (PRRS) (1991) Tierärtzl. Umschau, 46, pp. 703-708; Palmer, D.F., Coleman, M.T., Dowdle, W.R., Schild, G.C., Advanced laboratory techniques for influenza diagnosis (1975) Immunology Series No. 6, 6. , US Department of Health, Education and Welfare; Plana Duran, J., Vayreda, M., Vilarrasa, J., Bastons, M., Rosell, R., Martinez, M., San Gabriel, A., Domingo, M., Porcine epidemic abortion and respiratory syndrome (mystery swine disease). Isolation in Spain of the causative agent and experimental reproduction of the disease (1992) Vet. Microbiol., 33, pp. 203-211; Plana Duran, J., Vayreda, M., Vilarrasa, J., Bastons, M., Porquet, L., Urniza, A., PEARS (""mystery swine disease"") - Summary of the work conducted by our group (1992) American Association of Swine Practitioners Newsletter, International PRRS Symposium Edition, 4, pp. 16-18; Pol, J.M.A., Van Dijk, J.E., Wensvoort, G., Terpstra, C., Pathological, ultrastructural, and immunohistochemical changes caused by Lelystad virus experimentally induced infections of mystery swine disease (synonym:Porcine epidemic abortion and respiratory syndrome (PEARS)) (1991) Vet. Q., 13, pp. 137-143; Ramos, J., Pujols, J., Domingo, M., Miller, M., Rosell, R., Badiola, I., Pérez De Rozas, A., San Gabriel, A., Experimental infection of weaner pigs with PRRS (1992) American Association of Swine Practitioners Newsletter, International PRRS Symposium Edition, 4, p. 25; Van Reeth, K., Pensaert, M., Experimental infections with different porcine respiratory coronavirus field isolates: Clinical and virological aspects (1992) Proceedings of the 12th Congress of the International Pig Veterinary Society, p. 152. , The Hague, The Netherlands; Van Reeth, K., Pensaert, M.B., Porcine respiratory coronavirus - Mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) Am. J. Vet. Res., 55, pp. 1275-1281; Van Reeth, K., Pensaert, M., Prevalence of infections with enzootic respiratory and enteric viruses in feeder pigs entering fattening herds (1994) Vet. Rec., 135, pp. 594-597; Van Reeth, K., Pensaert, M., Production of interferon-α, tumor necrosis factor-α and interleukin-1 in the lungs of pigs infected with the porcine respiratory coronavirus (1994) Proceedings of the 3th Congress of the European Society for Veterinary Virology, pp. 197-201. , Interlaken, Switzerland, 4-7 September; Voets, M.Th., Pensaert, M.B., Rondhuis, P.R., Vaccination of pregnant sows against transmissible gastroenteritis using 2 attenuated virus strains and different inoculation routes (1980) Vet. Q., 2, pp. 211-219; Wensvoort, G., Terpstra, C., Pol, J.M.A., Ter Laak, E.A., Bloemraad, M., De Kluyver, E.P., Kragten, C., Braamskamp, J., Mystery swine disease in the Netherlands: The isolation of Lelystad virus (1991) Vet. Q., 13, pp. 121-130; Vynckier, A., Pensaert, M., Het porcien reproduktief en respiratoir syndroom: De isolatie van het virus en epidemiologisch onderzoek in belgië (1993) Vlaams Diergeneesk. Tijdschr., 62, pp. 118-122; Zhou, Y., Barghusen, S., Choi, C., Rossow, K., Collins, J., Laber, J., Molitor, T., Murtaugh, M., Effect of SIRS virus infection in leukocyte populations in the peripheral blood and on cytokine expression in alveolar macrophages of growing pigs (1992) American Association Swine Pract. Newsl. Int. PRRS Symposium Edition, 4, pp. 32-36","Van Reeth, K.; Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, 9820 Merelbeke, Belgium",,"Elsevier B.V.",03781135,,VMICD,"9054128","English","VET. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0029873804
"Schmidt W., Schneider T., Heise W., Weinke T., Epple H.-J., Stöffler-Meilicke M., Liesenfeld O., Ignatius R., Zeitz M., Riecken E.-O., Ullrich R.","57211731778;56835063000;7005709069;7005104389;55975584500;7003293053;7004026012;7003673138;33968271100;35447651500;7102394259;","Stool viruses, coinfections, and diarrhea in HIV-infected patients",1996,"Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology","13","1",,"33","38",,30,"10.1097/00042560-199609000-00006","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542744015&doi=10.1097%2f00042560-199609000-00006&partnerID=40&md5=97b0a4c0970ed4366a041fe10c033d1c","Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Institute of Virology, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Institute of Medical Microbiology, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Department of Medicine, Auguste-Viktoria Hospital, Berlin, Germany; Medizinische Klinik, Abteilung Gastroenterologie, Klinikum Benjamin Franklin, Hindenburgdamm 30, D-12200 Berlin, Germany; Department of Medicine, University of the Saarland, Homburg/Saar, Germany","Schmidt, W., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany, Medizinische Klinik, Abteilung Gastroenterologie, Klinikum Benjamin Franklin, Hindenburgdamm 30, D-12200 Berlin, Germany; Schneider, T., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany, Department of Medicine, University of the Saarland, Homburg/Saar, Germany; Heise, W., Department of Medicine, Auguste-Viktoria Hospital, Berlin, Germany; Weinke, T., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Epple, H.-J., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Stöffler-Meilicke, M., Institute of Virology, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Liesenfeld, O., Institute of Medical Microbiology, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Ignatius, R., Institute of Medical Microbiology, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Zeitz, M., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany, Department of Medicine, University of the Saarland, Homburg/Saar, Germany; Riecken, E.-O., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany; Ullrich, R., Department of Medicine, Univ. Klin. Benjamin Franklin, Free University of Berlin, Berlin, Germany","To examine the prevalence of stool viruses and their role in the pathogenesis of diarrhea in HIV infection, we evaluated biopsies and repeated stool samples of 256 HIV-infected patients undergoing diagnostic endoscopy because of diarrhea (n = 136) or other symptoms (n = 120) for bacterial, protozoal, and vital enteropathogens. In 70% of the patients with diarrhea, at least one potential enteropathogen was detected. Stool virus was detected by electron microscopy in 17% (44 of 256), adenovirus in 6.6% (17 of 256), and coronavirus in 11.3% (29 of 256) of the patients. Adenovirus and coronavirus were detected more frequently in patients with diarrhea than in patients without diarrhea [adenovirus 10% (13 of 136) vs. 3.3% (4 of 120), p = 0.0129; coronavirus 15% (21 of 136) vs. 6.6% (8 of 120), p = 0.0142]. Sixty-one percent of patients harboring stool virus were coinfected by another enteropathogen. Pathogens other than stool virus were detected more frequently in patients harboring adenovirus (82%) than in patients without stool virus (48%, p < 0.025). Adenovirus and coronavirus are frequently detected in stools of HIV-infected patients and may contribute to diarrhea. Adenovirus infection may facilitate the occurrence of other intestinal pathogens. Due to frequent coinfections, detection of stool viruses reduces the rate of diarrhea of unknown origin only by ~5%.","Adenovirus; AIDS; Coronavirus; Diarrhea; HIV; Stool virus; Viral gastroenteritis","Adenovirus; adult; article; Coronavirus; diarrhea; electron microscopy; feces analysis; female; human; human cell; Human immunodeficiency virus infection; human tissue; major clinical study; male; prevalence; priority journal; virus isolation; Adenoviridae; Bacteria (microorganisms); Coronavirus; Human immunodeficiency virus","Colebunders, R., Francis, H., Mann, J.M., Persistent diarrhea, strongly associated with HIV infection in Kinshasa, Zaire (1987) Am J Gastroenterol, 82, pp. 859-864; Janoff, E.N., Smith, P.D., Perspectives on gastrointestinal infections in AIDS (1988) Gastroenterol Clin North Am, 17, pp. 451-463; Smith, P.D., Quinn, T.C., Strober, W., Janoff, E.N., Masur, H., Gastrointestinal infections in AIDS. NIH conference, 1990 (1992) Ann Intern Med, 116, pp. 63-77; Laughon, B.E., Druckman, D.A., Vernon, A., Prevalence of enteric pathogens in homosexual men with and without acquired immunodeficiency syndrome (1988) Gastroenterology, 94, pp. 984-992; Grohmann, G.S., Glass, R.I., Reveira, H.G., Enteric viruses and diarrhea in HIV infected patients (1993) N Engl J Med, 329, pp. 14-20; Cunningham, A.L., Grohmann, G.S., Harkness, J., Gastro-intestinal viral infections in homosexual men who were symptomatic and seropositive for human immunodeficiency virus (1988) J Infect Dis, 158, pp. 386-391; Kaljot, K.T., Ling, J.P., Gold, J.W.M., Prevalence of acute enteric viral pathogens in acquired immunodeficiency syndrome patients with diarrhea (1989) Gastroenterology, 97, pp. 1031-1032; Ullrich, R., Heise, W., Bergs, C., L'Age, M., Riecken, E.O., Zeitz, M., Gastrointestinal symptoms in patients infected with human immunodeficiency virus: Relevance of infective agents isolated from gastrointestinal tract (1992) Gut, 33, pp. 1080-1084; Albrecht, H., Stellbrink, H.J., Fenske, S., Ermer, M., Raedler, A., Greten, H., Rotavirus antigen detection in patients with HIV infection and diarrhea (1993) Scand J Gastroenterol, 28, pp. 307-310; Maddox, A., Francis, N., Moss, J., Blanshard, C., Gazzard, B., Adenovirus infection of the large bowel in HIV positive patients (1992) J Clin Pathol, 45, pp. 684-688; Borum, M.L., Brumage, L.K., Orenstein, J.M., Parenti, D.M., Ward, D.J., Simon, G.L., Adenovirus associated diarrhea in patients with AIDS. International conference on antimicrobial agents and chemotherapy (1994) Interscience Conference on Antimicrobial Agents and Chemotherapy, , New Orleans, Abst. 270. New Orleans, 1993; Lessnau, K.-D., Milanese, S., Talavera, W., Mycobacterium gordonae: A treatable disease in HIV-positive patients (1993) Chest, 104, pp. 1779-1785; Dryden, M.S., Shanson, D.C., The microbial causes of diarrhoea in patients infected with the human immunodeficiency virus (1988) J Infect, 17, pp. 107-114; Kern, P., Müller, G., Schmitz, H., Detection of coronavirus-like particles in homosexual men with acquired immunodeficiency and related lymphadenopathy syndrome (1985) Klin Wochenschr, 63, pp. 68-72; Mathan, M., Mathan, V.J., Swaminathan, S.P., Yesudoss, S., Baker, S.J., Pleomorphic virus-like particles in human feces (1975) Lancet, 1, pp. 1068-1069; Schnagl, R.D., Holmes, J.H., Mackay-Scollay, E.M., Coronavirus-like particles in aboriginals and nonaboriginals in Western Australia (1978) Med J Aust, 1, pp. 307-309; Janoff, E.N., Orenstein, J.M., Manischewitz, J.F., Smith, P.D., Adenovirus colitis in the acquired immunodeficiency syndrome (1991) Gastroenterology, 100, pp. 976-979; Rice, A.P., Mathews, M.B., Trans-activation of the human immunodeficiency virus long terminal repeat sequences, expressed in an adenovirus vector, by the adenovirus E1A 13 S protein (1988) Proc Natl Acad Sci USA, 85, pp. 4200-4204; Kliewer, S., Garcia, J., Pearson, L., Soultanakis, E., Dasgupta, A., Gaynor, R., Multiple transcriptional regulatory domains in the human immunodeficiency virus type 1 long terminal repeat are involved in basal and E1A/E1B-induced promoter activity (1989) J Virol, 63, pp. 4616-4625; Varsano, I., Schonfeld, T.M., Matoth, Y., Severe disseminated adenovirus infection successfully treated with a thymic humoral factor, THF (1977) Acta Paediatr Scand, 66, pp. 329-332; Dagan, R., Schwartz, R.H., Insel, R.A., Menegus, M.A., Severe diffuse adenovirus 7a pneumonia in a child with combined immunodeficiency: Possible therapeutic effect of human immune serum globulin containing specific neutralizing antibody (1984) Pediatr Infect Dis, 3, pp. 246-251; Wigger, H.J., Blanc, W.A., Fatal hepatic and bronchial necrosis in adenovirus infection with thymic alymphoplasia (1966) N Engl J Med, 275, pp. 870-874; Lau, Y.L., Levinsky, R.J., Morgan, G., Strobel, S., Dual meningoencephalitis with echovirus type 11 and adenovirus in combined (common variable) immunodeficiency (1988) Pediatr Infect Dis J, 7, pp. 873-876; Baba, M., Mon, S., Shigeta, S., Clereq, E.D., Selective inhibitory effect of (S)-9-(3-hydroxy-2-phosphonylmethoxypropyl) adenine and 2′-nor-cyclic GMP on adenovirus replication in vitro (1987) Antimicrob Agents Chemother, 31, pp. 337-339","Schmidt, W.; Medizinische Klinik, Abteilung Gastroenterologie, Klinikum Benjamin Franklin, Hindenburgdamm 30, D-12200 Berlin, Germany",,"Lippincott Williams and Wilkins",10779450,,JDSRE,"8797684","English","J. ACQUIRED IMMUNE DEFIC. SYNDR. HUM. RETROVIROL.",Article,"Final",,Scopus,2-s2.0-1542744015
"Rice M.","12242393700;","Virus and virus-like particles observed in the intestinal contents of the possum, Trichosurus vulpecula",1996,"Archives of Virology","141","5",,"945","950",,9,"10.1007/BF01718168","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029686571&doi=10.1007%2fBF01718168&partnerID=40&md5=4b03a18d32f15fa7dc3eb16c43affad1","Department of Veterinary Pathology and Public Health, Massey University, Palmerston North, New Zealand","Rice, M., Department of Veterinary Pathology and Public Health, Massey University, Palmerston North, New Zealand","Intestinal contents derived from the Australian brush-tailed possum, Trichosurus vulpecula, were examined by negative stain electron microscopy for the presence of viruses. Out of 100 samples, 23 contained at least one type of vertebrate virus or virus-like particle. Adenovirus was identified in six samples, herpesvirus in two samples, coronavirus in four samples, and coronavirus-like particles in 14 samples. To date no viruses of the brush-tailed possum have been isolated in tissue culture but these results indicate that this species is probably host to several viral species. © Springer-Verlag 1996.",,"animal; article; intestine; isolation and purification; opossum; virion; virology; virus; Animals; Intestines; Opossums; Virion; Viruses","Almeida, J.D., Use and abuses of diagnostic electron microscopy (1983) Curr Top Microbiol Immunol, 104, pp. 147-158; Bagnall, B.G., Wilson, G.R., Molluscum contagiosum in a red kangaroo (1974) Aust J Derm, 15, pp. 115-120","Rice, M.; Department of Veterinary Pathology and Public Health, Massey University, Palmerston North, New Zealand",,"Springer Wien",03048608,,ARVID,"8678839","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0029686571
"Tsukamoto K.","57196917042;","Unique mechanism of coronavirus mRNA transcription",1996,"Uirusu. Journal of virology","46","2",,"99","107",,,"10.2222/jsv.46.99","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030345990&doi=10.2222%2fjsv.46.99&partnerID=40&md5=acac5717fa44d12d05c175038fce238f","Laboratory of Viral Pathogenesis, National Institute of Animal Health, Ibaraki, Japan","Tsukamoto, K., Laboratory of Viral Pathogenesis, National Institute of Animal Health, Ibaraki, Japan",[No abstract available],,"messenger RNA; virus protein; virus RNA; biosynthesis; Coronavirus; gene vector; genetic recombination; genetic transcription; genetics; metabolism; review; Coronavirus; Genetic Vectors; Recombination, Genetic; RNA, Messenger; RNA, Viral; Transcription, Genetic; Viral Proteins",,"Tsukamoto, K.",,,00426857,,,"9123893","Japanese","Uirusu",Review,"Final",Open Access,Scopus,2-s2.0-0030345990
"Vaughn E.M., Halbur P.G., Paul P.S.","7007145803;7005935318;7202714004;","Use of nonradioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates",1996,"Journal of Veterinary Diagnostic Investigation","8","2",,"241","244",,7,"10.1177/104063879600800216","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030113444&doi=10.1177%2f104063879600800216&partnerID=40&md5=9e302e6272b8938be7970a112f3771a4","Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Dept. Microbiol., Immunol., Prev. M., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States","Vaughn, E.M., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States, Dept. Microbiol., Immunol., Prev. M., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Halbur, P.G., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Paul, P.S., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States, Dept. Microbiol., Immunol., Prev. M., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States",[No abstract available],,"primer DNA; animal; animal disease; article; Coronavirus; differential diagnosis; DNA probe; genetics; isolation and purification; polymerase chain reaction; respiratory tract infection; restriction mapping; swine; swine disease; Transmissible gastroenteritis virus; virus infection; Animals; Coronavirus; Coronavirus Infections; Diagnosis, Differential; DNA Primers; DNA Probes; Gastroenteritis, Transmissible, of Swine; Polymerase Chain Reaction; Respiratory Tract Infections; Restriction Mapping; Swine; Swine Diseases; Transmissible gastroenteritis virus","Bae, I., Jackwood, D.J., Benfield, D.A., Differentiation of transmissible gastroenteritis virus from porcine respiratory coronavirus and other antigenically related coronaviruses by using cDNA probes specific for the 5′ region of the S glycoprotein gene (1991) J Clin Microbiol, 29, pp. 215-218; Benfield, D.A., Jackwood, D.J., Bae, I., Detection of transmissible gastroenteritis virus using cDNA probes (1992) Arch Virol, 116, pp. 91-106; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res, 21, pp. 181-198; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res Vet Sci, 48, pp. 165-169; Garwes, D.J., Stewart, F., Cartwright, S.F., Brown, I., Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet Rec, 122, pp. 86-87; Hill, H., Biwer, J., Woods, R., Wesley, R., Porcine respiratory coronavirus isolated from two U.S. swine herds (1990) Proc Am Assoc Swine Pract, pp. 333-335; Jackwood, D.J., Bae, I., Jackwood, R.J., Saif, L.J., Transmissible gastroenteritis virus and porcine respiratory coronavirus: Molecular characterization of the S gene using cDNA probes and nucleotide sequence analysis (1992) Coronaviruses: Molecular Biology and Virus-host Interactions, pp. 43-48. , eds. Laude H, Vautherot JF, Plenum Press, New York, NY; Laude, H., Van Reeth, K., Pensaert, M.B., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Meng, X.J., Paul, P.S., Vaughn, E.M., Zimmerman, J.J., Development of a radiolabeled nucleic acid probe for the detection of encephalomyocarditis virus of swine (1993) J Vet Diagn Invest, 5, pp. 254-258; Paul, P.S., Vaughn, E.M., Halbur, P.G., Characterization and pathogenicity of a new porcine respiratory coronavirus strain AR310 (1992) Proc Int Pig Vet Soc Congr, 12, p. 92; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Saif, L.J., Bohl, E.H., Transmissible gastroenteritis (1986) Diseases of Swine, pp. 255-274. , eds. Leman AD, Glock RD, Mengeling WL, Penny RHC, Scholl E, Straw B, 6th ed., Iowa State University Press, Ames, IA; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; Shockley, L.J., Kapke, P.A., Lapps, W., Diagnosis of porcine and bovine enteric coronavirus infections using cloned cDNA probes (1987) J Clin Microbiol, 25, pp. 1591-1596; Simkins, R.A., Weilnau, P.A., Van Cott, J., Competitive ELISA, using monoclonal antibodies to the transmissible gastroenteritis virus (TGEV) S protein, for serologic differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am J Vet Res, 54, pp. 254-259; Van Nieuwstadt, A.P., Boonstra, J., Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus, using monoclonal antibodies to antigenic sites A and X of the S glycoprotein (1992) Am J Vet Res, 53, pp. 184-190; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet Microbiol, 36, pp. 333-347; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J Clin Microbiol, 32, pp. 1809-1812; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J Vet Diagn Invest, 3, pp. 29-32; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317","Vaughn, E.M.; Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"8744748","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0030113444
"Smerdou C., Urniza A., Curtis III R., Enjuanes L.","6602856664;6507249554;7006668153;7006565392;","Characterization of transmissible gastroenteritis coronavirus S protein expression products in avirulent S. typhimurium Δcya Δcrp: Persistence, stability and immune response in swine",1996,"Veterinary Microbiology","48","1-2",,"87","100",,9,"10.1016/0378-1135(95)00141-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030069055&doi=10.1016%2f0378-1135%2895%2900141-7&partnerID=40&md5=a0863acb7535a418112edbd05c672aad","Dept. of Molecular and Cell Biology, CSIC, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Laboratorios Sobrino, Olot, Spain; Department of Biology, Washington University, One Brookings Drive, St. Louis, MO 63130, United States","Smerdou, C., Dept. of Molecular and Cell Biology, CSIC, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Urniza, A., Laboratorios Sobrino, Olot, Spain; Curtis III, R., Department of Biology, Washington University, One Brookings Drive, St. Louis, MO 63130, United States; Enjuanes, L., Dept. of Molecular and Cell Biology, CSIC, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain","The spike protein from transmissible gastroenteritis virus (TGEV) was expressed in attenuated S. typhimurium Δcya Δcrp Δasd χ39s7 Three partially overlapping fragments of TGEV S genet encoding the amino-terminal, intermediate, and carboxy-terminal end of the protein, as well as the full length gene were inserted into the asd+ plasmid pYA292 to generate recombinant plasmids pYATS-1, pYATS-2, pYATS-3, and pYATS-4, respectively, which were transformed into S. typhimurium χ3987 Recombinant S. typhimurium χ3987 pYATS-1 ) and χ3987 (pYATS-4) expressing constitutively a 53 Id}a amino-terminal fragment of the S protein and the full length protein (144 kDa), respectively, showed high stability. After 50 generations in vitro 60% and 20% of the bacteria transformed with pYATS-1 and pYATS-4, respectively, expressed the S-protein antigen. Since S. typhimurium χ3987 (pYATS-1) showed a better level of expression and stability in vitro, this recombinant strain was selected as a potential bivalent vector to induce both immunity to Salmonella and TGEV in swine. In order to study colonization of swine tissues by S. typhimurium Δ cya Δcrp, a gene conferring resistance to rifampicin was cloned into the chromosome of S. typhimurium χ3987, generating χ4509 strain. Both S. typhimurium χ4509 (pYA292) and χ4509 (pYATS-1) colonized the ileum of orally inoculated swine with clearance of bacteria between days 10-20 post-infection. The expression of the amino-terminal fragment of the S protein diminished the ability of S. typhimurium χ4509 (pYATS-1) to colonize deep tissues. The recombinant strain S. typhimurium χ3987 pYATS-1) induced TGEV specific antibodies in both serum and saliva of orally inoculated swine. This strain, as well as S. typhimurium χ3987 (pYA292), also elicited both systemic and mucosal immunity to Salmonella antigens.","Coronavirus; Mucosal immunity; Salmonella typhimurium; Swine; TGEV; Transmissible gastroenteritis virus","animal experiment; article; controlled study; Coronavirus; gastroenteritis; gene expression; humoral immunity; molecular cloning; nonhuman; Salmonella typhimurium; swine; Animalia; Coronavirus; Genetta; Salmonella typhimurium; Sus scrofa; Transmissible gastroenteritis virus; Typhimurium","Bacon, G.A., Burrows, T.W., Yates, M., The effects of biochemical mutation on the virulence of Bacterium typhosum: The virulence of mutants (1950) Brit. J. Exp. Pathol., 32, pp. 714-724; Bacon, G.A., Burrows, T.W., Yates, M., The effects of biochemical mutation on the virulence of Bacterium typhosum: The loss of virulence of certain mutants (1951) Brit. J. Exp. Pathol., 32, pp. 85-86; Bennell, M.A., Watson, D.L., The interactions of porcine and ovine, serum and colostral immunoglobulins with Staphylococcal protein A (1980) Microbiol. Immunol., 24, pp. 871-878; Birnboim, H.C., Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA (1979) Nucleic Acids Research, 7, pp. 1513-1517; Correa, I., Gebauer, F., Bullido, M.J., Suñé, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus (1990) J. Gen. Virol., 71, pp. 271-279; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus. Res., 10, pp. 77-94; Curtiss R. III, Chromosomal aberrations associated with mutation to bacteriophage resistance in Escherichia coli (1965) J. Bacteriol., 89, pp. 28-40; Curtiss R. III, Attenuated Salmonella strains as live vectors for the expression of foreign antigens (1990) New Generation Vaccines, pp. 161-188. , G.C. Woodrowand M.M. Levine, (Eds.), Marcel Dekker, Inc., New York; Curtiss R. III, Charamella, L.J., Stallions, D.R., Mays, J.A., Parental functions during conjugation in Escherichia coli K-12 (1968) Bacteriol. Rev., 32, pp. 320-348; Curtiss R. III, Galan, J.E., Nakayama, K., Kelly, S.M., Stabilization of recombinant avirulent vaccine strains in vivo (1990) Res. Microbiol., 141, pp. 797-805; Curtiss R. III, Kelly, S.M., Salmonella typhimurium deletion mutants lacking adenylate cyclase and cyclic AMP receptor protein are avirulent and immunogenic (1987) Infect. Immun., 55, pp. 3035-3043; De Groot, R.J., Luytjes, W., Horzineck, M.C., Van Der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike proteins of coronaviruses (1987) J. Mol. Biol., 196, pp. 963-966; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein (1986) J. Gen. Virol., 67, pp. 1405-1418; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike protein (1990) J. Gen. Virol., 71, pp. 1313-1323; Doggett, T.A., Jagusztyn-Krynicka, E.K., Curtiss R. III, Immune responses to Streptococcus sobrinus surface protein antigen A expressed by recombinant Salmonella typhimurium (1993) Infect. Immun., 61, pp. 1859-1866; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology (1995) The Coronaviridae, pp. 337-376. , S.G. Siddell (Eds.), Plenum Press, New York; Galan, J.E., Nakayama, K., Curtiss, R., Cloning and characterization of the asd gene of Salmonella typhimurium: Use in stable maintenance of recombinant plasmids in Salmonella vaccine strains (1990) Gene, 94, pp. 29-35; Garwes, D.J., Lucas, M.H., Higgins, D.A., Pike, B.V., Cartwright, S.F., Antigenicity of structural components from porcine transmissible gastroenteritis virus (1978) Vet. Microbiol., 3, pp. 179-190; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Germanier, R., Furer, E., Immunity in experimental salmonellosis. II. Basis for the avirulence and protective capacity of galE mutants of Salmonella typhimurium (1971) Infect. Immun., 4, pp. 663-673; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virol., 188, pp. 666-675; Hoiseth, S.K., Stocker, B.A.D., Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines (1981) Nature, 291, pp. 238-239; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Montgomery, P.C., Cohn, J., Lally, E.T., The induction and characterization of secretory antibodies (1974) Adv. Exp. Med., Biol., 45, p. 453; Nakayama, K., Kelly, S.M., Curtiss R. III, Construction of an asd+ expression-cloning vector: Stable maintenance and high level expression of cloned genes in a Salmonella vaccine strain (1988) Biotechnology, 6, pp. 693-697; Posthumus, W.P.A., Lenstra, J.A., Schaaper, W.M.M., Van Nieuwstadt, A.P., Enjuanes, L., Meloen, R.H., Analysis and simulation of a neutralizing epitope of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 3304-3309; Posthumus, W.P.A., Meloen, R.H., Enjuanes, L., Correa, I., Van Nieuwestadt, A., Koch, G., Linear neutralizing epitopes on the peplomer protein of coronaviruses (1990) Adv. Exp. Med. Biol., 276, pp. 181-188; Rasschaert, D., Laude, L., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Saif, L.J., Wesley, R.D., Transmissible Gastroenteritis (1992) Diseases of Swine, pp. 362-386. , A.D. Lemanet al., (Eds.), Wolfe Publishing Ltd; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: a Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, New York; Sáncher, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanz, A., García-Barreno, B., Nogal, M.L., Viñuela, E., Enjuanes, L., Monoclonal antibodies specific for African swine fever virus proteins (1985) J. Virol., 54, pp. 199-206; Schödel, F., Peterson, D., Hughes, J., Milich, D., Avirulent Salmonella expressing hybrid hepatitis B virus core/pre-S genes for oral vaccination (1993) Vaccine, 11, p. 143; Siddell, S., Wege, H., Volker, M., The biology of coronaviruses (1983) J. Gen. Virol, 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses (1990) Immunochemistry of Viruses II. The Basis for Serodiagnosis and Vaccines, pp. 359-379. , M.H.V. van Regenmorteland and A.R. Neurath (Eds.), Elsevier; Stabel, T.J., Mayfield, J.E., Tabatabai, L.B., Wannemuehler, M.J., Oral immunization of mice with attenuated Salmonella typhimurium containing a recombinant plasmid which codes for production of a 31-kilodalton protein of Brucella abortus (1990) Infect. Immun., 58, pp. 2048-2055; Stabel, T.J., Mayfield, J.E., Tabatabai, L.B., Wannemuehler, M.J., Swine immunity to an attenuated Salmonella typhimurium mutant containing a recombinant plasmid which codes for production of a 31-kilodalton protein of Brucella abortus (1991) Infect. Inmmun., 59, pp. 2941-2947; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG, and IgM(A) to protect neonatal pigs against the coronavirus transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Viral Res., 28, pp. 35-112; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet. Microbiol., 18, p. 197; Yanisch-Perron, P., Vieria, J., Messing, J., Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors (1985) Gene, 33, pp. 103-119; Zinder, N., Lysogenization and superinfection immunity in Salmonella (1958) Virology, 5, pp. 291-326","Enjuanes, L.; Dept. of Molecular/Cell Biology, Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain",,"Elsevier B.V.",03781135,,VMICD,"8701580","English","VET. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0030069055
"Phol-Koppe A., Raabe T., Siddell S.G., Ter Meulen V.","8117082200;56250084700;7005260816;7102867070;","Erratum: Detection of human coronavirus 229E-specific antibodies using recombinant fusion proteins (J. Virol. Methods 55 (1995) 175)",1996,"Journal of Virological Methods","56","1",,"123","",,,"10.1016/0166-0934(96)02012-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029983499&doi=10.1016%2f0166-0934%2896%2902012-5&partnerID=40&md5=d2dab97f48a50e4119ac4cdfae84a8f7","Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany","Phol-Koppe, A., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Raabe, T., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Ter Meulen, V., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany",[No abstract available],,"erratum; error; priority journal; Coronavirus; human coronavirus; Human coronavirus 229E",,"Phol-Koppe, A.; Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany",,"Elsevier B.V.",01660934,,JVMED,,"English","J. VIROL. METHODS",Erratum,"Final",,Scopus,2-s2.0-0029983499
"Cereda P.M., Gambaro F., Battaglia M., Cristallo A.","7003845258;6506375719;7201908369;6603250884;","Some features of Borna disease virus and human coronaviruses, and their possible involvement in human neurological diseases",1996,"Alpe Adria Microbiology Journal","5","2",,"87","103",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029821927&partnerID=40&md5=f786b644e212f525aee50e932ac3a70d","Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy","Cereda, P.M., Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy; Gambaro, F., Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy; Battaglia, M., Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy; Cristallo, A., Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy",[No abstract available],"Borna disease virus; human coronavirus 229E; human coronavirus OC43; human neurological diseases","borna disease; borna disease virus; clinical feature; coronavirus; histopathology; human; neurologic disease; review",,"Cereda, P.M.; Institute of Microbiology, University of Pavia, Via Brambilla 74, 27100 Pavia, Italy",,,11219750,,AAMJE,,"English","ALPE ADRIA MICROBIOL. J.",Review,"Final",,Scopus,2-s2.0-0029821927
"Herold J., Siddell S., Ziebuhr J.","7006838690;7005260816;7003783935;","Characterization of coronavirus RNA polymerase gene products",1996,"Methods in Enzymology","275",,,"68","89",,18,"10.1016/S0076-6879(96)75007-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029793870&doi=10.1016%2fS0076-6879%2896%2975007-3&partnerID=40&md5=d3cd735940f149a26be57f89d4365008",,"Herold, J.; Siddell, S.; Ziebuhr, J.",[No abstract available],,"gene product; messenger RNA; RNA polymerase; virus enzyme; Coronavirus; enzyme purification; genetic recombination; open reading frame; priority journal; protein domain; protein processing; review; RNA synthesis; sequence analysis; temperature sensitive mutant; virus characterization; virus gene; virus mutant; Coronavirus","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., (1987) J. Gen. Virol., 68, p. 57; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charité, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., (1990) Nucleic Acids Res., 18, p. 1825; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., (1991) Virology, 180, p. 567; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., (1993) Virology, 195, p. 680; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., (1994) Virology, 198, p. 736; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., (1995) Virology, 206, p. 817; Schaad, M.C., Stohlman, S.A., Egbert, J., Lum, K., Fu, K., Wei Jr., T., Baric, R.S., (1990) Virology, 177, p. 634; Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., (1990) Virology, 177, p. 646; Fu, K., Baric, R.S., (1994) J. Virol., 68, p. 7458; Schaad, M.C., Baric, R.S., (1994) J. Virol., 68, p. 8169; Ziebuhr, J., Herold, J., Siddell, S.G., (1995) J. Virol., 69, p. 4331; Dougherty, W.G., Semler, B.L., (1993) Microbiol. Rev., 57, p. 781; Koonin, E.V., (1991) J. Gen. Virol., 72, p. 2197; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., (1989) Nucleic Acids Res., 17, p. 4847; Gorbalenya, A.E., Koonin, E.V., (1989) Nucleic Acids Res., 17, p. 8413; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., (1987) EMBO J., 6, p. 3779; Brierley, I., Digard, P., Inglis, S.C., (1989) Cell (Cambridge, Mass.), 57, p. 537; Brierley, I., Rolley, N.J., Jenner, A.J., Inglis, S.C., (1991) J. Mol. Biol., 220, p. 889; Brierley, I., Jenner, A.J., Inglis, S.C., (1992) J. Mol. Biol., 227, p. 463; Herold, J., Siddell, S.G., (1993) Nucleic Acids Res., 21, p. 5838; Denison, M.R., Perlman, S., (1986) J. Virol., 60, p. 12; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M.M.C., (1987) J. Virol., 61, p. 3968; Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., (1989) J. Virol., 63, p. 3693; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., (1993) J. Virol., 67, p. 6056; Dong, S., Baker, S.C., (1994) Virology, 204, p. 541; Weiss, S.R., Hughes, S.A., Bonilla, P.J., Turner, J.D., Leibowitz, J.L., Denison, M.R., (1994) Arch. Virol., Suppl., 9, p. 349; Brayton, P.R., Lai, M.M.C., Patton, C.D., Stohlman, S.A., (1982) J. Virol., 42, p. 847; Dennis, D.E., Brian, D.A., (1982) J. Virol., 42, p. 153; Mahy, B.W.J., Siddell, S., Wege, H., Ter Meulen, V., (1983) J. Gen. Virol., 64, p. 103; Compton, S.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., (1987) J. Virol., 61, p. 1814; Leibowitz, J.L., De Vries, J.R., (1988) Virology, 166, p. 66; Jones, D.H., (1994) PCR Methods Appl, 3, p. 141; Hanahan, D., (1985) DNA Cloning: A Practical Approach, 1, p. 109. , (D. M. Glover, ed.), IRL Press, Oxford; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) ""Molecular Cloning: A Laboratory Manual,"" 2nd Ed., , Cold Spring Harbor Lab. Press, Cold Spring Harbor, NY; Laemmli, U.K., (1970) Nature (London), 227, p. 680; Prüfer, D., Tacke, E., Schmitz, J., Kull, B., Kaufmann, A., Rhode, W., (1992) EMBO J., 11, p. 1111; Melton, D.A., Krieg, P.A., Rebagliati, M.R., Maniatis, T., Zinn, K., Green, M.R., (1984) Nucleic Acids Res., 12, p. 7035; Baum, E.Z., Bebernitz, G.A., Palant, O., Mueller, T., Plotch, S.J., (1991) Virology, 185, p. 140; Wege, H., Wege, H., Nagashima, K., Ter Meulen, V., (1979) J. Gen. Virol., 42, p. 37; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., (1994) J. Virol., 68, p. 5772; Ellinger, S., Glockshuber, R., Jahn, G., Plückthun, A., (1989) J. Clin. Microbiol., 27, p. 971; Matsudeira, P., (1987) J. Biol. Chem., 262, p. 10035; Denison, M., Perlman, S., (1987) Virology, 157, p. 565; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., (1992) Virology, 189, p. 274; Denison, M.R., Hughes, S.A., Weiss, S.R., (1995) Virology, 207, p. 316; Harlow, E., Lane, D., (1988) Antibodies: A Laboratory Manual, , Cold Spring Harbor Lab. Press, Cold Spring Harbor, NY; Burdon, R.H., Van Knippenberg, P.H., (1988) Laboratory Techniques in Biochemistry and Molecular Biology, 19. , Elsevier, Amsterdam; Joo, M., Makino, S., (1995) J. Virol., 69, p. 272","Herold, J.; Institute of Virology, University of Wurzburg, Wurzburg, Germany",,"Academic Press Inc.",00766879,,MENZA,"9026661","English","METHODS ENZYMOL.",Article,"Final",Open Access,Scopus,2-s2.0-0029793870
"Kapil S., Richardson K.L., Radi C., Chard-Bergstrom C.","7003293348;19636522900;6507314570;6602711643;","Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line",1996,"Journal of Veterinary Diagnostic Investigation","8","1",,"96","99",,12,"10.1177/104063879600800115","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029679104&doi=10.1177%2f104063879600800115&partnerID=40&md5=8b2624aae249a8913370cf55b3e8dd20","Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Wisconsin Animal Health Laboratory, Madison, WI 53705, United States","Kapil, S., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Richardson, K.L., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Radi, C., Wisconsin Animal Health Laboratory, Madison, WI 53705, United States; Chard-Bergstrom, C., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States",[No abstract available],,"adenocarcinoma; animal; animal disease; article; cattle; cattle disease; cell culture; cell line; colon tumor; Coronavirus; feces; growth, development and aging; hemagglutination test; human; isolation and purification; rectum tumor; virology; virus infection; Adenocarcinoma; Animals; Cattle; Cattle Diseases; Cell Line; Colonic Neoplasms; Coronavirus Infections; Coronavirus, Bovine; Feces; Hemagglutination Tests; Humans; Rectal Neoplasms; Tumor Cells, Cultured","Athanassious, R., Marsobis, G., Assaf, R., Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dysentery in cattle in Quebec: Evaluation of three diagnostic methods (1994) Can Vet J, 35, pp. 163-169; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Bridger, J.C., Caul, E.O., Egglestone, S.I., Replication of an enteric bovine coronavirus in intestinal organ cultures (1978) Arch Virol, 57, pp. 43-51; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Craig, R.A., Kapil, S., (1994) Proc Annu Meet Am Assoc Vet Lab Diagn, 37, p. 107; Cyr-Coats, K.S.T., Payne, H.R., Storz, J., The influence of the host cell and trypsin treatment on bovine coronavirus infectivity (1988) J Vet Med B, 35, pp. 752-759; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation and cultivation in continuous cell lines (1980) Am J Vet Res, 41, pp. 30-38; Flewett, T.H., Electron microscopy in the diagnosis of infectious diarrhea (1978) J Am Vet Med Assoc, 173, pp. 538-541; Inaba, Y., Sato, K., Kurogi, H., Replication of bovine coronavirus in cell line BEK-1 culture (1976) Arch Virol, 50, pp. 339-342; Kapil, S., (1991) Intestinal Immune Response(s) of Newborn Calves to Bovine Enteric Coronavirus Infection, , PhD Dissertation, University of Minnesota, St. Paul, MN; Kapil, S., Laboratory diagnosis of canine viral enteritis (1995) Current Veterinary Therapy 12, Ed., pp. 697-701. , Bonugura JD, Kirk RW, WB Saunders Co., Philadelphia, PA; Kapil, S., Goyal, S.M., Bovine coronavirus-associated respiratory disease (1995) Compend Cont Ed Pract Vet, 17, pp. 179-181; Laporte, J., L'Haridon, R., Bobulesco, P., In vitro culture of bovine enteric coronavirus (BEC) (1979) Colloq INSERM, 90, pp. 99-102; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Stott, E.J., Thomas, L.H., Bridger, J.C., Replication of a bovine coronavirus in organ cultures of fetal trachea (1976) Vet Microbiol, 5, pp. 151-154; Tompkins, W.A.F., Watrach, A.M., Schmale, R.M., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 1101-1110","Kapil, S.; Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"9026088","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0029679104
"Smith D.R., Tsunemitsu H., Heckert R.A., Saif L.J.","7410366749;7004628959;7003443760;7102226747;","Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus",1996,"Journal of Veterinary Diagnostic Investigation","8","1",,"99","105",,36,"10.1177/104063879600800116","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029678915&doi=10.1177%2f104063879600800116&partnerID=40&md5=6c7a07fbae4857e061dc4a4e90ccb0b8","Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH, United States; Agriculture Canada, Animal Diseases Research Institute, Station H, PO Box 11300, Nepean, Ont. K2H 8P9, Canada","Smith, D.R., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH, United States; Tsunemitsu, H., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH, United States; Heckert, R.A., Agriculture Canada, Animal Diseases Research Institute, Station H, PO Box 11300, Nepean, Ont. K2H 8P9, Canada; Saif, L.J., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH, United States",[No abstract available],,"antibody; monoclonal antibody; animal; animal disease; article; cattle; cattle disease; cell culture; cell line; Coronavirus; enzyme linked immunosorbent assay; growth, development and aging; human; isolation and purification; laboratory diagnosis; methodology; rectum tumor; reproducibility; sensitivity and specificity; virus infection; Animals; Antibodies; Antibodies, Monoclonal; Cattle; Cattle Diseases; Cell Line; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; False Negative Reactions; False Positive Reactions; Humans; Rectal Neoplasms; Reproducibility of Results; Sensitivity and Specificity; Tumor Cells, Cultured","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., Bovine corona virus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet Scand, 32, pp. 163-170; Athanassious, R., Marsollais, G., Assaf, R., Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can Vet J, 35, pp. 163-169; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Crouch, C.F., Bielefeldt Ohman, H., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Crouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture enzyme-linked immunosorbent assay for detection of bovine enteric coronavirus (1984) J Clin Microbiol, 19, pp. 388-393; Czerney, C., Eichhorn, W., Characterization of monoclonal and polyclonal antibodies to bovine enteric coronavirus: Establishment of an efficient ELISA for antigen detection in feces (1989) Vet Microbiol, 20, pp. 111-122; Durham, P.J.K., Hassard, L.E., Armstrong, K.R., Naylor, J.M., Coronavirus associated diarrhea (winter dysentery) in adult cattle (1989) Can Vet J, 30, pp. 825-827; Hancock, D., Holler, S., Optimizing cutpoints of diagnostic tests (1995) Popul Med Newsl, 8, pp. 1-5; Heckert, R.A., Saif, L.J., Myers, G.W., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immunofluorescence of nasal epithelial cells (1989) Vet Microbiol, 19, pp. 217-231; Ilstrup, D.M., Statistical methods in microbiology (1990) Clin Microbiol Rev, 3, pp. 219-226; Kang, S.Y., Saif, L.J., Production and characterization of monoclonal antibodies against an avian group a rotavirus (1991) Avian Dis, 35, pp. 563-571; Martin, S.W., The evaluation of tests (1977) Can J Comp Med, 41, pp. 19-25; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.F., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of corona virus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Reynolds, D.J., Chasey, D., Scott, A.C., Bridger, J.C., Evaluation of ELISA (enzyme linked immunosorbent assay) and electron microscopy for the detection of coronavirus and rotavirus in bovine faeces (1984) Vet Rec, 114, pp. 397-401; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in southern Britain (1986) Vet Rec, 119, pp. 34-39; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Coronavirus immunogens (1993) Vet Microbiol, 37, pp. 285-297; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , ed. Saif LJ, Theil KW, CRC Press, Boca Raton, FL; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet Rec, 123, pp. 300-301; Sato, M., Akashi, H., Detection of bovine coronavirus by enzyme-linked immunosorbent assay using monoclonal antibodies (1994) J Vet Med Sci, 55, pp. 771-774; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Aetiology of diarrhoea in young calves (1986) Vet Rec, 119, pp. 31-34; Takahashi, E., Akashi, H., Inaba, Y., Bovine epizootic diarrhoea resembling winter dysentery caused by bovine coronavirus (1983) Japan Agricult Res Quart, 17, pp. 37-42; Thorns, C.J., Bell, M.M., Chasey, D., Development of monoclonal antibody ELISA for simultaneous detection of bovine coronavirus, rotavirus serogroup A, and Escherichia coli K99 antigen in feces of calves (1992) Am J Vet Res, 53, pp. 36-43; Trajstman, A.C., Diagnostic tests, sensitivity, specificity, efficiency and prevalence (1979) Aust Vet J, 55, p. 501; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Van Kruiningen, H.J., Castellano, V.P., Koopmans, M., Harris, L.L., A serologic investigation for coronavirus and Breda virus antibody in winter dysentery of dairy cattle in the northeastern United States (1992) J Vet Diagn Invest, 4, pp. 450-452; Van Kruiningen, H.J., Castellano, V.P., Torres, A., Sharpee, R.L., Serologic evidence of coronavirus infection in New York and New England dairy cattle with winter dysentery (1991) J Vet Diagn Invest, 3, pp. 293-296; Van Kruiningen, H.J., Khairallah, L.H., Sassevelle, V.G., Calfhood coronavirus enterocolitis: A clue to the etiology of winter dysentery (1987) Vet Pathol, 24, pp. 564-567; Welch, S.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity with virulent and attenuated virus (1988) Arch Virol, 101, pp. 221-235; Yolken, R.H., Enzyme immunoassays for the detection of infectious antigens in body fluids: Current limitations and future prospects (1982) Rev Infect Dis, 4, pp. 35-68","Smith, D.R.; Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"9026089","English","J. Vet. Diagn. Invest.",Review,"Final",Open Access,Scopus,2-s2.0-0029678915
"Muñoz M., Álvarez M., Lanza I., Cármenes P.","57213560309;7401846192;6701643399;6603172896;","Role of enteric pathogens in the aetiology of neonatal diarrhoea in lambs and goat kids in Spain",1996,"Epidemiology and Infection","117","1",,"203","211",,107,"10.1017/S0950268800001321","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029776351&doi=10.1017%2fS0950268800001321&partnerID=40&md5=be2c0e82a2cf9c33d6ad52fe7e969ec1","Departamento de Sanidad Animal, Facultad de Veterinaria, Campus de Vegazana, E-24071 León, Spain","Muñoz, M., Departamento de Sanidad Animal, Facultad de Veterinaria, Campus de Vegazana, E-24071 León, Spain; Álvarez, M., Departamento de Sanidad Animal, Facultad de Veterinaria, Campus de Vegazana, E-24071 León, Spain; Lanza, I., Departamento de Sanidad Animal, Facultad de Veterinaria, Campus de Vegazana, E-24071 León, Spain; Cármenes, P., Departamento de Sanidad Animal, Facultad de Veterinaria, Campus de Vegazana, E-24071 León, Spain","Faeces samples from diarrhoeic and non-diarrhoeic lambs and goat kids aged 1-45 days were examined for enteric pathogens. Cryptosporidium parvum was detected in both diarrhoeic lambs (45%) and goat kids (42%) but not in non-diarrhoeic animals. F5+ (K99+) and/or F41+ Escherichia coli strains were isolated from 26% and 22% of the diarrhoeic lambs and goat kids, respectively, although these strains, which did not produce enterotoxins ST I or LT I, were found with similar frequencies in non-diarrhoeic animals. A F5-F41-ST I+ E. coli strain was isolated from a diarrhoeic lamb (0.6%). Verotoxigenic E. coli was isolated from both diarrhoeic and non-diarrhoeic lambs (4.1% and 8.2%, respectively) and there was no association between infection and diarrhoea. The prevalence of group A rotavirus infection in diarrhoeic lambs was very low (2.1%). Groups A and B rotaviruses were detected in three (8.1%) and five (13.5%) diarrhoeic goat kids from two single outbreaks. Group C rotaviruses were detected in four non-diarrhoeic goat kids. An association of diarrhoea and infection was demonstrated only for group B rotavirus. Clostridium perfringens was isolated from 10.8% of the diarrhoeic goat kids but not from non-diarrhoeic goat kids or lambs. Salmonella arizonae was isolated from a diarrhoeic goat kid (2.7%) and the clinical characteristics of the outbreaks where these two latter enteropathogens were found different from the rest. Picobirnaviruses were detected in a diarrhoeic lamb. No coronaviruses were detected using a bovine coronavirus ELISA. No evidence was found of synergistic effect between the agents studied. Enteric pathogens were not found in four (8.7%) and three (20%) outbreaks of diarrhoea in lambs and goat kids, respectively.",,"enterotoxin; article; Clostridium perfringens; Coronavirus; Cryptosporidium parvum; diarrhea; enzyme linked immunosorbent assay; Escherichia coli; feces analysis; fetus; goat; lamb; newborn disease; nonhuman; prevalence; Rotavirus; Salmonella","Smith, M.C., Sherman, D.M., (1994) Goat Medicine, p. 342. , Pennsylvania: Lea & Febiger; Fassi-Fehri, M.M., Johnson, D.W., Taoudi, A., Berrada, J., Epidémiologie des diarrhées à Escherichia coli et à rotavirus chez le veau et l'agneau au Maroc (1988) Ann Rech Vét, 19, pp. 59-64; Nagy, B., Nagy, G., Palfi, V., Bozsó, M., Occurrence of Cryptosporidia, rotaviruses, coronavirus-like particles and K99+ Escherichia coli in goat kids and lambs (1983) Proceedings of the Third International Symposium of the World Association of Veterinary Laboratory Diagnosticians, pp. 525-531. , Ames, Iowa, USA; Ramisse, J., Lepareur, F., Poudelet, M., Brebion, M., Moinet, I., Mise en évidence de rotavirus et de cryptosporidies dans les diarrnées des jeunes agenaux (1984) Le Point Vétérinaire, 16, pp. 73-75; Yvore, P., Esnault, A., Naciri, M., Enquête épidémiologique sur les diarrhées néonatales des chevreaux dans les élevages de Touraine (1984) Les Maladies de La Chèvre, pp. 437-442. , Yvore, Perrin G, eds. Niort, France: Les colloques de l'INRA; Nagy, B., Palfi, V., Nagy, G., Hajtos, I., Merenyi, L., Infectious gastrointestinal diseases of young goats (1987) Proceedings of the Fourth International Conference on Goats, pp. 373-378. , Brasilia, Brasil; Snodgrass, D.R., Herring, J.A., Reid, H.W., Scott, F.M.M., Gray, E.W., Virus infections in cattle and sheep in Scotland 1975-1978 (1980) Vet Rec, 106, pp. 193-195; Adesiyun, A.A., Kaminjolo, J.S., Prevalence and epidemiology of selected enteric infections of livestock in Trinidad (1994) Prev Vet Med, 19, pp. 151-165; Beutin, L., Geier, D., Steinrück, H., Zimmermann, S., Scheutz, F., Prevalence and some properties of verotoxin (shiga-like toxin)-producing Escherichia coli in seven different species of healthy domestic animals (1993) J Clin Microbiol, 31, pp. 2483-2488; Cid, D., Ruiz Santa Quiteria, J.A., De La Fuente, R., F17 fimbriae in Escherichia coli from lambs and kids (1993) Vet Rec, 132, p. 251; Drolet, R., Fairbrother, J.M., Vaillancourt, D., Attaching and effacing Escherichia coli in a goat with diarrhoea (1994) Can Vet J, 35, pp. 122-123; García-Pastor, L., Ferrer-Mayayo, L.M., Cebrián-Yagüe, L.M., Casuística de procesos patológicos en 3 agrupaciones de defensa sanitaria de ganado ovino de la princia de Zaragoza. Sextas jornadas sobre producción animal (1995) Información Técnica Económica Agrarie, 16, pp. 592-594; Muñoz, M., Lanza, I., Alvarez, M., Cármenes, P., Rotavirus excretion by kids in a naturally infected goat herd (1994) Small Rum Res, 14, pp. 83-89; De Leeuw, P.W., Tiessink, J.W.A., Straver, P.J., Moerman, A., Bovine coronavirus infections in calves and their detection in the laboratory (1982) Proceedings of the Twelfth World Congress of Diseases of Cattle, 1, pp. 222-227. , The Netherlands; Guinée, P.A.M., Jansen, W.H., Agterberg, C., Detection of K99 antigen by means of agglutination and immunoelectrophoresis in Escherichia coli isolated from calves and its correlation with enterotoxigenicity (1976) Infect Immun, 8, pp. 731-735; Evans, D.J., Evans, D.G., Gorbach, S.L., Production of vascular permeability by enterotoxigenic Escherichia coli isolated from man (1973) Infect Immun, 8, pp. 725-730; Henriksen, S.A., Polenz, J.F.L., Staining of Cryptosporidia by a modified Ziehl-Neelsen technique (1981) Acta Vet Scand, 22, pp. 594-596; Muñoz, M., Álvarez, M., Lanza, I., Cármenes, P., An outbreak of diarrhoea associated with atypical rotaviruses in goat kids (1995) Res Vet Sci, 59, pp. 180-182; Gómez-Bautista, M., Ortega-Mora, L.M., Gass, A., Troncoso, J.M., Rojo-Vazquez, F.A., (1989) Epizootiología de La Cryptosporidiosis en Rumiantes (Terneros, Corderos y Cabritos), p. 253. , Cuarto congreso nacional y primer congreso ibérico de parasitología, Cáceres, España; Gouet, P., Pathologie digestive du chevreau nouveau-né (1984) Les Maladies de La Chèvre, pp. 433-436. , Yvore P, Perrin G, eds. Niort, France: Les colloques de l'INRA; Tzipori, S., Diarrhoea in goat kids attributed to Cryptosporidium infection (1982) Vet Rec, 111, pp. 35-36; Cid, D., Orden, J.A., Ruiz Santa-Quiteria, J.A., De La Fuente, R., (1991) Detección de Los Antígenos Fimbriales (F5yF41) y de Enterotoxina Termoestable (STa) en Cepas de E. Coli Aisladas de Procesos Diarreicos de Corderos y Cabritos Reden Nacidos, p. 243. , Décimotercer congreso nacional de microbiología. Salamanca, España: Sociedad Española de Microbiología; Mainil, J.G., Bex, F., Jacquemin, E., Pohl, P., Prevalence of four enterotoxin (STaP, STaH, STb, and LT) and four adhesin subunit (K99, K88, 987P, and F41) genes among Escherichia coli isolates from cattle (1990) Am J Vet Res, 2, pp. 187-190; Woodward, M.J., Wray, C., Nine DNA probes for detection of toxin and adhesin genes in Escherichia coli isolated form diarrhoeal disease in animals (1990) Vet Microbiol, 25, pp. 55-65; Carrol, P.J., Woodward, M.J., Wray, C., Detection of LT and STIa toxins by latex and EIA tests (1990) Vet Rec, 127, pp. 335-336; Reynolds, D.I., Morgan, I.H., Chanter, N., Microbiology of calf diarrhoea in southern Britain (1986) Vet Rec, 119, pp. 34-39; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet Rec, 119, pp. 31-34; Dorn, C.R., Scotland, S.M., Smith, H.R., Willshaw, G.A., Rowe, B., Properties of vero cytotoxin-producing Escherichia coli of human and animal origin belonging to serotypes other than 0157:H7 (1989) Epidemiol Inflet, 103, pp. 83-95; Chanter, N., Morgan, J.H., Bridger, J.C., Hall, G.A., Reynolds, D.J., Dysentery in gnotibiotic calves caused by atypical Escherichia coli (1984) Vet Rec, 114, p. 71; Smith, H.W., A search for transmissible pathogenic characters in invasive strains of Escherichia coli: The discovery of a plasmid-controlled toxin and a plasmid-controlled lethal character closely associated, or identical, with colicine V (1974) J Gen Microbiol, 83, pp. 95-111; Berrios, P., Celedón, M.O., Ramírez, V., Rotavirus en ovinos: Detección mediante ELISA y aislamiento en cultivos celulares MA-104 (1988) Arch Med Vet, 20, pp. 108-112; Snodgrass, D.R., Herring, J.A., A survey of rotaviruses in sheep in Scotland (1977) Vet Rec, 100, p. 341; Muñoz, M., Lanza, I., Álvarez, M., Cármenes, P., Prevalence of neutralizing antibodies to 9 rotavirus strains representing 7 G-serotypes in sheep sera (1995) Vet Microbiol, 45, pp. 351-361; Möstl, K., Nowotny, N., Abnehmende Häufigkeit der Beteiligung von Rotaviren an Ferkeldurchfállen in Österreich (1990) Wien Tierárztl Mschr, 77, pp. 314-317; Bridger, J.C., Rotavirus: The present situation in farm animals (1980) Vet Annual, 20, pp. 172-179; Chasey, D., Banks, J., The commonest rotaviruses from neonatal lamb diarrhoea in England and Wales have atypical electropherotypes (1984) Vet Rec, 115, pp. 326-327; Tzipori, S., Makin, T.J., Smith, M.L., Krautil, F.L., Clinical manifestation of diarrhoea in calves infected with rotavirus and enterotoxigenic Escherichia coli (1981) J Clin Microbiol, 13, pp. 1011-1016; Tzipori, S., Sherwood, D., Angus, K.W., Campbell, I., Gordon, M., Diarrhoea in lambs: Experimental infection with enterotoxigenic E. coli, rotavirus and Cryptosporidium sp (1981) Infect Immun, 33, pp. 401-406; Berrios, P., Nuñez, F., Celedón, M.O., Fiegehen, P., Santibáñez, M.C., Detección de rotavirus en caprinos de San José de Maipo, Región Metropolitana, Chile (1988) Avances en Ciencias Veterinarias, 3, pp. 98-101; Gatti, M.S.V., De Pestana Castro, A.F., Ferraz, M.M.G., Viruses with bisegmented double-stranded RNA in pig faeces (1989) Res Vet Sci, 47, pp. 397-399; Van Opdenbosch, E., Wellemans, G., Birna-type virus in diarrhoea calf faeces (1989) Vet Rec, 125, p. 610","Munoz, M.; Departamento de Sanidad Animal, Facultad de Veterinaria, Universidad de Leon, E-24071 Leon, Spain",,"Cambridge University Press",09502688,,EPINE,"8760970","English","EPIDEMIOL. INFECT.",Article,"Final",,Scopus,2-s2.0-0029776351
"Gueguen C., Maga A., McCrae M.A., Bataillon G.","7005855880;6506505329;7004653864;6603069353;","Caprine and bovine B rotaviruses in Western France: Group identification by Northern hybridization",1996,"Veterinary Research","27","2",,"171","176",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029693418&partnerID=40&md5=6c9b0d394945068f5cc37572128f584c","Lab. Veterinaire Departemental, 24, rue de Coëtlogon, 35031 Rennes, France; Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom","Gueguen, C., Lab. Veterinaire Departemental, 24, rue de Coëtlogon, 35031 Rennes, France; Maga, A., Lab. Veterinaire Departemental, 24, rue de Coëtlogon, 35031 Rennes, France; McCrae, M.A., Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom; Bataillon, G., Lab. Veterinaire Departemental, 24, rue de Coëtlogon, 35031 Rennes, France","In a survey of coronavirus and rotavirus-induced neonatal diarrhoea in 373 calves from 284 farms, nine (2.4%) of the animals were found to be infected with non-group A rotaviruses when their faeces were analysed in a commercial ELISA and by PAGE. Seven out of eight 1-4-day-old kids from a single farm were also infected with similar viruses. In a mini-PAGE, all the viruses displayed group B- and/or E-like 4223 electrophoretypes. In Northern hybridizations with cDNA chemiluminescent probes specific to rotavirus groups A (RF strain), B (adult diarrhoea rotavirus, ADRV) and C (Cowden strain) all the viruses belonged to group B.","B rotavirus; Northern blot; RT-PCR; Ruminant","Adult diarrheal rotavirus; Animalia; Bovinae; Capra; Coronavirus; Rotavirus; Rotavirus A; complementary DNA; primer DNA; virus RNA; animal; animal disease; article; cattle; cattle disease; chemoluminescence; classification; diarrhea; DNA probe; enzyme linked immunosorbent assay; France; genetics; goat; goat disease; isolation and purification; methodology; molecular genetics; newborn; Northern blotting; nucleotide sequence; oligonucleotide probe; polyacrylamide gel electrophoresis; polymerase chain reaction; Rotavirus; virology; virus infection; Animals; Animals, Newborn; Base Sequence; Blotting, Northern; Cattle; Cattle Diseases; Chemiluminescent Measurements; Diarrhea; DNA Primers; DNA Probes; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; France; Goat Diseases; Goats; Molecular Sequence Data; Oligonucleotide Probes; Polymerase Chain Reaction; RNA, Viral; Rotavirus; Rotavirus Infections","Bodkin, D.K., Knudson, D.L., Assessment of sequence relatedness of double-stranded RNA genes by RNA-RNA blot hybridization (1985) J Virol Methods, 10, pp. 45-52; Brémont, M., Chabanne-Vautherot, D., Vannier, P., McCrae, M.A., Cohen, J., Sequence analysis of the gene (6) encoding the major capsid protein (VP6) of group C Rotavirus: Higher than expected homology of the corresponding protein from group A virus (1990) Virology, 178, pp. 579-583; Bndger, J.C., Novel rotaviruses in animals and man (1987) Novel Diarrhea Viruses, pp. 5-23. , Ciba Foundation Symp 128, Wiley, London; Bridger, J.C., Non-A rotaviruses (1994) Viral Infections of the Gastrointestinal Tract, pp. 369-407. , (AZ Kapikian, ed), Marcel Dekker. New York; Brown, D.W.G., Beards, G.M., Chen, G.M., Flewett, T.H., Prevalence of antibody to group B (atypical) rotavirus in humans and animals (1987) J Clin Microbiol, 25, pp. 316-319; Chasey, D., Davies, P., Atypical rotaviruses in pigs and cattle (1984) Vet Rec, 114, pp. 16-17; Chasey, D., Banks, J., The commonest rotaviruses from neonatal lamb diarrhea in England and Wales have atypical electrophoretypes (1984) Vet Rec, 115, pp. 326-327; Chen, G.M., Werner-Eckert, R., Tao, H., Mackow, E.R., Expression of the major inner capsid protein of the group B Rotavirus ADRV: Primary characterization of genome segment 5 (1991) Virology, 182, pp. 820-829; Cohen, J., Lefèvre, F., Estes, M.K., Brémont, M., Cloning of bovine rotavirus (RF strain): Nucleotide sequence of the gene coding for the major capsid protein (1984) Virology, 138, pp. 178-182; Francki, R.I.B., Fauquet, C.M., Knudson, D.L., Brown, F., Classification and nomenclature of viruses Fifth report of the International Committee on Taxonomy of Viruses (1991) Arch Virol, pp. 186-191; Herring, A.J., Inglis, N.F., Ojeh, C.K., Snodgrass, D.R., Menzies, J.D., Rapid diagnosis of rotavirus infection by direct detection of viral nucleic acid in silverstained polyacrylamide gels (1982) J Clin Microbiol, 16, pp. 473-477; Hung, T., Chen, G., Wang, C., Rotavirus-like agent in adult non-bacterial diarrhoea in China (1983) Lancet, 2, pp. 1078-1079; Hung, T., Wang, C., Fang, Z., Waterborne outbreak of rotavirus diarrhoea in adults in China caused by a novel rotavirus (1984) Lancet, 1, pp. 1139-1142; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (Lond), 227, pp. 680-685; L'Haridon, R., Scherrer, R., In vitro culture of a rotavirus associated with neonatal calf scours (1976) Ann Rech Vét, 7, pp. 373-381; McCrae, M.A., Nucleic acid-based analyses of non-group a rotaviruses (1987) Novel Diarrhea Viruses, pp. 24-48. , Ciba Foundation Symp 128, Wiley, London; Pedley, S., Bridger, J.C., Chasey, D., McCrae, M.A., Definition of two new groups of atypical rotaviruses (1986) J Gen Virol, 67, pp. 131-137; Saif, L.J., Bohl, E.H., Theil, K.W., Cross, R.F., House, J.A., Rotavirus-like, Calicivirus-like and 23 nm virus-like particles associated with diarrhea in young pigs (1980) J Clin Microbiol, 12, pp. 105-111; Saif, L.J., Jiang, B., Non group A Rotaviruses of humans and animals (1994) Curr Topics Microbiol Immunol, 185, pp. 339-407; Scherrer, R., Cohen, J., L'Haridon, R., Feynerol, C., Fayet, J.C., Reovirus-like agent (Rotavirus) associated with neonatal calf gastroenteritis in France (1976) Ann Rech Vét, 7, pp. 25-31; Snodgrass, D.R., Herring, A.J., Campbell, I., Inglis, J.M., Hargreaves, F.D., Comparison of atypical rotaviruses from calves, piglets, lambs and man (1984) J Gen Virol, 65, pp. 909-914; Tanaka, T.N., Conner, M.E., Graham, D.Y., Estes, M.K., Molecular characterization of three rabbit rotavirus strains (1988) Arch Virol, 98, pp. 253-265; Thorns, C.J., Bell, M.M., Chasey, D., Chesham, J., Roeder, P.L., Development of monoclonal antibody ELISA for simultaneous detection of bovine coronavirus, rotavirus serogroup A, and Escherichia coli K99 antigen in feces of calves (1992) Am J Vet Res, 53, pp. 36-43; Tosser, G., Labbé, M., Brémont, M., Cohen, J., Expression of the major capsid protein VP6 of group C rotavirus and synthesis of chimeric single-shelled particles by using recombinant baculoviruses (1992) J Virol, 66, pp. 5825-5831; Xu, L., Harbour, D., McCrae, M.A., The application of polymerase chain reaction to the detection of rotaviruses in faeces (1990) J Virol Methods, 27, pp. 29-37","Bataillon, G.; Lab. Veterinaire Departemental, 24, rue de Coëtlogon, 35031 Rennes, France",,"EDP Sciences",09284249,,VEREE,"8721296","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0029693418
"Shoup D.I., Swayne D.E., Jackwood D.J., Saif L.J.","7003909464;35768368400;7005468303;7102226747;","Immunohistochemistry of transmissible gastroenteritis virus antigens in fixed paraffin-embedded tissues",1996,"Journal of Veterinary Diagnostic Investigation","8","2",,"161","167",,13,"10.1177/104063879600800204","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030113485&doi=10.1177%2f104063879600800204&partnerID=40&md5=68a0d058f9b3c3159eba0869cae1a330","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","Shoup, D.I., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Swayne, D.E., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Jackwood, D.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","An immunohistochemistry technique was developed using fixed tissues to study the presence and location of transmissible gastroenteritis virus (TGEV) antigens in situ. Experimentally infected gnotobiotic and conventional pigs as well as pigs with natural TGEV infection were examined. The staining technique was based on detection of the major structural protein of TGEV, the nucleocapsid, by using a pool of 3 monoclonal antibodies. Formalin and periodate-lysine-paraformaldehyde (PLP)-fixed intestinal tissues from a gnotobiotic pig inoculated with virulent TGEV were used to determine optimal antibody concentrations and incubation times. The intestinal tissues remained in their respective fixatives for 6 months, and serial sections were removed at sequential times and embedded in paraffin blocks. PLP and 10% neutral buffered formalin were acceptable fixatives and preserved TGEV nucleocapsid antigenicity for up to 6 months. Formalin, in comparison with PLP as a fixative, was better for preserving original tissue morphology and provided better antigen detection. Conventional crossbred pigs were inoculated with virulent TGEV, and animals were euthanized on various postexposure days. Intestinal tissues were positive for TGEV nucleocapsid antigens on postexposure days 2, 4, and 8. The immunohistochemistry technique detected TGEV antigen in stored paraffin-embedded tissues from 14 naturally infected pigs previously confirmed as positive for TGEV using a direct immunofluorescence assay on intestinal mucosal smears, whereas 9 naturally infected pigs confirmed negative for TGEV antigen by the same immunofluorescence assay showed no staining consistent with the presence of TGEV antigen. Immunohistochemistry provides a method to detect TGEV and possibly other closely related coronaviruses such as porcine respiratory coronavirus in situ. A diagnostic test using the same fixed tissues processed for histopathology provides veterinary practitioners an alternative to delivering live pigs or refrigerated fresh intestinal samples containing infectious virus to a diagnostic laboratory. Investigators can utilize this technique to retrospectively screen fixed tissues for TGEV antigen.",,"formaldehyde; paraffin; virus antigen; animal; animal disease; article; diarrhea; duodenum; enzyme immunoassay; female; fluorescent antibody technique; histology; ileum; immunohistochemistry; intestine mucosa; isolation and purification; jejunum; methodology; pathology; swine; swine disease; Transmissible gastroenteritis virus; virology; Animals; Antigens, Viral; Diarrhea; Duodenum; Female; Fluorescent Antibody Technique, Direct; Formaldehyde; Gastroenteritis, Transmissible, of Swine; Histological Techniques; Ileum; Immunoenzyme Techniques; Immunohistochemistry; Intestinal Mucosa; Jejunum; Paraffin; Swine; Transmissible gastroenteritis virus","Adegboye, D.S., Rasberry, U., Halbur, P.G., Monoclonal antibody-based immunohistochemical technique for the detection of Mycoplasma bovis in formalin-fixed, paraffin-embedded calf lung tissues (1995) J Vet Diagn Invest, 7, pp. 261-265; Chu, R.M., Li, N.J., Glock, R.D., Ross, R.F., Applications of peroxidase-antiperoxidase staining technique for detection of transmissible gastroenteritis virus in pigs (1982) Am J Vet Res, 43, pp. 77-81; Cubero, M.J., Bernard, S., Leon, L., Pathogenicity and antigen detection of the Nouzilly strain of transmissible gastroenteritis coronavirus, in 1-week-old piglets (1992) J Comp Pathol, 106, pp. 61-73; Frederick, G.T., Bohl, E.H., Cross, R.F., Pathogenicity of an attenuated strain of transmissible gastroenteritis virus for newborn pigs (1976) Am J Vet Res, 37, pp. 165-169; Haines, D.M., Kendall, J.C., Remenda, B.W., Monoclonal and polyclonal antibodies for immunohistochemical detection of bovine parainfluenza type 3 virus in frozen and formalin-fixed paraffin-embedded tissues (1992) J Vet Diagn Invest, 4, pp. 393-399; Huang, S.N., Minassian, H., More, J.D., Application of immunofluorescent staining on paraffin sections improved by trypsin digestion (1976) Lab Invest, 35, pp. 383-390; King, B.N., Contributions and needs of animal health and disease research (1981) Am J Vet Res, 42, pp. 1093-1108; Larochelle, R., Magar, R., The application of immunogold silver staining (IGSS) for the detection of transmissible gastroenteritis virus in fixed tissues (1993) J Vet Diagn Invest, 5, pp. 16-20; Laude, H., Chapsal, J.M., Gelfi, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J Gen Virol, 67, pp. 119-130; Magar, R., Larochelle, R., Robinson, Y., Dubuc, C., Immunochemical detection of porcine reproductive and respiratory syndrome virus using colloidal gold (1993) Can J Vet Res, 57, pp. 300-304; Moon, H.W., Norman, J.O., Lambert, G., Age dependent resistance to transmissible gastroenteritis of swine (TGE). 1. Clinical signs and some mucosal dimensions in small intestine (1973) Can J Comp Med, 37, pp. 157-166; Pensaert, M.B., Caillebaut, P., Vergote, J., Isolation of a new porcine respiratory, nonenteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Saif, L.J., Wesley, R., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , ed. Leman AD, Straw B, Glock RD, et al., 7th ed., Iowa State University Press, Ames, IA; Saunders, G.C., Development and evaluation of an enzyme labeled antibody test for the rapid detection of hog cholera antibodies (1977) Am J Vet Res, 38, pp. 21-25; Simkins, R.A., Saif, L.J., Weilnau, P.A., Epitope mapping and detection of transmissible gastroenteritis viral proteins in cell culture using biotinylated monoclonal antibodies in a fixed-cell ELISA (1989) Arch Virol, 107, pp. 179-190; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am J Vet Res, 53, pp. 1253-1258; Smith, G.H., Collins, J.K., Carman, J., Miocha, H.C., Detection of cytopathic and noncytopathic bovine viral diarrhea virus in cell culture with an immunoperoxidase test (1988) J Virol Methods, 19, pp. 319-324; Solorzano, R.F., Martin, M., Morehouse, L.G., The use of immunofluorescence techniques for the laboratory diagnosis of transmissible gastroenteritis of swine (1978) Can J Comp Med, 42, pp. 385-391; To, L.T., Bernard, S., Effect of fixation on the detection of transmissible gastroenteritis coronavirus antigens by the fixed-cell immunoperoxidase technique (1992) J Immunol Methods, 154, pp. 195-204; To, L.T., Bernard, S., Bottreau, E., Transmissible gastroenteritis coronavirus: Surface antigens induced by virulent and attenuated strains (1992) Res Virol, 143, pp. 241-248; Welch, S.K.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity against the attenuated and virulent virus strains (1988) Arch Virol, 102, pp. 221-236; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317","Shoup, D.I.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"8744736","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0030113485
"Yamaguchi N., Macdonald D.W., Passanisi W.C., Harbour D.A., Hopper C.D.","7402846932;7401463172;6508159980;7005502394;7006171924;","Parasite prevalence in free-ranging farm cats, Felis silvestris catus",1996,"Epidemiology and Infection","116","2",,"217","223",,64,"10.1017/S0950268800052468","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029912574&doi=10.1017%2fS0950268800052468&partnerID=40&md5=22daa353d8200d48f143f8d1ba116c60","Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Dept. of Clinical Veterinary Science, Div. of Molec. and Cellular Biology, University of Bristol, Langford, Bristol BS18 7DY, United Kingdom","Yamaguchi, N., Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Macdonald, D.W., Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Passanisi, W.C., Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Harbour, D.A., Dept. of Clinical Veterinary Science, Div. of Molec. and Cellular Biology, University of Bristol, Langford, Bristol BS18 7DY, United Kingdom; Hopper, C.D., Dept. of Clinical Veterinary Science, Div. of Molec. and Cellular Biology, University of Bristol, Langford, Bristol BS18 7DY, United Kingdom","No animals tested were positive for feline leukaemia virus antigen and Chlamydia psittaci antibodies, but all were positive for antibodies to feline calicivirus (FCV), feline herpesvirus 1 (FHV1) and rotavirus. They had antibodies to feline parvovirus (96%), feline coronavirus (84%) and cowpox virus (2%). Antibody to feline immunodeficiency virus (FIV) was found in 53% of animals, which were less likely to be infected with Haemobartonella felis, and had higher FHV antibody titres than cats without FIV. FCV was isolated from 51% cats and FHV1 and feline reovirus each from 4%. H. felis was present in 42% of animals, and antibody to Toxoplasma gondii in 62%. Clinical abnormality had a significant association with FIV and feline calicivirus infections, but sex, age, social status and feeding group had no significant association with prevalence of any parasites. Toxocara cati and Toxascaris leonina eggs were found, respectively, in 91% and 82% of animals tested.",,"bacterium antibody; virus antigen; Anaplasmataceae; antibody titer; article; Calicivirus; cat; Chlamydophila psittaci; Coronavirus; Cowpox virus; Feline immunodeficiency virus; Feline leukemia virus; Herpes simplex virus 1; nonhuman; parasite prevalence; Parvovirus; Reovirus; Rotavirus; Toxoplasma gondii","Dubey, J.P., Feline toxoplasmosis and coccidiosis: A survey of domiciled and stray cats (1973) J Am Vet Med Assoc, 162, pp. 873-877; Nichol, S., Ball, S.J., Snow, K.R., Prevalence of intestinal parasites in domestic cats from the London area (1981) Vet Rec, 109, pp. 252-253; Chandler, E.A., Gaskell, C.J., Gaskell, R.M., (1994) Feline Medicine and Therapeutics, 2nd Ed., , Oxford: Blackwell Scientific Publications; Parsons, J.C., Ascarid infections of cats and dogs (1987) Vet Clin North Am [Small Anim Pract], 17, pp. 1307-1339; Hosie, M.J., Robertson, C., Jarrett, O., Prevalence of feline leukaemia virus and antibodies to feline immunodeficiency virus in cats in the United Kingdom (1989) Vet Rec, 128, pp. 293-297; August, J.R., (1994) Consultations in Feline Internal Medicine, 2. , Philadelphia: W. B. Saunders; Roelke, M.E., Forrester, D.J., Jacobson, E.R., Seroprevalence of infectious disease agents in free-ranging Florida panthers (Felis concolor coryi) (1993) J Wildl Dis, 29, pp. 36-49; McOrist, S., Boid, R., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Some viral and protozoal diseases in the European wildcat (Felis silvestris) (1991) J Wildl Dis, 27, pp. 693-696; Artois, M., Remond, M., Viral diseases as a threat to free-living wild cats (Felis silvestris) in Continental Europe (1994) Vet Rec, 134, pp. 651-652; Mochizuki, M., Akuzawa, M., Nagatomo, H., Serological survey of the Iriomote cat (Felis iriomotensis) in Japan (1990) J Wildl Dis, 26, pp. 236-245; Shelton, G.H., Management of the feline immunodeficiency virus-positive patient (1994) Consultations in Feline Internal Medicine, 2, pp. 27-32. , August JR, ed. Philadelphia: W. B. Saunders; Pedersen, N.C., Ho, E.W., Brown, M.L., Yamamoto, J.K., Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome (1987) Science, 235, pp. 790-793; Gaskell, R.M., Dawson, S., Viral-induced upper respiratory tract disease (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 453-472. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Wardley, R.C., Gaskell, R.M., Povey, R.C., Feline respiratory viruses: Their prevalence in clinically healthy cats (1974) J Small Anim Pract, 15, pp. 579-586; Gaskell, R.M., Bennett, M., Feline poxvirus infection (1987) Virus Infections of Carnivores, pp. 267-286. , Appel M, ed. Amsterdam: Elsevier Science Publishers BV; Pedersen, N.C., Feline coronavirus infection (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 506-514. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Lappin, M.R., Diagnosis of toxoplasmosis (1994) Consultations in Feline Internal Medicine, 2, pp. 41-46. , August JR, ed. Philadelphia: W. B. Saunders; Wright, A.I., Endoparasites (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 595-610. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Webster, J.P., Prevalence and transmission of Toxoplasma gondii in wild brown rats, Rattus norvegicus (1994) Parasitology, 108, pp. 407-411; Gaskell, R.M., Bennett, M., Other feline virus infections (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 535-543. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Gaskell, R.M., Feline panleucopenia (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 445-452. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Macdonald, D.W., Apps, P.J., Carr, G.M., Kerby, G., Social dynamics, nursing coalitions and infanticide among farm cats, Felis catus (1987) Adv Ethology, 28, pp. 1-64; Kerby, G., Macdonald, D.W., Cat society and the consequences of colony size (1988) The Domestic Cat: The Biology of Its Behaviour, pp. 67-82. , Turner DC, Bateson P, eds. Cambridge: Cambridge University Press; Liberg, O., Sandell, M., Spatial organisation and reproductive tactics in the domestic cat and other felids (1988) The Domestic Cat: The Biology of Its Behaviour, pp. 83-98. , Turner DC, Bateson P, eds. Cambridge: Cambridge University Press; Caro, T.M., Holt, M.E., Fitzgibbon, C.D., Bush, M., Hawkey, C.M., Kock, R.A., Health of adult free-living cheetahs (1987) J Zool Lond, 212, pp. 573-584; Wills, J.M., (1986) Chlamydial Infection in the Cat, p. 250. , [Ph.D. thesis]. Bristol: University of Bristol; Muir, P., Harbour, D.A., Gruffydd-Jones, T.J., A clinical and microbiological study of cats with protruding nictitating membranes and diarrhoea: Isolation of a novel virus (1990) Vet Rec, 127, pp. 324-330; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Gaskell, C.J., Virus shedding and immune responses in cats inoculated with cell culture-adapted feline infectious peritonitis virus (1988) Vet Microbiol, 16, pp. 145-148; O'Dair, H.A., Hopper, C.D., Gruffydd-Jones, T.J., Harbour, D.A., Waters, L.A., Clinical aspects of Chlamydia psittaci infection in cats infected with feline immunodeficiency virus (1994) Vet Rec, 134, pp. 365-368; Gaskeli, R.M., Gaskell, C.J., Evans, R.J., Natural and experimental poxvirus infection in the domestic cat (1983) Vet Rec, 112, pp. 164-170; Scott, F.W., Evaluation of a feline viral rhinotracheitis-feline calicivirus disease vaccine (1977) Am J Vet Res, 38, pp. 229-234; Harbour, D.A., Howard, P.E., Gaskell, R.M., Isolation of feline calicivirus and feline herpesvirus from domestic cats 1980 to 1989 (1991) Vet Rec, 128, pp. 77-80; Courchamp, F., Pontier, D., Feline immunodeficiency-virus: An epidemiological review (1994) C R Acad Sci Paris, 317, pp. 1123-1134; Bennett, M., McCracken, H., Lutz, H., Prevalence of antibody to feline immunodeficiency virus in some cat population (1989) Vet Rec, 124, pp. 397-398; Bennett, M., Lloyd, G., Jones, N., Prevalence of antibody to hantavirus in some cat populations in Britain (1990) Vet Rec, 127, pp. 548-549; Van Rensburg, P.J.J., Skinner, J.D., Van Aarde, R.J., Effects of feline panleucopaenia on the population characteristics of feral cats on Marion Island (1987) J Appl Ecol, 24, pp. 63-73; Wills, J.M., Gaskell, R.M., Feline chlamydial infection (feline pneumonitis) (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 544-551. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Jarrett, O., Feline leukaemia virus (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 473-487. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Scott, F.W., Kahn, D.E., Gillespie, J.H., Feline viruses; isolation, characterisation and pathogenicity of a feline reovirus (1970) Am J Vet Res, 31, pp. 11-20; Snodgrass, D.R., Angus, K.W., Gray, E.W., A rotavirus from kittens (1979) Vet Rec, 104, pp. 222-223; Stoddart, M.E., Bennett, M., Feline coronavirus infection (1994) Feline Medicine and Therapeutics 2nd Ed., pp. 506-514. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am J Vet Res, 37, pp. 1449-1453; Nichol, S., Ball, S.J., Snow, K.R., Prevalence of intestinal parasites in domestic cats from the London area (1981) Vet Rec, 109, pp. 252-253; Kerby, G., (1987) The Social Organisation of Farm Cats (Felis catus L.) [D.Phil. Thesis], , Oxford: University of Oxford; Hopper, C.D., Sparkes, A.H., Harbour, D.A., Feline immunodeficiency virus (1994) Feline Medicine and Therapeutics, 2nd Ed., pp. 488-505. , Chandler EA, Gaskell CJ, Gaskell RM, eds. Oxford: Blackwell Scientific Publications; Grossman, C.J., Interactions between the gonadal steroids and the immune system (1985) Science, 227, pp. 257-261; Alexander, J., Stimson, W.H., Sex hormones and the course of parasitic infection (1988) Parasitol Today, 4, pp. 189-193; Morell, V., Serengeti's big cats are going to the dogs (1994) Science, 264, p. 1664; Heeney, J.L., Evermann, J.F., McKeirnan, A.J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) J Virol, 64, pp. 1964-1972; French, D.D., Corbett, L.K., Easterbee, N., Morphological discriminants of Scottish wildcats (Felis silvestris), domestic cats (F. catus) and their hybrids (1988) J Zool Lond, 214, pp. 235-259","Macdonald, D.W.; Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom",,"Cambridge University Press",09502688,,EPINE,"8620914","English","EPIDEMIOL. INFECT.",Article,"Final",,Scopus,2-s2.0-0029912574
"Williams E.S., Thorne E.T.","35553183900;7006857611;","Infectious and parasitic diseases of captive carnivores, with special emphasis on the black-footed ferret (Mustela nigripes)",1996,"OIE Revue Scientifique et Technique","15","1",,"91","114",,21,"10.20506/rst.15.1.915","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0040159511&doi=10.20506%2frst.15.1.915&partnerID=40&md5=4958afc225aa9131cb2903521f04cf81","Department of Veterinary Sciences, University of Wyoming, Laramie, WY 82070, United States; Wyoming Game and Fish Department, Box 3312, University Station, Laramie, WY 82071, United States","Williams, E.S., Department of Veterinary Sciences, University of Wyoming, Laramie, WY 82070, United States; Thorne, E.T., Wyoming Game and Fish Department, Box 3312, University Station, Laramie, WY 82071, United States","Captive carnivores are susceptible to a wide array of infectious and parasitic diseases, which reflects the diversity of the seven families of Carnivora. Unfortunately, relatively few in-depth studies have been conducted on diseases of non-domestic carnivores, and much remains to be learned, especially regarding diseases of small carnivores (e.g. mustelids, viverrids and procyonids). The more important infectious diseases of carnivores include rabies, canine distemper, and diseases caused by parvoviruses, coronaviruses and herpesviruses. Few parasitic or bacterial pathogens are significant in captive populations, and appropriate husbandry, therapy, vaccines and quarantine minimize the risk of disease. Extrapolations from one species to another regarding disease susceptibility may be incorrect. The black-footed ferret (Mustela nigripes) serves as an example of a carnivore significantly affected by infectious diseases, some of which were expected while others could not have been predicted from generalized knowledge of diseases of mustelids. This highlights the need to understand the natural history of each species maintained in captivity.","Black-footed ferret; Canidae; Carnivora; Felidae; Hyaenidae; Infectious diseases; Mustela nigripes; Mustelidae; Procyonidae; Ursidae; Viverridae","Bacteria (microorganisms); Canidae; Canis familiaris; Carnivora; Felidae; Hyaenidae; Mustela nigripes; Mustela putorius furo; Mustelidae; Parvovirus; Procyonidae; Ursidae; Viverridae; animal; animal disease; animal parasitosis; bacterial infection; Carnivora; ferret; human; parasitosis; review; virus infection; zoo animal; zoonosis; Animals; Animals, Zoo; Bacterial Infections; Carnivora; Ferrets; Humans; Parasitic Diseases; Parasitic Diseases, Animal; Virus Diseases; Zoonoses","Addison, E.M., Barker, I.K., Hunter, D.B., Diseases and parasites of furbearers (1987) Wild Furbearer Management and Conservation in North America, pp. 894-908. , M. Novak, J.A. Baker, M.E. Obbard & B. Malloch, eds. 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Elsevier Science Publishers, New York; Appel, M.J.G., Yates, R.A., Foley, G.L., Bernstein, J.J., Santinelli, S., Spelman, L.H., Miller, L.D., Summers, B.A., Canine distemper epizootic in lions, tigers, and leopards in North America (1994) J. Vet. Diagn. Invest., 6, pp. 277-288; Barker, I.K., Povey, R.C., Voigt, D.R., Response of mink, skunk, red fox and raccoon to inoculation with mink virus enteritis, feline panleukopenia and canine parvovirus and prevalence of antibody to parvovirus in wild carnivores in ontario (1983) Can. J. Comp. Med., 47, pp. 188-197; Barnes, A.M., Surveillance and control of bubonic plague in the United States (1982) Symp. Zool. Soc., Lond., 50, pp. 237-270; Barr, M.C., Calle, P.P., Roelke, M.E., Scott, F.W., Feline immunodeficiency virus infection in nondomestic felids (1989) J. Zoo Wildl. Med., 20, pp. 265-272; Berry, H.H., Surveillance and control of anthrax and rabies in wild herbivores and carnivores in Namibia (1993) Rev. Sci. Tech. Off. Int. 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Dis., 27, pp. 441-445; Williams, E.S., Thorne, E.T., Kwiatkowski, D.R., Oakleaf, B., Overcoming disease problems in the black-footed ferret recovery program (1992) Trans. North Am. Wildl. Nat. Res. Conf., 57, pp. 474-485; Williams, E.S., Mills, K., Kwiatkowski, D.R., Thorne, E.T., Boerger-Fields, A., Plague in a black-footed ferret (Mustela nigripes) (1994) J. Wildl. Dis., 30, pp. 581-585; Williams, E.S., Anderson, S.E., Cavender, J., Lynn, C., List, K., Hearne, C., Appel, M.J.G., Vaccination of black-footed ferret (Mustela nigripes) x siberian polecat (M. Eversmanni) hybrids and domestic ferrets (M. Putorius furo) against canine distemper (1996) J. Wildl. Dis., 32. , in press; Willoughby, K., Kelly, D.F., Lyon, D.G., Wells, G.A.H., Spongiform encephalopathy in a captive puma (Felis concolor) (1992) Vet. Rec., 131, pp. 431-434; Wilson, J.F., Rausch, R.E., Alveolar hydatid disease. A review of clinical features of 33 indigenous cases of Echinococcus multilocularis infection in alaskan eskimos (1980) Am. J. Trop. Med. Hyg., 29, pp. 1340-1355; Witter, J.F., Brucellosis (1981) Infectious Diseases of Wild Mammals, 2nd Ed., pp. 280-287. , (J.W. Davis, L.H. Karstad & D.O. Trainer, eds). Iowa State University Press, Ames, Iowa; Wolff, P.L., Parasites of new world primates (1993) Zoo and Wild Animal Medicine. Current Therapy, 3, pp. 378-389. , (M.E. Fowler, ed.). W.B. Saunders Company, Philadelphia, Pennsylvania; Wood, S.L., Thomson, G.W., Haines, D.M., Canine distemper-like infection in a captive lioness (1995) Can. Vet. J., 36, pp. 34-35; Worley, M., Feline coronavirus (1987) Virus Infections of Carnivores, pp. 431-436. , (M.J. Appel, ed.). Elsevier Science Publishers, New York; Zimmerman, W.J., Trichinosis (1971) Parasitic Diseases of Wild Mammals, pp. 127-139. , (J.W. Davis & R.C. Anderson, eds). Iowa State University Press, Ames, Iowa","Williams, E.S.; Department of Veterinary Sciences, University of Wyoming, Laramie, WY 82070, United States",,"Office International des Epizootes",02531933,,,"8924718","English","OIE Rev. Sci. Tech.",Article,"Final",,Scopus,2-s2.0-0040159511
"Muir P., Nicholson F., Illavia S.J., McNeil T.S., Ajetunmobi J.F., Dunn H., Starkey W.G., Reetoo K.N., Cary N.R.B., Parameshwar J., Banatvala J.E.","57211544210;7006599356;6602543532;16943587800;6506114563;57192734026;7004933142;8523955400;7003592820;7004288524;35601723700;","Serological and molecular evidence of enterovirus infection in patients with end-stage dilated cardiomyopathy",1996,"Heart","76","3",,"243","249",,38,"10.1136/hrt.76.3.243","https://www.scopus.com/inward/record.uri?eid=2-s2.0-9544221632&doi=10.1136%2fhrt.76.3.243&partnerID=40&md5=8d53bf272d500ab67fe2021a87e12c81","Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Department of Histopathology, Papworth Hospital, Papworth Everard, Cambridge, United Kingdom; Transplant Unit, Papworth Hospital, Papworth Everard, Cambridge, United Kingdom; Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, Lambeth Palace Road, London SE1 7EH, United Kingdom","Muir, P., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom, Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, Lambeth Palace Road, London SE1 7EH, United Kingdom; Nicholson, F., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Illavia, S.J., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; McNeil, T.S., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Ajetunmobi, J.F., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Dunn, H., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Starkey, W.G., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Reetoo, K.N., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom; Cary, N.R.B., Department of Histopathology, Papworth Hospital, Papworth Everard, Cambridge, United Kingdom; Parameshwar, J., Transplant Unit, Papworth Hospital, Papworth Everard, Cambridge, United Kingdom; Banatvala, J.E., Department of Virology, U. Med. and Dental Schools of Guy's, St. Thomas' Hospitals, London, United Kingdom","Objective - To study the relative diagnostic value of enterovirus-specific molecular biological and serological assays in patients with end-stage dilated cardiomyopathy, and to investigate the possible role of other cardiotropic viruses in dilated cardiomyopathy. Design - Analysis of recipient myocardial tissue and serum from patients with dilated cardiomyopathy and controls undergoing cardiac transplantation for end-stage cardiac disease. Setting - University virology department and transplantation unit. Methods - Reverse transcriptase-polymerase chain reaction and nucleotide sequence analysis of myocardial RNA and DNA; enterovirus-specific in situ hybridisation; enterovirus-specific immunoglobulin M detection. Results - Enterovirus RNA was detected in myocardial tissue from only a small proportion of (five of 75) hearts. However, although enterovirus-specific immunoglobulin M responses were detected in 22 (28%) of 39 controls patients, a significantly higher prevalence was observed among patients with dilated cardiomyopathy (22 (56%) of 39 patients; P < 0.005). All enteroviruses detected in myocardium showed greatest nucleotide sequence homology with coxsackievirus type B3. Detection of enterovirus RNA in myocardium by the polymerase chain reaction and by in situ hybridisation gave comparable results. Other potentially cardiotropic virus genomes, including human cytomegalovirus, influenzaviruses, and coronaviruses were not detected in myocardium. Conclusion - This study found that enterovirus-specific immunoglobulin M responses provided the strongest evidence of enterovirus involvement in patients with end-stage dilated cardiomyopathy. However, the high background prevalence of these responses limits their diagnostic value. The finding that enteroviruses detected in myocardium were coxsackievirus type B3 accords with recent findings in patients with acute myocarditis, and indicates that this serotype is the major cardiotropic human enterovirus.","Cardiomyopathy; Enterovirus RNA detection; Enterovirus-specific immunoglublin M responses","immunoglobulin M; virus RNA; article; cardiomyopathy; controlled study; diagnostic value; Enterovirus; human; major clinical study; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; virus detection","Grist, N.R., Reid, D., Epidemiology of viral infections of the heart (1993) Viral Infections of the Heart, pp. 23-31. , Banatvala JE, ed. London: Edward Arnold; Cambridge, G., MacArthur, C.G.C., Waterson, A.P., Goodwin, J.F., Oakley, C.M., Antibodies to coxsackie B viruses in primary congestive cardiomyopathy (1979) Br Heart J, 41, pp. 692-696; Muir, P., Nicholson, F., Tilzey, A.J., Signy, M., English, T.A.H., Banatvala, J.E., Chronic relapsing pericarditis and dilated cardiomyopathy: Serological evidence of persistent enterovirus infection (1989) Lancet, 1, pp. 804-807; Keeling, P.J., Lukaszyk, A., Poloniecki, J., Caforio, A.L., Davies, M.J., Booth, J.C., A prospective case-control study of antibodies to coxsackie B virus in idiopathic dilated cardiomyopathy (1994) J Am Coll Cardiol, 23, pp. 593-598; Archard, L.C., Freeke, C., Richardson, P., Meany, B., Olsen, E., Morgan-Capner, P., Persistence of enterovirus RNA in dilated cardiomyopathy: A progression from dilated cardiomyopathy (1988) New Concepts in Viral Heart Disease, pp. 349-362. , Schultheiss H-P, ed. Berlin: Springer-Verlag; Bewles, N.E., Rose, M.L., Taylor, P., Banner, N.R., Morgan-Capner, P., Cunningham, L., End-stage dilated cardiomyopathy. Persistence of enterovirus RNA in myocardium at cardiac transplantation and lack of immune response (1989) Circulation, 80, pp. 1128-1136; Kandolf, R., Canu, A., Klingel, K., Kirschner, P., Schönke, H., Mertsching, R., Molecular studies on enteroviral heart disease (1990) New Aspects of Positive-strand RNA Viruses, pp. 340-348. , Brinton MA, Heinz FX, eds. Washington DC: American Society of Microbiology; Schwaiger, A., Umlauft, F., Weyrer, K., Larcher, C., Lyons, J., Mühlberger, V., Detection of enterovirus ribonucleic acid in myocardial biopsies from patients with idiopathic dilated cardiomyopathy by polymerase chain reaction (1993) Am Heart J, 126, pp. 406-410; Kämmerer, U., Kunkel, B., Korn, K., Nested polymerase chain reaction for specific detection and rapid identification of human picornaviruses (1994) J Clin Microbiol, 32, pp. 285-291; Khan, M., Why, H., Richardson, P., Archard, L.C., Nucleotide sequencing of polymerase chain reaction products shows the presence of Coxsackie-B3 virus in endomyocardial biopsies from patients with myocarditis or dilated cardiomyopathy (1994) Biochem Soc Trans, 22, pp. 176S; Muir, P., Enteroviruses and heart disease (1993) Br J Biomed Sci, 50, pp. 258-271; Schönian, U., Crombach, M., Maisch, B., Does CMV infection play a role in myocarditis? New aspects from in-situ hybridisation (1991) Eur Heart J, 12 (SUPPL. D), pp. 65-68; Landsdown, A.B.G., Viral infections and diseases of the heart (1978) Prog Med Viral, 24, pp. 70-113; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J Med Virol, 6, pp. 259-265; Alexander, L.K., Small, J.D., Edwards, S., Baric, R.S., An experimental model for dilated cardiomyopathy after rabbit coronavirus infection (1992) J Infect Dis, 166, pp. 978-985; Task force on the definition and classification of cardiomyopathies (1980) Br Heart J, 44, pp. 672-673; Muir, P., Nicholson, F., Jhetam, M., Neogi, S., Banatvala, J.E., Rapid diagnosis of enterovirus infection by magnetic bead extraction and polymerase chain reaction detection of enterovirus RNA in clinical specimens (1993) J Clin Microbiol, 31, pp. 31-38; Nicholson, F., Meetoo, G., Aiyar, S., Banatvala, J.E., Muir, P., Detection of enterovirus RNA in clinical samples by nested polymerase chain reaction for rapid diagnosis of enterovirus infection (1994) J Virol Mcth, 48, pp. 155-166; Nicholson, F., Illavia, S.J., Ajetunmobi, J.F., Shackleton, E.A., Li, M., Starkey, W.G., Molecular detection and serotypic analysis of enterovirus RNA in myocardium of patients with acute myocarditis (1995) Br Heart J, 74, pp. 522-527; Darlington, J., Super, M., Patel, K., Grundy, J.E., Griffiths, P.D., Emery, V.C., Use of the polymerase chain reaction to analyse sequence variation within a major neutralizing epitope of glycoprotein B (gp58) in clinical isolates of human cytomegalovirus (1991) J Gen Virol, 72, pp. 1985-1989; Landis, J.R., Koch, G.C., The measurement of observer agreement for categorical data (1977) Biometrics, 33, pp. 159-174; Muir, P., Nicholson, F., Banatvala, J.E., Bingley, P.J., Coxsackie B virus and postviral fatigue syndrome (1991) Br Med J, 302, pp. 658-659; Liljeqvist, J.-Å., Bergström, T., Holmström, S., Samuelson, A., Yousef, G.E., Waagstein, F., Failure to demonstrate enterovirus aetiology in Swedish patients with dilated cardiomyopathy (1993) J Med Virol, 39, pp. 6-10; Sliika, M.S., Matloubian, M., Ahmed, R., Bone marrow is a major site of long-term antibody production after acute viral infection (1995) J Virol, 69, pp. 1895-1902; Why, H.J., Meany, B.T., Richardson, P.J., Olsen, E.G., Bowles, N.E., Cunningham, L., Clinical and prognostic significance of detection of enteroviral RNA in the myocardium of patients with myocarditis with myocarditis or dilated cardiomyopathy (1994) Circulation, 89, pp. 2582-2589; Figulla, H.R., Stille-Siegener, M., Mall, G., Heim, A., Kreuzer, H., Myocardial enterovirus infection with left ventricular dysfunction: A benign disease compared with idiopathic dilated cardiomyopathy (1995) J Am Coll Cardiol, 25, pp. 1170-1175; Zhang, H.Y., Yousef, G.E., Cunningham, L., Blake, N.W., Ouyang, X., Bayston, T.A., Attenuation of a reactivated cardiovirulent coxsackievirus B3: The 5′-nontranslated region does not contain major attenuation determinants (1993) J Med Virol, 41, pp. 129-137; Tu, Z., Chapman, N.M., Hufnagel, G., Tracy, S., Romero, J.R., Barry, W.H., The cardiovirulent phenotype of coxsackievirus B3 is determined at a single site in the genomic 5′ nontranslated region (1995) J Virol, 69, pp. 4607-4618; Martin, A.B., Webber, S., Fricker, F.J., Jaffe, R., Demmler, G., Kearney, D., Acute myocarditis. Rapid diagnosis by polymerase chain reaction in children (1994) Circulation, 90, pp. 330-339; Rotbart, H.A., Sawyer, M.H., Fast, S., Lewinski, C., Murphy, N., Keyser, E.F., Diagnosis of enteroviral meningitis by using polymerase chain reaction with a colorimetric microwell detection assay (1994) J Clin Microbiol, 32, pp. 2590-2592","Muir, P.; Department of Virology, United Medical/Dental Schools, Guy's and St Thomas' Hospitals, Lambeth Palace Road, London SE1 7EH, United Kingdom",,"BMJ Publishing Group",13556037,,HEARF,"8868984","English","HEART",Article,"Final",Open Access,Scopus,2-s2.0-9544221632
"Adzhar A., Shaw K., Britton P., Cavanagh D.","6508344752;7202206256;57203302770;26642890500;","Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction",1996,"Avian Pathology","25","4",,"817","836",,57,"10.1080/03079459608419184","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030469893&doi=10.1080%2f03079459608419184&partnerID=40&md5=68a14b46d59949e141681b4cb541a889","Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berks RG20 7NN, United Kingdom; Veterinary Research Institute, PO Box 369, 30740 Ipoh, Malaysia","Adzhar, A., Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berks RG20 7NN, United Kingdom, Veterinary Research Institute, PO Box 369, 30740 Ipoh, Malaysia; Shaw, K., Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berks RG20 7NN, United Kingdom; Britton, P., Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berks RG20 7NN, United Kingdom; Cavanagh, D., Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berks RG20 7NN, United Kingdom","The universality of seven pairs of oligonucleotides for detection of the coronavirus infectious bronchitis virus (IBV) by reverse-transcription polymerase chain reaction (RT-PCR) was examined using 41 isolates of IBV collected over five decades from Europe, Japan and the USA. Oligonucleotides specific for sequences within the S2 region of the spike (S) gene (Lin et al., 1991a) and nucleocapsid (N) gene (Zwaagstra et al., 1992) gave the appropriate products with all 41 isolates. Oligonucleotide pair UTR1-/UTR2+, corresponding to sequences within the 3' untranslated region (UTR) of the genome, also gave the predicted product with all the isolates. Oligonucleotide pair UTR3-/UTR4+ was internal to oligonucleotides UTR1- /UTR2+ and was used in a nested-set arrangement for greater specificity and sensitivity, giving the correct product with the 39 isolates examined. Oligonucleotide pair S1Uni1-/S1Uni2+ was used to produce a 1.6 kb cDNA, corresponding to most of the S1 region of the S gene, with 24/24 isolates tested. This oligonucleotide pair was less suited than the others for routine detection of IBV but is recommended for the amplification of the S1 region of the S gene of new isolates for subsequent analysis. Other oligonucleotide pairs, yielding cDNA corresponding to the variable region of the IBV genome where genes 3 and 4 (M) overlap, were selected to be largely specific for Massachusetts serotype isolates, in the context of European strains. RT-PCR analysis using these oligonucleotide pairs showed that a number of field isolate preparations also contained a small amount of Massachusetts serotype virus, probably of vaccine origin and indicative of low level persistent infection. These results suggest that any strain of IBM is likely to be detectable by RT-PCR with at least one of our primer pairs.",,"Aves; Avian infectious bronchitis virus; Coronavirus","Adzhar, A.B., Shaw, J.K.A., Britton, P., Cavanagh, D., Avian infectious bronchitis virus differences between 793/B and other strains (1995) Veterinary Record, 136, p. 548; Alexander, D.J., Gough, R.E., Isolation of avian infectious bronchitis virus from experimentally infected chickens (1977) Research in Veterinary Science, 23, pp. 344-347; Alexander, D.J., Gough, R.E., A long-term study of the pathogenesis of infection of fowls with three strains of avian infectious bronchitis virus (1978) Research in Veterinary Science, 24, pp. 228-233; Andreason, J.R., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Diseases, 35, pp. 216-220; Binns, M.M., Boursnell, M.E.G., Tomley, F.M., Brown, T.D.K., Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) Journal of General Virology, 67, pp. 2825-2831; Boursnell, M.E.G., Brown, T.D.K., Binns, M.M., Sequence of the membrane protein gene from avian coronavirus IBV (1984) Virus Research, 1, pp. 303-313; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) Journal of General Virology, 66, pp. 573-580; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Cavanagh, D., Advances in avian diagnostic technology (1993) Proceedings of the Xth World Veterinary Poultry Association Congress, Sydney, 1993, pp. 57-70; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-114. , S. G. SIDDELL (Ed.) New York, Plenum Press; Cavanagh, D., Davis, P.J., Evolution of coronavirus IBV, sequence of the matrix glycoprotein gene and intergenic region of several serotypes (1988) Journal of General Virology, 69, pp. 621-629; Cavanagh, D., Davis, P.J., Sequence analysis of strains of avian infectious bronchitis coronavirus isolated during the 1960s in the U.K (1992) Archives of Virology, 130, pp. 471-476; Cavanagh, D., Davis, P.J., Mockett, A.P.A., Amino acids within hypervariable region I of avian coronavirus IBV (Massachusetts serotype) spike glycoprotein are associated with neutralization epitopes (1988) Virus Research, 11, pp. 141-150; Cavanagh, D., Davis, P.J., Cook, J.K.A., Infectious bronchitis virus evidence for recombination within the Massachusetts serotype (1992) Avian Pathology, 21, pp. 401-408; Cavanagh, D., Davis, P.J., Cook, J.K.A., Li, D., Kant, A., Koch, G., Location of the amino acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious bronchitis virus (1992) Avian Pathology, 21, pp. 33-43; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analytical Biochemistry, 162, pp. 156-159; Cook, J.K.A., Duration of experimental infectious bronchitis in chickens (1968) Research in Veterinary Science, 9, pp. 506-514; Cook, J.K.A., The classification of new serotypes of infectious bronchitis virus isolated from poultry flocks in Britain between 1981 and 1983 (1984) Avian Pathology, 13, pp. 733-741; Cook, J.K.A., Huggins, M.B., Newly isolated serotypes of infectious bronchitis virus: Their role in disease (1986) Avian Pathology, 15, pp. 129-138; Cumming, R.B., The aetiology of 'uraemia' of chickens (1962) Australian Veterinary Journal, 38, p. 554; Darbyshire, J.K., Rowell, J.G., Cook, J.K.A., Peters, R.W., Taxonomic studies on strains of avian infectious bronchitis virus using neutralization tests in tracheal organ cultures (1979) Archives of Virology, 61, pp. 227-238; Davelaar, F.G., Kouwenhoven, B., Burger, A.G., Occurrence and significance of infectious bronchitis virus variant strains in egg and broiler production in the Netherlands (1984) Veterinary Quarterly, 6, pp. 114-120; Dawson, P.S., Gough, R.E., Antigenic variation in strains of avian infectious bronchitis virus (1971) Archives fur Die Gesampte Virusforschung, 34, pp. 32-39; Gough, R.E., Randall, C.J., Dagless, M., Alexander, D.J., Cox, W.J., Pearson, D., A 'new' strain of infectious bronchitis virus infecting domestic fowl in Great Britain (1992) Veterinary Record, 130, pp. 493-494; Hopkins, S.R., Serological comparisons of strains of infectious bronchitis virus using plaque-purified isolants (1974) Avian Diseases, 18, pp. 231-239; Jackwood, M.W., Kwon, H.M., Hilt, D.A., Infectious bronchitis virus detection in allantoic fluid using the polymerase chain reaction and a DNA probe (1992) Avian Diseases, 36, pp. 403-409; Jones, R.C., Ambali, A.G., Re-excretion of an enterotropic infectious bronchitis virus by hens at point of lay after experimental infection at day old (1987) Veterinary Record, 120, pp. 617-618; Kusters, J.G., Niesters, G.M., Bleumink-Pluym, N.M.C., Davelaar, F.G., Horzinek, M.C., Van Der Zeijst, B.A.M., Molecular epidemiology of infectious bronchitis virus in the Netherlands (1987) Journal of General Virology, 68, pp. 343-352; Kwon, H.M., Jackwood, M.W., Brown, T.P., Hilt, D.A., Polymerase chain reaction and a biotin-labeled DNA probe for detection of infectious bronchitis virus in chickens (1993) Avian Diseases, 37, pp. 149-156; Kwon, H.M., Jackwood, M.W., Gelb, J., Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Diseases, 37, pp. 194-202; Lin, Z., Kato, A., Kudou, Y., Ueda, S., A new typing method for the avian infectious bronchitis virus using polymerase chain reaction and restriction enzyme fragment polymorphism (1991) Archives of Virology, 116, pp. 19-31; Lin, Z., Kato, A., Kudou, Y., Umeda, K., Ueda, S., Typing of recent infectious bronchitis virus isolates causing nephritis in chicken (1991) Archives of Virology, 120, pp. 145-149; Parsons, D., Ellis, M.M., Cavanagh, D., Cook, J.K.A., Characterisation of an infectious bronchitis virus isolated from vaccinated broiler breeder flocks (1992) Veterinary Record, 131, pp. 408-411; Piatti, P., Hassard, S., Newman, J.F.E., Brown, F., Antigenic variants in a plaque-isolate of foot-and-mouth disease virus: Implications for vaccine production (1995) Vaccine, 13, pp. 781-784; Picault, J.P., Drouln, P., Guittet, M., Bennejean, G., Protais, J., L'Hospitaler, R., Gillet, J.P., Le Bacheler, A., Isolation, characterisation and preliminary cross-protection studies with a new pathogenic avian infectious bronchitis virus (strain PL-84084) (1986) Avian Pathology, 15, pp. 367-383; Williams, A.K., Wang, L., Sneed, L.W., Colusson, E.W., Analysis of a hypervariable region in the 3′ non-coding end of the infectious bronchitis virus genome (1993) Virus Research, 28, pp. 19-27; Zwaagstra, K.A., Van Der Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1992) Journal of Clinical Microbiology, 30, pp. 79-84","Cavanagh, D.; Division of Molecular Biology, Compton Laboratory, Institute for Animal Health, Compton, Newbury, Berks RG20 7NN, United Kingdom",,"Taylor and Francis Ltd.",03079457,,AVPAD,,"English","AVIAN PATHOL.",Article,"Final",,Scopus,2-s2.0-0030469893
"Middleton P.J.","7101676460;","Viruses that multiply in the gut and cause endemic and epidemic gastroenteritis",1996,"Clinical and Diagnostic Virology","6","2-3",,"93","101",,12,"10.1016/0928-0197(96)00231-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030220218&doi=10.1016%2f0928-0197%2896%2900231-0&partnerID=40&md5=037cf6ff362ed53c84e3334202821d01","Provincial Laboratory, B.C. Centre for Disease Control, 828 West 10th Avenue, Vancouver, BC V5Z 1L8, Canada","Middleton, P.J., Provincial Laboratory, B.C. Centre for Disease Control, 828 West 10th Avenue, Vancouver, BC V5Z 1L8, Canada","Background: Acute infectious diarrhea in young children is a leading cause of morbidity and mortality in developing countries. Even in developed countries, infectious enteritis is second only to respiratory infections as a cause of morbidity in early childhood. Objective: To nominate the various viral agents that cause enteritis, discuss the pathogenesis, clinical features, epidemiology and diagnostic procedures employed. Study design: Pertinent literature was reviewed and the findings of investigations carried out on viral enteritis by various colleagues recalled. Results: The viruses causing gastroenteritis include: Rotaviruses; Adenoviruses-especially Ad 31, Ad 40 and Ad 41; members of the Caliciviridae, e.g. Norwalk virus, Hawaii virus, Snow Mountain virus, Taunton virus, Southampton virus, Toronto virus (formerly mini-reovirus) and others; Astrovirus; Coronavirus; Torovirus; Cytomegalovirus (CMV) and possibly Picobirnavirus. Enteritis-producing viruses replicate in columar epithelial cells in the distal parts of villi of the small intestine. Two mechanisms are addressed to explain why diarrhea occurs. Clinically the main expression of illness is a watery diarrhea that lasts 24 h to about 7 days. Vomiting is of shorter duration and may not always accompany the diarrhea. Fever is generally ≤38.5°C. Virus is shed in the stool for about 3-7 days. Diagnostic procedures employ electron microscopy (EM), immune electron microscopy (IEM), enzyme-linked immunosorbent assay (ELISA), time-resolved fluoroimmunoassay (TR-FIA), latex agglutination, polyacrylamide gel electrophoresis (PAGE) and the polymerase chain reaction (PCR). Conclusion: In developed countries viral enteritis among young children may be up to three times more common than bacterial gut disease. With the exception of CMV enteric involvement, the stool is characteristically not bloody and white blood cells are not found. Patient management may involve the employment of IV replacement therapy to counter dehydration and electrolyte imbalance. Milder cases may be managed with oral rehydration.","Diagnostic procedures; Enteritis-producing viruses; Gastroenteritis; Pathogenesis of viral enteritis; Viral epidemiology","acute diarrhea; acute gastroenteritis; Adenovirus; article; Astrovirus; Calicivirus; child; clinical feature; Coronavirus; Cytomegalovirus; developing country; endemic disease; enzyme linked immunosorbent assay; epidemic; female; fluid therapy; human; human tissue; immunoelectron microscopy; major clinical study; male; Picornavirus; polymerase chain reaction; priority journal; Reovirus; Rotavirus; Torovirus; virus infection; virus replication","Alford, C.A., Britt, W.J., Cytomegalovirus (1990) Fields Virology, 2, pp. 1981-2010. , 2nd edn., Raven Press, New York; Bachmann, P.A., Hess, R.G., Comparative aspects of pathogenesis and immunity in animals (1982) Virus Infections of the Gastrointestinal Tract, pp. 361-397. , D.A.J. Tyrrell and A.Z. Kapikian (Eds.), Marcel Dekker, New York; Barnes, G.L., Doyle, L.W., Hewson, P.H., A randomized trial of oral gamma globulin in low-birthweight infants infected with rotavirus (1982) Lancet, 1, pp. 1371-1373; Bishop, R.F., Davidson, G.P., Holmes, I.H., Ruck, B.J., Virus particles in epithelial cells of duodenal mucosa from children with acute non-bacterial gastroenteritis (1973) Lancet, 2, pp. 147-151; Bishop, R.F., Other small virus-like particles in humans (1982) Virus Infections of the Gastrointestinal Tract, pp. 195-207. , D.A.J. Tyrrell and A.Z. Kapikian (Eds.), Marcel Dekker, New York; Black, R.F., Greenburg, H.B., Kapikian, A.Z., Acquisition of serum antibody to Norwalk virus and rotavirus and relation to diarrhea in a longitudinal study of young children in rural Bangladesh (1982) J. Infect. Dis., 145, pp. 483-489; Brandt, C.D., Kim, H.W., Rodriguez, W.J., Pediatric viral gastroenteritis during eight years of study (1983) J. Clin. Microbiol., 18, pp. 71-78; Caul, E.O., Egglestone, S.I., Coronaviruses in humans (1982) Virus Infections of the Gastrointestinal Tract, pp. 179-193. , D.A.J. Tyrrell and A.Z. Kapikian (Eds.), Marcel Dekker, New York; Doane, F.W., Anderson, N., Birnaviridae (1987) Electron Microscopy in Diagnostic Virology. A Practical Guide and Atlas, pp. 105-107. , Cambridge University Press, New York; Flewett, T.H., Bryden, A.S., Davies, H., Diagnostic electron microscopy of faeces. I. The viral flora of the faeces as seen by electron microscopy (1974) J. Clin. Pathol., 27, pp. 603-614; Fortsas, E., Grydsuk, J.D., Brown, M., Petric, M., Monolconal antibody recognizes common epitope on protein VI of enteric adenoviruses (1993) CACMID Meeting, , Vancouver, BC, Canada, Nov. 1993 (Abstract, J-2); Garwes, D.J., Coronaviruses in animals (1982) Virus Infections of the Intestinal Tract, pp. 315-359. , D.A.J. Tyrell and A.Z. Kapikian (Eds.), Marcel Dekker, New York; Grohmann, G.S., Glass, R.I., Pereira, H.G., Enteric viruses and diarrhea in HIV-infected patients (1993) New Eng. J. Med., 329, pp. 14-20; Halonen, P., Meurman, O., Lövgren, T., Hemmilä, I., Soini, E., Detection of viral antigens by time-resolved fluoroimmunoassay (1983) Curr. Top. Microbiol., 104, pp. 133-146; Hamilton, J.R., Gall, D.G., Pathophysiology and clinical features of viral enteritis (1982) Virus Infections of the Gastroentestinal Tract, pp. 227-238. , D.A.J. Tyrrell and A.Z. Kapikian (Eds.), Marcel Dekker, New York; Hieber, J.P., Shelton, S., Nelson, J.D., Comparison of human rotavirus disease in tropical and temperate settings (1978) Am. J. Dis. Child., 132, pp. 853-858; Jiang, X., Graham, D.Y., Wang, K., Estes, M.K., Norwalk virus gene cloning and characterization (1990) Science, 250, pp. 1580-1583; Jiang, X., Wang, M., Wang, K., Estes, M.K., Sequence and genomic organization of Norwalk virus (1993) Virology, 195, pp. 51-61; Kapembwa, M., Fleming, S., Serwadda, D., Diarrhoea in advanced HIV infection associated with increased small intestinal permeability in both African and Caucasian patients (1990) Int. Conf. AIDS, 368, p. 214. , San Francisco, June 1990 (Abstract VI), 1 Th.B; Kapikian, A.Z., Chanock, R.M., Viral gastroenteritis (1989) Viral Infections of Human Epidemiology and Control, 3rd Edn, pp. 293-340. , A.S. Evans (Ed.). Plenum, New York; Kapikian, A.Z., Chanock, R.M., Rotavirus (1990) Virology, 2, pp. 1353-1404. , B.N. Fields, D.M. Knipe, R.M. Chanock, M.S. Hirsh, J.L. Melnick, T.P. Monath and B. Roizman (Eds.), 2nd edn, Raven Press, New York; Kapikian, A.Z., Wyatt, R.G., Dolin, R., Visualization by immune electron microscopy of a 27-nm particle associated with acute infectious non-bacterial gastroenteritis (1972) J. Virol., 10, pp. 1075-1081; Kaplan, J.E., Gary, G.W., Baron, R.C., Epidemiology of Norwalk gastroenteritis and role of Norwalk virus in outbreaks of acute nonbacterial gastroenteritis (1982) Ann. Intern. Med., 96, pp. 756-761; Krajden, M., Brown, M., Petrasek, A., Middleton, P.J., Clinical features of adenovirus enteritis, a review of 127 cases (1990) Pediatr. Infect. Dis. J., 9, pp. 636-641; Lew, J.F., Glass, R.I., Petric, M., Six-year retrospective surveillance of gastroenteritis viruses identified by ten electron microscopy centers in the United States and Canada (1990) Pediatr. Infect. Dis. J., 9, pp. 709-714; Lew, J.F., Kapikian, A.Z., Valdesuso, J., Green, K.Y., Molecular characterization of Hawaii virus and other Norwalk-like viruses, evidence for genetic polymorphism among human caliciviruses (1994) J. Infect. Dis., 170, pp. 535-542; Madeley, C.R., Cosgrove, B.P., 28 nm particles in faeces in infantile gastroenteritis (1975) Lancet, 2, pp. 451-452; McCarthy, P.H., General considerations in the care of sick children: Pathophysiology of body fluid, parenteral fluid therapy (1992) Textbook of Pediatrics, 14th Edn, pp. 171-211. , R.E. Behrman, R.M. Kliegman, W.E. Nelson and V.C. Vaughan III (Eds.), W.B. Saunders Coy, Philadelphia; McCreedy, B.J., Callaway, T.H., Laboratory design and work flow (1993) Diagnostic Molecular Microbiology: Principles and Applications, pp. 149-159. , D.H. Persing, T.F. Smith, F.C. Tenover and T.J. White (Eds.), American Society for Microbiology, Washington, DC; Middleton, P.J., Role of viruses in pediatric gastrointestinal disease and epidemiologic factors (1982) Virus Infections of the Gastrointestinal Tract, pp. 211-225. , D.A.J. Tyrrell and A.Z. Kapikian (Eds.). Marcel Dekker, New York; Middleton, P.J., Szymanski, M.T., Abbott, G.H., Orbivirus acute gastroenteritis of infancy (1974) Lancet, 1, pp. 1241-1244; Middleton, P.J., Szymanski, M.T., Petric, M., Viruses associated with acute gastroenteritis in young children (1977) Am. J. Dis. Child., 131, pp. 733-737; Sherlock, C.H., Brandt, C.J., Middleton, P.J., Smith, J.A., Laboratory diagnosis of viral infections producing enteritis (1989) CUMITECH 26, pp. 1-12. , American Society of Microbiologists, Washington, DC; Tellier, R., Petric, M., Human torovirus purification from faeces (1993) Int. Congr. Virology, p. 47. , Glasgow, Scotland, Aug. 1993 (Abstract IX), W 24-4","Middleton, P.J.; Provincial Laboratory, BC Centre for Disease Control, 828 West 10th Avenue, Vancouver, BC V5Z 1L8, Canada",,"Elsevier B.V.",09280197,,CDVIE,,"English","CLIN. DIAGN. VIROL.",Article,"Final",,Scopus,2-s2.0-0030220218
"Greiff L., Åkerlund A., Andersson M., Svensson C., Alkner U., Persson C.G.A.","7006426396;6701441885;7402879512;7202512750;6604092201;35493943900;","Day-night differences in mucosal plasma proteins in common cold",1996,"Acta Oto-Laryngologica","116","1",,"85","90",,8,"10.3109/00016489609137719","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030030730&doi=10.3109%2f00016489609137719&partnerID=40&md5=d79cd707cc2c71379e1baad18a9a4a17","Department of Otorhinolaryngology, University Hospital, Lund, Sweden; Department of Bioanalysis, Astra Draco, Lund, Sweden; Department of Clinical Pharmacology, University Hospital, Lund, Sweden; Dept. Clinical Pharmacology, University Hospital, S-221 85 Lund, Sweden","Greiff, L., Department of Otorhinolaryngology, University Hospital, Lund, Sweden; Åkerlund, A., Department of Otorhinolaryngology, University Hospital, Lund, Sweden; Andersson, M., Department of Otorhinolaryngology, University Hospital, Lund, Sweden; Svensson, C., Department of Otorhinolaryngology, University Hospital, Lund, Sweden; Alkner, U., Department of Bioanalysis, Astra Draco, Lund, Sweden; Persson, C.G.A., Department of Clinical Pharmacology, University Hospital, Lund, Sweden, Dept. Clinical Pharmacology, University Hospital, S-221 85 Lund, Sweden","Aggravation of symptoms in inflammatory airway diseases is common in the early morning hours, but little is known about day-night differences in the occurrence of plasma exudate on the airway surface. We have therefore examined the plasma macromolecules on the nasal mucosa at different time points. The study comprised 20 subjects who had been inoculated (day 0) with coronavirus intranasally. Ten subjects remained healthy and 10 developed common cold with significant symptoms from day 2 to day 6. Starting on day 3 at 8.00 h and repeated at 4 h intervals until 4.00 h on day 4, nasal lavages were carried out by employment of a nasal pool-device which fills the entire unilateral nasal cavity and gently but effectively irrigates its surface. Lavage fluid levels of albumin (Mw 69,000 D) and fibrinogen (Mw 340,000 D) were determined. In the healthy subjects the levels of albumin and fibrinogen remained low throughout the experiment, however, with mean peak values of the two proteins occurring at 4.00 h (p < 0.05 compared to daytime nadir at 16.00 h). In subjects with common cold both albumin (p < 0.05) and fibrinogen (p < 0.01) exhibited marked variation with individual and mean peak levels recorded at 8.00 h day 3, and 4.00 h day 4. These mean peak values were 5-20 times higher (p < 0.01-p < 0.05) than the mean levels recorded in these subjects at the other time periods. The present data indicate a marked day-night difference in the occurrence of plasma proteins on the airway surface in common cold, whereas in health the difference is much less. We conclude that different-sized plasma proteins may accumulate on the mucosa in healthy airways during late night hours and that in common cold this nocturnal accumulation may be considerably increased.","Albumin; Circadian variation; Coronavirus; Exudation; Fibrinogen; Inflammation; Rhinitis","albumin; fibrinogen; protein; adult; article; circadian rhythm; common cold; Coronavirus; human; human experiment; inoculation; normal human; priority journal; protein blood level; rhinitis","De Vries, K., Goei, J.T., Booy-Nord, H., Orie, N.G.M., Changes during 24 hours in the lung function and histamine hyperreactivity of the bronchial tree in asthmatic and bronchitic patients (1962) Int Arch Allergy, 20, pp. 93-101; Martin, R.J., Cicutto, L.C., Smith, H.R., Ballard, R.D., Szefler, S.J., Airways inflammation in nocturnal asthma (1991) Am Rev Respir Dis, 143, pp. 351-357; Smith, A., Tyrrell, D., Coyle, K., Higgins, P., Willman, J., Diurnal variation in the symptoms of colds and influenza (1988) Chronobiol Int, 5, pp. 411-416; Reinberg, A., Gervais, P., Levi, F., Smolensky, M., Del Cerro, L., Ugolinin, C., Circadian and circannual rhythms of allergic rhinitis: An epidemiological study involving chronobiologic methods (1988) J Allergy Clin Immunol, 88, pp. 51-62; Smolensky, M.H., Barnes, B.J., Reinberg, A., McGovern, J.P., Chronobiology and asthma I. Day-night differences in bronchial patency and dyspnea and circadian rhythm dependencies (1986) J Asthma, 23, pp. 321-343; Martin, J.G., Circadian rhythms, nocturnal asthma, and management (1992) Ann Allergy, 69, pp. 267-272; Persson, C.G.A., Svensson, C., Greiff, L., The use of the nose to study the inflammatory response in the respiratory tract (1992) Thorax, 47, pp. 993-1000; Persson, C.G.A., Airway epithelium and microcirculation (1994) Eur Respir Rev, , in press; Persson, C.G.A., Erjefält, I., Alkner, U., Plasma exudation as a first line respiratory mucosal defence (1991) Clin Exp Allergy, 21, pp. 17-24; Greiff, L., Erjefält, I., Wollmer, P., (1991) Nicotine Evokes Neurogenic Mucosal Exudation of Plasma in Guinea-pig but Not in Human Airways, pp. 109-123. , Thesis, University of Lund; Erjefält, I., Persson, C.G.A., Inflammatory passage of plasma macromolecules into airway wall and lumen (1989) Pulm Pharmacol, 2, pp. 93-102; Åkerlund, A., Greiff, L., Andersson, M., Bende, M., Alkner, U., Persson, C.G.A., Mucosal exudation of fibrinogen in coronavirus-induced common cold (1993) Acta Otolaryngol, 113, pp. 642-648. , Stockh; Beare, A., Reed, S., The study of antiviral compounds in volunteers (1977) Chemoprophylaxis and Virus Infections of the Respiratory Tract, 2, pp. 28-55. , Oxford JS, ed. Cleveland: CRC Press; Greiff, L., Pipkorn, U., Alkner, U., Persson, C.G.A., The nasal pool-device applies controlled concentrations of solutes on human nasal airway mucosa and samples its surface exudations/secretions (1990) Clin Exp Allergy, 20, pp. 253-259; Mygind, N., Thomsen, J., Diurnal variation of nasal protein concentration (1976) Acta Otolaryngol, 82, pp. 219-221. , Stockh; Erjefält, I., Persson, C.G.A., On the use of absorbing discs to sample mucosal surface liquids (1990) Clin Exp Allergy, 20, pp. 193-197; Reinberg, A., Schuller, E., Clench, J., Smolensky, M.H., Circadian and cirannual rhythms of leucocyte, proteins, and immunoglobulins (1980) Recent Advances in the Chronobiology of Allergy and Immunology, pp. 251-259. , Smolensky MH, McGovern J, Reinberg A, eds. Oxford: Pergamon Press; Sasaki, Y., Togo, Y., Wagner, H.N., Hornick, R.B., Schwarz, A.R., Proctor, D.F., Mucociliary function during experimentally induced rhinovirus infection in man (1973) Ann Otol, 82, pp. 203-211; Brugman, S.M., Larsen, G.L., Henson, P.M., Honor, J., Irvin, C.G., Increased lower airways responsiveness associated with sinusitis in a rabbit model (1993) Am Rev Respir Dis, 147, pp. 314-320; Persson, C.G.A., Role of plasma exudation in asthmatic airways (1986) Lancet, 2, pp. 1126-1129; Persson, C.G.A., Erjefält, I., Gustafsson, B., Luts, A., Subepithelial hydrostatic pressure may regulate plasma exudation across the mucosa (1990) Int Arch Allergy Appl Immunol, 92, pp. 148-153; Gustafsson, B., Persson, C.G.A., Asymmetrical effects of increases in hydrostatic pressure on macromolecular movement across the airway mucosa. A study in guinea-pig tube preparations (1991) Clin Exp Allergy, 21, pp. 121-126; Grega, G.J., Persson, C.G.A., Svensjö, E., Endothelial cell reactions to inflammatory mediators assessed in vivo by fluid and solute flux analysis (1988) Endothelial Cells, pp. 103-122. , Ryan US, ed. Boca Raton: CRC","Persson, C.G.A.; Department of Clinical Pharmacology, University Hospital, S-221 85 Lund, Sweden",,"Informa Healthcare",00016489,,AOLAA,"8820357","English","ACTA OTO-LARYNGOL.",Article,"Final",,Scopus,2-s2.0-0030030730
"Duval D., Giger U.","7007029452;7004892238;","Vaccine-associated Immune-Mediated Hemolytic Anemia in the dog",1996,"Journal of Veterinary Internal Medicine","10","5",,"290","295",,117,"10.1111/j.1939-1676.1996.tb02064.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030228347&doi=10.1111%2fj.1939-1676.1996.tb02064.x&partnerID=40&md5=421d5a04558547b9429069d7fae020df","Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, United States; Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, 3900 Delancey St, Philadelphia, PA 19104-6010, United States","Duval, D., Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, United States; Giger, U., Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, United States, Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, 3900 Delancey St, Philadelphia, PA 19104-6010, United States","Vaccination has been incriminated as a trigger of immune-mediated hemolytic anemia (IMHA) in dogs and in people, but evidence to support this association is lacking. In a controlled retrospective study, idiopathic IMHA was identified in 58 dogs over a 27-month period. When compared with a randomly selected control group of 70 dogs (presented for reasons other than IMHA) over the same period, the distribution of cases versus time since vaccination was different (P < .05). Fifteen of the dogs (26%) had been vaccinated within 1 month (mean, 13 days; median, 14 days; range, 1 to 27 days) of developing IMHA (P < .0001), whereas in the control group no marked increase in frequency of presentation was seen in the first month after vaccination. The dogs with IMHA were divided into 2 groups based on time since vaccination: the vaccine IMHA group included dogs vaccinated within 1 month of developing IMHA; the nonvaccine IMHA group included dogs that developed IMHA more than 1 month after vaccination. The recently vaccinated dogs with IMHA (vaccine IMHA group) had significantly lower platelet counts (P < .05) and a trend towards increased prevalence of intravascular hemolysis and autoagglutination when compared with the nonvaccine IMHA group. Similar mortality rates were seen in the vaccine IMHA group (60%) and the nonvaccine IMHA group (44%), with the majority of fatalities (>75%) occurring in the first 3 weeks after presentation. Persistent autoagglutination was a negative prognostic indicator for survival in both groups (P < .05). Presence of icterus and hyperbilirubinemia were negative prognostic indicators for survival in the nonvaccine IMHA group (P < .0001 and P < .01, respectively) but not in the vaccine IMHA group. In the recently vaccinated dogs, combination vaccines from various manufacturers against canine distemper, adenovirus type 2, leptospirosis, parainfluenza, and parvovirus (DHLPP) were involved in each case. Vaccines against rabies virus, Bordetella spp, coronavirus, and Lyme Borrelia were administered concomitantly to some dogs. This study provides the first clinical evidence for a temporal relationship of vaccine-associated IMHA in the dog. Copyright © 1996 by the American College of Veterinary Internal Medicine.",,"animal; animal disease; article; dog; dog disease; erythrocyte count; hematocrit; hemolytic anemia; immunology; leukocyte count; medical record; mortality; retrospective study; season; survival rate; vaccination; Anemia, Hemolytic; Animals; Dog Diseases; Dogs; Erythrocyte Count; Hematocrit; Leukocyte Count; Medical Records; Retrospective Studies; Seasons; Survival Rate; Vaccination","Klag, A.R., Giger, U., Shofer, F.S., Idiopathic immune-mediated hemolytic anemia in dogs: 42 cases (1986-1990) (1993) J Am Vet Med Assoc, 202, pp. 783-788; Dodds, W.J., Immune-mediated diseases of the blood (1983) Adv Vet Sci Comp Med, 27, pp. 163-196; Stockham, S.L., Ford, R.B., Weiss, D.J., Canine autoimmune hemolytic disease with a delayed erythroid regeneration (1980) J Am Anim Hosp Assoc, 16, pp. 927-931; Dodds, W.J., Contributions and future directions of hemostasis research (1988) J Am Vet Med Assoc, 193, pp. 1157-1160; Werner, L.L., Coombs' positive anemias in the dog and cat (1980) Compend Cont Ed Pract Vet, 2, pp. 96-102; Dodds, W.J., Immune-mediated blood diseases in Dogs. Part I - Signs and diagnosis (1983) Mod Vet Pract, MAY, pp. 375-379; Jackson, M.L., Kruth, S.A., Immune-mediated hemolytic anemia and thrombocytopenia in the dog: A retrospective study of 55 cases diagnosed from 1969 through 1983 at the Western College of Veterinary Medicine (1985) Can Vet J, 26, pp. 245-250; Jacobs, R.M., Murtaugh, R.J., Crocker, D.B., Use of a microtiter Coombs' test for study on age, gender, and breed distributions in immunohemolytic anemia of the dog (1984) J Am Vet Med Assoc, 185, pp. 66-69; Schalm, O.W., Autoimmune hemolytic anemia in the dog (1975) Canine Pract, 2, pp. 37-45; Switzer, J.W., Jain, N.C., Autoimmune hemolytic anemia in dogs and cats (1981) Vet Clin North Am Small Anim Pract, 11, pp. 405-420; Feller, W., (1950) An Introduction to Probability Theory and Applications, p. 54. , New York,NY: Wiley; Haneberg, B., Matre, R., Winsnes, R., Acute hemolytic anemia related to diphtheria-pertussis-tetanus vaccination (1978) Acta Paediatr Scand, 67, pp. 345-350; Howson, C.P., Fineberg, H.V., Adverse events following pertussis and rubella vaccines (1992) J Am Med Assoc, 267, pp. 392-396; Greene, C.E., Immunoprophylaxis and immunotherapy (1990) Infectious Diseases of the Dog and Cat, pp. 21-54. , Green CE, ed. Philadelphia, PA: WB Saunders; Hendrick, M.J., Dunagan, C.A., Focal necrotizing granulomatous panniculitis associated with subcutaneous injection of rabies vaccine in cats and dogs: 10 cases (1988-1989) (1991) J Am Vet Med Assoc, 198, pp. 304-305; Tizard, I., (1987) Veterinary Immunology - An Introduction, 3rd Ed., p. 381. , Philadelphia, PA: WB Saunders; Kass, P.H., Barnes, W.G., Spangler, W.L., Epidemiologic evidence for a causal relation between vaccination and fibrosarcoma tumorigenesis in cats (1993) J Am Vet Med Assoc, 203, pp. 396-405; Hendrick, M.J., Goldschmidt, M.H., Shofer, F.S., Postvaccination sarcomas in the cat: Epidemiology and electron probe microanalytical identification of aluminum (1992) Cancer Res, 52, pp. 5391-5394; Hendrick, M.J., Shofer, F.S., Goldschmidt, M.H., Comparison of fibrosarcomas that developed at vaccination sites and at nonvaccination sites in cats: 239 cases (1991-1992) (1994) J Am Vet Med Assoc, 205, pp. 1425-1429; Pineau, A., Durand, C., Guillard, O., Role of aluminium in skin reactions after diptheria-tetanus-pertussis-poliomyelitis vaccination: An experimental study in rabbits (1992) Toxicology, 73, pp. 117-125; Fine, P.E., Methodological issues in the evaluation and monitoring of vaccine safety (1995) Combined Vaccines and Simultaneous Administration. Current Issues and Perspectives, pp. 300-308. , Williams JC, Goldenthal KL, Burns DL, et al, eds. New York, NY: New York Academy of Sciences; Azeemuddin, S., Thrombocytopenia purpura after combined vaccine against measles, mumps, and rubella (1987) Clin Pediatr, 26, p. 318; Citron, M.L., Moss, B.M., Pneumococcal-vaccine-induced thrombocytopenia (1982) J Am Med Assoc, 248, p. 1178; Kelton, J.G., Vaccination-associated relapse of immune thrombocytopenia (1981) J Am Med Assoc, 245, pp. 369-371; Neiderud, J., Thrombocytopenic purpura after a combined vaccine against morbilli, parotitis and rubella (1983) Acta Paediatr Scand, 72, pp. 613-614; McAnulty, J.F., Rudd, R.G., Thrombocytopenia associated with vaccination of a dog with a modified-live paramyxovirus vaccine (1985) J Am Vet Med Assoc, 186, pp. 1217-1219; Pineau, S., Belbeck, L.W., Moore, S., Levamisole reduces the thrombocytopenia associated with myxovirus vaccination (1980) Can Vet J, 21, pp. 82-84; Straw, B., Decrease in platelet count after vaccination with distemper-hepatitis (DH) vaccine (1978) Vet Med Small Anim Clin, JUNE, pp. 725-726; Axthelm, M.K., Krakowka, S., Canine distemper virus-induced thrombocytopenia (1987) Am J Vet Res, 48, pp. 1269-1275; Olivares, M., Walter, T., Osorio, M., Anemia of a mild viral infection: The measles vaccine as a model (1989) Pediatrics, 84, pp. 851-855; Patterson, R., Anderson, J., Allergic reactions to drugs and biologic agents (1982) J Am Med Assoc, 248, pp. 2637-2645; Fischlack, M., Roubinian, J.R., Talal, N., Lipopolysaccharide induction of IgM antibodies to polyadenylic acid in normal mice (1978) J Immunol, 120, pp. 1856-1861; Atkinson, J.P., Factors that alter erythrocyte clearance patterns (1977) Ann Intern Med, 87, pp. 213-217; Packman, C.H., Leddy, J.P., Acquired hemolytic anemia due to warm-reacting autoantibodies (1990) Hematology, 4th Ed., pp. 666-675. , Williams JW, Beutler E, Erslev AJ, et al, eds. New York,NY: McGraw-Hill; Smith, C.A., Current concepts: Are we vaccinating too much? (1995) J Am Vet Med Assoc, 207, pp. 421-425","Giger, U.; Department of Clinical Studies, School of Veterinary Medicine, University of Pennsylvania, 3900 Delancey St, Philadelphia, PA 19104-6010, United States",,"American College of Veterinary Internal Medicine",08916640,,,"8884713","English","J. Vet. Intern. Med.",Article,"Final",,Scopus,2-s2.0-0030228347
"Cebolla Á., Guzmán C., De Lorenzo V.","6603638237;7103258580;7005588312;","Nondisruptive detection of activity of catabolic promoters of Pseudomonas putida with an antigenic surface reporter system",1996,"Applied and Environmental Microbiology","62","1",,"214","220",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030049029&partnerID=40&md5=47fd638ef2876473f35c6869cea55178","Ctro. de Invest. Biológicas, Consejo Sup. de Investigacions Cie., Madrid 28006, Spain; Natl. Ctr. for Res. in Biotechnology, Braunschweig 38124, Germany; Ctro. de Invest. Biológicas, C/Velázquez 144, 28006 Madrid, Spain","Cebolla, Á., Ctro. de Invest. Biológicas, Consejo Sup. de Investigacions Cie., Madrid 28006, Spain; Guzmán, C., Natl. Ctr. for Res. in Biotechnology, Braunschweig 38124, Germany; De Lorenzo, V., Ctro. de Invest. Biológicas, Consejo Sup. de Investigacions Cie., Madrid 28006, Spain, Ctro. de Invest. Biológicas, C/Velázquez 144, 28006 Madrid, Spain","A simple procedure to detect the switching on and off of catabolic promoters of Pseudomonas putida, at the level of single cells based on the immunodetection of a reporter epitope expressed on the surface of bacterial cells, has been developed. To do this, the antigenic sequence Asp-Leu-Pro- Pro-Asn-Ser-Asp-Val-Val-Asp, from a coronavirus, was inserted genetically in the permissive site around amino acid position 153 of the LamB protein (maltose and lambda phage receptor) of Escherichia coli. When the hybrid lamB gene is transcribed, the epitope becomes presented on the surface of the bacterial cells in a configuration available to specific antibodies. To validate this notion in nonenteric bacteria, the expression and correct processing of LamB were confirmed by coupling the lamB gene to the salicylate-responsive Psal promoter of the NAH7 (naphthalene degradation) plasmid in Pseudomonas putida. Subsequently, a hybrid lamB gene carrying the sequence of the coronavirus antigen was placed downstream of the m-toluate- responsive Pm promoter of the TOL (toluene degradation) plasmid. Exposure of the epitope on the Pseudomonas cell surface was monitored through fluorescence of whole cells treated with a monoclonal antibody against the heterologous antigen. Fluorescence emission was dependent on the presence of m-toluate in the medium, thus permitting detection of the Pm promoter switching on by simple optical inspection of individual cells, even in situations when these are a very minor component of a complex bacterial community.",,"bacterial antigen; virus antigen; antigen detection; antigen expression; article; bacterial membrane; cell surface; coronavirus; escherichia coli; genetic transcription; nonhuman; pseudomonas putida; reporter gene; Amino Acid Sequence; Antibodies, Monoclonal; Antigens, Viral; Base Sequence; Benzoates; Benzoic Acids; Coronavirus; Epitopes; Gene Expression Regulation, Bacterial; Genes, Reporter; Genetic Vectors; Membrane Glycoproteins; Molecular Sequence Data; Naphthalenes; Plasmids; Promoter Regions (Genetics); Pseudomonas putida; Receptors, Virus; Recombinant Fusion Proteins; Toluene; Viral Envelope Proteins; Bacteria (microorganisms); Coronavirus; Escherichia coli; Pseudomonas; Pseudomonas putida","Beckwith, J.R., A deletion analysis of the lac operator region in Escherichia coli (1964) J. 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Bacteriol., 176, pp. 3013-3020; De Lorenzo, V., Designing microbial systems for gene expression in the field (1994) Trends Biotechnol., 12, pp. 365-371; De Lorenzo, V., Fernandez, S., Herrero, M., Jakubzik, U., Timmis, K.N., Engineering of alkyl- And haloaromatic-responsive gene expression with mini-transposons containing regulated promoters of biodegradative pathways of Pseudomonas (1993) Gene, 130, pp. 41-46; De Lorenzo, V., Timmis, K.N., Analysis and construction of stable phenotypes in Gram-negative bacteria with Tn5- And Tn10-derived minitransposons (1994) Methods Enzymol., 235, pp. 386-405; De Vries, G.E., Raymond, C.K., Ludwig, R.A., Extension of the bacteriophage λ host range: Selection, cloning, and characterization of a constitutive λ receptor gene (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 6080-6084; Gebauer, F., Posthumus, W.P.A., Correa, I., Suñé, C., Smerdou, C., Sanchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virology, 183, pp. 225-238; Herrero, M., De Lorenzo, V., Timmis, K., Transposon vectors containing non-antibiotic resistance selection markers for cloning and stable chromosomal insertion of foreign genes in gram-negative bacteria (1990) J. Bacteriol., 172, pp. 6557-6567; Huang, J., Schell, M.A., In vivo interactions of the NahR transcrip-tional activator with its target sequences (1991) J. Biol. Chem., 266, pp. 10830-10838; Izard, J., Kendall, D.A., Signal peptides: Exquisitely designed transport promoters (1994) Mol. Microbiol., 13, pp. 765-773; Kessler, B., Herrero, M., Timmis, K., De Lorenzo, V., Genetic evidence that the XylS regulator of the TOL meta-operon of Pseudomonas controls Pm promoter through weak DNA-protein interaction (1994) J. Bacteriol., 176, pp. 3171-3176; Laemmli, V.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Legocki, R.P., Legocki, M., Baldwin, T.O., Szalay, A.A., Bioluminescence in soybean root nodules: Demonstration of general approach to assay gene expression in vivo by using bacterial luciferase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 9080-9084; Lewis, P.J., Nwoguh, C.E., Barer, M.R., Harwood, C.R., Errington, J., Use of digitized video microscopy with a fluorogenic enzyme substrate to demonstrate cell- And compartment-specific gene expression in Salmonella enteriditis and Bacillus subtilis (1994) Mol. Microbiol., 13, pp. 655-662; Lewis, P.J., Partridge, S.R., Errington, J., σ factors, asymmetry and the determination of the cell fate in Bacillus subtilis (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 3849-3853; Marqués, S., Ramos, J.L., Transcriptional control of the Pseudomonas putida TOL plasmid catabolic pathways (1993) Mol. Microbiol., 9, pp. 923-929; Meens, J., Frings, E., Klose, M., Freudi, R., An outer membrane protein (OmpA) of Escherichia coli can be translocated across the cytoplasmatic membrane of Bacillus subtilis (1993) Mol. Microbiol., 9, pp. 847-855; Morales, V.M., Bäckman, A., Bagdasarian, M., A series of widehost-range low-copy-number vectors that allow direct screening for recombinants (1991) Gene, 97, pp. 39-47; Palva, E.T., Harkki, A., Karkku, H., Läng, H., Pirhonen, M., Lambda vehicles provide new tools for genetic analysis of Gram-negative bacteria (1987) Microb. Pathog., 3, pp. 227-230; Roszack, D.B., Colwell, R.R., Survival strategies of bacteria in the natural environment (1987) Microbiol. Rev., 51, pp. 365-379; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Schell, M.A., Molecular biology of the LysR family of transcriptional regulators (1993) Annu. Rev. Microbiol., 47, pp. 597-626; Silcock, D.J., Waterhouse, R.N., Glover, L.A., Presser, J.I., Killham, K., Detection of a single genetically modified bacterial cell in soil by using charge coupled device-enhanced microscopy (1992) Appl. Environ. Microbiol., 58, pp. 2444-2448; Steidler, L., Remaut, E., Fiers, W., LamB as a carrier molecule for the functional exposition of IgG-binding domains of the Staphylococcus aureus protein A al the surface of Escherichia coli K12 (1993) Mol. Gen. Genet., 236, pp. 187-192; Stewart, G.S.A., Williams, P., Lux genes and the applications of bacterial bioluminescence (1992) J. Gen. 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Bacteriol., 167, pp. 473-479; Yen, K.-M., Serdar, C.M., Genetics of naphthalene metabolism in pseudomonads (1988) Crit. Rev. Microbiol., 15, pp. 247-268; Zaat, A.J., Slegtenhorst-Eegdeman, K., Tommanssen, J., Geli, V., Wijffelman, W.C.A., Lugtenberg, B.J.J., Construction of phoE-caa, a novel PCR- And immunologically detectable marker gene for Pseudomonas putida (1994) Appl. Environ. Microbiol., 60, pp. 3965-3973","De Lorenzo, V.; Centro de Investigaciones Biologicas, CSIC, C/Velazquez 144, 28006 Madrid, Spain",,,00992240,,AEMID,"8572699","English","APPL. ENVIRON. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0030049029
"Luytjes W., Gerritsma H., Spaan W.J.M.","6701683324;6507424618;7007172944;","Replication of synthetic defective interfering RNAs derived from coronavirus mouse hepatitis virus-A59",1996,"Virology","216","1",,"174","183",,26,"10.1006/viro.1996.0044","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029664639&doi=10.1006%2fviro.1996.0044&partnerID=40&md5=3d114481cee9df81953f4667f6e6fc9e","Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands","Luytjes, W., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Gerritsma, H., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands","We have analyzed the replication of deletion mutants of defective interfering (DI) RNAs derived from the coronavirus mouse hepatitis virus (MHV)-A59 in the presence of MHV-A59. Using two parental DI RNAs, MIDI and MIDIΔH, a twin set of deletion mutants was generated with progressively shorter stretches of 5′ sequence colinear with the genomic RNA. All deletion mutants contained in-frame ORFs. We show that in transfected cells and after one passage the DI RNAs were detectable and that their accumulation was positively correlated with the length of 5′ sequence they contained. However, accumulation of two twin mutants, Δ2, in which sequences from nucleotide position 467 were fused to those from position 801, was undetectable. In passage 4 cells, but not in transfected or in passage 1 cells, recombination with genomic RNA led to the appearance of the parental DI RNAs. The accumulation of these parental RNAs was inversely correlated with the length of 5′ sequence on the deletion mutants and was highest in the Δ2 samples. In sharp contrast to the data reported for MHV-JHM-derived DI RNAs, we show that MHV-A59-derived mutant RNAs do not require an internal sequence domain for replication. The data suggest that coronavirus replication involves an RNA superstructure at the 5′ end of the genome or one comprising both ends of the genomic RNA. We also conclude from the recombination data that in-frame mutants with impaired replication signals are more fit than out-frame mutants with intact replication signals, © 1995 Academic Press, Inc.",,"Coronavirus; Murine hepatitis virus; virus RNA; animal; article; biosynthesis; cell line; defective virus; gene deletion; genetics; helper virus; L cell; molecular genetics; mouse; Murine hepatitis coronavirus; nucleotide sequence; physiology; virus replication; controlled study; deletion mutant; murine hepatitis coronavirus; nonhuman; priority journal; virus mutant; Animals; Base Sequence; Cell Line; Defective Viruses; Gene Deletion; Helper Viruses; L Cells (Cell Line); Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Viral; Virus Replication","Andino, R., Rieckhof, G.E., Baltimore, D., A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA (1990) Cell, 63, pp. 369-380; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; De Groot, R.J., Van Der Most, R.G., Spaan, W.J., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5898-5905; Fodor, E., Pritlove, D.C., Brownlee, G.G., The influenza virus panhandle is involved in the initiation of transcription (1994) J. Virol., 68, pp. 4092-4096; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Hofmann, M.A., Sethna, P.B., Brian, D.A., Bovine coronavirus mRMA replication continues throughout persistent infection in cell culture (1990) J. Virol., 64, pp. 4108-4114; Kim, Y.N., Makino, S., Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal (1995) J. Virol., 69, pp. 4963-4971; Kim, Y.N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 3-63; Lai, M.M., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333. , Review; Lai, M.M.C., Patton, C.D., Stohlman, S.A., Replication of mouse hepatitis virus: Negative-stranded RNA and replicative form RNA are of genome length (1982) J. Virol., 44, pp. 487-492; Lin, Y.J., Lai, M.M., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.J., Liao, C.L., Lai, M.M., Identification of the cisacting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Luo, G., Luytjes, W., Enami, M., Palese, P., The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure (1991) J. Virol., 65, pp. 2861-2867; Luytjes, W., Coronavirus gene expression (1995) The Coronaviridae, pp. 33-54. , S. G. Siddell, Ed., Plenum, New York; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol., 54, pp. 329-336; Makino, S., Shieh, C.K., Soe, L.H., Baker, S.C., Lai, M.M., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Pogue, G.P., Hall, T.C., The requirement for a 5′ stem - Loop structure in brome mosaic virus replication supports a model for viral positive-strand RNA initiation (1992) J. Virol., 66, pp. 674-684; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) ""Molecular Cloning: A Laboratory Manual,"" 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbour, NY; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronavi-ruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Strauss, H.S., Strauss, E.G., The alphaviruses: Gene expression, replication, and evolution (1994) Microbiol. Rev., 58, pp. 491-562; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-32. , S. G. Siddell, Ed., Plenum, New York; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of Coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of Coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Van Der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the Coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Zhao, X., Shaw, K., Cavanagh, D., Presence of subgenomic mRNAs in virions of Coronavirus IBV (1993) Virology, 196, pp. 172-178","Luytjes, W.; Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; email: wluytjes@ullf2.LeidenUniv.nl",,"Academic Press Inc.",00426822,,VIRLA,"8614984","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0029664639
"Wesley R.D., Woods R.D.","7103154080;7401706916;","Induction of protective immunity against transmissible gastroenteritis virus after exposure of neonatal pigs to porcine respiratory coronavirus",1996,"American Journal of Veterinary Research","57","2",,"157","162",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030075310&partnerID=40&md5=c94c227f709ebd66e2fe4a93114ef25a","USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States","Wesley, R.D., USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States; Woods, R.D., USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States","Objective - To test the ability of porcine respiratory coronavirus (PRCV) to induce protective immunity to antigenically related transmissible gastroenteritis virus (TGEV) in neonatal pigs Design - Neonatal pigs were exposed to PRCV when they were 2, 4, or 6 days old and challenge-exposed to virulent TGEV at 10 days of age. Animals - 34 hysterectomy-derived, colostrum-deprived pigs. Procedure - After challenge exposure, clinical signs were observed, body weight, antibody response, and virus shedding were measured, and mortality was determined. Results - After exposure to PRCV, principals had a slightly slower rate of weight gain than did controls, with 1 exception (a PRCV-exposed pig that was dyspneic for 1 day), principals and controls remained clinically normal until shortly after challenge exposure, when all pigs became listless and anorectic and developed watery diarrhea. However, by day 3, most of the pigs that had been exposed to PRCV when they were either 2 or 4 days old began to recover and most (15/18) survived Conversely, the clinical condition of most of the other pigs worsened and most (14/16) died. Pigs exposed to PRCV when they were 2 or 4 days old also differed from all other pigs in that they had serum virus-neutralizing antibodies for PRCV and TGEV at the time of challenge exposure. Conclusions - The PRCV can induce protective immunity to TGEV in neonatal pigs and such immunity develops at or about 6 days after exposure to PRCV. Moreover, protective immunity may be coincident with the appearance of virus-neutralizing antibody Clinical Relevance - Exposure to PRCV should enhance a TGE herd vaccination program.",,"virus antibody; aging; animal; animal disease; article; biosynthesis; body weight; Coronavirus; female; immunology; mortality; newborn; physiology; survival rate; swine; swine disease; vaccination; virus shedding; Aging; Animals; Animals, Newborn; Antibodies, Viral; Body Weight; Coronavirus; Female; Gastroenteritis, Transmissible, of Swine; Survival Rate; Swine; Vaccination; Virus Shedding","Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine 7th Ed., pp. 362-386. , Leman AD, Straw BE, Mengeling WL, et al, eds. Ames, Iowa: Iowa State University Press; Moon, H.W., Kemeny, L.J., Lambert, G., Age dependent resistance to transmissible gastroenteritis of swine. III Effects of epithelial cell kinetics on coronavirus production and on atrophy of intestinal villi (1975) Vet Pathol, 12, pp. 434-445; Hooper, B.E., Haelterman, E.O., Concepts of pathogenesis and passive immunity in transmissible gastroenteritis of swine (1966) J Am Vet Med Assoc, 149, pp. 1580-1586; Bohl, E.H., Gupta, R.K.P., Olquin, M.V.F., Antibody responses in serum, colostrum, and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect Immunol, 6, pp. 289-301; Bernard, S., Bottreau, E., Aynaud, J.M., Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis (1989) Vet Microbiol, 21, pp. 1-8; Callebaut, P., Cox, E., Pensaert, M., Induction of milk IgA by a porcine respiratory coronavirus (1990) Coronaviruses and Their Disease, pp. 421-428. , Cavanagh D, Brown TDK, eds. London: Plenum Publishing Corp; Wesley, R.D., Woods, R.D., Immunization of pregnant gilts with PRCV induces lactogenic immunity for protection of nursing piglets from challenge with TGEV (1993) Vet Microbiol, 38, pp. 31-40; Lanza, I., Shoup, D.I., Saif, L.J., Lactogenic immunity and milk antibody isotypes to transmissible gastroenteritis virus in sows exposed to porcine respiratory coronavirus during pregnancy (1995) Am J Vet Res, 56, pp. 739-748; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; De Diego, M., Laviada, M.D., Enjuanes, L., Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J Virol, 66, pp. 6502-6508; Van Nieuwstadt, A.P., Zetstra, T., Boonstra, J., Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet Rec, 125, pp. 58-60; Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vacate, 11, pp. 267-272; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis virus of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) J Comp Med Vet Sci, 30, pp. 190-198; Wesley, R.D., Woods, R.D., Hill, H.T., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; Hill, H., Biwer, J., Woods, R.D., Porcine respiratory coronavirus isolated from two U.S. swine herds (1990) Proceedings. Annu Meet Am Assoc Swine Pract, pp. 333-335; Wesley, R.D., Woods, R.D., Correa, I., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet Microbiol, 18, pp. 197-208; Mengeling, W.L., Lager, K.M., Vorwald, A.C., Identification and titration of antibodies to porcine reproductive and respiratory syndrome virus using indirect immunofluorescence microscopy and microwell cell culture plates (1993) Proceedings Annu Meet Livestock Conserv Inst, pp. 95-99; Woods, R.D., Wesley, R.D., Kapke, P.A., Neutralization of porcine transmissible gastroenteritis virus by complement-dependent monoclonal antibodies (1988) Am J Vet Res, 49, pp. 300-304; Saif, L.J., Van Cott, J.L., Brim, T.A., Immunity to transmissible gastroenteritis virus and porcine respiratory coronavirus infections in swine (1994) Vet Immunol Immunopathol, 43, pp. 89-97; VanCott, J.L., Brim, T.A., Simkins, R.A., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J Immunol, 150, pp. 3990-4000","Wesley, R.D.; USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States",,,00029645,,AJVRA,"8633800","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0030075310
"Elvander M.","55959255600;","Severe respiratory disease in dairy cows caused by infection with bovine respiratory syncytial virus",1996,"Veterinary Record","138","5",,"101","105",,76,"10.1136/vr.138.5.101","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030567107&doi=10.1136%2fvr.138.5.101&partnerID=40&md5=32d960df4257c6b09ec17b3f6a2e9a99","Department of Cattle and Sheep, National Veterinary Institute, PO Box 7073, S-750 07 Uppsala, Sweden","Elvander, M., Department of Cattle and Sheep, National Veterinary Institute, PO Box 7073, S-750 07 Uppsala, Sweden","Outbreaks of severe respiratory disease caused by bovine respiratory syncytial virus (BRSV) were recorded in dairy herds throughout Sweden in 1988 and subsequently. The virus was demonstrated in nasopharyngeal swab material from animals in the acute stage of the disease by culture, the polymerase chain reaction (PCR) and by immunofluorescence. Serological data from the herds investigated showed that the cows had seroconverted to BRSV rather than to bovine coronavirus, bovine viral diarrhoea virus or parainfluenza-3 virus. It was predominantly dairy herds in isolated areas that contracted a severe primary BRSV infection, often after the purchase of new animals. A nationwide survey for BRSV antibodies in bulk milk samples showed the highest prevalence, of 84 to 89 per cent, in the southernmost regions of Sweden and the lowest preva3 lence, of 41 to 51 per cent, in the north of the country. The prevalence of BRSV was highest in areas with the highest populations of cattle.",,"Animalia; Bos taurus; Bovinae; Bovine coronavirus; Bovine respiratory syncytial virus; Coronavirus; parainfluenza 3; parainfluenza 3 virus; Respiratory syncytial virus; Syncytial virus; virus antibody; acute disease; animal; animal disease; article; blood; cattle; cattle disease; epidemic; female; immunology; isolation and purification; milk; prevalence; Respiratory syncytial pneumovirus; Sweden; virology; virus infection; Acute Disease; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Disease Outbreaks; Female; Milk; Prevalence; Respiratory Syncytial Virus Infections; Respiratory Syncytial Virus, Bovine; Sweden","Ames, T.R., (1993) Vaterinary Medicine, 88, p. 881; Baker, J.C., Ames, T.R., Markham, R.J.F., (1986) American Journal of Veterinary Research, 47, p. 240; Baker, J.C., Velicer, L.F., (1991) Compendium on Continuing Education for the Practicing Veterinarian, 13, p. 1323; Baker, J.C., Wilson, E.G., McKay, G.L., Stanek, R.J., Underwood, W.J., Velicer, L.F., Mufson, M.A., (1992) Journal of Clinical Microbiology, 30, p. 1120; Bryson, D.G., McFerran, J.B., Ball, H.J., Neill, S.D., (1978) Veterinary Record, 103, p. 485; Cannon, R.M., Roe, R.T., (1982) Livestock Disease Surveys a Field Manual for Veterinarians, , Canberra, Australia, Australian Bureau of Animal Health, Australian Government Publishing service; Elvander, M., Alenius, S., Jacobsson, S.O., (1990) Proceedings of the 16th World Buiatrics Congress, 1, p. 461. , Bahia, Brazil. Salvador, Interlink Consultoria & Eventos; Elvander, M., Edwards, S., Naslund, K., Linde, N., (1995) Journal of Veterinary Diagnostic Investigations, 7, p. 177; Frey, M.L., (1983) Bovine Practitioner, 18, p. 73; Furze, J., Wertz, G., Lerch, R., Taylor, G., (1994) Journal of General Virology, 75, p. 363; Harrison, L.H., Pursell, A.R., (1985) Journal of the American Veterinary Medical Association, 187, p. 716; Inaba, Y., Tanaka, Y., Sato, K., Omori, T., Matumoto, M., (1972) Japanese Journal of Microbiology, 16, p. 373; Jacobs, J.W., Edfngton, N., (1971) Veterinary Record, 88, p. 694; Jacobsson, S.O., Alentus, S., Ottander, G., Palmer, H., Persson, J., Wennberg, K., Juntti, N., (1989) Svensk Veterinärtidning, 41, p. 641; Kimman, T.G., Westenbrink, F., (1990) Archives of Virology, 112, p. 1; Kimman, T.G., Zlmmer, G.M., Westenbrink, F., Mars, J., Van Leeuwen, E., (1988) Veterinary Record, 124, p. 104; Leamaster, B.R., Evermann, J.F., Mueller, G.M., Prieur, M.K., Van Der Schalie, J., (1983) Proceedings of the American Association of Veterinary Laboratory Diagnosticians, p. 265; Mallipeddi, S.K., Samal, S.K., (1993) Journal of General Virology, 74, p. 2001; Ödegaard, Ö.A., Krogsrud, J., (1977) Acta Veterinaria, Scandinavica, 18, p. 429; Paccaud, M.F., Jacquier, C., (1970) Archiv fur die Gesamte Virusforschung, 30, p. 327; Pirie, H.M., Petrie, L., Allan, E.M., (1981) Veterinary Record, 109, p. 87; Sharma, R., Woldehiwet, Z., (1991) Veterinary Bulletin, 61, p. 1117; Smith, M.H., Frey, M.L., Dierks, R.E., (1974) Veterinary Record, 94, p. 599; Smith, M.H., Lehmkul, H.D., Philips, S.M., (1979) Proceedings of the American Association of Veterinary Laboratory Diagnosticians, p. 259; Stott, E.I., Taylor, G., (1985) Archives of Virology, 84, p. 1; Stott, E.J., Thomas, L.H., Collins, A.P., Crouch, S., Jebbet, J., Smith, G.S., Luther, P.D., Caswell, R., (1980) Journal of Hygiene, 85, p. 257; Van Der Poel, W.H.M., Kramps, J.A., Middel, W.G.J., Van Oirschot, J.T., (1993) Archives of Virology, 133, p. 309; Verhoeff, J., Van Nieuwstadt, A.P.K.M.I., (1984) Veterinary Record, 114, p. 288; Vilcek, S., Elvander, M., Ballagi-Pordány, A., Belak, S., (1994) Journal of Clinical Microbiology, 32, p. 2225; Wellemans, G., (1990) Virus Infections in Ruminants, 3, p. 363. , Ed Z. Dinter Elsevier Science Publishers; Wellemans, G., Leunen, J., Luchsinger, E., (1970) Annales de Mèdicine Veterinère, 114, p. 89","Elvander, M.; Department of Cattle and Sheep, National Veterinary Institute, PO Box 7073, S-750 07 Uppsala, Sweden",,"British Veterinary Association",00424900,,VETRA,"8650902","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0030567107
"Hooks J.J., Wang Y., Detrick B.","7006661655;56802808200;7003911483;","Coronavirus infection of the retina is associated with increased levels of cytokines (IL-1, IL-6 and IFN-γ) within the vitreous",1996,"Investigative Ophthalmology and Visual Science","37","3",,"","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33750155072&partnerID=40&md5=d8d6cbced2e17e14a4bd00f5fbc8aedf","National Eye Institute, NIH, Bethesda, MD, United States; George Washington University Medical Center, Washington, DC, United States","Hooks, J.J., National Eye Institute, NIH, Bethesda, MD, United States; Wang, Y., National Eye Institute, NIH, Bethesda, MD, United States; Detrick, B., George Washington University Medical Center, Washington, DC, United States","Purpose: The murine coronavirus (MHV) induces a biphasic retinal disease in BALB/c mice. This virus model allows us to explore virologie, immunologic and genetic aspects involved in the pathogenesis of retinal tissue damage. In this report, we evaluate the induction of cytokines within the vitreous. Methods. BALB/c mice were inoculated by the intravitreal route with 104.5 TCID50 of virus or media. At varying times after inoculation, sera and eyes were removed. Formalin fixed samples were evaluated histologically and vitreous and serum samples were assayed for the presence of cytokines (IL-1α, IL-4, IL-6, TNF-α and IFN-γ) by ELISA assays. Frozen sections were immunocytochemically evaluated for lymphoid cells and virus. Results: Days 1-6 are associated with an acute retinal infection characterized by an infiltration of macrophages and T cells. At this time, elevated levels of IL-1α, IL-6 and IFN-γ were detected in the vitreous from virus infected mice in comparison to levels detected in mock injected or untreated mice. IL-6 was in 41% of vitreous samples from 27 virus infected mice whereas IL-6 was in 4% of 27 mock injected mice. IL-1α was in 50% of the vitreous samples from virus infected mice and was not detected in mock injected mice. Elevated cytokine levels in the vitreous did not correspond with serum levels. IL-4 and TNF-α were detected in all animals tested and did not correlate with infection. Days 10-21 are associated with the second phase of the infection, retinal degeneration. At this time, cytokine levels in the vitreous of virus infected mice were not different from levels detected in normal mice. Conclusion: These studies show that inflammatory cytokines, IL-1α, IL-6 and IFN-γ, are present within the vitreous during the early phase of the coronavirus - induced retinopathy. These data suggest that these cytokines may contribute to pathologic processes triggered by the virus infection.",,,,"Hooks, J.J.; National Eye Institute, NIH, Bethesda, MD, United States",,,01460404,,IOVSD,,"English","Invest. Ophthalmol. Vis. Sci.",Article,"Final",,Scopus,2-s2.0-33750155072
"Wang Y., Zhang J., Yu Z., Detrick B., Hooks J.J.","56802808200;7601342242;57199729869;7003911483;7006661655;","Apoptosis as a mechanism for tissue damage in murine coronavirus induced retinopathy",1996,"Investigative Ophthalmology and Visual Science","37","3",,"","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33750148182&partnerID=40&md5=9ebc717005a61c0d92e3a1c454c55206","National Eye Institute, NIH, Bethesda, MD, United States; National Heart, Lung and Blood Institute, NIH, Bethesda, MD, United States; George Washington University Medical Center, Washington, DC, United States","Wang, Y., National Eye Institute, NIH, Bethesda, MD, United States; Zhang, J., National Heart, Lung and Blood Institute, NIH, Bethesda, MD, United States; Yu, Z., National Heart, Lung and Blood Institute, NIH, Bethesda, MD, United States; Detrick, B., George Washington University Medical Center, Washington, DC, United States; Hooks, J.J., National Eye Institute, NIH, Bethesda, MD, United States","Purpose: The coronavirus, MHV, infection in BALB/c mice is a biphasic disease which culminates in a retinal degeneration. This model is characterized by a genetic predisposition associated with immunopathologic and autoimmune factors. In this study we evaluate apoptosis as a mechanism of retinal cell damage. Methods: BALB/c mice were inoculated by the intravitreal route with 104,5 TCID50 / 5 ul of MHV, JHM strain or with media. At varying times after inoculation, eyes were removed and fixed in 10% formalin for H&amp;E staining and in situ Apoptosis analysis or in glutaraldehyde for electron microscopy. Apoptosis was detected by two methods: (1) terminal dUTP nick end labeling (TUNEL) in situ detection of DNA fragmentation and (2) electron microscopic evaluation for morphologic changes. Results: A total of 35 eyes from virus infected mice, 10 eyes from mock injected mice and 12 eyes from untreated mice were obtained at 1, 3, 6, 10, 20, 41 and 62 days after inoculation. The retinas from untreated mice contained 1 to 3 TUNEL positive (apoptotic) cells while retinas from mock injected mice contained 0.5 to 6.5 apoptotic cells. In contrast, the retinas from virus infected mice contained 3.6 to 39.8 apoptotic cells. The number of apoptotic cells seen in the virus infected retinas is low at day 1 and 3, reaches a maximum at day 6 to 10, remains elevated at day 20, returning to normal levels after day 40. The difference between the apoptotic events in the virus infected retina in comparison to the control retina is P &lt; 0.01 (paired T test). Electron microscopic analysis revealed condensed chromatin, membrane blebbing and apoptotic bodies. Conclusion: These studies demonstrate that apoptosis may be one of the mechanisms involved in virus induced retinal tissue damage.",,,,"Wang, Y.; National Eye Institute, NIH, Bethesda, MD, United States",,,01460404,,IOVSD,,"English","Invest. Ophthalmol. Vis. Sci.",Article,"Final",,Scopus,2-s2.0-33750148182
"Tibbles K.W., Brierley I., Cavanagh D., Brown T.D.K.","6507790687;7004639098;26642890500;56248391000;","Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus",1996,"Journal of Virology","70","3",,"1923","1930",,37,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030069011&partnerID=40&md5=954d3c92452394c9cd27992c25933d74","Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP 1, United Kingdom; Institute for Animal Health, Compton Laboratory, Newbury, Berks, United Kingdom; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom","Tibbles, K.W., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP 1, United Kingdom; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP 1, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Newbury, Berks, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP 1, United Kingdom, Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom","A region of the infectious bronchitis virus (IBV) genome between nucleotide positions 8693 and 10927 which encodes the predicted 3C-like proteinase (3CLP) domain and several potential cleavage sites has been cloned into a T7 transcription vector. In vitro translation of synthetic transcripts generated from this plasmid was not accompanied by detectable processing activity of the nascent polypeptide unless the translation was carried out in the presence of microsomal membrane preparations. The processed products so obtained closely resembled in size those expected from cleavage at predicted glutamine-serine (Q/S) dipeptides and included a protein with a size of 35 kDa (p35) that corresponds to the predicted size of 3CLP. Efficient processing was dependent on the presence of membranes during translation; processing was found to occur when microsomes were added posttranslationally, but only after extended periods of incubation. C-terminal deletion analysis of the encoded polyprotein fragment revealed that cleavage activity was dependent on the presence of most but not all of the downstream and adjacent hydrophobic region MP2. Dysfunctional mutagenesis of the putative active- site cysteine residue of 3CLP to either serine or alanine resulted in polypeptides that were impaired for processing, while mutagenesis at the predicted Q/S release sites implicated them in the release of the p35 protein. Processed products of the wild-type protein were active in trans cleavage assays, which were used to demonstrate that the IBV 3CLP is sensitive to inhibition by both serine and cysteine protease class-specific inhibitors. These data reveal the identity of the IBV 3C-like proteinase, which exhibits characteristics in common with the 3C proteinases of picornaviruses.",,"proteinase; article; avian infectious bronchitis virus; carboxy terminal sequence; coronavirus; enzyme active site; in vitro study; mutagenesis; nonhuman; nucleotide sequence; priority journal; protein domain; protein processing; virus characterization; virus genome; Animals; Binding Sites; Catalysis; Cloning, Molecular; Cysteine; Cysteine Endopeptidases; Dipeptides; Infectious bronchitis virus; Mutagenesis, Site-Directed; Protein Processing, Post-Translational","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N.G., Picornavirat 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature (London), 369, pp. 72-76; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Baltimore, D., Polio is not dead (1971) Perspectives in Virology, 7, pp. 1-14. , M. Pollard (ed.), Academic Press, New York; Baum, E.Z., Bebernitz, G.A., Palant, O., Mueller, T., Plotch, S.J., Purification, properties, and mutagenesis of poliovirus 3C protease (1991) Virology, 185, pp. 140-150; Bazan, J.F., Fletterick, R.J., Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications (1988) Proc. Natl. Acad. Sci USA, 85, pp. 7872-7876; Boursnell, M.E., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen Virol., 68, pp. 57-77; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J, 6, pp. 3779-3785; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Rolley, N.J., Brown, T.D.K., Inglis, S.C., Products of the polymerase-encoding region of the coronavirus IBV (1990) Adv. Exp. Med. Biol., 276, pp. 275-281; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Brown, T.D.K., Brierley, I., The coronavirus nonstructural proteins (1995) The Coronaviridae, pp. 191-217. , S. G Siddell (ed), Plenum Press, New York; Denison, M., Perlman, S., Identification of putative polymerase gene product in cells infected with murine coronavirus A59 (1987) Virology, 157, pp. 565-568; Denison, M.R., Zolhik, P.W., Hughes, S.A., Giangreco, B., Olsen, A.L., Perlman, S., Liebowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Dotto, G.P., Enea, V., Zinder, N.D., Functional analysis of bacteriophage f1 intergenic region (1981) Virology, 159, pp. 274-284; Gorbalenya, A.E., Donchenko, A.P., Blinov, V.M., Koonin, E.V., Cysteine proteases of the positive strand viruses and chymotrypsin-like serine proteases (1989) FEBS Lett., 243, pp. 103-114; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Hames, B.D., An introduction to polyacrylamide gel electrophoresis (1981) Gel Electrophoresis of Proteins - A Practical Approach, pp. 1-91. , B. D. Hames and D. Rickwood (ed.), IRL Press, Oxford; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polyerase locus (1993) Virology, 195, pp. 680-691; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kadam, S., Poddig, J., Humphrey, P., Karwowski, J., Jackson, M., Tennent, S., Fung, L., McAlpine, J., Citrinin hydrate and radicin. human rhinovirus 3C-protease inhibitors discovered in a target-directed microbial screen (1994) J. Antibiot., 47, pp. 836-839; Kean, K.M., Howell, M.T., Grunert, S., Girard, M., Jackson, R.J., Substitution mutations at the putative catalytic triad of the polioviius 3C protease have differential effects on cleavage at different sites (1993) Virology, 194, pp. 360-364; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d (1995) Virology, 208, pp. 1-8; Kunkel, T.A., Rapid and efficient site-specific mutagenesis without phenotypic selection (1985) Proc Natl. Acad. Sci. USA, 82, pp. 488-492; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu Rev Microbiol., 44, pp. 303-333. , Review; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brierley, I., Brown, T.D.K., Identification of a trypsin-like serine protease domain encoded by ORF 1a of the coronavirus IBV Adv. Exp. Med. Biol., , in press; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J Virol, 68, pp. 5772-5780; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87-kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Matthews, D.A., Smith, W.W., Ferre, R.A., Condon, B., Budahazi, G., Sisson, W., Villafranca, J.E., Worland, S., Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein (1994) Cell, 77, pp. 761-771; McCall, J.O., Kadam, S., Katz, L., A high capacity microbial screen for inhibitors of human rhinovirus protease 3C (1994) Bio/Technology, 12, pp. 1012-1016; North, M.J., Prevention of unwanted protcolysis (1989) Protcolytic Enzymes - A Practical Approach, pp. 105-124. , R J Beynon and J. S. Bond (ed.), IRL Press. Oxford; Russell, M., Kidd, S., Kelley, M.R., An improved filamentous helper phage for generating single stranded plasmid (1986) DNA Gene, 45, pp. 333-338; Soe, L.H., Shieh, C.-K., Baker, S.C., Chang, M.-F., Lai, M.M.C., Sequence and translation of the murine coronavirus 5′-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase (1987) J. Virol., 61, pp. 3968-3976; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen. Virol, 69, pp. 2939-2952; Tibbles, K. W. Personal observation; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., A region of the infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate (1995) J. Gen. Virol, 76, pp. 3059-3070; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol, 69, pp. 4331-4338","Brown, T.D.K.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QP, United Kingdom",,,0022538X,,JOVIA,"8627718","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030069011
"Jeong Y.S., Repass J.F., Kim Y.-N., Hwang S.-M., Makino S.","57198837031;57186535600;55699505200;36725567100;7403067550;","Coronavirus transcription mediated by sequences flanking the transcription consensus sequence",1996,"Virology","217","1",,"311","322",,28,"10.1006/viro.1996.0118","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029863433&doi=10.1006%2fviro.1996.0118&partnerID=40&md5=329f91a34455cb744701c114a006ae9f","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Biology, College of Arts and Sciences, Kyung-Hee University, Seoul, South Korea","Jeong, Y.S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Biology, College of Arts and Sciences, Kyung-Hee University, Seoul, South Korea; Repass, J.F., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Kim, Y.-N., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Hwang, S.-M., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States","In our studies of murine coronavirus transcription, we continue to use defective interfering (DI) RNAs of mouse hepatitis virus (MHV) in which we insert a transcription consensus sequence in order to mimic subgenomic RNA synthesis from the nondefective genome. Using our subgenomic DI system, we have studied the effects of sequences flanking the MHV transcription consensus sequence on subgenomic RNA transcription. We obtained the following results, (i) Insertion of a 12-nucleotide-long sequence including the UCUAAAC transcription consensus sequence at different locations of the DI RNA resulted in different efficiencies of subgenomic DI RNA synthesis. (ii) Differences in the amount of subgenomic DI RNA were defined by the sequences that flanked the 12-nucleotide-long sequence and were not affected by the location of the 12-nucleotide-long sequence on the DI RNA. (iii) Naturally occurring flanking sequences of intergenic sequences at gene 6-7, but not at genes 1-2 and 2-3, contained a transcription suppressive element(s). (iv) Each of three naturally occurring flanking sequences of an MHV genomic cryptic transcription consensus sequence from MHV gene 1 also contained a transcription suppressive element(s). These data showed that sequences flanking the transcription consensus sequence affected MHV transcription. © 1996 Academic Press, Inc.",,"animal cell; article; controlled study; murine hepatitis coronavirus; nonhuman; priority journal; rna sequence; rna transcription; transcription regulation; Animals; Base Sequence; Cell Line; Consensus Sequence; Defective Viruses; DNA, Viral; Gene Expression Regulation, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Point Mutation; Regulatory Sequences, Nucleic Acid; RNA, Viral; Transcription, Genetic; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Baric, R.S., Shieh, C.K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Compton, S.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., In vitro replication of mouse hepatitis virus strain A59 (1987) J. Virol., 61, pp. 1814-1820; Dveksler, G.S., Pensiero, M.N., Cardellicjio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Diffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Higuchi, R., Recombinant PCR (1990) PCR Protocols, pp. 177-183. , M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White, Eds. Academic Press, San Diego; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforch., 44, pp. 298-302; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effect of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Kim, K.H., Makino, S., Two murine coronavirus genes suffice for viral RNA synthesis (1995) J. 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"Talbot P.J., Paquette J.-S., Ciurli C., Antel J.P., Ouellet F.","7102670281;57214517152;6602358072;7103054531;56962075500;","Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis",1996,"Annals of Neurology","39","2",,"233","240",,84,"10.1002/ana.410390213","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030030561&doi=10.1002%2fana.410390213&partnerID=40&md5=3d26148fef47c81b1dc86ea754a42daf","Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Laboratory of Immunology, Inst. de Rech. Cliniques de Montreal, Montréal, Qué., Canada; Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Qué., Canada; Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Qué. H7N 4Z3, Canada","Talbot, P.J., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada, Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531, boulevard des Prairies, Laval, Qué. H7N 4Z3, Canada; Paquette, J.-S., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Ciurli, C., Laboratory of Immunology, Inst. de Rech. Cliniques de Montreal, Montréal, Qué., Canada; Antel, J.P., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Qué., Canada; Ouellet, F., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada","Multiple sclerosis (MS) is an inflammatory demyelinating neurological disease in which autoreactive T lymphocytes sensitized to myelin components of the central nervous system are postulated to contribute to pathogenesis. The possible relevance of molecular mimicry between a human coronavirus and the myelin basic protein component of myelin in the generation of this autoimmune reaction was evaluated. Myelin basic protein- and virus-reactive T-cell lines were established from 16 MS patients and 14 healthy donors and shown to be mostly CD4+. In contrast to healthy donors, several T-cell lines isolated from MS patients showed cross-reactivity between myelin and coronavirus antigens. Overall, 29% of T-cell lines from MS patients (10 donors) but only 1.3% of T-cell lines from normal control subjects (2 donors) showed an HLA-DR-restricted cross-reactive pattern of antigen activation after in vitro selection with either myelin basic protein or human coronavirus strain 229E antigens. Moreover, reciprocal reactivities were only observed in MS patients (4 donors). This establishes molecular mimicry between a common vital pathogen, such as this human coronavirus, and myelin as a possible immunopathological mechanism in MS and is consistent with the possible involvement of more than one infectious pathogen as an environmental trigger of disease.",,"cd4 antigen; HLA DR antigen; myelin basic protein; virus antigen; adult; antigen presenting cell; article; autoimmunity; clinical article; controlled study; coronavirus; cross reaction; demyelinating disease; female; human; human cell; human tissue; immune response; male; multiple sclerosis; priority journal; t lymphocyte; Adult; Cell Line; Coronavirus; Coronavirus 229E, Human; Cross Reactions; Female; Humans; Male; Middle Aged; Molecular Mimicry; Multiple Sclerosis; Myelin Basic Proteins; Reference Values; T-Lymphocytes","Ffrenchconstant, C., Pathogenesis of multiple sclerosis (1994) Lancet, 343, pp. 271-275; Sadovnick, A.D., Ebers, G.C., Epidemiology of multiple sclerosis - A critical overview (1993) Can J Neurol Sci, 20, pp. 17-29; 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Richert, J.R., Reuben-Burnside, C.A., Deibler, G.E., Kies, M.W., Peptide specificities of myelin basic protein-reactive human T-cell clones (1988) Neurology, 38, pp. 739-742; Inobe, J.-I., Yamamura, T., Kunishita, T., Tabira, T., T lymphocyte lines and clones selected against synthetic myelin basic protein 82-102 peptide from Japanese multiple sclerosis patients (1993) J Neuroimmunol, 46, pp. 83-90; Labrecque, N., McGrath, H., Subramanyam, M., Human T cells respond to mouse mammary tumor virus encoded super-antigen - V-beta restriction and conserved evolutionary features (1993) J Exp Med, 177, pp. 1735-1743; Matzinger, P., Tolerance, danger, and the extended family (1994) Annu Rev Immunol, 12, pp. 991-1045; Selin, L.K., Nahill, S.R., Welsh, R.M., Cross-reactivities in memory cytotoxic T lymphocyte recognition of heterologous viruses (1994) J Exp Med, 179, pp. 1933-1943; Gautam, A.M., Lock, C.B., Smilek, D.E., Minimum structural requirements for peptide presentation by major histocompatibility complex class II molecules - Implications in induction of autoimmunity (1994) Proc Natl Acad Sci USA, 91, pp. 767-771; Wucherpfennig, K.W., Strominger, J.L., Molecular mimicry in T-cell mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein (1995) Cell, 80, pp. 695-705; Wucherpfennig, K.W., Sette, A., Southwood, S., Structural requirements for binding of an immunodominant myelin basic protein peptide to DR2 isotypes and for its recognition by human T cell clones (1994) J Exp Med, 179, pp. 279-290; Riethmuller, A., Kalbus, M., Dubois, E., T-cell-reactivity against CNPase (a minor myelin component) in multiple sclerosis patients and normals (1994) J Neuroimmunol, 54, p. 191; Van Noort, J.M., Van Sechel, A.C., Bajramovic, J.J., The small heat-shock protein αB-crystallin as candidate autoantigen in multiple sclerosis (1995) Nature, 375, pp. 798-801; Panitch, H.S., Influence of infection on exacerbations of multiple sclerosis (1994) Ann Neurol, 36, pp. S25-S28; Duquette, P., Girard, M., Despault, L., Interferon beta-1b is effective in relapsing-remitting multiple sclerosis. I. Clinical results of a multicenter, randomized, double-blind, placebo-controlled trial (1993) Neurology, 43, pp. 655-661; Paty, D.W., Li, D.K.B., Duquette, P., Interferon beta-1b is effective in relapsing-remitting multiple sclerosis. II. MRI analysis results of a multicenter, randomized, double-blind, placebo-controlled trial (1993) Neurology, 43, pp. 662-667; Jacobs, L., Cookfair, D., Rudick, R., Results of a phase III trial of IM recombinant beta interferon as treatment for MS (1994) J Neuroimmunol, 54, p. 170","Talbot, P.J.; Centre de Recherche/Virologie, Institut Armand-Frappier, Universite du Quebec, 531, boulevard des Prairies, Laval, Que. H7N 4Z3, Canada",,,03645134,,ANNED,"8967755","English","ANN. NEUROL.",Article,"Final",Open Access,Scopus,2-s2.0-0030030561
"Méndez A., Smerdou C., Izeta A., Gebauer F., Enjuanes L.","36823007700;6602856664;6602523425;7004526580;7006565392;","Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity",1996,"Virology","217","2",,"495","507",,54,"10.1006/viro.1996.0144","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342902630&doi=10.1006%2fviro.1996.0144&partnerID=40&md5=ad026b85e0b9a01d50c1c4fd798834ba","Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Méndez, A., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Smerdou, C., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Gebauer, F., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Three transmissible gastroenteritis virus (TGEV) defective RNAs were selected by serial undiluted passage of the PUR46 strain in ST cells. These RNAs of 22, 10.6, and 9.7 kb (DI-A, DI-B, and DI-C, respectively) were detected at passage 30, remained stable upon further passage in cell culture, and significantly interfered with helper mRNA synthesis. RNA analysis from purified virions showed that the three defective RNAs were efficiently packaged. Virions of different densities containing either full-length or defective RNAs were sorted in sucrose gradients, indicating that defective and full-length genomes were Independently encapsidated. DI-B and DI-C RNAs were amplified by the reverse transcription-polymerase chain reaction, cloned, and sequenced. DI-B and DI-C genomes are formed by three and four discontinuous regions of the wild-type genome, respectively. DI-C contains 2144 nucleotides (nt) from the 5'-end of the genome, two fragments of 4540 and 2531 nt mostly from gene 1b, and 493 nt from the 3' end of the genome. DI-B and DI-C RNAs include sequences with the pseudoknot motif and encoding the polymerase, metal ion binding, and helicase motifs. DI-B RNA has a structure closely related to DI-C RNA with two main differences it maintains the entire ORF 1b and shows heterogeneity in the size of the 3' end deletion. This heterogeneity maps at the beginning of the S gene, where other natural TGEV recombination events have been observed, suggesting that either a process of template switching occurs with high frequency at this point or that the derived genomes have a selective advantage.",,"animal cell; article; controlled study; Coronavirus; electrophoresis; gene mapping; genetic heterogeneity; nonhuman; Northern blotting; priority journal; swine; virus genome; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Ballesteros, M.L., Sánchez, C.M., Méndez, A., Enjuanes, L., Recombination between transmissible gastroenteritis coronavirus related isolates which differ in tropism and virulence (1995) Adv. Exp. Med. Biol., 380, pp. 557-562; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. 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Virol., 68, pp. 2615-2623; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Kim, K.H., Makino, S., Two murine coronavirus genes suffice for viral RNA synthesis (1995) J. Virol., 69, pp. 2313-2321; Lai, M.M.C., Coronavirus - Organization, replication and expression of genome (1990) Ann. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. 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Virol., 69, pp. 5475-5484; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochemie, 69, pp. 591-600; Roux, L., Simon, A.E., Holland, J.J., Effects of defective interfering viruses on virus replication and pathogenesis in vitro and in vivo (1991) Adv. Virus Res., 40, pp. 181-211; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , (A. D. Leman, B. Straw, W. L. Mengeling, S. D' Allaire, and D. J. Taylor, Eds.), Iowa State Univ. 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Virol., 69, pp. 2939-2952; Spaan, W.H., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Tai, H.T., Smith, C.A., Sharp, P.A., Vinograd, J., Sequence heterogeneity in closed simian virus 40 deoxyribonucleic acid (1972) J Virol., 9, pp. 317-325; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., Degroot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , (S. G. Siddell, Ed.), Plenum, New York; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Zhang, X., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633","Enjuanes, L.; Centro Nacional de Biotecnologia, CSIC, Department of Molecular/Cell Biology, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",,"Academic Press Inc.",00426822,,VIRLA,"8610441","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0342902630
"Chang R.-Y., Brian D.A.","36725275000;7006460232;","cis Requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication",1996,"Journal of Virology","70","4",,"2201","2207",,45,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029872237&partnerID=40&md5=57bbd26678eae73d1d6b141f7c99507a","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan","Chang, R.-Y., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","A naturally occurring 2.2-kb defective interfering (DI) RNA of the bovine coronavirus, structurally a simple fusion of the genomic termini, contains a single contiguous open reading frame (ORF) of 1.7 kb composed of the 5'- terminal 288 nucleotides of polymerase gene 1a and all 1,344 nucleotides of the nucleocapsid protein (N) gene. The ORF must remain open throughout most of its sequence for replication to occur. To determine the qualitative importance of the N portion of the chimeric ORF in DI RNA replication, transcripts of mutated reporter-containing constructs were tested for replication in helper virus-infected cells. It was determined that the N ORF could not be replaced by the naturally occurring internal I protein ORF, accomplished by deleting the first base in the N start codon which leads to a +1 frameshift, nor could it be replaced by the chloramphenicol acetyltransferase ORF. Furthermore, 3'-terminal truncations of the N gene leaving less than 85% of its total length were likewise not tolerated. Small in-frame deletions and in-frame foreign sequence insertions of up to 99 nucleotides within certain regions of the N ORF were tolerated, however, but the rate of DI RNA accumulation in these cases was lower. These results indicate that there is a requirement for translation of most if not all of the N protein in cis for optimal replication of the bovine coronavirus DI RNA and suggest that a similar requirement may exist for viral genome replication.",,"amino acid sequence; article; coronavirus; frameshift mutation; gene deletion; gene insertion; nonhuman; open reading frame; priority journal; rna replication; rna translation; start codon; virus genome; virus nucleocapsid; Base Sequence; Capsid; Cell Line; Cloning, Molecular; Coronavirus, Bovine; Defective Viruses; DNA Repair; DNA-Directed DNA Polymerase; Molecular Sequence Data; Mutagenesis, Insertional; Oligodeoxyribonucleotides; Open Reading Frames; RNA, Viral; Sequence Deletion; Viral Core Proteins; Virus Replication","Ball, L.A., Li, Y., cis-acting requirements for the replication of flock house virus RNA2 (1993) J. 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Virol, 75, pp. 3041-3046; Torczynski, R.M., Fuke, M., Bollon, A.P., Cloning and sequencing of a human 18S ribosomal RNA gene (1985) DNA, 4, pp. 283-291; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J Virol., 65, pp. 3219-3226; Van der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1991) Nucleic Acids Res., 20, pp. 3375-3381; Van der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Weiland, J.J., Dreher, T.W., cis-preferential replication of the turnip yellow mosaic virus RNA genome (1993) Proc Natl. Acad Sci. USA, 90, pp. 6095-6099; White, K.A., Bancroft, J.B., Mackie, G.A., Coding capacity determines in vivo accumulation of a defective RNA of clover yellow mosaic virus (1992) J. Virol., 66, pp. 3069-3076","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States",,,0022538X,,JOVIA,"8642643","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029872237
"Suzuki H., Taguchi F.","7407715967;7103209890;","Analysis of the receptor-binding site of murine coronavirus spike protein",1996,"Journal of Virology","70","4",,"2632","2636",,54,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029918145&partnerID=40&md5=ad57e1413179264de439f2487f0f7c46","National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187, Japan; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Suzuki, H., National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187, Japan, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","It has been found that a domain composed of 330 amino acids of the N terminus of murine coronavirus spike protein [S1N(330)] is involved in receptor-binding activity (H. Kubo, Y. K. Yamada, and F. Taguchi, J. Virol. 68:5403-5410, 1994). To delineate the amino acid sequences involved in receptor-binding activity, we have compared the S1N(330) proteins of seven different mouse hepatitis virus MHV strains that are able to utilize the MHV receptor protein. Three conserved regions (sites I, II, and III) were found to consist of more than 10 identical amino acids, and they were analyzed for receptor-binding activity by site-directed mutagenesis. S1N(330) with a substitution at position 62 from the N terminus of S1 in region I and that with substitutions at positions 212, 214, and 216 in region II showed no receptor-binding activity. The SIN(330) mutants without receptor-binding activity were not able to prevent virus binding to the receptor. These results suggest that the receptor-binding site on SIN(330) is composed of regions located apart from each other in the protein's primary structure, in which Thr at position 62 as well as amino acids located at positions 212, 214, and 216 are particularly important.",,"receptor protein; virus protein; virus receptor; amino acid sequence; animal cell; article; cell strain bhk; controlled study; murine hepatitis coronavirus; nonhuman; priority journal; receptor binding; virus adsorption; virus cell interaction; Amino Acid Sequence; Animals; Base Sequence; Cell Line; Cricetinae; DNA, Viral; Glycoproteins; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Receptors, Virus; Viral Envelope Proteins","De Groot, R.J., Lnytjes, W., Horzinek, M.C., Van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike of coronaviruses (1987) J. Mol. 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Virol., 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen. Virol., 69, pp. 2939-2952; Sturman, L.S., Holmes, K.V., Proteolytic cleavage of peplomer glycoprotein E2 of MHV yields two 90 K subunits and activates cell fusion (1984) Adv Exp. Med Biol., 173, pp. 25-35; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; Taguchi, F., Fleming, J.O., Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein (1989) Virology, 169, pp. 233-235; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J Gen. 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Immunol., 99, pp. 165-200; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yamada, Y.K., Abe, M., Yamada, A., Taguchi, F., Detection of mouse hepatitis virus by the polymerase chain reaction and its application to the rapid diagnosis of infection (1993) Lab. Anim. Sci., 43, pp. 285-290; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinonoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,0022538X,,JOVIA,"8642698","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029918145
"Bos E.C.W., Luytjes W., Van Der Meulen H., Koerten H.K., Spaan W.J.M.","7005778356;6701683324;7003561981;7005962038;7007172944;","The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus",1996,"Virology","218","1",,"52","60",,113,"10.1006/viro.1996.0165","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029947390&doi=10.1006%2fviro.1996.0165&partnerID=40&md5=ea8641c0a0c1e27d1fa3d67faaeff211","Department of Virology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Laboratory for Electron Microscopy, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands","Bos, E.C.W., Department of Virology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Luytjes, W., Department of Virology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Van Der Meulen, H., Laboratory for Electron Microscopy, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Koerten, H.K., Laboratory for Electron Microscopy, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands","We have studied the production and release of infectious DI-particles in vaccinia-T7-polymerase recombinant virus-infected L cells that were transfected with five different plasmids expressing the synthetic DI RNA MIDI-HD and the four structural proteins (M, N, S, and E) of the murine coronavirus MHV-A59. The DI cDNA contains the hepatitis delta ribozyme sequences to generate in the transfected cells a defined 3' end. In EM studies of transfected cells virus-like particles (VLP) were observed in vesicles. Release of the particles into the medium was studied by immunoprecipitations of proteins released into the culture supernatant. Particle release was independent of S or N, but required M and E. Coexpression of E and M was sufficient for particle release. Coexpression of the structural proteins and the MIDI-HD RNA resulted in the production and release of infectious DI-particles. Infectivity of the DI-particles was determined by adding helper virus MHV-A59 to the medium containing the VLPs and using this mixture to infect new L cells. Intracellular RNA of several subsequent undiluted passages was isolated to detect the MIDI-HD RNA. Passage of the MIDI-HD RNA was dependent on the expression of the structural proteins of MHV-A59 in the transfected cells. In the absence of either E or M, MIDI-HD RNA could not be passaged to fresh L cells. We have thus developed a system in which we can produce coronavirus-like particles and an assay to test their infectivity.",,"animal cell; article; controlled study; Coronavirus; gene expression; molecular cloning; mouse; nonhuman; packaging; priority journal; virus assembly; virus infectivity; virus particle","Allison, S.L., Schalich, J., Stiasny, K., Mandl, C.W., Kunz, C., Heinz, F.X., Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH (1995) J. 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Virol., 33, pp. 449-462; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 9OK cleavage fragments (1985) J. Virol., 56, pp. 904-911; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH8.0 and 37C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Suomalainen, M., Liljestrom, P., Garoff, H., Spike protein-nucleocapsid interactions drive the budding of alphaviruses (1992) J. Virol., 66, pp. 4737-4747; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHM variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Tooze, J., Tooze, S.A., Fuller, S.D., Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells (1987) J. Cell Biol., 105, pp. 1215-1226; Tooze, S.A., Tooze, J., Warren, G., Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 (1988) J. Cell Biol., 106, pp. 1475-1487; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for the encapsidation of coronavirus Defective Interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids. Res., 20, pp. 3375-3381; Vennema, H., Heijnen, L., Zjderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins; implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M.C., Spaan, W.J.M., Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system with encephalomyocarditis virus 5′ untranslated region sequences (1991) Gene, 108, pp. 201-210; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virions envelope protein (1994) Virology, 202, pp. 1018-1023","Spaan, W.J.M.; Department of Virology, Leiden University, P.O. Box 320, 2300 AH Leiden, Netherlands",,"Academic Press Inc.",00426822,,VIRLA,"8615041","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0029947390
"Gutzwiller A., Blum J.W.","6701628224;7401777548;","Effects of oral lactose and xylose loads on blood glucose, galactose, xylose, and insulin values in healthy calves and calves with diarrhea",1996,"American Journal of Veterinary Research","57","4",,"560","563",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029970540&partnerID=40&md5=021d57074b4d4f843cf07f8346352554","Swiss Fed. Res. Stn. for Anim. Prod., 1725 Posieux, Switzerland; Division of Nutrition Pathology, Institute for Animal Breeding, University of Berne, Bremgartenstrasse 109a, 3012 Berne, Switzerland","Gutzwiller, A., Swiss Fed. Res. Stn. for Anim. Prod., 1725 Posieux, Switzerland; Blum, J.W., Division of Nutrition Pathology, Institute for Animal Breeding, University of Berne, Bremgartenstrasse 109a, 3012 Berne, Switzerland","Objective - 2 hypotheses were tested: calves with acute, mild diarrhea digest lactose less efficiently than healthy calves, and they are in a catabolic state, which influences plasma glucose concentration after glucose absorption. Design - Clinical study; 2 treatments with 10 repetitions/treatment. Animals - 20 preruminant Brown Swiss and Simmental Red Holstein calves; 10 calves with mild diarrhea, and 10 age-matched healthy calves. Procedure - Blood metabolite and hormone concentrations were determined before and after an oral lactose load. Plasma xylose concentration was determined after an oral xylose load. III calves were tested 1 day after the onset of diarrhea. Results - Calves with diarrhea (cryptosporidia, coronavirus) had lower preprandial concentrations of plasma glucose, insulin-like growth factor I, and 3,5,3'-triiodothyronine (P < 0.01) and a higher concentration of free fatty acids (P = 0.03) than did healthy calves. After the oral lactose and xylose loads, blood galactose and plasma xylose concentrations were lower in ill calves (P = 0.10 and P = 0.07, respectively). In calves with diarrhea, there was a larger increase of plasma glucose concentration (P = 0.12) and a smaller increase of plasma insulin concentration (P = 0.04) above baseline values after lactose ingestion. Conclusions - Lactose digestion is slightly impaired in calves with mild diarrhea. Calves with acute diarrhea are in a catabolic state and, therefore, respond with a larger increase of plasma glucose concentration to a given amount of absorbed glucose than do healthy calves. Clinical relevance - Plasma glucose concentration is not a reliable measure for glucose absorption in animals that are in a catabolic state.",,"galactose; glucose; insulin; lactose; liothyronine; somatomedin; xylose; article; cattle; controlled study; diarrhea; glucose blood level; insulin blood level; nonhuman; oral drug administration; veterinary medicine; Acute Disease; Administration, Oral; Animals; Blood Glucose; Cattle; Cattle Diseases; Diarrhea; Female; Galactosemias; Insulin; Lactose; Male; Reference Values; Time Factors; Xylose","Heath, S.E., Naylor, J.M., Guedo, B.L., The effects of feeding milk to diarrheic calves supplemented with oral electrolytes (1989) Can J Vet Res, 53, pp. 477-485; Landsverk, T., An enzyme histochemical investigation of the intestinal mucosa in diarrheic calves (1981) Acta Vet Scand, 22, pp. 449-458; Tzipori, S., Smith, M., Halpin, C., Experimental cryptosporidiosis in calves, clinical manifestations and pathological findings (1983) Vet Rec, 112, pp. 116-120; Coombe, N.B., Smith, R.H., Absorption of glucose and galactose and digestion and absorption of lactose by the preruminant calf (1973) Br J Nutr, 30, pp. 331-344; Hammond, J.B., Littmann, A., Disaccharide malabsorption (1985) Bockus Gastroenterology Vol 3 4th Ed., 3, pp. 1703-1718. , Berk JE, ed Philadelphia: WB Saunders Co; St Jean, G.D., Rings, D.M., Schmall, L.M., Jejunal mucosal lactase activity from birth to 3 weeks in conventionally raised calves (1989) Am J Vet Res, 50, pp. 1496-1498; Ferguson, A., Paul, G., Snodgrass, D.R., Lactose tolerance in lambs with rotavirus diarrhoea (1981) Gut, 22, pp. 114-119; Youanes, Y.D., Herdt, T.H., Changes in small intestinal morphology and flora associated with decreased energy digestibility in calves with naturally occurring diarrhea (1987) Am J Vet Res, 48, pp. 719-725; Vacher, P.Y., Schmitz, M., Hirni, H., Concentration plasmatique postprandiale de 3-methylhistidine, comparée à celle de lysine, d'homoarginine et de xylose dans des conditions normales et en cas de malabsorption chez le veau prēruminant (1990) Reprod Nutr Dev, 30, pp. 471-482; Blum, J.W., Schnyder, W., Kunz, P.L., Reduced and compensatory growth: Endocrine and metabolic changes during energy restriction and realimentation in steers (1985) J Nutr, 115, pp. 417-425; Hostettler-Allen, R., Tappy, L., Blum, J.W., Insulin resistance, hyperglycemia and glucosuria in intensively milk-fed calves (1994) J Anim Sci, 72, pp. 160-173; Kinsbergen, M., Sallmann, H.P., Blum, J.W., Metabolic, endocrine and haematological changes in 1-week-old calves after milk intake, in response to fasting and during total parenteral nutrition (1994) J Vet Med A, 41, pp. 268-282; Holland, R.E., Herdt, T.H., Refsal, K.R., Pulmonary excretion of H2 in calves with Cryptosporidium-induced malabsorption (1989) Dig Dis Sci, 34, pp. 1399-1404; Nappert, G., Hamilton, D., Petrie, L., Determination of lactose and xylose malabsorption in preruminant diarrheic calves (1993) Can J Vet Res, 57, pp. 152-158; Cole, N.A., Hallford, D.M., Gallavan, R., Influence of a glucose load in fed or unfed lambs on blood metabolites and hormone patterns (1993) J Anim Sci, 71, pp. 765-773; Hill, F.W., Kidder, D.E., The oral glucose tolerance test in canine pancreatic malabsorption (1972) Br Vet J, 128, pp. 207-214; Schonfeld, W.B., Kalser, M.H., Tests related to the small intestine (1985) Bockus Gastroenterology. Vol 1 4th Ed., 1, pp. 378-387. , Berk JE, ed Philadelphia. WB Saunders Co; Krishna, G.G., Steigerwalt, S.P., Pikus, R., Hypokalemic states (1994) Maxwell and Kleeman's Clinical Disorders of Fluid and Electrolyte Metabolism. 5th Ed., pp. 659-696. , Narins RG, ed. New York: McGraw-Hill Book Co; Whitlock, R.H., Diarrhea in cattle (1992) Veterinary Gastroenterology. 2nd Ed, pp. 755-803. , Anderson NV, ed. Philadelphia: Lea & Febiger; Newcomer, A.D., McGill, D.B., Thomas, P.J., Prospective comparison of indirect methods for detecting lactase deficiency (1975) N Engl J Med, 293, pp. 1232-1235; Holmes, M.A., Arthur, P.G., Hartmann, P.E., Changes in the concentrations of glucose and galactose in the peripheral blood of sucking piglets (1990) J Dairy Res, 57, pp. 331-337; De Vrese, M., Keller, B., Barth, C.A., Enhancement of intestinal hydrolysis of lactose by microbial β-galactosidase (EC 3.2.1.23) of kefir (1992) Br J Nutr, 67, pp. 67-75; Kaempf, J.W., Li, H., Groothuis, J.R., Galactose, glucose, and lactate concentrations in the portal venous and arterial circulations of newborn lambs after nursing (1988) Pediatr Res, 23, pp. 598-602; Kaempf, J.W., Battaglia, F.C., Sparks, J.W., Galactose clearance and carbohydrate metabolism across the gastrointestinal tract in the newborn lamb (1990) Metabolism, 39, pp. 698-703; Cornelius, C.E., A review of new approaches to assessing hepatic function in animals (1987) Vet Res Commun, 11, pp. 423-441; Sherlock, S., Assessment of liver function (1989) Diseases of the Liver and Biliary System. 8th Ed, pp. 19-35. , Oxford, England. Blackwell Scientific Publications","Gutzwiller, A.; Swiss Federal Research Station, Animal Production, 1725 Posieux, Switzerland",,,00029645,,AJVRA,"8712525","English","AM. J. VET. RES.",Article,"Final",,Scopus,2-s2.0-0029970540
"Krishnan R., Chang R.-Y., Brian D.A.","36943098500;36725275000;7006460232;","Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the downstream-most initiation site",1996,"Virology","218","2",,"400","405",,36,"10.1006/viro.1996.0210","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029946796&doi=10.1006%2fviro.1996.0210&partnerID=40&md5=16817bac9d37ae64f4970934be6594ab","Laboratory of Molecular Microbiology, Natl. Inst. Allerg. and Infect. Dis., National Institutes of Health, Bethesda, MD 20892, United States; Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Krishnan, R., Laboratory of Molecular Microbiology, Natl. Inst. Allerg. and Infect. Dis., National Institutes of Health, Bethesda, MD 20892, United States, Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Chang, R.-Y., Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Insertion of the 17-nucleotide promoter region for the bovine coronavirus N gene as part of a 27-nucleotide cassette into the open reading frame of a cloned synthetic defective-interfering (DI) RNA resulted in synthesis of subDI RNA transcripts from the replicating DI RNA genome. Duplicating and triplicating the promoter sequence in tandem caused a progressive increase in the efficiency of subgenomic mRNA synthesis despite a concurrent decrease in the rate of DI RNA accumulation that was not specific to the promoter sequences being added. Although initiation of transcription (leader fusilon) occurred at each of the three promoter sites in the tandem construct, almost all of the transcripts were found as a product of the most downstream (3'-most on the genome) promoter. These results show that enhancement of subgenomic mRNA synthesis is a property that can reside within sequence situated near the promoter. A possible role for the plus strand in the downstream promoter choice is suggested.",,"messenger RNA; transcription factor; article; Coronavirus; gene insertion sequence; genome; messenger RNA synthesis; nonhuman; priority journal; promoter region","Hofmann, M.A., Sethna, P.B., Brian, D.A., (1990) J. Virol., 64, pp. 4108-4114; Lai, M.M.C., (1990) Annu. Rev. 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Virol., 64, pp. 1050-1056; Sethna, P.B., Hung, S.-L., Brian, D.A., (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Sethna, P.B., Hofmann, M.A., Brian, D.A., (1991) J. Virol., 65, pp. 320-325; Brian, D.A., Chang, R.-Y., Sethna, P.B., Hofmann, M.A., (1993) Arch. Virol. Suppl., 9, pp. 173-180. , ""Positive-Strand RNA Viruses"" (M. A. Britton, C. H. Calisher, and R Reuckert, Eds.); Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., (1994) J. Virol., 68, pp. 8223-8231; Eisenberg, R.J., Long, D., Hogue-Angeletti, R., Cohen, G.H., (1984) J. Virol., 49, pp. 265-268; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning, , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY; Hofmann, M.A., Chang, R.-Y., Ku, S., Brian, D.A., (1993) Virology, 196, pp. 163-171; Hofmann, M.A., Brian, D.A., (1991) PCR Methods Appl., 1, pp. 43-45; Hofmann, M.A., Senanayake, S.D., Brian, D.A., (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 11733-11737; Makino, S., Stohlman, S., Lai, M.M.C., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 4204-4208; Hogue, B.G., King, B., Brian, D.A., (1984) J. Virol., 51, pp. 384-388; Lapps, W., Hogue, B.H., Brian, D.A., (1987) Virology, 157, pp. 47-57; La Monica, N., Yokomori, K., Lai, M.M.C., (1992) Virology, 188, pp. 402-407; Makino, S., Soe, L.H., Shieh, C.-K., Lai, M.M.C., (1988) J. Virol., 62, pp. 3870-3873; Shieh, C.-K., Lee, H.-J., Yokomori, K., La Monica, N., Lai, M.M.C., (1989) J. Virol., 63, pp. 3729-3736; Joo, M., Makino, S., (1995) J. Virol., 69, pp. 272-280; Van Der Most, R.G., DeGroot, R.J., Spaan, W.J.M., (1994) J. Virol., 68, pp. 3656-3666; Sethna, P.B., Brian, D.A., unpublished data; Schaad, M.C., Baric, R.S., (1993) J. Virol., 68, pp. 8169-8179; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., (1988) J. Virol., 62, pp. 4280-4287; Furuya, T., Lai, M.M.C., (1993) J. Virol., 67, pp. 7215-7222; Stohlman, S.A., Baric, R.S., Nelson, G.W., Soe, L.H., Welter, L.M., Deans, R.J., (1988) J. Virol., 62, pp. 4288-4295; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., (1986) Virology, 150, pp. 402-410; Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., (1993) EMBO J., 12, pp. 3587-3598; Harris, K.S., Xiang, W., Alexander, L., Lane, W.S., Paul, A.V., Wimmer, E., (1994) J. Biol. Chem., 269, pp. 27004-27014; Chang, R.-Y., Krishnan, R., Brian, D.A., J. Virol., 70 (5). , in press; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., (1995) J. Virol., 69, pp. 6219-6227","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0854, United States",,"Academic Press Inc.",00426822,,VIRLA,"8610468","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0029946796
"Vennema H., Godeke G.-J., Rossen J.W.A., Voorhout W.F., Horzinek M.C., Opstelten D.-J.E., Rottier P.J.M.","7003697291;6603099700;7005977394;7003796069;7102624836;7003742658;7006145490;","Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes",1996,"EMBO Journal","15","8",,"2020","2028",,274,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029933250&partnerID=40&md5=0509e16d3aef4460159e0b8e65ca85d8","Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands; Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands; Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Center for Biotechnology, Karolinska Institute, Novum, 141 57 Huddinge, Sweden","Vennema, H., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands; Godeke, G.-J., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands; Rossen, J.W.A., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands; Voorhout, W.F., Department of Functional Morphology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands; Opstelten, D.-J.E., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands, Center for Biotechnology, Karolinska Institute, Novum, 141 57 Huddinge, Sweden; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Division of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Division of Virology, PO Box 80.165, 3508 TD Utrecht, Netherlands","Budding of enveloped viruses has been shown to be driven by interactions between a nucleocapsid and a proteolipid membrane. By contrast, we here describe the assembly of viral envelopes independent of a nucleocapsid. Membrane particles containing coronaviral envelope proteins were assembled in and released from animal cells co-expressing these proteins' genes from transfected plasmids. Of the three viral membrane proteins only two were required for particle formation, the membrane glycoprotein (M) and the small envelope protein (E). The spike (S) protein was dispensable but was incorporated when present. Importantly, the nucleocapsid protein (N) was neither required nor taken into the particles when present. The E protein, recently recognized to be a structural protein, was shown to be an integral membrane protein. The envelope vesicles were found by immunogold labelling and electron microscopy to form a homogeneous population of spherical particles indistinguishable from authentic coronavirions in size (~ 100 nm in diameter) and shape. They were less dense than virions and sedimented slightly slower than virions in sucrose velocity gradients. The nucleocapsid-independent formation of apparently bona fide viral envelopes represents a novel mode of virus assembly.","Budding; Coronavirus; Envelope protein; Virus assembly; Virus-like particle","membrane protein; structural protein; virus envelope protein; animal cell; article; controlled study; coronavirus; electron microscopy; gene expression; immunogold staining; nonhuman; plasmid; priority journal; virion; virus assembly; virus envelope; virus gene; virus nucleocapsid; virus particle; Animals; Capsid; Cell Line; Gene Expression; Genes, Viral; Membrane Glycoproteins; Mice; Microscopy, Electron; Models, Biological; Murine hepatitis virus; Viral Envelope Proteins","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Allison, S.L., Stadler, K., Mandl, C.W., Kunz, C., Heinz, F.X., Synthesis and secretion of recombinant tick-borne encephalitis virus protein e in soluble and particulate form (1995) J. 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"Parwani A.V., Lucchelli A., Saif L.J.","7004273180;7003729751;7102226747;","Identification of group B rotaviruses with short genome electropherotypes from adult cows with diarrhea",1996,"Journal of Clinical Microbiology","34","5",,"1303","1305",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029918879&partnerID=40&md5=cee25e7a404b08c22a65b59d2697df13","Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","Parwani, A.V., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Lucchelli, A., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","Two held strains (BB-RVLV and KD) of group B rotaviruses from adult dairy cows with diarrhea displayed short genome electropherotypes. Gnotobiotic calves inoculated with fecal filtrates of each group B rotavirus developed diarrhea, and only group B rotaviruses or antigens were detected in the feces by immunoelectron microscopy and in intestinal epithelial cells by immunofluorescent staining, respectively. The feces or intestinal contents of the cows and inoculated calves were negative for group A and C rotaviruses by enzyme-linked immunosorbent assay, immunoelectron microscopy, or cell culture immunofluorescence assays. Comparison of the genome electropherotypes of the calf-passaged BB-RVLV and KD strains with the original samples and reference bovine group A, B, and C rotaviruses revealed conservation of their short- genome electropherotypes and double-stranded RNA migration patterns characteristic of group B rotaviruses. To our knowledge, our previous study (L. J. Saif, K. V. Brock, D. R. Redman, and E. M. Kohler, Vet. Rec. 128:447- 449, 1991) and this report are the first description of bovine group B rotaviruses (in a mixed infection with bovine coronavirus or singly in fecal contents) in adult cows with diarrhea and this is the first report of short- genome electropherotypes among group B rotaviruses.",,"article; cattle; dairy industry; diarrhea; electrophoresis; enzyme linked immunosorbent assay; epithelium cell; nonhuman; priority journal; rotavirus; strain difference; virus capsid; virus characterization; virus genome; Animals; Cattle; Cattle Diseases; Diarrhea; Electrophoresis; Evaluation Studies; Genome, Viral; Microscopy, Electron; RNA, Double-Stranded; RNA, Viral; Rotavirus; Rotavirus Infections; Virology","Allen, S., Mitchell, J., Jones, W., Quinn, M., A novel bovine rotavirus electrophelotype from outbreaks of neonatal diarrhea in Utah beef herds (1989) J. Vet. Diagn. Invest., 1, pp. 74-75; Bridger, J.C., Novel rotaviruses in animals and man (1987) Novel Diarrhoea Viruses John Wiley and Sons, pp. 5-24. , G. Bock and J. Whelan (ed.), Chichester, United Kingdom; Chasey, L., Banks, J., The commonest rotaviruses from neonatal lamb diarrhoea in England and Wales have atypical electropherotypcs (1984) Vet Rec., 115, pp. 326-327; Estes, M.K., Cohen, J., Rotavirus gene structure and function (1989) Microbiol. Rev, 53, pp. 410-449; Kapikian, A.Z., Chanock, R.M., Rotaviruses (1990) Virology, 2nd Ed, pp. 1353-1404. , B. M. Fields and D. M Knipe (ed), Raven Press, New York; Parwani, A.V., Hussein, H.A., Rosen, B.I., Lucchelli, A., Navarro, L., Saif, L.J., Characterization of field strains of group A bovine rotaviruses by using polymerase chain reaction-generated G and P type-specific cDNA probes (1993) J. Clin. Microbiol, 31, pp. 2010-2015; Parwani, A.V., Munoz, M., Tsunemitsu, H., Lucchclli, A., Saif, L.J., Molecular and serologic characterization of a group A bovine rotavirus with a short genome pattern (1995) J. Vet. Diagn. Invest, 7, pp. 255-261; Paul, P.S., Lyoo, Y.S., Woode, G.N., Zheng, S., Greenberg, H.B., Matsui, S., Schwartz, K.J., Hill, H.T., Isolation of a bovine rotavirus with a super-short RNA electropherotypic pattern from a calf with diarrhea (1988) J Clin. Microbiol., 26, pp. 2139-2143; Penaranda, M.E., Ho, M.S., Fang, Z.Y., Dong, H., Bai, X.S., Duan, S.C., Ye, W.W., Glass, R.I., Seroepidemiology of adult diarrhea rotavirus in China, 1977-1987 (1989) J. Clin. Microbiol, 27, pp. 2180-2183; Pocock, D.H., Isolation and characterization of two group A rotaviruses with unusual genome profiles (1987) J. Gen Virol, 68, pp. 653-660; Saif, L.J., Non group A rotaviruses (1990) Viral Diarrheas of Man and Animals, pp. 73-95. , L. J. Saif and K. W. Theil (ed.), CRC Press, Boca Raton, Fla; Saif, L.J., Bovine rotavirus (1991) Diagnostic Veterinary Virology: A Practitioner's Guide, pp. 126-130. , A. E. Castro and W. P. Heuschele (ed.), Williams and Wilkins Baltimore; Saif, L.J., Unpublished data; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am. J. Vet. Res, 38, pp. 13-20; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds' electron microscopic and serological evidence for an association with coronavirus infections in affected cows (1991) Vet. Rec, 128, pp. 447-449; Saif, L.J., Jiang, B.M., Nongroup A rotaviruses (1994) Curr. Top. Microbiol Immunol., 185, pp. 339-371; Saif, L.J., Redman, D.R., Smith, K.L., Theil, K.W., Passive immunity to bovine rotavirus in newborn calves fed colostrum supplements from immunized or nonimmunized cows (1983) Infect. Immun., 41, pp. 1118-1131; Saif, L.J., Redman, D.R., Theil, K.W., Experimental coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J. Vet. Res., 47, pp. 1426-1432; Saif, L.J., Rosen, B.I., Rang, S.Y., Miller, K.L., Cell culture propagation of rotaviruses (1988) J. Tissue Culture Methods, 11, pp. 147-156; Saif, L.J., Rosen, B.I., Parwani, A.V., Animal rotaviruses (1994) Viral Infections of the Gastrointestinal Tract, 2nd Ed, pp. 289-314. , A. Z Kapikian (ed.), Marcel Dekker, New York; Scott, G.E., Tarlow, O., McCrae, M.A., Detailed structural analysis of a genome rearrangement in bovine rotavirus (1989) Virus Res, 14, pp. 119-128; Theil, K.W., Group A rotaviruses (1990) Viral Diarrheas of Man and Animals, pp. 35-72. , L. J. Saif and K. W. Theil (ed.), CRC Press, Boca Raton, Fla; Theil, K.W., Grooms, D.L., McCloskey, C.M., Redman, U.R., Group B rotavirus associated with an outbreak of neonatal lamb diarrhea (1995) J. Vet. Diagn. Invest., 7, pp. 148-150; Theil, K.W., McCloskey, C.M., Partial characterization of a bovine group A rotavirus with a short genome electropherotype (1988) J. Clin. Microbiol., 26, pp. 1094-1099; Tsunemitsu, H., Saif, L.J., Jiang, B., Shimizu, M., Hiro, M., Yamaguchi, H., Ishiyama, T., Hirai, T., Isolation, characterization, and serial propagation of a bovine group C rotavirus in a monkey kidney cell line (MA104) (1991) J. Clin. Microbiol., 29, pp. 2609-2613","Saif, L.J.; Food Animal Health Research Program, Ohio Agricultural Res./Devt. Center, Ohio State University, Wooster, OH 44691, United States",,,00951137,,JCMID,"8727926","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0029918879
"Storz J., Stine L., Liem A., Anderson G.A.","7006694594;6701699357;7006066946;7404223734;","Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping",1996,"Journal of the American Veterinary Medical Association","208","9",,"1452","1455",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030137216&partnerID=40&md5=2228ba86e56483928e1716bc587e04ec","Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Research and Development Center, Sanofi Animal Health Inc., Lenexa, KS 66285, United States; Immtech Biologies Inc., Bucyras, KS 66013, United States","Storz, J., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States, Immtech Biologies Inc., Bucyras, KS 66013, United States; Stine, L., Research and Development Center, Sanofi Animal Health Inc., Lenexa, KS 66285, United States, Immtech Biologies Inc., Bucyras, KS 66013, United States; Liem, A., Research and Development Center, Sanofi Animal Health Inc., Lenexa, KS 66285, United States, Immtech Biologies Inc., Bucyras, KS 66013, United States; Anderson, G.A., Research and Development Center, Sanofi Animal Health Inc., Lenexa, KS 66285, United States, Immtech Biologies Inc., Bucyras, KS 66013, United States","Objective - To monitor the prevailing viral respiratory tract infections in cattle after transportation to feedlots. Animals - 100 cattle with signs of respiratory tract disease on arrival at 2 feedlots. Procedures - Nasal swab samples were obtained from each animal and were used for inoculation of defined cell culture systems that detected bovine viruses known to cause respiratory tract infections, as well as viruses previously not recognized as respiratory pathogens for cattle. Results - Bovine respiratory coronaviruses were isolated from 38 of the 100 cattle, including 6 of 50 cattle from California, 22 of 31 cattle from Oklahoma, 6 of 11 cattle from Texas, and 4 of 8 cattle of unknown origin. Parainfluenza 3 viruses also were isolated from 4 California cattle, but other bovine viruses were not detected. Clinical Implications - The high rate of coronavirus isolations from feedlot cattle with signs of respiratory tract disease implied wide distribution and high susceptibility among cattle to this infection, which had not been detected by use of viral isolation systems in previous etiologic evaluations of feedlot cattle affected with bovine respiratory disease complex.",,"animal; animal disease; article; cattle; cattle disease; cell line; Coronavirus; isolation and purification; nose mucosa; prevalence; respiratory tract infection; traffic and transport; United States; virology; virus infection; Animals; Arizona; California; Cattle; Cattle Diseases; Cell Line; Coronavirus; Coronavirus Infections; Kansas; Nasal Mucosa; Oklahoma; Prevalence; Respiratory Tract Infections; Texas; Transportation","Hoerlein, A.B., Shipping fever (1980) Bovine Medicine and Surgery, pp. 99-160. , Amstutz HE, ed. Santa Barbara, Calif: American Veterinary Publications Inc; Madin, S.H., York, C.F., McKercher, D.G., Isolation of the infectious bovine rhinotracheitis virus (1956) Science, 124, pp. 721-722; McKercher, D.G., Moulton, J.E., Madin, S.H., Infectious bovine rhinotracheitis - A newly recognized virus disease of cattle (1957) Am J Vet Res, 18, pp. 246-256; Reismger, R.C., Heddleston, K.L., Manthei, C.A., A myxovirus (SF-4) associated with shipping fever of cattle (1959) J Am Vet Med Assoc, 135, pp. 147-154; Rosenquist, B.D., Isolation of respiratory syncytial virus from calves with acute respiratory disease (1974) J Infect Dis, 130, pp. 177-182; Ciszewski, D.K., Baker, J.C., Slocombe, R.F., Experimental reproduction of respiratory tract disease with bovine respiratory syncynal virus (1991) Vet Microbiol, 28, pp. 39-60; Potgieter, L.N.D., McCracken, M.D., Hopkins, F.M., Experimental production of bovine respiratory tract disease with bovine viral diarrhea virus (1984) Am J Vet Res, 43, pp. 1582-1585; Potgieter, L.N.D., Current concepts on the role of viruses in respiratory tract disease of cattle (1977) Bovine Pract, 12, pp. 75-81; Tompkins, W.A.T., Watrach, A.M., Schmale, J.D., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 904-911; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Laporte, J., Bobulesco, P., Rossi, F., Une lignee particulierement sensible a la replication du coronavirus enteritique bovin. les cellules HRT-18 (1980) CR Acad Sci III, 290 D, pp. 623-626; St Cyr-Coats, K., Payne, H.R., Storz, J., The influence of the host cell and trypsin treatment on bovine coronavirus infectivity (1988) Zentralbl Veterinarmed [B], 35, pp. 752-759; Dea, S., Garzon, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (bluecomb) coronaviruses in a continuous human rectal adenocarcinoma cell line (1989) Am J Vet Res, 50, pp. 1310-1318; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Zhang, X.M., Herbst, W., Kousoulas, K.G., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 4, pp. 152-161; Payne, H.R., Storz, J., Scanning electron microscopic characterization of bovine coronavirus plaques (1990) Zentralbl Veterinarmed [B], 37, pp. 501-508; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; St Cyr-Coats, K., Storz, J., Bovine coronavirus-induced cytopathic expression and plaque formation, host cell and virus strain determine trypsin dependence (1988) Zentralbl Veterinarmed [B], 35, pp. 48-56; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Mebus, C.A., Stair, E.L., Rhodes, M.B., Neonatal calf diarrhea: Propagation, attenuation and characteristics of coronavirus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentry in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet Rec, 123, pp. 300-301; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Mostl, K., Burki, F., Ursāchliche Beteiligung boviner Coronaviren an respiratorischen Krankheitsausbrūchen bei Kālbern und pathogenetisch-immunologische Ūberlegungen hierzu (1988) Dtsch Tierārztl Wothenschr, 95, pp. 19-22; Herbst, W., Klatt, E., Schliesser, T., Serologisch-diagnostische Untersuchungen zum Vorkommen von Coronavirusinfektionen bei Atemwegserkrankungen des Rindes (1989) Berl Munch Tierarztl Wochenschr, 102, pp. 129-131; Heckert, R.A., Saif, L.J., Hoblet, K.H., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet Microbiol, 22, pp. 187-201; Thomas, L.H., Gourlay, R.N., Stott, E.J., A search for new microorganisms in calf pneumonia by inoculation of gnotobiotic calves (1982) Res Vet Sci, 33, pp. 170-182; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; McNulty, M.S., Bryson, D.G., Allan, G.M., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-434; Jiminez, C., Herbst, W., Biermann, U., Isolierung von Coronaviren in der Zellkultur aus Nasentupferproben atemwegskranker Kalber in der Bundesrepublik Deutschland (1989) Zentralbl Veterinarmed [B], 36, pp. 635-638; Kapil, S., Pomeroy, K.A., Goyal, S.A., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J Vet Diagn Invest, 3, pp. 88-89; Tsunemitsu, H., Yenemichi, T., Hirai, T., Isolation of bovine coronavirus from, feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437","Storz, J.; Immtech Biologies Inc., Bucyras, KS 66013, United States",,,00031488,,JAVMA,"8635997","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0030137216
"Sestak K., Lanza I., Park S.-K., Weilnau P.A., Saif L.J.","6701814572;6701643399;7501833051;6507477894;7102226747;","Contribution of passive immunity to porcine respiratory coronavirus to protection against transmissible gastroenteritis virus challenge exposure in suckling pigs",1996,"American Journal of Veterinary Research","57","5",,"664","671",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030147183&partnerID=40&md5=acdaee87cc3703467e327ed41076bc39","Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","Sestak, K., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Lanza, I., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Park, S.-K., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Weilnau, P.A., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","Objective - To determine the ability of porcine respiratory coronavirus (PRCV) infections to induce passive immunity in suckling pigs to transmissible gastroenteritis virus (TGEV) challenge exposure. Design and Animals - 4 TGEV seronegative sows and their litters (group A) served as controls, whereas 2 other groups (B and C) of sows (also TGEV seronegative) were oronasally inoculated with live PRCV during 1 or 2 subsequent pregnancies, respectively. Procedure - Effectiveness of passive immunity provided to pigs via colostrum and milk was assessed after TGEV challenge exposure, and TGEV antibody responses in colostrum and milk were analyzed. Results - Mortality in the 3 groups of young pigs correlated with seventy of clinical signs of TGEV infection and was highest in control litters (86% in group-A pigs) and lowest in litters of sows inoculated with PRCV in 2 subsequent pregnancies (14% in group-C pigs). Virusneutralization and IgA and IgG TGEV antibody titers of milk collected from sows at challenge exposure had significant positive correlation with litter survival. Significantly higher numbers of TGEV-speciftc IgA and IgG antibody-secreting cells were found in group-A pigs than in group-C pigs, suggesting that high titer of maternal antibodies (induced in group-C sows multiply exposed to PRCV) may interfere with active antibody responses. Conclusions and Clinical Relevance - Results suggest that, in PRCV-infected pig herds, multiple exposures of pregnant sows are associated with higher IgA and IgG antibody titers to TGEV in milk, and these titers contribute to protection against TGEV infection.",,"immunoglobulin A; immunoglobulin G; virus antibody; virus antigen; animal; animal disease; article; colostrum; Coronavirus; enzyme linked immunosorbent assay; female; immunology; milk; passive immunization; pregnancy; suckling; swine; swine disease; Transmissible gastroenteritis virus; virus infection; Animals; Animals, Suckling; Antibodies, Viral; Antigens, Viral; Colostrum; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Female; Gastroenteritis, Transmissible, of Swine; Immunity, Maternally-Acquired; Immunoglobulin A; Immunoglobulin G; Milk; Pregnancy; Swine; Swine Diseases; Transmissible gastroenteritis virus","Doyle, L.P., Hutchings, L.M., A transmissible gastroenteritis in pigs (1946) J Am Vet Med Assoc, 108, pp. 257-259; Bohl, E.H., Transmissible gastroenteritis virus (1989) Virus Infections of Parcines, pp. 139-153. , Pensacrt MB, ed. Amsterdam: Elsevier Publishers BV; Laude, H., Van-Recth, K., Pensaert, M., Porcine respiratory coronavirus molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Lanza, I., Shoup, D.I., Saif, L.J., Lactogenic immunity and milk antibody isotypes to transmissible gastroenteritis virus in sows exposed to porcine respiratory coronavirus during pregnancy (1995) Am J Vet Res, 56, pp. 739-748; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Hill, H., Biwer, J., Woods, R.D., Porcine respiratory coronavirus isolated from two US swine herds (1990) Proceedings Am Assoc Swine Pract, pp. 333-335; Wesley, R.D., Woods, R.D., Hill, H.T., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; Cox, E., Pensaert, M., Hooyberghs, J., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Coronaviruses and Their Diseases, pp. 429-433. , Cavanagh D, Brown TDK, eds New York Plenum Press; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine 7th Ed, pp. 362-386. , Leman AD, Straw B, Mengeling W, et al, eds. Ames, Iowa: Iowa State University Press; Van-Cott, J.L., Brim, T.A., Lunney, J.K., Contribution of antibody secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J Immunol, 152, pp. 3980-3990; Welch, S.K.W., Saif, L.J., Ram, S., Cell-mediated immune responses of suckling pigs inoculated with attenuated or virulent transmissible gastroenteritis virus (1988) Am J Vet Res, 49, pp. 1228-1234; Bernard, S., Bottreau, E., Aynaud, J.M., Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis (1989) Vet Microbiol, 21, pp. 1-8; Van Nieuwstadt, A.P., Zetstra, T., Boonstra, J., Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet Rec, 125, pp. 58-60; Paton, D.J., Brown, I.H., Sows infected in pregnancy with porcine respiratory coronavirus show no evidence of protecting their suckling piglets against transmissible gastroenteritis (1990) Vet Res Commun, 14, pp. 329-337; DeDiego, M., Laviada, M.D., Enjuanes, L., Epitope sensitivity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J Virol, 66, pp. 6502-6508; Welter, M.W., Horstman, M.P., Welter, C.J., An overview of successful TGEV vaccination strategies and discussion on the interrelationship between TGEV and PRCV (1993) Adv Exp Med Biol, 342, pp. 463-468; Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-273; Wesley, R.D., Woods, R.D., Immunization of pregnant gilts with PRCV induces lactogenic immunity for protection of nursing piglets from challenge with TGEV (1993) Vet Microbiol, 38, pp. 31-40; Callebaut, P., Cox, E., Pensaert, M., Induction of milk IgA antibodies by porcine respiratory coronavirus infection (1990) Cotonaviruses and Their Diseases, pp. 421-428. , Cavanagh D, Brown TDK, eds. New York: Plenum Press; Wesley, R.D., Woods, R.D., Hill, H.T., Evidence for a poicine respiratory coronavirus antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; Simkins, R.A., Weilnau, P.A., Van Coll, J., Competition ELISA, using monoclonal antibodies to the transmissible gastroenteritis virus (TGEV) S protein, for serologic differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am J Vet Res, 54, pp. 254-259; Van-Cott, J.L., Brim, T.A., Simkins, R.A., Isotype-specific antibody secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J Immunol, 150, pp. 3990-4000; Simkins, R.A., Saif, L.J., Weilnau, P.A., Epitope mapping and the detection of transmissible gastroenteritis viral proteins in cell culture using biotinylated monoclonal antibodies in a fixed-cell ELISA (1989) Arch Virol, 107, pp. 179-190; Bohl, E.H., Gupta, R.K.P., Olquin, M.V.F., Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect Immun, 6, pp. 289-301; Lanza, I., Rubio, P., Munoz, M., Comparison of a monoclonal antibody capture ELISA (MACELISA) to indirect ELISA and virus neutralization test for the serodiagnosis of transmissible gas-troenteritis virus (1993) J Vet Diagn Invent, 5, pp. 21-25; Saif, L.J., Jackwood, D.J., Enteric virus vaccines: Theoretical considerations, current status, and future approaches (1990) Viral Diariheas of Man and Animals, pp. 313-329. , Saif LJ, Theil KW, eds Boca. Raton, Fla CRC Press Inc; Nandapalan, N., Taylor, R., Scott, R., Mammary immunity in mothers of infants with respiratory syncytial virus infection (1987) J Med Virol, 22, pp. 277-287; McGhoe, J.R., Mestecky, J., Dertzbaugh, H.T., The mucosal immune system from fundamental concepts to vaccine development (1992) Vaccine, 10, pp. 75-88; Sminia, M.Z., Structure and function of bronchus-associated lymphoid tissue (BALT) (1989) Critical Reviews in Immunology, pp. 118-150. , Amos DB, Bachrach HL, eds. Boca Raton, Fla: CRC Press Inc; Rudzik, R., Clancy, R.L., Percy, D.E., Repopulation with IgA-containing cells of bronchial and intestinal lamina propria after transfer of homologous Peyer's patches and bronchial lymphocytes (1975) J Immunol, 114, pp. 1599-1610; Hess, R.G., Chcn, Y.S., Bachmann, P.A., Active immunization of feeder pigs against transmissible gastroenteritis (TGE): Influence of maternal antibodies (1982) Proceedings Int Pig Vet Soc, p. 2; Saif, L.J., Bohl, E.H., Role of secretory IgA in passive immunity of swine to enteric viral infections (1979) Immunology of Bicast Milk, pp. 237-248. , Ogra PL, Dayton D, eds. New York: Raven Press","Saif, L.J.; Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States",,,00029645,,AJVRA,"8723879","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0030147183
"Novinger M.S., Sullivan P.S., McDonald T.P.","6505971652;7402033120;7401593419;","Determination of the lifespan of erythrocytes from Greyhounds, using an in vitro biotinylation technique",1996,"American Journal of Veterinary Research","57","5",,"739","742",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030144178&partnerID=40&md5=d78f1f71c0e20b84d59d711d8dcc659c","Department of Animal Science, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States","Novinger, M.S., Department of Animal Science, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Sullivan, P.S., Department of Animal Science, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; McDonald, T.P., Department of Animal Science, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States","Objective - To determine the RBC lifespan of Greyhounds, using an in vitro labeling technique. Design - RBC from dogs were labeled with NHS-biotin and their disappearance measured over time to determine RBC lifespan. Sample Population - 5 Greyhounds that had been vaccinated against distemper, adenovirus 1 and 2 infections, parainfluenza, leptospirosis, parvovirus, and coronavirus infections, Bordetella bronchiseptica infection, and rabies the previous year; 3 sexually intact 14-month-old Beagles served as controls Procedure - After venipuncture for CBC, catheters were inserted in the cephalic vein of each dog. Butorphanol was then administered to achieve mild sedation and analgesia, and glycopyrrolate was administered to ensure maintenance of adequate heart rate during phlebotomy. Dogs were positioned in lateral recumbency; blood was removed via jugular venipuncture, using a standard laboratory donor blood bag containing citrate-phosphate-dextrose solution Blood was transferred aseptically into sterile polystyrene containers and IMHS-biotin was added. After incubation, the labeled RBC were reinfused into the dogs and the blood was allowed to recirculate for 1 hour before the first postinfusion sample was taken At frequent intervals, blood to be analyzed was taken by jugular venipuncture, and the percentage of labeled cells was determined by flow cytometry. Results - The mean RBC lifespan of non-Greyhounds was significantly longer than that of Greyhounds (104.3 ± 2.2 days vs 53.6 ± 6.5 days; P = 0.001). A negative linear correlation was also found between age of the Greyhounds and their RBC lifespan (P = 0 01, R2 = 0 91). Conclusions - The shorter RBC lifespan of the Greyhounds may explain the finding of macrocytosis reported in earlier work. The reason for the shorter RBC lifespan in Greyhounds may be caused by differences in Greyhound RBC membrane structure or accelerated RBC removal from the circulation.",,"biotin; hemoglobin; animal; animal disease; article; blood; breeding; cell survival; cytology; dog; erythrocyte; erythrocyte lifespan; erythrocyte membrane; female; flow cytometry; genetics; in vitro study; male; metabolism; methodology; physiology; statistical model; thrombocyte count; time; ultrastructure; Animals; Biotin; Breeding; Cell Survival; Dogs; Erythrocyte Aging; Erythrocyte Membrane; Erythrocytes; Female; Flow Cytometry; Hemoglobins; Linear Models; Male; Platelet Count; Time Factors","Doxey, D.L., Cellular changes in the blood as an aid to diagnosis (1966) J Small Anim Pract, 7, pp. 77-89; Porter, J.A., Canaday, W.R., Hematologic values in mongrel and Greyhound dogs being screened for research use (1971) J Am Vet Med Assoc, 159, pp. 1603-1606; Heneghan, T., Haematological and biochemical variables in the Greyhound (1977) Vet Sci Commun, 1, pp. 277-284; Sullivan, P.S., Evans, H.L., McDonald, T.P., Platelet concentration and hemoglobin function in Greyhounds (1994) J Am Vet Med Assoc, 205, pp. 838-841; Christian, J.A., Rebar, A.H., Boon, G.D., Senescence of canine biounylated erythrocytesL increased autologous immunoglobulin binding occurs on erythrocytes aged in vivo for 104 to 110 days (1993) Blood, 82, pp. 3469-3473; Hoffmann-Fezer, G., Mysliwietz, J., Mortlbauer, W., Biotin labeling as an alternative nonradioactive approach to determination of red cell survival (1993) Ann Hematol, 67, pp. 81-87; Russo, V., Barker-Gear, R., Gates, R., Studies with biotinylated RBC: (1) use of flow cytometry to determine posttransfusion survival and (2) isolation using Strepiavidin conjugated magnetic beads (1992) Adv Exp Med Biol, 326, pp. 101-107; Suzuki, T., Dale, G.L., Biotinylated erythrocytes: In vivo survival and in vitro recovery (1987) Blood, 70, pp. 791-795; Hoffmann-Fezer, G., Maschke, H., Zeitler, H.J., Direct in vivo biotinylation of erythrocytes as an assay for red cell survival studies (1991) Ann Hematol, 63, pp. 214-217; Animal Welfare Act of 1966 as Ammended; McDonald, T.P., Effect of thrombopoietin on platelet size of mice (1980) Exp Hematol, 8, pp. 527-532; Lassen, E.D., Craig, A.M., Blythe, L.L., Effects of racing on hematologic and serum biochemical values in Greyhounds (1986) J Am Vet Med Assoc, 188, pp. 1299-1303; Brown, I.W., Eadie, G.S., An analytical study of in vivo survival of limited populations of animal red blood cells tagged with radioiron (1953) J Gen Physiol, 36, pp. 327-343; Weissman, S.M., Waldman, T.A., Berlin, N.I., Quantitative measurement of erythropoiesis in the dog (1960) Am J Physiol, 198, pp. 183-186; Jain, N.C., (1993) Essentials of Veterinary Hematology, pp. 141-143. , Philadelphia: Lea & Febiger; Schalm, O.W., Jain, N.C., Carroll, E.J., (1975) Veterinary Hematology. 3rd Ed, pp. 382-411. , Philadelphia: Lea & Febiger","Novinger, M.S.; Department of Animal Science, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States",,,00029645,,AJVRA,"8723892","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0030144178
"Chang R.-Y.I., Krishnan R., Brian D.A.","36725275000;36943098500;7006460232;","The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA",1996,"Journal of Virology","70","5",,"2720","2729",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029880854&partnerID=40&md5=520fcd528b8dbf42d9b0c6e62dc3e367","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan; NIAID, Laboratory of Molecular Microbiology, National Institutes of Health, Bethesda, MD 20892, United States","Chang, R.-Y.I., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan; Krishnan, R., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, NIAID, Laboratory of Molecular Microbiology, National Institutes of Health, Bethesda, MD 20892, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","The 65-nucleotide leader on the cloned bovine coronavirus defective interfering (DI) RNA, when marked by mutations, has been shown to rapidly convert to the wild-type leader of the helper virus following DI RNA transfection into helper virus-infected cells. A model of leader-primed transcription in which free leader supplied in trans by the helper virus interacts by way of its flanking 5'UCUAAAC3' sequence element with the 3'- proximal 3'AGAUUUG5' promoter on the DI RNA minus strand to prime RNA replication has been used to explain this phenomenon. To test this model, the UCUAAAC element which occurs only once in the BCV 5' untranslated region was either deleted or completely substituted in input DI RNA template, and evidence of leader conversion was sought. In both cases, leader conversion occurred rapidly, indicating that this element is not required on input RNA for the conversion event. Substitution mutations mapped the crossover region to a 24-nucleotide segment that begins within the UCUAAAC sequence and extends downstream. Although structure probing of the bovine coronavirus 5' untranslated region indicated that the UCUAAAC element is in the loop of a prominent stem and thus theoretically available for base pair-directed priming, no evidence of an unattached leader early in infection that might have served as a primer for transcription was found by RNase protection studies. These results together suggest that leader conversion on the DI RNA 5' terminus is not guided by the UCUAAAC element and might arise instead from a high-frequency, region-specific, homologous recombination event perhaps during minus-strand synthesis rather than by leader priming during plus- strand synthesis.",,"virus rna; animal cell; article; cattle; coronavirus; crossing over; molecular cloning; nonhuman; priority journal; promoter region; rna analysis; sequence homology; virus mutation; virus recombination; virus transcription; Animals; Base Composition; Base Sequence; Cattle; Cells, Cultured; Coronavirus, Bovine; Defective Viruses; DNA Primers; Helper Viruses; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Polymerase Chain Reaction; Promoter Regions (Genetics); Recombination, Genetic; RNA, Viral; Templates, Genetic; Transcription, Genetic; Transfection","Baker, S.C., Lai, M.M.C., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) EMBO J., 9, pp. 4173-4179; Baric, R.S., Shieh, C.-K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Brian, D.A., Chang, R.-Y., Sethna, P.B., Hofmann, M.A., Role of subgenomic minus-strand RNA in coronavirus replication (1993) Arch. Virol. Suppl., 9, pp. 173-180; Budzilowicz, C.J., Wikzynski, S., Weiss, S.R., Three intergenic regions of nucleotide sequence that are homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Carpenter, C.D., Oh, J.-W., Zhang, C., Simon, A.E., Involvement of a stem-loop structure in the location of junction sites in viral RNA recombination (1995) J. Mol. Biol., 245, pp. 608-622; Chang, R.-Y., Brian, D.A., Cis requirement of N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J Virol., 70, pp. 2201-2207; Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Chastain, M., Tinoco, I., Structural elements in RNA (1991) Prog. Nucleic Acid Res. Mol. Biol., 41, pp. 131-177; Hofmann, M.A., Brian, D.A., The 5-prime end of coronavirus minus-strand RNAs contain a short poly(U) tract (1991) J. Virol., 65, pp. 6331-6333; Hofmann, M.A., Chang, R.-Y., Ku, S., Brian, D.A., Leader-mRNA junction sequences are unique for each subgenomic mRNA species in the bovine coronavirus and remains so throughout persistent infection (1993) Virology, 196, pp. 163-171; Hofmann, M.A., Senanayake, S.D., Brian, D.A., A translation-attenuating intraleader open reading frame is selected on coronavirus mRNAs during persistent infection (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 11733-11737; Hofmann, M.A., Sethna, P.B., Brian, D.A., Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture (1990) J Virol., 64, pp. 4108-4114; Jaeger, J.A., Turner, D.H., Zuker, M., Improved predictions of secondary structure of RNA (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 7706-7710; Jarvis, T.C., Kirkegaard, K., The polymerase in its labyrinth mechanisms and implications of RNA recombination (1991) Trends Genet., 7, pp. 186-191; Jarvis, T.C., Kirkegaard, K., Poliovirus RNA recombination, mechanistic studies in the absence of selection (1992) EMBO J., 11, pp. 3135-3145; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; King, A.M.Q., Genetic recombination in positive strand RNA viruses (1988) RNA Genetics, 2, pp. 149-165. , E. Domingo, J. J. Holland, and P. Ahlquist (ed), CRC Press, Inc., Boca Raton, Fla; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Krishnan, R., Chang, R.-Y., Brian, D.A., Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the down-stream-most initiation site Virology, , in press; Lai, M.M.C., Coronavirus: Organization, replication, and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; La Monica, N., Yokomori, K., Lai, M.M.C., Coronavirus mRNA synthesis: Identification of novel transcription initiation signals which are differentially regulated by different leader sequences (1992) Virology, 188, pp. 402-407; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Li, Y., Ball, L.A., Nonhomologous RNA recombination during negative-strand synthesis of flock house virus RNA (1993) J. Virol., 67, pp. 3854-3860; Liao, C.-L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol., 66, pp. 6117-6124; Makino, S., Joo, M., Effect of intergenic consensus flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Makino, S., Lai, M.M.C., Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol, 63, pp. 5285-5292; Makino, S., Soe, L.H., Shieh, C.-K., Lai, M.M.C., Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs (1988) J. Virol., 62, pp. 3870-3873; Makino, S., Stohlman, S., Lai, M.M.C., Leader sequence of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA in transcription (1986) Proc. Natl. Acad Sci. USA, 83, pp. 4204-4208; Pollack, J.R., Ganem, D., An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation (1993) J. Virol, 67, pp. 3254-3263; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in mRNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNA and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci USA, 86, pp. 5626-5630; Shieh, C.-K., Lee, H.-J., Yokomori, K., La Monica, N., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol., 63, pp. 3729-3736; Shieh, C.-K., Soe, L.H., Makino, S., Chang, M.-F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genome: Implications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Simon, A.E., Bujarski, J.J., RNA-RNA recombination and evolution in virus-infected plants (1994) Annu. Rev. Phytopathol, 32, pp. 337-362; Skinner, M.A., Racaniello, V.R., Dunn, G., Cooper, J., Minor, P.D., Almond, J.W., New model for the secondary structure of the 5′ non-coding RNA of poliovirus is supported by biochemical and genetic data that also show that RNA secondary structure is important in neurovirulence (1989) J. Mol. Biol., 207, pp. 379-392; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Ziejst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Tinoco, I., Borer, P.N., Dengler, B., Levine, M.D., Uhlenbeck, O.C., Crothers, D.M., Gralla, J., Improved estimation of secondary structure in ribonucleic acids (1973) Nature (London) New Biol., 246, pp. 40-41; Van der Most, R.G., DeGroot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Yokomori, K., Banner, L.R., Lai, M.M.C., Heterogeneity of gene expression of hemagglutinin-esterase (HE) protein of murine coronavirus (1991) Virology, 183, pp. 647-657; Znang, X., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States",,,0022538X,,JOVIA,"8627745","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029880854
"Okumura A., Machii K., Azuma S., Toyoda Y., Kyuwa S.","55844839600;7005995877;7005048788;7101966291;7006444820;","Maintenance of pluripotency in mouse embryonic stem cells persistently infected with murine coronavirus",1996,"Journal of Virology","70","6",,"4146","4149",,21,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029893141&partnerID=40&md5=374b1feba67f7816effd5bb8cbba45ae","Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan; Dept. of Veterinary Public Health, Institute of Public Health, Tokyo 108, Japan; Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan; Department of Microbiology, National Defense Medical College, Saitama 359, Japan; Res. Ctr. Protozoan Molec. Immunol., Obihiro Univ. Agric./Vet. Medicine, Ohihiro, Hokkaido 080, Japan","Okumura, A., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan, Department of Microbiology, National Defense Medical College, Saitama 359, Japan; Machii, K., Dept. of Veterinary Public Health, Institute of Public Health, Tokyo 108, Japan; Azuma, S., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan; Toyoda, Y., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan, Res. Ctr. Protozoan Molec. Immunol., Obihiro Univ. Agric./Vet. Medicine, Ohihiro, Hokkaido 080, Japan; Kyuwa, S., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan, Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan","A persistently coronavirus-infected embryonic stem (ES) cell line A3/MHV was established by infecting an ES cell line, A3-1, with mouse hepatitis virus type-2. Although almost all A3/MHV cells were found infected, both A3/MHV and A3-1 cells expressed comparable levels of cell surface differentiation markers. In addition, A3/MHV cells retained the ability to form embryoid bodies. These results suggest that persistent coronavirus infection does not affect the differentiation of ES cells.",,"animal cell; article; cell differentiation; embryo cell; mouse; murine hepatitis coronavirus; nonhuman; persistent infection; priority journal; virus cell interaction; Animals; Cell Differentiation; Cell Line; Embryo; Female; Mice; Murine hepatitis virus; Pregnancy; Stem Cells","Aoyama, H., Delouvee, A., Thiery, J.P., Cell adhesion mechanisms in gangliogenesis studied in avian embryo and in a model system (1985) Cell. Differ., 17, pp. 247-260; Asanaka, M., Lai, M.M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Azuma, S., Toyoda, Y., Production of germ-line chimera mouse derived newly established embryonic stem cells (1990) Jpn. J. Anim. Reprod, 37, pp. 37-43; Baybutt, H.N., Wege, H., Carter, M.J., Ter Meulen, V., Adaptation of coronavirus JHM to persistent infection of murine sac (-) cells (1984) J. Gen. Virol., 65, pp. 915-924; Bradley, A., Evans, M., Kaufman, M.H., Robertson, E., Formation of germ-line chimeras from embryo-derived teratocarcinoma cell lines (1984) Nature (London), 309, pp. 255-256; Castro, R.F., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J. Virol., 69, pp. 8127-8131; Doetschman, T., Williams, P., Maeda, N., Establishment of hamster blastocyst-derived embryonic stem (ES) cells (1988) Dev. Biol., 127, pp. 224-227; Dveksler, G.S., Basile, A.A., Cardellichio, C.B., Holmes, K.V., Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain (1995) J. Virol., 69, pp. 543-546; Evans, M.J., Kaufman, M.H., Establishment in culture of pluripotential cells from mouse embryos (1981) Nature (London), 292, pp. 154-156; Fleming, J.O., Stohlman, S.A., Harmon, R.A., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Flintoff, W.F., Van Dinter, S., Several rat cell lines share a common defect in their inability to internalize murine coronaviruses efficiently (1989) J. Gen. Virol., 70, pp. 1713-1724; Grwer, A., Andrews, G., Anderson, E.D., Role of laminin in epithelium formation by F9 aggregates (1983) J. Cell. Biol., 97, pp. 137-144; Grover, A., Oshima, R.G., Anderson, E.D., Epithelial layer formation in differentiating aggregates of F9 embryonal carcinoma cells (1983) J. Cell. Biol., 96, pp. 1690-1696; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol., 67, pp. 923-932; Kooi, C., Mizzen, L., Anderson, C., Daya, M., Anderson, R., Early events of importance in determining host cell permissiveness to mouse hepatitis virus infection (1988) J. Gen. Virol., 69, pp. 1125-1135; Kubo, H., Yoden, S.T., Taguchi, F., Neutralization and fusion inhibition activities of monoclonal antibodies specific for the S1 subunit of the spike protein of neurovirulent murine coronavirus JHMV cl-2 variant (1993) J. Gen. 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Immun., 29, pp. 42-49; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Vestweber, D., Kemler, R., Identification of a putative cell adhesion domain of uvomorulin (1985) EMBO J., 4, pp. 3393-3398; Wege, H., Siddell, S.G., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Williams, H.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56","Kyuwa, S.; Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan",,,0022538X,,JOVIA,"8648758","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029893141
"Torres J.M., Alonso C., Ortega A., Mittal S., Graham F., Enjuanes L.","35516513600;7201579122;57197446770;57212988795;35821642700;7006565392;","Tropism of human adenovirus type 5-based vectors in swine and their ability to protect against transmissible gastroenteritis coronavirus",1996,"Journal of Virology","70","6",,"3770","3780",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029992355&partnerID=40&md5=bb5acba08fe3b47ea7694cfc937c6cd7","Department of Molecular, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Ctro. de Invest. en Sanid. Anim, Inst. Nacl. Investigaciones Agrarias, Valdeolmos, 28130 Madrid, Spain; Department of Biology, McMaster University, Hamilton, Ont. L8S 4K1, Canada; Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN, United States","Torres, J.M., Department of Molecular, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Alonso, C., Ctro. de Invest. en Sanid. Anim, Inst. Nacl. Investigaciones Agrarias, Valdeolmos, 28130 Madrid, Spain; Ortega, A., Ctro. de Invest. en Sanid. Anim, Inst. Nacl. Investigaciones Agrarias, Valdeolmos, 28130 Madrid, Spain; Mittal, S., Department of Biology, McMaster University, Hamilton, Ont. L8S 4K1, Canada, Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN, United States; Graham, F., Department of Biology, McMaster University, Hamilton, Ont. L8S 4K1, Canada; Enjuanes, L., Department of Molecular, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The infection of epithelial swine testicle and intestinal porcine epithelial (IPEC-1) cell lines by adenovirus type 5 (Ad5) has been studied in vitro by using an Ad5-luciferase recombinant containing the firefly luciferase gene as a reporter. Porcine cell lines supported Ad5 replication, showing virus titers, kinetics of virus production, and luciferase expression levels similar to those obtained in human 293 cells, which constitutively express the 5'-end 11% of the Ad5 genome. The tropism of Ad5-based vectors in swine and its ability to induce an efficient immune response against heterologous antigens expressed by foreign genes inserted in these vectors has been determined. Ad5 vectors replicate and express heterologous antigens in porcine lungs and mediastinal and mesenteric lymph nodes. Significant levels of heterologous antigen expression were also demonstrated in the small intestine (jejunum and ileum), but Ad5 replication in this organ was very poor, suggesting that Ad vectors undergo an abortive replication in the porcine small intestine. The tissues infected by Ad5 were dependent on the inoculation route. The oronasal route appeared to be best for inoculation of bronchus-associated lymphoid tissue infection, while the intraperitoneal route was best for gut-associated lymphoid tissue infection. Epithelial cells of bronchioles, macrophages, type II pneumocytes, and follicular dendritic cells were identified as targets for Ad5, while epithelial cells of the intestine were not infected by Ad5. Viruses with a deletion from 79.5 to 84.8 map units in the E3 region, with or without heterologous inserted genes, replicated to lower levels in porcine tissues than did wild-type Ad5. It was also shown that an Ad5 recombinant expressing the four antigenic sites (A, B, C, and D) of transmissible gastroenteritis coronavirus (TGEV) spike protein induced in swine immune responses which neutralized TGEV infectivity. In addition, porcine serum from Ad-TGEV-immune animals provide passive protection when mixed with fully virulent TGEV and orally administered to highly susceptible newborn piglets. These results taken together indicate that swine may be a good animal model for human Ad5 lung infection to aid in the evaluation of candidate adenovirus vaccines and that Ad5 may be suitable as a recombinant viral vaccine or for other applications in swine.",,"animal cell; article; coronavirus; human; human adenovirus; human cell; infection sensitivity; nonhuman; priority journal; swine; virus replication; virus transmission; Adenoviruses, Human; Animals; Antibodies, Viral; Gastroenteritis, Transmissible, of Swine; Genetic Vectors; Humans; Luciferases; Swine; Transmissible gastroenteritis virus; Vaccines, Synthetic; Viral Vaccines; Virus Replication","Alonso, C., Unpublished results; Anderson, M., Paabo, S., Nilsson, T., Peterson, P.A., Impaired intracellular transport of class I MHC antigens as a possible means for adenovirus to evade immune surveillance (1985) Cell, 43, pp. 215-222; Berkner, K.L., Development of adenovirus vectors for the expression of heterologous genes (1988) BioTechniques, 6, pp. 616-629; Berschneider, H.M., Powell, D.W., Fibroblasts modulate intestinal secretory response to inflammatory mediators (1992) J. 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Tumbleason (ed.), Plenum Press, New York; Meiklejohn, G., Viral respiratory disease at Lowry Air Force Base in Denver, 1952-1982 (1983) J. Infect. Dis., 148, pp. 775-784; Mittal, S.K., McDermott, M.R., Johnson, D.C., Prevec, L., Graham, F.L., Monitoring foreign gene expression by a human adenovirus based vector using the firefly luciferase as a reporter gene (1993) Virus. Res., 28, pp. 67-90; Natuk, R.J., Lubeck, M.D., Chanda, P.K., Chengalvala, M., Wade, M.S., Murthy, S.C.S., Wilhelm, J., Hung, P.P., Immunogenicity of recombinant human adenovirus-human immunodeficiency virus vaccines in chimpanzees (1993) AIDS Res. Hum. Retroviruses, 9, pp. 395-404; Nevins, J.R., Regulation of early adenovirus gene expression (1987) Microbiol. Rev., 51, pp. 419-430; Prevec, L., Schneider, M., Rosenthal, K.L., Belbeck, L.W., Derbyshire, J.B., Graham, F.L., Use of human adenovirus-based vectors for antigen expression in animals (1989) J. Gen. Virol., 70, pp. 429-434; Prince, G.A., Porter, D.D., Jenson, A.B., Horswood, R.L., Chanock, R.M., Ginsberg, H.S., Pathogenesis of adenovirus type-5 pneumonia in cotton rats (Sigmodon hispidus) (1993) J. Virol., 67, pp. 101-111; Saif, L.J., Bohl, E.H., Gupta, R.K.P., Isolation of porcine immunoglobulins and determination of the immunoglobulin class of transmissible gastroenteritis viral antibodies (1972) Infect. Immun., 6, pp. 600-609; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , A. D. Leman, B. Straw, W. L. Mengeling, S. D' Allaire, and D. J. Taylor (ed.), Iowa State University Press, Ames, Iowa; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Scicchitano, R., Stanistz, A., Ernst, P.B., Bienenstock, J., A common mucosal immune system revisited (1988) Migration and Homing of Lymphoid Cells, pp. 1-34. , A. J. Husband (ed.), CRC Press Inc., Boca Raton, Fla; Silverstein, G., Strohl, W.A., Restricted replication of adenovirus type 2 in mouse Balb/3T3 cells (1986) Arch. Virol., 87, pp. 241-264; Spaan, W., Cavanagh, D., Horzinek, M.C., Immunochemistry of viruses. II. The basis for serodiagnosis and vaccines (1990) Coronaviruses, pp. 359-379. , M. H. V. van Regenmortel and A. R. Neurath (ed.), Elsevier. Amsterdam; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Takafuji, E., Gaydos, J.C., Allen, R.G., Top, F.H., Simultaneous administration of live, enteric-coated adenovirus types 4, 7, and 21 vaccines: Safety and immunogenicity (1979) J. Infect. Dis., 140, pp. 48-53; Tew, J.G., Kosco, M.H., Burton, G.F., Szakal, A.K., Follicular dendritic cells as accessory cells (1990) Immunol. Rev., 117, pp. 185-211; Torres, J.M., Sanchez, C., Suñé, C., Smerdou, C., Prevec, L., Graham, F.L., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; Vancott, J.L., Brim, T.A., Lunney, J.K., Saif, L.J., Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J. Immunol., 152, pp. 3980-3990; Vancott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- And bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Wold, W.S.M., Gooding, L.R., Region E3 of adenovirus: A cassette of genes involved in host immunosurveillance and virus-cell interactions (1991) Virology, 184, pp. 1-8","Enjuanes, L.; Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain",,,0022538X,,JOVIA,"8648712","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029992355
"Dveksler G.S., Gagneten S.E., Scanga C.A., Cardellichio C.B., Holmes K.V.","6603790777;6602898805;6701713751;6602071538;7201657724;","Expression of the recombinant anchorless N-terminal domain of mouse hepatitis virus (MHV) receptor makes hamster or human cells susceptible to MHV infection",1996,"Journal of Virology","70","6",,"4142","4145",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029888103&partnerID=40&md5=0f98979168276644d6a41604e8fbaff9","Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States; Department of Microbiology, University of Colorado, Health Sciences Center, 4200 E. Ninth Ave., Denver, CO 80262, United States; Natl. Inst. Diabet./Digest./K.D., Bethesda, MD 20892, United States; University of Pittsburgh, Pittsburgh, PA 15260, United States","Dveksler, G.S., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States; Gagneten, S.E., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States, Natl. Inst. Diabet./Digest./K.D., Bethesda, MD 20892, United States; Scanga, C.A., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States, University of Pittsburgh, Pittsburgh, PA 15260, United States; Cardellichio, C.B., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States; Holmes, K.V., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814-4799, United States, Department of Microbiology, University of Colorado, Health Sciences Center, 4200 E. Ninth Ave., Denver, CO 80262, United States","Mouse hepatitis virus (MHV) receptor, the receptor for the murine coronavirus MHV, was expressed in MHV-resistant hamster and human cells as a series of mutant, recombinant glycoproteins with carboxyterminal deletions lacking the cytoplasmic tail, transmembrane domain, and various amounts of the immunoglobulin constant-region-like domains. The soluble receptor glycoproteins containing the N-terminal virus-binding domain were released into the supernatant medium and inactivated the infectivity of MHV-A59 virions in a concentration-dependent manner. Surprisingly, some of the anchorless glycoproteins were found on the plasma membranes of transfected cells by flow cytometry, and these cells were rendered susceptible to infection with three strains of MHV. Thus, in the cells in which the anchorless, recombinant receptor glycoprotein is synthesized, some of the protein is bound to an unidentified moiety on the plasma membrane, which allows it to serve as a functional virus receptor.",,"amino terminal sequence; article; hamster; human; human cell; infection sensitivity; murine hepatitis coronavirus; priority journal; protein expression; virus cell interaction; Amino Acid Sequence; Animals; Cricetinae; Humans; Mice; Molecular Sequence Data; Murine hepatitis virus; Receptors, Virus; Recombinant Proteins; Transfection","Beauchemin, N., Turbide, C., Afar, D., Bell, J., Raymond, M., Stanners, C.P., Fuks, A., A mouse analogue of the human carcinoembryonic antigen (1989) Cancer Res., 49, pp. 2017-2021; Byrn, R.A., Sekigawa, I., Chamow, S.M., Johnson, J.S., Gregory, T.J., Capon, D.J., Groopman, J.E., Characterization of in vitro inhibition of human immunodeficiency virus by purified recombinant CD4 (1989) J. Virol., 63, pp. 4370-4375; Casasnovas, J.M., Springer, T.A., Pathway of rhinovirus disruption by soluble intercellular adhesion molecule 1 (ICAM-1): An intermediate in which ICAM-1 is bound and RNA is released (1994) J. Virol., 68, pp. 5882-5889; Chen, D.S., Asanaka, M., Yokimori, K., Wang, F.-I., Hwang, S.B., Li, H.-P., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Clapham, P.R., Weber, J.N., Whitby, D., McIntosh, K., Dalgleish, A.G., Madden, P.J., Deen, K.C., Weiss, R.A., Soluble CD4 blocks the infectivity of diverse strains of HIV and SIV for T cells and monocytes but not for brain and muscle cells (1989) Nature (London), 337, pp. 368-370; Deen, K.C., McDougal, J.S., Inacker, R., Wasserman, G., Arthos, J., Rosenberg, J., Maddon, P.J., Sweet, R., A soluble form of CD4 (T4) protein inhibits AIDS virus infection (1988) Nature (London), 331, pp. 82-84; Dveksler, G.S., Basile, A.A., Cardellichio, C.B., Holmes, K.V., Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain (1995) J. Virol., 69, pp. 543-546; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.-S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse coronavirus MHV-A59 and blocking anti-receptor monoclonal antibody bind to the N-terminal domain of cellular receptor MHVR (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1715-1720; Fuerst, T.R., Niles, E.G., Studier, W.F., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bactcriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8128; Kaplan, G., Freistadt, M.S., Racaniello, V.R., Neutralization of poliovirus by cell receptors expressed in insect cells (1990) J. Virol., 64, pp. 4697-4702; Marlin, S.D., Staunton, D.E., Springer, T.A., Stratowa, C., Sommerguber, W., Merluzzi, V., A soluble form of intercellular adhesion molecule-l inhibits rhinovirus infection (1990) Nature (London), 344, pp. 70-72; Meinick, J., Dull, J.L., Argon, Y., Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum (1994) Nature (London), 370, pp. 373-375; Nédellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; Obrink, B., Personal communication; Rudert, F., Saunders, A.M., Rebstock, S., Thompson, J.A., Zimmermann, W., Characterization of murine carcinoembryonic antigen gene family members (1992) Mamm. Genome, 3, pp. 262-273; Smith, A.L., Cardellichio, C.B., Vinograd, D.F., DeSouza, M.S., Barthold, S.W., Holmes, K.V., Monoclonal antibody to the receptor for murine coronavirus MHV-A59 inhibits virus replication in vivo (1991) J. Infect. Dis., 163, pp. 879-882; Thompson, J.A., Molecular cloning and expression of carcinoembryonic antigen gene family members (1995) Tumor Biol., 16, pp. 10-16; Vallejo, A.N., Pogulis, R.J., Pease, L.R., Mutagenesis and synthesis of novel recombinant genes using PCR (1995) PCR Primer. A Laboratory Manual, pp. 603-612. , C. W. Dieffenbach and G. S. Dveksler (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Williams, A.F., Barclay, A.N., The immunoglobulin superfamilydomains for cell surface recognition (1988) Annu. Rev. Immunol., 6, pp. 381-405; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938","Holmes, K.V.; Department of Microbiology, Colorado Univ. Health Sciences Ctr., 4200 E. Ninth Ave., Denver, CO 80262, United States",,,0022538X,,JOVIA,"8648757","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029888103
"Risco C., Antón I.M., Enjuanes L., Carrascosa J.L.","56251715300;57198264385;7006565392;35481302900;","The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins",1996,"Journal of Virology","70","7",,"4773","4777",,86,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029979024&partnerID=40&md5=c37b3fd95bdafac24422658592b0339a","Macromolecular Structure Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain; Molec. and Cell Biology Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain; Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain; Children's Hospital, Boston, MA 02115, United States","Risco, C., Macromolecular Structure Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain; Antón, I.M., Macromolecular Structure Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain, Children's Hospital, Boston, MA 02115, United States; Enjuanes, L., Molec. and Cell Biology Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain; Carrascosa, J.L., Macromolecular Structure Department, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, 28049 Madrid, Spain, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain","Coronaviruses are enveloped RNA viruses involved in a variety of pathologies that affect animals and humans. Existing structural models of these viruses propose a helical nucleocapsid under the virion envelope as the unique internal structure. In the present work, we have analyzed the structure of the transmissible gastroenteritis coronavirus. The definition of its organization supports a new structural model for coronaviruses, since a spherical, probably icosahedral, internal core has been characterized. Disruption of these cores induces the release of N-protein-containing helical nucleocapsids. Immunogold mapping and protein analysis of purified cores showed that they consist of M and N proteins, M being the main core shell component. This surprising finding, together with the fact that M protein molecules are also located in the virion envelope, indicates that a reconsideration of the assembly and maturation of coronaviruses, as well as a study of potential M-protein subclasses, is needed.",,"article; coronavirus; cryoelectron microscopy; immunogold staining; nonhuman; priority journal; protein analysis; protein structure; virion; virus envelope; virus nucleocapsid; Animals; Capsid; Cell Line; Polyethylene Glycols; Swine; Transmissible gastroenteritis virus; Viral Core Proteins; Viral Matrix Proteins; Virion","Armstrong, J., Nieman, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Booy, F.P., Cryoelectron microscopy (1993) Viral Fusion Mechanisms, pp. 21-54. , J. Bentz (ed.), CRC Press, Inc., Boca Raton, Fla; Burnette, W.N., Western-blotting: Electrophoretic transfer from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with radioiodinated protein A (1981) Anal. Biochem., 112, pp. 195-203; Caul, E.O., Ashley, C.R., Ferguson, M., Egglestone, S.I., Preliminary studies on the isolation of coronavirus 229E nucleocapsids (1979) FEMS Microbiol. Lett., 5, pp. 101-105; Cavanagh, D., Revision of the taxonomy of the Coronavirus. Torovirus, and Arterivirus genera (1994) Arch. Virol., 135, pp. 226-237; Davies, H.A., Dourmashkin, R.R., MacNaughton, R., Ribonucle-oprotein of avian infectious bronchitis virus (1981) J. Gen. Virol., 53, pp. 67-74; Enjuanes, L., Van der Zeijst, B.A.M., Molecular basis of the transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, pp. 337-376. , S. G. Siddell (ed.), Plenum Press, New York; Garwes, D.J., Pocock, D.H., Pike, B.V., Isolation of subviral components from transmissible gastroenteritis virus (1976) J. Gen. Virol., 32, pp. 283-294; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV corona virus ORF 4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lai, M.M.C., Coronavirus. Organization, replication, and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; MacNaughton, M.R., Davies, H.A., Nermut, M.V., Ribonucleoprotein-like structures from coronavirus particles (1978) J. Gen. Virol., 39, pp. 545-549; Murphy, F.A., Fauquet, C.M., Bishop, D.H.L., Ghabrial, S.A., Jarvis, A.W., Martinelli, G.P., Mayo, M.A., Summers, M.D., (1995) Virus Taxonomy, Classification and Nomenclature of Viruses, p. 23. , Springer-Verlag, New York; Risco, C., Antón, I.M., Suñé, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Risco, C., Carrascosa, J.L., Pedregosa, A.M., Humphrey, C.D., Sánehez-Fauquier, A., Ultrastructure of the human astrovirus serotype 2 (1995) J. Gen. Virol., 76, pp. 2075-2080; Risco, C., Pinto da Silva, P., Cellular functions during activation and damage by pathogens: Immunogold studies of the interaction of bacterial endotoxins with target cells (1995) Microsc. Res. Tech., 31, pp. 141-158; Risco, C., Romero, C., Bosch, M.A., Pinto da Silva, P., Type II pneumocytes revisited: Intracellular membranous systems, surface characteristics, and lamellar body secretion (1994) Lab. Invest., 70, pp. 407-417; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The Coronaviridae. An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.). Plenum Press, New York; Spaan, W., Cavanagh, D., Horzinek, H.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-112; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462","Carrascosa, J.L.; Centro Nacional de Biotecnologia, Campus Universidad Autonoma, 28049 Madrid, Spain",,,0022538X,,JOVIA,"8676505","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029979024
"Gallagher T.M.","7202310503;","Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein",1996,"Journal of Virology","70","7",,"4683","4690",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029948532&partnerID=40&md5=d900e287ea180e091349475c752a47e4","Department of Microbiology, Loyola University, Medical Center, Maywood, IL 60153-5500, United States; Department of Microbiology, Loyola University, Medical Center, 2160 S. First Ave, Maywood, IL 60153-5500, United States","Gallagher, T.M., Department of Microbiology, Loyola University, Medical Center, Maywood, IL 60153-5500, United States, Department of Microbiology, Loyola University, Medical Center, 2160 S. First Ave, Maywood, IL 60153-5500, United States","The envelopes of murine hepatitis virus (MHV) particles are studded with glycoprotein spikes that function both to promote virion binding to its cellular receptor and to mediate virion-cell membrane fusion. In this study, the cysteine-rich spikes were subjected to chemical modification to determine whether such structural alterations impact the virus entry process. Ellman reagent, a membrane-impermeant oxidizing agent which reacts with exposed cysteine residues to effect covalent addition of large thionitrobenzoate moieties, was incubated at 37°C with the JHM strain of MHV. Relative to untreated virus, 1 mM Ellman reagent reduced infectivity by 2 log10 after 1 h. This level of inhibition was not observed at incubation temperatures below 21°C, suggesting that virion surface proteins undergo thermal transitions that expose cysteine residues to modification by the reagent. Quantitative receptor binding and membrane fusion assays were developed and used to show that Ellman reagent specifically inhibited membrane fusion induced by the MHV JHM spike protein. However, this inhibition was strain specific, because the closely related MHV strain A59 was unaffected. To identify the basis for this strain specificity, spike cDNAs were prepared in which portions encoded either JHM or A59 residues. cDNAs were expressed with vaccinia virus vectors and tested for sensitivity to Ellman reagent in the fusion assays. The results revealed a correlation between the severity of inhibition mediated by Ellman reagent and the presence of a JHM-specific cysteine (Cys-1163). Thus, the presence of this cysteine increases the availability of spikes for a thiol modification that ultimately prevents fusion competence.",,"5,5' dithiobis(2 nitrobenzoic acid); cysteine; envelope protein; virus rna; animal cell; animal tissue; article; controlled study; coronavirus; membrane fusion; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein binding; protein modification; quantitative assay; receptor binding; virus envelope; Animals; Cell Line; Cysteine; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Hela Cells; Humans; Membrane Fusion; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Protein Conformation; Rabbits; Receptors, Virus; Structure-Activity Relationship; Sulfhydryl Compounds; Viral Envelope Proteins","Abell, B.A., Brown, D.T., Sindbis virus membrane fusion is mediated by reduction of glycoprotein disulfide bridges at the cell surface (1993) J. Virol., 67, pp. 5496-5501; Bullough, P.A., Hughson, F.M., Skehel, J.J., Wiley, D.C., Structure of influenza haemagglutinin at the pH of membrane fusion (1994) Nature (London), 371, pp. 37-43; Carr, C.M., Kim, P.S., A spring-loaded mechanism for the conformational change of influenza hemagglutinin (1993) Cell, 73, pp. 823-832; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, , S. G. Siddell (ed.), Plenum Press, New York; Chambers, P., Pringle, C.R., Easton, A.J., Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins (1990) J. Gen. Virol., 71, pp. 3075-3080; Davies, H.A., Macnaughton, M.R., Comparison of the morphology of three coronaviruses (1979) Arch. Virol., 59, pp. 25-33; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence lor a coiled-coil structure in the spike proteins of coronaviruses (1987) J. Mol. Biol., 196, pp. 963-966; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5167-5375; Doms, R.W., Protein conformational changes in virus-cell fusion (1993) Methods Enzymol., 221, pp. 61-72; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse coronavirus MHV-A59 and blocking anti-receptor monoclonal antibody bind to the N-terminal domain of cellular receptor MHVR (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Elroy-Stein, O., Moss, B., Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6743-6747; Falkner, F.G., Moss, B., Escherichia coli gpt gene provides dominant selection for vaccinia virus open reading frame expression vectors (1988) J. Virol., 62, pp. 1849-1854; Fuerst, T.R., Earl, P.L., Moss, B., Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target eenes (1987) Mol. Cell. Biol., 7, pp. 2538-2544; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Gallagher, T.M., Overexpression of the MHV receptor: Effect on progeny virus secretion (1995) Adv. Exp. Med. Biol., 380, pp. 331-336; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus arc generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gossen, M., Bujard, H., Tight control of gene expression on mammalian cells by tetracycline-responsive promoters (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 5547-5551; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Hirano, N., Murakami, T., Fujiwara, K., Matsumoto, M., Utility of mouse cell line DBT for propagation and assay of mouse hepatitis virus (1978) Jpn. J. Exp. Med., 48, pp. 71-75; Innis, M.A., Gelfand, D.H., Optimization of PCRs (1990) PCR Protocols, pp. 3-12. , M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), Academic Press, Inc., San Diego, Calif; Kawasaki, E.S., Amplification of RNA (1990) PCR Protocols, pp. 21-27. , M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.), Academic Press, Inc., San Diego, Calif; Klausner, R.D., Donaldson, J.G., Lippincott-Schwartz, J., Brefeldin A: Insights into the control of membrane traffic and organelle structure (1992) J. Cell Biol., 116, pp. 1071-1080; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charik, J., Van der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Moss, B., Elroy-Stein, O., Mizukami, T., Alexander, W.A., Fuerst, T.R., New mammalian expression vectors (1990) Nature (London), 348, pp. 91-92; Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) J. Virol., 68, pp. 5411-5422; Opstelten, D.-J.E., De Groote, P., Horzinek, M.C., Vennema, H., Rottier, P.J.M., Disulfide bonds in folding and transport of mouse hepatitis coronavirus glycoproteins (1993) J. Virol., 67, pp. 7394-7401; Parker, S.E., Gallagher, T.M., Buehmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Rey, F.A., Heinz, F.X., Mandl, C., Kunz, C., Harrison, S.C., The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution (1995) Nature (London), 375, pp. 291-298; Riddles, P.W., Blakeley, R.L., Zerner, B., Ellman's reagent: 5,5′-dithiohis(2-nitrohenzoic acid) - A reexamination (1979) Anal. Biochem., 94, pp. 75-81; Ryser, H.J.-P., Levy, E.M., Mandel, R., DiSciullo, G.J., Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 4559-4563; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: a Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Stauber, R., Pfleiderara, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37̈C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect. Immun., 6, pp. 501-507; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; White, J.M., Membrane fusion (1992) Science, 258, pp. 917-924; Wild, C., Dubay, J.J., Greenwell, T., Baird Jr., T., Oas, T.G., McDanal, C., Hunter, E., Matthews, T., Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 12676-12680; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Wilson, I.A., Skehel, J.J., Wiley, D.C., Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution (1981) Nature (London), 289, pp. 366-373; Yoo, D., Parker, M.D., Babiuk, L.A., The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells (1991) Virology, 180, pp. 395-399","Gallagher, T.M.; Dept. of Microbiology/Immunology, Loyola University Medical Center, 2160 S. First Ave., Maywood, IL 60153-5500, United States",,,0022538X,,JOVIA,"8676494","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029948532
"Cristallo A., Biamonti G., Battaglia M., Cereda P.M.","6603250884;7007029268;7201908369;7003845258;","cDNA probe for the human coronavirus OC43 also detects neonatal calf diarrhea coronavirus (NCDCV)",1996,"New Microbiologica","19","3",,"251","256",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030184610&partnerID=40&md5=3618dfc871ea623bae8bbdd9e76fc2e5","Istituto di Microbiologia, Università di Pavia, via Brambilla 74, 27100 Pavia, Italy; Istituto di Genetica, Biochim. ed Evoluzionistica del CNR, via Abbiategrasso 207, 27100 Pavia, Italy; Ist. di Med. Sperimentale del CNR, via Marx 15-43, 00137 Roma, Italy","Cristallo, A., Istituto di Microbiologia, Università di Pavia, via Brambilla 74, 27100 Pavia, Italy; Biamonti, G., Istituto di Genetica, Biochim. ed Evoluzionistica del CNR, via Abbiategrasso 207, 27100 Pavia, Italy; Battaglia, M., Ist. di Med. Sperimentale del CNR, via Marx 15-43, 00137 Roma, Italy; Cereda, P.M., Istituto di Microbiologia, Università di Pavia, via Brambilla 74, 27100 Pavia, Italy","Human coronaviruses (HCV) OC43 and 229E are the second most frequently isolated agents of common colds, and have also been associated with severe upper respiratory infections in children and with gastroenteritis of unknown etiology, such as infantile necrotizing enterocolitis. While HCV-OC43 and neonatal calf diarrhea coronavirus NCDCV cannot be held responsible for enteric infection in man, serological data suggest the possible existence of a human coronavirus, antigenically related to HCV-OC43 and NCDCV, and responsible for enteric infections. We developed a rapid and sensitive method for the diagnosis of human respiratory coronavirus infections, and for detecting these viruses in suspect coronavirus infections. This assay entails a reverse transcriptase polymerase chain reaction, followed by Southern blot analysis with a probe specific for the amplification products.","229E; cDNA probe; Human coronavirus; Neonatal calf diarrhea coronavirus; OC43; Reverse transcription polymerase chain reaction","complementary DNA; RNA directed DNA polymerase; virus RNA; article; cell line; Coronavirus; fibroblast; genetics; human; isolation and purification; methodology; molecular genetics; polymerase chain reaction; sensitivity and specificity; Southern blotting; Blotting, Southern; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Coronavirus, Bovine; DNA, Complementary; Fibroblasts; Humans; Molecular Sequence Data; Polymerase Chain Reaction; RNA, Viral; RNA-Directed DNA Polymerase; Sensitivity and Specificity","Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) Journal of Virology, 48, pp. 633-640; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of leader-related small RNAs in coronavirus-infected cells: Further evidence for leader-primed mechanism of transcription (1985) Virus Research, 3, pp. 19-33; Boursnell, M.E., Brown, T.D., Foulds, L.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Brown, T.D., Boursnell, M.E., Binns, M.M., A leader sequence is present on mRNA a of avian infectious bronchitis virus (1984) Journal of General Virology, 65, pp. 1437-1442; Burks, J.S., Devald, B.L., Jankovsky, L.D., Gerdes, C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Gerna, G., Cattaneo, E., Cereda, P.M., Revello, M.G., Achilli, G., Coronavirus OC43 serum inhibitor and neutralizing antibody by a new plaque-reduction assay (1980) Proceeding of the Society for Experimental Biology and Medicine, 163, pp. 360-366; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) Journal of Virology, 51, pp. 384-388; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Research, 12, pp. 1-9; Lai, M.M.C., Patton, C.D., Stohlman, S.A., Replication of mouse hepatitis virus: Negative-stranded RNA and replicative form RNA are of genome length (1982) Journal of Virology, 44, pp. 487-492; Lai, M.M.C., Coronavirus leader-RNA-primed transcription: An alternative mechanism to RNA splicing (1986) Bioessays, 5, pp. 257-260; Lapps, W., Brian, D.A., Oligonucleotide fingerprints of antigenically related bovine coronavirus and human coronavirus OC43 (1985) Archives of Virology, 86, pp. 101-108; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein gene (1987) Virology, 157, pp. 47-57; Mathan, M., Mathan, V.I., Swaminathan, S.P., Yesudoss, S., Baker, S.J., Pleomorphic virus-like particles in human faeces (1975) Lancet, 1, pp. 1068-1069; Macnaughton, M.R., Davies, H.A., Human enteric coronaviruses: Brief review (1981) Archives of Virology, 70, pp. 301-313; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) Journal of General Virology, 64, pp. 761-776; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Current Topics in Microbiology Immunity, 99, pp. 165-200","Cristallo, A.; Istituto di Microbiologia, Università di Pavia, via Brambilla 74, 27100 Pavia, Italy",,,11217138,,,"8841041","English","New Microbiol.",Article,"Final",,Scopus,2-s2.0-0030184610
"Lavi E., Wang Q., Weiss S.R., Gonatas N.K.","7006986911;16044062200;57203567044;7005884981;","Syncytia formation induced by coronavirus infection is associated with fragmentation and rearrangement of the Golgi apparatus",1996,"Virology","221","2",,"325","334",,34,"10.1006/viro.1996.0382","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030586022&doi=10.1006%2fviro.1996.0382&partnerID=40&md5=a3339b688ffb1ae6d55efd19bec22fcc","Dept. of Pathol./Laboratory Medicine, Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States","Lavi, E., Dept. of Pathol./Laboratory Medicine, Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States; Wang, Q., Dept. of Pathol./Laboratory Medicine, Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States; Gonatas, N.K., Dept. of Pathol./Laboratory Medicine, Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6079, United States","Coronavirus mouse hepatitis virus (MHV) possesses a membrane glycoprotein (M) which is targeted to the Golgi apparatus (GA). We used immunocytochemistry with an organelle-specific antiserum to investigate the morphologic changes of the GA during infection of L2 murine fibroblasts with MHV-A59. Twenty-four hours after infection the GA was fragmented and translocated in the center of syncytia, while the microtubular network was also rearranged displaying radiating elements toward the center of syncytia. Two fusion defective mutants, which contain an identical amino acid substitution in the cleavage signal sequence of the spike glycoprotein (S), induced fragmentation of the GA. However, the GA migrated only partially to the centers of syncytia during infection with these mutants. Revertant viruses, in which the above mutation was corrected, had fusion properties and GA staining similar to wtMHV-A59. Experiments with brefeldin A (BFA), which induces redistribution of the GA into the rough endoplasmic reticulum (RER), revealed that an intact GA for a period of 4-16 hr postinfection, is required for coronavirus replication and syncytia formation. Thus, during MHV infection, syncytia formation is associated with fragmentation of the GA, followed by a previously undescribed phenomenon of migration of the organelle into the centers of syncytia. The fragmentation of the GA, however, may occur without the formation of syncytia. Therefore, two distinct mechanisms may be responsible for the fragmentation of the GA and its subsequent migration to the center of syncytia.",,"amino acid substitution; animal cell; article; cell migration; Coronavirus; depolymerization; gene induction; gene rearrangement; Golgi complex; immunocytochemistry; mouse; nonhuman; priority journal; rough endoplasmic reticulum; syncytium; virus infection; virus replication; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Armstrong, J., Patel, S., The Golgi sorting domain of coronavirus e1 protein (1991) J. Cell Sci., 98, pp. 567-575; Campadelli, G., Brandimarti, R., Di Lazzaro, C., Ward, P.L., Roizman, B., Ttorrisi, M.R., Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1 (1993) Proc. Natl. Acad. Sci. 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Sch. of Medicine, Philadelphia, PA 19104-6079, United States",,"Academic Press Inc.",00426822,,VIRLA,"8661443","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030586022
"Schijns V.E.C.J., Wierda C.M.H., Van Hoeij M., Horzinek M.C.","7003814597;8112395100;57212298974;7102624836;","Exacerbated viral hepatitis in IFN-γ receptor-deficient mice is not suppressed by IL-12",1996,"Journal of Immunology","157","2",,"815","821",,48,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029949634&partnerID=40&md5=6140b04395f3245fa9233e16143338f8","Virology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Immunology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Virology Unit, Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Schijns, V.E.C.J., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands, Virology Unit, Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Wierda, C.M.H., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Van Hoeij, M., Immunology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands","Both IL-12 and IFN-γ have been implicated as principal inducers of type 1 immune responses required for the elimination of intracellular pathogens, such as viruses. We examined the in vivo antiviral role of both cytokines during coronavirus-induced hepatitis in a mouse hepatitis virus (MHV) model. The absence of IFN-γ function in mice with a targeted disruption of the IFN- γR α-chain gene (IFN-γR-/-) resulted in increased susceptibility to coronaviral hepatitis associated with augmented viral replication and increased hepatocellular injury. The mutant mice showed a type 1 lymphokine response characterized by the normal high IFN-γ and low IL-4 production. Unlike MHV-infected wild-type mice, however, the mutant IFN-γR-/- mice showed no increase in IL-12 p40 gene expression, similar to that in naive animals. IL-12 treatment failed to restore host resistance in IFN-γR-/- mice, but significantly protected MHV-susceptible C57BL/6 mice against lethal infection, although less than IFN-γ treatment. Mice protected by IL-12 or IFN-γ showed resistance against an otherwise lethal second MHV infection. Our data demonstrate that despite reduced IL-12 gene expression and defective IFN-γR function, virus-induced IFN-γ production can occur. Furthermore, they emphasize the pivotal antiviral role of IFN-γ in protection against acute coronavirus-induced hepatitis.",,"gamma interferon; gamma interferon receptor; interleukin 12; interleukin 4; recombinant gamma interferon; recombinant interleukin 12; animal model; animal tissue; antiviral activity; article; controlled study; female; host resistance; infection prevention; infection resistance; liver cell damage; male; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virus hepatitis; Acute Disease; Animals; Antigens, CD; Base Sequence; Female; Hepatitis, Viral, Animal; Immunosuppressive Agents; Interferon Type II; Interleukin-12; Male; Mice; Mice, Inbred C57BL; Mice, Mutant Strains; Molecular Sequence Data; Receptors, Interferon; Recombinant Proteins","Scott, P., Kaufmann, S.H.E., The role of T-cell subset and cytokines in the regulation of infection (1991) Immunol. 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Immunol., 140, p. 4245; Dalton, D.K., Pitts-Meek, S., Keshav, S., Figari, I.S., Bradley, A., Stewart, T.A., Multiple defects of immune function in mice with disrupted interferon-γ genes (1993) Science, 259, p. 1739; Tsuji, M., Miyahira, Y., Nussenzweig, R.S., Aguet, M., Reichel, M., Zavala, F., Development of antimalaria immunity in mice lacking IFN-γ receptor (1995) J. Immunol., 154, p. 5338","Schijns, V.E.C.J.; Infectious Diseases/Immunology Dept., Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,00221767,,JOIMA,"8752933","English","J. IMMUNOL.",Article,"Final",,Scopus,2-s2.0-0029949634
"Trigg C.J., Nicholson K.G., Wang J.H., Ireland D.C., Jordan S., Duddle J.M., Hamilton S., Davies R.J.","7003495587;7103216939;7701336529;57198124543;57202042177;16149556000;16180157300;35372726700;","Bronchial inflammation and the common cold: A comparison of atopic and non-atopic individuals",1996,"Clinical and Experimental Allergy","26","6",,"665","676",,61,"10.1111/j.1365-2222.1996.tb00593.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029971899&doi=10.1111%2fj.1365-2222.1996.tb00593.x&partnerID=40&md5=68f863e90a0b1855a5647c02116bc04f","Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom; Department of Immunocytochemistry, St. Bartholomew's Hospital, London, United Kingdom; Department of Microbiology, Leicester University, Leicester, United Kingdom; Dept. of Allerg. and Resp. Medicine, Guy's Hospital, London SE1 9RT, United Kingdom","Trigg, C.J., Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom, Dept. of Allerg. and Resp. Medicine, Guy's Hospital, London SE1 9RT, United Kingdom; Nicholson, K.G., Department of Microbiology, Leicester University, Leicester, United Kingdom; Wang, J.H., Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom; Ireland, D.C., Department of Microbiology, Leicester University, Leicester, United Kingdom; Jordan, S., Department of Immunocytochemistry, St. Bartholomew's Hospital, London, United Kingdom; Duddle, J.M., Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom; Hamilton, S., Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom; Davies, R.J., Department of Respiratory Medicine, St. Bartholomew's Hospital, London, United Kingdom","Background. Cold virus infections are associated with asthma attacks and with increased bronchial responsiveness even in normal subjects. Possible mechanisms include epithelial damage, interaction with adhesion molecules or with T-helper cell subsets. Objective. To determine whether colds increase lower airway inflammation, comparing atopic with non-atopic normal subjects. Methods. Thirty healthy volunteers (15 atopic) took part. Baseline tests included viral serology, microbiological culture and polymerase chain reaction for rhinovirus infection (HRV-PCR), histamine bronchial provocation and bronchoscopy. Twenty subjects (eight atopic) underwent repeat tests when they developed a cold. Results. Forced expiratory volume in one second (FEV1) was significantly lower during colds (-0.19 L [95% confidence interval -0.10, -0.29], P = 0.0004) and there was a significant increase in bronchial responsiveness (+0.62 doublings of the dose-response slope [+0.24, +1.00], P = 0.003). Eight subjects (two atopic) had a diagnosed viral infection: two HRV, three coronavirus (HCV), one HRV + HCV, one parainfluenza III (PI) and one respiratory syncytial virus (RSV) (also Haemophilus influenzae). In biopsies, during colds, total eosinophils (EG1+) increased significantly (geometric mean 6.73-fold [1.12,40.46], P = 0.04). Activated eosinophils (EG2+) only increased significantly in the subgroup without diagnosed viral infection and particularly in atopic rhinitics. T-suppressor (CD8+) cells also increased significantly (median +178.3 cells mm2, P = 0.004). Epithelial expression of intercellular adhesion molecule-1 (ICAM-1) expression increased in four atopic rhinitics during colds. Bronchial washings showed a significant increase in neutrophils (GM 1.53-fold [1.04,2.25], P = 0.02). Conclusion. Lower airway inflammation was present in atopic and non-atopic normal subjects with colds. Atopic subjects differed in that they were less likely to have positive virological tests and were more likely to show activated eosinophilia in the lower airway, despite a similar spectrum of symptoms.","Allergic; Atopy; Bronchial inflammation; Common cold; Eosinophil; Intercellular adhesion molecule-1; Rhinitis","cell adhesion molecule; intracellular adhesion molecule 1; unclassified drug; adult; article; atopy; bronchitis; clinical article; common cold; controlled study; eosinophil; eosinophilia; human; priority journal; rhinitis; spirometry; Adolescent; Adult; Bronchitis; Common Cold; Female; Humans; Hypersensitivity, Immediate; Male; Middle Aged; Respiratory Function Tests","Graham, V.A.L., Milton, A.F., Knowles, G.K., Davies, R.J., Routine antibiotics in hospital management of acute asthma (1982) Lancet, 1, pp. 418-421; McIntosh, K., Ellis, E.F., Hoffman, L.S., The association of viral and bacterial respiratory infections with exacerbations of wheezing in young asthmatic children (1973) J Pediatr, 82, pp. 578-900; Horn, M.E.C., Brain, E.A., Gregg, I., Respiratory viral infection and wheezy bronchitis in childhood (1979) Thorax, 34, pp. 23-28; Hudgel, D.W., Langston, L., Selner, J.C., McIntosh, K., Viral and bacterial infections in adults with chronic asthma (1979) Am Rev Respir Dis, 120, pp. 393-397; Mitchell, I., Inglis, J.M., Simpson, H., Viral infections as a precipitant of wheeze in children: Combined home and hospital study (1978) Arch Dis Child, 53, pp. 106-111; Johnston, S., Sanderson, G., Pattemore, P., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Ireland, D., Kent, J., Nicholson, K.G., Improved detection of rhinoviruses in nasal and throat swabs by semi-nested RT-PCR (1993) J Med Virol, 40, pp. 96-101; Empey, D.W., Laitinen, L.A., Jacobs, L., Gold, W.M., Nadel, J.A., Mechanisms of bronchial hyperreactivity in normal subjects after upper respiratory tract infection (1976) Am Rev Respir Dis, 113, pp. 131-139; Clough, J., Williams, J.D., Holgate, S.T., Effect of atopy on the natural history of symptoms, peak expiratory flow and bronchial hyperresponsiveness in 7 and 8-year-old children with cough and wheeze (1991) Am Rev Respir Dis, 143, pp. 755-760; Lemanske, R.F., Dick, E.C., Swenson, C.A., Vrtis, R.F., Rhino-virus upper respiratory tract infection increases airway hyperreactivity and late asthmatic reactions (1989) J Clin Invest, 83, pp. 1-10; Walsh, J.J., Dietlein, L.F., Low, F.N., Burch, G.E., Mogabgab, W.J., Bronchotracheal response in human influenza (1961) Arch Intern Med, 108, pp. 98-110; Soderberg, M., Hellstrom, S., Lundgren, R., Bergh, A., Bronchial epithelium in humans recently recovering from respiratory infections caused by Influenza A or Mycoplasma (1990) Eur Respir J, 3, pp. 1023-1028; Fraenkel, D.J., Bardin, P.G., Johnston, S.L., Sanderson, G., Holgate, S.T., Nasal biopsies in human rhinovirus 16 infection: An immunohistochemical study (1993) Thorax, 48, p. 1070; Naclerio, R.M., Proud, D., Lichtenstein, L.M., Kinins are generated during experimental rhinoviral colds (1987) J Infect Dis, 157, pp. 133-142; Winther, B., Gwaltney, J.M., Owen Hendley, J., Respiratory virus infection of monolayer cultures of human nasal epithelial cells (1990) Am Rev Respir Dis, 141, pp. 839-845; Turner, R.B., Owen Hendley, J., Gwaltney, J.M., Shedding of infected epithelial cells in rhinovirus colds (1982) J Infect Dis, 145, pp. 849-853; Staunton, D.E., Merluzzi, V.J., Rothlein, R., A cell adhesion molecule ICAM-1 is the major surface receptor for rhinoviruses (1989) Cell, 56, pp. 849-853; Wegner, C.D., Gundel, R.H., Reilly, P., Intercellular adhesion molecule-1 (ICAM-1) in the pathogenesis of asthma (1990) Science, 247, pp. 456-459; Campbell, A.M., Vignola, A.M., Chanez, P., HLA-DR and ICAM-1 expression on bronchial epithelial cells in asthma and chronic bronchitis (1993) Am Rev Respir Dis, 148, pp. 689-694; Manolitsas, N.D., Trigg, C.J., McAulay, A., The expression of intercellular adhesion molecule-1 and the 31-integrins in asthma (1994) Eur Resp J, 7, pp. 1439-1444; Look, D.C., Rapp, S.R., Keller, B.T., Holtzman, M.J., Selective induction of intercellular adhesion molecule-1 by interferon-gamma in human airway epithelial cells (1992) Am J Physiol, 263, pp. L79-L87; Hsia, J., Goldstein, A.L., Simon, G.L., Sztein, M., Hayden, F.G., Peripheral blood mononuclear cell interleukin-2 and interferon-gamma production, cytotoxicity and antigen-stimulated blastogenesis during experimental rhinovirus infection (1990) J Infect Dis, 162, pp. 591-597; Dustin, M.L., Rothlein, R., Bhan, A.K., Dinarello, C.S., Springer, T.A., Induction by IL-1 and interferon-gamma: Tissue distribution, biochemistry and function of a natural adherence molecule (ICAM-1) (1986) J Immunol, 137, pp. 245-253; Djukanovic, R., Wilson, J.W., Britten, K.M., Quantification of mast cells and eosinophils in the bronchial mucosa of symptomatic atopic asthmatics and healthy control subjects using immunohistochemistry (1990) Am Rev Respir Dis, 142, pp. 863-871; Knudson, R.J., Lebowitz, M.D., Holberg, C.J., Burrows, B., Changes in the normal maximal expiratory flow-volume curve with growth and aging (1983) Am Rev Respir Dis, 127, pp. 725-734; Trigg, C.J., Bennett, J.B., Tooley, M., D'Souza, M.F., Davies, R.J., A general practice survey of bronchial hyperresponsiveness and its relation to symptoms, sex, age, atopy and smoking (1990) Thorax, 45, pp. 866-872; O'Connor, G., Sparrow, D., Taylor, D., Segal, M., Weiss, S., Analysis of dose response curves to methacholine (1987) Am Rev Respir Dis, 136, pp. 1412-1417; Bancroft, J.D., Stevens, A., (1990) Theory and Practice of Histological Techniques. 3rd Ed., , London: Churchill Livingstone; Hsu, S.M., Raine, L., Fanger, H., Use of avidin-biotin complex (ABC) in immunoperoxidase techniques. A comparison between ABC and unlabelled (PAP) techniques (1981) J Histochem Cytochem, 29, pp. 577-580; Doyle, W.J., Skoner, D.P., Fireman, P., Rhinovirus 39 infection in allergic and nonallergic subjects (1992) J Allergy Clin Immunol, 89, pp. 968-978; Bardin, P., Fraenkel, D.J., Sunderson, G., Amplified rhinovirus colds in atopic subjects (1994) Clin Exp Allergy, 24, pp. 457-464; Calderon, M.A., Devalia, J.L., Prior, A.J., Davies, R.J., Synthesis of TNF-α, IL-8 and GM-CSF by cultured nasal epithelial cells from atopic and non-atopic non-rhinitic subjects and the effect of exposure for 6 h to nitrogen dioxide (NO2) (1994) Clin Exp Allergy, 24, p. 977; Halperin, S.A., Eggleston, P.A., Hendley, J.O., Pathogenesis of lower respiratory tract symptoms in experimental rhinovirus infection (1983) Am Rev Respir Dis, 128, pp. 806-810; Calhoun, W.J., Reed, H.E., Stevens, C.A., Busse, W.W., Experimental rhinovirus 16 infection potentiates airway inflammation only in allergic subjects (1991) Am Rev Respir Dis, 143, pp. A47; Levandowski, R.A., Weaver, C.W., Jackson, G.G., Nasal secretion leukocyte populations determined by flow cytometry during acute rhinovirus infection (1988) J Med Virol, 25, pp. 423-432; Levandowski, R.A., Ou, D.W., Jackson, G.G., Acute-phase decrease of T-lymphocyte subsets in rhinovirus infection (1986) J Infect Dis, 153, pp. 743-748; Igarashi, Y., Skoner, D.P., Doyle, W.J., Analysis of nasal secretions during experimental rhinovirus upper respiratory infections (1993) J Allergy Clin Immunol, 92, pp. 722-731; Skoner, D.P., White-side, T.L., Wilson, J.W., Effect of rhinovirus 39 infection on cellular immune parameters in allergic and non-allergic subjects (1993) J Allergy Clin Immunol, 92, pp. 732-743","Trigg, C.J.; Dept. of Allergy and Resp. Medicine, Guy's Hospital, London SE1 9RT, United Kingdom",,,09547894,,CLEAE,"8809424","English","CLIN. EXP. ALLERGY",Article,"Final",,Scopus,2-s2.0-0029971899
"Grötzinger C., Heusipp G., Ziebuhr J., Harms U., Süss J., Siddell S.G.","6602152610;6603559110;7003783935;7006641137;7005307130;7005260816;","Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E",1996,"Virology","222","1",,"227","235",,29,"10.1006/viro.1996.0413","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242673508&doi=10.1006%2fviro.1996.0413&partnerID=40&md5=3a41c8b98946152199d15a55b3f40afd","Department of Viral Zoonoses, Fed. Inst. for Hlth. Protect. of C., 12277 Berlin, Germany; Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Grötzinger, C., Department of Viral Zoonoses, Fed. Inst. for Hlth. Protect. of C., 12277 Berlin, Germany, Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Heusipp, G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Harms, U., Department of Viral Zoonoses, Fed. Inst. for Hlth. Protect. of C., 12277 Berlin, Germany, Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Süss, J., Department of Viral Zoonoses, Fed. Inst. for Hlth. Protect. of C., 12277 Berlin, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Gene 1 of the human coronavirus HCV 229E encompasses approximately 20.7 kb and contains two overlapping open reading frames, ORF 1a and ORF 1b. The downstream ORF 1b is expressed by a mechanism involving (-1) ribosomal frameshifting. Translation of mRNA 1, which is thought to be equivalent to the viral genomic RNA, results in the synthesis of two large polyproteins, pp1a and pp1ab. These polyproteins contain motifs characteristic of papain-like and 3C-like proteinases, RNA-dependent RNA polymerases, helicases, and metal-binding proteins. In this study, we have produced pp1ab-specific monoclonal antibodies and have used them to detect an intracellular, 105-kDa viral polypeptide that contains the putative RNA polymerase domain. Furthermore, using trans cleavage assays with bacterially expressed HCV 229E 3C-like proteinase, we have demonstrated that the 105-kDa polypeptide is released from pp1ab by cleavage at the dipeptide bonds Gln-4068/Ser-4069 and Gln-4995/Ala-4996. These data contribute to the characterization of coronavirus 3C-like proteinase-mediated processing of pp1ab and provide the first identification of an HCV 229E ORF 1ab-encoded polypeptide in virus-infected cells.",,"monoclonal antibody; proteinase; virus protein; article; controlled study; Coronavirus; epitope mapping; human; human cell; molecular cloning; open reading frame; priority journal; protein analysis; protein processing; Coronavirus; Hepatitis C virus; human coronavirus","Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Brierley, I., Jenner, A.J., Inglis, S.C., Mutational analysis of the 'slippery-sequence' component of a coronavirus ribosomal frameshifting signal (1992) J. Mol. Biol., 227, pp. 463-479; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Fu, K., Baric, R.S., Map locations of mouse hepatitis virus temperature-sensitive mutants: Confirmation of variable rates of recombination (1994) J. Virol., 68, pp. 7458-7466; Gallagher, S., Winston, S.E., Fuller, S.A., Hurrell, J.G.R., Immunoblotting and immunodetection (1991) Current Protocols in Immunology, pp. 8101-81017. , J. E. Coligan et al., Eds. Wiley, New York; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Harlow, E., Lane, D., (1988) Antibodies: A Laboratory Manual, , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275. , in press; Johnston, S., Holgate, S., Epidemiology of viral respiratory tract infections (1996) Viral and Other Infections of the Human Respiratory Tract, pp. 1-38. , S. Myint and D. Taylor-Robinson, Eds. Chapman & Hall, London; Kozak, M., Compilation and analysis of sequences upstream from the translational start site in eucaryotic mRNAs (1984) Nucleic Acids Res., 12, pp. 857-872; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Ia Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., DeVries, J.R., Haspel, M.V., Genetic analysis of murine hepatitis virus strain JHM (1982) J. Virol., 42, pp. 1080-1087; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Myint, S.H., Human coronavirus infections (1995) The Coronaviridae, pp. 389-401. , S. G. Siddell, Ed. Plenum, New York; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glykoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Rüther, U., Müller-Hill, B., Easy identification of cDNA clones (1983) EMBO J., 2, pp. 1791-1794; Schaad, M.C., Stohlman, S.A., Egbert, J., Lum, K., Fu, K., Wei, T., Baric, R.S., Genetics of mouse hepatitis virus transcription: Identification of cistrons which may function in positive and negative strand RNA synthesis (1990) Virology, 177, pp. 634-645; Tabor, S., Richardson, C.C., A bacteriophage T7 polymerase/promoter system for controlled exclusive expression of specific genes (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 1074-1078; Wege, H., Wege, H., Nagashima, K., Ter Meulen, V., Structural polypeptides of the murine coronavirus JHM (1979) J. Gen. Virol., 42, pp. 37-47; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J. Med. Virol., 44, pp. 152-161; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Siddell, S.G.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,"Academic Press Inc.",00426822,,VIRLA,"8806502","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0242673508
"Schultze B., Krempl C., Ballesteros M.L., Shaw L., Schauer R., Enjuanes L., Herrler G.","7006104520;6602462665;7006110601;7402572957;7102195839;7006565392;7006339246;","Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-Glycolylneuraminic acid) binding activity",1996,"Journal of Virology","70","8",,"5634","5637",,84,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030004116&partnerID=40&md5=486f500f52c17ca5a2f464fea836e90d","Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg, Germany; Institut für Biochemie, Chrstn.-Albrechts-Univ. Kiel, D-24098 Kiel, Germany; Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Universidad Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany","Schultze, B., Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg, Germany; Krempl, C., Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg, Germany; Ballesteros, M.L., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Universidad Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Shaw, L., Institut für Biochemie, Chrstn.-Albrechts-Univ. Kiel, D-24098 Kiel, Germany; Schauer, R., Institut für Biochemie, Chrstn.-Albrechts-Univ. Kiel, D-24098 Kiel, Germany; Enjuanes, L., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Universidad Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Herrler, G., Institut für Virologie, Philipps-Universität Marburg, 35037 Marburg, Germany, Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany","The hemagglutinating activity of transmissible gastroenteritis virus (TGEV), an enteric porcine coronavirus, was analyzed and found to be dependent on the presence of α-2,3-linked sialic acid on the erythrocyte surface. N-Glycolylneuraminic acid was recognized more efficiently by TGEV than was N-acetylneuraminic acid. For an efficient hemagglutination reaction the virions had to be treated with sialidase. This result suggests that the sialic acid binding site is blocked by virus-associated competitive inhibitors. Porcine respiratory coronavirus (PRCV), which is serologically related to TGEV but not enteropathogenic, was found to be unable to agglutinate erythrocytes. Incubation with sialidase did not induce a hemagglutinating activity of PRCV, indicating that the lack of this activity is an intrinsic property of the virus and not due to the presence of competitive inhibitors. Only monoclonal antibodies to an antigenic site that is absent from the S protein of PRCV were able to prevent TGEV from agglutinating erythrocytes. The epitope recognized by these antibodies is located within a stretch of 224 amino acids that is missing in the S protein of PRCV. Our results indicate that the sialic acid binding activity is also located in that portion of the S protein. The presence of a hemagglutinating activity in TGEV and its absence in PRCV open the possibility that the sialic acid binding activity contributes to the enterotropism of TGEV.",,"hemagglutinin; sialic acid; virus protein; antigen binding; article; binding site; controlled study; coronavirus; hemagglutination; nonhuman; priority journal; protein analysis; protein binding; Animals; Binding Sites; Coronavirus; N-Acetylneuraminic Acid; Transmissible gastroenteritis virus; Viral Proteins","Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J. Gen. Virol., 76, pp. 2235-2241; Bingham, R.W., Madge, M.H., Tyrrell, D.A.J., Haemagglutination by avian infectious bronchitis virus - A coronavirus (1975) J. Gen. 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Virol., 67, pp. 1405-1418; Delmas, B., Gelfl, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-420; Delmas, B., Gelfi, J., Sjöström, H., Noren, O., Laude, H., Further characterisation of aminopeptidase-N as a receptor for coronaviruses (1993) Coronaviruses: Molecular Biology and Virus-host Interactions, pp. 293-298. , H. Laude and J. F. Vautherot (ed.), Plenum Press, New York; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, pp. 337-376. , S. G. Siddell (ed.), Plenum Press, New York; Gebauer, F., Posthumus, W.A.P., Correa, I., Suné, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Herrler, G., Hausmann, J., Klenk, H.-D., Sialic acid as receptor determinant of ortho- and paramyxoviruses (1995) Biology of the Sialic Acids, pp. 315-336. , A. Rosenberg (ed.), Plenum Press. New York; King, B., Potts, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Res., 2, pp. 1010-1013; Lepers, A., Shaw, L., Cacan, R., Schauer, R., Montreuil, J., Verbert, A., Transport of CMP-N-glycoloylneuraminic acid into mouse liver Golgi vesicles (1989) FEBS Lett., 250, pp. 245-250; Morrison, L.A., Fields, B.N., Parallel mechanisms in neuropathogenesis of enteric virus infections (1991) J. Virol., 65, pp. 2767-2772; Noda, M., Koide, F., Asagi, M., Inaba, Y., Physicochemical properties of transmissible gastroenteritis virus hemagglutinin (1988) Arch. Virol., 99, pp. 163-172; Noda, M., Yamashita, H., Koide, F., Kadoi, K., Omori, T., Asagi, M., Naba, Y., Hemagglutination with transmissible gastroenteritis virus (1987) Arch. Virol., 96, pp. 109-115; Pensaert, M., Callebaut, P., Cox, E., Enteric coronaviruses of animals (1993) Viral Infections of the Gastrointestinal Tract, pp. 627-696. , A. Z. Kapikian (ed.), Marcel Dekker, New York; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-260; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Reuter, G., Stoll, S., Kamerling, J.P., Vliegenthart, J.F.G., Schauer, R., Sialic acids on erythrocytes and in blood plasma of mammals (1988) Proceedings of the Japanese-German Symposium on Sialic Acids, pp. 88-89. , R. Schauer and T. Yamakawa (ed.), Sialic acids 1988. Kieler Verlag Wissenschaft und Bildung, Kiel, Germany; Saif, L.J., Comparative aspects of enteric viral infections (1990) Viral Diarrheas of Man and Animals, pp. 9-31. , L. J. Saif and K. W. Theil (ed.), CRC Press, Inc., Boca Raton, Fia; Sánchez, C.M., Gebauer, F., Suné, C., Jiménez, G., Laviada, M.D., Correa, I., Maria, J.B., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanchez, C.M., Jiménez, G., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Schultze, B., Cavanagh, D., Herrler, G., Neuraminidase treatment of avian infectious bronchitis virus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes (1992) Virology, 189, pp. 792-794; Schultze, B., Gross, H.-J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Schultze, B., Gross, H.J., Brossmer, R., Klenk, H.-D., Herrler, G., Hemagglutinating encephalomyelitis virus attaches to N-acetyl-9-O-acetylneuraminic acid-containing receptors on erythrocytes: Comparison with bovine coronavirus and influenza C virus (1990) Virus Res., 16, pp. 185-194; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J. Gen. Virol., 73, pp. 901-906; Sehultze, B., Wahn, K., Klenk, H.-D., Herrler, G., Isolated HE protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Suné, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Vlasak, R., Luyrjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 4526-4529; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Herrler, G.; Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany",,,0022538X,,JOVIA,"8764078","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030004116
"Castro R.F., Perlman S.","7202082372;7102708317;","Differential antigen recognition by T cells from the spleen and central nervous system of coronavirus-infected mice",1996,"Virology","222","1",,"247","251",,14,"10.1006/viro.1996.0415","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030219038&doi=10.1006%2fviro.1996.0415&partnerID=40&md5=5b8bda55bb6e22f7412debea6c2f13fb","Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Castro, R.F., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","CD8+ cytotoxic T lymphocytes (CTLs) isolated from the central nervous system (CNS) of C57Bl/6 mice acutely infected with mouse hepatitis virus, strain JHM (MHV-JHM), and analyzed in a direct ex vivo cytotoxicity assay recognize two epitopes (H-2Db- and H-2Kb-restricted encompassing amino acids 510-518 and 598-605, respectively) within the surface (S) glycoprotein. In contrast, CD8+ T cells isolated from the spleens of mice inoculated intraperitoneally with MHV-JHM and restimulated in vitro only respond to the H-2Db-restricted epitope. In this report, the preferential recognition of the H-2Db-restricted epitope is confirmed using splenocytes stimulated in vitro with either MHV-JHM-infected MC57 cells or with a cell line expressing the S protein and analyzed in secondary CTL assays. To determine whether these results represent a difference in epitope recognition between the spleen and CNS, secondary CTL assays were performed using spleen cells coated with peptides encompassing the CTL epitopes as stimulators. Under these conditions, both epitopes sensitized cells for lysis by spleen-derived CTLs, suggesting that both epitopes were recognized by splenic CD8+ T cells after infection in vivo. Furthermore, limiting dilution analysis indicated that the precursor frequency of splenic CD8+ T cells specific for both the H-2Kb- and H-2Db-restricted epitopes were not significantly different. Thus, the results suggest that in vitro stimulation of splenocytes specific for the H-2Kb-restricted epitope is inefficient after endogenous processing but that this inefficiency can be corrected if peptide is provided exogenously at sufficiently high concentrations. As a consequence, the results also show that cells responsive to both of the previously identified CNS-derived CD8+ T cell epitopes are present in the infected spleen at nearly the same frequency.",,"CD8 antigen; epitope; animal cell; antigen recognition; article; central nervous system; controlled study; Coronavirus; cytotoxic T lymphocyte; mouse; nonhuman; priority journal; spleen; T lymphocyte; Animalia; Coronavirus; Murine hepatitis virus","Castro, R.F., Perlman, S., (1995) J. Virol., 69, pp. 8127-8131; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., (1996) J. Gen. Virol., 77, pp. 315-325; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., (1949) J. Exp. Med., 90, pp. 181-194; Lampert, P.W., Sims, J.K., Kniazeff, A.J., (1973) Acta Neuropathol., 24, pp. 76-85; Nagashima, K., Wege, H., Meyermann, R.T., Meulen, V., (1978) Acta Neuropathol., 44, pp. 63-70; Perlman, S., Schelper, R., Bolger, E., Ries, D., (1987) Microb. Pathog., 2, pp. 185-194; Sorensen, O., Perry, D., Dales, S., (1980) Arch. Neurol., 37, pp. 478-484; Weiner, L.P., (1973) Arch. Neurol., 28, pp. 298-303; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., (1991) J. Neuroimmunol., 32, pp. 1-9; Wang, F., Fleming, J.O., Lai, M.M.C., (1992) Virology, 186, pp. 742-749; Taguchi, F., Kubo, H., Takahashi, H., Suzuki, H., (1995) Virology, 208, pp. 67-74; Stohlman, S.A., Bergmann, C.C., Van Der Veen, R.C., Hinton, D.R., (1995) J. Virol., 69, pp. 684-694; Stohlman, S.A., Matsushima, G.K., Casteel, N., Weiner, L.P., (1986) J. Immunol., 136, pp. 3052-3056; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., (1989) Virology, 173, pp. 664-673; Nakanaga, K., Yamanouchi, K., Fujiwara, K., (1986) J. Virol., 59, pp. 168-171; LaMonica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., (1991) Virology, 182, pp. 883-888; Lecomte, J., Cainelli-Gebara, V., Mercier, G., Mansour, S., Talbot, P.J., Lussier, G., Oth, D., (1987) Arch. Virol., 97, pp. 123-130; Körner, H., Schliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S., Wege, H., (1991) J. Immunol., 147, pp. 2317-2323; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., (1989) Virology, 168, pp. 162-167; Haspel, M.V., Lampert, P.W., Oldstone, M.B.A., (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 4033-4036; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., (1986) J. Virol., 59, pp. 463-471; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., (1984) Virology, 132, pp. 261-270; Williamson, J.S., Stohlman, S.A., (1990) J. Virol., 64, pp. 4589-4592; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., (1994) J. Virol., 68, pp. 5483-5495; Gombold, J., Sutherland, R., Lavi, E., Paterson, Y., Weiss, S.R., (1995) Microb. Pathog., 18, pp. 211-221; Castro, R.F., Evans, G.D., Jaszewski, A., Perlman, S., (1994) Virology, 200, pp. 733-743; Stohlman, S.A., Kyuwa, S., Cohen, M., Bergmann, C., Polo, J.M., Yen, J., Anthony, R., Keck, J.G., (1992) Virology, 189, pp. 217-224; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., (1993) Virology, 196, pp. 45-56; Moskophidis, D., Assmann-Wischer, U., Simon, M.M., Lehmann-Grube, F., (1987) Eur. J. Immunol., 17, pp. 937-942; Tripp, R.A., Hou, S., McMickle, A., Houston, J., Doherty, P.C., (1995) J. Immunol., 154, pp. 6013-6021; Kyuwa, S., Cohen, M., Nelson, G., Tahara, S.M., Stohlman, S.A., (1994) J. Virol., 68, pp. 6815-6819; Correale, J., Li, S., Weinter, L., Gilmore, W., (1995) J. Neurosci. Res., 40, pp. 10-21; Heemskerk, M., Schoemaker, H., Spaan, W., Boog, C., (1995) Immunology, 84, pp. 521-527; Castelmur, I., Dipaolo, C., Bachmann, M.F., Hengartner, H., Zinkernagel, R.M., Kundig, T.M., (1993) Cell, Immunol., 151, pp. 460-466; Mobley, J., Evans, G., Dailey, M.O., Perlman, S., (1992) Virology, 187, pp. 443-452; Taswell, C., (1981) J. Immunol., 126, pp. 1614-1619","Perlman, S.; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States",,"Academic Press Inc.",00426822,,VIRLA,"8806504","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030219038
"Suresh Christopher D., Esther Sheela S., Veni M., Rajashree B., Murugan M., Rajendran M.P., Anbumani S.P., Doraiswami J.","6602706597;6508270093;7801561245;7801351829;7003444937;57197489604;6603492231;6602355552;","An outbreak of infectious bronchitis in poultry : Epidemiology, clinicopathology and isolation and identification of virus",1996,"Indian Journal of Animal Sciences","66","8",,"755","759",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030506538&partnerID=40&md5=14c92b4f5740172ccd660b4729e194be","Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Referal Lab., Madras 600 018, India; Department of Animal Husbandry, Madras, Tamil Nadu 600 006, India","Suresh Christopher, D., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Esther Sheela, S., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Veni, M., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Rajashree, B., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Murugan, M., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Rajendran, M.P., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India; Anbumani, S.P., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India, Department of Animal Husbandry, Madras, Tamil Nadu 600 006, India; Doraiswami, J., Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India, Referal Lab., Madras 600 018, India","An acute drop in egg production in layers of Tamil Nadu during 1992 was investigated. Epidemiology and clinicopathological findings led to the suspicion for avian infectious bronchitis (AIB). A filterable virus was isolated in chicken embryos (CE) and was confirmed to be infectious bronchitis virus (IBV) by haemagglutination (HA) after treatment with phospholipase-C and specific inhibition (HI) with reference IBV-M41 antiserum. The virus isolate interfered with NDV replication in CE, resulting in 2 log2 reduction in HA activity. Transmission electron microscopy showed the isolate to be a Coronavirus which was serologically related to IBV-M41, as assessed by HI test. Possible concurrent infection with NDV/EDS'76 viruses were ruled out.",,,"Beach, J.R., Schalm, O.W., A filterable virus, distinct from that of laryngotracheitis : The cause of a respiratory disease of chick (1936) Poultry Science, 15, pp. 199-206; Berry, D.M., Cruickshank, J.G., Chu, H.P., Wells, R.J.H., The structure of infectious bronchitis virus (1964) Virology, 23, pp. 403-407; Cunningham, C.H., Immunity to avian infectious bronchitis (1975) Developments in Biological Standardization, 28, pp. 546-562. , International Symposium on Immunity to Infections of Respiratory Systems of Man and Animals; Hidalgo, H., Gallando, R., Vivan, J., Toro, H., Identification of field isolates of infectious bronchitis virus by interference with the LaSota strain of Newcastle disease virus (1985) Avian Diseases, 29, pp. 335-340; Hofstad, M.S., Avian infectious bronchitis (1978) Diseases of Poultry. 7th Edn, pp. 487-503. , (Eds) Hofstad M S, Calneck B W, Helmboldt C F, Reid W M and Yoder H W (Jr). Iowa State University Press, Ames, Iowa; Lashgari, M.S., Newman, J.A., Preparing a haemagglutinating antigen from isolates of infectious bronchitis virus (1982) Avian Diseases, 26, pp. 508-519; Lashgari, M.S., Newman, J.A., Determination of the antigenic relationship within the Massachusetts (M-41) type of infectious bronchitis virus using the haemagglutination-inhibition test (1984) Avian Diseases, 28, pp. 444-452; McFerran, J.B., Rowley, H.M., McNutty, M.S., Montgomerty, L.J., Serological studies in flocks showing depressed egg production (1977) Avian Diseases, 6, pp. 405-413; McFerran, J.B., McNutty, M.S., Curran, W.L., Diagnosis of avian viral diseases by electron microscopy (1978) American Journal of Veterinary Research, 39, pp. 505-508; Melnick, J.L., Classification and nomenclature of viruses (1972) Progress in Medical Virology, 15, pp. 382-384; Schalk, A.F., Hawn, M.C., An apparently new respiratory disease of baby chicks (1931) JAVMA, 78, pp. 413-422; Senovian, M., Levine, P.P., Effects of infectious bronchitis on the reproductive tracts, egg production and egg quality of laying chickens (1957) Avian Diseases, 1, pp. 136-164; Sukumar, S., Prabhakar, T.G., An outbreak of infectious bronchitis among poultry in Tamil Nadu (1993) Indian Journal of Animal Sciences, 63, pp. 820-822; Verma, K.C., Mallick, B.S., Isolation of infectious bronchitis virus (IBV) of poultry in India (1971) Indian Veterinary Journal, 48, pp. 887-892; Wadey, C.N., Faragher, J.F., Australian infectious bronchitis viruses : Identification of nine serotypes by a neutralization test (1981) Research in Veterinary Sciences, 30, pp. 70-74; Zellen, G.K., Thorsen, J., Standardization and application of the enzyme-linked immunosorbent assay for infectious bronchitis (1986) Avian Diseases, 30, pp. 695-698","Suresh Christopher, D.; Inst. of Vet. Preventive Medicine, Ranipet, Tamil Nadu 632 402, India",,,03678318,,,,"English","Indian J. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0030506538
"Uttenthal A., Jensen N.P.B., Blom J.Y.","6701449735;7201410580;57197578006;","Viral aetiology of enzootic pneumonia in Danish dairy herds: Diagnostic tools and epidemiology",1996,"Veterinary Record","139","5",,"114","117",,33,"10.1136/vr.139.5.114","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030567779&doi=10.1136%2fvr.139.5.114&partnerID=40&md5=9d0721e32652d679b4daa2c68cbe7857","Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Uggerslev Animal Clinic, DK-5450 Otterup, Denmark; Natl. Comm. on Danish Cattle Husb., Udkaersvej 15, Skejby, DK-8200 Århus, Denmark","Uttenthal, A., Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Jensen, N.P.B., Uggerslev Animal Clinic, DK-5450 Otterup, Denmark; Blom, J.Y., Natl. Comm. on Danish Cattle Husb., Udkaersvej 15, Skejby, DK-8200 Århus, Denmark","Ten outbreaks of calf respiratory disease in Danish dairy herds were investigated by lung lavage, and in eight of the herds paired blood samples were tested serologically. In six of the 10 herds bovine respiratory syncytial virus (BRSV) antigen was detected in the lung lavage fluids. In only one calf was coronavirus and BRSV detected simultaneously. The paired blood samples confirmed that four of the herds were BRSV-infected, and in one herd the BRSV infection was diagnosed by the paired blood samples alone. Significant increases in antibody titres against coronavirus were observed in two herds, both in combination with other virological agents. No adenovirus antigen was detected in any of the lavage samples, but in two herds a significant increase in antibody titres against adenovirus was observed. Parainfluenza-3 (PI-3) virus was not detected in the lung lavage fluids, and in four of the herds no antibodies to PI-3 were detected. In three herds no viral involvement could be found. The findings suggest that BRSV may be an important causative agent in calf respiratory disease in Denmark, even in very young calves.",,"Adenoviridae; Bovinae; Bovine respiratory syncytial virus; Coronavirus; parainfluenza 3; Respiratory syncytial virus; Syncytial virus; virus antigen; animal; animal disease; article; cattle; cattle disease; comparative study; Denmark; epidemic; female; isolation and purification; lung; Respiratory syncytial pneumovirus; virology; virus infection; Animals; Antigens, Viral; Cattle; Cattle Diseases; Denmark; Disease Outbreaks; Female; Lung; Respiratory Syncytial Virus Infections; Respiratory Syncytial Virus, Bovine","Baker, C.J., Werdin, R.E., Ames, T.R., Markham, R.J.F., Larson, V.I., (1986) Journal of the American Veterinary Medical Association, 189, p. 66; Bitsch, V., Friis, N.F., Krogh, H.V., (1976) Acta Veterinaria Scandinavica, 17, p. 32; Blom, J.Y., (1981), PhD thesis, Royal Veterinary and Agricultural University, Denmark; Harlow, E., Lane, D., (1988) Antibodies, a Laboratory Manual, p. 341. , Cold Spring Harbour, Cold Spring Harbour Laboratoy; Højbjerg, A., (1983) Bovine Practitioner, 18, p. 68; Kimman, T.G., Westenbrink, F., Schreuder, B.E.C., Straver, P.J., (1987) Journal of Clinical Microbiology, 25, p. 1097; Kimman, T.G., Zimmer, G.M., Straver, P.J., Deleeuw, P.W., (1986) American Journal of Velertnary Research, 47, p. 147; Madsen, E.B., (1984), PhD thesis, Royal Veterinary and Agricultural University. - Denmark; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., (1984) Veterinary Microbiology, 9, p. 425; Meyling, A., (1982) Current Topics in Veterinary Medicine and Animal Science, 22, p. 161; Meyling, A., Jensen, A.M., (1988) Veterinary Microbiology, 17, p. 97; Mohanty, S.B., (1978) Advances in Vetennaiy Science and Comparative Medicine, 22, p. 83; Palfi, V., Houe, H., Philipsen, J., (1993) Acta Veterinaria Scandinavica, 34, p. 105; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., (1985) Archives of Virology, 85, p. 71; Uttenthal, Å., Philipsen, J.S., (1994) Proceedings of the 9th International Conference on Negative RNA Viruses, p. 134. , Estoril, Portugal; Van Der Poel, W.H.M., Kramps, J.A., Middel, W.G.J., Van Oirschot, J.T., Brand, A., (1993) Archives of Virology, 133, p. 309; Van Donkersgoed, J., Ribbe, C.S., Boyer, L.G., Townsend, G.C., (1993) Canadian Journal of Veterinary Research, 57, p. 247; Verhoeff, J., Van Nieuwstadt, A.P.K.M.I., (1984) Veterinary Record, 114, p. 288; Østergaard, V., Blom, J.Y., Thysen, I., (1986) The Effect of Sectioning Calf Houses on Calf Health, Weight Gain and Economy, , Report 610, National Institute of Animal Science, Denmark","Uttenthal, A.; Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark",,"British Veterinary Association",00424900,,VETRA,"8856889","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0030567779
"Lu X., Lu Y., Denison M.R.","56137171400;47661483000;7101971810;","Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59",1996,"Virology","222","2",,"375","382",,43,"10.1006/viro.1996.0434","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030586696&doi=10.1006%2fviro.1996.0434&partnerID=40&md5=249d7109e4b4da6459d5cef50c1957db","Department of Pediatrics, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States; Dept. of Microbiology/Immunology, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States","Lu, X., Department of Pediatrics, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States; Lu, Y., Dept. of Microbiology/Immunology, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States; Denison, M.R., Department of Pediatrics, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States, Dept. of Microbiology/Immunology, Vanderbilt Univ. Medical Center, Nashville, TN 37232-2581, United States","The coronavirus mouse hepatitis virus-A59 (MHV-A59) encodes a serine-like proteinase (3C-like proteinase or 3CLpro) in ORF 1a of gene 1 between nucleotides 10209 and 11114. We previously have demonstrated that proteins expressed in vitro from a cDNA clone of the 3CLpro region possess proteinase activity, and that the proteinase is able to cleave substrate in trans. We sought to determine if the 27-kDa in vitro cleavage product (p27) was an active form of the 3CLpro and whether this was consistent with the 3CLpro expressed in virus-infected cells. Antibodies directed against the 3CLpro domain detected 27-kDa MHV proteins in vitro and in MHV-A59-infected cells. The 27-kDa proteins were able to cleave substrate in trans without other protein cofactors or supplemental membranes, and the p27 proteinase activity was retained after purification by immunoprecipitation and gel electrophoresis. When p27 was expressed in vitro with portions of the amino- and carboxy-terminal flanking domains (MP1 and MP2), p27 was not liberated by cis cleavage. The proteolytic activity of the 27-kDa proteins was inhibited by a variety of cysteine and serine proteinase inhibitors, and was eliminated by the cysteine proteinase inhibitor E64d. These results indicate that the 27-kDa protein is a mature proteinase in MHV-A59-nfected cells, and that appropriate processing of this molecule occurs in vitro.",,"proteinase; animal cell; article; controlled study; Coronavirus; enzyme activity; in vitro study; mouse; nonhuman; priority journal; protein processing; RNA translation","Amberg, S.M., Nestorowicz, A., McCourt, D.W., Rice, C.M., NS2B-3 proteinase-mediated processing in the yellow fever virus structural region: In vitro and in vivo studies (1994) J. Virol., 68, pp. 3794-3802; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Pinon, J.D., Weiss, S.R., Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bouffard, P., Bartenschlager, R., Ahlborn, L.L., Mous, J., Roberts, N., Jacobsen, H., An in vitro assay for hepatitis C virus NS3 serine proteinase (1995) Virology, 209, pp. 52-59; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Gorbalenya, A., Koonin, E., Comparative analysis of amino-acid sequences of key enzymes of replication and expression of positive-strand RNA viruses: Validity of approach and functional and evolutionary implications (1993) Sov. Sci. Rev. Sect. D: Physiochem. Biol., 11, pp. 1-81; Gorbalenya, A.E., Donchenko, A.P., Blinov, V.M., Koonin, E.V., Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases (1989) FEBS Lett., 243, pp. 103-114; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.-C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS, 288, pp. 201-205; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor, E64d (1995) Virology, 208, pp. 1-8; Kleina, L.G., Grubman, M.J., Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus (1992) J. Virol., 66, pp. 7168-7175; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadhzyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Pachuk, C.J., Breedenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Tans, G., Janssen, C.T., Rosing, J., Amidolytic detection of prothrombin activation products after SDS-gel electrophoresis (1989) Thromb. Haemostasis, 61, pp. 386-391; Wagner, O.F., Bergmann, I., Binder, B.R., Chromogenic substrate autography: A method for detection, characterization, and quantitative measurement of serine proteases after sodium dodecyl sulfate-polyacrylamide gel electrophoresis or isoelectric focusing in polyacrylamide gels (1985) Anal. Biochem., 151, pp. 7-12; Zebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Denison, M.R.; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States",,"Academic Press Inc.",00426822,,VIRLA,"8806521","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030586696
"Komurasaki Y., Nagineni C.N., Wang Y., Hooks J.J.","6603421049;6701316964;56802808200;7006661655;","Virus RNA persists within the retina in coronavirus-induced retinopathy",1996,"Virology","222","2",,"446","450",,13,"10.1006/viro.1996.0442","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030586739&doi=10.1006%2fviro.1996.0442&partnerID=40&md5=f48823312a00b2af45e1661cf56f9412","Immunology and Virology Section, Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States","Komurasaki, Y., Immunology and Virology Section, Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States; Nagineni, C.N., Immunology and Virology Section, Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States; Wang, Y., Immunology and Virology Section, Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States; Hooks, J.J., Immunology and Virology Section, Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States","The murine coronavirus, mouse hepatitis virus (MHV), JHM strain, induces a biphasic retinal disease in adult BALB/c mice. In the early phase, Day 1 to Day 7, a retinal vasculitis is noted which is associated with the presence of viral proteins and infectious virus. In the late phase, Day 10 to Day 140, a retinal degeneration is associated with the absence of viral proteins, infectious virus, and inflammatory cells. The purpose of this study was to determine if viral RNA persists within the retina during the retinal degenerative phase of the disease. BALB/c mice were inoculated by the intravitreal route with 104.0 TCID50/5 μl of virus. The presence of viral RNA was detected by in situ hybridization with a viral cDNA probe and viral proteins were identified by immunocytochemical staining. During the acute phase of the infection, viral RNA was found in the retina, RPE, ciliary body epithelium, and the iris epithelium. During the late phase of the infection, viral RNA was almost exclusively found within the retina and RPE and not in the anterior segment of the eye. Within the retina, viral RNA was detected in the ganglion cell layer, the inner retina, the outer retina, and the RPE cell. Immunocytochemical staining identified viral protein within the retina only from Day 1 to Day 8. This ocular disease was also associated with a persistent systemic infection. Both viral RNA and viral proteins were identified within the liver during the first 8 days. However, only viral RNA was detected in the liver from Day 8 to Day 60. These studies demonstrate that MHV established an acute infection (Day 1-8) where infectious virus and viral proteins were identified. This was followed by a persistent infection within the retina and liver where only viral RNA were detected by in situ hybridization.",,"RNA; animal experiment; animal tissue; article; controlled study; Coronavirus; in situ hybridization; mouse; Murine hepatitis coronavirus; nonhuman; persistent virus infection; priority journal; retina; retinopathy","Ryan, S.J., Maumenee, A.E., (1972) Am. J. Ophthalmol., 74, pp. 1066-1074; Wright, B.E., Bird, A.C., Hamilton, A.M., (1978) Br. J. Ophthalmol., 62, pp. 609-621; Culbertson, W.W., Blumenkranz, M.S., Pepose, J.S., Stewart, J.A., Curtin, V.T., (1986) Ophthalmology, 93, pp. 559-569; Sarkies, N., Gregor, Z., Forsey, T., Darougar, S., (1986) Br. J. Ophthalmol., 70, pp. 81-84; Jabs, D.A., Green, W.R., Fox, R., Polk, B.F., (1989) Ophthalmology, 96, pp. 1092-1099; Hogan, R.N., Kingsbury, D.T., Baringer, J.R., Prusiner, S.B., (1983) Lab. Invest., 49, pp. 708-715; Payne, F.E., Baublis, J.V., Itabashi, H.H., (1969) N. Engl. J. Med., 281, pp. 585-589; Robbins, S.G., Hamel, C.P., Detrick, B., Hooks, J.J., (1990) Lab. Invest., 62, pp. 417-426; Robbins, S.G., Detrick, B., Hooks, J.J., (1991) Invest. Ophthalmol. Vis. Sci., 32, pp. 1883-1893; Hooks, J.J., Robbins, S.G., Wiggert, B., Chader, G.J., Detrick, B., (1991) Retinal Degenerations, pp. 529-534. , (R. E. Anderson, J. G. Hollyfield, and M. M. LaVail, Eds.), CRC Press, Boca Raton, FL; Hooks, J.J., Percopo, C., Wang, Y., Detrick, B., (1993) J. Immunol., 151, pp. 3381-3389; Lavi, E., Fishman, P.S., Highkin, M.K., Weiss, S.R., (1988) Lab. Invest., 58, pp. 31-36; Wang, Y., Detrick, B., Hooks, J.J., (1993) Virology, 193, pp. 124-137; Detrick, B., Newsome, D.A., Percopo, C., Hooks, J.J., (1985) Clin. Immunol. Immunopathol., 36, pp. 201-211; Detrick, B., Rodrigues, M., Chan, C.C., Tso, M.O.M., Hooks, J.J., (1986) Am. J. Ophthalmol., 101, pp. 584-590; Hooks, J.J., Chan, C.C., Detrick, B., (1988) Invest. Ophthalmol. Vis. Sci., 29, pp. 1444-1451; Percopo, C., Hooks, J.J., Shinohara, T., Capsi, R., Detrick, B., (1990) J. Immunol., 145, pp. 4101-4107; Wege, H., (1995) Springer Semin. Immunopathol., 17, pp. 133-148; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., (1984) Neurology, 34, pp. 597-603; Stohlman, S.A., Weiner, L.P., (1981) Neurology, 31, pp. 38-44; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., (1984) J. Virol., 51, pp. 563-566; Perlman, S., Jacobsen, G., Moore, S., (1988) Virology, 166, pp. 328-338; Perlman, S., Jacobsen, G., Afifi, A., (1989) Virology, 170, pp. 556-560; Perlman, S., Evans, G., Afifi, A., (1990) J. Exp. Med., 172, pp. 1127-1132; Barnett, E., Perlman, S., (1993) Virology, 194, pp. 185-191; Jacobsen, G., Perlman, S., (1990) Adv. Exp. Med. Biol., 276, pp. 573-578; Decimo, D., Boespflug, Q., Meunier-Rotival, M., Hadchouel, M., Tardieu, M., (1993) Arch. Virol., 130, pp. 269-277; Murray, R.S., Cai, G.-Y., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., (1992) Virology, 188, pp. 274-284; Sorensen, O., Dales, S., (1985) J. Virol., 56, pp. 434-438; Wang, Y., Burnier, M.N., Detrick, B., Hooks, J.J., (1996) Invest. Ophthal. Vis. Sci., 37, pp. 250-254; Fujuinami, R.S., Oldstone, M.B.A., Concepts in Viral Pathogenesis, pp. 187-193. , (A. L. Notkins and M. B. A. Oldstone, Eds.), Springer-Verlag, New York; Ayata, M., Hirano, A., Wong, T.C., (1989) J. Virol., 63, pp. 1162-1173","Hooks, J.J.; Immunology and Virology Section, Laboratory of Immunology, National Eye Institute/NIH, Bethesda, MD, United States",,"Academic Press Inc.",00426822,,VIRLA,"8806529","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030586739
"Joo M., Banerjee S., Makino S.","23008647300;55851941930;7403067550;","Replication of murine coronavirus defective interfering RNA from negative-strand transcripts",1996,"Journal of Virology","70","9",,"5769","5776",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029843982&partnerID=40&md5=61e3054c9024974facd7496e6626a14d","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Microbiology, University of Texas Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States; Department of Pathology, Harvard University, Boston, MA 02115, United States","Joo, M., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Pathology, Harvard University, Boston, MA 02115, United States; Banerjee, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Microbiology, University of Texas Austin, ESB 304, 24th at Speedway, Austin, TX 78712-1095, United States","The positive-strand defective interfering (DI) RNA of the murine coronavirus mouse hepatitis virus (MHV), when introduced into MHV-infected cells, results in DI RNA replication and accumulation. We studied whether the introduction of negative-strand transcripts of MHV DI RNA would also result in replication. At a location downstream of the T7 promoter and upstream of the human hepatitis delta virus ribozyme domain, we inserted a complete cDNA clone of MHV DI RNA in reverse orientation; in vitro- synthesized RNA from this plasmid yielded a negative-strand RNA copy of the MHV DI RNA. When the negative-strand transcripts of the DI RNA were expressed in MHV-infected cells by a vaccinia virus T7 expression system, positive-strand DI RNAs accumulated in the plasmid-transfected cells. DI RNA replication depended on the expression of T7 polymerase and on the presence of the T7 promoter. Transfection of in vitro-synthesized negative-strand transcripts into MHV-infected cells and serial passage of virus samples from RNA-transfected cells also resulted in accumulation of the DI RNA. Positive- strand DI RNA transcripts were undetectable in sample preparations of the in vitro-synthesized negative-strand DI RNA transcripts, and DI RNA did not accumulate after cotransfection of a small amount of positive-strand DI RNA and truncated-replication-disabled negative-strand transcripts; clearly, the DI RNA replicated from the transfected negative-strand transcripts and not from minute amounts of positive-strand DI RNAs that might be envisioned as artifacts of T7 transcription. Sequence analysis of positive-strand DI RNAs in the cells transfected with negative-strand transcripts showed that DI RNAs maintained the DI-specific unique sequences introduced within the leader sequence. These data indicated that positive-strand DI RNA synthesis occurred from introduced negative-strand transcripts in the MHV-infected cells; this demonstration, using MHV, of DI RNA replication from transfected negative-strand DI RNA transcripts is the first such demonstration among all positive-stranded RNA viruses.",,"signal peptide; article; coronavirus; dna flanking region; genetic transfection; murine hepatitis coronavirus; nonhuman; priority journal; promoter region; rna replication; rna transcription; sequence analysis; virus replication; Animals; Artifacts; Base Sequence; Cell Line; Cloning, Molecular; Defective Viruses; DNA, Complementary; Genetic Vectors; Hepatitis Delta Virus; Humans; Mice; Molecular Sequence Data; Murine hepatitis virus; Oligodeoxyribonucleotides; Polymerase Chain Reaction; Promoter Regions (Genetics); Regulatory Sequences, Nucleic Acid; RNA, Catalytic; RNA, Viral; Transcription, Genetic; Transfection; Vaccinia virus","Ball, L.A., Replication of the genomic RNA of a positive-strand RNA animal virus from negative-sense transcripts (1994) Proc. 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Virol, 68, pp. 2615-2623; Jeong, Y.S., Repass, J.F., Kim, Y.-N., Hwang, S.M., Makino, S., Coronavirus transcription mediated by sequences flanking the transcription consensus sequence (1996) Virology, 217, pp. 311-322; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. 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USA, 81, pp. 3626-3630; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol., 46, pp. 1027-1033; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leihowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Liao, C.-L., Lai, M.M.C., A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA (1995) Virology, 209, pp. 428-436; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. 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Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shaklee, P.N., Negative-strand RNA replication by Qβ and MS positive-strand RNA phage replicases (1990) Virology, 178, pp. 340-343; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1939-1944; Tousch, D., Jacquemond, M., Tepfer, M., Replication of cucumber mosaic virus satellite RNA from negative-sense transcripts produced either in vitro or in transgenic plants (1994) J. Gen. Virol., 75, pp. 1009-1014; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Van Der Werf, S., Bradley, J., Wimmer, E., Studier, F.W., Dunn, J.J., Synthesis of infectious poliovirus RNA by purified T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 2330-2334; Weis, J.H., Race no more: An alternative approach to cloning the 5′ end of transcripts (1994) Nucleic Acids Res., 22, pp. 3427-3428; Winship, P.R., An improved method for directly sequencing PCR material using demethyl sulfoxide (1989) Nucleic Acids Res., 17, p. 1266","Makino, S.; Department of Microbiology, ESB 304, University of Texas at Austin, 24th at Speedway, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"8709192","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029843982
"Rossen J. W. A., Bekker C. P. J., Strous G. J. A. M., Horzinek M. C., Dveksler G. S., Holmes K. V., Rottier P. J. M.","7005977394;56403027300;7004975908;7102624836;6603790777;7201657724;7006145490;","A murine and a porcine coronavirus are released from opposite surfaces of the same epithelial cells",1996,"Virology","224","1",,"345","351",,15,"10.1006/viro.1996.0540","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030273298&doi=10.1006%2fviro.1996.0540&partnerID=40&md5=f6b8d3b35554d01ced1165b0c6f6829b","Virology Division, Dept. of Infect. Dis./Immunol., Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Laboratory of Cell Biology, Medical School, Utrecht University, Heidelberglaan 100, AZU-H02.314, 3584 CX Utrecht, Netherlands; Department of Pathology, Uniformed Serv. Univ. of the Hlth., Bethesda, MD 20814-4799, United States; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Campus Box B-175, 4200 East Ninth Avenue, Denver, CO 80262, United States","Rossen, J. W. A., Virology Division, Dept. of Infect. Dis./Immunol., Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Bekker, C. P. J., Virology Division, Dept. of Infect. Dis./Immunol., Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Strous, G. J. A. M., Laboratory of Cell Biology, Medical School, Utrecht University, Heidelberglaan 100, AZU-H02.314, 3584 CX Utrecht, Netherlands; Horzinek, M. C., Virology Division, Dept. of Infect. Dis./Immunol., Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Dveksler, G. S., Department of Pathology, Uniformed Serv. Univ. of the Hlth., Bethesda, MD 20814-4799, United States; Holmes, K. V., Department of Pathology, Uniformed Serv. Univ. of the Hlth., Bethesda, MD 20814-4799, United States, Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Campus Box B-175, 4200 East Ninth Avenue, Denver, CO 80262, United States; Rottier, P. J. M., Virology Division, Dept. of Infect. Dis./Immunol., Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Epithelial cells are important target cells for coronavirus infection. Earlier we have shown that transmissible gastroenteritis coronavirus (TGEV) and mouse hepatitis coronavirus (MHV) are released from different sides of porcine and murine epithelial cells, respectively. To study the release of these viruses from the same cells, we constructed a porcine LLC-PK1 cell line stably expressing the recombinant MHV receptor cDNA (LMR cells). The MHV and TGEV receptor glycoproteins were shown by immunofluorescence to appear at the surface of the cells and to be functional so that the cells were susceptible to both MHV and TGEV infection. Both coronaviruses entered polarized LMR cells only through the apical surface. Remarkably, while the cells remained susceptible to TGEV for long periods, infectability by MHV decreased with time after plating of the cells onto filters. This was not due to a lack of expression of the MHV receptor, since this glycoprotein was still abundant on the apical surface of these cells. TGEV and MHV appeared to exit LMR cells from opposite sides. Whereas TGEV was released preferentially at the apical membrane, MHV was released preferentially at the basolateral surface. These results show that vesicles containing the two coronaviruses are targeted differently in LMR cells. We propose that the viruses are sorted at the Colgi complex into different transport vesicles that carry information directing them to one of the two surface domains. The apical release of TGEV and the basolateral release of MHV might be factors contributing to the difference in virus spread found between TGEV and MHV in their respective natural hosts, the former causing mainly a localized enteric infection, the latter spreading through the body to other organs.",,"animal cell; article; cell surface; controlled study; Coronavirus; epithelium cell; mouse; nonhuman; priority journal; swine; virus shedding; Animalia; Coronavirus; Mouse hepatitis coronavirus; Murinae; Murine hepatitis virus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Holmes, K.V., (1990) Virology, pp. 841-856. , B. N. Fields, D. M. Knipe, R. M. Chanock, M. S. Hirsch, J. L. Melnick, T. P. Monath, and B. Roizman, Eds., Chap. 29, Raven Press, New York; Tucker, S.P., Compans, R.W., (1993) Adv. Virus Res., 42, pp. 187-247; Zurzolo, C., Polistina, C., Saini, M., Gentile, R., Aloj, L., Migliaccio, G., Bonatti, S., Nitsch, L., (1992) J. Cell Biol., 117, pp. 551-564; Tooze, J., Tooze, S.A., Warren, G., (1984) Eur. J. Cell Biol., 33, pp. 281-293; Klumperman, J., Krijnse Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., (1994) J. Virol., 68, pp. 6523-6534; Krijnse Locker, J., Lricsson, M., Rottier, P.J.M., Griffiths, G., (1994) J. Cell Biol., 124, pp. 55-70; Tooze, J., Tooze, S.A., Fuller, S.D., (1987) J. Cell Biol., 105, pp. 1215-1226; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., (1994) J. Virol., 68, pp. 7966-7973; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Horzinek, M.C., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., (1995) Adv. Exp. Med. Biol., 380, pp. 135-138; Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Van Der Ende, A., Strous, G.J.A.M., Rottier, P.J.M., (1995) Virology, 210, pp. 54-66; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P.J.M., Rossen, J.W.A., Holmes, K.V., (1995) J. Virol., 69, pp. 889-895; Graham, F.L., Van Der Eb, A.J., (1973) Virology, 52, pp. 456-461; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., (1990) J. Virol., 64, pp. 3817-3823; Blau, D.M., Compans, R.W., (1990) Virology, 210, pp. 91-99; Yokomori, K., Lai, M.M.C., (1992) J. Virol., 66, pp. 6931-6938; Yokomori, K., Assanaka, M., Stohlman, S.A., Lai, M.M.C., (1993) Virology, 196, pp. 45-56; Cavanagh, D., (1995) The Coronaviridae, pp. 73-113. , S. G. Siddell, Ed., Plenum, New York; Rottier, P.J.M., (1995) The Coronaviridae, pp. 115-139. , S. G. Siddell, Ed., Plenum, New York; Kitagawa, Y., Sano, Y., Ueda, M., Higashio, K., Narita, H., Okano, M., Matsumoto, S.-I., Sasaki, R., (1994) Exp. Cell Res., 213, pp. 449-457; Scheiffele, P., Peränen, J., Simons, K., (1995) Nature, 378, pp. 96-98; Rossen, J.W.A., Horzinek, M.C., Rottier, P.J.M., (1995) Trends Microbiol., 3, pp. 486-490","Rottier, P.J.M.; Dept. of Infect. Diseases/Immunol., Inst. of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,"Academic Press Inc.",00426822,,VIRLA,"8862433","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030273298
"Lin Y.-J., Zhang X., Wu R.-C., Lai M.M.C.","7406589398;55715175900;57215104575;7401808497;","The 3' untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA",1996,"Journal of Virology","70","10",,"7236","7240",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029836505&partnerID=40&md5=5ae31ea1a456b0edc5204c9d34d055e0","Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, 2011 Zonal Ave., HMR-401, Los Angeles, CA 90033-1054, United States; Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, United States","Lin, Y.-J., Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, United States; Zhang, X., Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Wu, R.-C., Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Dept. Molec. Microbiol. and Immunol., University of Southern California, School of Medicine, 2011 Zonal Ave., HMR-401, Los Angeles, CA 90033-1054, United States","The 3'-end of mouse hepatitis virus (MHV) genomic RNA contains a recognition sequence (55 nucleotides [nt]) required for minus-strand RNA synthesis. To determine whether the 3'-end sequence is also involved in subgenomic mRNA transcription, we have constructed MHV defective interfering (DI) RNAs which contain a chloramphenicol acetyltransferase (CAT) gene placed behind an intergenic sequence and a 3'-end sequence with various degrees of internal deletions. The DI RNAs were transfected into MHV-infected cells, and CAT activities, which represent subgenomic mRNA transcription from the intergenic site, were determined. The results demonstrated that the deletions of sequence upstream of the 350 nt at the 3'-end, which include the 3'- untranslated region (3'-UTR), of MHV genomic RNA did not affect subgenomic mRNA transcription. However, deletions that reduced the 3'-end sequences to 270 nt or less completely abolished the mRNA transcription despite the fact that all of these clones synthesized minus-strand RNAs. These results indicated that mRNA transcription from an intergenic site in the MHV DI RNA requires most of the 3'-UTR as a cis-acting signal, which likely exerts its effects during plus-strand RNA synthesis. A substitution of the corresponding bovine coronavirus sequence for the MHV sequence within nt 270 to 305 from the 3'-end abrogated the CAT gene expression, suggesting a very rigid sequence requirement in this region. The deletion of a putative pseudoknot structure within the 3'-UTR also abolished the CAT gene expression. These findings suggest that the 3'-UTR may interact with the other RNA regulatory elements to regulate mRNA transcription.",,"chloramphenicol acetyltransferase; messenger rna; virus rna; article; gene deletion; messenger rna synthesis; molecular cloning; murine hepatitis coronavirus; nonhuman; priority journal; rna sequence; rna transcription; transcription regulation; virus transcription; Animals; Cattle; Coronavirus; Mice; RNA, Viral; Transcription, Genetic","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., The complete nucleotide sequence of avian infectious bronchitis virus: Analysis of the polymerase-coding region (1987) Coronaviruses, 218, pp. 15-29. , M. M. C. Lai and S. A. Stohlman (ed.), Plenum Press, New York; Danthinne, X., Seurinck, J., Meulewaeter, F., Van Montagu, M., Cornelissen, M., The 3′ untranslated region of satellite tobacco necrosis virus RNA stimulates translation in vitro (1993) Mol. Cell. Biol., 13, pp. 3340-3349; Furuya, T., Lai, M.M.C., Three different cellular proteins bind to the complementary sites on the 5′-end positive- and 3′-end negative-strands of mouse hepatitis virus RNA (1993) J. Virol., 67, pp. 7215-7222; Goodwin, E.B., Okkema, P.G., Eyans, T.C., Kimble, J., Translational regulation of tra-2 by its 3′ untranslated region controls sexual identity in C. elegans (1993) Cell, 75, pp. 329-339; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Brilton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Hsu, M.-T., Parvin, J.D., Gupta, S., Krystal, M., Palese, P., Genomic RNAs of influenza viruses are held in a circular conformation in virions and in infected cells by a terminal panhandle (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 8140-8144; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effects of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Jeong, Y.S., Makino, S., Evidence for curonavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kwon, Y.K., Hecht, N.B., Binding of a phosphoprotein to the 3′ untranslated region of the mouse protamine 2 mRNA temporally represses its translation (1993) Mol. Cell. Biol., 13, pp. 6547-6557; Lahser, F.C., Marsh, L.E., Hall, T.C., Contributions of the brome mosaic virus RNA-3 3′-nontranslated region to replication and translation (1993) J. Virol., 67, pp. 3295-3303; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., Liao, C.-L., Lin, Y.-J., Zhang, X., Coronavirus: How a large RNA viral genome is replicated and transcribed (1994) Infect. Agents Dis., 3, pp. 98-105; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., The presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol., 46, pp. 1027-1033; Lai, M.M.C., Stohlman, S.A., The RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Leathers, V., Tanguay, R., Kobayashi, M., Gallie, D.R., A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation (1993) Mol. Cell. Biol., 13, pp. 5331-5347; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzyahdzhyan, A., Lai, M.M.-C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liao, C.-L., Lai, M.M.C., Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J. Virol., 68, pp. 4727-4737; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective-interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.-J., Liao, C.L., Lai, M.M.C., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Luo, G., Luytjes, W., Enami, M., Palese, P., The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure (1991) J. Virol., 65, pp. 2861-2867; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective-interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Stohlman, S.A., Lai, M.M.C., Leader sequences of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA in transcription (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 4204-4208; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J. Virol., 64, pp. 6045-6053; Ostareck-Lederer, A., Ostareck, D.H., Standart, N., Thiele, B.J., Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region (1994) EMBO J., 13, pp. 1467-1481; Ou, J.-H., Strauss, E.G., Strauss, J.H., The 5′ terminal sequences of the genomic RNAs of several alphaviruses (1983) J. Mol. Biol., 168, pp. 1-15; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus strain A59 (1989) Virology, 171, pp. 141-148; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) Proc. Natl. Acad. Sci. USA, 64, pp. 1050-1056; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Skinner, M.A., Siddell, S.G., Coronavirus JHM: Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acids Res., 11, pp. 5045-5054; Song, C., Simon, A.E., RNA-dependent RNA polymerase from plants infected with turnip crinkle virus can transcribe (+)- and (-)-strands of virus-associated RNAs (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 8792-8796; Spaan, W.J.M., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Van Belkum, A., Abrahams, J.P., Pleij, C.W.A., Bosch, L., Five pseudoknots are present at the 204-nucleotides long 3′ noncoding region of tobacco mosaic virus RNA (1985) Nucleic Acids Res., 13, pp. 7673-7686; Wertz, G.W., Whelan, S., LeGrone, A., Ball, L.A., Extent of terminal complementarity modulates the balance between transcription and replication of vesicular stomatitis virus RNA (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 8587-8591; Williams, G.D., Chang, R.-Y., Brian, D.A., Evidence for a pseudoknot in the 3′-untranslated region of the bovine Coronavirus genome (1995) Corona and Related Viruses, 380, pp. 511-514. , P. J. Talbot and G. A. Levy (ed.), Plenum Press, New York; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zhang, X., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Lai, M.M.C.; Molecular Microbiol./Immunol. Dept., USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States",,,0022538X,,JOVIA,"8794374","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029836505
"Hofmann-Lehmann R., Fehr D., Grob M., Elgizoli M., Packer C., Martenson J.S., O'Brien S.J., Lutz H.","7003867023;7004257478;16934599100;55284946000;7103089793;7006232043;7402355306;57202819852;","Prevalence of antibodies to feline parvovirus, calicivirus, herpesvirus, coronavirus, and immunodeficiency virus and of feline leukemia virus antigen and the interrelationship of these viral infections in free-ranging lions in east Africa",1996,"Clinical and Diagnostic Laboratory Immunology","3","5",,"554","562",,86,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029817018&partnerID=40&md5=da4d0c9cab5aadb8368c75a79917f48c","Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, CH-8057 Zurich, Switzerland; Veterinaria AG, CH-8021 Zurich, Switzerland; Dept. of Ecol., Evol. and Behavior, College of Biological Sciences, University of Minnesota, St. Paul, MN 55108, United States; Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick Cancer Res./Devmt. Ctr., Frederick, MD 21702-1201, United States; Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstr. 260, CH-8057 Zurich, Switzerland","Hofmann-Lehmann, R., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, CH-8057 Zurich, Switzerland, Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstr. 260, CH-8057 Zurich, Switzerland; Fehr, D., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, CH-8057 Zurich, Switzerland; Grob, M., Veterinaria AG, CH-8021 Zurich, Switzerland; Elgizoli, M., Veterinaria AG, CH-8021 Zurich, Switzerland; Packer, C., Dept. of Ecol., Evol. and Behavior, College of Biological Sciences, University of Minnesota, St. Paul, MN 55108, United States; Martenson, J.S., Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick Cancer Res./Devmt. Ctr., Frederick, MD 21702-1201, United States; O'Brien, S.J., Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick Cancer Res./Devmt. Ctr., Frederick, MD 21702-1201, United States; Lutz, H., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, CH-8057 Zurich, Switzerland","While viral infections and their impact are well studied in domestic cats, only limited information is available on their occurrence in free-ranging lions. The goals of the present study were (i) to investigate the prevalence of antibodies to feline calicivirus (FCV), herpesvirus (FHV), coronavirus (FCoV), parvovirus (FPV), and immunodeficiency virus (FIV) and of feline leukemia virus (FeLV) antigen in 311 serum samples collected between 1984 and 1991 from lions inhabiting Tanzania's national parks and (ii) to evaluate the possible biological importance and the interrelationship of these viral infections. Antibodies to FCV, never reported previously in free-ranging lions, were detected in 70% of the sera. In addition, a much higher prevalence of antibodies to FCoV (57%) was found than was previously reported in Etosha National Park and Kruger National Park. Titers ranged from 25 to 400. FeLV antigen was not detectable in any of the serum samples. FCoV, FCV, FHV, and FIV were endemic in the Serengeti, while a transient elevation of FPV titers pointed to an outbreak of EPV infection between 1985 and 1987. Antibody titers to FPV and FCV were highly prevalent in the Serengeti (FPV, 75%; FCV, 67%) but not in Ngorongoro Crater (FPV, 27%; FCV, 2%). These differences could be explained by the different habitats and biological histories of the two populations and by the well-documented absence of immigration of lions from the Serengeti plains into Ngorongoro Crater after 1965. These observations indicate that, although the pathological potential of these viral infections seemed not to be very high in free-ranging lions, relocation of seropositive animals by humans to seronegative lion populations must be considered very carefully.",,"virus antibody; africa; article; calicivirus; cat; feline immunodeficiency virus; feline leukemia virus; herpes virus; lion; nonhuman; parvovirus; priority journal; tanzania; virus infection; Africa, Eastern; Animals; Antibodies, Viral; Antigens, Viral; Calicivirus, Feline; Coronavirus; Coronavirus, Feline; Feline panleukopenia virus; Herpesviridae; Immunodeficiency Virus, Feline; Leukemia Virus, Feline; Lions","Barlough, J.E., Adsit, J.C., Scott, F.W., The worldwide occurrence of feline infectious peritonitis (1982) Feline Pract., 12, pp. 26-30; Barr, M.C., Calle, P.P., Roelke, M.E., Scott, F.W., Feline immunodeficiency virus infection in nondomestic felids (1989) J. Zoo Wildl. Med, 20, pp. 265-272; Boever, W.J., McDonald, S., Solorzano, R.F., Feline viral rhinotracheitis in a colony of clouded leopards (1977) Vet. Med. Small Anim. Clin., 72, pp. 1859-1866; Boid, R., McOrist, S., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Isolation of FeLV from a wild feud (Felis silvestris) (1991) Vet. Rec., 128, p. 256; Brown, E.W., Olmsted, R.A., Martenson, J.S., O'Brien, S.J., Exposure to FIV and FIPV in wild and captive cheetahs (1993) Zoo Biol., 12, pp. 135-142; Brown, E.W., Yuhki, N., Packer, C., O'Brien, S.J., A lion lentivirus related to feline immunodeficiency virus: Epidemiologic and phylogenetic aspects (1994) J. Virol., 68, pp. 5953-5968; Bürki, F., Starustka, B., Ruttner, O., Attempts to serologically classify feline caliciviruses on a national and an international basis (1976) Infect. Immun., 14, pp. 876-881; Callahan III, L.T., Woodhour, A.F., Meeker, J.B., Hilleman, M.R., Enzyme-linked immunosorbent assay for measurement of antibodies against pneumococcal polysaccharide antigens: Comparison with radioimmunoassay (1979) J. Clin. Microbiol., 10, pp. 459-463; Colby, E.D., Low, R.J., Feline infectious peritonitis (1970) Vet. Med. Small Anim. Clin., 65, pp. 783-786; Evermann, J.F., Burns, G., Roelke, M.E., Mckeirnan, A.J., Greenlee, A., Ward, A.C., Pfeifer, M.L., Diagnostic features of an epizootic of feline infectious peritonitis in captive cheetahs (1983) Am. Assoc. Vet. Lab. Diagn., 26, pp. 365-382; Evermann, J.F., Heeney, J.L., McKeirnan, A.J., O'Brien, S.J., Comparative features of a coronavirus isolated from a cheetah with feline infectious peritonitis (1989) Virus Res., 13, pp. 15-27; Evermann, J.F., Heeney, J.L., Roelke, M.E., McKeirnan, A.J., O'Brien, S.J., Biological and pathological consequences of feline infectious peritonitis virus infection in the cheetah (1988) Arch. Virol., 102, pp. 155-171; Fargeaud, D., Jeannin, B.C., Kato, F., Chappuis, G., Biochemical study of feline herpesvirus 1 identification of glycoproteins by affinity (1984) Arch. Virol., 80, pp. 69-82; Fehr, D., Bolla, S., Herrewegh, A.A.P.M., Horzinek, M.C., Lutz, H., Nachweis feliner Coronaviren mittels RT-PCR: Grundlage zum Studium der Pathogenese der Felinen infektiösen Peritonitis (FIP) (1995) Schweiz. Arch. Tierheilkd., 138, pp. 74-79; Hardy Jr., W.D., McClelland, A.J., Feline leukemia virus. Its related diseases and control (1977) Vet. Clin. North Am., 7, pp. 93-103; Heeney, J.L., Evermann, J.F., Mckeirnan, A.J., Marker-Kraus, L., Roelke, M.E., Bush, M., Wildt, D.E., Lukas, J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) J. Virol., 64, pp. 1964-1972; Herrewegh, A.A., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Jarrett, W.F., Crawford, E.M., Martin, W.M., Daue, F., A virus-like particle associated with leukaemia (lymphosarcoma) (1964) Nature (London), 202, pp. 567-568; Jessup, D.A., Pettan, K.C., Lowenstine, L.J., Pedersen, N.C., Feline leukemia virus infection and renal spirochetosis in free-ranging cougar (felis concolor) (1993) J. Zoo Wildl. Med, 24, pp. 73-79; Johnson, R.H., Isolation of a virus from a condition simulating feline panleucopaenia in a leopard (1964) Vet. Rec., 76, pp. 1008-1013","Hofmann-Lehmann, R.; Clinical Laboratory, Dept. Internal Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland",,,1071412X,,CDIME,"8877134","English","CLIN. DIAGN. LAB. IMMUNOL.",Article,"Final",,Scopus,2-s2.0-0029817018
"Saif L.J.","7102226747;","Mucosal immunity: An overview and studies of enteric and respiratory coronavirus infections in a swine model of enteric disease",1996,"Veterinary Immunology and Immunopathology","54","1-4",,"163","169",,45,"10.1016/S0165-2427(96)05702-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030292720&doi=10.1016%2fS0165-2427%2896%2905702-9&partnerID=40&md5=52e192490b3bc774c9bbd9fb4c5940e0","Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Ohio State University, Wooster, OH 44691, United States","Saif, L.J., Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, Ohio State University, Wooster, OH 44691, United States","Based on the tenet of a common mucosal immune system, antigenic stimulation at one mucosal site results in the distribution of antigen-specific IgA precursor cells to distant mucosal sites. However, recent studies suggest that functional compartmentalization and limited reciprocity may exist within some components of the common mucosal immune system. Although oral immunization is often very effective in inducing immunity to respiratory pathogens, the converse (respiratory immunization to prevent enteric diseases) may not be as effective. To address this question and to study interactions between the bronchus-associated (BALT) and gut-associated (GALT) lymphoid tissues related to protective immunity, we used as a model two antigenically related porcine coronaviruses which replicate primarily in the intestine (transmissible gastroenteritis virus, TGEV) or respiratory tract (porcine respiratory coronavirus, PRCV). The tissue distribution and magnitude of the antibody secreting cell (ASC) responses (measured by ELISPOT) and cell-mediated immune responses (measured by lymphoproliferative assays, LPA) coincided with the viral tissue tropisms. Immunization via GALT (gut infection with TGEV) elicited high numbers of IgA ASC and high LPA responses in GALT (gut lamina propria, LP or mesenteric lymph nodes, MLN), but lower responses in BALT (bronchial lymph nodes, BLN) and induced complete protection against enteric TGEV challenge. In contrast immunization via BALT (respiratory infection with PRCV) elicited systemic type responses (high numbers of IgG ASC in the BLN), but few ASC and low LPA responses in the gut LP or MLN and induced only partial protection against enteric TGEV challenge. Thus administration of vaccines intranasally may not be optimally effective for inducing intestinal immunity in contrast to the reported efficacy of oral vaccines for inducing respiratory immunity.",,"immunoglobulin A; vaccine; conference paper; Coronavirus; immunization; intestine lymphatic tissue; intestine mucosa; intranasal drug administration; nonhuman; oral drug administration; respiratory tract infection; stem cell; swine; Administration, Intranasal; Administration, Oral; Animals; Coronavirus; Coronavirus Infections; Disease Models, Animal; Gastroenteritis, Transmissible, of Swine; Immunity, Mucosal; Respiratory Tract Diseases; Swine; Transmissible gastroenteritis virus; Viral Vaccines; Bronchus; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Anderson, A.D., Wood, O.L., King, A.D., Stephenson, E.H., (1987) Adv. Exp. Med. 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Rec., 125, p. 58","Saif, L.J.; Food Animal Health Research Program, Dept. of Veterinary Preventive Med., Ohio State University, Wooster, OH 44691, United States",,,01652427,,VIIMD,"8988861","English","VET. IMMUNOL. IMMUNOPATHOL.",Conference Paper,"Final",Open Access,Scopus,2-s2.0-0030292720
"Kalicharran K., Mohandas D., Wilson G., Dales S.","6602516345;6602281198;35597345700;7005597434;","Regulation of the initiation of coronavirus JHM infection in primary oligodendrocytes and L-2 fibroblasts",1996,"Virology","225","1",,"33","43",,9,"10.1006/viro.1996.0572","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030297277&doi=10.1006%2fviro.1996.0572&partnerID=40&md5=ce39a7f1b0f24ffcbcfcc24d0c899005","Dept. of Microbiology and Immunology, Health Sciences Center, University of Western Ontario, London, Ont. N6A 5C1, Canada; Jeneil Biotech. Inc., Milwaukee, WS, United States; Allelix Biopharmaceutical Inc., Mississuaga, Ont., Canada; Rockeffeller University, New York, NY, United States; 262 Central Park West, New York, NY 10024, United States","Kalicharran, K., Dept. of Microbiology and Immunology, Health Sciences Center, University of Western Ontario, London, Ont. N6A 5C1, Canada; Mohandas, D., Jeneil Biotech. Inc., Milwaukee, WS, United States; Wilson, G., Allelix Biopharmaceutical Inc., Mississuaga, Ont., Canada; Dales, S., Rockeffeller University, New York, NY, United States, 262 Central Park West, New York, NY 10024, United States","Upon maturation, primary rat oligodendrocytes become resistant to coronavirus JHM (JHMV) infection at an early stage. Involvement of cAMP-dependent protein kinase (PK) in the regulation of oligodendrocyte differentiation has been established (S. Beushausen et al. (1987). J. Virol. 61, 3795-3803). An inducer which accelerates maturation, dibutyryl cyclic AMP (dbcAMP) also upregulates the expression of the regulatory subunit, R1 of PK1. Since (i) early block preventing infection of mature oligodendrocytes can be bypassed when transfection with genomic RNA is used and (ii) inhibitors of PKs counteract the dbcAMP effect, so as to alleviate the inhibition of JHMV, enhanced expression of R1 appeared to be connected with virus restriction. This idea was confirmed following upregulation of the R1 gene in fully permissive L-2 cells. There was a connection between an effect due to R1 and dephosphorylation of the nucleocapsid protein N by an endosomal phosphoprotein phosphatase (PPPase) having the properties of types 1 or 2A enzyme which occurs during penetration of inoculum virions. An inhibition in vitro (cell free) of N dephosphorylation by R1 together with evidence that in vivo (cell culture) overexpression of R1 inhibited the endosomal PPPase as well as replication of JHMV supports the hypothesis that uncoating of the JHMV inoculum occurs after dephosphorylation, a step obligatory for dissociation of the N protein from the genome. Thus inhibition by R prevents uncoating and thereby interferes with the commencement of replication. These observations intimate the existence of a novel mechanism controlling a virus infection of specific cell target(s) undergoing a process of differentiation and maturation in the central nervous system.",,"cyclic AMP; protein kinase; animal cell; article; cell differentiation; controlled study; Coronavirus; dephosphorylation; fibroblast; gene expression regulation; maturation; nonhuman; oligodendroglia; priority journal; rat; virus infection; virus replication; Animalia; Coronavirus","Asanaka, M., Lai, M.M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between Coronavirus nucleocapsid protein and viral RNAs: Implication for viral transcription (1988) J. 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Int., 16, pp. 303-310; Stohlman, S.A., Fleming, J.O., Patton, C.D., Lai, M.M.C., Synthesis and subcellular localization of the murine coronavirus nucleocapsid protein (1983) Virology, 130, pp. 527-532; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4355; Van Alstyne, D., Paty, D.W., The effect of dibutyryl cyclic AMP on restricted replication of rubella virus in rat glial cells in culture (1983) Virology, 124, pp. 173-180; Van Dinter, S., Flintoff, W.F., Rat glial C6 cells are defective in murine coronavirus internalization (1987) J. Gen. Virol., 68, pp. 1677-1685; Wilbur, S.M., Nelson, G.W., Lai, M.M.C., McMillan, M., Stohlman, S.A., Phosphorylation of the mouse hepatitis virus nucleocapsid protein (1986) Biochem. Biophys. Res. Commun., 141, pp. 7-12; Wilson, G.A.R., Beushausen, S., Dales, S., In vivo and in vitro models of demyelinating diseases. XV. Differentiation influences the regulation of coronavirus infection in primary explants of mouse CNS (1986) Virology, 151, pp. 253-264; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein dependent cellular factor other than the virus receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56","Dales, S.; Dept. of Microbiology/Immunology, Health Sciences Center, University of Western Ontario, London, Ont. N6A 5C1, Canada",,"Academic Press Inc.",00426822,,VIRLA,"8918531","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030297277
"Foley J., Hirsh D.C., Pedersen N.C.","7402872921;7103338436;7202299909;","An outbreak of Clostridium perfringens enteritis in a cattery of Bengal cats and experimental transmission to specific pathogen free cats",1996,"Feline Practice","24","6",,"31","35",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-21444451792&partnerID=40&md5=ecc34ecb8f154750aac6c986273d0f72","Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Department of Pathology, Microbiology, and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Foley, J., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Hirsh, D.C., Department of Pathology, Microbiology, and Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","An outbreak of enteritis with diarrhea, fever, and lethargy was observed in a purebred Bengal cattery. Three kittens developed diarrhea shortly after being introduced to this cattery. All cats were found to be shedding feline coronavirus (FCoV) in their feces (as determined by polymerase chain reaction), but cats with signs of enteritis also shed Clostridium perfringens enterotoxin. As part of an ongoing experiment involving feline coronaviral pathogenesis, four specific pathogen free cats were inoculated with crude fecal extract from this cattery. All four cats developed fever, malaise, and diarrhea. The donor cat was subsequently shown to be positive for both the FCoV and C. perfringens enterotoxin. Clinical signs in all cats were not responsive to metronidazole, despite favorable in vitro indications, but symptoms did resolve with either clindamycin or amoxycillin/clavulanate therapy. Two cats remained chronic shedders of C. perfringens spores and enterotoxin even after antibiotic therapy.",,,"Kanoe, M., Inoue, S., Abe, T., Isolation of Clostridium perfringens in Foals (1990) Microbios, 64 (260-261), pp. 153-158; Twedt, D.C., Clostridium perfringens Associated Diarrhea in Dogs (1993) Proceedings of the 11th ACVIM Forum, pp. 121-125; Werdeling, F., Amtsberg, G., Tewes, S., The Occurrence of Enterotoxigenic Clostridium perfringens Strains in the Feces of Dogs and Cats (1991) Berliner and Munchener Tierarztliche Wochenschrift, 104 (7), pp. 228-233; Ahtonen, P., Lehtonen, O.P., Kero, P., Clostridium perfringens in Stool, Intrapartum Antibiotics and Gastrointestinal Signs in a Neonatal Intensive Care Unit (1994) Acta Pediatrica, 83 (4), pp. 389-390; Turk, J., Fales, W., Miller, M., Enteric Clostridium perfringens infection Associated with Parvoviral Enteritis in Dogs: 74 Cases (1987-1990) (1992) JAVMA, 200 (7), pp. 991-994; Brett, M.M., Rodhouse, J.C., Donovan, T.J., Detection of Clostridium perfringens and its Enterotoxin in Cases of Sporadic Diarrhoea (1992) J Clin Path, 45 (7), pp. 609-611; Tschirdewahn, B., Notermans, S., Wernars, K., Untermann, F., The Presence of Enterotoxigenic Clostridium perfringens Strains in Feces of Various Animals (1991) Int J Food Microbiol, 14 (2), pp. 175-178; Timoney, J.F., Gillespie, J.H., Scott, F.W., Barlough, J.E., (1988) Hagen and Bruner's Microbiology and Infectious Diseases of Infectious Animals, pp. 223-228. , Ithaca, New York, Comstock Publications; Saito, M., Excretion of Enterotoxin-Producing Clostridium perfringens in Feces by Patients during and after Diarrhea (1991) J Japanese Assoc Inf Diseases, 65 (5), pp. 571-576; Citino, S.B., Chronic, Intermittent Clostridium perfringens Enterotoxicosis in a Group of Cheetahs (Acinonyx jubatus jubatus) (1995) J Zoo Wildl Med, 26 (2); El Sanousi, S.M., El Shazly, M.O., Al-Dughyem, A., Gameel, A.A., Enterotoxaemia in Cats (1991) Vet Rec, OCTOBER 12, p. 344; Cheung, R.C., Matsui, S.M., Greenberg, H.B., Rapid and Sensitive Method for Detection of Hepatitis C Virus RNA by Using Silica Particles (1994) J Clin Microbiol, 32 (10), pp. 2593-2597; Foley, J., Pedersen, N.C., Poland, A., Carlson, J., The Natural History and Epidemiology of Feline Coronaviruses in Catteries (1996) JAVMA, , in press; Vennema, H., Poland, A., Floyd-Hawkins, K., Pedersen, N.C., A Comparison of the Genomes of FECVs and FIPVs and What They Tell Us about the Relationships between Feline Coronaviruses and Their Evolution (1995) Feline Pract, 23 (3), pp. 40-45; Pedersen, N.C., (1988) Feline Infectious Diseases, pp. 41-44. , St Louis, Mosby","Foley, J.; Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States",,,10576614,,,,"English",,Article,"Final",,Scopus,2-s2.0-21444451792
"Méchin M.-C., Der Vartanian M., Martin C.","57195160292;6602094816;57212178599;","The major subunit ClpG of Escherichia coli CS31A fibrillae as an expression vector for different combinations of two TGEV coronavirus epitopes",1996,"Gene","179","2",,"211","218",,13,"10.1016/S0378-1119(96)00348-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030583743&doi=10.1016%2fS0378-1119%2896%2900348-4&partnerID=40&md5=b9690a9fadd3c40ae9d8a6871f33f884","Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de C., 63122 Saint-Genès-Champanelle, France","Méchin, M.-C., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de C., 63122 Saint-Genès-Champanelle, France; Der Vartanian, M., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de C., 63122 Saint-Genès-Champanelle, France; Martin, C., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de C., 63122 Saint-Genès-Champanelle, France","Previously, two B-cell epitopes from the entero-pathogenic transmissible gastroenteritis virus (TGEV), namely the C epitope (TGEV-C) amino acids (aa) 363-371 and the A epitope (TGEV-A) aa 522-531 of the spike S protein (TGEV-S), have been separately expressed on the CS31A fibrillae at the surface of Escherichia coli following insertion into a same region of ClpG. However, the resulting chimeras induced a marginal TGEV-neutralizing antibody (Ab) response in mice. Here, with the view to improving this response, we introduced TGEV-C alone or in different tandem association with TGEV-A (A::C or C::A) in twelve putatively exposed regions of ClpG. Among the 28 resulting engineered proteins only 15, carrying up to 51 extra aa, had not essentially disturbed the correct CS31A fibrillae formation process. Six partially permissive sites accepting only TGEV-C and three highly permissive sites tolerating A::C or C::A tandem peptide, were identified throughout ClpG. Intact bacteria or extracted CS31A hybrid fibrillae expressing TGEV epitopes at any of the permissive sites, were recognized by Ab directed against the foreign parent protein, providing a direct argument for exposure of the corresponding ClpG region at the cell surface and for antigenicity of the epitopes in the polymeric CS31A fibrillae context. The potential of CS31A fibrillae as carriers of the TGEV peptides indicates that there may be three positions (N terminus, aa 202-204 and 202-218) in ClpG which may turn out to be important fusion sites and therefore be relevant for the eventual design of TGEV vaccines. Unexpectedly, TGEV-A, whatever its position in ClpG, mediated the partial proteolytic degradation of the hybrid proteins, suggesting that it functions as a substrate for a cellular protease, and thereby that its suitability as a vaccine antigen candidate is doubtful.","Genetic fusion; Hybrid protein; Peptide presentation; Recombinant DNA; Surface exposure; Tandem insertion; Transmissible gastroenteritis virus","epitope; article; cell surface; chimera; coronavirus; escherichia coli; expression vector; nonhuman; priority journal; vaccine production; Amino Acid Sequence; Antigens, Bacterial; Bacterial Proteins; Base Sequence; Cloning, Molecular; DNA, Recombinant; Epitopes; Escherichia coli; Escherichia coli Proteins; Genetic Vectors; Molecular Sequence Data; Recombinant Fusion Proteins; Transmissible gastroenteritis virus; Coronavirus; Escherichia coli; Transmissible gastroenteritis virus","Benito, A., Mateu, M.G., Villaverde, A., Improved mimicry of a foot-and-mouth disease virus antigenic site by a viral peptide displayed on β-galactosidase surface (1995) Bio/Technology, 13, pp. 801-804; Bousquet, F., Martin, C., Girardeau, J.P., Méchin, M.C., Der Vartanian, M., Laude, H., Contrepois, M., CS31A capsule-like antigen as an exposure vector for heterologous antigenic determinants (1994) Infect. Immun., 62, pp. 2553-2561; Broekhuijsen, M.P., Blom, T., Ven Rijn, T., Pouwels, P.H., Klassen, E.A., Fasbender, M.J., Enger-Valk, B.E., Synthesis of fusion proteins with multiple copies of an antiigenic determinant of foot-and-mouth disease virus (1986) Gene, 49, pp. 189-197; Charbit, A., Ronco, J., Michel, V., Werts, C., Hofnung, M., Permissive sites and topology of an outer membrane protein with a reporter epitope (1991) J. Bacteriol., 173, pp. 262-275; Correa, I., Gebauer, F., Bullido, M.J., Suné, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus (1990) J. Gen. Virol., 71, pp. 271-279; Delmas, B., Rasschaaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike protein (1990) J. Gen. Virol., 71, pp. 1313-1323; Deng, W.P., Nickoloff, J.A., Site-directed mutagenesis of virtually any plasmid by eliminating a unique site (1992) Anal. Biochem., 200, pp. 81-88; Der Vartanian, M., Méchin, M.C., Jaffeux, B., Bertin, Y., Félix, I., Gaillard-Martinie, B., Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences (1994) Gene, 148, pp. 23-32; Gebauer, F., Posthumus, W.A.P., Correa, I., Suné, C., Sanchez, C.M., Smerdon, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the s protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Girardeau, J.P., Bertin, Y., Martin, C., Der Vartanian, M., Boeuf, C., Sequence analysis of the clpG gene, which codes for surface antigen CS31A subunit: Evidence of an evolutionary relationship between CS31A, K88 and F41 subunit genes (1991) J. Bacteriol., 173, pp. 7676-7683; Girardeau, J.P., Der Vartanian, M., Ollier, J.L., Contrepois, M., CS31A, a new K88-related fimbrial antigen on bovine enterotoxigenic and septicemic Escherichia coli strains (1988) Infect. Immun., 56, pp. 2180-2188; Jung, R., Scott, M.P., Oliveira, L.O., Nielsen, N.C., A simple and efficient method for the oligodeoxyribonucleotide-directed mutagenesis of double-stranded plasmid DNA (1992) Gene, 121, pp. 17-24; Khan, C.M.A., Villarreal-Ramos, B., Pierce, R.J., Demarco De Hormaeche, R., McNeill, H., Ali, T., Chatfield, S., Hormaeche, C.E., Construction, expression and immunogenicity of multiple tandem copies of the Schistosoma mansoni peptide 115-131 of the P28 glutathione s-transferase expressed as C-terminal fusions to tetanus toxin fragment C in a live Aro-attenuated vaccine strain of Salmonella (1994) J. Immunol., 153, pp. 5634-5642; Martineau, P., Guillet, J.G., Leclere, C., Hofnung, M., Expression of heterologous peptides at two permissive sites of the Ma1E protein: Antigenicity and immunogenicity of foreign B-cell and T-cell epitopes (1992) Gene, 113, pp. 35-46; Méchin, M.C., Bertin, Y., Girardeau, J.P., Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins of Escherichia coli share a common overall fold and differ structurally from other fimbrial subunits (1995) FEBS Lett., 364, pp. 319-324; Moulard, M., Bahraoui, E., Role of proteolytic processing of viral envelope glycoproteins (1995) Médecine/sciences, 11, pp. 73-80; Rabinovich, N.R., McInnes, P., Klein, D.L., Hall, B.F., Vaccine technologies: View to the future (1994) Science, 265, pp. 1401-1404; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Stanssens, P., Opsomer, C., McKeown, Y.M., Kramer, W., Zabeau, H., Fritz, H.J., Efficiency oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternative selectable markers (1989) Nucleic Acids Res., 17, pp. 4441-4454; Tishminetzky, S.G., Scodeller, R.A., Evangelisti, P., Chen, Y., Schiappacassi, M., Porro, F., Bizik, F., Baralle, F.E., Immunoreactivity of chimeric proteins carrying the HIV-1 epitope IGPGRAF: Correlation between predicted conformation and antigenicity (1994) FEBS Lett., 353, pp. 1-4; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354","Der Vartanian, M.; Laboratoire de Microbiologie, Inst. National Recherche Agronomique, Ctr. Rech. Clermont-Ferrand-Theix, 63122 Saint-Genes-Champanelle, France",,,03781119,,GENED,"8972902","English","GENE",Article,"Final",Open Access,Scopus,2-s2.0-0030583743
"Addie D.D., Toth S., Herrewegh A.A.P.M., Jarrett O.","7003910352;57189707374;6602355430;7006845693;","Feline coronavirus in the intestinal contents of cats with feline infectious peritonitis",1996,"Veterinary Record","139","21",,"522","523",,17,"10.1136/vr.139.21.522","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030599485&doi=10.1136%2fvr.139.21.522&partnerID=40&md5=9e9d41e1c06eb388e88849b33841dfff","Department of Veterinary Pathology, University of Glasgow, Veterinary School, Bearsden Road, Glasgow G61 IQH, United Kingdom; Department of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands","Addie, D.D., Department of Veterinary Pathology, University of Glasgow, Veterinary School, Bearsden Road, Glasgow G61 IQH, United Kingdom; Toth, S., Department of Veterinary Pathology, University of Glasgow, Veterinary School, Bearsden Road, Glasgow G61 IQH, United Kingdom; Herrewegh, A.A.P.M., Department of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Jarrett, O., Department of Veterinary Pathology, University of Glasgow, Veterinary School, Bearsden Road, Glasgow G61 IQH, United Kingdom",[No abstract available],,"Coronavirus; Felidae; Feline coronavirus; Felis catus; animal; article; cat; cat disease; Coronavirus; isolation and purification; pathology; polymerase chain reaction; virology; Animals; Cat Diseases; Cats; Coronavirus; Feline Infectious Peritonitis; Polymerase Chain Reaction","Addie, D.D., Jarrett, O., (1992) Veterinary Record, 130, p. 133; Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., (1995) American Journal of Veterinary Research, 56, p. 429; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., (1995) Journal of Clinical Microbiology, 33, p. 684; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., (1981) American Journal of Velerinary Research, 42, p. 368; Pedersen, N.C., Evermann, J.F., McKiernan, A.J., Ott, R.L., (1984) American Journal of Veterinary Research, 45, p. 2580; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Gaskell, C.J., (1988) Veterinary Microbiology, 16, p. 145","Addie, D.D.; Department of Veterinary Pathology, University of Glasgow, Veterinary School, Bearsden Road, Glasgow G61 IQH, United Kingdom",,"British Veterinary Association",00424900,,VETRA,"8953694","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0030599485
"Tresnan D.B., Levis R., Holmes K.V.","6602328481;7005215033;7201657724;","Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I",1996,"Journal of Virology","70","12",,"8669","8674",,150,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029861760&partnerID=40&md5=699e9e97bfb90abf59d6ee4cc9abffb6","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814, United States; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Box B-175, 4200 E. Ninth Ave., Denver, CO 80262, United States; Ctr. for Biologies Eval. and Res., Food and Drug Administration, Bethesda, MD 20892, United States","Tresnan, D.B., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Box B-175, 4200 E. Ninth Ave., Denver, CO 80262, United States; Levis, R., Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814, United States, Ctr. for Biologies Eval. and Res., Food and Drug Administration, Bethesda, MD 20892, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Department of Pathology, Uniformed Services, University of the Health Sciences, Bethesda, MD 20814, United States","Two members of coronavirus serogroup I, human respiratory coronavirus HCV-229E and porcine transmissible gastroenteritis virus (TGEV), use aminopeptidase N (APN) as their cellular receptors. These viruses show marked species specificity in receptor utilization, as HCV-229E can utilize human but not porcine APN, while TGEV can utilize porcine but not human APN. To determine whether feline APN could serve as a receptor for two feline coronaviruses in serogroup I, feline infectious peritonitis virus (FIPV) and feline enteric coronavirus (FeCV), we cloned the cDNA encoding feline APN (fAPN) by PCR from cDNA isolated from a feline cell line and stably expressed it in FIPV- and FeCV-resistant mouse and hamster cells. The predicted amino acid sequence of fAPN shows 78 and 77% identity with human and porcine APN, respectively. When inoculated with either of two biologically different strains of FIPV or with FeCV, fAPN-transfected mouse and hamster cells became infected and viral antigens developed in the cytoplasm. Infectious FIPV was released from hamster cells stably transfected with fAPN. The fAPN- transfected mouse and hamster cells were challenged with other coronaviruses in serogroup I including canine coronavirus, porcine coronavirus TGEV, and human coronavirus HCV-229E. In addition to serving as a receptor for the feline coronaviruses, fAPN also served as a functional receptor for each of these serogroup I coronaviruses as shown by development of viral antigens in the cytoplasm of infected mouse or hamster cells stably transfected with fAPN. In contrast, fAPN did not serve as a functional receptor for mouse hepatitis virus (MHV-A59), which is in serogroup II and utilizes mouse biliary glycoprotein receptors unrelated to APN. Thus, fAPN serves as a receptor for a much broader range of group I coronaviruses than human and porcine APNs. The human, porcine, and canine coronaviruses in serogroup I that are able to use fAPN as a receptor have previously been shown to infect cats without causing disease. Therefore, host factors in addition to receptor specificity apparently affect the virulence and transmissibility of nonfeline serogroup I coronaviruses in the cat.",,"complementary dna; microsomal aminopeptidase; virus antigen; virus receptor; animal cell; article; coronavirus; dna sequence; gene expression; hamster; molecular cloning; mouse; nonhuman; priority journal; serotyping; species difference; virus cell interaction; 3T3 Cells; Amino Acid Sequence; Animals; Antigens, CD13; Base Sequence; Cats; Cell Line; Cloning, Molecular; Coronavirus; Coronavirus 229E, Human; Coronavirus, Feline; Cricetinae; DNA, Complementary; Dogs; Humans; Mice; Molecular Sequence Data; Receptors, Virus; Recombination, Genetic; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Swine; Transmissible gastroenteritis virus","Barlough, J.E., Johnson-Lussenburg, C.M., Stoddart, C.A., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis virus (1985) Can. J. Comp. Med., 49, pp. 303-307; Barlough, J.E., Stoddart, C.A., Feline coronaviral infections (1990) Infectious Diseases of the Dog and Cat, pp. 300-312. , C. E. Greene (ed.), W. B. Saunders Co., Philadelphia; Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab. Anim. Sci., 34, pp. 592-597; Boyle, J.F., Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Otl, R.L., Black, J.W., Plaque assay, polypeptide composition and immunohistochemistry of feline infectious peritonitis virus and feline enteric coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 133-147; Castrucci, M.R., Donatelli, I., Sidoli, L., Barigazzi, G., Kawaoka, Y., Webster, R.G., Genetic reassortment between avian and human influenza A viruses in Italian pigs (1993) Virology, 193, pp. 503-506; Compton, S.R., Stephensen, C.B., Snyder, S.W., Weismiller, D.G., Holmes, K.V., Coronavirus species specificity: Murine coronavirus hinds to a mouse-specific epitope on its carcinoembryonic antigen-related receptor glycoprotein (1992) J. Virol., 66, pp. 7420-7428; Delmas, B., Gelfi, J., Kut, E., Sjöström, H., Norén, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidasc N that is distinct from the enzymatic site (1994) J. Virol., 68, pp. 5216-5224; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-419; Delmas, B., Gelfi, J., Sjöström, H., Norén, O., Laude, H., Further characterization of aminopeptidase N as a receptor for coronaviruses (1994) Adv. Exp. Med. Biol., 342, pp. 293-298; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.-S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Holland, J., Spindler, K., Horodyski, F., Grabau, E., Nichol, S., Vandepol, S., Rapid evolution of RNA genomes (1982) Science, 215, pp. 1577-1585; Holmberg, C.A., Gribble, D.H., Feline infectious peritonitis diagnostic gross and microscopic lesions (1973) Feline Pract., 3, pp. 11-14; Holmes, K.V., Compton, S.R., Coronavirus receptors (1995) The Coronaviridae, pp. 55-71. , S. G. Siddell (ed.). Plenum Press, New York; Holmes, K.V., Lai, M.M.C., Coronaviridac: The viruses and their replication (1996) Virology (Fields), 3rd Ed., pp. 1075-1093. , B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia; Keck, J.G., Makino, S., Soe, L.H., Fleming, J.O., Stohlman, S.A., Lai, M.M.C., RNA recombination of coronavirus (1987) Adv. Exp. Med. Biol., 218, pp. 99-107; Kenny, A.J., Maroux, S., Topology of microvillar membrane hydrolases of kidney and intestine (1982) Physiol, Rev., 62, pp. 91-128; Levis, R., Cardellichio, C.B., Scanga, C.A., Compton, S.R., Holmes, K.V., Multiple receptor-dependent steps determine the species specificity of HCV-229E infection (1995) Adv. Exp. Med. Biol., 380, pp. 337-343; Levis, R., Holmes, K.V., Unpublished data; Levis, R., Holmes, K.V., Delmas, B., Laude, H., Unpublished data; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) J. Clin. Invest., 83, pp. 1299-1307; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High frequency RNA recombination of murine coronaviruses (1986) J. Virol., 56, pp. 729-737; McKeirnan, A.J., Evermann, J.F., Hargis, A., Miller, L.M., Ott, R.L., Isolation of feline coronaviruses from two cats with diverse disease manifestations (1981) Feline Pract., 11 (3), pp. 16-20; Montali, R.J., Strandberg, J.D., Extraperitoneal lesions in feline infectious peritonitis (1972) Vet. Pathol., 9, pp. 109-121; O'Brien, S.J., Roelke, M.E., Marker, L., Nemnan, A., Winkler, C.A., Meltzer, D., Colly, L., Wildt, D.E., Genetic basis for species vulnerability in the cheetah (1985) Science, 227, pp. 1428-1434; Olsen, J., Cowell, G.M., Kønigshøfer, E., Uanielsen, E.M., Møller, J., Laustsen, L., Hansen, O.C., Norén, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Lett., 238, pp. 307-314; Pedersen, N.C., Morphologic and physical characteristics of feline infectious peritonitis virus and its growth in autochthonous peritoneal cell cultures (1976) Am. J. Vet. Res., 37, pp. 567-572; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections. Pari 2. Feline infectious peritonitis (1983) Feline Pract., 13, pp. 5-20; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Pedersen, N.C., Bojle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pfeifer, P.L., Evermann, J.F., Roelke, M.E., Gallina, A.M., Ott, R.L., McKeirnan, A.J., Feline infectious peritonitis in a captive cheetah (1983) J. Am. Vet. Med. Assoc., 183, pp. 1317-1319; Reynolds, D.J., Garwes, D.J., Virus isolation and serum antibody responses after infection of cats with transmissible gastroenteritis virus (1979) Arch. Virol., 60, pp. 161-166; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schultze, B., Gross, H.-J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-O-acetylneuraminic acid as a receptor determinant to initiate infection of cultured cells (1992) J. Gen. Virol., 73, pp. 901-906; Scott, F.W., Feline infectious peritonitis and other feline coronaviruses (1986) Current Veterinary Therapy IX, pp. 1059-1062. , R. W. Kirk (ed.), W. B. Saunders Co., Philadelphia; Scott, F.W., Immunization against feline coronaviruses (1986) Adv. Exp. Med. Biol., 218, pp. 569-576; Semenza, G., Anchoring and biosynthesis of stalked brush border membrane proteins: Glycosidases and peptidases of enterocytes and renal tubuli (1986) Annu. Rev. Cell Biol., 2, pp. 255-313; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Stoddart, C.A., Scott, F.W., Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence (1989) J. Virol., 63, pp. 436-440; Watt, V.M., Yip, C.C., Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N (1989) J. Biol. Chem., 264, pp. 5480-5487; Webster, R.G., Laver, W.G., Air, G.M., Schild, G.C., Molecular mechanisms of variation in influenza viruses (1982) Nature (London), 296, pp. 115-121; Wege, H., Siddell, S., Ter Meulen, V., The Biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Woods, R.D., Cheville, N.F., Gallagher, J.E., Lesions in the small intestine of newborn pigs inoculated with porcine, feline and canine coronaviruses (1981) Am. J. Vet. Res., 42, pp. 1163-1169; Yang, X.F., Milhiet, P.E., Gaudoux, F., Crine, P., Boileau, G., Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney using in situ hybridization (1993) Biochem. Cell Biol., 71, pp. 278-287; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature (London), 357, pp. 420-422; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two earcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Tresnan, D.B.; Department of Microbiology, Univ. of Colorado Health Sci. Center, Box B-175, 4200 E. Ninth Ave., Denver, CO 80262, United States",,,0022538X,,JOVIA,"8970993","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029861760
"Hornberger F.R., Zhang L., Thomann P.E.","6508000786;15039884400;35901831700;","PCR as a tool in studying murine coronaviruses [Der Einsatz der PCR zum Studium muriner Coronaviren]",1996,"Schweizer Archiv fur Tierheilkunde","138","2",,"67","73",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030541167&partnerID=40&md5=5ea2dc876fab0ccdf4db144093e5d712","Institut für Labortierkunde, Veterinarmedizinische Fak., Universität Zürich; Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland","Hornberger, F.R., Institut für Labortierkunde, Veterinarmedizinische Fak., Universität Zürich, Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland; Zhang, L., Institut für Labortierkunde, Veterinarmedizinische Fak., Universität Zürich; Thomann, P.E., Institut für Labortierkunde, Veterinarmedizinische Fak., Universität Zürich","This paper describes a number of applications of the Polymerase Chain Reaction (PCR) in the study of enterotropic murine coronaviruses [mouse hepatitis virus (MHV)]. A diagnostic PCR was developed which detected all of 11 different MHV strains. This fast and reliable method was also able to differentiate MHV from other non-murine coronaviruses. On the basis of this assay a quantitative PCR was designed using a mutant template containing a point mutation which competed for the PCR primers. The amplification and cloning of the structural protein genes of enterotropic MHV strains in plasmid vectors for subsequent sequencing is described. In addition an RT PCR was developed which was able to selectively detect artificially generated recombinant coronavirus.","Coronavirus; Mouse; Mouse hepatitis virus; PCR","primer DNA; virus protein; animal; animal hepatitis; article; biosynthesis; classification; comparative study; Coronavirus; genetics; isolation and purification; methodology; molecular genetics; mouse; Murine hepatitis coronavirus; nucleotide sequence; polymerase chain reaction; virus infection; Animals; Base Sequence; Coronavirus; Coronavirus Infections; DNA Primers; Hepatitis, Viral, Animal; Mice; Molecular Sequence Data; Murine hepatitis virus; Polymerase Chain Reaction; Viral Structural Proteins","Barthold, S.W., Mouse hepatitis virus Biology and epidemiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents Effect on Biomedical Research, pp. 571-601. , eds. Bhatt P.N., Jacoby R.O., Morse III H C., New A.E. Academic Press; Compton, S.R., Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors (1994) Virology, 203, pp. 197-201; Campton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Arum. Sci., 43, pp. 15-28; Souza, M., Smith, A.L., Comparison of isolation in cell cultures with conventional and modified mouse antibody production tests for detection of murine viruses (1989) J. Clin. Microbiol., 27, pp. 185-187; Gilliland, G., Perrin, S., Brunn, H.F., Competitive PCR for quantititation of mRNA (1989) PCR Protocols: a Guide to Methods and Amplifications, pp. 60-69. , eds. Innis M A., Gelfand D.H , Sninsky J.J., White T J, Academic Press; Holmes, K.V., Replication of coronaviruses (1986) Fundamental Virology, pp. 513-525. , eds Field B.N., Knipe D M , Chanock R.M., Melnick J.L., Roizman B., Shope RE, Raven Press; Homberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res., 31, pp. 49-56; Homberger, F.R., Sequence analysis of the nucleoprotein genes of three enterotropic strains of murine coronavirus (1995) Arch. Virol., 140, pp. 571-579; Homberger, F.R., Mausehepatitis-Virus Schweiz Arch. Tierheilk., , im Druck; Hornberger, F.R., Barthold, S.W., Passively acquired challenge immunity to enterotropic coronavirus in mice (1992) Arch. Virol, 126, pp. 35-43; Homberger, F.R., Thomann, P.E., Prevalence and transmission of murine viruses and Mycoplasma in laboratory mouse colonies with respect to housing conditions (1994) Lab. Anim., 28, pp. 113-120; Homberger, F.R., Smith, A.L., Barthold, S.W., Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. Clin Microbiol., 29, pp. 2789-2793; Homberger, F.R., Barthold, S.W., Smith, A.L., Duration and strain specificity of immunity to enterotropic mouse hepatitis virus (1992) Lab Anim. Sci., 42, pp. 347-351; Kunita, S., Zbang, L., Hornberger, F.R., Compton, S.R., Molecular characterization of the S proteins of two enterotropic murine coronavirus strains (1995) Virus Res., 35, pp. 277-289; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Siddell, S.G., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, H.D., MacNaughton, M.R., Pensaert, M., Van der Zeijst, B.A.M., (1983) Coronaviridae Intervirology, 20, pp. 181-189; Van der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavinis MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Zhang, L., Luytjes, W., Hornberger, E.R., Spaan, W.J.M., A Study of the Site Specific Mutagenesis of MHV Spike Gene by Using Homologous RNA Recombination between MHV Genome and Synthetic DI RNAs, , In preparation","Hornberger, F.R.; Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland",,,00367281,,SATHA,"8720730","German","Schweiz. Arch. Tierheilkd.",Article,"Final",,Scopus,2-s2.0-0030541167
"Tobler K., Ackermann M.","6701508835;7102624625;","Identification and characterisation of new and unknown coronaviruses by using RT-PCR and degenerated primers [Identifikation und Charakterisierung von neuen und unbekannten Coronaviren mit Hilfe von RT-PCR und degenerierten Primern]",1996,"Schweizer Archiv fur Tierheilkunde","138","2",,"80","86",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030306053&partnerID=40&md5=a39004d20000ff6b8492a175f1133993","Institut für Virologie, Veterinavr-Med. Fakultät, Universität Zürich; Institut für Virologie, Vet.-Med. Fakultät, Universität Zürich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland","Tobler, K., Institut für Virologie, Veterinavr-Med. Fakultät, Universität Zürich; Ackermann, M., Institut für Virologie, Veterinavr-Med. Fakultät, Universität Zürich, Institut für Virologie, Vet.-Med. Fakultät, Universität Zürich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland","A modified method of the reverse transcription followed by polymerase chain reaction (RT-PCR) was developed in order to examine the genome of a recently discovered virus, the porcine epidemic diarrhoea virus (PEDV), which resembled morphologically the coronaviruses. The published sequences of the genomes of various coronaviruses were compared. On the level of the amino acid sequence, conserved regions, common to all coronaviruses, were found in the gene encoding the nonstructural protein 1b as well as in the genes coding for the major structural proteins (S, M, and N). Due to the degeneration of the genetic code, some amino acids may be encoded by different nucleotide triplets. In order to compensate for this degeneration, mixtures of primers were synthesized, containing a variety of nucleotide sequences which together represented all possible codons for the conserved amino acid sequences. This method allowed to amplify and clone approximately 4000 base pairs of the genome of PEDV. An analysis of the genomic sequences revealed that PEDV holds an interesting intermediate position between human coronavirus 229E and Transmissible Gastroenteritis virus. We postulate that the method presented in this contribution may be useful to study and characterize other unknown viruses, especially viruses for which no cell cultures for propagation are available.","Coronavirus; Degenerated primers; PED virus; RT-PCR","primer DNA; RNA directed DNA polymerase; virus protein; amino acid sequence; animal; animal disease; article; biosynthesis; chemistry; comparative study; Coronavirus; genetics; isolation and purification; methodology; molecular genetics; nucleotide sequence; polymerase chain reaction; sequence homology; swine; swine disease; virus genome; virus infection; Amino Acid Sequence; Animals; Base Sequence; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; DNA Primers; Genome, Viral; Molecular Sequence Data; Polymerase Chain Reaction; RNA-Directed DNA Polymerase; Sequence Homology, Amino Acid; Swine; Swine Diseases; Viral Proteins","Bridgen, A., Duarte, M., Tabler, K., Laude, H., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen Virol, 74, pp. 1795-1804; Bridgen, A., Tabler, K., Ackermann, M., Identification of coronaviral conserved sequences and application to viral genome amplification (1994) Coronaviruses. Molecular Biology and Virus-host Interactions, , H Laude and J. V. Vautherot. New York, Plenum; Duarte, M., Laude, H., Sequence of the spike protein of the porcine epidemic diarrhoea virus (1994) J. Gen. Virol., 75, pp. 1195-1200; Duarte, M., Tabler, K., Bridgen, A., Rasscbaert, D., Ackermann, M., Laude, H., Sequence analysis of the porcine epidemic diarrhoea virus genome between the nucleocapsid and the spike protein genes reveals, a polymorphic ORE (1994) Virology, 198, pp. 466-476; Frohman, M.A., Dush, M.K., Martin, G.R., Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer (1988) Proc. Natl. Acad. Sci., U. S. A., 85, pp. 8998-9002; Hofmann, M., Wyler, R., Propagation of virus of porcine epidemic diarrhoea in cell culture (1988) J. Clin Microbiol., 26, pp. 2235-2239; Kingston, R.E., (1991) Current Protocols in Molecular Biology, , New York, Greene Publishing Associates; Knittel, T., Picard, D., PCR with degenerate primers containing deoxyinosine fails with Pfu DNA polymerasc (1993) PCR Methods and Applications, 2, pp. 346-347; Pensaert, M.B., Debouck, P., A new coronavirus-like particle associated with diarrhoea in swine (1978) Arch, in Virology, 58, pp. 243-247; Tobler, K., Bridgen, A., Ackermann, M., Sequence analysis of the nucleocapsid protein gene of porcine epidemic diarrhoea virus (1994) Coronaviruses: Molecular Biology and Virus-host Interactions, , H. Laude and J. V. Vautherot New York, Plenum; Utiger, A., Frei, A., Carvajal, A., Ackermann, M., Studies on the in vitro and in vivo host range of porcine epidemic diarrhoea virus (1995) Corona- and Related Viruses, , P. J Talbot and G. A. Levy. New York, Plenum; Wirth, U.V., Vogt, J.B., Schwyzer, M., The three major immediate-early transcripts of bovine herpesvirus 1 arise from two divergent and spliced transcription units (1991) J Virol., 65, pp. 195-205","Ackermann, M.; Institut für Virologie, Vet.-Med. Fakultät, Universität Zürich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland",,,00367281,,SATHA,"8720732","German","Schweiz. Arch. Tierheilkd.",Article,"Final",,Scopus,2-s2.0-0030306053
"Richter M., Schinkinger M.F., Möstl K.","57196729261;57196486426;6603843340;","Detection of feline coronavirus type II infections in blood of cats using a reverse transcriptase polymerase-chain reaction (RT-PCR) [Nachweis von Infektionen mit felinen coronaviren typ II im blut von katzen mittels reverser transcriptase polymerase-kettenreaktion (RT-PCR)]",1996,"Wiener Tierarztliche Monatsschrift","83","9",,"263","268",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345611436&partnerID=40&md5=a7d783d9eb3733c8a9a64ee5cea78d06","Forschungslabor der Werfft Chem. G., Veterinarmedizinischen Univ. Wien; Neufeld und dem Inst. Virologie, Veterinarmedizinischen Univ. Wien; Landeggerstraße 7, A-2491 Neufeld a. d. Leitha; Josef Baumann-Gasse 1, A-1210 Wien","Richter, M., Forschungslabor der Werfft Chem. G., Veterinarmedizinischen Univ. Wien, Landeggerstraße 7, A-2491 Neufeld a. d. Leitha; Schinkinger, M.F., Neufeld und dem Inst. Virologie, Veterinarmedizinischen Univ. Wien; Möstl, K., Forschungslabor der Werfft Chem. G., Veterinarmedizinischen Univ. Wien, Josef Baumann-Gasse 1, A-1210 Wien","In order to detect coronaviral RNA in blood samples of cats infected with feline coronaviruses type II a reverse transcriptase PCR (RT-PCR) was developed. 81 blood samples were tested in parallel for the presence of viral RNA by the RT-PCR and for antibodies using an immunofluorescence assay. 39 % of the clinically healthy cats without a special risk of coronavirus infection were seropositive and 57 % PCR-positive; in the group of clinically healthy cats, but with a higher risk for infection, 85 % showed antibodies and 95 % were identified as virus carriers; 100 % of the cats with symptoms of Feline Infectious Peritonitis (FIP) were seropositive and 90 % PCR-positive; in the group of cats with unspecific clinical symptoms 61 % were seropositive and 82 % PCR-positive. In 57 % of the seronegative animals viral RNA could be detected. As most of these cats were between 8 and 12 weeks of age, it is probable that the blood samples were collected during the time of seroconversion after the first infection with feline coronaviruses. These results show that the RT-PCR proves helpful in identifying latent virus carriers, not only among seropositive animals, but especially among seronegative cats during the period of seroconversion. So it will be a tool to prevent spreading of feline coronavirus infections into free catteries. However, the RT-PCR is not suitable for diagnosing FIP, as a high percentage of virus carriers was detected among ill as well as healthy cats.","Cat; Coronaviruses; FIP; RT-PCR",,"Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; Barlough, J.E., Scott, F.W., Feline infectious peritonitis (1988) Manual of Small Animal Infectious Diseases, pp. 63-78. , J. E. BARLOUGH (ed.): Churchill Livingston, NY; Fehr, D., Bolla, S., Herrewegh, A.A.P.M., DeGroot, R.J., Horzinek, M.C., Lutz, H., Detection of feline coronavirus (FCoV) in different samples of cats using polymerase chain reaction (PCR) (1994) Proc. 3rdrd Congress of the European Society for Veterinary Virology, pp. W5-3. , Interlaken, Schweiz; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Herrewegh, A.A.P.M., DeGroot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet. Microbiol., 42, pp. 65-77; Möstl, K., Nachweis von Antikörpern gegen das Virus der Felinen Infektiösen Peritonitis in Katzenseren und Peritonealexsudaten (1983) Wien. Tierärztl. Mschr., 70, pp. 318-323; Möstl, K., (1996), persönl. Mitteilung; Möstl, K., Richter, M., (1996), persönl. Mitteilung; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type 1 (1995) Arch. Virol., 140, pp. 469-480; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections. Part2: Feline infectious peritonitis (1983) Feline Pract., 13, pp. 5-14; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV- UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Compend. Contin. Educ. Pract. Vet ., 7, pp. 1001-1011; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am, J. Vet. Res., 42, pp. 368-377; Richter, M., Schinkinger, M., Möstl, K., One step reverse transcriptase-polymerase chain reaction (RT-PCR) for detection of feline infectious peritonitis virus (FIPV) (1994) Proc. 3rd Congress of the European Society for Veterinary Virology, pp. P5-4. , Interlaken, Schweiz; Scott, F.W., Update on FIP (1989) Proc. of the 12th KalKan Symposium, pp. 43-47; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs: What they tell us about the relationships between feline coronaviruses and their evolution (1985) Proc. to the FIPV/FECV Workshop 1994 in Davis, Ca., 23, pp. 40-44. , Feline Practice; Weiss, R.C., Scott, F.W., Pathogenesis of Feline Infectious Peritonitis: Nature and development of viremia (1981) Am. J. Vet. Res., 42, pp. 382-390","Forschungslabor der Werfft Chem. G., Veterinarmedizinischen Univ. Wien",,,02539411,,WTMOA,,"German","Wien. Tierarztl. Monatsschr.",Article,"Final",,Scopus,2-s2.0-0345611436
"Tamás T.","6604015064;","Recent knowledge in the enteral coronaviruses in pig. Review article [Újabb ismeretek a sertések enterális coronavírusairól. Szemlecikk]",1996,"Magyar Allatorvosok Lapja","51","6",,"361","365",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3242874190&partnerID=40&md5=2e48144301674a1a992105a7bad6d9b2","MTA, Allatorvos-tudomanyi Kutatointezet, Hungária krt. 21, H-1143 Budapest, Hungary","Tamás, T., MTA, Allatorvos-tudomanyi Kutatointezet, Hungária krt. 21, H-1143 Budapest, Hungary","The article, based on the latest literary data, briefly summarizes the most important aspects of the porcine coronaviruses commonly found in pig herds throughout the world, namely transmissible gastroenteritis virus (TGEV), porcine respiratory coronavirus (PRCV) and porcine epidemic diarrhoea virus (PEDV). It deals with the results of the molecular biological methods applied in corona virology, such as the description of two cellular TGEV receptor proteins, the localization of the putative receptor binding sites on the spike protein of the virion. According to the latest findings published in the literature there are certain characteristic differences in the genome of TGEV and PRCV. The most important one of these, is the deletion localized on the spike gene of the PRCV. This deletion seems to be responsible for the different tissue tropism of the two viruses, and the paper points out the practical importance of this finding. According to the data gethered on passive and active immunization experiments of pigs, the missing sequences code for epitopes crucial in the induction of protective immunity in piglets. The difference of the genomes can be utilized in the diagnostics, to differentiate PRCV and TGEV infections on a serological basis, or by the currently developed nucleic acid analysing techniques. The author mentions the genetic relationships of the three porcine coronaviruses and coronaviruses of other species according to a recent phylogenetic analysis. Based on this analysis there is a marked distance between the closely related TGEV/PRCV and the PEDV. Compares some of the characteristics of the epidemiology and pathogenesis of TGE and PED. In addition it gives some points of reference of the new differential diagnostic methods of the field, such as the use of monoclonal antibodies or the development of polymerase chain reaction assays and the application of non-radioactive probes in in situ hybridisation tests.",,,"Benyeda, J., Drávai, G.Y., Gajdács, G.Y., Lázár, I., (1971) Magy. Állatorv. Lapja, 26, p. 99; Benyeda, J., Mocsári, E., (1973) Magy. Állatorv. Lapja, 28, p. 409; (1994) Arch. Virol., 135, p. 227; Correa, I., Gebauer, F., (1990) J. Gen. Virol., 71, p. 271; Bridgen, A., Duarte, M., (1993) J. Gen. Virol., 74, p. 1795; De Diego, M., Rodríguez, F., (1994) J. Gen. Virol., 75, p. 2585; Delmas, B., Gelfi, J., (1992) Nature, 357, p. 417; Duarte, M., Laude, H., (1994) J. Gen. Virol., 75, p. 1195; Duarte, M., Tobler, K., (1994) Virology, 198, p. 466; Eleouet, J., Rasschaert, D., (1995) Virology, 205, p. 817; Have, P., Moving, V., (1992) Vet. Microbiol., 31, p. 1; Hoffmann, M., Wyler, R., (1988) J. Clin. Microbiol., 26, p. 2235; Horváth, I., Mocsári, E., (1979) Magy. Állatorv. Lapja, 34, p. 819; Jacobs, L., De Groot, R., (1987) Virus Res., 8, p. 363; Mensik, J., Salajka, J., (1978) Ann. Rech. Vet., 9, p. 255; Mocsári, E., (1977) Magy. Állatorv. Lapja, 32, p. 508; Mocsári, E., Csontos, L., Horváth, I., (1984) Magy. Állatorv. Lapja, 39, p. 537; Pensaert, M., Callebaut, P., Vergote, J., (1986) Vet. Quart., 8, p. 257; Pensaert, M., Cox, K., (1993) Vet. Quart., 15, p. 16; Sánchez, C., Gebauer, G., (1992) Virology, 190, p. 92; Stewart, J., Mounir, S., Talbot, P., (1992) Virology, 191, p. 502; Szent-Iványi, T., Szabó, I., Temesi, Z., Ratalics, L., (1964) Magy. Állatorv. Lapja., 19, p. 11; Weingartl, H., Derbyshire, B., (1994) J. Virol., 68, p. 7253; Wesley, R., Woods, R., (1988) Vet. Microbiol., 18, p. 197; Wesley, R., Woods, R., (1993) Vet. Microbiol., 38, p. 31; Wesley, R., Woods, R., (1990) J. Vet. Diagn. Invest., 2, p. 312; Woods, R., Wesley, R., (1992) Can. J. Vet. Res., 56, p. 170","Tamás, T.; MTA, Allatorvos-tudomanyi Kutatointezet, Hungária krt. 21, H-1143 Budapest, Hungary",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Review,"Final",,Scopus,2-s2.0-3242874190
"Gagneten S., Scanga C.A., Dveksler G.S., Beauchemin N., Percy D., Holmes K.V.","6602898805;6701713751;6603790777;7005461095;16140219400;7201657724;","Attachment glycoproteins and receptor specificity of rat coronaviruses",1996,"Laboratory Animal Science","46","2",,"159","166",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030124218&partnerID=40&md5=50814740a7903ee02f5b14a3e916fb54","Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD, United States; McGill Cancer Centre, Montreal, Que., Canada; University of Guelph, Guelph, Ont., Canada; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States","Gagneten, S., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD, United States; Scanga, C.A., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD, United States; Dveksler, G.S., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD, United States; Beauchemin, N., McGill Cancer Centre, Montreal, Que., Canada; Percy, D., University of Guelph, Guelph, Ont., Canada; Holmes, K.V., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States","Murine coronavirus (MHV) and rat coronavirus (RCV) are antigenically related viruses that have different natural rodent hosts. Both MHV and RCV can be propagated in the L2(Percy) and CMT-93 mouse cell lines. In these cell lines MHV uses the MHV receptor (MHVR or Bgp1a) and several related murine Bgp glycoproteins in the immunoglobulin superfamily as receptors. To determine whether RCV also uses these murine glycoproteins as receptors, we characterized the envelope glycoproteins of two strains of RCV and compared the effects of anti-MHVR monoclonal antibody on susceptibility of the mouse cells to MHV and RCV. The Parker (RCV-P) and sialodacryoadenitis (RCV-SDAV) strains of RCV expressed the spike glycoprotein S, but only RCV-P expressed a hemagglutinin-esterase glycoprotein that had acetylesterase activity. Therefore RCV-SDAV must bind to cellular receptors by the viral S glycoprotein, whereas RCV-P might bind to cells by its hemagglutinin-esterase glycoprotein as well as by S. Pretreatment of L2(Percy) 41.a or CMT-93 cells with anti-MHVR monoclonal antibody blocked infection with MHV-A59 but did not prevent infection of these murine cells with RCV-P or RCV-SDAV. Baby hamster kidney cells transfected with cDNAs encoding MHVR (Bgp1a) or Bgp2 were susceptible to MHV-A59 but not to RCV-P or RCV-SDAV. Thus the RCV strains cannot use these murine coronavirus receptors and must be infecting murine cells by another, as yet unknown, receptor.",,"CD66 antigens; Ceacam2 protein, mouse; cell adhesion molecule; complementary DNA; glycoprotein; hemagglutinin esterase; leukocyte antigen; monoclonal antibody; virus fusion protein; virus hemagglutinin; virus protein; virus receptor; animal; article; C3H mouse; cell line; Coronavirus; drug antagonism; genetic transfection; genetics; growth, development and aging; hamster; immunoblotting; kidney; metabolism; mouse; physiology; rat; Animals; Antibodies, Monoclonal; Antigens, CD; Cell Adhesion Molecules; Cell Line; Coronavirus, Rat; Cricetinae; DNA, Complementary; Glycoproteins; Hemagglutinins, Viral; Immunoblotting; Kidney; Mice; Mice, Inbred C3H; Rats; Receptors, Virus; Transfection; Viral Fusion Proteins; Viral Proteins","Lindsey, J.R., Prevalence of viral and mycoplasmal infections in laboratory rodents (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, pp. 801-808. , P. N. Bhatt, R. O. Jacoby, H. C. Morse III, et al. (ed.). Academic Press, Inc., New York; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Barthold, S.W., Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents. Effects on Biomedical Research, pp. 571-601. , P. N. Bhatt, R. O. Jacoby, H. C. Morse III, et al. (ed.), Academic Press, Orlando, Fla; Barthold, S.W., Beck, D.S., Smith, A.L., Mouse hepatitis virus nasoeneephalopathy is dependent upon virus strain and host genotype (1986) Arch. Virol., 91, pp. 247-256; Wege, H., Siddell, S., Ter Meulen, V., (1982) The Biology and Pathogenesis of Coronaviruses, 99, pp. 165-200; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Nedellec, P., Dveksler, G.S., Daniels, E., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Coutelier, J.-P., Godfraind, C., Dveksler, G.S., B lymphocyte and macrophage expression of carcinoembryonic antigen-related adhesion molecules that serve as receptors for murine coronavirus (1994) Eur. J. Immunol., 24, pp. 1383-1390; Jacoby, R.O., Rat coronavirus (1986) Viral and Mycoplasmal Infections of Rodents, pp. 625-638. , P. N. Bhatt, R. O. Jacoby, H. C. Morse, et al. (ed.), Academic Press, Inc., New York; Parker, J.S., Cross, S.S., Rowe, W.R., Rat coronavirus (RCV), a prevalent naturally occurring pneumotropic virus of rats (1970) Arch. Gesamte Virusforsch., 31, pp. 293-302; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Pathogenesis of sialodacryoadenitis in gnotobiotic rats (1975) Vet. Pathol., 12, pp. 196-209; Percy, D.H., Williams, K.L., Experimental Parker's coronavirus infection in Wistar rats (1990) Lab. Anim. Sci., 40, pp. 603-607; Barthold, S.W., De Souza, M.S., Smith, A.L., Susceptibility of laboratory mice to intranasal and contact infection with coronaviruses of other species (1990) Lab Anim. Sci., 40, pp. 481-485; La Regina, M., Woods, L., Klender, P., Transmission of sialodacryoadenitis virus (SDAV) from infected rats to rats and mice through handling, close contact, and soiled bedding (1992) Lab. Anim. Sci., 42, pp. 344-346; Bhatt, P.N., Percy, D., Jones, A.M., Characterization of the virus of sialodacryoadenitis of rats: A member of the coronavirus group (1972) J. Infect. Dis., 126, pp. 123-130; Hirano, N., Takamaru, H., Ono, K., Replication of sialodacryoadenitis virus of rat in LBC cell culture (1986) Arch. Virol., 88, pp. 121-125; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Susceptibility of rodent cell lines to rat coronaviruses and differential enhancement by trypsin or DEAE-dextran (1991) Arch. Virol., 118, pp. 57-66; Percy, D., Bond, S., MacInnes, J., Replication of sialodacryoadenitis virus in mouse L-2 cells (1989) Arch. Virol., 104, pp. 323-333; Percy, D.H., Williams, K.L., Bond, S.J., Characteristics of Parker's rat coronavirus (PRC) replicated in L-Z cells (1990) Arch. Virol., 112, pp. 195-202; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect Immun., 6, pp. 501-507; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect. Immun., 31, pp. 1214-1222; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronaviras envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Vlasak, R., Luytjes, W., Leider, J., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J. Virol., 62, pp. 4686-4690; Williams, R.K., Jiang, G.-S., Snyder, S.W., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Arvan, P., Cameron, R.S., Castle, J.D., Secretory membranes of the rat parotid gland: Preparation and comparative characterization (1983) Methods in Enzymology, 98, pp. 75-87. , Academic Press, Inc., New York; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Hogue, B.G., Kienzle, T.E., Brian, D.A., Synthesis and processing of the bovine enteric coronavirus hemagglutinin protein (1989) J. Gen. Virol., 70, pp. 345-352; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J. Virol., 51, pp. 384-388; Percy, D.H., Bond, S.J., Paturzo, F.X., Duration of protection from reinfection following exposure to sialodacryoadenitis virus in Wistar rats (1990) Lab. Anim. Care, 40, pp. 144-149. , Published erratum appears in Lab. Anim. Sci. 41:292; Luytjes, W., Bredenbeek, P.J., Noten, A.F., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Sugiyama, K., Ishikawa, R., Fukuhara, N., Structural polypeptides of the murine coronavirus DVIM (1986) Arch. Virol., 89, pp. 245-254; Yokomori, K., Banner, L.R., Lai, M.M., Heterogeneity of gene expression of the hemagglutininesterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Gagneten, S., Gout, O., Dubois-Dalcq, M., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. Virol., 61, pp. 185-189; Drexler, K., Dannull, J., Hindennach, I., Single mutations in a gene for a tail fiber component of an Escherichia coli phage can cause an extension from a protein to a carbohydrate as a receptor (1991) J. Mol. Biol., 219, pp. 655-663","Holmes, K.V.; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States",,,00236764,,LBASA,"8723231","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0030124218
"Poland A.M., Vennema H., Foley J.E., Pedersen N.C.","7006803895;7003697291;7402872921;7202299909;","Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus",1996,"Journal of Clinical Microbiology","34","12",,"3180","3184",,128,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029860662&partnerID=40&md5=cfd14170a6813ffc48db22895ac08e29","Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Dept. of Med. and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3508 TD Utrecht, Netherlands","Poland, A.M., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Vennema, H., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States, Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3508 TD Utrecht, Netherlands; Foley, J.E., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States, Dept. of Med. and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Two groups of cats were experimentally infected orally with the cat- passaged RM strain of feline enteric coronavirus (FECV-RM). One group of cats (n = 19) had been chronically infected with feline immunodeficiency virus (FIV) for over 6 years, while a second control group (n = 20) consisted of FIV-naive siblings. Fecal virus shedding of FECV occurred in both groups starting on day 3 postinfection, nearly ceased by 4 weeks in FIV-uninfected cats, but remained at high levels in FIV-infected animals. FIV-infected cats shed virus for a longer period of time and at levels 10 to 100 times greater than those for FIV-uninfected cats. The coronavirus antibody response of the FIV-infected cats was delayed and of reduced tiler compared with that of the FIV-uninfected animals. Cats in both groups remained asymptomatic for the first two months following FECV-RM infection; however, 8 to 10 weeks postinfection two cats in the FIV-infected group developed feline infectious peritonitis (FIP). The FIP viruses (designated FIPV-UCD9 and -UCD10) isolated from these two cats had almost complete genetic homology to each other and to the infecting FECV-RM. However, unlike FECV-RM, they readily induced FIP when inoculated intraperitoneally into specific-pathogen-free cats. This study confirms that FIPVs are frequently and rapidly arising mutants of FECV. Immunosuppression caused by chronic FIV infection may have enhanced the creation and selection of FIPV mutants by increasing the rate of FECV replication in the bowel and inhibiting the host's ability to combat the mutant viruses once they occurred.",,"animal cell; animal experiment; antibody response; article; cat disease; controlled study; coronavirus; feline immunodeficiency virus; nonhuman; priority journal; virus infection; virus mutant; virus shedding; Animals; Base Sequence; Cats; Coronavirus; Coronavirus Infections; Coronavirus, Feline; DNA Primers; Feline Acquired Immunodeficiency Syndrome; Feline Infectious Peritonitis; Immunocompromised Host; Mutation; Opportunistic Infections; Polymerase Chain Reaction; Viremia; Animalia; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline immunodeficiency virus; Feline infectious peritonitis virus; Felis catus","Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-van Dillen, P.M.E., Van Der Noordaa, J., Rapid and simple method for purification of nucleic acids (1990) J. Clin. Microbiol., 29, pp. 1804-1811; Cavanagh, D., Davis, P.J., Sequence analysis of strains of avian infectious bronchitis virus isolated during the 1960s in the U.K (1993) Arch. Virol., 130, pp. 471-476; Cheung, R.C., Matsui, S.M., Greenberg, H.B., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) J. Clin. Microbiol., 32, pp. 2593-2597; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Res, 12, pp. 387-395; Dougherty, R.M., Phillips, P.E., Gibson, S., Young, L., Restriction endonuclease digestion eliminates product contamination in reverse transcribed polymerase chain reaction (1993) J. Virol. Methods, 41, pp. 235-238; (1994) Program Manual for the Wisconsin Package, Version 8, , Genetics Computer Group, Madison, Wis; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hickman, M.A., Morris, J.G., Rogers, Q.R., Pedersen, N.C., Elimination of feline coronavirus infection from a large experimental specific pathogen-free cat breeding colony by serologic testing and isolation (1995) Feline Pract, 23, pp. 96-102; Horzinek, M.C., Herrewegh, A., De Groot, R.J., Perspectives on feline coronavirus evolution (1995) Feline Pract, 23, pp. 34-39; Kusters, J.G., Jager, E.J., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-20; Pedersen, N.C., The history and interpretation of feline coronavirus serology (1995) Feline Pract, 23, pp. 46-51; Pedersen, N.C., Boyle, J.F., Immunologic phenomenon in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Pedersen, N.C., Boyle, J.F., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Comp. Cont. Edu., 7, pp. 1001-1011; Rasschaert, D., Daurte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Reubel, G.H., Dean, G.A., George, J.W., Barlough, J.E., Pedersen, N.C., Effects of incidental infections and immune activation on disease progression in experimentally feline immunodeficiency virus infected cats (1994) J. Acquired Immune Defic. Syndr., 7, pp. 1003-1015; Reubel, G.H., George, J.W., Barlough, J.E., Higgins, J., Pedersen, N.C., Grant, C.K., Interaction of acute feline herpesvirus-1 and chronic feline immunodeficiency virus infections in experimentally infected specific pathogen free cats (1992) Vet. Immunol. Immunopathol., 35, pp. 95-120; Reubel, G.H., George, J.W., Higgins, J., Pedersen, N.C., Effect of chronic feline immunodeficiency virus infection on experimental feline caliciviral-induced disease (1994) Vet. Microbiol., 39, pp. 335-351; Torten, M., Franchini, M., Barlough, J.E., George, J.W., Mozes, E., Lutz, H., Pedersen, N.C., Progressive immune dysfunction in cats experimentally infected with feline immunodeficiency virus (1990) J. Virol., 65, pp. 2225-2230; Vennema, H., Pedersen, N.C., Unpublished observations; Vennema, H., Poland, A., Floyd-Hawkins, K., Pedersen, N.C., A comparison of the genomes of FeCVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-44; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Pedersen, N.C.; School of Veterinary Medicine, Center for Companion Animal Health, University of California, Davis, CA 95616, United States",,,00951137,,JCMID,"8940468","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0029860662
"Febr D., Bolla S., Herrewegb A.A.P.M., Horzinek M.C., Lutz H.","6506556269;6602952093;6503881531;7102624836;35480426400;","Detection of feline coronavirus RNA using RT-PCR: Basis for the study of the pathogenesis of feline infectious peritonitis (FIP) [Nachweis feliner Coronaviren mittels RT-PCR: Grundlage zum Studium der Pathogenese der Felinen Infektiösen Peritonitis (FIP)]",1996,"Schweizer Archiv fur Tierheilkunde","138","2",,"74","79",,21,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029690758&partnerID=40&md5=0b40e451dfe00d37488661362aeffa85","Veterinär-Medizinisches Labor, Dept. Inn. Veterinärmedizin, Universitavt Zurich; Institut Veternär-Virologie, Universität Utrecht; Klinisches Labor, Dept. Inn. Veterinär-Medizin, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland","Febr, D., Veterinär-Medizinisches Labor, Dept. Inn. Veterinärmedizin, Universitavt Zurich, Klinisches Labor, Dept. Inn. Veterinär-Medizin, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland; Bolla, S., Veterinär-Medizinisches Labor, Dept. Inn. Veterinärmedizin, Universitavt Zurich; Herrewegb, A.A.P.M., Institut Veternär-Virologie, Universität Utrecht; Horzinek, M.C., Institut Veternär-Virologie, Universität Utrecht; Lutz, H., Veterinär-Medizinisches Labor, Dept. Inn. Veterinärmedizin, Universitavt Zurich","The aim of this study was to further investigate the pathogenesis and epidemiology of feline coronavirus (FCoV)-infections and among others to determine the prognostic value of a positive result in the RT-PCR for FCoV in serum samples collected from cats with abdominal signs. Viral RNA was isolated from 100 μl of serum and subsequently amplified by a nested RT-PCR using primers binding to a highly conserved region of the 3′-end of the FCoV-genome. Sixty-three serum samples collected from 62 cats with abdominal signs were examined by RT-PCR and the clinical outcome was followed up. Four of these cats with a positive PCR-result are healthy more than 70 months after the collection of the blood sample. It can be concluded that viremia with FCoV does not necessarily lead to FIP and death. With respect of diagnosing FIP, a positive FCoV-RT-PCR is of low prognostic and diagnostic value. It can not be recommended to use this assay as sole indication to euthanize cats. Further studies will have to be carried out to demonstrate if the prognostic and diagnostic value of this PCR-assay in other samples such as peripheral blood mononuclear cells is more reliable. However, this method was found to be an important tool to further study the pathogenesis and epidemiology of FIP.","Coronavirus; Detection of viral RNA; Feline Infectious Peritonitis; RT-PCR","primer DNA; virus RNA; animal; animal disease; article; blood; cat; cat disease; Coronavirus; genetics; isolation and purification; methodology; mortality; nucleotide sequence; pathophysiology; polymerase chain reaction; prediction and forecasting; prognosis; reference value; Animals; Base Sequence; Cats; Conserved Sequence; Coronavirus, Feline; DNA Primers; Feline Infectious Peritonitis; Polymerase Chain Reaction; Predictive Value of Tests; Prognosis; Reference Values; RNA, Viral","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., (1984) Experimental Inoculation of Cats with Canine Coronavirus and Subsequent Challenge with Feline Infectious Peritonitis Virus, 34, pp. 592-597. , Laboratory animal Science; Barlough, J.E., Cats, coronaviruses and coronavirus antibody tests (1985) J Small Anim. Pract, 26, pp. 353-362; Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-Van Dillen, P.M.E., Van der Nordaa, J., Rapid and simple method for purification of nucleic acids (1990) J. Clin Microbiol., 28, pp. 495-503; Febr, D., Attenuierter Lebendimpfstoff (Primucell FIP™) gegen die Feline Infektiöse Peritonitis der Katze: Plazebo-kontrollierte Evaluation unter Feldbedingungen (1995) Vet -Med. Diss. Zurich.; Febr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A.P.M., Horzinek, M.C., Lutz, H., Evaluation of the safety and efficacy of a modified live FIPV vaccine under field conditions (1995) Feline Practice, 23, pp. 83-88. , Proceedings to the FIPV/FECV Workshop 1994 in Davis, Ca; Herrewegh, A.A.P.M., DeGroot, R.J., Egberink, H.F., Cepica, A., Horzinek, M.C., Rottier, R.J.M., Detection of feline coronavirus RNA in feces, tissues and body fluids of naturally infected cats by reverse transcriptase polymerase chain reaction (1995) J. Clin. Microbiol., 33, pp. 684-689; Holzworth, J., Some important disorders in cats (1963) Cornell Vet., 53, pp. 157-160; Lutz, H., Lebmann, R., Winkler, G., Kottwitz, B., Dittmer, A., Wolfensberger, C., Arnold, P., Das feline Immunschwachevirus in der Schweiz Klinik und Epidemiologie im Vergleich mit dem Leukämie- Und dem Coronavirus (1990) Schweiz. Arch. Tierheilk., 132, pp. 217-225; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res, 53, pp. 1500-1506; Pedersen, N.C., Morphologic and physical characteristics of feline infectious peritonitis virus and its growth in autochthonous peritoneal cell cultures (1976) Am. J. Vet. Res., 37, pp. 567-572; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Off, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am J. Vet. Res, 45, pp. 2580-2585; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv Exp. Med. Biol, 173, pp. 365-380; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Comp. Contin Educ. Pract Vet, 7, pp. 1001-1011; Pfeifer, M.L., Evermann, J.F., Roelke, M.E., Gallina, A.M., Ott, R.L., McKeirnan, A.J., Feline infectious peritonitis in a captive cheetah (1983) J. Am. Vet Med. Ass, 11, pp. 1317-1319; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs: What they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Practice, 23, pp. 40-44. , Proceedings to the FIPV/FECV Workshop 1994 in Davis, Ca; Watt, N.J., MacIntyre, N.J., Mc Orist, S., An extended outbreak of infectious peritonitis in a closed colony of curopean wildcats (Felis silvestris) (1993) J. Comp Path., 108, pp. 73-79","Febr, D.; Klinisches Labor, Dept. Inn. Veterinär-Medizin, Winterthurerstrasse 260, CH-8057 Zürich, Switzerland",,,00367281,,SATHA,"8720731","German","Schweiz. Arch. Tierheilkd.",Article,"Final",,Scopus,2-s2.0-0029690758
"Zhang X., Lai M.M.C.","55715175900;7401808497;","A 5′-proximal RNA sequence of murine coronavirus as a potential initiation site for genomic-length mRNA transcription",1996,"Journal of Virology","70","2",,"705","711",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030028804&partnerID=40&md5=0c52c6f73676993d7fd4747a6cf6a30e","Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Department of Molecular Microbiology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States","Zhang, X., Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Department of Molecular Microbiology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States, Howard Hughes Medical Institute, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States","Coronavirus transcription is a discontinuous process, involving interactions between a trans-acting leader and the intergenic transcription initiation sequences. A 9-nucleotide (ni) sequence (UUUAUAAAC), which is located immediately downstream of the leader at the 5′ terminus of the mouse hepatitis virus (MHV) genomic RNA, contains a sequence resembling the consensus intergenic sequence (UCUAAAC). It has been shown previously that the presence of the 9-nt sequence facilitates leader RNA switching and may enhance subgenomic mRNA transcription. It is unclear how the 9-nt sequence exerts these functions. In this study, we inserted the 9-nt sequence into a defective interfering (DI) RNA reporter system and demonstrated that mRNA transcription could be initiated from the 9-nt sequence almost as efficiently as from the intergenic sequence between genes 6 and 7. Sequence analysis of the mRNAs showed that the 9-nt sequence served as a site of fusion between the leaders and mRNA. The transcription initiation function of the 9-nt sequence could not be substituted by other 5′-terminal sequences. When the entire 5′-terminal sequence, including four copies of the UCUAA sequence plus the 9-nt sequence, was present, transcription could be initiated from any of the UCUAA copies or the 9-nt sequence, resulting in different copy numbers of the UCUAA sequence and the deletion of the 9-nt sequence in some mRNAs. All of these heterogeneous RNA species were also detected from the 5′-terminal region of the viral genomic-length RNA in MHV-infected cells. These results thus suggest that the heterogeneity of the copy number of UCUAA sequences at the 5′ end, the deletion of the 9-nt sequence in viral and DI RNAs, and the leader RNA switching are the results of transcriptional initiation from the 9-nt site. They also show that an mRNA species (mRNA 1) that lacks the 9-nt sequence can be synthesized during MHV infection. Therefore, MHV genomic RNA replication and mRNA 1 transcription may be distinguishable.",,"article; coronavirus; genome; murine hepatitis coronavirus; nucleotide sequence; priority journal; rna replication; rna sequence; rna transcription; sequence analysis; transcription initiation; Animals; Base Sequence; Binding Sites; Cell Line; Gene Expression Regulation, Viral; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; RNA, Messenger; RNA, Viral; Sequence Deletion; Trans-Activation (Genetics)","Baker, S.C., Lai, M.M.C., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) EMBO J, 9, pp. 4173-4179; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Chang, R.-Y., Krishnan, R., Brian, D.A., The leader UCUAAAC sequence element on the bovine coronavirus defective-interfering RNA replicon is not required for rapid reversion of a mutated leader (1995) Abstracts of the 14th Scientific Meeting of the American Society for Virology 1995, p. 181. , abstr W32-7, American Society for Virology. Austin, Tex; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J Virol, 66, pp. 3522-3530; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol, 69, pp. 272-280; Keck, J.G., Stohlman, S.A., Soe, L.H., Makino, S., Lai, M.M.C., Multiple recombination sites at the 5′-end of murine coronavirus RNA (1987) Virology, 156, pp. 331-341; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Charaterization of leader RNA on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3026-3630; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: Messenger RNA structure and genetic localization of the sequence divergence from the hepatotropic strain MHV3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Makino, S., Soe, L.H., Shieh, C.-K., Keck, J.G., Fleming, J.O., Coronavirus: A jumping RNA transcription (1987) Cold Spring Harbor Symp. Quant. Biol., 52, pp. 359-365; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J Virol, 46, pp. 1027-1033; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., Wilhemsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Liao, C.-L., Lai, M.M.C., Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J Virol, 68, pp. 4727-4737; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J Virol, 54, pp. 329-336; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Lai, M.M.C., Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Soe, L.H., Shieh, C.K., Lai, M.M.C., Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs (1988) J. Virol., 62, pp. 3570-3873; Makino, S., Stohlman, S.A., Lai, M.M.C., Leader sequences of murine coronavirus mRNAs can be freely reasserted: Evidence for the role of free leader RNA in transcription (1986) Proc Natl. Acad. Sci. USA, 83, pp. 4204-4208; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intercellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 39, pp. 138-151; Manaker, R.A., Piczak, C.V., Miller, A.A., Stanton, M.F., A hepatitis virus complicating studies with mouse leukemia (1961) J. Natl. Cancer Inst., 27, pp. 29-51; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 463-5467; Shieh, C.K., Lee, H.J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J Virol, 63, pp. 3729-3736; Shieh, C.K., Soe, L.H., Makino, S., Chang, M.F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genomeimplications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J, 2, pp. 1839-1844; Van der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J Virol, 68, pp. 3656-3666; Zhang, X.M., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J Virol, 68, pp. 6626-6633; Zhang, X.M., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X.M., Lai, M.M.C., Regulation of coronavirus RNA transcription is likely mediated by protein-RNA interactions (1995) Corona and Related Viruses, pp. 515-521. , P. J. Talbot and G. A. Levy (ed.), Plenum Press, New York; Zhang, X.M., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J Virol, 68, pp. 4738-4746","Zhang, X.; Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033-1054, United States; email: Xumingzh@hsc.usc.edu",,,0022538X,,JOVIA,"8551606","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0030028804
"Pénzes Z., Wroe C., Brown T.D.K., Britton P., Cavanagh D.","55761804900;7004689887;56248391000;57203302770;26642890500;","Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame",1996,"Journal of Virology","70","12",,"8660","8668",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029864544&partnerID=40&md5=9f3619fd2576b083ddd6bee2b90c71a0","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, United Kingdom; Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Ctro. Nac. de Biotechnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Pénzes, Z., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, United Kingdom, Ctro. Nac. de Biotechnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Wroe, C., Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, United Kingdom, Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, United Kingdom","The construction of a full-length clone of the avian coronavirus infectious bronchitis virus (IBV) defective RNA (D-RNA), CD-91 (9,080 nucleotides [Z. Penzes et al., Virology 203:286-293]), downstream of the bacteriophage T7 promoter is described. Electroporation of in vitro T7- transcribed CD-91 RNA into IBV helper virus-infected primary chick kidney cells resulted in the production of CD-91 RNA as a replicating D-RNA in subsequent passages. Three CD-91 deletion mutants were constructed-CD-44, CD- 58, and CD-61-in which 4,639, 3,236, and 2,953 nucleotides, respectively, were removed from CD-91, resulting in the truncation of the CD-91 long open reading frame (ORF) from 6,465 to 1,311, 1,263, or 2,997 nucleotides in CD- 44, CD-58, or CD-61, respectively. Electroporation of in vitro T7- transcribed RNA from the three constructs into IBV helper virus-infected cells resulted in the replication and packaging of CD-58 and CD-61 but not CD-44 RNA. The ORF of CD-61 was further truncated by the insertion of stop codons into the CD-61 sequence by PCR mutagenesis, resulting in constructs CD-61T11 (ORF: nucleotides 996 to 1,058, encoding 20 amino acids), CD-61T22 (ORF: nucleotides 996 to 2,294, encoding 432 amino acids), and CD-61T24 (ORF: nucleotides 996 to 2,450, encoding 484 amino acids), all of which were replicated and packaged to the same levels as observed for either CD-61 or CD-91. Analysis of the D-RNAs showed that the CD-91- or CD-61-specific long ORFs had not been restored. Our data indicate that IBV D-RNAs based on the natural D-RNA, CD-91, do not require a long ORF for efficient replication. In addition, a 1.4-kb sequence, corresponding to IBV sequence at the 5' end of the lb gene, may be involved in the packaging of IBV D-RNAs or form part of a cis-acting replication element.",,"complementary dna; messenger rna; virus rna; animal cell; article; avian infectious bronchitis virus; coronavirus; deletion mutant; embryo; nonhuman; nucleotide sequence; open reading frame; polymerase chain reaction; priority journal; virus genome; virus replication; virus transcription; Animals; Bacteriophage T7; Base Sequence; Cloning, Molecular; Defective Viruses; DNA, Complementary; Gene Deletion; Infectious bronchitis virus; Molecular Sequence Data; Open Reading Frames; Protein Biosynthesis; RNA, Viral; Sequence Deletion; Virus Assembly; Virus Replication","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Chang, R.-Y., Brian, D.A., cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5898-5905; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription using T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Huang, A.S., Baltimore, D., Defective viral particles and viral disease processes (1970) Nature, 226, pp. 325-327; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.-N., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Kozak, M., Comparison of initiation of protein synthesis in prokaryotes, eukaryotes and organelles (1983) Microbiol. Rev., 47, pp. 1-45; Kozak, M., Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes (1986) Cell, 44, pp. 283-292; Kozak, M., The scanning model for translation: An update (1989) J. Cell Biol., 108, pp. 229-241; Liao, C.-L., Lai, M.M.C., A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA (1995) Virology, 209, pp. 428-436; Lin, Y.J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol., 54, pp. 329-336; Makino, S., Shieh, C., Keck, J.G., Lai, M.M.C., Defective-interfering particles of murine coronavirus: Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Makino, S., Taguchi, F., Fujiwara, K., Defective interfering particles of mouse hepatitis virus (1984) Virology, 133, pp. 9-17; Makino, S., Yokotnori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J. Virol., 64, pp. 6045-6053; Meinkoth, J., Wahl, G., Hybridization of nucleic acids immobilized on solid supports (1984) Anal. Biochem., 138, pp. 267-284; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Muhlrad, D., Parker, R., Premature translational termination triggers mRNA decapping (1994) Nature, 370, pp. 578-581; Pénzes, Z., Tibbies, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Pulak, R., Anderson, P., mRNA surveillance by Caenorhabditis elegans smg genes (1993) Genes Dev., 7, pp. 1885-1897; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, New York; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751","Britton, P.; Compton Laboratory, Division of Molecular Biology, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom",,,0022538X,,JOVIA,"8970992","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029864544
"Homberger F.R.","7003348988;","Mouse hepatitis virus [Mäusehepatitis-Virus]",1996,"Schweizer Archiv fur Tierheilkunde","138","4",,"183","188",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2742585028&partnerID=40&md5=b0873c7c97de69bd89b3776b909028b4","Institut für Labortierkunde, Veterinärmedizinische Fak., Universität Zürich; Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland","Homberger, F.R., Institut für Labortierkunde, Veterinärmedizinische Fak., Universität Zürich, Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland","Mouse hepatitis virus (MHV), the coronavirus of the mouse (mus musculus), is one of the most important viral pathogens in contemporary laboratory mouse colonies. It is a highly mutable virus consisting of numerous antigenically distinct serotypes with different pathology. These can be divided according to their tissue tropism into respiratory and enterotropic strains. The course of an MHV infection is dependent on virus strain and host factors. Generally MHV causes an acute, self limiting infection which is inapparent in adult mice. Neonates are highly susceptible to disease and show high mortality. In an enzootically infected colony however, they are protected by maternally derived passive immunity. MHV's importance in biomedical research on one hand stems from its potential as an interfering agent, mainly in the field of immunology. On the other hand MHV serves as a model for coronaviruses of other species including man in studies on virus replication and tissue tropism. Since MHV infections are usually subclinical, detection depends on serological screening of colonies using Enzyme-linked immunosorbent assay (ELISA) or immunofluorescence. MHV is controlled by culling and rederivation of the affected colony using hysterectomy or embryo transfer or by elimination by cessation of breeding.","Coronavirus; Mouse; Mouse hepatitis virus; Tissue tropism","animal; animal disease; animal hepatitis; classification; disease model; experimental animal; mouse; Murine hepatitis coronavirus; newborn; physiology; review; rodent disease; virology; virus infection; Animals; Animals, Laboratory; Animals, Newborn; Coronavirus Infections; Disease Models, Animal; Hepatitis, Viral, Animal; Mice; Murine hepatitis virus; Rodent Diseases","Barthold, S.W., Mouse hepatitis virus. Biology and epidemiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents. Effect on Biomedical Research, pp. 571-601. , eds. Bhatt P.N., Jacoby R.O., Morse III H.C , New A.E., Academic Press; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim Sci., 43, pp. 15-28; Hierholzer, J.C., Broderson, J.R., Murphy, F.A., New strain of mouse hepatitis virus as the cause of lethal enteritis in infant mice (1979) Infect. Immun., 24, pp. 508-522; Holmes, K.V., Boyle, J.F., Frana, M.F., Mouse hepatitis virus-Molecular biology and implications for pathogenesis (1986) Viral and Mycoplasmal Infections of Laboratory Rodents. Effect on Biomedical Research, pp. 603-624. , eds. Bhatt P.N., Jacoby R.O., Morse III H.C., New A.E., Academic Press; Homberger, F.R., Maternally-derived passive immunity to enterotropic mouse hepatitis virus (1992) Arch. Virol, 122, pp. 133-141; Homberger, F.R., Barthold, S.W., Passively acquired challenge immunity to enterotropic coronavirus in mice (1992) Arch. Virol, 126, pp. 35-43; Homberger, F.R., Barthold, S.W., Smith, A.L., Duration and strain specificity of immunity to enterotropic mouse hepatitis virus (1992) Lab. Anim. Sci, 42, pp. 347-351; Lai, M.M.C., Coronavirus: Organization, Replication and expression of Genome (1990) Annu. Rev. Microbiol, 44, pp. 303-333; (1991) Infectious Diseases of Mice and Rats, , National Academy Press; Weir, E.C., Bhatt, P.N., Barthold, S.W., Cameron, G.A., Simack, P.A., Elimination of mouse hepatitis virus from a breeding colony by temporary cessation of breeding Lab (1987) Anim. Sci., 37, pp. 455-458","Homberger, F.R.; Institut für Labortierkunde, Universität Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland",,,00367281,,SATHA,"8677422","German","Schweiz. Arch. Tierheilkd.",Article,"Final",,Scopus,2-s2.0-2742585028
"Haagmans B.L., Egberink H.F., Horzinek M.C.","6701371301;7004767057;7102624836;","Apoptosis and T-cell depletion during feline infectious peritonitis",1996,"Journal of Virology","70","12",,"8977","8983",,59,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029861194&partnerID=40&md5=9cb7687cb4f0e3e775fd73b0f499a262","Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Haagmans, B.L., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands, Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Egberink, H.F., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands","Cats that have succumbed to feline infectious peritonitis, an immune- mediated disease caused by variants of feline coronaviruses, show apoptosis and T-cell depletion in their lymphoid organs. The ascitic fluid that develops in the course of the condition causes apoptosis in vitro but only in activated T cells. Since feline infectious peritonitis virus does not infect T cells, and vital proteins did not inhibit T-cell proliferation, we postulate that soluble mediators released during the infection cause apoptosis and T-cell depletion.",,"virus protein; animal experiment; animal model; animal tissue; apoptosis; article; ascites fluid analysis; cat disease; controlled study; coronavirus; lymphocyte depletion; lymphocyte proliferation; nonhuman; priority journal; t lymphocyte activation; Animals; Antigens, CD3; Apoptosis; Ascitic Fluid; Cats; Cell Division; Cells, Cultured; Coronavirus, Feline; Feline Infectious Peritonitis; Humans; Lymph Nodes; Lymphocyte Depletion; Mesentery; Spleen; T-Lymphocytes; Thymus Gland","Banda, N.K., Bernier, J., Kurahara, D.K., Kurrie, R., Haigwood, N., Sekaly, R.-P., Finkel, T.H., Crosslinking CD4 by human immunodeficiency virus gp120 primes T cells for activation-induced apoptosis (1992) J. Exp. Med., 176, pp. 1099-1106; Cohen, J.J., Duke, R.C., Fadok, V.A., Sellins, K.S., Apoptosis and programmed cell death in immunity (1992) Annu. Rev. Immunol., 10, pp. 267-293; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , S. G. Sidell (ed.), Plenum Press, New York; Dive, C., Gregory, C.D., Phipps, D.J., Evans, D.L., Milner, A.E., Wyllie, A.H., Analysis and discrimination of necrosis and apoptosis (programmed cell death) by multiparameter flow cytometry (1992) Biochim. Biophys. Acta, 1133, pp. 275-285; Esolen, L.M., Park, S.W., Hardwick, J.M., Griffin, D.E., Apoptosis as a cause of death in measles virus-infected cells (1995) J. Virol., 69, pp. 3955-3958; Gavrieli, Y., Sherman, Y., Ben-Sasson, S.A., Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation (1992) J. Cell Biol., 119, pp. 493-501; Godfraind, C., Holmes, K.V., Coutelier, J.-P., Thymus involution induced by mouse hepatitis virus A59 in BALB/c mice (1995) J. Virol., 69, pp. 6541-6547; Gruber, J., Sgonc, R., Hu, Y.H., Beug, H., Wick, G., Thymocyte apoptosis induced by elevated endogenous corticosterone levels (1994) Eur. J. Immunol., 24, pp. 1115-1121; Haagmans, B.L., Unpublished data; Hayashi, T., Sasaki, N., Ami, Y., Fujiwara, K., Role of thymus-dependent lymphocytes and antibodies in feline infectious peritonitis after oral infection (1983) Jpn. J. Vet. Sci., 45, pp. 759-766; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Hinshaw, V.S., Olsen, C.W., Dybdahl-Sissoko, N., Evans, D., Apoptosis: A mechanism of cell killing by influenza A and B viruses (1994) J. Virol., 68, pp. 7383-7388; Jacobse-Geels, H.E.L., Daha, M.R., Horzinek, M.C., Isolation and characterization of feline C3 and evidence for the immune complex pathogenesis of feline infectious peritonitis (1980) J. Immunol., 125, pp. 1606-1610; Jeurissen, S.H., Wagenaar, F., Pol, J.M., Van Der Eb, A.J., Noteborn, M.H., Chicken anemia virus causes apoptosis of thymocytes after in vivo infection and of cell lines after in vitro infection (1992) J. Virol., 66, pp. 7383-7388; Lam, K.M., Vasconcelos, A.C., Newcastle disease virus-induced apoptosis in chicken peripheral blood lymphocytes (1994) Vet. Immunol. Immunopathol., 44, pp. 45-56; Levine, B., Huang, Q., Isaacs, J.T., Reed, J.C., Griffin, D.E., Hardwick, J.M., Conversion of lytic to persistent alphavirus infection by the bcl-2 cellular oncogene (1993) Nature (London), 361, pp. 739-742; Liu, Y., Janeway, C.A., Interferon γ plays a critical role in induced cell death of effector T cell: A possible third mechanism of self-tolerance (1990) J. Exp. Med., 172, pp. 1735-1743; Meyaard, L., Otto, S.A., Jonker, R.R., Mijnster, M.J., Keet, R.P.M., Miedema, F., Programmed cell death of T cells in HIV infection (1992) Science, 257, pp. 217-219; Meyaard, L., Otto, S.A., Keet, I.P.M., Roos, M.T.L., Miedema, F., Programmed death of T cells in human immunodeficiency virus infection. No correlation with disease progression (1994) J. Clin. Invest., 93, pp. 982-988; Mosier, D., Sieburg, H., Macrophage-tropic HIV: Critical for AIDS pathogenesis? (1994) Immunol. Today, 15, pp. 332-339; Moskophidis, D., Lechner, F., Pircher, H., Zinkernagel, R.M., Virus persistence in acutely infected immunocompetent mice by exhaustion of antiviral cytotoxic T cells (1993) Nature (London), 362, pp. 758-782; Muro-Cacho, C.A., Pantaleo, G., Fauci, A.S., Analysis of apoptosis in lymph nodes of HIV infected persons. Intensity of apoptosis correlates with the general state of activation of the lymphoid tissue and not with the stage of disease or viral burden (1995) J. Immunol., 154, pp. 5555-5566; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Contin. Educ. Pract. Vet., 7, pp. 1001-1011; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus J. Clin. Microbiol., , in press; Razvi, E.S., Welsh, R.M., Programmed cell death of T lymphocytes during acute viral infection: A mechanism for virus-induced immune deficiency (1993) J. Virol., 67, pp. 5754-5765; Rimstad, E., Reubel, G.H., Dean, G.A., Higgins, J., Pedersen, N.C., Cloning, expression and characterization of biologically active feline tumour necrosis factor-α (1995) Vet. Immunol. Immunopathol., 45, pp. 297-310; Rojko, J.L., Olsen, R.G., The immunobiology of the feline leukemia virus (1984) Vet. Immunol. Immunolpathol., 3, pp. 585-590; Saha, K., Yuen, P.H., Wong, P.K.Y., Murine retrovirus-induced depletion of T cells is mediated through activation-induced death by apoptosis (1994) J. Virol., 68, pp. 2735-2740; Schijns, V.E.C.J., Wierda, C.M.H., Vahlenkamp, T.W., Horzinek, M.C., De Groot, R.J., Molecular cloning and expression of cat interferon-γ (1995) Immunogenetics, 42, pp. 440-441; Shibata, S., Kyuwa, S., Lee, S.K., Toyoda, Y., Goto, N., Apoptosis induced in mouse hepatitis virus-infected cells by a virus-specific CD8+ cytotoxic T-lymphocyte clone (1994) J. Virol., 68, pp. 7540-7545; Stoddart, C.A., Scott, F.W., Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence (1989) J. Virol., 63, pp. 436-440; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Gaskell, C.J., Virus shedding and immune responses in cats inoculated with cell culture-adapted feline infectious peritonitis virus (1988) Vet. Microbiol., 16, pp. 145-158; Surh, C.D., Sprent, J., T-cell apoptosis detected in situ during positive and negative selection in the thymus (1994) Nature (London), 372, pp. 100-103; Terai, C., Kornbluth, R.S., Pauza, C.D., Richman, D.D., Carson, D.A., Apoptosis as a mechanism of cell death in cultured T lymphoblasts acutely infected with HIV-1 (1991) J. Clin. Invest., 87, pp. 1710-1715; Vennema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J. Virol., 64, pp. 1407-1409; Weller, M., Constam, D.B., Malipiero, U., Fontana, A., Transforming growth factor-beta 2 induces apoptosis of murine T cell clones without down-regulating bcl-2 mRNA expression (1994) Eur. J. Immun., 24, pp. 1293-1300; Westendorp, M.O., Frank, R., Ochsenbauer, C., Stricker, K., Dhein, J., Walczak, H., Debatin, K.-M., Krammer, P.H., Sensitization of T cells to CD95-mediated apoptosis by HIV-1 tat and gp120 (1995) Nature (London), 375, pp. 497-500; Zheng, L., Fisher, G., Miller, R.E., Peschon, J., Lynch, D.H., Leonardo, M.J., Induction of apoptosis in mature T cells by tumor necrosis factor (1995) Nature (London), 377, pp. 348-351","Haagmans, B.L.; Infectious Diseases/Immunology Dept., Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,0022538X,,JOVIA,"8971027","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0029861194
"Nicod L.P.","57214431927;","Part of respiratory viruses in asthma [Rôle des virus respiratoires dans l'asthme]",1996,"Medecine et Hygiene","54","2141",,"2245","2248",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3242858688&partnerID=40&md5=879a2fec014d709e4266a1f9354dae3c",,"Nicod, L.P.","Viruses have probably been underestimated in their capacity la induce bronchial hyperreactivity or asthma. Rhinoviruses are the most frequently involved but other respiratory viruses have to be considered such as influenza, parainfluenza, coronavirus and respiratory syncitial viruses. The pathogenicity of these viruses is at the level of the respiratory epithelium, by the attraction and activation of inflammatory cells or through several inflammatory cascades with the release of cytokines, metabolites derived from membranes or kinines. These viral infections can result in severe asthma in previously mild and stable asthma.",,,"Dodge, R.R., Burrows, B., The prevalence and incidence of asthma and asthma-like symptoms in a general population sample (1980) Am Rev Respir Dis, 122, pp. 567-575; Leuenberger, P., Schwartz, J., Ackermann-Liebrich, U., Passive smoking exposure in adults and chronic respiratory symptoms (Sapaldia study) (1994) Am J Respir Crit Care Med, 150, pp. 1222-1228; Martinez, F.D., Antognoni, G., Macri, F., Parental smoking enhances bronchial responsiveness in nine-year-old children (1988) Am Rev Respir Dis, 138, pp. 518-523; Beasley, R., Coleman, E.D., Herman, Y., Viral respiratory tract infection and exacerbations of asthma in adult patients (1988) Thorax, 43, pp. 679-683; Carlsen, K.H., Orstavik, I., Leegaard, J., Hoeg, H., Respiratory virus infections and aeroallergens in acute bronchial asthma (1984) Arch Dis Child, 59, pp. 310-315; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) Br Med J, 310, pp. 1225-1229; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) Br Med J, 307, pp. 982-986; Kondo, S., Abe, K., The effects of influenza virus infection on FEV1 in asthmatic children: The time-course study (1991) Chest, 100, pp. 1235-1238; Lemanske Jr., R.F., Dick, E.C., Swenson, C.A., Rhinovirus upper respiratory infection increases airway hyperreactivity and late asthmatic reactions (1989) J Clin Invest, 83, pp. 1-10; Folkerts, G., Nijkamp, F.P., Virus-induced airway hyperresponsiveness (1995) Am J Respir Crit Care Med, 151, pp. 1666-1674; Bardin, P.G., Johnston, S.L., Pattemore, P.K., Viruses as precipitants of asthma symptoms: Physiology and mechanisms (1992) Clin Exp All, 22, pp. 809-822; Jacoby, D.B., Tamaoki, J., Borson, D.B., Nadel, J.A., Influenza infection causes airway hyperresponsiveness by decreasing enkephalimise (1988) J Appl Physiol, 64, pp. 2653-2658; Fryer, A.D., Jacoby, D.B., Parainfluenza virus infection damages inhibitory M2 muscarinic receptors on pulmonary parasympathetic nerves in the guinea-pig (1991) Br J Pharmacol, 102, pp. 267-271; Hegele, R.G., Hayashi, S., Hogg, J.C., Paré, P.D., Mechanisms of airway narrowing and hyperresponsiveness in viral respiratory tract infections (1995) Am J Respir Crit Care Med, 151, pp. 1659-1665; Busse, W.W., Viral infections in humans (1995) Am J Respir Crit Care Med, 151, pp. 1675-1677; Einarsson, O., Geba, G.P., Zhu, Z., Interleukin-11: Stimulation in vivo and in vitro by respiratory viruses and induction of airways hyperresponsiveness (1996) J Clin Invest, 97, pp. 915-924; Okamoto, Y., Kudo, K., Ishikawa, K., Presence of respiratory syncytial virus genomic sequences in middle ear fluid and its relationship to expression of cytokines and cell adhesion molecules (1993) J Inf Dis, 168, pp. 1277-1281; Becker, S., Soukup, J., Yankaskas, J.R., Respiratory syncytial virus infection of human primary nasal and bronchial epithelial cell cultures and bronchoalveolar macrophages (1992) Am J Respir Cell Mol Biol, 6, pp. 369-374; Busse, W.W., The role of respiratory infections in airway hyperresponsiveness and asthma (1994) Am J Respir Crit Care Med, 150, pp. S77-S9; Rothbarth, P.H., Kempen, B.M., Sprenger, M.J.W., Sense and nonsense of influenza voccinatin in asthma and chronic obstructive pulmonary disease (1995) Am J Respir Crit Care Med, 151, pp. 1682-1686",,,,00256749,,MEHGA,,"French","Med. Hyg.",Article,"Final",,Scopus,2-s2.0-3242858688
"Macy Jr. J.D., Weir E.C., Barthold S.W.","7005966543;35517171100;7103367422;","Reproductive Abnormalities Associated with a Coronavirus Infection in Rats",1996,"Laboratory Animal Science","46","1",,"129","132",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030001819&partnerID=40&md5=ecbef87674fb66082b9a8f1eb62b2c22","Yale University, School of Medicine, New Haven, CT, United States","Macy Jr., J.D., Yale University, School of Medicine, New Haven, CT, United States; Weir, E.C., Yale University, School of Medicine, New Haven, CT, United States; Barthold, S.W., Yale University, School of Medicine, New Haven, CT, United States",[No abstract available],,"animal tissue; article; coronavirus; female; nonhuman; rat; reproduction; virus infection; Abnormalities; Animals; Coronavirus Infections; Cytopathogenic Effect, Viral; Estrus; Female; Male; Nose; Rats; Rats, Inbred Lew; Rats, Sprague-Dawley; Reproduction; Rhinitis; Rodent Diseases","Brown-Grant, K., The effects of progesterone and of pentobarbitone administered at the dioestrous stage on the ovarian cycle of the rat (1969) J. Endocrinol., 43, pp. 539-552; Barthold, S.W., De Souza, M.S., Smith, A.L., Susceptibility of laboratory mice to intranasal and contact infection with coronaviruses of other species (1990) Lab. Anim. Sci., 40, pp. 481-485; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Susceptibility of rodent cell lines to rat coronaviruses and differential enhancement by trypsin or DEAE-dextran (1991) Arch. Virol., 118, pp. 57-66; Smith, A.L., An immunofluorescence test for detection of serum antibody to rodent coronaviruses (1983) Lab. Anim. Sci., 33, pp. 157-160; Jacoby, R.O., Bhatt, P.N., Gaertner, D.J., The pathogenesis of rat virus infection in infant and juvenile rats after oronasal inoculation (1987) Arch. Virol., 95, pp. 251-270; Tattersall, P., Cotmore, S.F., The rodent parvoviruses (1986) Viral and Mycoplasma Infections of Laboratory Rodents, pp. 324-325. , P. N. Bhatt, R. O. Jacoby, H. C. Morse, et al. (ed.), Academic Press, Inc., Orlando, Fla; Gaertner, D.J., Jacoby, R.O., Johnson, E.A., Characterization of acute rat parvovirus infection in situ hybridization (1993) Virus Res., 28, pp. 1-18; Paturzo, F.X., Jacoby, R.O., Bhatt, P.N., Persistence of rat virus in seropositive rats as detected by explant culture (1987) Arch. Virol., 95, pp. 137-142; Jacoby, R.O., Rat coronavirus (1986) Viral and Mycoplasma Infections of Laboratory Rodents, pp. 625-637. , P. N. Bhatt, R. O. Jacoby, H. C. Morse, et al. (ed.), Academic Press, Inc., Orlando, Fla; Utsumi, K., Ishikawa, T., Maeda, T., Infectious sialodacryoadenitis and rat breeding (1980) Lab. Animals, 14, pp. 303-307; Utsumi, K., Maeda, Y., Yokota, Y., Reproductive disorders in female rats infected with sialodacryoadenitis virus (1991) Exp. Anim., 40, pp. 361-365; Utstuni, K., Yokota, Y., Ishikawa, T., Reproductive disorders in female SHE rats infected with sialo-dacryoadentitis virus (1990) Coronaviruses and Their Diseases, pp. 525-532. , Cavanaugh and T. D. K. Brown (ed.), Plenum Press, New York; Cold, C.R., Wardman, G., The effect of parainfluenza type 1 (Sendai) virus infection on early pregnancy in the rat (1971) J. Reprod. Fertil., 24, pp. 39-43; Okamoto, S., Oka, T., Evidence for physiological function of epidermal growth factor: Progestational sialoadenectomy of mice decreases milk production and increases offspring mortality during lactation period (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 6059-6063; Percy, D.H., Hayes, M.A., Kocal, T.E., Depletion of salivary gland epidermal growth factor by sialodacryoadenitis infection (1988) Vet Pathol, 25, pp. 183-192; Naftolin, F., Brown-Grant, K., Corker, C.S., Plasma and pituitary luteinizing hormone and peripheral plasma oestradiol concentrations in the normal oestrus cycle of the rat and after experimental manipulation of the cycle (1972) J. Endocrinol., 53, pp. 17-30","Macy Jr., J.D.; Yale University, School of Medicine, New Haven, CT, United States",,,00236764,,LBASA,"8699812","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0030001819
"Marshall J.A., Doultree J.C.","35496563700;6602948136;","Chronic Excretion of Coronavirus-Like Particles in Laboratory Guinea Pigs",1996,"Laboratory Animal Science","46","1",,"104","106",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029920637&partnerID=40&md5=4adc01ccd9bbdf0f03fc50f6bfcb1859","Vic. Infect. Dis. Ref. Laboratory, Fairfield Hospital, Melbourne, Vic., Australia; VIDRL, Fairfield Hospital, Yarra Bend Rd., Fairfield, Vic. 3078, Australia","Marshall, J.A., Vic. Infect. Dis. Ref. Laboratory, Fairfield Hospital, Melbourne, Vic., Australia, VIDRL, Fairfield Hospital, Yarra Bend Rd., Fairfield, Vic. 3078, Australia; Doultree, J.C., Vic. Infect. Dis. Ref. Laboratory, Fairfield Hospital, Melbourne, Vic., Australia",[No abstract available],,"article; coronavirus; feces analysis; female; male; nonhuman; ultrastructure; Animals; Coronavirus; Coronavirus Infections; Feces; Female; Guinea Pigs; Male; Microscopy, Electron; Pregnancy","Marshall, J.A., Thompson, W.L., Gust, I.D., Coronavirus-like particles in adults in Melbourne, Australia (1989) J. Med. Virol., 29, pp. 238-243; Schnagl, R.D., Holmes, I.H., Coronavirus-like particles in stools from dogs from some country areas of Australia (1978) Vet. Rec., 102, pp. 528-529; Marshall, J.A., Healey, D.S., Studdert, M.J., Viruses and virus-like particles in the feces of dogs with and without diarrhea (1984) Aust. Vet. J., 61, pp. 33-38; Hoshino, Y., Scott, F.W., Coronavirus-like particles in the feces of normal cats (1980) Arch. Virol., 63, pp. 147-152; Marshall, J.A., Fagan, M.J., Johnston, N., Virus and virus-like particles in the feces of normal laboratory mice (1991) Lab. Anim. Sci., 41, pp. 283-284; Mathan, M., Mathan, V.I., Swaminathan, S.P., Pleomorphic virus-like particles in human feces (1975) Lancet, 1, pp. 1068-1069; Marshall, J.A., Birch, C.J., Williamson, H.G., Coronavirus-like particles and other agents in the feces of children in Efate, Vanuatu (1982) J. Trop. Med., 85, pp. 213-215; Sitbon, M., Human-enteric-coronavirus-like particles (CVLP) with different epidemiological characteristics (1985) J. Med. Virol., 16, pp. 67-76; Kidd, A.H., Esrey, S.A., Ujfalusi, M.J., Shedding of coronavirus-like particles by children in Lesotho (1989) J. Med. Virol., 27, pp. 164-169; Oliver, B., Ng, S., Marshall, J., Prolonged outbreak of Norwalk gastroenteritis in an isolated guest house (1985) Med. J. Aust., 142, pp. 391-395; Schnagl, R.D., Foti, R., Brookes, S., Serum antibodies to human enteric coronavirus-like particles in Australia, South Africa, Indonesia, Niue and Papua New Guinea (1990) Acta. Virol. (Praha.), 34, pp. 239-245; Cavanagh, D., Brien, D.A., Brinton, M., Revision of the taxonomy of the Coronavirus, Torovirus and Arterivirus genera (1994) Arch. Virol., 135, pp. 227-237; Macnaughton, M.R., Davies, H.A., Coronaviridae (1987) Animal Virus Structure, pp. 173-183. , M. V. Nermut and A. C. Steven (ed.), Elsevier Science Publishers, Amsterdam; Magnussen, P., Hyllseth, B., Marusyk, H., Morphological studies on equine arteritis virus (1970) Arch. Gesamt. Virusforsch., 30, pp. 105-112; Koopmans, M., Horzinek, M.C., Toroviruses of animals and humans: A review (1994) Adv. Virus Res., 43, pp. 233-273; Harper, L.V., Behaviour (1976) The Biology of the Guinea Pig, pp. 31-51. , J. E. Wagner and P. J. Manning (ed.), Academic Press, Inc., New York","Marshall, J.A.; VIDRL, Fairfield Hospital, Yarra Bend Rd., Fairfield, Vic. 3078, Australia",,,00236764,,LBASA,"8699803","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0029920637
"Lina B., Valette M., Foray S., Luciani J., Stagnara J., See D.M., Aymard M.","7006493939;7003960469;8128058500;57198192269;56255271800;7003408526;55306003900;","Surveillance of community-acquired viral infections due to respiratory viruses in Rhone-Alpes (France) during winter 1994 to 1995",1996,"Journal of Clinical Microbiology","34","12",,"3007","3011",,97,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029860572&partnerID=40&md5=8d0c829b64c067c4793da3b4079b21df","Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France; Laboratoire de Virologie, D. Rockefeller, 8, Ave. Rockefeller, 69373 Lyon Cedex 08, France; Reseau Survlnc. Grp. Reg. O., Laboratoire de Virologie, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France","Lina, B., Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France, Laboratoire de Virologie, D. Rockefeller, 8, Ave. Rockefeller, 69373 Lyon Cedex 08, France, Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Valette, M., Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France, Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Foray, S., Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France, Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Luciani, J., Reseau Survlnc. Grp. Reg. O., Laboratoire de Virologie, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Stagnara, J., Reseau Survlnc. Grp. Reg. O., Laboratoire de Virologie, Domaine Rockefeller, 69373 Lyon Cedex 08, France; See, D.M., Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France, Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France; Aymard, M., Laboratoire de Virologie, Ctr. Natl. Ref. Grippe-France Sud, 69373 Lyon Cedex 08, France, Fac. de Med. Lyon Grange Blanche, Domaine Rockefeller, 69373 Lyon Cedex 08, France","Nasal swab samples from patients with acute flu-like illness were evaluated for the presence of respiratory viruses in the Rhone-Alpes region of France from 1 October 1994 through 2 May 1995. The relative frequencies and seasonal distributions of the specific viruses were assessed. In addition, virus type was correlated with specific clinical signs and symptoms. During the study, 962 samples were collected by 75 medical practitioners participating in the Groupe Regional d'Observation de la Grippe surveillance network. One or more viruses were detected from 348 samples (36.1%), including 108 respiratory syncytial virus (RSV), 64 influenza virus A type H3N2, 47 influenza virus B, 64 coronavirus, 35 rhinovirus, 22 adenovirus, 5 enterovirus, and 3 parainfluenza strains. There were 16 mixed infections. RSV infections peaked in the early winter, and influenza viruses A and B infections peaked during the late winter and early spring. There were two peaks of coronavirus infections (late fall and late winter). Other viruses were detected at lower levels throughout the study period. Patients from whom adenovirus was isolated were significantly more likely to have a fever of >39.5°C than were patients with other detectable viruses (P < 0.001). Furthermore, there was a significant correlation between influenza and cough (P < 0.01) and RSV and bronchiolitis (P < .001). Thus, the current study defined the overall and relative frequencies of respiratory virus detection from nasal swab specimens in patients with an acute flu-like illness in the Rhone-Alpes region of France during a 7-month period. Correlation with clinical signs and symptoms and provisional conclusions regarding seasonality were also determined.",,"adenovirus; article; bronchiolitis; controlled study; coronavirus; coughing; enterovirus; enzyme linked immunosorbent assay; epidemiological data; human; immunohistochemistry; influenza; influenza virus; major clinical study; medical practice; priority journal; rhinovirus; rna virus infection; tissue culture; virus infection; Adenovirus Infections, Human; Adolescent; Adult; Age Distribution; Aged; Child; Child, Preschool; Common Cold; Community-Acquired Infections; Coronavirus Infections; Enterovirus Infections; France; Humans; Infant; Influenza, Human; Middle Aged; Paramyxoviridae Infections; Respiratory Syncytial Virus Infections; Respiratory Tract Infections; Seasons; Virus Diseases; Adenoviridae; Coronavirus; Enterovirus; Human adenovirus type 5; Influenza virus; Influenzavirus A; Influenzavirus B; Respiratory syncytial virus; Rhinovirus; Rice stripe virus; RNA viruses; Syncytial virus","Avila, M.M., Carballal, S., Rovaletti, H., Ebekian, B., Cusminsky, M., Weissenbacher, M., Viral etiology in acute lower respiratory infections in children from a closed community (1989) Am. Rev. Respir. Infect., 140, pp. 634-637; Aymard, M.A., Identification of pandemic viral strains. Role of the national reference center (1994) Eur. J. Epidemiol., 10, pp. 463-464; Aymard, M.A., Unpublished data; Aymard, M.A., Chomel, J.J., Allard, J.P., Thouvenot, D., Honegger, D., Floret, D., Boissel, J., Gillel, J., Epidemiology of viral infections and evaluation of the potential benefit of OM-85 BV on the virologic status of children attending day-care centers (1994) Respiration, 61 (1 SUPPL.), pp. 24-31; Aymard, M., Lina, B., Thouvenot, D., Luciani, J., Stagnara, J., A five years survey of respiratory syncytial virus infections in outpatients, abstr. BI (1996) Abstracts of the Second International Congress on Pediatric Pulmonology, , ICCP, Nice, France; Ayres, J.G., Ny, N.D., Fy, D.M., Incidence of episodes of acute asthma and acute bronchitis in general practice (1993) Br. J. Gen. Pract., 43, pp. 361-364; Chomel, J.J., Pardon, D., Thouvenot, D., Allard, J.P., Aymard, M., Comparison between three rapid methods for direct diagnosis of influenza and the conventional isolation procedure (1991) Biologicals, 95, pp. 287-292; Couch, R.B., Rhinoviruses (1996) Fields Virology, pp. 713-734. , B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Raven Press, New York; Domingez, E.A., Taber, L.H., Couch, R.B., Comparison of rapid diagnostic techniques for respiratory syncytial and influenza a virus respiratory infections in young children (1993) J. Clin. Microbiol., 31, pp. 2286-2290; Falsey, A.R., McCann, R.M., Hall, W.J., Tanner, M.A., Criddle, M.M., Formica, M.A., Irvine, C.S., Treavor, J.J., Acute respiratory tract infection in daycare centers for older persons (1995) J. Am. Geriatr. Soc., 43, pp. 30-36; Fleming, D.M., The prediction of epidemics of respiratory infection (1994) Eur. J. Epidemiol., 10, pp. 481-483; Fleming, D.M., Cross, K.W., Respiratory syncytial virus or influenza? (1993) Lancet, 342, pp. 8886-8887; Fox, J.P., Cooney, M.K., Hall, C.E., Fox, H.M., Rhinoviruses in Seattle families: 1975-1979 (1985) Am. J. Epidemiol., 122, pp. 830-846; Hannoun, C., Role of international networks for the surveillance of influenza (1994) Eur. J. Epidemiol., 10, pp. 449-450; Hemming, V.G., Viral respiratory diseases in children: Classification, etiology, epidemiology, and risk factors (1994) J. Pediatr., 124, pp. 513-516; Henrickson, K.J., Lower respiratory viral infections in immunocompetent children (1994) Adv. Pediatr. Infect. Dis., 9, pp. 59-96; Hughes, J.H., Physical and chemical methods for enhancing rapid detection of viruses and other agents (1993) Clin. Microbiol. Rev., 6, pp. 150-175; Jensen, C., Johnson, F.B., Comparison of various transport media for viability maintenance of herpes simplex virus, respiratory syncytial virus and adenovirus (1994) Diagn. Microbiol. Infect. Dis., 19, pp. 137-142; McAnerney, J.M., Johnson, S., Schoub, B.D., Surveillance of respiratory viruses. A 10-year laboratory-based study (1994) S. Afr. Med. J., 84, pp. 473-477; McIntosh, K., McQuillin, J., Reed, S.B., Gardner, P.S., Diagnosis of human coronavirus infection by immunofluorescence: Method and application to respiratory disease in hospitalized children (1978) J. Med. Virol., 2, pp. 341-346; Melnick, J.L., Rennick, V., Hampil, B., Schmidt, N.J., Ho, H.H., Lyophilized combination pools of enterovirus equine antisera: Preparation and test procedures for the identification of field strains of 42 enteroviruses (1973) Bull W. H. O., 48, pp. 263-268; Palmer, D.F., Dowdle, W.R., Coleman, M.T., Schild, G.C., Hemagglutination inhibition test (1975) Advanced Laboratory Techniques for Influenza Diagnosis, pp. 25-62. , Immunology series no. 6. Procedural guide. U.S. Department of Health, Education and Welfare, Atlanta; Panuska, J.R., Merolla, R., Rebert, N.A., Hoffman, S.P., Tsivitse, P., Cirino, N.M., Silverman, R.H., Rankin, J.A., Respiratory syncytial virus induces interleukin-10 production by human alveolar macrophages. Suppression of early cytokine production and implications for incomplete immunity (1995) J. Clin. Invest., 96, pp. 2445-2453; Pereira, M.S., Global surveillance of Influenza (1979) Br. Med. Bull., 35, pp. 9-14; Pothier, P., Nicolas, J.C., Prudhomme De Saint Maur, G., Ghim, S., Kazmierczak, A., Bricout, F., Monoclonal antibodies against respiratory syncytial virus and their use for rapid detection of virus in nasopharyngeal secretions (1985) J. Clin. Microbiol., 21, pp. 286-287; Ray, C.G., Minnich, L.L., Efficiency of immunofluorescence for rapid detection of common respiratory viruses (1987) J. Clin. Microbiol., 25, pp. 355-357; See, D.M., Tilles, J.G., Treatment of coxsackievirus A9 myocarditis in mice with WIN 54954 (1992) Antimicrob. Agents Chemother., 36, pp. 425-428; Shepard, D.A., Heinz, B.A., Rueckert, R.R., WIN 52035-2 inhibits both attachment and eclipse of human rhinovirus 14 (1993) J. Virol., 67, pp. 2245-2254; Stuart-Harris, C., Epidemiology of influenza in man (1979) Br. Med. Bull., 35, pp. 3-8; Van Lierde, S., Corbeel, L., Eggermont, E., Clinical and laboratory findings in children with adenovirus infections (1989) Eur. J. Pediatr., 148, pp. 423-425; Woods, G.L., Johnson, A.M., Rapid 24-well plate centrifugation assay for detection of influenza a virus in clinical specimens (1989) J. Virol. Methods, 24, pp. 35-42; Wright, S.A., Bieluch, V.M., Selected nosocomial viral infections (1993) Heart Lung, 22, pp. 183-187","Lina, B.; Laboratoire de Virologie, Domaine Rockefeller, 8, avenue Rockefeller, 69373 Lyon Cedex 08, France",,,00951137,,JCMID,"8940439","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0029860572
[No author name available],[No author id available],"The pork industry and risks for human health [L'industrie porcine et les risques relies a la sante humaine]",1996,"Vecteur Environnement","29","3",,"27","31",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030467424&partnerID=40&md5=8a9dc5a5d6c154cff329d5b8d154d736",,"","The pork industry is being expanded in eastern Quebec. These new farms created much apprehension amongst the local population, prompting the public health authorities to assemble information concerning the risks associated with this type of farming activity. Risks for the general population are not well documented. The major risk involves contamination of the drinking water sources by pathogenic bacteria (Salmonella spp., Yersinia spp., etc) and viruses (Rotavirus spp., Coronavirus spp., etc). The decay of pork faeces can also result in high levels of nitrates in ground water. Overfertilization by pig wastes can increase the concentration of dissolved organic carbon in water bodies, which, following chlorination, can result in elevated levels of trihalomethanes in the drinking water.",,"drinking water; health risk; industrial pollution; pollution source; pork industry; water quality; Canada, Quebec",,,"Laferriere M.",,1200670X,,,,"French",,Article,"Final",,Scopus,2-s2.0-0030467424
"Jäkel C.","8558185100;","Klinische Prüfung von Coliporc PLUS in Ferkelerzeugerbetrieben mit der Indikation Escherichia-coli-Enterotoxikose",1996,"Praktische Tierarzt","77","4",,"334","339",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-24644439676&partnerID=40&md5=a9c993b267bcf2b1c139059982f01be9","Impfstoffwerk Dessau-Tornau GmbH, Streetzer Weg, 06862 Rodleben, Germany","Jäkel, C., Impfstoffwerk Dessau-Tornau GmbH, Streetzer Weg, 06862 Rodleben, Germany","The use of Coliporc PLUS, an inactivated vaccine with the antigens K88, K99, 987p and the toxoid of heat labile enterotoxin (HLT), in all herds yielded a marked reduction in the incidence of diarrhoea in piglets aged up to 14 days. Depending on the pathogen spectrum, no further direct losses of suckling piglets of vaccinated sows were observed at the end of the test period. There were isolated cases of diarrhoea but these were mainly restricted to animals aged 15 do 20 days. Vaccination of dams led to an improvement in the health status of the piglets and a reduction in the number of animals lost through E.-coli-enterotoxicosis. Following the use of Coliporc PLUS a higher number of piglets were weaned per sow in all herds, reflected in a better reproductive performance of the units. All studies clearly demonstrate that the incidence of diarrhoea in suckling piglets is a multifactorial event, with not just bacteria but also viruses (rotavirus, coronavirus) and housing and feeding conditions playing a decisive role.",,,"Bauer, G., E.-coli-Diarrhoe der Saug- Und Absetzferkel (1986) Der Praktische Tierarzt, 5, pp. 388-398; Bauer, G., Wieler, L.H., E.-coli-Diarrhö der Saug- Und Absetzferkel: Aktueller Stand immunprophylaktischer Möglichkeiten (1993) Collegium Veterinarium, 24, pp. 87-91; Gaastra, W., De Graaf, F.K., Host specific fimbrial adhesins of non - Invasive enterotoxigenic E. coli strains (1982) Microbial Review, 46, p. 129","Jäkel, C.; Impfstoffwerk Dessau-Tornau GmbH, Streetzer Weg, 06862 Rodleben, Germany",,,0032681X,,,,"German","Prakt. Tierarzt",Article,"Final",,Scopus,2-s2.0-24644439676
"Kirk J., Zhou A.-L.","55270659600;57200868300;","Viral infection at the blood-brain barrier in multiple sclerosis: - An ultrastructural study of tissues from a UK Regional Brain Bank",1996,"Multiple Sclerosis","1","4",,"242","252",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030072649&partnerID=40&md5=09c9cb6c0969115dcc497703641b00a2","Multiple Sclerosis Research Laboratory, Queens University School of Clinical Medicine (Neuropathology), Institute of Pathology, Grosvenor Road, Belfast BT12 6BA, United Kingdom; Department of Physiology, Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom","Kirk, J., Multiple Sclerosis Research Laboratory, Queens University School of Clinical Medicine (Neuropathology), Institute of Pathology, Grosvenor Road, Belfast BT12 6BA, United Kingdom; Zhou, A.-L., Department of Physiology, Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom","Although viral infections are often invoked as environmental factors in the aetiology and pathogenesis of multiple sclerosis (MS) it is only recently that a specific, indirect, cytokine-mediated mechanism for triggering of relapses during viral infections has been demonstrated. It is not yet clear however whether this indirect mechanism can account for all reported viral associations with the aetiopathogenesis of MS. A direct causal role of central nervous system (CNS) viral infection in MS has largely been discounted following repeated failures to demonstrate virus within the oligodendrocyte-myelin unit In the light of increasing evidence of blood-brain barrier (BBB) dysfunction in MS and to further explore the issue of possible viral involvement in MS, an ultrastructural search for viruses was undertaken in the CNS microvasculature, in autopsy and biopsy tissue from human CNS primary demyelinating diseases, including MS (20 cases), idiopathic monophasic CNS demyelinating disease (Mdemy, four cases) and metabolic or immunopathological demyelinating disease (two cases). For comparison , tissues from CNS viral disease in which demyelination is a major feature (nine cases) were examined in the same way. Control CNS tissues (nine cases) from a range of other neurological and non-neurological diseases were also examined. Outside the MS and Mdemy groups, morphological evidence of virus assotiations with the BBB were found only in the acute and subacute viral encephalitides (three cases subacute sclerosing panencephalitis, one case of Herpes encephalitis) and in one case of disseminated Cytomegalovirus infection. In a small proportion of MS and Mdemy cases, particles resembling either adenovirus (one case of MS) or paramyxovirus (one case of MS, one case of Mdemy) were found in the vicinity of microvessels. In each case a different cell type or extracellular compartment was involved and an exact correlation between the virus particles and the demyelinating lesions could not be demonstrated. Furthermore, corroborative clinical or laboratory evidence of current CNS infection in these primary demyelinating disease cases was available only from the single positive Mdemy case and not from the two cases of MS. This and other previously published evidence from MS (which implicated a Coronavirus) and other diseases highlights the potential vulnerability to viral infection of cells associated with the BBB. Furthermore it is concluded that the detection rate of such infections in pathological tissue could underestimate their true frequency. A possible role of transient virus-BBB interactions in triggering focal inflammation, BBB breakdown and demyelination in some cases of MS and parainfectious demyelinating disease cannot be discounted. © 1996 Stockton Press All rights reserved.","Astrocytes; Blood-brain barrier; Endothelial cells; Lymphocytes; Multiple sclerosis; Virus infection","acute disease; adult; aged; article; blood brain barrier; brain; case report; chronic disease; disease course; health care facility; human; middle aged; multiple sclerosis; pathology; physiology; ultrastructure; United Kingdom; virology; virus infection; Acute Disease; Adult; Aged; Blood-Brain Barrier; Brain; Chronic Disease; Disease Progression; Great Britain; Humans; Middle Aged; Multiple Sclerosis; Tissue Banks; Virus Diseases","Hughes, R.A.C., Pathogenesis of multiple sclerosis (1992) J Roy Soc Med, 85, pp. 373-376; Sadovnick, A.D., Ebers, G.C., Genetic factors in the pathogenesis of MS (1994) Int MS Journal, 1, pp. 16-24; Sayetta, R.B., Theories of the etiology of multiple sclerosis: A critical review (1986) J Clin Lab Immunol, 21, pp. 55-70; Kennedy, P.G.E., Steiner, I., On the possible viral aetiology of multiple sclerosis (1994) Quart J Med, 87, pp. 523-528; Johnson, R.T., Viral aspects of multiple sclerosis (1985) Handbook of Clinical Neurology, 3 (47), pp. 319-336. , Koetsier JC (ed) Demyelinating Diseases. Elsevier, Amsterdam (N); Compston, D.A.S., Viral infection in patients with multiple sclerosis and HLA-DR matched controls (1986) Brain, 109, pp. 325-344; Martyn, C.N., Cruddas, M., Compston, D.A.S., Symptomatic Epstein-Barr virus infection and multiple sclerosis (1992) J Neurol Neurosurg Psychiat, 56, pp. 167-168; Allen, I.V., Brankin, B., Pathogenesis of multiple sclerosis - The immune diathesis and the role of viruses (1993) J Neuropathol Exp Neurol, 52, pp. 95-105; Kurtzke, J.F., Epidemiologic evidence for multiple sclerosis as an infection (1993) Clin Microbiol Rev, 6, pp. 382-427; Andersen, O., Viral infections trigger multiple sclerosis relapses - A prospective seroepidemiological study (1993) J Neurol, 240, pp. 417-422; Panitch, H.S., Influence of infection on exacerbations of multiple sclerosis (1994) Ann Neurol, 36 (1 SUPPL.), pp. S25-S28; Millar, J.H.D., (1971) Multiple Sclerosis, a Disease Acquired in Childhood, , CC Thomas, Springfield, Illinois","Kirk, J.; Multiple Sclerosis Research Laboratory, Queens University School of Clinical Medicine (Neuropathology), Institute of Pathology, Grosvenor Road, Belfast BT12 6BA, United Kingdom",,,13524585,,MUSCF,"9345442","English","Mult. Scler.",Article,"Final",,Scopus,2-s2.0-0030072649
"Blasi F.","57211284402;","Diagnosis of asthma: Laboratory procedures for identifying respiratory pathogens",1996,"European Respiratory Review","6","38",,"235","239",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029828792&partnerID=40&md5=193ebb8812f79cd09b932fc3a5eff00c","Institute of Respiratory Diseases, University of Milan, IRCCS Ospedale Maggiore, via F Sforza 35, I-20122 Milan, Italy","Blasi, F., Institute of Respiratory Diseases, University of Milan, IRCCS Ospedale Maggiore, via F Sforza 35, I-20122 Milan, Italy","In the past, research on the effects of infection in asthma has been hampered by difficulties in identifying respiratory pathogens. The viruses most commonly involved in asthma exacerbations are rhinovirus, coronavirus, influenza, parainfluenza, adenovirus and respiratory syncytial virus. Among bacteria, recent data have drawn attention to Mycoplasma pneumoniae and Chlamydia pneumoniae. Typical viral culture methods take 5-7 days. More recently, antigen detection methods, enzyme immunoassay (EIA), direct fluorescent antigen detection (DFA), and Latex agglutination have been proposed with variable sensitivity and specificity. Molecular biology techniques, particularly for rhinovirus, have proved to be highly sensitive and specific in the aetiological diagnosis of asthma exacerbations. Microbiological techniques for identification of M. pneumoniae and C. pneumoniae are based on culture, antigen detection, serology and deoxyribonucleic acid (DNA) detection by polymerase chain reaction (PCR). M. pneumoniae culture is time-consuming and requires specialized media M. pneumoniae antigen may be detected by several methods with suboptimal sensitivity. DNA detection still lacks sensitivity and must be combined with serology. The human line HL cells demonstrate high sensitivity for C. pneumoniae isolation and propagation. Cycloheximide-treated Hep-2 or NCl-H 292 monolayers also seem to be highly sensitive for isolation. Serology, particularly microimmunofluorescence, seems to be the gold standard for C. pneumoniae diagnosis, but requires paired serum samples. Antigen detection by means of DFA shows a very low sensitivity. DNA detection by PCR presents high sensitivity and specificity. New laboratory procedures, including molecular methods, should greatly improve the aetiological diagnosis of asthma exacerbations and clarify the role of chronic infection in asthma inflammation and hyperresponsiveness.","Asthma; Chlamydia pneumoniae; Culture; Mycoplasma pneumoniae; Polymerase chain reaction; Serology","antigen; cycloheximide; DNA; Adenovirus; antigen detection; asthma; bacterium culture; cell culture; Chlamydophila pneumoniae; conference paper; Coronavirus; culture medium; enzyme immunoassay; HEp 2 cell; human; immunofluorescence; Influenza virus; laboratory diagnosis; latex agglutination test; molecular biology; monolayer culture; Mycoplasma pneumoniae; Parainfluenza virus; polymerase chain reaction; Respiratory syncytial pneumovirus; respiratory tract infection; Rhinovirus; virus culture",,"Blasi, F.; Institute of Respiratory Diseases, University of Milan, IRCCS Ospedale Maggiore, via F Sforza 35, I-20122 Milan, Italy",,,09059180,,EREWE,,"English","EUR. RESPIR. REV.",Conference Paper,"Final",,Scopus,2-s2.0-0029828792
"Antón I.M., González S., Bullido M.J., Corsín M., Risco C., Langeveld J.P.M., Enjuanes L.","57198264385;34770112800;6603788749;6504134746;56251715300;7006720028;7006565392;","Cooperation between transmissible gastroenteritis coronavirus (TGEV) structural proteins in the in vitro induction of virus-specific antibodies",1996,"Virus Research","46","1-2",,"111","124",,35,"10.1016/S0168-1702(96)01390-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030580553&doi=10.1016%2fS0168-1702%2896%2901390-1&partnerID=40&md5=3d26ca8e9cdaa681c1e0ea56e0e0ee3f","Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Inst. for Anim. Sci. and H., Postbus 65, 8200 AB Lelystad, Netherlands; Children's Hospital, Division of Immunology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, United States","Antón, I.M., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain, Children's Hospital, Division of Immunology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, United States; González, S., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Bullido, M.J., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Corsín, M., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Risco, C., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Langeveld, J.P.M., Inst. for Anim. Sci. and H., Postbus 65, 8200 AB Lelystad, Netherlands; Enjuanes, L., Centro Nacional de Biotecnologia, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain","Following infection of haplotype defined NIH-miniswine with virulent transmissible gastroenteritis coronavirus (TGEV), isolated mesenteric lymph node CD4+ T-cells mounted a specific proliferative response against infectious or inactivated purified virus in secondary in vitro stimulation. A specific, dose-dependent response to the three major recombinant viral proteins: spike (S), membrane (M), and nucleoprotein (N), purified by affinity chromatography, was characterized. Induction of in vitro antibody synthesis was analyzed. The purified recombinant viral proteins induced the in vitro synthesis of neutralizing TGEV-specific antibodies when porcine TGEV-immune cells were stimulated with each of the combinations made with two of the major structural proteins: S + N, S + M, and to a minor extent with M + N, but not by the individual proteins. S-protein was dissociated from purified virus using NP-40 detergent and then micellar S-protein oligomers (S-rosettes) were formed by removing the detergent. These occurred preferentially by the association of more than 10 S-protein trimmers. These S-rosettes in collaboration with either N or M-proteins elicited TGEV-specific antibodies with titers up to 84 and 60%, respectively, of those induced by the whole virus. N-protein could be partially substituted by a 15-mer peptide that represents a T helper epitope previously identified in N-protein (Anton et al. (1995)). These results indicate that the induction of high levels of TGEV-specific antibodies requires stimulation by at least two viral proteins, and that optimum responses are induced by a combination of S-rosettes and the nucleoprotein.","antibody synthesis; coronavirus; TGEV","nucleoprotein; virus protein; animal cell; animal experiment; antibody production; article; controlled study; coronavirus; nonhuman; priority journal; swine; t lymphocyte; Animals; Antibodies, Blocking; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Surface; Cell Line; Epithelium; Haplotypes; Lymphocyte Activation; Male; Micelles; Recombinant Proteins; Species Specificity; Swine; Swine, Miniature; T-Lymphocytes; Testis; Transmissible gastroenteritis virus; Viral Proteins; Viral Structural Proteins; Animalia; Coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Antón, I.M., Suñé, C., Meloen, R.H., Borrás-Cuesta, F., Enjuanes, L., A transmissible gastroenteritis coronavirus nucleoprotein epitope elicits T helper cells that collaborate in the in vitro antibody synthesis to the three major structural viral proteins (1995) Virology, 212, pp. 746-751; Bellone, M., Karachunski, P.I., Ostlie, N., Lie, S., Conti-Tronconi, B.M., Preferential pairing of T and B-cells for production of antibodies without covalent association of T and B epitopes (1994) Eur. J. Immunol., 24, pp. 799-804; Bergmann, G., McMillan, M., Stohlman, S., Characterization of the Ld-restricted cytotoxic T-lymphocyte epitope in the mouse hepatitis virus nucleocapsid protein (1993) J. Virol., 67, pp. 7041-7049; Berthon, P., Bernard, S., Salmon, H., Binns, R.M., Kinetics of the in vitro antibody response to transmissible gastroenteritis (TGE) virus from pig mesenteric lymph node cells, using the ELISASPOT and ELISA tests (1990) J. Immunol. Methods, 131, pp. 173-182; Bohl, E.H., Saif, L.J., Passive immunity in transmissible gastroenteritis of swine: Immunoglobulin characteristics of antibodies in milk after inoculating virus by different routes (1975) Infect. Immunol, 11, pp. 23-32; Boots, A.M., Van-Lierop, M.J., Kusters, J.G., Van-Kooten, G.J., Van-Der-Zeijst, B.A., Hensen, E.J., MHC ClassII-restricted T-cell hybridomas recognizing the nucleocapsid protein of avian coronavirus IBV (1991) Immunology, 72, pp. 10-14; Boots, A.M.H., Benaissatrouw, B.J., Hesselink, W., Rijke, E., Schrier, C., Hensen, E.J., Induction of anti-viral immune responses by immunization with recombinant-DNA encoded avian coronavirus nucleocapsid protein (1992) Vaccine, 10, pp. 119-124; Brim, T.A., VanCott, J.L., Lunney, J.K., Saif, L.J., Lymphocyte proliferation responses of pigs inoculated with transmissible gastroenteritis virus or porcine respiratory coronavirus (1994) Am. J. Vet. Res., 55, pp. 494-501; Bullido, M.J., Correa, I., Jiménez, G., Suñé, C., Gebauer, F., Enjuanes, L., Induction of transmissible gastroenteritis coronavirus-neutralizing antibodies in vitro by virus-specific T helper cell hybridomas (1989) J. Gen. Virol., 70, pp. 659-672; Cavanagh, D., Coronavirus IBV: Structural characterization of the spike protein (1983) J. Gen. Virol., 64, pp. 2577-2583; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-94; De Diego, M., Laviada, M.D., Enjuanes, L., Escribano, J.M., Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 6502-6508; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike protein (1990) J. Gen. Virol., 71, pp. 1313-1323; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Enjuanes, L., Development of protection against coronavirus induced diseases (1995) A Review. Adv. Exp. Med. Biol., 380, pp. 197-211; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology (1995) The Coronaviridae, pp. 337-376. , S.G. Siddell (Ed.). Plenum Press, New York; Flory, E., Pfleiderer, M., Stuhler, A., Wege, H., Induction of protective immunity against coronavirus-induced encephalomyelitis: Evidence for an important role of CD8+ T-cells in vivo (1993) Eur. J. Immunol., 23, pp. 1757-1761; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S-protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Geysen, N.M., Meloen, R.H., Barteling, S.J., Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3998-4002; Godet, M., Ĺharidon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Heemskerk, M.H.M., Schoemaker, H.M., Spaan, W.J.M., Boog, C.J.P., Predominance of MHC class II-restricted CD4+ cytotoxic T-cells against mouse hepatitis virus A59 (1994) Immunology, 84, pp. 521-527; Heinz, F.X., Allison, S.L., Stiasny, K., Schalich, J., Holzmann, H., Mandl, C.W., Kunz, C., Recombinant and virion-derived soluble and particulate immunogens for vaccination against tick-borne encephalitis (1995) Vaccine, 13, pp. 1636-1642; Helenius, A., Bonsdorff, C.-H.V., Semliki Forest virus membrane proteins: Preparation and characterization of spike complexes soluble in detergent-free medium (1976) Biochim. Biophys. Acta, 436, pp. 895-899; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Körner, H., Schiliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S.G., Wege, H., Nucleocapsid or spike protein-specific CD4+ T-lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CDS+ T-cells (1991) J. Neuroimmunol., 147, pp. 2317-2323; La Bonnardière, C., Laude, H., High interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infect. Immunol., 32, pp. 28-31; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S.G.J., Antigenic structure of transmissible gastroenteritis virus. I Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Laude, H., Charley, B., Gelfi, J., Replication of transmissible gastroenteritis coronavirus (TGEV) in swine alveolar macrophages (1984) J. Gen. Virol., 65, pp. 327-335; Lenstra, J.A., Kusters, J.G., Koch, G., Van Der Zeijst, B.A.M., Antigenicity of the peplomer protein of infectious bronchitis virus (1989) Mol. Immunol., 26, pp. 7-15; Lunney, J.K., Pescovitz, M.D., Sachs, D.H., The swine major histocompatibility complex: Its structure and function (1986) Swine in Biomedical Research, pp. 1821-1836. , M.E. Tumbleson (Ed.). Plenum Press, New York; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci., 30, pp. 190-198; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Mobley, J., Evans, G., Dailey, M.O., Perlman, S., Immune response to a murine coronavirus: Identification of a homing receptor-negative CD4+ T-cell subset that responds to viral glycoproteins (1992) Virology, 187, pp. 443-452; Noelle, R.J., Snow, E.C., T helper cell-dependent B-cell activation (1991) FASEB J., 5, pp. 2770-2776; Pescovitz, M.D., Lunney, J.L., Sachs, D., Preparation and characterization of monoclonal antibodies reactive with porcine PBL (1984) J. Immunol., 133, pp. 368-375; Risco, C., Antón, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N-proteins (1996) J. Virol., 70, pp. 4773-4777; Roehrig, J.T., Johnson, A.J., Hunt, A.R., Beaty, B.J., Mathews, J.H., Enhancement of the antibody response to flavivirus B-cell epitope by using homologous or heterologous T-cell epitopes (1992) J. Virol., 66, pp. 3385-3390; Rothschild, M.F., Hill, H.T., Christian, L.L., Lie, W.R., Warner, C.M., Genetic differences in serum neutralization titers of pigs after vaccination with Pseudorabies modified live-virus vaccine (1984) Am. J. Vet. Res., 45, pp. 1216-1218; Saalmüller, A., Reddehase, M.J., Bühring, H., Jonjic, S., Koszinowski, U.H., Simultaneous expression of CD4 and CD8 antigens by a substantial proportion of resting porcine T-lymphocytes (1987) Eur. J. Immunol., 17, pp. 1297-1301; Sachs, D., Leight, G., Cone, J., Schwarz, S., Stuart, L., Rosemberg, S., Transplantation in miniature swine. I. Fixation of the major histocompatibility complex (1976) Transplantation, 22, pp. 559-567; Saif, L.J., Bohl, E.H., Transmissible gastroenteritis (1986) Diseases of Swine, pp. 255-274. , B.S.A.D. Leman, R.D. Glock, W.L. Mengeling, R.H.C. Penny and E. Scholl (Eds.), Iowa State University, Ames, Iowa; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sarobe, P., Lasarte, J.J., Golvano, J.J., Gullón, A., Civeira, M.P., Prieto, J., Borrás-Cuesta, F., Induction of antibodies against a peptide hapten does not require covalent linkage between the hapten and a class II presentable peptide (1991) Eur. J. Immunol., 21, pp. 1555-1558; Simons, K., Helenius, A., Garoff, H., Solubilization of the membrane proteins from Semliki Forest virus with Triton X-100 (1973) J. Mol. Biol., 80, pp. 119-133; Smerdou, C., Antón, I.M., Plana, J., Curtiss, R., Enjuanes, L., A continues epitope from Transmissible gastroenteritis coronavirus S-protein fused to E. Coli heatlabile toxin B subunit expressed by attenuated Salmonella induces serum and secretory immunity (1996) Virus Res., 41, pp. 1-9; Stohlman, S.A., Bergmann, C., Van Der Veen, R.C., Hinton, D.R., Mouse hepatitis virus-specific cytotoxic T-lymphocytes protect from lethal infection without eliminating virus from the central nervous system (1995) J. Virol., 69, pp. 684-694; Stohlman, S.A., Kyuwa, S., Cohen, M., Bergmann, C., Polo, J.M., Yeh, J., Anthony, R., Keck, J.G., Mouse hepatitis virus nucleocapsid protein-specific cytotoxic T-lymphocytes are Ld restricted and specific for the carboxy terminus (1992) Virology, 189, pp. 217-224; Stone, S.S., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG and IgM(A) to protect neonatal pigs against the coronavirus transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288. , J., K.L; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Towbin, H., Staehlin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354; Underdahl, N.R., Mebus, C.A., Stair, E.L., Rhodes, M.B., McGill, L.D., Twiehaus, M.J., Isolation of transmissible gastroenteritis virus from lungs of market-weight swine (1974) Am. J. Vet. Res., 35, pp. 1209-1216; Valero, R.M., Bray, A.M., Campbell, R.A., Dipasquale, A., Margellis, C., Rodda, S.J., Geysen, H.M., Maeji, N.J., Multipin peptide synthesis at the micromole scale using 2-hydroxyethyl methacrylate grafted polyethylene supports (1993) Int. J. Protein, 42, pp. 1-9; VanCott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut-and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Wege, H., Schliephake, A., Korner, H., Flory, E., Wege, H., An immunodominant CD4+ T-cell site on the nucleocapsid protein of murine coronavirus contributes to protection against encephalomyelitis (1993) J. Gen. Virol., 74, pp. 1287-1294; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet. Microbiol., 18, pp. 197-208; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesseling, J.G., Godeke, G.J., Schijns, V.E.C.J., Prevec, L., Frank, F.L., Horzinek, M.C., Rottier, P.J.M., Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vector protect mice against a lethal infection (1993) J. Gen. Virol., 74, pp. 2061-2069; Xue, S., Jaszewski, A., Perlman, S., Identification of a CD4+ T-cell epitope within the M-protein of a neurotropic coronavirus (1995) Virology, 208, pp. 173-179","Enjuanes, L.; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain; email: lenjuanes@samba.cnb.uam.es",,,01681702,,VIRED,"9029784","English","VIRUS RES.",Article,"Final",Open Access,Scopus,2-s2.0-0030580553
"Sapats S.I., Ashton F., Wright P.J., Ignjatovic J.","6602500837;36765347700;7404316387;6603952729;","Novel variation in the N protein of avian infectious bronchitis virus",1996,"Virology","226","2",,"412","417",,37,"10.1006/viro.1996.0670","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030589670&doi=10.1006%2fviro.1996.0670&partnerID=40&md5=bd5b00ab26c5d580f4e7c5f265afdc1a","CSIRO, Australian Annual Health Laboratory, Geelong, Vic. 3220, Australia; Department of Microbiology, Monash University, Clayton, Vic. 3168, Australia","Sapats, S.I., CSIRO, Australian Annual Health Laboratory, Geelong, Vic. 3220, Australia, Department of Microbiology, Monash University, Clayton, Vic. 3168, Australia; Ashton, F., CSIRO, Australian Annual Health Laboratory, Geelong, Vic. 3220, Australia; Wright, P.J., Department of Microbiology, Monash University, Clayton, Vic. 3168, Australia; Ignjatovic, J., CSIRO, Australian Annual Health Laboratory, Geelong, Vic. 3220, Australia","The nucleocapsid protein of coronaviruses has been considered highly conserved, showing greater than 94% conservation within strains of a given species. We determined the nucleotide sequence of the N gene and the 3' untranslated region (UTR) of eight naturally occurring strains of IBV which differed in pathogenicity and tissue tropism. In pairwise comparisons, the deduced amino acid sequences of N of five strains Vic S, N1/62, N9/74, N2/75, and V5/90 (group I) shared 92.3-98.8% identity. The three strains N1/88, Q3/88, and V18/91 (group II) shared 85.8-89.2% identity with each other, but only 60.0-63.3% identity with viruses of group I. Amino acid substitutions, deletions, and insertions occurred throughout the N protein and involved regions previously identified as being conserved. Despite the considerable variation observed between the two virus groups, all N proteins contained a high proportion of basic residues, 80% of which were conserved in position. In addition, all strains contained approximately 30 serine residues of which 10 were conserved, the majority occurring between positions 168 and 194. As for all other coronaviruses, the region between positions 92 and 103 was highly conserved. Hence, a large number of amino acid changes can be tolerated within the N protein without affecting its integrity or functioning. The 3' UTR immediately downstream from the N gene was highly heterogeneous with extensive deletions occurring in the group II strains.",,"amino acid sequence; article; Avian infectious bronchitis virus; nonhuman; nucleotide sequence; priority journal; protein structure; RNA virus","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., (1987) J. Gen. Virol., 68, pp. 57-77; Laude, H., Masters, P.S., (1995) The Coronaviridae, pp. 141-163. , (S. G. Sidel, Ed.), Plenum Press, New York; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., (1985) J. Gen. Virol., 66, pp. 573-580; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., (1992) Virus Res., 25, pp. 213-222; Zwaagstra, K.A., Van Der Zeijst, B.A.M., Kusters, J.G., (1992) J. Clin. Microb., 30, pp. 79-84; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., (1989) Virology, 169, pp. 217-221; Tung, F.Y.T., Abracham, S., Sethna, M., Hung, S.-L., Sethna, P., Hogue, B.G., Braian, D.A., (1993) Virology, 186, pp. 676-683; Vennema, H., Rossen, J.W.A., Wesseling, J., Horzinek, M.C., Rottier, P.J.M., (1992) Virology, 191, pp. 134-140; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., (1993) Virus Res., 28, pp. 19-27; Sapats, S.I., Ashton, F., Wright, P.J., Ignjatovic, J., (1996) J. Gen. Virol., 77, pp. 413-418; Ignjatovic, J., McWaters, P.G., (1991) J. Gen. Virol., 72, pp. 2915-2922; Niesters, H.G.M., Lenstra, J.A., Spaan, W.J.M., Zijderveld, A.J., Bleumink-Pluym, N.M.C., Hong, F., Van Scharrenburg, G.J.M., Van Der Zeijst, B.A.M., (1986) Virus Res., 5, pp. 253-263; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., (1994) J. Virol., 68, pp. 328-337; Parker, M.M., Masters, P.S., (1990) Virology, 179, pp. 463-468; Boots, A.M.H., Kusters, J.G., Van Noort, J.M., Zwaagstra, K.A., Rjke, E., Van Der Zeijst, B.A.M., Hensen, E.J., (1991) Immunology, 74, pp. 8-13; Kozak, M., (1987) J. Mol. Biol., 196, pp. 947-950; Higgins, D.J., Sharp, P.M., (1988) Gene, 73, pp. 237-244; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., (1988) Virology, 165, pp. 589-595; Saitou, N., Nei, M., (1987) Mol. Biol. Evol., 4, pp. 406-425","Sapats, S.I.; CSIRO, Australian Annual Health Laboratory, Geelong, Vic. 3220, Australia",,"Academic Press Inc.",00426822,,VIRLA,"8955062","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030589670
"Falsey A.R., McCann R.M., Hall W.J., Criddle M.M., Formica M.A., Wycoff D., Kolassa J.E.","7003365074;7102761124;35416533700;6603037162;7006308372;6603301019;7003722609;","The 'common cold' in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center",1997,"Journal of the American Geriatrics Society","45","6",,"706","711",,60,"10.1111/j.1532-5415.1997.tb01474.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031011376&doi=10.1111%2fj.1532-5415.1997.tb01474.x&partnerID=40&md5=67044b365d415ca60bbc7b26bf37a4bd","Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States; Department of Medicine, Univ. Rochester Sch. Med. and Dent., United States; Department of Biostatistics, Univ. Rochester Sch. Med. and Dent., United States; Infectious Disease Unit, Rochester General Hospital, 1425 Portland Ave., Rochester, NY 14621, United States","Falsey, A.R., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States, Infectious Disease Unit, Rochester General Hospital, 1425 Portland Ave., Rochester, NY 14621, United States; McCann, R.M., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States; Hall, W.J., Department of Medicine, Univ. Rochester Sch. Med. and Dent., United States; Criddle, M.M., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States; Formica, M.A., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States; Wycoff, D., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., United States; Kolassa, J.E., Department of Biostatistics, Univ. Rochester Sch. Med. and Dent., United States","OBJECTIVE: To evaluate the incidence and impact of rhinovirus and coronavirus infections in older persons attending daycare. DESIGN: Prospective descriptive study. SETTING: Three senior daycare centers in Rochester, New York. PATIENTS: Frail older persons and staff members of the daycare centers who developed signs or symptoms of an acute respiratory illness MEASUREMENTS: Demographic, medical, and physical findings were recorded on subjects at baseline and during respiratory illness. Nasopharyngeal specimens for viral culture as well as acute and convalescent sera for coronavirus 229E enzyme immunoassay (EIA) were obtained for all illnesses. RESULTS: During the 44 months of study, 352 older persons experienced 522 illnesses. Thirty-five (7%) of 522 cultures were positive for rhinovirus and 37 (8%) of 451 serologies were positive for coronavirus 229E infection. The clinical syndromes associated with rhinovirus and coronavirus infection were similar and characterized by nasal congestion, cough, and constitutional symptoms. No patient died or was hospitalized, but approximately 50% had evidence of lower respiratory tract involvement. The average illness lasted 14 days. During the same period, 113 staff developed 338 respiratory illnesses. Eight percent were identified as coronavirus and 9% as rhinovirus. Cough, sputum production, and constitutional symptoms were significantly more common among older persons. CONCLUSIONS: Rhinovirus and coronavirus 229E are common causes of moderately debilitating attire respiratory illnesses among older persons attending daycare.",,"aged; article; common cold; controlled study; Coronavirus; day care; disease severity; elderly care; human; human cell; human tissue; major clinical study; Rhinovirus; symptomatology; virus transmission","Fleming, D.M., Cross, K.W., Respiratory syncytial virus or influenza? (1993) Lancet, 342, pp. 1507-1510; Larson, H.E., Reed, S.E., Tyrell, D.A.J., Isolation of rhinoviruses and coronaviruses from 38 colds in adults (1980) J Med Virol, 5, pp. 221-229; Monto, A.S., Byran, E.R., Ohmit, S., Rhinovirus infections in Tecumseh, Michigan: Frequency of illness and number of serotypes (1987) J Infect Dis, 156, pp. 43-49; Isaacs, D., Flowers, D., Clark, J.R., Epidemiology of coronavirus infections (1983) Arch Dis Child, 58, pp. 500-503; Reed, S., The behavior of recent isolates of human respiratory coronavirus in vitro and in volunteers: Evidence of heterogeneity among 229E-related strains (1984) J Med Virol, 13, pp. 179-192; Callow, K.A., Parry, H.F., Sergeant, M., Tyrrell, D.A.J., The time course of the immune response to experimental coronavirus infection of man (1990) Epidemiol Infect, 105, pp. 435-446; Gwaltney, J.M., Hendley, J.O., Simon, G., Jordan, W.S., Rhinovirus infections in an industrial population. II. 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New York: Churchill Livingstone; Wiselka, M.J., Kent, J., Cookson, J.B., Nicholson, K.G., Impact of respiratory virus infection in patients with chronic chest disease (1993) Epidemiol Infect, 111, pp. 337-346; Buscho, R.O., Saxtan, D., Shultz, P.S., Infections with viruses and mycoplasma pneumonia during exacerbations of chronic bronchitis (1978) J Infect Dis, 137, pp. 377-383; Smith, C.B., Golden, C.A., Kanner, R.E., Renseh, A.D., Association of viral and mycoplasma pneumoniae infections with acute respiratory illness in patients with chronic obstructive pulmonary diseases (1980) Am Rev Respir Dis, 121, pp. 225-232; Minor, T.E., Dirk, E.C., Demco, A.N., Viruses as precipitants of asthmatic attacks in children (1974) JAMA, 227, pp. 292-298; Falsey, A.R., Cummingham, C.K., Barker, W.H., Respiratory syncytial virus and influenza A infections in the hospitalized elderly (1995) J Infect Dis, 172, pp. 389-394; Parainfluenza outbreaks in extended-care facilities - United States (1978) MMWR, 27, pp. 475-476; Barker, W.H., Excess pneumonia and influenza hospitalization in the US due to infzuenza epidemics, 1970-78 (1986) Am J Public Health, 76, pp. 761-765; Naclerio, R.M., Proud, D., Lichtenstein, L.M., Kinins are generated during experimental rhinovirus colds (1988) J Infect Dis, 157, p. 133; Graman, P.G., Hall, C.B., Epidemiology and control of nosocomial virus infections (1989) Infect Dis Clin North Am, 3, pp. 815-841; Gwaltney, J.M., Moskalski, P.B., Hendley, J.O., Hand-to-hand transmission of rhinovirus colds (1978) Ann Intern Med, 88, pp. 463-467; Dick, E.C., Jennings, L.C., Mink, K.A., Aerosol transmission of rhinovirus colds (1987) J Infect Dis, 156, pp. 442-448; Thacker, S.B., Addiss, D.G., Goodman, R.A., Infectious diseases and injuries in child day care: Opportunities for healthier children (1992) JAMA, 268, pp. 1720-1726; Drinka, P.J., Krause, P., Schilling, M., Report of an outbreak: Nursing home architecture and Influenza - A attack rates (1996) J Am Geriatr Soc, 44, pp. 910-913","Falsey, A.R.; Infectious Disease Unit, Rochester General Hospital, 1425 Portland Ave., Rochester, NY 14621, United States",,"Blackwell Publishing Inc.",00028614,,JAGSA,,"English","J. AM. GERIATR. SOC.",Article,"Final",Open Access,Scopus,2-s2.0-0031011376
"Brian D.A., Spaan W.J.M.","7006460232;7007172944;","Recombination and coronavirus defective interfering RNAs",1997,"Seminars in Virology","8","2",,"101","111",,54,"10.1006/smvy.1997.0109","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031441843&doi=10.1006%2fsmvy.1997.0109&partnerID=40&md5=16d7858eae4629152c4808d7877cb4af","Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 RC Leiden, Netherlands; Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States","Brian, D.A., Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 RC Leiden, Netherlands","Naturally occurring defective interfering RNAs have been found in 4 of 14 coronavirus species. They range in size from 2.2 kb to approximately 25 kb, or 80% of the 30-kb parent virus genome. The large DI RNAs do not in all cases appear to require helper virus for intracellular replication and it has been postulated that they may on their own function as agents of disease. Coronavirus DI RNAs appear to arise by internal deletions (through nonhomologous recombination events) on the virus genome or on DI RNAs of larger size by a polymerase strand-switching (copy-choice) mechanism. In addition to their use in the study of virus RNA replication and virus assembly, coronavirus DI RNAs are being used in a major way to study the mechanism of a high-frequency, site-specific RNA recombination event that leads to leader acquisition during virus replication (i.e., the leader fusion event that occurs during synthesis of subgenomic mRNAs, and the leader-switching event that can occur during DI RNA replication), a distinguishing feature of coronaviruses (and arteriviruses). Coronavirus DI RNAs are also being engineered as vehicles for the generation of targeted recombinants of the parent virus genome.","Leader fusion; Recombinant coronaviruses; RNA recombination","virus RNA; Coronavirus; gene deletion; genetic recombination; nonhuman; review; RNA replication; virus assembly; virus genome; virus replication; Coronavirus; RNA viruses","Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol., 54, pp. 329-336; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. 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Virol., 64, pp. 6045-6053; Masters, P., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Mounir, S., Talbot, P.J., Human coronavirus OC43 RNA 4 lacks two open reading frames located downstream of the S gene of bovine coronavirus (1993) Virology, 192, pp. 355-360; Taguchi, F., Ikeda, T., Makino, S., Yoshikura, H., A murine coronavirus MHV-S isolate from persistently infected cells has a leader and two consensus sequences between the M and N genes (1994) Virology, 198, pp. 355-359; Lai, M.M.C., Coronavirus: Organization, replication, and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. 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Ahlquist, Eds.), CRC Press, Boca Raton, FL; Chang, R.Y., Brian, D.A., Cis-requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5898-5905; Kim, Y.N., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Van Der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hapatitis virus (1995) J. 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USA, 86, pp. 5626-5630; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Zhang, X., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Hofmann, M.A., Chang, R.Y., Ku, S., Brian, D.A., Leader-mRNA junction sequences are unique for each subgenomic mRNA species in the bovine coronavirus and remain so throughout persistent infection (1993) Virology, 196, pp. 163-171; Jarvis, T.C., Kirkegaard, K., The polymerase in its labyrinth: Mechanisms and implications of RNA recombination (1991) Trends Genet., 7, pp. 186-191; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Carpenter, C.D., Oh, J.W., Zhang, C., Simon, A.E., Involvement of a stem-loop structure in the location of junction sites in viral RNA recombination (1995) J. Mol. Biol., 245, pp. 608-622; White, A.K., Morris, T.J., RNA determinants of junction site selection in RNA virus recombinants and defective interfering RNAs (1995) RNA, 1, pp. 1029-1040; Nagy, P.D., Bujarski, J.J., Homologous RNA recombination in brome mosaic virus: AU-rich sequences decrease the accuracy of crossovers (1996) J. Virol., 70, pp. 415-426; Simon, A.E., Bujarski, J.J., RNA-RNA recombination and evolution in virus-infected plants (1994) Annu. Rev. Phytopathol., 32, pp. 337-362; Zhang, X., Liao, C.L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-14736; Liao, C.L., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol., 66, pp. 6117-6124; Joo, M., Banerjee, S., Makino, S., Replication of murine coronavirus defective interfering RNA from negative-strand transcripts (1996) J. Virol., 70, pp. 5769-5776; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus and nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1991) Nucleic Acids Res., 20, pp. 3375-3381; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Zhang, L., Homberger, F., Spaan, W., Luytjes, W., Recombinant genomic RNA of coronavirus MHV-A59 after co-replication with a DI RNA containing the MHV-RI spike gene (1997) Virology, 230, pp. 93-102; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J.M., Characterization of defective interfering RNAs of Berne virus (1991) J. Gen. Virol., 72, pp. 1635-1643; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Bos, E.C., Luytjes, W., Van Der Meulen, H.V., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60","Brian, D.A.; Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States",,"Academic Press Inc.",10445773,,SEVIE,,"English","Semin. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0031441843
"Kolb A.F., Hegyi A., Siddell S.G.","7005622195;6603368848;7005260816;","Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N",1997,"Journal of General Virology","78","11",,"2795","2802",,31,"10.1099/0022-1317-78-11-2795","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030720509&doi=10.1099%2f0022-1317-78-11-2795&partnerID=40&md5=2efcfe694bbf27c803f815ea21e4e8be","Institute of Virology and Immunology, University of Würzburg, Versbacherstrasse 7, 97078 Würzburg, Germany","Kolb, A.F., Institute of Virology and Immunology, University of Würzburg, Versbacherstrasse 7, 97078 Würzburg, Germany; Hegyi, A., Institute of Virology and Immunology, University of Würzburg, Versbacherstrasse 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacherstrasse 7, 97078 Würzburg, Germany","Aminopeptidase N (APN) is the major cell surface receptor for group 1 coronaviruses. In this study, we have isolated and characterized a feline APN cDNA and shown that the transfection of human embryonic kidney cells with this cDNA renders them susceptible to infection with the feline coronavirus feline infectious peritonitis virus, the human coronavirus (HCV) 229E and the porcine coronavirus porcine transmissible gastroenteritis virus. By using chimeric APN genes, assembled from porcine and feline sequences, we have shown that, analogously to the human APN protein, a region within the amino-terminal part of the feline APN protein (encompassing amino acids 132-295) is essential for its HCV 229E receptor function. Furthermore, by comparing the relevant feline, human and porcine APN sequences, we were able to identify a hypervariable stretch of eight amino acids that are more closely related in the feline and human APN proteins than in the porcine APN molecule. Using PCR-directed mutagenesis, we converted this stretch of amino acids within the porcine APN molecule to the corresponding residues of the human APN molecule. These changes were sufficient to convert porcine APN into a functional receptor for HCV 229E and thus define a small number of residues that are critically important for the HCV 229E receptor function of human APN.",,"cell surface receptor; complementary DNA; microsomal aminopeptidase; virus protein; virus receptor; amino acid sequence; amino terminal sequence; article; chimera; controlled study; Coronavirus; genetic transfection; infection sensitivity; kidney cell; mutagenesis; nonhuman; polymerase chain reaction; priority journal; virus infection; Coronavirus; Felidae; Feline infectious peritonitis virus; Hepatitis C virus; human coronavirus; Human coronavirus 229E; Suidae; Transmissible gastroenteritis virus","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline enteric coronavirus isolates (1984) Laboratory Animal Science, 34, pp. 592-597; Barlough, J.E., Johnson-Lussenburg, C.M., Stoddart, C.A., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis virus (1985) Canadian Journal of Comparative Medicine, 49, pp. 303-307; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) Journal of Virology, 71, pp. 734-737; Chen, C., Okayama, H., High efficiency transformation of mammalian cells by plasmid DNA (1987) Molecular and Cellular Biology, 7, pp. 2745-2752; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Edited by S. G. Siddell. New York & London: Plenum Press; De Groot, R.J., Haar, R.T.J., Horzinek, M.C., Van Der Zeijst, B.A.M.V., Intracellular RNAs of the feline peritonitis coronavirus strain 79-1146 (1987) Journal of General Virology, 68, pp. 995-1002; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Advances in Experimental Medicine and Biology, 342, pp. 293-298; Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) Journal of Virology, 68, pp. 5216-5224; Garwes, D.J., Pathogenesis of the porcine coronaviruses (1995) The Coronaviridae, pp. 377-388. , Edited by S. G. Siddell. New York & London: Plenum Press; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline and canine coronaviruses (1982) Infection and Immunity, 37, pp. 1148-1155; Kolb, A.F., Siddell, S.G., Genomic targeting with an MBP-Cre fusion protein (1996) Gene, 183, pp. 53-60; Kolb, A.F., Gunzburg, W.H., Albang, R., Brem, G., Erfle, V., Salmons, B., Negative regulatory element in the mammary specific whey acidic protein promoter (1994) Journal of Cellular Biochemistry, 56, pp. 245-261; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) Journal of General Virology, 77, pp. 2515-2521; Myint, S.H., Human coronavirus infections (1995) The Coronaviridae, pp. 389-401. , Edited by S. G. Siddell. New York & London: Plenum Press; Olsen, J., Cowell, G.M., Konigshofer, E., Danielsen, E.M., Moller, J., Laustsen, L., Hansen, O.C., Noren, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Letters, 238, pp. 307-314; Pedersen, N.C., Ward, J., Mengeling, W.E., Antigenic relationship of the feline infectious peritonitis virus to coronaviruses of other species (1978) Archives of Virology, 58, pp. 45-53; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens, using feline infectious peritonitis virus propagated in cell culture (1981) American Journal of Veterinary Research, 42, pp. 363-367; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) Journal of General Virology, 71, pp. 1065-1073; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Suné, C., María, J.B., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Edited by S. G. Siddell. New York: Plenum Press; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) Journal of Virology, 70, pp. 8669-8674; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human amino-peptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Ziebuhr, J., (1995) Expression der 3C-like-Proteinase des Humanen Coronavirus HCV 229E, , PhD thesis, University of Würzburg, Germany","Kolb, A.F.; Institute of Virology and Immunology, University of Wurzburg, Versbacherstrasse 7, 97078 Wurzburg, Germany",,"Microbiology Society",00221317,,JGVIA,"9367365","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0030720509
"Guy J.S., Barnes H.J., Smith L.G., Breslin J.","7202723649;7102581732;37109180900;7004753945;","Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys",1997,"Avian Diseases","41","3",,"583","590",,66,"10.2307/1592148","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031193716&doi=10.2307%2f1592148&partnerID=40&md5=959f0d4b0482cb7c15b99c20300c3c4a","Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Dept. of Food Anim. and Equine Med., North Carolina State University, Raleigh, NC 27606, United States","Guy, J.S., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Barnes, H.J., Dept. of Food Anim. and Equine Med., North Carolina State University, Raleigh, NC 27606, United States; Smith, L.G., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Breslin, J., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States","A turkey coronavirus (TCV [NC95]) was characterized by antigenic comparison with other avian and mammalian coronaviruses using immunofluorescence (FA) and immunoperoxidase (IP)procedures. Based on FA and IP procedures, TCV (NC95) was determined to be antigenically indistinguishable from turkey enteric (bluecomb) coronavirus (TECV). In addition, TCV (NC95) and TECV were found to be closely related to infectious bronchitis virus (IBV); a one-way antigenic relationship was demonstrated. Polyclonal anti-bodies specific for TECV and IBV reacted strongly against TCV (NC95), as determined by FA procedures. Monoclonal antibodies (MAbs) specific for IBV matrix protein (MAb 919) reacted strongly against TCV (NC95) and TECV as determined by FA and IP procedures; an IBV peplomer protein-specific MAb (MAb 94) did not recognize the two viruses. These studies suggest an identification of TCV (NC95) as a strain of TECV, and provide evidence of a close antigenic relationship between these viruses and IBV.","Coronavirus; Infectious bronchitis virus; Turkey coronavirus","Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Enteric coronavirus; Gallus gallus; Mammalia; Meleagris gallopavo; Turkey coronavirus","Cavanagh, D., Structural polypeptides of coronavirus IBV (1981) J. Gen. Virol., 53, pp. 93-103; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1986) Avian Dis., 30, pp. 319-326; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J.S., Barnes, H.J., Poult enteritis and mortality syndrome (""spiking mortality""): An acute, transmissible disease of unknown etiology (1996) Proceedings of the 68th Northeastern Conference on Avian Disease, pp. 31-34; Guy, J.S., Barnes, H.J., Smith, L.G., Rapid diagnosis of infectious laryngotracheitis using a monoclonal antibody-based immunoperoxidase procedure (1992) Avian Pathol., 21, pp. 77-86; Karaca, K., Naqi, S., Gelb J., Jr., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Dis., 36, pp. 903-915; King, D.J., Cavanagh, D., Infectious bronchitis (1991) Diseases of Poultry, 9th Ed., pp. 471-484. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoder, Jr., eds. Iowa State University Press, Ames, IA; McNulty, M.S., Allan, G.M., Applications of immunofluorescence in veterinary viral diagnosis (1984) Recent Advances in Virus Diagnosis, pp. 15-26. , M. S. McNulty and J. B. McFerran, eds. Martinus Nijhoff, The Hague, The Netherlands; Naqi, S.A., Panigrahy, B., Hall, C.F., Bursa of Fabricius, a source of bluecomb infectious agent (1972) Avian Dis., 16, pp. 937-939; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Pomeroy, B.S., Nagaraja, K.V., Coronaviral enteritis of turkeys (bluecomb disease) (1991) Diseases of Poultry, 9th Ed., pp. 745-752. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoder, Jr., eds. Iowa State University Press, Ames, IA; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; Robb, J.A., Bond, C.W., Coronaviridae (1979) Comprehensive Virology, 14, pp. 193-247. , H. Fraenkel-Conrat and R. R. Wagner, eds. Plenum Press, New York, NY; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , L. J. Saif and K. W. Theil, eds. CRC Press, Boca Raton, FL; Schat, K.A., Purchase, H.G., Cell culture methods (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 3rd Ed., pp. 167-175. , H. G. Purchase, L. H. Arp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Senne, D.A., Virus propagation in embryonating eggs (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 3rd Ed., pp. 176-181. , H. G. Purchase, L. H. Arp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200","Guy, J.S.; DMPP, North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"9356703","English","AVIAN DIS.",Article,"Final",,Scopus,2-s2.0-0031193716
"Bonaviva A., Arbour N., Yong V.W., Talbot P.J.","7801311533;6602762564;7005214860;7102670281;","Infection of primary cultures of human neural cells by human coronaviruses 229E and OC43",1997,"Journal of Virology","71","1",,"800","806",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031060562&partnerID=40&md5=367adde338598167e1ac9657971b1cc3","Laboratory of Neuroimmunovirology, Virology Research Center, University of Quebec, Laval, Que., H7N 4Z3, Canada; Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montreal, Que., H3A 2B4, Canada; Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 Blvd. des Prairies, Laval, Que., H7N 4Z3, Canada; Department of Microbiology, University of Colorado, School of Medicine, Denver, CO 80262, United States","Bonaviva, A., Laboratory of Neuroimmunovirology, Virology Research Center, University of Quebec, Laval, Que., H7N 4Z3, Canada, Department of Microbiology, University of Colorado, School of Medicine, Denver, CO 80262, United States; Arbour, N., Laboratory of Neuroimmunovirology, Virology Research Center, University of Quebec, Laval, Que., H7N 4Z3, Canada; Yong, V.W., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montreal, Que., H3A 2B4, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Virology Research Center, University of Quebec, Laval, Que., H7N 4Z3, Canada, Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 Blvd. des Prairies, Laval, Que., H7N 4Z3, Canada","We evaluated the ability of human coronaviruses to infect primary cultures of human neural cells. Double immunofluorescence with antibodies to virus and cell markers showed infection of fetal astrocytes and of adult microglia and astrocytes by strain OC43. RNA amplification revealed infection of fetal astrocytes, adult microglia, and a mixed culture of adult oligodendrocytes and astrocytes by strain 229E. Infectious virus was released only from fetal astrocytes, with higher liters for OC43. Human coronaviruses have the capacity to infect some cells of the central nervous system, although infection of adult cells appears abortive.",,"virus antigen; virus rna; adult; article; astrocyte; brain; central nervous system infection; controlled study; coronavirus; fetus; human; human cell; immunofluorescence test; infection sensitivity; microglia; oligodendroglia; priority journal; reverse transcription polymerase chain reaction; southern blotting; virus infection; Adult; Antigens, Viral; Astrocytes; Brain; Cells, Cultured; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Fluorescent Antibody Technique, Indirect; Humans; Immunoenzyme Techniques; Microglia; Oligodendroglia; Virion","Burks, J.S., Devald, B.L., Jankovski, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Cabirac, G.F., Murray, R.S., McLaughlin, L.B., Skolnick, D.M., Hogue, B., Dorovini-Zis, K., Didier, P.J., In vitro interaction of coronaviruses with primate and human brain microvascular endothelial cells (1995) Adv. Exp. Med. Biol., 380, pp. 79-88; Cabirac, G.F., Soike, K.F., Zhang, J.Y., Hoel, K., Butunoi, C., Cai, G.Y., Johnson, S., Murray, R.S., Entry of coronavirus into primate CNS following peripheral infection (1994) Microb. Pathog., 16, pp. 349-357; Collins, A.R., Sorensen, O., Regulation of viral persistence in human glioblastoma and rhabdomyosarcoma cells infected with coronavirus OC43 (1986) Microb. Pathog., 1, pp. 573-582; Evan, G.I., Lewis, G.K., Ramsay, G., Bishop, J.M., Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product (1985) Mol. Cell. Biol., 5, pp. 3610-3616; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Lamarre, A., Talbot, P.J., Protection from lethal coronavirus infection by immunoglobulin fragments (1995) J. Immunol., 154, pp. 3975-3984; Lehky, T.J., Fox, C.H., Koenig, S., Levin, M.C., Flerlage, N., Izumo, S., Sato, E., Jacobson, S., Detection of human T-lymphotropic virus type I (HTLV-I) tax RNA in the central nervous system of HTLV-I-associated myelopathy/tropical spastic paraparesis patients hy in situ hybridization (1995) Ann. Neurol., 37, pp. 167-175; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Mucke, L., Eddleston, M., Astrocytes in infectious and immune-mediated diseases of the central nervous system (1993) FASEB J., 7, pp. 1226-1232; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann. Neurol., 31, pp. 525-533; Murray, R.S., Cai, G.-Y., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primate central nervous system (1992) Virology, 188, pp. 274-284; Myint, S.H., Human coronaviruses - A brief review (1994) Rev. Med. Virol., 4, pp. 35-46; Nuovo, G.J., Gallery, F., MacConnell, P., Braun, A., In situ detection of polymerase chain reaction-amplified HIV-1 nucleic acids and tumor necrosis factor-alpha RNA in the central nervous system (1994) Am. J. Pathol., 144, pp. 659-666; Oleszak, E.L., Kuzmak, J., Hogue, B., Parr, R., Collisson, E.W., Rodkey, L.S., Leibowitz, J.L., Molecular mimicry between Fc receptor and S peplomer protein of mouse hepatitis virus, bovine coronavirus, and transmissible gastroenteritis virus (1995) Hybridoma, 14, pp. 1-8; Pearson, J., Mims, C.A., Differential susceptibility of cultured neural cells to the human coronavirus OC43 (1985) J. Virol., 53, pp. 1016-1019; Salmi, A., Ziola, B., Hovi, T., Reunanen, M., Antibodies to coronaviruses OC43 and 229E in multiple sclerosis patients (1982) Neurology, 32, pp. 292-295; Sharpless, N., Gilbert, D., Vandercam, B., Zhou, J.M., Verdin, E., Ronnett, G., Friedman, E., Dubois-Dalcq, M., The restricted nature of HIV-1 tropism for cultured neural cells (1992) Virology, 191, pp. 813-825; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Talbot, P.J., Implication of viruses in multiple sclerosis (1995) Med. Sci., 11, pp. 837-843; Talbot, P.J., Ékandé, S., Cashman, N.R., Mounir, S., Stewart, J.N., Neurotropism of human coronavirus 229E (1994) Adv. Exp. Med. Biol., 342, pp. 339-346; Talbot, P.J., Jouvenne, P., Neurotropic potential of coronaviruses (1992) Med. Sci., 8, pp. 119-125; Talbot, P.J., Paquette, J.-S., Ciurli, C., Antel, J.P., Ouellet, F., Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis (1996) Ann. Neurol., 39, pp. 233-240; Weiss, S.R., Coronavirus SD and SK share extensive nucleotide homology with murine coronavirus MHV-A59, more than that shared between human and murine coronaviruses (1983) Virology, 126, pp. 669-677; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yong, V.W., Antel, J.P., Culture of glial cells from human brain biopsies (1992) Protocols for Neural Cell Culture, pp. 81-96. , S. Fedoroff and A. Richardson (ed.). Humana Press, Totowa, N.J; Yong, V.W., Tejada-Berges, T., Goodyer, C.G., Antel, J.P., Yong, F.P., Different proliferative response of human and mouse astrocytes to gamma-interferon (1992) Glia, 6, pp. 269-280","Talbot, P.J.; Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 Blvd. des Prairies, Laval, Que. H7N 4Z3, Canada",,,0022538X,,JOVIA,"8985420","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031060562
"Seybert A., Ziebuhr J., Siddell S.G.","7004923617;7003783935;7005260816;","Expression and characterization of a recombinant murine coronavirus 3C-like proteinase",1997,"Journal of General Virology","78","1",,"71","75",,26,"10.1099/0022-1317-78-1-71","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031013797&doi=10.1099%2f0022-1317-78-1-71&partnerID=40&md5=75a5a98e437844122e24904285dd9ec8","Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Seybert, A., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","The replication of coronaviruses involves proteolytic processing of the gene 1 translation products, pp1a and pp1ab. One of the key enzymes in this process is predicted to be a virus-encoded 3C-like proteinase. In this report, we describe a bacterial system that has allowed us to express and characterize a recombinant murine coronavirus (MHV-JHM) 3C-like proteinase. The partially purified protein has been shown to exhibit proteolytic activity in trans and mutation analysis has been used to demonstrate the indispensability of Cys-3495 for enzymatic activity. Finally, the effect of class-specific proteinase inhibitors on the trans cleavage activity of the MHV 3C-like proteinase has been used to demonstrate the functional and structural homology of this enzyme to the picornavirus 3C proteinases.",,"proteinase; proteinase inhibitor; virus enzyme; amino acid sequence; article; controlled study; Coronavirus; enzyme activity; enzyme inhibition; enzyme structure; nonhuman; Picornavirus; priority journal; protein degradation; protein expression; sequence homology; structure activity relation; virus recombinant; Bacteria (microorganisms); Coronavirus; Murinae; Murine hepatitis virus; Picornaviridae","Baum, E.Z., Bebernitz, G.A., Palant, O., Mueller, T., Plotch, S.J., Purification, properties, and mutagenesis of poliovirus 3C protease (1991) Virology, 185, pp. 140-150; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charité, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Research, 18, pp. 1825-1832; Brierley, I., Boursnell, M.E.G., Binns, M.M., Billimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frameshifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO Journal, 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshift signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Research, 17, pp. 4847-4861; Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Süss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus 229E (1996) Virology, 222, pp. 227-235; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Research, 21, pp. 5838-5842; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods in Enzymology, 275. , (in press); Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) Journal of Virology, 68, pp. 5772-5780; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) Journal of Virology, 69, pp. 3554-3559; Malcolm, B.A., Chin, S.M., Jewell, D.A., Stratton-Thomas, J.R., Thudium, K.B., Ralston, R., Rosenberg, S., Expression and characterization of recombinant hepatitis A virus 3C proteinase (1992) Biochemistry, 31, pp. 3358-3363; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., A region of the infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate (1995) Journal of General Virology, 76, pp. 3059-3070; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) Journal of Virology, 70, pp. 1923-1930; Yao, Z., Jones, D.H., Grose, C., Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction (1992) PCR Methods and Applications, 1, pp. 205-207; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) Journal of Virology, 69, pp. 4331-4338","Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,"Microbiology Society",00221317,,JGVIA,"9010287","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0031013797
"Stühler A., Flory E., Wege H., Lassmann H., Wege H.","6602388166;7003965470;7005516646;35420677900;7005516649;","No evidence for quasispecies populations during persistence of the coronavirus mouse hepatitis virus JHM: Sequence conservation within the surface glycoprotein gene S in Lewis rats",1997,"Journal of General Virology","78","4",,"747","756",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842288544&partnerID=40&md5=01924316f253c76d7958dc8e3606b531","Institute of Virology, University of Würzburg, Versbacher Straße 7, D-97078 Würzburg, Germany; Res. U. for Exp. Neuropathology, Schwarzspanier Straße 17, A-1090 Vienna, Austria; Institute of Diagnostic Virology, Fed. Res. Ctr. Virus Dis. of Animals, Friedrich-Loeffler-Institutes, D-17498 Insel Riems, Germany; Institute of Diagnostic Virology, Germany; Ludwig Institute for Cancer Research, Imp. Coll. Sch. Med. at St. Mary's, Norfolk Place, London W2 1PG, United Kingdom; Inst. Med. Radiobiol. and Cell Res., University of Würzburg, Versbacher Straße 5, D-97078 Würzburg, Germany","Stühler, A., Institute of Virology, University of Würzburg, Versbacher Straße 7, D-97078 Würzburg, Germany, Ludwig Institute for Cancer Research, Imp. Coll. Sch. Med. at St. Mary's, Norfolk Place, London W2 1PG, United Kingdom; Flory, E., Institute of Virology, University of Würzburg, Versbacher Straße 7, D-97078 Würzburg, Germany, Inst. Med. Radiobiol. and Cell Res., University of Würzburg, Versbacher Straße 5, D-97078 Würzburg, Germany; Wege, H., Institute of Virology, University of Würzburg, Versbacher Straße 7, D-97078 Würzburg, Germany; Lassmann, H., Res. U. for Exp. Neuropathology, Schwarzspanier Straße 17, A-1090 Vienna, Austria; Wege, H., Institute of Virology, University of Würzburg, Versbacher Straße 7, D-97078 Würzburg, Germany, Institute of Diagnostic Virology, Fed. Res. Ctr. Virus Dis. of Animals, Friedrich-Loeffler-Institutes, D-17498 Insel Riems, Germany, Institute of Diagnostic Virology, Germany","The surface glycoprotein S (spike) of coronaviruses is believed to be an important determinant of virulence and displays extensive genetic polymorphism in cell culture isolates. This led us to consider whether the observed heterogeneity is reflected by a quasispecies distribution of mutated RNA molecules within the infected organ. Coronavirus infection of rodents is a useful model system for investigating the pathogenesis of virus-induced central nervous system (CNS) disease. Here, we investigated whether genetic changes in the S gene occurred during virus persistence in vivo. We analysed the variability of S gene sequences directly from the brain tissue of Lewis rats infected with the coronavirus mouse hepatitis virus (MHV) variant JHM-Pi using RT-PCR amplification methods. The S gene sequence displayed a remarkable genetic stability in vivo. No evidence for a quasispecies distribution was found by sequence analysis of amplified S gene fragments derived from the CNS of Lewis rats. Furthermore, the S gene also remained conserved under the selection pressure of a neutralizing antibody. Only a few mutations predicted to result in amino acid changes were detected in single clones. The changes were not represented in the consensus sequence. These results indicate that to retain functional proteins under the constraints of a persistent infection in vivo, conservation of sequence can be more important than heterogeneity.",,"neutralizing antibody; virus envelope protein; virus glycoprotein; amino acid substitution; animal cell; animal experiment; animal tissue; article; brain tissue; consensus sequence; controlled study; gene mutation; gene sequence; genetic polymorphism; genetic selection; genetic stability; Murine hepatitis coronavirus; nonhuman; persistent virus infection; priority journal; rat; reverse transcription polymerase chain reaction; virus gene","Adami, C., Pooly, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Baczko, K., Lampe, J., Liebert, U.G., Brinckmann, U., Ter Meulen, V., Pardowitz, I., Budka, H., Rima, B.K., Clonal expansion of hypermutated measles virus in a SSPE brain (1993) Virology, 197, pp. 188-195; Banner, L.R., Keck, G.K., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Barac-Latas, V., Suchanek, G., Breitschopf, H., Stühler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in coronavirus induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, , in press; Baybutt, H.N., Wege, H., Carter, M.J., Ter Meulen, V., Adaptation of coronavirus JHM to persistent infection of murine Sac(-) cells (1984) Journal of General Virology, 65, pp. 915-924; Birnboim, H.C., Doly, J., A rapid alkaline extraction method for screening recombinant plasmid DNA (1979) Nucleic Acids Research, 7, pp. 1513-1523; Cattaneo, R., Billeter, M.A., Mutations and A/I hypermutations in measles virus persistent infections (1992) Current Topics in Microbiology and Immunology, 176, pp. 63-74; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analytical Biochemistry, 162, pp. 156-159; Dalziel, R.G., Lamport, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alterations of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) Journal of Virology, 59, pp. 463-471; Domingo, E., Diez, J., Martinez, M.A., Hernandez, J., Holguin, A., Borrego, B., Mateu, M.G., New observations on antigenic diversification of RNA viruses. 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Siddell, S.G., (1995) The Coronaviridae, , New York & London: Plenum Press; Stühler, A., Wege, H., Siddell, S.G., Localization of antigenic sites on the surface glycoprotein of mouse hepatitis virus (1991) Journal of General Virology, 72, pp. 1655-1658; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brains after infection by coronavirus mouse hepatitis virus JHM (1985) Journal of Virology, 54, pp. 429-435; Vartanian, J.P., Meyerhans, A., Henry, M., Wain-Hobson, S., High resolution structure of an HIV-1 quasispecies: Identification of novel coding sequences (1992) AIDS, 6, pp. 1095-1098; Wang, F.I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wang, L., Junker, D., Hock, L., Ebiary, E., Collison, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Research, 34, pp. 327-338; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions by BMP stimulated lymphocytes from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Seminars in Immunopathology, 17, pp. 133-148; Wege, H., Siddell, S.G., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Current Topics in Microbiology and Immunology, 99, pp. 165-200; Wege, H., Dörries, R., Wege, H., Hybridoma antibodies to the murine coronavirus JHM: Characterization of epitopes on the peplomer protein (E2) (1984) Journal of General Virology, 65, pp. 1931-1942; Wege, H., Watanabe, R., Ter Meulen, V., Relapsing subacute demyelinating encephalomyelitis in rats in the course of coronavirus JHM infection (1984) Journal of Neuroimmunology, 6, pp. 325-336; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) Journal of General Virology, 69, pp. 87-98; Wong, T.C., Ayata, H., Ueda, S., Hirano, A., Role of biased hypermutation on evolution of subacute sclerosing panencephalitis virus from progenitor acute measles virus (1991) Journal of Virology, 65, pp. 2191-2199; Yokomori, K., Stohlman, S.A., Lai, H.H.C., The detection and characterization of multiple hemagglutinin-esterase (HE)-defective viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178; Zimprich, F., Winter, J., Wege, H., Lassmann, H., Coronavirus induced primary demyelination: Indications for the involvement of a humoral immune response (1991) Neuropathology and Applied Neurobiology, 17, pp. 469-484","Wege, H.; Institute of Diagnostic Virology, Fed. Res. Ctr Virus Diseases Animals, Friedrich-Loeffler-lnstitutes, D-17498 Insel Riems, Germany; email: wege@rie.bfav.de",,"Society for General Microbiology",00221317,,JGVIA,,"English","J. GEN. VIROL.",Article,"Final",,Scopus,2-s2.0-1842288544
"Lane T.E., Buchmeier M.J.","24722465300;7006201704;","Murine coronavirus infection: A paradigm for virus-induced demyelinating disease",1997,"Trends in Microbiology","5","1",,"9","14",,87,"10.1016/S0966-842X(97)81768-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031053499&doi=10.1016%2fS0966-842X%2897%2981768-4&partnerID=40&md5=71a7eb726669229f0f41ca34498a63ab","Dept of Neuropharmacology, Scripps Research Institute, 10666 N. Torrey Pines Rd, San Diego, CA 92037, United States","Lane, T.E., Dept of Neuropharmacology, Scripps Research Institute, 10666 N. Torrey Pines Rd, San Diego, CA 92037, United States; Buchmeier, M.J., Dept of Neuropharmacology, Scripps Research Institute, 10666 N. Torrey Pines Rd, San Diego, CA 92037, United States","A variety of neurological diseases in humans, including multiple sclerosis (MS), have been postulated to have a viral etiology. The use of animal models provides insights into potential mechanism(s) involved in the disease process. The murine coronavirus-induced demyelinating disease in rodents is one such model for demyelinating disease in humans.",,"animal model; Coronavirus; demyelination; disease model; immune response; mouse; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; priority journal; review; virus cell interaction; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Rodentia","Oldstone, M.B.A., (1996) Curr. Top. Microbiol. Immunol., 206, pp. 67-83; Allen, I., Brankin, B., (1993) J. Neuropathol. Exp. Neurol., 52, pp. 95-105; Steinman, L., (1996) Cell, 85, pp. 299-302; McIntosh, K., (1996) Fields Virology (3rd Edn), pp. 401-430. , Fields, B.N. et al., eds, Lippincott-Raven; Myint, S.H., (1995) The Coronaviridae, pp. 389-398. , Siddell, S.G., ed., Plenum Press; Murray, R.S., (1992) Ann. Neurol., 31, pp. 525-533; Stewart, J.N., Mounir, S., Talbot, P.J., (1992) Virology, 191, pp. 502-505; Salmi, A., (1982) Neurology, 32, pp. 292-295; Murray, R.S., (1992) Virology, 188, pp. 274-284; Bergstrom, T., Andersen, O., Vahlne, A., (1989) Ann. Neurol., 26, pp. 283-285; Field, E.J., (1972) Lancet, 2, pp. 387-390; Koprowski, H., (1985) Nature, 318, pp. 154-160; Johnson, R.T., (1994) Ann. Neurol., 36, pp. 554-560; Dales, S., Anderson, R., (1995) The Coronaviridae, pp. 257-282. , Siddell, S.G., ed., Plenum Press; Fazakerley, J.K., Buchmeier, M.J., (1993) Advances in Virus Research, 42, pp. 249-297. , Maramorosch, K. et al., eds, Academic Press; Buchmeier, M.J., Dalziel, R.G., Koolen, M.J.M., (1988) J. Neuroimmunol., 20, pp. 111-116; Kyuma, S., (1992) Microb. Pathog., 12, pp. 95-104; Raine, C.S., (1994) Ann. Neurol., 36, pp. 561-572; Lampert, P.W., Sims, J.K., Kniazeff, A.J., (1973) Acta Neuropathol., 24, pp. 76-85; Weiner, L.P., (1973) Arch. Neurol., 28, pp. 298-303; Hofman, F.M., (1986) J. Immunol., 136, pp. 3239-3245; Hofman, F.M., (1989) Exp. Med., 170, pp. 607-612; Selmaj, K.W., (1992) Semin. Neurosci., 4, pp. 221-229; Bö, L., (1994) Ann. Neurol., 36, pp. 778-786; Sun, N., (1995) Virology, 213, pp. 482-493; Nathan, C., Xie, Q., (1994) Cell, 78, pp. 915-918; Tsunoda, I., Fujinami, R.S., (1996) J. Neuropathol. Exp. Neurol., 55, pp. 673-686; Holmes, K.V., Lai, M.M.C., (1996) Fields Virology (3rd Edn), pp. 1075-1094. , Fields, B.N. et al., eds, Lippincott-Raven; Dalziel, R.G., (1986) J. Virol., 59, pp. 463-471; Williams, R.K., (1990) J. Virol., 64, pp. 3817-3823; Chen, D.S., (1995) Proc. Natl. Acad. Sci. U. S. A., 92, pp. 12095-12099; Knobler, R.L., Haspel, M.V., Oldstone, M.B.A., (1981) J. Exp. Med., 153, pp. 832-843; Dveksler, G.S., (1993) Adv. Exp. Med. Biol., 342, pp. 267-272; Fleming, J.O., (1986) J. Virol., 58, pp. 869-875; Haspel, M.V., Lampert, P.W., Oldstone, M.B.A., (1978) Proc. Natl. Acad. Sci. U. S. A., 75, pp. 4033-4036; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., (1991) J. Virol., 65, pp. 1916-1928; Fazakerley, J.K., (1992) Virology, 187, pp. 178-188; Dorries, R., (1994) J. Neurol. Neurosurg. Psychiatry, 57, pp. 518-520; Wang, F.-L., Stohlman, S.A., Fleming, J.O., (1990) J. Neuroimmunol., 30, pp. 31-41; Houtman, J.J., Fleming, J.O., (1996) J. Neurol. Virol., 2, pp. 101-110; Suzumura, A., (1986) Science, 232, pp. 991-993; Gilmore, W., Correale, J., Weiner, L.P., (1994) J. Exp. Med., 180, pp. 1013-1023; Joseph, J., (1990) Adv. Exp. Med. Biol., 276, pp. 579-591; Gombold, J.L., (1995) Microb. Pathog., 18, pp. 211-221; Borrow, P., Nash, A.A., (1992) Immunology, 76, pp. 133-139; Massa, P.T., Ter Meulen, V., Fontana, A., (1987) Proc. Natl. Acad. Sci. U.S.A., 84, pp. 4219-4227; Massa, P.T., Brinkman, R., Ter Meulen, V., (1987) J. Exp. Med., 166, pp. 259-266; Massa, P.T., (1987) Adv. Exp. Med. Biol., 218, pp. 203-211; Talbot, P.J., (1996) Ann. Neurol., 39, pp. 233-240; Watanabe, R., Wege, H., Ter Meulen, V., (1983) Nature, 305, pp. 150-152; Jouvenne, P., (1992) Virus Res., 22, pp. 125-141; Adami, C., (1995) Virology, 209, pp. 337-346; Parker, S., Gallagher, T., Buchmeier, M.J., (1989) Virology, 173, pp. 664-673; Banner, L.R., Lai, M.M., (1991) Virology, 185, pp. 441-445; Perlman, S., (1987) Microb. Pathog., 2, pp. 185-194; Perlman, S., (1990) Virology, 175, pp. 418-426; Pewe, L., (1996) Immunity, 5, pp. 253-262; Perlman, S., Reis, A., (1987) Microb. Pathog., 3, pp. 309-314; Merrill, J.E., (1993) J. Immunol., 151, pp. 2132-2141; Selmaj, K.W., Raine, C.S., (1988) Ann. Neurol., 23, pp. 339-346; Selmaj, K.W., (1991) J. Immunol., 147, pp. 1522-1529; Cross, A.H.M., (1993) J. Clin. Invest., 93, pp. 2684-2690; Boullerne, A.I., (1995) J. Neuroimmunol., 60, pp. 117-124; Stohlman, S.A., (1995) J. Virol., 69, pp. 5898-5903; Hayashi, M., (1995) J. Neuroimmunol., 60, pp. 143-150; Godiska, R., (1995) J. Neuroimmunol., 58, pp. 167-176","Lane, T.E.; Dept. of Neuropharmacology, Scripps Research Institute, 10666 N. Torrey Pines Rd., La Jolla, CA 92037, United States",,"Elsevier Ltd",0966842X,,TRMIE,"9025229","English","TRENDS MICROBIOL.",Review,"Final",Open Access,Scopus,2-s2.0-0031053499
"Kapil S., Basaraba R.J.","7003293348;6701555831;","Infectious bovine rhinotracheitis, parainfluenza-3, and respiratory coronavirus.",1997,"The Veterinary clinics of North America. Food animal practice","13","3",,"455","469",,33,"10.1016/S0749-0720(15)30308-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031262988&doi=10.1016%2fS0749-0720%2815%2930308-X&partnerID=40&md5=16dd201d83132dd01a81109b1cfb6bc7","Department of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, USA.","Kapil, S., Department of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, USA.; Basaraba, R.J., Department of Diagnostic Medicine and Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, USA.","A number of viruses have been proven to be primary respiratory pathogens of cattle. Viruses may play an important role in making cattle susceptible to secondary respiratory bacterial pathogens. Epidemiology, pathogenesis, laboratory diagnosis, and important properties in infectious bovine rhinotracheitis (IBR), parainfluenza-3 (PI-3), and bovine respiratory coronavirus (BRCV) are described in this article.",,"virus vaccine; animal; animal disease; cattle; cattle disease; Coronavirus; Herpes virus infection; immunology; Infectious bovine rhinotracheitis virus; Paramyxovirus; prevalence; respiratory tract infection; review; RNA virus infection; virology; virus infection; Animals; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Herpesviridae Infections; Herpesvirus 1, Bovine; Prevalence; Respiratory Tract Infections; Respirovirus; Respirovirus Infections; Viral Vaccines",,"Kapil, S.",,,07490720,,,"9368989","English","Vet. Clin. North Am. Food Anim. Pract.",Article,"Final",Open Access,Scopus,2-s2.0-0031262988
"Kyuwa S.","7006444820;","Replication of Murine Coronaviruses in Mouse Embryonic Stem Cell Lines in vitro",1997,"Experimental Animals","46","4",,"311","313",,19,"10.1538/expanim.46.311","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031254077&doi=10.1538%2fexpanim.46.311&partnerID=40&md5=107b6f55f0d03a7d355c50bd7c93d385","Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan","Kyuwa, S., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan","Replication of murine coronaviruses in eight mouse embryonic stem (ES) cell lines of several genetic backgrounds was examined. Both mouse hepatitis virus (MHV) type 2 and MHV, strain A59 replicated well with no or minimal cytopathic effect in all the ES cell lines tested. The results suggest the possibility that MHV-infected ES cells may disseminate MHV in mouse colonies due to embryo manipulation.","Embryonic stem cells; Mouse hepatitis virus; Viral replication","animal; article; cell line; disease transmission; embryo; genetic engineering; in vitro study; mouse; Murine hepatitis coronavirus; physiology; stem cell; virology; virus replication; Animals; Cell Line; Disease Transmission; Embryo; Genetic Engineering; Mice; Murine hepatitis virus; Stem Cells; Virus Replication","Bowen, G.S., Calisher, C.H., Winkler, W.G., Kraus, A.L., Fowler, E.H., German, R.H., Fraser, D.W., Hinman, A.R., (1975) Am. J. Epidemiol., 102, pp. 233-240; Casebolt, D.B., Qian, B., Stephensen, C.B., (1997) Lab. Anim. Sci., 47, pp. 6-10; Casebolt, D.B., Stephensen, C.B., (1992) J. Clin. Microbiol., 30, pp. 608-612; Collins, M.J., Parker, J.C., (1972) J. Natl. Cancer Inst., 49, pp. 1139-1143; Doetschman, T., Gregg, R.G., Maeda, N., Hooper, M.L., Melton, D.W., Thompson, S., Smithies, O., (1987) Nature, 330, pp. 576-578; Gossler, A., Doetschman, T., Korn, R., Serfling, E., Kemler, R., (1986) Proc. Natl. Acad. Sci. U.S.A., 83, pp. 9065-9069; Homberger, F.R., Smith, A.L., Barthold, S.W., (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Kunita, S., Terada, E., Goto, K., Kagiyama, N., (1992) Lab. Anim. Sci., 42, pp. 593-598; Kyuwa, S., Yamaguchi, K., Hayami, M., Hilgers, J., Fujiwara, K., (1988) J. Virol., 62, pp. 3506-3508; Ledermann, B., Bürki, K., (1991) Exp. Cell Res., 197, pp. 254-258; Li, E., Bestor, T.H., Jaenisch, R., (1992) Cell, 69, pp. 915-926; McMahon, A.P., Bradley, A., (1990) Cell, 62, pp. 1073-1085; Nagy, A., Rossant, J., Nagy, R., Abramow-Newerly, W., Roder, J.C., (1993) Proc. Natl. Acad. Sci. U.S.A., 90, pp. 8424-8428; Nicklas, W., Giese, M., Zawatzky, R., Kirchner, H., Eaton, P., (1988) Lab. Anim. Sci., 38, pp. 152-154; Nicklas, W., Kraft, V., Meyer, B., (1993) Lab. Anim. Sci., 43, pp. 296-300; Okumura, A., Machii, K., Azuma, S., Toyoda, Y., Kyuwa, S., (1996) J. Virol., 70, pp. 4146-4149; Robertson, E.J., (1987) Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, , IRL press, Oxford, UK; Smith, A.L., Bottomly, K., Winograd, D.F., (1987) J. Immunol., 128, pp. 480-485; Wood, S.A., Allen, N.D., Rossant, J., Auerbach, A., Nagy, A., (1993) Nature, 365, pp. 87-89; Yagi, T., Tokunaga, T., Furuta, Y., Nada, S., Yosida, M., Tsukada, T., Saga, Y., Aizawa, S., (1993) Anal. Biochem., 214, pp. 70-76; Yamada, Y.K., Yabe, M., Yamada, A., Taguchi, F., (1993) Lab. Anim. Sci., 43, pp. 285-290; Yamanishi, K., Dantas, J.R., Takahashi, M., Yamanouchi, T., Domae, K., Kawamata, J., Kurata, T., (1983) Biken J., 26, pp. 155-160","Kyuwa, S.; Department of Animal Pathology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan",,"International Press Editing Centre Incorporation",13411357,,JIDOA,"9353641","English","Exp. Anim.",Article,"Final",Open Access,Scopus,2-s2.0-0031254077
"Lamarre A., Talbot P.J.","7004646746;7102670281;","Characterization of phage-displayed recombinant anti-idiotypic antibody fragments against coronavirus-neutralizing monoclonal antibodies",1997,"Viral Immunology","10","4",,"175","182",,9,"10.1089/vim.1997.10.175","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031406872&doi=10.1089%2fvim.1997.10.175&partnerID=40&md5=0e71bca983607de68e2d987ba9fd70dd","Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Lamarre, A., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que., Canada, Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Murine coronaviruses provide useful animal models for human neurological disorders such as multiple sclerosis. In an effort to better understand the mechanisms involved in protection from coronavirus infection, we are studying the role of the idiotypic network in the modulation of viral infectivity. We have explored the feasibility of using single-chain antibodies displayed on phage surfaces for the isolation of recombinant anti-idiotypic antibodies (anti-Ids) with antigen-mimicking properties, which has proven to be difficult with conventional hybridoma approaches. A phage-display library containing more than 108 different antibody specificities was screened for the presence of anti-Ids by successive rounds of panning with three different in vitro neutralizing and in vivo protective antiviral monoclonal antibodies, After five rounds of panning, between 32% and 84% of all individual clones tested showed antibody-binding in an enzyme-linked immunosorbent assay (ELISA). Although several clones showed identical antibody sequences, a number of different clones were identified and further characterized. None of the selected clones induced the production of antiviral or neutralizing antibodies or conferred reproducible protection from viral challenge in BALB/c and C57BL/6 mice. These results demonstrate that anti-Ids can be isolated from a phage-display library, although high-affinity antigen-mimicking phages with antiviral protective capacities were apparently not represented in this library. This argues for the development of more diverse phage-display libraries.",,"antiidiotypic antibody; monoclonal antibody; neutralizing antibody; recombinant protein; virus antibody; antibody specificity; antigen binding; article; Coronavirus; enzyme linked immunosorbent assay; nonhuman; phage display; Animalia; Coronavirus; Murinae; RNA viruses","Anders, E.M., Kapaklis-Deliyannis, G.P., White, D.O., Induction of immune response to influenza virus with anti-idiotypic antibodies (1989) J. Virol., 63, pp. 2758-2767; Brack, C., Co, M.S., Slaoui, M., Gaulton, G.N., Smith, T., Fields, B.N., Mullins, J.I., Greene, M.I., Nucleic acid sequence of an internal image-bearing monoclonal anti-idiotype and its comparison to the sequence of the external antigen (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 6578-6582; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Daniel, C., Talbot, P.J., Protection from lethal coronavirus infection by affinity-purified spike glycoprotein of murine hepatitis virus, strain A59 (1990) Virology, 174, pp. 87-94; Daniel, C., Anderson, R., Buchmeier, M.J., Fleming, J.O., Spaan, W.J.M., Wege, H., Talbot, P.J., Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronaviras spike glycoprotein and evidence that it forms part of a complex tridimensional structure (1993) J. Virol., 67, pp. 1185-1194; De La Cruz, V.F., Lal, A.A., McCutchan, T.F., Immunogenicity and epitope mapping of foreign sequences via genetically engineered filamentous phage (1988) J. Biol. Chem., 263, pp. 4318-4322; Griffiths, A.D., Williams, S.C., Hartley, O., Tomlinson, I.M., Waterhouse, P., Crosby, W.L., Kontermann, R.E., Winter, G., Isolation of high affinity human antibodies directly from large synthetic repertoires (1994) EMBO J., 13, pp. 3245-3260; Grzych, J.M., Capron, M., Lambert, P.H., Dissous, C., Torres, S., Capron, A., An anti-idiotype vaccine against experimental schistosomiasis (1985) Nature, 316, pp. 74-76; Hoogenboom, H.R., Winter, G., By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro (1992) J. Mol. Biol., 227, pp. 381-388; Jerne, N.K., Towards a network theory of the immune system (1974) Ann. Immunol., 125 C, pp. 373-389; Kennedy, R.C., Eichberg, J.W., Lanford, R.E., Dreesman, G.R., Anti-idiotypic antibody vaccine for type B viral hepatitis in chimpanzees (1986) Science, 232, pp. 220-223; Lamarre, A., Lecomte, J., Talbot, P.J., Antiidiotypic vaccination against murine coronavirus infection (1991) J. Immunol., 147, pp. 4256-4262; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronaviras MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; McNamara, M.K., Ward, R.E., Kohler, H., Monoclonal idiotope vaccine against Streptococcus pneumoniae infection (1984) Science, 226, pp. 1325-1326; Nissim, A., Hoogenboom, H.R., Tomlinson, I.M., Flynn, G., Midgley, C., Lane, D., Winter, G., Antibody fragments from a 'single pot' phage display library as immunochemical reagents (1994) EMBO J., 13, pp. 692-698; Reagan, K.J., Wunner, W.H., Wiktor, T.J., Koprowski, H., Anti-idiotypic antibodies induce neutralizing antibodies to rabies virus glycoprotein (1983) J. Virol., 48, pp. 660-666; Sacks, D.L., Sher, A., Evidence that anti-idiotype induced immunity to experimental african trypanosomiasis is genetically restricted and requires recognition of combining site-related idiotopes (1983) J. Immunol., 131, pp. 1511-1515; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses (1990) Immunochemistry of Viruses. The Basis for Serodiagnosis and Vaccines, 2, pp. 359-379. , M.H.V. van Regenmortel, and A.R. Neurath (eds.): Elsevier Science Publishers B.V., Amsterdam; Stein, K.E., Söderström, T., Neonatal administration of idiotype or antiidiotype primers for protection against Escherichia coli K13 infection in mice (1984) J. Exp. Med., 160, pp. 1001-1011; Tomlinson, I.M., Walter, G., Marks, J.D., Llewelyn, M.B., Winter, G., The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops (1992) J. Mol. Biol., 227, pp. 776-798; Uytdehaag, F.G.C.M., Osterhaus, A.D.M.E., Induction of neutralizing antibody in mice against poliovirus type II with monoclonal anti-idiotypic antibody (1985) J. Immunol., 134, pp. 1225-1229; Wege, H., St Siddell, Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yu, M., Talbot, P.J., Induction of a protective immune response to murine coronavirus with non-internal image anti-idiotypic antibodies (1995) Corona- and Related Viruses. Current Concepts in Molecular Biology and Pathogenesis, pp. 165-172. , P.J. Talbot, and G.A. Levy (eds): Plenum Press, New York; Yu, M.W.N., Lemieux, S., Talbot, P.J., Genetic control of anti-idiotypic vaccination against coronavirus infection (1996) Eur. J. Immunol., 26, pp. 3230-3233; Zaghouani, H., Anderson, S.A., Sperber, K.E., Daian, C., Kennedy, R.C., Mayer, L., Bona, C.A., Induction of antibodies to the human immunodeficiency virus type 1 by immunization of baboons with immunoglobulin molecules carrying the principal neutralizing determinant of the envelope protein (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 631-635","Talbot, P.J.; Virology Research Center, Institut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada",,"Mary Ann Liebert Inc.",08828245,,VIIME,"9473148","English","Viral Immunol.",Article,"Final",,Scopus,2-s2.0-0031406872
"Mochizuki M., Mitsutake Y., Miyanohara Y., Higashihara T., Shimizu T., Hohdatsu T.","7403050664;18340926900;6507150145;57196694692;7408151653;57197786893;","Antigenic and Plaque Variations of Serotype II Feline Infectious Peritonitis Coronaviruses",1997,"Journal of Veterinary Medical Science","59","4",,"253","258",,11,"10.1292/jvms.59.253","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031110229&doi=10.1292%2fjvms.59.253&partnerID=40&md5=d8d100a5faffeeff24101567d3ac2fdc","Lab. of Veterinary Microbiology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Laboratory of Veterinary Pathology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Laboratory of Clinical Microbiology, Kyoritsu Shoji Co., Chiyoda-ku, Tokyo 102, Japan; Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitazato University, Towada, Aomori 034, Japan","Mochizuki, M., Lab. of Veterinary Microbiology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan, Laboratory of Clinical Microbiology, Kyoritsu Shoji Co., Chiyoda-ku, Tokyo 102, Japan; Mitsutake, Y., Laboratory of Veterinary Pathology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Miyanohara, Y., Laboratory of Veterinary Pathology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Higashihara, T., Lab. of Veterinary Microbiology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Shimizu, T., Laboratory of Veterinary Pathology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan; Hohdatsu, T., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitazato University, Towada, Aomori 034, Japan","Three feline coronavirus (FCoV) isolates KUK-H, M91-266, and M91-267 were examined to elucidate their biological and antigenic properties as well as disease potential in cats. Immune stainings of virus-infected cells by using FCoV type-specific monoclonal antibodies indicated that their antigenic specificity was serotype II. However, antigenic variations among these serotype II FCoVs were detected by neutralization assay with hyperimmune antisera against FCoVs and canine coronaviruses, and with experimentally infected cat sera; there were two subtypes in serotype II FCoVs. The isolates efficiently grew in fcwf-4 cell culture showing lytic CPE enough to form distinct plaques; when measured 48 hr after infection, plaque sizes of both M91-266 and M91-267 were approximately 1 mm in diameter, and a mixture of small (less than 1mm in diameter) and large (approximately 3 mm in diameter) plaques were produced in the case of KUK-H. Strains KUK-H, M91-266 and M91-267 produced feline infectious peritonitis (FIP) in 50%, 67% and 89% of experimentally inoculated kittens, respectively. Furthermore, 80% of the kittens inoculated with the small plaque former of KUK-H developed FIP accompanied by more prominent clinical signs as well as pathological changes when compared with 28.6% of kittens inoculated with the large plaque former. These results suggest that serotype II FIPVs producing smaller size of plaques are more virulent than those producing larger size of plaques.","Coronavirus; Feline; Feline infectious peritonitis; Plaque; Virulence","monoclonal antibody; virus antigen; animal; animal disease; antibody specificity; antigenic variation; article; cat; cat disease; classification; Coronavirus; cytopathogenic effect; growth, development and aging; hospitalization; immunology; incidence; kidney; liver; methodology; pathogenicity; pathology; serotyping; spleen; time; virology; virulence; virus culture; Animals; Antibodies, Monoclonal; Antibody Specificity; Antigenic Variation; Antigens, Viral; Cats; Coronavirus, Feline; Cytopathogenic Effect, Viral; Feline Infectious Peritonitis; Incidence; Kidney; Liver; Plaque Assay; Serotyping; Severity of Illness Index; Spleen; Time Factors; Virulence","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.D., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab. Anim. Sci., 34, pp. 592-597; Boyle, J.F., Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Black, J.W., Plaque assay, polypeptide composition and immunochemistry of feline infectious peritonitis virus and feline enteric coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 133-147; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J.D., Characterization of a temperature sensitive feline infectious peritonitis coronavirus (1989) Arch. Virol., 109, pp. 185-196; Evermann, J.F., Kckeirnan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Vet. Microbiol., 28, pp. 243-255; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hess, R.G., Bachmann, P.A., In vitro differentiation and pH sensitivity of field and cell culture-attenuated strains of transmissible gastroenteritis virus (1976) Infect. Immun., 13, pp. 1642-1646; Hirano, N., Ono, K., Goto, N., Establishment of persistently infected DBT cell cultures with mouse hepatitis virus strains, MHV-2 and MHV-3 (1984) Jpn. J. Vet. Sci., 46, pp. 757-760; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of type I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs): Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol., 28, pp. 13-24; Horzinek, M.C., Herrewegh, A., De Groot, R.J., Perspectives on feline coronavirus evolution (1995) Feline Pract., 23, pp. 34-39; Jacobse-Geels, H.E.L., Horzinek, M.C., Expression of feline infectious peritonitis coronavirus antigens on the surface of feline macrophage-like cells (1983) J. Gen. Virol., 64, pp. 1859-1866; Liou, P.P., In vitro differentiation of transmissible gastroenteritis virus strains by plaque sizes in swine testis cell culture (1983) J. Chinese Soc. Vet. Sci., 9, pp. 161-166; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; McKeirnan, A.J., Evermann, J.F., Davis, E.V., Ott, R.L., Comparative properties of feline coronaviruses in vitro (1987) Can. J. Vet. Res., 51, pp. 212-216; Mochizuki, M., Furukawa, H., An enzyme-linked immunosorbent assay using canine coronavirus-infected CRFK cells as antigen for detection of anti-coronavirus antibody in cat (1989) Comp. Immun. Microbiol. Infect. Dis., 12, pp. 139-146; Mochizuki, M., Sugiura, R., Akuzawa, M., Microneutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-20; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Compend. Contin. Educ. Pract. Vet., 7, pp. 1001-1011; Stoddart, C.A., Barlough, J.E., Baldwin, C.A., Scott, F.W., Attempted immunisation of cats against feline infectious peritonitis using canine coronavirus (1988) Res.Vet.Sci., 45, pp. 383-388; Stoddart, C.A., Scott, F.W., Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence (1989) J. Virol., 63, pp. 436-440; Takemoto, K.K., Plaque mutants of animal viruses (1966) Prog. Med. Virol., 8, pp. 314-348; Tuchiya, K., Horimoto, T., Azetaka, M., Takahashi, E., Konishi, S., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet. Microbiol., 26, pp. 41-51; Tupper, G.T., Evermann, J.F., Russell, R.G., Thouless, M.E., Antigenic and biological diversity of feline coronaviruses: Feline infectious peritonitis and feline enteritis virus (1987) Arch. Virol., 96, pp. 29-38; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766","Mochizuki, M.; Lab. of Veterinary Microbiology, Department of Veterinary Medicine, Kagoshima University, Kagoshima 890, Japan",,"Maruzen Co. Ltd.",09167250,,,"9152932","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0031110229
"Woo K., Joo M., Narayanan K., Kim K.H., Makinno S.","36792166400;23008647300;7101933409;7409323179;7403067550;","Murine coronavirus packaging signal confers packaging to nonviral RNA",1997,"Journal of Virology","71","1",,"824","827",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031060108&partnerID=40&md5=7d63dfc3b799e3cdbb2f5f372eef5e86","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Pathology, Harvard University, Boston, MA 02115, United States; Division of Biology, California Institute of Technology, Pasadena, CA 91125, United States","Woo, K., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Joo, M., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Pathology, Harvard University, Boston, MA 02115, United States; Narayanan, K., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Kim, K.H., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Division of Biology, California Institute of Technology, Pasadena, CA 91125, United States; Makinno, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States","Studies of defective interfering (DI) RNAs of the murine coronavirus mouse hepatitis virus (MHV) suggest that a 69-nucleotide-long packaging signal is necessary for MHV genomic RNA packaging into MHV particles. In this study we showed that when RNA transcripts that consisted of a non-MHV sequence and the packaging signal were expressed in MHV-infected cells, they were packaged into MHV particles. Those RNA transcripts that lacked the packaging signal or those containing a mutated packaging signal did not package efficiently. Thus, the presence of the packaging signal was sufficient for RNA packaging into MHV particles.",,"chloramphenicol acetyltransferase; dna fragment; virus rna; article; controlled study; defective virus; murine hepatitis coronavirus; nonhuman; packaging; priority journal; rna replication; virus particle; Animals; Cell Line; Murine hepatitis virus; Ribonuclease, Pancreatic; RNA; Signal Transduction; Virion; Virus Assembly","Adam, M.A., Miller, D., Identification of a signal in a murine retrovirus that is sufficient for packaging of nonretroviral RNA into virions (1988) J. Virol., 62, pp. 3802-3806; Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature (London), 308, pp. 751-752; Bos, E.C.W., Luytjes, W., Van der Meulen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. 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Virol., 70, pp. 5769-5776; Junker-Niepmann, M., Bartenschlager, R., Schallen, H., A short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA (1990) EMBO J., 9, pp. 3389-3396; Kim, K.H., Makino, S., Unpublished data; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: M RNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerasc (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Lin, V.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Luytjes, W., Krystal, M., Enami, M., Parvin, J.D., Palese, P., Amplification, expression, and packaging of a foreign gene by influenza virus (1989) Cell, 59, pp. 1107-1113; Macnaughton, M.R., Davies, H.A., Nermut, M.V., Ribonucleoprotein-like structures from coronavirus particles (1978) J. Gen. Virol., 39, pp. 545-549; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis; a regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J. Virol., 64, pp. 6045-6053; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Arch. Virol., 125, pp. 141-160; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis virus, strain A59 (1989) Virology, 171, pp. 141-148; Pattnaik, A.K., Ball, L.A., Legrone, A., Wertz, G., The termini of VSV DI particle RNAs are sufficient to signal RNA encapsidation, replication, and budding to generate infectious particles (1995) Virology, 206, pp. 760-764; Risen, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1939-1944; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interactions between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) CUIT. Top. Microbiol. Immunol., 99, pp. 165-200; Wei, N., Heaton, L.A., Morris, T.J., Harrison, S.C., Structure and assembly of turnip crinkle virus. VI. Identification of coat protein virus binding sites on the RNA (1990) J. Mol. Biol., 214, pp. 85-95; Weiss, B., Nitschko, H., Ghattas, I., Wright, R., Schlesinger, S., Evidence for specificity in the encapsidation of Sindbis virus RNAs (1989) J. Virol., 63, pp. 5310-5318; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zhao, X., Shaw, K., Cavanagh, D., Presence of subgenomic mRNAs in virions of coronavirus IBV (1993) Virology, 196, pp. 172-178; Zhong, W., Dasgupta, R., Rueckert, R., Evidence that the packaging signal for nodaviral RNA2 is a bulged stem-loop (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 11146-11150; Zimmern, D., The nucleotide sequence at the origin for assembly on tobacco mosaic virus RNA (1977) Cell, 11, pp. 455-462","Makino, S.; Department of Microbiology, University of Texas, Austin, TX 78712-1095, United States",,,0022538X,,JOVIA,"8985424","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031060108
"Senanayake S.D., Brian D.A.","7004008817;7006460232;","Bovine coronavirus I protein synthesis follows ribosomal scanning on the bicistronic N mRNA",1997,"Virus Research","48","1",,"101","105",,24,"10.1016/S0168-1702(96)01423-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031128258&doi=10.1016%2fS0168-1702%2896%2901423-2&partnerID=40&md5=987d14a3f84fc5f3c0f5a155fa59725e","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Senanayake, S.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","The mRNA encoding the 49-kDa nucleocapsid protein (N) of the bovine coronavirus is bicistronic. A 23-kDa protein, termed the I protein for the 'internal' open reading frame (ORF), is also synthesized but in the +1 reading frame beginning 61 nt downstream of the N start codon. Sequences flanking the N and I start codons suggest that the I ORF might be accessed by scanning ribosomes passing over the N start codon. Here we test this idea and demonstrate with translation studies both in vitro and in vivo that the I protein is synthesized according to the leaky scanning model for initiation of translation on the subgenomic N mRNA molecule.","Coronavirus bicistronic N mRNA; Nucleocapsid protein; Ribosoma scanning","messenger RNA; animal cell; controlled study; Coronavirus; nonhuman; open reading frame; priority journal; protein synthesis; ribosome; short survey; translation initiation; virus nucleocapsid; Animalia; Bovinae; Bovine coronavirus; Coronavirus","Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen. Virol., 74, pp. 1795-1804; Elroy-Stein, O., Moss, B., Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6743-6747; Jackson, R.L., Hunt, S.L., Reynolds, J.E., Kaminski, A., Cap-dependent and cap-independent translation: Operational distinctions and mechanistic interpretations (1995) Curr. Top. Microbiol. Immunol., 203, pp. 1-29; Hofmann, M.A., Senanayake, S.D., Brian, D.A., A translation-attenuating intraleader open reading frame is selected on coronavirus mRNAs during persistent infection (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 11733-11737; Homberger, F.R., Sequence analysis of the nucleoprotein genes of three enterotropic strains of murine coronavirus (1995) Arch. Virol., 140, pp. 571-579; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Kozak, M., Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes (1986) Cell, 44, pp. 283-292; Kozak, M., The scanning model for translation: An update (1989) J. Cell Biol., 108, pp. 229-241; Kunita, S., Mori, M., Terada, E., Sequence analysis of the nucleocapsid protein gene of rat coronavirus SDAV-681 (1993) Virology, 193, pp. 520-523; Lai, M.M.C., Stohlman, S.A., Comparative analysis of RNA genomes of mouse hepatitis viruses (1981) J. Virol., 38, pp. 661-670; Le, S.-Y., Sonenberg, N., Maizel, J., Distinct structural elements and internal entry of ribosomes in mRNA3 encoded by infectious bronchitis virus (1994) Virology, 198, pp. 405-411; Leibowitz, J.L., Perlman, S., Weinstock, G., Devries, J.R., Budzilowicz, C., Weissemann, J.M., Weiss, S.R., Detection of a murine coronavirus nonstructural protein encoded in a downstream open reading frame (1988) Virology, 164, pp. 156-164; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol., 66, pp. 6143-6154; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene in bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Skinner, M.A., Siddell, S.G., Coronavirus JHM: Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acids Res., 11, pp. 5045-5054; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5 (1994) J. Gen. Virol., 75, pp. 3041-3046; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrant: Protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,"Elsevier B.V.",01681702,,VIRED,"9140198","English","VIRUS RES.",Article,"Final",Open Access,Scopus,2-s2.0-0031128258
"Murray R.S., Cai G.-Y., Soike K.F., Cabirac G.F.","7403022204;57199040369;7006220553;6602498805;","Further observations on coronavirus infection of primate CNS",1997,"Journal of NeuroVirology","3","1",,"71","75",,7,"10.3109/13550289709015795","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031045133&doi=10.3109%2f13550289709015795&partnerID=40&md5=defa026e867b5b4742c314978293e898","Colorado Multiple Sclerosis Center, Englewood, CO 80110, United States; National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80262, United States; Tulane Regional Primate Research Center, Covington, LA 70433, United States; Rocky Mountain MS Center, Englewood, CO 80110, United States; Department of Biochemistry, Biophysics and Genetics, University of Colorado, Health Sciences Center, Denver, CO 80262, United States","Murray, R.S., Colorado Multiple Sclerosis Center, Englewood, CO 80110, United States, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80262, United States; Cai, G.-Y., Rocky Mountain MS Center, Englewood, CO 80110, United States; Soike, K.F., Tulane Regional Primate Research Center, Covington, LA 70433, United States; Cabirac, G.F., Rocky Mountain MS Center, Englewood, CO 80110, United States, Department of Biochemistry, Biophysics and Genetics, University of Colorado, Health Sciences Center, Denver, CO 80262, United States","Previously we demonstrated that intracerebral (IC) inoculation of a murine coronavirus, MHV-JHM, into two species of primates can result in acute encephalomyelitis. Infectious virus isolated from acutely infected animals, designated JHM-OMp1, was inoculated IC into a second group of monkeys. In this report we describe observations on the acutely infected animals and those surviving the acute infection that were sacrificed at later times post-infection. Results from dual in situ hybridization/immunohistochemistry screening of tissues show that astrocytes are target cells in white matter lesions during acute infection. In animals sacrificed 150 days post-infection, areas of demyelinated gliotic lesions, prominent in the spinal cord, were seen throughout the neuraxis. No virus products were detected in these late-infection lesions.","Astrocytes; Brain disease; Demyelinating disease; Virus disease","animal experiment; animal tissue; article; astrocyte; central nervous system infection; controlled study; Coronavirus; demyelinating disease; immunohistochemistry; in situ hybridization; nonhuman; primate; priority journal; spinal cord; virus infection; virus infectivity; white matter; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Primates","Burks, J.S., DeVald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Fleming, J.O., Wang, F.-I., Trousdale, M.D., Hinton, D.R., Stohlman, S.A., Interaction of immune and central nervous systems: Contribution of anti-viral Thy-1+ cells to demyelination induced by coronavirus JHM (1993) Regional Immunol, 5, pp. 37-43; Gerdes, J.C., Klein, I., DeVald, B.L., Burks, J.S., Coronavirus isolates SK and SD from multiple sclerosis patients are serologically related to murine coronaviruses A59 and JHM and human coronavirus OC43; but not to human coronavirus 229E (1981) J Virology, 38, pp. 231-238; Lampert, P.W., Sims, J.K., Kniazeff, A.J., Mechanism of demyelination in JHM virus encaphalomyelitis (1973) Acta Neuropathol, 24, pp. 76-85; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S., Persistence of mouse hepatitis virus A59 RNA in a slow virus demyelinating infection in mice as detected by in situ hybridization (1984) J Virol, 51, pp. 563-566; Lowe, J., Cox, G., (1990) Theory and Practice of Histological Techniques, 3rd Edtion, pp. 347-348. , Bancroft JD, Stevens A (eds). Churchill and Livingstone; Massa, P.T., Wege, H., Ter Meulen, V., Analysis of murine hepatitis virus (JHM strain) tropism toward Lewis rat glial cell in vitro. Type I astrocytes and brain macrophages (microglia) as primary cell targets (1986) Lab Invest, 55, pp. 318-327; Murray, R.S., Cai, G.-Y., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primates (1992) Virol, 188, pp. 274-284; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann Neurol, 31, pp. 525-533; Perlman, S., Ries, D., The astrocyte is a target cell in mice persistently infected with mouse hepatitis virus, strain JHM (1987) Microb Pathog, 3, pp. 309-314; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Sun, N., Grzybicki, D., Castro, R.F., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virol, 213, pp. 482-493; Vafai, A., Murray, R.S., Wellish, M., Devlin, M., Gilden, D.H., Expression of varicella-zoster and herpes simplex virus in normal human trigeminal ganglia (1988) Proc Natl Acad Sci USA, 85, p. 2362; Wang, F.-I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J Neuroimmunol, 30, pp. 31-41; Watanbe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch Neurol, 28, pp. 298-303; Weiss, S.R., Coronaviruses SD and SK share extensive nucleotide homology with murine coronavirus MHV-A59, more than that shared between human and murine coronavirus (1983) Virol, 126, pp. 669-677","Murray, R.S.; Colorado Multiple Sclerosis Center, Englewood, CO 80110, United States",,"Springer New York LLC",13550284,,JNVIF,"9147824","English","J. NEUROVIROL.",Article,"Final",,Scopus,2-s2.0-0031045133
"Ahn K., Chae C., Kweon C.-H.","21633313800;36523220500;6701508553;","Immunohistochemical Identification of Porcine Respiratory Coronavirus Antigen in the Lung of Conventional Pigs",1997,"Veterinary Pathology","34","2",,"167","169",,12,"10.1177/030098589703400213","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031092821&doi=10.1177%2f030098589703400213&partnerID=40&md5=8bcbd8fae731f9ee62913c0364301b90","Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon, Kyoung-Ki Do 441-744, South Korea","Ahn, K.; Chae, C., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon, Kyoung-Ki Do 441-744, South Korea; Kweon, C.-H.","Nine 3-week-old conventional pigs were inoculated intranasally with a Korean isolate of porcine respiratory coronavirus (PRCV). Three 3-week-old conventional pigs were kept as noninoculated controls. Three inoculated and one control pig were euthanatized at 5, 10, and 15 days postinoculation (DPI), respectively. All nine inoculated pigs developed respiratory disease. Interstitial pneumonia characterized by mononuclear inflammatory cell infiltration into alveolar septa were seen microscopically in all nine PRCV-infected pigs. Histopathologic changes were severe at 5 DPI, modest at 10 DPI, and almost resolved at 15 DPI. PRCV antigen was not detected in bronchial and bronchiolar epithelium but was detected in interstitial macrophages in the lungs. This Korean isolate of PRCV appeared to replicate primarily within alveolar macrophages in the respiratory system of the pig.","Pigs; Pneumonia; Porcine respiratory coronavirus; Respiratory virus","virus antigen; animal; animal disease; article; Coronavirus; immunohistochemistry; immunology; interstitial lung disease; pathology; swine; swine disease; virology; virus infection; Animals; Antigens, Viral; Coronavirus; Coronavirus Infections; Immunohistochemistry; Lung Diseases, Interstitial; Swine; Swine Diseases","Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res, 21, pp. 181-198; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res Vet Sci, 48, pp. 165-169; Haines, D.M., Chelack, B.J., Technical considerations for developing enzyme immunohistochemical staining procedures on formalin-fixed paraffin-embedded tissues for diagnostic pathology (1991) J Vet Diagn Invest, 3, pp. 101-112; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J Vet Diagn Invest, 5, pp. 184-188; Jabrane, A., Girard, C., Elazhary, Y., Pathogenicity of porcine respiratory coronavirus isolated in Quebec (1994) Can Vet J, 35, pp. 86-92; Lanza, I., Brown, I.H., Paton, D.J., Pathogenicity of concurrent infection of pigs with porcine respiratory coronavirus and swine influenza virus (1992) Res Vet Sci, 53, pp. 309-314; Laude, H., Reeth, K.V., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; O'Toole, D., Brown, I., Budges, A., Cartwright, S.P., Pathogenicity of experimental infection with ""pneumotropic"" porcine coronavirus (1989) Res Vet Sci, 47, pp. 23-29; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Van Nieuwstadt, A.P., Pol, J.M.A., Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pigs (1989) Vet Rec, 124, pp. 43-44; Vannier, P., Disorders induced by the experimental infection of pigs with the porcine respiratory coronavirus (P.R.C.V.) (1990) J Vet Med Ser B, 37, pp. 177-180; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J Clin Microbiol, 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317","Chae, C.; Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon, Kyoung-Ki Do 441-744, South Korea",,"American College of Veterinary Pathologists Inc.",03009858,,VTPHA,"9066087","English","Vet. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0031092821
"Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.","6506805240;6603135299;6602382869;7006652624;7003294168;","Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus",1997,"Journal of Virology","71","1",,"734","737",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031060291&partnerID=40&md5=bd617b9f15ccc106e86e9f5328afe1e0","U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France","Benbacer, L., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France; Kut, E., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France; Besnardeau, L., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France; Laude, H., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France; Delmas, B., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78850 Jouy-en-Josas, France","We report that cells refractory to canine coronavirus (CCV) and feline infectious peritonitis virus (FIPV) became susceptible when transfected with a chimeric aminopeptidase-N (APN) cDNA containing a canine domain between residues 643 and 841. This finding shows that APN recognition by these viruses is species related and associated with this C-terminal domain. The human/canine APN chimera was also able to confer susceptibility to the porcine transmissible gastroenteritis virus (TGEV), whereas its human/porcine homolog failed to confer susceptibility to CCV and FIPV. A good correlation was observed between the capacity of CCV, FIPV, and TGEV to recognize the different interspecies APN chimeras and their ability to infect cells derived from the relevant species. As an exception, TGEV was found to use a human/bovine APN chimera as a receptor although itself unable to replicate in bovine cells.",,"chimeric protein; complementary dna; microsomal aminopeptidase; virus receptor; animal cell; article; carboxy terminal sequence; cell line; controlled study; coronavirus; dna library; dna transfection; flow cytometry; infection sensitivity; molecular interaction; nonhuman; polymerase chain reaction; priority journal; protein domain; protein expression; species difference; virus replication; Amino Acid Sequence; Aminopeptidases; Animals; Base Sequence; Cats; Cattle; Cell Line; Coronavirus, Canine; Coronavirus, Feline; Cricetinae; DNA, Complementary; Dogs; Humans; Molecular Sequence Data; Receptors, Virus; Recombinant Fusion Proteins; Species Specificity; Transmissible gastroenteritis virus; Virus Replication","Barlough, J.E., Jacobsen, R.H., Scott, F.W., Microtiter assay for coronavirus neutralizing activity in cats using a canine continuous cell line (A-72) (1983) Lab. Anim. Sci., 33, pp. 567-570; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L., Sjöström, H., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-419; Delmas, B., Gelfi, J., Sjöström, H., Norén, O., Laude, H., Further characterization of aminopeptidase N as a receptor for coronaviruses (1993) Adv. Exp. Med. Biol., 342, pp. 292-298; Delmas, B., Gelfi, J., Kut, E., Sjöström, H., Norén, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) J. Virol., 68, pp. 5216-5224; Duarte, M., Gelfi, J., Lambert, P., Rasschaert, D., Laude, H., Genome organization of porcine epidemic diarrhoea virus (1993) Adv. Exp. Med. Biol., 342, pp. 55-60; Holmes, K.V., Compton, S.R., Coronavirus receptors (1995) The Coronaviridae, pp. 55-71. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Hooper, N.M., Families of zinc metalloproteases (1994) FEBS Lett., 354, pp. 1-6; Laude, H., Chapsal, J.-M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Louvard, D., Apical membrane aminopeptidase appears at site of cell-cell contact in cultured kidney epithelial cells (1980) Proc. Natl. Acad. Sci. USA, 77, pp. 4132-4136; Olsen, J., Cowell, G., Konigshofer, E., Danielsen, E.M., Moller Laustsen, J., Hansen, L.O.C., Welinder, K., Norén, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Lett., 238, pp. 307-314; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Shipp, M.A., Look, A.T., Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key! (1993) Blood, 82, pp. 1052-1070; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44; Welter, C.J., TGE of swine. I. Propagation of virus in cell cultures and development of a vaccine (1965) Vet. Med. Small Anim. Clin., 60, pp. 1054-1058; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature (London), 337, pp. 420-422","Delmas, B.; UVIM, Inst. Natl. de Recherche Agronomique, 78850 Jouy-en-Josas, France",,,0022538X,,JOVIA,"8985407","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031060291
"Heusipp G., Grötzinger C., Herold J., Siddell S.G., Ziebuhr J.","6603559110;6602152610;7006838690;7005260816;7003783935;","Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells",1997,"Journal of General Virology","78","11",,"2789","2794",,25,"10.1099/0022-1317-78-11-2789","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842370236&doi=10.1099%2f0022-1317-78-11-2789&partnerID=40&md5=dd75d4090cd656b9c1c3c06798ec8e73","Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Inst. of Molec. Biol. and Biochem., Arnimallee 22, 14195 Berlin, Germany","Heusipp, G., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Grötzinger, C., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany, Inst. of Molec. Biol. and Biochem., Arnimallee 22, 14195 Berlin, Germany; Herold, J., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","The translation products of the human coronavirus (HCV) 229E open reading frames 1a and 1b, the polyproteins 1a and 1ab, are processed by virus-encoded proteinases. One of the key enzymes in this process is a chymotrypsin-like enzyme, the 3C-like proteinase. In this study we have identified an ORF 1b-encoded, 41 kDa processing product in HCV 229E-infected cells by using a monoclonal antibody with defined specificity. We show that this polypeptide is released from polyprotein 1ab by 3C-like proteinase-mediated cleavage of the peptide bonds Gln-6110/Gly-6111 and Gln-6458/Ser-6459. Also, we have investigated the subcellular localization of the 41 kDa processing product. Immunofluorescence microscopy revealed a punctate, perinuclear distribution of the 41 kDa polypeptide in infected cells and an identical subcellular localization was observed for three additional pp1ab-derived polypeptides. In contrast, the virus nucleocapsid protein showed a homogeneous cytoplasmic localization.",,"chymotrypsin; monoclonal antibody; proteinase; virus enzyme; virus protein; article; cellular distribution; chemical bond; Coronavirus; cytoplasm; human; human cell; immunofluorescence microscopy; nonhuman; open reading frame; priority journal; protein processing; virus nucleocapsid; Coronavirus; Hepatitis C virus; human coronavirus; Human coronavirus 229E","Barco, A., Carrasco, L., A human virus protein, human poliovirus protein 2BC, induces membrane proliferation and blocks the exocytic pathway in the yeast Saccharomyces cerevisiae (1995) EMBO Journal, 14, pp. 3349-3364; Bienz, K., Egger, D., Troxler, M., Pasamontes, L., Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region (1990) Journal of Virology, 64, pp. 1156-1163; Bienz, K., Egger, D., Pfister, T., Troxler, M., Structural and functional characterization of the poliovirus replication complex (1992) Journal of Virology, 66, pp. 2740-2747; Chambers, T.J., Hahn, C.S., Galler, R., Rice, C.M., Flavivirus genome organization, expression, and replication (1990) Annual Review of Microbiology, 44, pp. 649-688; Dubois-Dalq, M., Holmes, K.V., Rentier, B., Assembly of Coronaviridae (1984) Assembly of Enveloped RNA Viruses, pp. 100-119. , Wien: Springer-Verlag; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes (1988) Journal of Cell Biology, 107, pp. 2075-2086; Gorbalenya, A.E., Snijder, E.J., Viral cysteine proteinases (1996) Perspectives in Drug Discovery and Design, 6, pp. 64-86; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Research, 17, pp. 4847-4861; Grötzinger, C., (1996) Expression des RNA-Polymeraselocus des Humanen Coronavirus 229E, , PhD thesis, Humboldt University, Berlin; Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Süss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Research, 21, pp. 5838-5842; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kDa polypeptide encoded in gene 1 of the human coronavirus 229E (1997) Journal of Virology, , in press; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein : Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) Journal of Virology, 71, pp. 1814-1820; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) Journal of Virology, 69, pp. 3554-3559; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 222, pp. 375-382; Seybert, A., Ziebuhr, J., Siddell, S.G., Expression and characterization of a recombinant murine coronavirus 3C-like proteinase (1997) Journal of General Virology, 78, pp. 71-75; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) Journal of Virology, 70, pp. 1923-1930; Van Dinten, L.C., Wassenaar, A.L.M., Gorbalenya, A.E., Spaan, W.J.M., Snijder, E.J., Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) Journal of Virology, 70, pp. 6625-6633; Ziebuhr, J., (1995) Expression der 3C-like-Proteinase des Humanen Coronavirus HCV 229E, , PhD thesis, University of Würzburg, Germany; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) Journal of Virology, 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) Journal of Virology, 71, pp. 3992-3997","Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,"Microbiology Society",00221317,,JGVIA,"9367364","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-1842370236
"Barac-Latas V., Suchanek G., Breitschopf H., Stuehler A., Wege H., Lassmann H.","6506163291;6603076780;6602583169;6504795553;7005516649;35420677900;","Patterns of oligodendrocyte pathology in coronavirus-induced subacute demyelinating encephalomyelitis in the Lewis rat",1997,"GLIA","19","1",,"1","12",,44,"10.1002/(SICI)1098-1136(199701)19:1<1::AID-GLIA1>3.0.CO;2-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031032151&doi=10.1002%2f%28SICI%291098-1136%28199701%2919%3a1%3c1%3a%3aAID-GLIA1%3e3.0.CO%3b2-5&partnerID=40&md5=cb638c47f5ec657d838e0ba9c15f0088","Dept. of Physiology and Immunology, University of Rijeka, C-51000 Rijeka, Croatia; Austrian Academy of Sciences, A-1010 Vienna, Austria; Clinical Institute of Neurology, University of Vienna, A-1090 Vienna, Austria; Institute of Virology and Immunology, University of Wuerzburg, D-97078 Wuerzburg, Germany; Institute of Diagnostic Virology, Fed. Res. Ctr. Virus Dis. of Animals, Friedrich-Loeffler-Institutes, D-17498 Insel Riems, Germany; Clinical Institute of Neurology, University of Vienna, Schwarzpanierstrasse 17, A-1090 Vienna, Austria","Barac-Latas, V., Dept. of Physiology and Immunology, University of Rijeka, C-51000 Rijeka, Croatia; Suchanek, G., Austrian Academy of Sciences, A-1010 Vienna, Austria; Breitschopf, H., Clinical Institute of Neurology, University of Vienna, A-1090 Vienna, Austria; Stuehler, A., Institute of Virology and Immunology, University of Wuerzburg, D-97078 Wuerzburg, Germany; Wege, H., Institute of Diagnostic Virology, Fed. Res. Ctr. Virus Dis. of Animals, Friedrich-Loeffler-Institutes, D-17498 Insel Riems, Germany; Lassmann, H., Clinical Institute of Neurology, University of Vienna, A-1090 Vienna, Austria, Clinical Institute of Neurology, University of Vienna, Schwarzpanierstrasse 17, A-1090 Vienna, Austria","Intracerebral infection of rats with JHM coronavirus induces a chronic inflammatory demyelinating disease, which in many respects mimicks the pathology of multiple sclerosis. We investigated the patterns of demyelination and oligodendrocyte pathology in this model. In early stages of the disease infection of oligodendrocytes was associated with a downregulation of expression of mRNA for proteolipid protein in the absence of myelin destruction. When demyelinating lesions were formed infected oligodendrocytes were destroyed by necrosis, whereas oligodendrocytes that did not contain detectable virus antigen or RNA were in part dying by apoptosis. At this stage of the disease remyelination of the lesions was pronounced. At later stages after infection virus antigen was nearly completely cleared from the lesions. In spite of the lack of detectable virus, ongoing demyelination and unspecific tissue destruction occurred, and oligodendrocytes were mainly destroyed by apoptosis. These late lesions revealed only minimal central remyelination, but they were frequently repaired by Schwann cells. Our studies suggest that the mechanisms of myelin destruction in this model of virus-induced demyelination are complex and that the patterns of tissue damage may change during the course of the disease.","apoptosis; demyelination; necrosis; remyelination","biological marker; DNA fragment; messenger RNA; proteolipid protein; virus antigen; animal; apoptosis; article; cell differentiation; cell nucleus; chemistry; demyelinating disease; genetics; germfree animal; immunohistochemistry; immunology; in situ hybridization; Lewis rat; mouse; Murine hepatitis coronavirus; oligodendroglia; pathology; physiology; rat; RNA probe; time; virology; virus encephalitis; virus infection; Animals; Antigens, Viral; Apoptosis; Biological Markers; Cell Differentiation; Cell Nucleus; Coronavirus Infections; Demyelinating Diseases; DNA Fragmentation; Encephalitis, Viral; Immunohistochemistry; In Situ Hybridization; Mice; Murine hepatitis virus; Myelin Proteolipid Protein; Oligodendroglia; Rats; Rats, Inbred Lew; RNA Probes; RNA, Messenger; Specific Pathogen-Free Organisms; Time Factors","Barac-Latas, V., Wege, H., Lassmann, H., Apoptosis of T lymphocytes in coronavirus-induced encephalomyelitis (1995) Reg. 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Invest., 54, pp. 515-522; Schwender, S., Imrich, H., Doerries, R., The pathogenic role of virus specific antibody-secreting cells in the central nervous system of rats with different susceptibility to coronavirus-induced demyelinating encephalitis (1991) Immunology, 74, pp. 533-538; Selmaj, K.W., Raine, C.S., Tumor necrosis factor mediates myelin and oligodendrocyte damage in vitro (1988) Ann. Neurol., 23, pp. 339-346; Selmaj, K., Raine, C.S., Farooq, M., Norton, W.T., Brosnan, C.F., Cytokine cytotoxicity against oligodendrocytes. Apoptosis induced by lymphotoxin (1991) J. Immunol., 147, pp. 1522-1529; Sorensen, O., Perry, D., Dales, S., In vivo and in vitro models of demyelinating diseases. III. JHM virus infection of rats (1980) Arch. Neurol., 37, pp. 478-484; Stohlman, S.A., Bergmann, C.C., Van Der Veen, R.C., Hinton, D.R., Mouse hepatitis virus-specific cytotoxic T lymphocytes protect from lethal infection without eliminating virus from the central nervous system (1995) J. Virol., 69, pp. 684-694; Stoner, G.L., Brosnan, C.F., Wisniewski, H.M., Bloom, B.R., Studies on demyelination by activated lymphocytes in the rabbit eye. I. Effects of a mononuclear cell infiltrate influenced by products of activated lymphocytes (1977) J. Immunol., 118, pp. 2094-2102; Subak-Sharpe, I., Dyson, H., Fazakerly, J., In vivo depletion of CDS+ T cells prevents lesions of demyelination in Semliki Forest virus infection (1993) J. Virol., 67, pp. 7629-7633; Vass, K., Lassmann, H., Wekerle, H., Wisniewski, H.M., The distribution of Ia-antigen in the lesions of rat acute experimental allergic encephalomyelitis (1986) Acta Neuropathol. (Berl.), 70, pp. 149-160; Vass, K., Berger, M.L., Nowak, T.S., Welch, W.J., Lassmann, H., Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat (1989) Neurosci. Lett., 100, pp. 259-264; Wang, F.I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wege, H., Watanabe, R., Ter Meulen, V., Relapsing subacute demyelinating encephalomyelitis in rats in the course of coronavirus JHM infection (1984) J. Neuroimmunol., 6, pp. 325-336; Wege, H., Schliephake, A., Koerner, H., Flory, E., Wege, H., An immunodominant CD4+ T cell site on the nucleocapsid protein of murine coronavirus contributes to protection against encephalomyelitis (1993) J. Gen. Virol., 74, pp. 1287-1294; Winter, J., (1992) Coronavirus-Persistenz in Hirnzellen-Untersuchungen zur Pathogenese von Entmarkungsenzephalomyelitiden, , Doctoral thesis, University of Wuerzburg; Wisniewski, H.M., Bloom, B.R., Primary demyelination as a nonspecific consequence of a cell mediated immune reaction (1975) J. Exp. Med., 141, pp. 346-359; Yamada, M., Zurbriggen, A., Fujinami, R.S., The relationship between viral RNA, myelin-specific mRNA's, and demyelination in central nervous system disease during Theiler's virus infection (1990) Am. J. Pathol., 137, pp. 1467-1479; Zimprich, F., Winter, H., Wege, H., Lassmann, H., Coronavirus induced primary demyelination: Indications for the involvement of a humoral immune response (1991) Neuropathol. Appl. Neurobiol., 17, pp. 469-484","Lassmann, H.; Clinical Institute of Neurology, University of Vienna, Schwarzpanierstrasse 17, A-1090 Vienna, Austria",,,08941491,,GLIAE,"8989563","English","GLIA",Article,"Final",Open Access,Scopus,2-s2.0-0031032151
"Riffault S., Grosclaude J., Vayssier M., Laude H., Charley B.","6603556292;7004095202;57215995078;7006652624;55246691600;","Reconstituted coronavirus TGEV virosomes lose the virus ability to induce porcine interferon-alpha production",1997,"Veterinary Research","28","1",,"77","86",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030639436&partnerID=40&md5=07936557add656a31dc0f22791548447","Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France","Riffault, S., Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France; Grosclaude, J., Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France; Vayssier, M., Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France; Laude, H., Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France; Charley, B., Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France","The transmissible gastroenteritis virus (TGEV) is a coronavirus which induces a strong interferon-alpha (IFN-α) production in vivo and in vitro. Previous studies have shown that the TGEV external protein M plays a major role in IFN-α induction by a non-infectious virus, whereas protein S is not involved. The present study extended these results by showing that monoclonal antibodies (MAbs) directed at the external viral protein sM could not block IFN-α induction, which argues against a direct role for this protein. In the same type of blocking experiment, MAbs to the TGEV receptor aminopeptidase N did not inhibit IFN-α induction, which strongly indicates that viral replication or entry through the receptor is not needed for TGEV induction of IFN-α in leukocytes. In an attempt to isolate functional envelope proteins, TGEV virions were detergent-solubilized and reconstituted in virosomes. Although BIAcore antigenic analysis revealed that the three external viral proteins were present on the virosomes, these proteins were unable to induce IFN-α in porcine leukocytes, and seemed to compete with the native virus for IFN-α induction. These data indicated that IFN-α inducing interactions between TGEV external proteins and leukocytes required a complex native envelope protein structure which has been lost in the virosomes.","BIAcore; Coronavirus; Interferon-alpha; Transmissible gastroenteritis virus; Virosome","Coronavirus; Suidae; Transmissible gastroenteritis virus; alpha interferon; microsphere; monoclonal antibody; virus antibody; virus antigen; virus envelope protein; virus receptor; animal; article; biosynthesis; enzyme linked immunosorbent assay; immunology; mononuclear cell; mouse; swine; Transmissible gastroenteritis virus; virion; virology; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Enzyme-Linked Immunosorbent Assay; Interferon-alpha; Leukocytes, Mononuclear; Mice; Microspheres; Receptors, Virus; Swine; Transmissible gastroenteritis virus; Viral Envelope Proteins; Virion","Ankel, H., Capobianchi, M.R., Castilletti, C., Dianzani, F., Interferon induction by HIV glycoprotein 120: Role of the V3 loop (1994) Virology, 205, pp. 34-43; Ankel, H., Capobianchi, M.R., Frezza, F., Castilletti, C., Dianzani, F., A possible role of sulfatide- Related glycolipids in mterferon induction by HIV- 1 glycoprotein 120 (1995) J Interferon Cytokine Res, 15, pp. S61; Artursson, K., (1993) Studies on the Interferon-α/β System of Pigs, , PhD thesis in veterinary microbiology. Swedish University of Agricultural Sciences, Uppsala, Sweden; Baudoux, P., (1996) Étude de la Glycoprotéine M de Coronavirus : Rôle dans L'induction D'interféron Alpha et le Bourgeonnement des Particules Virales, , PhD thesis, Institut national de la recherche agronomique, Paris-Grignon, France; Bron, R., Ortiz, A., Dijkstra, J., Stegmann, T., Wilschut, J., Preparation, properties, and applications of reconstituted influenza virus envelopes (virosomes) (1993) Methods Enzymol, 220, pp. 313-331; Capobianchi, M.R., Ankel, H., Ameglio, F., Paganelli, R., Pizzoli, P., Dianzani, F., Recombinant glycoprotein 120 of human immunodeficiency virus is a potent interferon inducer (1992) AIDS Res Hum Retroviruses, 8, pp. 575-579; Charley, B., Laude, H., Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of a transmembrane glycoprotein E1 (1988) J Virol, 62, pp. 8-11; Charley, B., Nowacki, W., Vaiman, M., Frequency of interferon-alpha-secreting blood leukocytes in irradiated and bone-marrow grafted pigs (1995) Vet Res, 26, pp. 292-299; De Arce, H.D., Artursson, K., L'Haridon, R., Perers, A., La Bonnardière, C., Alm, G.V., A sensitive immunoassay for porcine interferon-α (1992) Vet Immunol Immunopathol, 30, pp. 319-327; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-419; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein (1986) J Gen Virol, 67, pp. 1405-1418; Fitzgerald-Bocarsly, P., Human natural interferon-α producing cells (1993) Pharmac Ther, 60, pp. 39-62; Godet, M., L'Haridon, R., Vautherot, J.-F., Laude, H., TGEV coronavinis ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Harmsen, M.C., Wilschut, J., Scherphof, G., Hulstaert, C., Hoekstra, D., Reconstitution and fusogenic properties of sendai virus envelopes (1985) Eur J Biochem, 149, pp. 591-599; Horigome, T., Sugano, H., A rapid method for removal of detergents from protein solution (1983) Anal Biochem, 130, pp. 393-396; Ito, Y., Bando, H., Komada, H., Tsurudome, M., Nishio, M., Kawano, M., Matsumura, H., Watanabe, N., HN proteins of human parainfluenza type 4A virus expressed in cell lines transfected with a cloned cDNA have an ability to induce interferon in mouse spleen cells (1994) J Gen Virol, 75, pp. 567-572; Ito, Y., Nishiyama, Y., Shimokata, K., Takeyarna, H., Kunii, A., Active component of HVJ (Sendai virus) for interferon induction in mice (1978) Nature, 274, pp. 801-802; Johnsson, B., Löfas, S., Immobilization of proteins to a carboxymethyldextran modified gold surface for biospecific interaction analysis in surface plasmon resonance (1991) Anal Biochem, 198, pp. 268-277; La Bonnardière, C., Laude, H., High Interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infect Immunol, 32, pp. 28-31; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion protein (1986) J Gen Virol, 67, pp. 119-130; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the corona- Virus transmissible gastroenteritis virus (1992) J Virol, 66, pp. 743-749; Lebon, P., Inhibition of herpes simplex virus type 1-induced interferon synthesis by monoclonal antibodies against viral glycoprotein D and by lysosomotropic drugs (1985) J Gen Virol, 66, pp. 2781-2786; Lebon, P., Commoy-Chevalier, M.J., Robert-Galliot, B., Chany, C., Different mechanisms for α and β interferon induction (1982) Virology, 119, pp. 504-507; Metsikkö, K., Van Meer, G., Simons, K., Reconstitution of the fusogenic activity of vesicular stomatitis virus (1986) EMBO J, 5, pp. 3429-3435; Nowacki, W., Charley, B., Enrichment of coronavirus-Induced interferon-producing blood leukocytes increases the interferon yield per cell: A study with pig leukocytes (1993) Res Immunol, 144, pp. 111-120; Nussbaum, O., Lapidot, M., Loyter, A., Reconstitution of functional influenza virus envelopes and fusion with membranes and liposomes lacking virus receptors (1987) J Virol, 61, pp. 2245-2252; Opsteken, D.I.E., Raamsman, M.J.B., Wolfs, K., Horzinek, M.C., Rottier, P.J.M., Envelope glycoprotein interactions in coronavirus assembly (1995) J Cell Biol, 131, pp. 339-349; Scheule, R.K., Novel preparation of functional sindbis virosomes (1986) Biochemistry, 25, pp. 4223-4232; Splichal, I., Bonneau, M., Charley, B., Ontogeny of interferon-alpha secreting cells in the porcine fetal hematopoietic organs (1994) Immunol Lett, 43, pp. 203-208; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opsteiten, D.I.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J, 15, pp. 2020-2028","Riffault, S.; Virologie/Immunol. Molec., Inra, 78350 Jouy-en-Josas, France; email: riffault@biotec.jouy.inra.fr",,"EDP Sciences",09284249,,VEREE,"9172843","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0030639436
"Riffault S., Grosclaude J., Vayssier M., Laude H., Charley B.","6603556292;7004095202;57215995078;7006652624;55246691600;","Reconstituted coronavirus TGEV virosomes lose the virus ability to induce porcine interferon-alpha production",1997,"Veterinary Research","28","2",,"105","114",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030631961&partnerID=40&md5=1829d2b18c2ce900491663c3810c92f7","Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France","Riffault, S., Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France; Grosclaude, J., Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France; Vayssier, M., Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France; Laude, H., Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France; Charley, B., Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France","Summary -The transmissible gastroenteritis virus (TGEV) is a coronavirus which induces a strong interferon-alpha (IFN-α) production in vivo and in vitro. Previous studies have shown that the TGEV external protein M plays a major role in IFN-α induction by a non-infectious virus, whereas protein S is not involved. The present study extended these results by showing that monoclonal antibodies (MAbs) directed at the external viral protein sM could not block IFN-α induction, which argues against a direct role for this protein. In the same type of blocking experiment, MAbs to the TGEV receptor aminopeptidase N did not inhibit IFN-α induction, which strongly indicates that viral replication or entry through the receptor is not needed for TGEV induction of IFN-α in leukocytes. In an attempt to isolate functional envelope proteins, TGEV virions were detergent-solubilized and reconstituted in virosomes. Although BIAcore antigenic analysis revealed that the three external viral proteins were present on the virosomes, these proteins were unable to induce IFN-α in porcine leukocytes, and seemed to compete with the native virus for IFN-α induction. These data indicated that IFN-α inducing interactions between TGEV external proteins and leukocytes required a complex native envelope protein structure which has been lost in the virosomes.","BIAcore; Coronavirus; Interferon-alpha; Transmissible gastroenteritis virus; Virosome","Coronavirus; Suidae; Transmissible gastroenteritis virus; alpha interferon; monoclonal antibody; virus protein; virus receptor; animal; antibody specificity; article; biosynthesis; enzyme linked immunosorbent assay; immunology; lymphocyte; physiology; swine; Transmissible gastroenteritis virus; virology; Animals; Antibodies, Monoclonal; Antibody Specificity; Enzyme-Linked Immunosorbent Assay; Interferon-alpha; Lymphocytes; Receptors, Virus; Swine; Transmissible gastroenteritis virus; Viral Proteins","Ankel, H., Capobianchi, M.R., Castilletti, C., Dianzani, F., Interferon induction by HIV glycoprotein 120: Role of the V3 loop (1994) Virology, 205, pp. 34-43; Ankel, H., Capobianchi, M.R., Frezza, F., Castilletti, C., Dianzani, F., A possible role of sulfatide-related glycolipids in interferon induction by HIV-1 glycoprotein 120 (1995) J Interferon Cytokine Res, 15, pp. S61; Artursson, K., (1993) Studies on the Interferon-α/β System of Pigs, , PhD thesis in veterinary microbiology, Swedish University of Agricultural Sciences, Uppsala, Sweden; Baudoux, P., (1996) Étude de La Glycoprotéine m de Corona Virus : Rôle Dans L'induction D'interféron Alpha et le Bourgeonnement Des Particules Virales, , PhD thesis. Institut national de la recherche agronomique, Paris-Grignon, France; Bron, R., Ortiz, A., Dijkstra, J., Stegmann, T., Wilschut, J., Preparation, properties, and applications of reconstituted influenza virus envelopes (virosomes) (1993) Methods Enzymol, 220, pp. 313-331; Capobianchi, M.R., Ankel, H., Ameglio, F., Paganelli, R., Pizzoli, P., Dianzani, F., Recombinant glycoprotein 120 of human immunodeficiency virus is a potent interferon inducer (1992) AIDS Res Hum Retroviruses, 8, pp. 575-579; Charley, B., Laude, H., Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of a transmembrane glycoprotein E1 (1988) J Virol, 62, pp. 8-11; Charley, B., Nowacki, W., Vaiman, M., Frequency of interferon-alpha-secreting blood leukocytes in irradiated and bone-marrow grafted pigs (1995) Vet Res, 26, pp. 292-299; De Arce, H.D., Artursson, K., L'Haridon, R., Perers, A., La Bonnardière, C., Alm, G.V., A sensitive immunoassay for porcine interferon-α (1992) Vet Immunol Immunopathol, 30, pp. 319-327; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-419; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. 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Properties of monoclonal antibodies directed against virion protein (1986) J Gen Virol, 67, pp. 119-130; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus (1992) J Virol, 66, pp. 743-749; Lebon, P., Inhibition of herpes simplex virus type 1-induced interferon synthesis by monoclonal antibodies against viral glycoprotein D and by lysosomotropic drugs (1985) J Gen Virol, 66, pp. 2781-2786; Lebon, P., Commoy-Chevalier, M.J., Robert-Galliot, B., Chany, C., Different mechanisms for α and β interferon induction (1982) Virology, 119, pp. 504-507; Metsikkö, K., Van Meer, G., Simons, K., Reconstitution of the fusogenic activity of vesicular stomatitis virus (1986) EMBO J, 5, pp. 3429-3435; Nowacki, W., Charley, B., Enrichment of coronavirus-induced interferon-producing blood leukocytes increases the Interferon yield per cell: A study with pig leukocytes (1993) Res Immunol, 144, pp. 111-120; Nussbaum, O., Lapidot, M., Loyter, A., Reconstitution of functional influenza virus envelopes and fusion with membranes and liposomes lacking virus receptors (1987) J Virol, 61, pp. 2245-2252; Opstelten, D.J.E., Raamsman, M.J.B., Wolfs, K., Horzinek, M.C., Rottier, P.J.M., Envelope glycoprotein interactions in coronavirus assembly (1995) J Cell Biol, 131, pp. 339-349; Scheule, R.K., Novel preparation of functional sindbis virosomes (1986) Biochemistry, 25, pp. 4223-4232; Splichal, I., Bonneau, M., Charley, B., Ontogeny of interferon-alpha secreting cells in the porcine fetal hematopoietic organs (1994) Immunol Lett, 43, pp. 203-208; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J, 15, pp. 2020-2028","Riffault, S.; Virologie et Immunol. Moléc., Inra, 78350 Jouy-en-Josas, France; email: riffault@biotec.jouy.inra.fr",,"EDP Sciences",09284249,,VEREE,"9112732","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0030631961
"Milane G., Kourtesis A.B., Dea S.","6508002405;6507567386;7006056287;","Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates",1997,"Journal of Clinical Microbiology","35","1",,"33","40",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031060047&partnerID=40&md5=8eb1a8ee17477d4d9095d4fb71c3c8d2","Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, Que. H7N 4Z3, Canada; Centre de Recherche en Virologie, Institut Armand Frappier, Université du Québec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Milane, G., Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, Que. H7N 4Z3, Canada; Kourtesis, A.B., Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, Que. H7N 4Z3, Canada; Dea, S., Centre de Recherche en Virologie, Institut Armand Frappier, Université du Québec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada","Seven hybridoma cell lines producing monoclonal antibodies (MAbs) to the hemagglutinin-esterase (HE) glycoprotein of bovine coronavirus (BCV) were obtained from BALB/c mice that were immunized with an enriched peplomeric fraction of the winter dysentery (WD)-associated strain BCQ.2590. The specificities of these MAbs to either the dimeric (140-kDa) or the monomeric (65-kDa) form of the HE glycoprotein were determined by Western immunoblotting experiments with purified virus and immunoprecipitation tests with [35S]methionine-labelled infected cell extracts. Four of these anti- HE MAbs inhibited the hemagglutinating activity of the virus and three weakly neutralized its infectivity in vitro. In addition, competition binding assays allowed for the definition of two independent antigenic domains (domains A and D) and two overlapping antigenic domains (domains B and C) for the HE glycoprotein of the WD-associated strain; epitopes located within antigenic domain A were not associated with hemagglutination inhibition (HAI) and virus neutralization activities. In HAI tests, the four anti-HA MAbs defined two distinct antigenic subgroups among 24 BCV field isolates that have been associated with either typical outbreaks of WD or neonatal calf diarrhea (NCD) in Quebec dairy herds from 1986 to 1996. The Quebec WD-associated strains of BCV, as well as some of the NCD-associated strains isolated since 1991, fell within a subgroup distinct from that of the prototype Mebus strain.",,"cross reacting antibody; esterase; monoclonal antibody; virus enzyme; virus glycoprotein; virus hemagglutinin; animal cell; antigen antibody reaction; antigen binding; article; binding competition; coronavirus; cross reaction; dysentery; nonhuman; priority journal; Animals; Antibodies, Monoclonal; Antibodies, Viral; Cattle; Coronavirus, Bovine; Cross Reactions; Dysentery; Hemagglutinins, Viral; Mice; Viral Fusion Proteins; Viral Proteins; Animalia; Bovinae; Bovine coronavirus; Coronavirus","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1991) Virology, 176, pp. 296-301; Athanassious, R., Marsolais, G., Assaf, R., Dea, S., Descóteaux, J.P., Dulude, S., Montpetit, C., Detection of bovine coronavirus and type a rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can. Vet. J., 35, pp. 163-169; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J. Clin. Microbiol., 28, pp. 1454-1457; Crouch, C.F., Bielefeldt Ohmann, H., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen antibody complexes by clinically normal cows (1985) J. Gen. Virol., 66, pp. 1489-1500; Dea, S., Garzon, S., Identification of coronaviruses by the use of indirect protein A-gold immunoelectron microscopy (1991) J. Vet. Diagn. Invest., 3, pp. 297-305; Dea, S., Tijssen, P., Identification of the structural proteins of turkey enteric coronavirus (1988) Arch. Virol., 99, pp. 173-186; Dea, S., Tijssen, P., Antigenic and polypeptide structure of turkey enteric coronaviruses as defined by monoclonal antibodies (1989) J. Gen. Virol., 70, pp. 1725-1741; Dea, S., Garzon, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (Bluecomb) coronaviruses in a continuous HRT-18 cell line (1989) Am. J. Vet. Res., 50, pp. 1310-1318; Dea, S., Michaud, L., Milane, G., Comparison of bovine coronavirus isolates associated with neonatal calf diarrhoea and winter dysentery in adult dairy cattle in Québec (1995) J. Gen. Virol., 76, pp. 1263-1270; Dea, S., Roy, R.S., Begin, M.E., Bovine coromavirus isolation in continuous cell lines (1980) Am. J. Vet. Res., 41, pp. 30-38; Dea, S., Roy, R.S., Elazhary, M.A.S.Y., Antigenic variations among calf diarrhoea coronaviruses by immunodiffusion and counterimmuno-electrophoresis (1982) Ann. Rech. Vet., 13, pp. 351-356; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Dea, S., Gagnon, C.A., Mardassi, H., Milane, G., Antigenic variability among North American and European strains of porcine reproductive and respiratory syndrome virus as defined by monoclonal antibodies to the matrix protein (1996) J. Clin. Microbiol., 34, pp. 1488-11193; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Sabara, M., Babiuk, L.A., Structural protiens of bovine coronavirus and their intracellular processing (1988) J. Gen. Virol., 68, pp. 2863-2877; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoprotiens E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; Durham, P.J.K., Hassard, L.E., Armstrong, K.R., Naylor, J.M., Coronavirus-associated diarrhea (winter dysentery) in adult cattle (1989) Can. Vet.J., 30, pp. 825-827; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch. Virol., 104, pp. 241-248; Espinasse, J., Viso, M., Laval, A., Savey, M., Leyac, L.E., Winter dysentery: A coronavirus-like agent in the feces of beef and dairy cattle with diarrhoea (1982) Vet. Rec., 110, p. 385; Holmes, K.V., Coronaviridae and their replication (1991) Fundamental Virology, pp. 471-488. , B. N. Fields and D. M. Knipe (ed.). Raven Press, New York, N.Y; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike protein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Kendall, C., Ionescu-Matiu, I., Dreesman, G.R., Utilization of the biotine/avidin system to amplify the sensitivity of the enzyme-linked immunosorbent assay (ELISA) (1983) J. Immunol. Methods, 56, pp. 329-339; Kienzle, T.E., Abraham, S., Hogue, B.G., Brian, D.A., Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein (1990) J. Virol., 60, pp. 1834-1838; Kimura-Kuroda, Yasui, K., Topographical analysis of antigenic determinants on envelope glycoprotein V3 (E) of Japanese encephalitis virus using monoclonal antibodies (1983) J. Virol., 45, pp. 124-132; King, B., Potts, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Res., 2, pp. 53-59; King, B., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 2, pp. 700-707; Mebus, C.A., Pathogenesis of coronaviral infection in calves (1978) J. Am. Vet. Med. Assoc., 173, pp. 631-632; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhoea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavius and antigenic varitions among Quebec isolates (1993) Arcg. Virol., 131, pp. 455-465; Niesters, H.G.M., Bleumink-Pluym, N.M.C., Osterhaus, A.D.M.E., Horzinek, M.C., Van Der Zeijst, B.A.M., Epitopes on the peplomer protein of infectious bronchitis virus strain M41 as defined by monoclonal antibodies (1987) Virology, 161, pp. 511-519; Parker, M.D., Cox, G.J., Deregt, D., Fitzpatrick, D., Babiuk, L.A., Cloning and in vitro expression of the gene for the E3 haemagglutinin glycoprotein of bovine corona-virus (1989) J. Gen. Virol., 70, pp. 155-164; Parker, M.D., Yoo, D., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) J. Gen. Virol., 71, pp. 263-270; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch. Virol., 85, pp. 71-83; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckerr, R.A., Winter dysentery in adult dairy cattle: Detection of coronaviruses in the feces (1988) Vet. Rec., 123, pp. 300-301; Saif, L.J., Brock, K.V., Redmam, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet. Rec., 128, pp. 447-449; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-binding activity (1991) Virology, 180, pp. 221-228; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation fromnasal swab samples in cattle with signs of respiratory tract disease alter shipping (1996) J. Am. Vet. Med. Assoc., 208, pp. 1452-1455; Tsunemitsu, H., Saif, L., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol., 140, pp. 1303-1311; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: Detailed antigenic analysis of S1, S2 and HE (1992) J. Gen. Virol., 73, pp. 1725-1737; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J. Virol., 62, pp. 4686-4690; Yoo, D., Parker, M.D., Song, J., Cox, G.J., Deregt, D., Babiuk, L.A., Structural analysis of the conformational domains involved in neutralization of bovine coronavirus using deletion mutants of the spike glycoprotein S1 subunit expressed by recombinant baculoviruses (1991) Virology, 183, pp. 91-98","Dea, S.; Centre de Recherche en Virologie, Institut Armand Frappier, Universite du Quebec, 531 boul. des Prairies, Laval, Que. H7N 4Z3, Canada",,,00951137,,JCMID,"8968877","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0031060047
"Šplíchal I., Řeháková Z., Šinkora M., Šinkora J., Trebichavský I., Laude H., Charley B.","6701407816;7004319797;6603766374;15745691500;7004387808;7006652624;7004130118;","In vivo study of interferon-alpha-secreting cells in pig foetal lymphohaematopoietic organs following in utero TGEV coronavirus injection",1997,"Research in Immunology","148","4",,"247","256",,13,"10.1016/S0923-2494(97)80866-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343487805&doi=10.1016%2fS0923-2494%2897%2980866-8&partnerID=40&md5=b94b83a7f07788160dd4d273ac3fb4a3","Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic; Lab. de Virologie et Immunol. M., INRA, 78350 Jouy-en-Josas, France; National Institute of Animal Health, Kannondai, Tsukuba, Ibaraki 305, Japan","Šplíchal, I., Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic, National Institute of Animal Health, Kannondai, Tsukuba, Ibaraki 305, Japan; Řeháková, Z., Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic; Šinkora, M., Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic; Šinkora, J., Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic; Trebichavský, I., Division of Immunology, Inst. Microbiol. Acad. Sci. Czech R., 54922 Nový Hrádek, Czech Republic; Laude, H., Lab. de Virologie et Immunol. M., INRA, 78350 Jouy-en-Josas, France; Charley, B., Lab. de Virologie et Immunol. M., INRA, 78350 Jouy-en-Josas, France","Non-infectious UV-inactivated transmissible gastroenteritis virus (TGEV) was previously shown to induce interferon alpha (IFNα) secretion following in vitro incubation with blood mononuclear cells. In this study, pig foetuses at different stages of gestation were injected in utero with (a) partially UV- inactivated wild TGEV or (b) fully UV-inactivated wild or dm49-4 mutant TGEV coronavirus. Nucleated cells from foetal liver, bone marrow, spleen and blood were isolated 10 or 20 h after injection and assayed ex vivo for IFNα secretion by ELISPOT and ELISA techniques. The administration of TGEV induced IFNα-secreting cells in foetal lymphohaematopoietic organs at mid-gestation. In contrast, IFNα was not detected in control sham-operated foetuses. A specific point mutation in the amino acid sequence of the viral membrane glycoprotein M of TGEV mutant dm49-4 was associated with lower or absent IFNα in utero inducibility by mutant virus as compared with wild virus. Flow cytometry analysis did not show differences in leukocyte surface marker expression between control and TGEV- or between dm49-4 and wild virus-treated foetus cells, with the exception of a reduction in percentages of polymorphonuclear cells in TGEV-treated lymphohaematopoietic tissues, which is probably due to IFNα secretion. The present data provided in vivo evidence of IFNα secretion at the cell level in foetal lymphohaematopoietic organs. Such IFNα-secreting cells in lymphohaematopoietic tissues may be the source of IFNα detected during foetal infections.","Coronavirus, Transmissible gastroenteritis virus, IFNα; ELISA, ELISPOT, Foetus, Pig","alpha interferon; animal experiment; article; Coronavirus; fetus; flow cytometry; hematopoiesis; immunostimulation; interferon production; lymphopoiesis; nonhuman; priority journal; swine","Artursson, K., (1993) Studies on the Interferon-a/β System of Pigs, , Ph.D. thesis, Uppsala; Capobianchi, M.R., Facchini, J., Di Marco, P., Antonelli, G., Dianzani, F., Induction of alpha interferon by membrane interaction between viral surface and peripheral blood mononuclcar cells (1985) Proc. Soc. Exp. Biol. Med., 178, pp. 551-556; Cederblad, B., Alm, G., Infrequent but efficient interferon-α-producing human mononuclear leukocytes induced by herpes simplex virus in vitro studied by immunoplaque and limiting dilution assays (1990) J. 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Virol., 66, pp. 743-749; Lebon, P., Inhibition of herpes simplex virus type 1-induced interferon synthesis by monoclonal antibodies against viral glycoprotein D and by lysosomotropic drugs (1985) J. Gen. Virol, 6, pp. 2781-2785; Lebon, P., Commoy-Chevalier, M.J., Robert-Galliot, B., Chany, C., Different mechanisms for α and β interferon induction (1982) Virology, 119, pp. 504-507; Lebon, P., Daffos, F., Checoury, A., Grangeot-Keros, L., Forestier, F., Toublanc, J.E., Presence of an acid-labile alpha-interferon in sera from fetuses and children with congenital rubella (1985) J. Clin. Microbiol., 21, pp. 775-778; Lebon, P., Girard, S., Thépot, F., Chany, Ch., The presence of α-interferon in human amniotic fluid (1982) J. Gen. Virol, 59, pp. 393-396; Nowacki, W., Charley, B., Enrichment of coronavirus-induced interferon-producing blood leukocytes increases the interferon yield per cell: A study with pig leukocytes (1993) Res. Immunol., 144, pp. 111-120; Riffault, S., Eloranta, M.-L., Carrat, Ch., Sandberg, K., Charley, B., Alm, G., Herpes simplex virus induces appearance of interferon-α/β producing cells and partially interferon-α/β dependent accumulation of leukocytes in murine regional lymph nodes (1996) J. Interferon Cytok. Res., 16, pp. 1007-1014; Roberts, N.J., Douglas, R.G., Simons, R.M., Diamond, M.E., Virus induced interferon production by human macrophages (1979) J. Immunol., 123, pp. 365-369; Romero, R., Gomez, R., Galasso, M., Munoz, H., Acosta, L., Yoon, B.H., Svinarich, D., Cotton, D.B., Macrophage inflammatory protein-1 alpha in term and preterm parturition : Effect of microbial invasion of the amniotic cavity (1994) Am. J. Reprod. Immunol., 32, pp. 108-113; Saksela, E., Virtanen, I., Hovi, T., Secher, D.S., Cantell, K., Monocyte is the main producer of human alpha interferons following Sendai virus induction (1984) Prog. Med. Virol, 30, pp. 78-86; Sandberg, K., Matsson, P., Alm, G.V., A distinct population of nonphagocytic and CD4+ null lymphocytes produce interferon-α after stimulation by herpes simplex virus-infected cells (1990) J Immunol., 145, pp. 1015-1020; Šplíchal, I., Bonneau, M., Charley, B., Ontogeny of interferon alpha secreting cells in the porcine fetal hematopoietic organs (1994) Immunol. Lett., 43, pp. 203-208; Šterzl, J., Kováf̌ů, F., Development of lymphatic tissue and immunocompetency in pig foetus and germ-free piglets (1977) Acta. Vet. Brno, 46 (SUPPL. 3), pp. 13-53; Šterzl, J., Rejnek, J., Trávníček, J., Impermeability of pig placenta for antibodies (1966) Folia Microbiol., 11, pp. 7-10; Svensson, H., Johannisson, A., Nikkila, T., Alm, G.V., Cederblad, B., The cell surface phenotype of human natural interferon-α producing cells as determined by flow cytometry (1996) Scand. J. Immunol., 44, pp. 164-172","Splichal, I.; Div. of Immunology/Gnotobiology, IMAS of the Czech Republic, 54922 Novy Hradek, Czech Republic",,"Elsevier Masson SAS",09232494,,RIMME,"9300531","English","RES. IMMUNOL.",Article,"Final",Open Access,Scopus,2-s2.0-0343487805
"Brown T.P., Garcia A., Kelly L.","7404319500;16401453800;7202968991;","Spiking mortality of turkey poults: 2. Effect of six different in vitro disinfection techniques on organ homogenates capable of reproducing SMT",1997,"Avian Diseases","41","4",,"906","909",,2,"10.2307/1592345","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031252219&doi=10.2307%2f1592345&partnerID=40&md5=62c0d73c18dc971db324bf4f2c321257","Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States","Brown, T.P., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Garcia, A., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Kelly, L., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States","Spiking mortality of turkeys (SMT) is an infectious disease of 5-to-25-day-old turkey poults characterized by acute enteritis and bursal and thymic atrophy. It is reproducible by exposure to organ homogenates or contaminated litter. We studied methods potentially useful for decontamination of turkey houses contaminated with SMT. Organ homogenates capable of producing SMT and containing turkey intestinal coronavirus were exposed in vitro for 5 hr to either 5.0% NaCl, pH 2.0, pH 12, 1.0% formaldehyde, 57 C, or lyophilization. Results were assessed by oral garage of treated inocula into 1-day-old turkeys and measurement of subsequent coronavirus shedding, growth rate, feed conversion, and mortality from 1 to 21 days of age. Formaldehyde treatment rendered the inoculum nonpathogenic, whereas other treatments failed to ameliorate its negative effects.",,,"Brown, T.P., Emory, W.H., Howell D., Jr., Acute enteritis in turkey poults: Chickens and cattle as subclinical carriers (1995) 132nd Annual Meeting of American Veterinary Medical Association, p. 115. , Pittsburg, PA; Brown, T.P., Garcia, A.P., Kelley, L., Spiking mortality of turkey poults: 1. Experimental reproduction in isolation facilities Avian Dis., 41, pp. 604-609; Brown, T.P., Glisson, J.R., Villegas, P.V., Acute enteritis as a cause of ""spiking mortality"" in young turkey poults (1992) Proc. 3rd Eli Lilly Turkey Technical Seminar, pp. 20-29. , Nashville, TN. May 8-10; Brown, T.P., Howell, D.R., Garcia, A.P., Adult cattle as inapparent carriers of spiking mortality of turkeys (1996) 133rd Annual Meeting of American Veterinary Medical Association, p. 373. , Louisville, KY; Dea, S., Tijssen, P., Viral agents associated with outbreaks of diarrhea in turkey flocks in Quebec, Canada (1988) J. Vet. Res., 52, pp. 53-57; Dea, S., Verbeek, A., Tijssen, P., Transmissible enteritis of turkeys: Experimental inoculation studies with tissue-culture-adapted turkey and bovine coronaviruses (1991) Avian Dis., 35, pp. 767-777; Deshmukh, D.R., Larsen, C.T., Dutta, S.K., Pomeroy, B.S., Characterization of pathogenic filtrates and viruses isolated from turkeys with bluecomb (1969) Am. J. Vet. Res., 30, pp. 1019-1025; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) Am. J. Vet. Res., 35, pp. 1549-1552; Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis/spiking mortality (1995) Avian Pathol., 24, pp. 497-505; Patel, B.L., Gonder, E., Pomeroy, B.S., Detection of turkey coronaviral enteritis (bluecomb) in field epiornithics, using the direct and indirect fluorescent antibody tests (1977) Am. J. Vet. Res., 38, pp. 1407-1411","Brown, T.P.; Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"9454925","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0031252219
"Rossen J.W.A., Strous G.J.A.M., Horzinek M.C., Rottier P.J.M.","7005977394;7004975908;7102624836;7006145490;","Mouse hepatitis virus strain A59 is released from opposite sides of different epithelial cell types",1997,"Journal of General Virology","78","1",,"61","69",,12,"10.1099/0022-1317-78-1-61","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031031740&doi=10.1099%2f0022-1317-78-1-61&partnerID=40&md5=c5ff4c314462e564941c9dc9a22dbe38","Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Medical School, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Rossen, J.W.A., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Strous, G.J.A.M., Medical School, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Coronaviruses infect humans and animals through epithelial cells of the gastrointestinal and respiratory tracts that serve as their primary target. When studying infections in cultured polarized epithelial cells, we found previously that coronaviruses are released from specific plasma-membrane domains; thus, mouse hepatitis virus (strain A59; MHV-A59) leaves murine epithelial kidney cells from the basolateral surface, whereas release of transmissible gastroenteritis virus from porcine epithelial kidney cells is confined to the apical membrane. This observation begged the question whether a particular coronavirus is consistently shed through the same membrane, irrespective of the nature of the epithelial cell. We therefore extended our studies with MHV-A59 to Madin-Darby canine kidney (MDCK) strain I and human colon carcinoma (Caco-2) cells, both of which are naturally refractory to MHV-A59 but were made susceptible to infection by transfection with recombinant MHV receptor cDNA. The release of MHV-A59 from Caco(MHVR) cells occurred preferentially from the basolateral side, consistent with our previous observations. In contrast, release from MDCK(MHVR) cells occurred almost exclusively from the apical surface. Because of this difference, we studied MHV-A59 infection of MDCK(MHVR) cells in more detail. The virus entered the cells preferentially from the apical side, a situation similar to that in murine epithelial cells, where the highest density of MHV receptor glycoprotein was found. The results from this and previous studies show that targeting of vesicles containing MHV-A59 to a specific side of epithelial cells may vary in different epithelial cell types.",,"complementary DNA; virus receptor; animal cell; apical membrane; article; basolateral membrane; cancer cell culture; cell polarity; cell type; colon carcinoma; DNA transfection; epithelium cell; human; human cell; Murine hepatitis coronavirus; nonhuman; priority journal; receptor density; virus infection; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Suidae; Transmissible gastroenteritis virus","Blau, D.M., Compans, R.W., Entry and release of measles virus are polarized in epithelial cells (1995) Virology, 210, pp. 91-99; Brown, W.J., Constantinescu, E., Farquhar, M.G., Redistribution of mannose-6-phosphate receptors induced by tunicamycin and chloroquine (1984) Journal of Cell Biology, 99, pp. 320-326; Caplan, M.J., Stow, J.L., Newman, A.P., Madri, J., Anderson, C., Farquhar, M.G., Palade, G.E., Jamieson, J.D., Dependence on pH of polarized sorting of secreted proteins (1987) Nature, 329, pp. 632-635; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , Edited by S. G. Siddell. New York: Plenum Press; Cerneus, D.P., Strous, G.J., Van Der Ende, A., Bidirectional transcytosis determines the steady state distribution of the transferrin receptor at opposite plasma membrane domains of BeWo cells (1993) Journal of Cell Biology, 122, pp. 1223-1230; Compans, R.W., Srinivas, R.V., Protein sorting in polarized epithelial cells (1991) Current Topics in Microbiology and Immunology, 170, pp. 141-181; De Almeida, J.B., Stow, J.L., Disruption of microtubules alters polarity of basement membrane proteoglycan secretion in epithelial cells (1991) American Journal of Physiology, 260, pp. C691-C700; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) Journal of Virology, 67, pp. 1-8; Eaton, S., Simons, K., Apical basal, and lateral cues for epithelial polarization (1995) Cell, 82, pp. 5-8; Fuller, S.D., Von Bonsdorff, C.-H., Simons, K., Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK (1984) Cell, 38, pp. 65-77; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P.J.M., Rossen, J.W.A., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) Journal of Virology, 69, pp. 889-895; Gottlieb, T.A., Beaudry, T.A.G., Rizzolo, L., Coleman, A., Rindler, M., Adesnik, M., Sabatini, D.D., Secretion of endogenous and exogenous proteins from polarized MDCK cell monolayers (1986) Proceedings of the National Academy of Sciences, USA, 83, pp. 2100-2104; Holmes, K.V., Coronaviridae and their replication (1990) Virology, 2nd Edn, pp. 841-856. , Edited by B. N. Fields, D. M. Knipe, R. M. Chanock, M. S. Hirsch, J. L. Melnick, T. P. Monath & B. Roizman. New York: Raven Press; Klumperman, J., Krijnse-Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) Journal of Virology, 68, pp. 6523-6534; Kondor-Koch, C., Bravo, R., Fuller, S.D., Cutler, D., Garoff, H., Exocytic pathways exist to both the apical and the basolateral cell surfaces of the polarized epithelial cell MDCK (1985) Cell, 43, pp. 297-306; Krijnse-Locker, J., Ericsson, M., Rottier, P.J.M., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) Journal of Cell Biology, 124, pp. 55-70; Low, S.H., Wong, S.H., Tang, B.L., Hong, W., Effects of NH4Cl and nocadozole on polarized fibronectin secretion vary amongst different epithelial cell types (1994) Molecular Membrane Biology, 11, pp. 45-54; Matter, K., Mellman, I., Mechanisms of cell polarity: Sorting and transport in epithelial cells (1994) Current Opinion in Cell Biology, 6, pp. 545-554; Mays, R.W., Beck, K.A., Nelson, W.J., Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery (1994) Current Opinion in Cell Biology, 6, pp. 16-24; Mostov, K.E., Cardone, M.H., Regulation of protein traffic in polarized epithelial cells (1995) Bioessays, 17, pp. 129-138; Rindler, M.J., Traber, M.G., A specific sorting signal is not required for the polarized secretion of newly synthesized proteins from cultured intestinal epithelial cells (1988) Journal of Cell Biology, 107, pp. 471-479; Rodriguez-Boulan, E., Sabatini, D.D., Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity (1978) Proceedings of the National Academy of Sciences, USA, 75, pp. 5071-5075; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells (1994) Journal of Virology, 68, pp. 7966-7973; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Horzinek, M.C., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., Coronaviruses in polarized epithelial cells (1995) Advances in Experimental Medicine and Biology, 380, pp. 135-138; Rossen, J.W.A., Horzinek, M.C., Rottier, P.J.M., Coronavirus infection of polarized epithelial cells (1995) Trends in Microbiology, 3, pp. 486-490; Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Van Der Ende, A., Strous, G.J.A.M., Rottier, P.J.M., MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally (1995) Virology, 210, pp. 54-66; Rottier, P.J.M., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Translation of three mouse hepatitis virus strain A59 subgenomic RNAs in Xenopus laevis oocytes (1981) Journal of Virology, 38, pp. 20-26; Simons, K., Wandinger-Ness, A., Polarized sorting in epithelia (1990) Cell, 62, pp. 207-210; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in sac cells: Determination of the first site of budding of progeny virions (1984) European Journal of Cell Biology, 33, pp. 281-293; Tooze, J., Tooze, S.A., Fuller, S.D., Sorting of progeny coronavirus from condensed secretory proteins at the exit from the transGolgi network of AtT20 cells (1987) Journal of Cell Biology, 105, pp. 1215-1226; Traber, M.G., Kayden, H.J., Rindler, M.J., Polarized secretion of newly synthesized lipoproteins by the Caco-2 human intestinal cell line (1987) Journal of Lipid Research, 28, pp. 1350-1363; Tucker, S.P., Compans, R.W., Virus infection of polarized epithelial cells (1993) Advances in Virus Research, 42, pp. 187-247; Tucker, S.P., Melsen, L.R., Compans, R.W., Migration of polarized epithelial cells through permeable membrane substrates of defined pore size (1992) European Journal of Cell Biology, 58, pp. 280-290; Van Meer, G., Simons, K., Viruses budding from either the apical or basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions (1982) EMBO Journal, 1, pp. 847-852; Weaver, S.C., Tesh, R.B., Guzman, H., Ultrastructural aspects of replication of New Jersey serotype of vesicular stomatitis virus in a suspected sand fly vector, Lutzomyia shannoni (Diptera: Psychodidae) (1992) American Journal of Tropical Medicine and Hygiene, 46, pp. 201-210; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) Journal of Virology, 64, pp. 3817-3823; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) Journal of Virology, 66, pp. 6931-6938; Yokomori, K., Assanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56; Zurzolo, C., Polistina, C., Saini, M., Gentile, R., Aloj, L., Migliaccio, G., Bonatti, S., Nitsch, L., Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues (1992) Journal of Cell Biology, 117, pp. 551-564","Rossen, J.W.A.; Virology Division, Dept. Infectious Diseases Immunology, Utrecht Univ., Fac. Veterinary Med., Yalelaan 1, 3584 CL Utrecht, Netherlands; email: J.Rossen@vetmic.dgk.ruu.nl",,"Microbiology Society",00221317,,JGVIA,"9010286","English","J. GEN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0031031740
"Marsilio F., Tiscar P.-G., Gentile L., Roth H.U., Boscagli G., Tempesta M., Gatti A.","55788078800;6508312567;7006532232;7202681802;6603314674;7005599031;15753442300;","Serologic survey for selected viral pathogens in brown bears from Italy",1997,"Journal of Wildlife Diseases","33","2",,"304","307",,21,"10.7589/0090-3558-33.2.304","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031115395&doi=10.7589%2f0090-3558-33.2.304&partnerID=40&md5=fb3566b585ef5d40bb4cde80ae2f8197","Istituto di Malattie Infettive degli Animali M. Compagnucci, Facoltà di Medicina Veterinaria, Università degli Studi di Teramo, 64020 Piano d'Accio di Teramo, Italy; Centro Studi Ecologici Appenninici, Parco Nazionale d'Abruzzo, 67032 Pescasseroli (AQ), Italy; Parco Regionale Sirente-Velino, Italy","Marsilio, F., Istituto di Malattie Infettive degli Animali M. Compagnucci, Facoltà di Medicina Veterinaria, Università degli Studi di Teramo, 64020 Piano d'Accio di Teramo, Italy; Tiscar, P.-G., Istituto di Malattie Infettive degli Animali M. Compagnucci, Facoltà di Medicina Veterinaria, Università degli Studi di Teramo, 64020 Piano d'Accio di Teramo, Italy; Gentile, L., Centro Studi Ecologici Appenninici, Parco Nazionale d'Abruzzo, 67032 Pescasseroli (AQ), Italy; Roth, H.U., Centro Studi Ecologici Appenninici, Parco Nazionale d'Abruzzo, 67032 Pescasseroli (AQ), Italy; Boscagli, G., Parco Regionale Sirente-Velino, Italy; Tempesta, M., Centro Studi Ecologici Appenninici, Parco Nazionale d'Abruzzo, 67032 Pescasseroli (AQ), Italy; Gatti, A., Istituto di Malattie Infettive degli Animali M. Compagnucci, Facoltà di Medicina Veterinaria, Università degli Studi di Teramo, 64020 Piano d'Accio di Teramo, Italy","Blood samples were collected from six captive bears and nine free-ranging Marsican brown bears (Ursus arctos marsicanus) in the Abruzzo National Park, Italy, between 1991 and 1995. Sera were tested for evidence of exposure to canine distemper virus (CDV), canine adenovirus type 2, canine coronavirus, and canine parvovirus type 2 (CPV-2). Serologic evidence of CDV and CPV-2 exposure was found in both captive and free-ranging bears. This may be the first report of CDV exposure in free-ranging bears. © Wildlife Disease Association 1997.","European brown bear; Marsican brown bear; Serologic survey; Ursus arctos; Viral pathogens","virus antibody; virus antigen; Adenovirus; animal; animal disease; article; bear; blood; Canine distemper morbillivirus; Coronavirus; dog disease; female; fluorescent antibody technique; hemagglutination test; immunology; Italy; male; Parvovirus; serodiagnosis; virus infection; Adenoviridae Infections; Adenoviruses, Canine; Animals; Antibodies, Viral; Antigens, Viral; Coronavirus Infections; Coronavirus, Canine; Distemper; Distemper Virus, Canine; Female; Fluorescent Antibody Technique, Indirect; Hemagglutination Tests; Italy; Male; Neutralization Tests; Parvoviridae Infections; Parvovirus, Canine; Ursidae","Appel, M.J.G., Summers, B.A., Pathogenicity of morbillivirus for terrestrial carnivores (1995) Veterinary Microbiology, 44, pp. 187-191; Binn, L.N., Marchwicki, R.H., Stephenson, E.H., Establishment of a canine cell line: Derivation, characterization, and viral spectrum (1980) American Journal of Veterinary Research, 41, pp. 855-860; Boscagli, G., L'Orso bruno marsicano (1994) Abruzzo Guida Alla Fauna Selvatica, pp. 47-52. , D. Febbo and M. Pellegrini (eds.). Regione Abruzzo/CARSA Editore, Pescara, Italy; Buonavoglia, C., Tollis, M., Di Trani, L., Orfei, Z., Ricerca sulla immunizzazione del cane verso la gastroenterite da parvovirus con un vaccino sperimentale omologo inattivato (1981) La Clinica Veterinaria, 104, pp. 287-289; Carmichael, L.E., Joubert, J.C., Pollock, R.V.H., Hemagglutination by canine parvovirus: Serologic studies and diagnostic applications (1980) American Journal of Veterinary Research, 41, pp. 784-792; Collins, J.E., Leslie, P., Johnson, D., Nelson, D., Peden, W., Boswell, R., Draayer, H., Epizootic of adenovirus infection in American black bear (1984) Journal of American Veterinary Medicine Association, 185, pp. 1430-1432; Fabbri, M., Boscagli, G., Lovari, S., The brown bear population of Abruzzo (1983) Acta Zoologica Fennica, 174, pp. 163-164; Hatlapa, H.H.M., Wisner, H., (1988) Pratica Anestetica degli Animali Selvatici, pp. 1-88. , Edagricole, Bologna, Italy; Jalanka, H.H., The use of medetomidine, medetomidine-ketamine combinations, and atipamezole in non domestic-mammals: A review (1990) Journal of Zoo and Wildlife Medicine, 21, pp. 259-282; Lennette, E.H., Halonen, P., Murphy, F.A., (1988) Laboratory Diagnosis of Infectious Diseases: Principles and Practice, 2, pp. 180-182. , Springer-Verlag Publisher, Berlin, Germany; Madic, J., Huber, D., Lugovic, B., Serological survey for selected viral and rickettsial agent of brown bears (Ursus arctos) in Croatia (1993) Journal of Wildlife Diseases, 29, pp. 572-576; Marsilio, F., Tiscar, P.G., Varvara, B., Lucatorto, G., Lavazza, A., Isolamento e caratterizzazione di un ceppo di coronavirus del cane (CCV) (1993) Atti Della Società Italiana Delle Scienze Veterinarie, 47, pp. 1213-1217; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro neutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Japanese Journal of Veterinary Science, 49, pp. 563-565; Montali, R.J., Bartz, C.R., Bush, M., Canine distemper virus (1987) Virus Infection of Carnivores, pp. 437-443. , M. J. G. Appel (ed.). Elsevier Science Publishers, Amsterdam, Netherlands; Randi, R., Gentile, L., Boscagli, G., Huber, D., Roth, H.U., Mithocondrial DNA sequence divergence among some west European brown bear (Ursus arctos L.) population (1994) Lesson for Conservation. Heredity, 73, pp. 480-489; Spendlove, R.S., Microscopic techniques (1967) Methods in Virology, 3, pp. 475-520. , K. Maramorosch and H. Koprowski (eds.). Academic Press Inc., New York, New York; Stonenberg, R.P., Jonkel, C.J., Age determination of black bears by cementum layers (1966) The Journal of Wildlife Management, 30, pp. 411-414; Taylor, W.P., Reynolds, H.V., Ballard, W.B., Immobilization of grizzly bears with tiletamine hydrocloride and zolazepam hydrocloride (1989) The Journal of Wildlife Management, 53, pp. 978-981; Toschi, A., (1965) Fauna d'Italia, 3, pp. 294-305. , Edizioni Calderini, Bologna, Italia; Zarnke, R.L., Evans, M.B., Serological evidence for infectious canine hepatitis virus in grizzly bear (1989) Journal of Wildlife Diseases, 25, pp. 568-573; Zunino, F., Orso bruno marsicano (1976) SOS Fauna, pp. 603-710. , Edizioni World Wildlife Found, Camerino, Italy","Marsilio, F.; Istituto di Malattie Infettive degli Animali M. Compagnucci, Facoltà di Medicina Veterinaria, Università degli Studi di Teramo, 64020 Piano d'Accio di Teramo, Italy",,"Wildlife Disease Association, Inc.",00903558,,,"9131563","English","J. Wildl. Dis.",Review,"Final",,Scopus,2-s2.0-0031115395
"Smelianskaia M.V., Prokhoriatova E.V., Volianskii I.L., Babkin V.F., Panchenko L.A.","6506789382;6506932779;57215952720;7102998050;7103100652;","The use of the fluorescent probe method for the diagnosis of acute coronavirus intestinal infections in people [Primenenie metoda fluorestsentnykh zondov dlia diagnostiki koronavirusnykh ostrykh kishechnykh infektsii u liudei.]",1997,"Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993)","59","3",,"86","90",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031136889&partnerID=40&md5=df47bb61c6c8b2a363b64fefc94fc554",,"Smelianskaia, M.V.; Prokhoriatova, E.V.; Volianskii, I.L.; Babkin, V.F.; Panchenko, L.A.","The scientific investigations conducted first allow using a method of fluorescent probes for the diagnosis of human coronaviral intestinal infection. The method is characterised by sensitivity, specificity, reproductivity and proximity. It is comparable, according to these parameters, with the methods of the third generation and may be recommended for putting into practical work of virological laboratories.",,"2 (4 (dimethylamino)styryl) 1 methylpyridinium; 2-(4-(dimethylamino)styryl)-1-methylpyridinium; antiserum; diagnostic agent; fluorescent dye; pyridinium derivative; acute disease; article; cell culture; child; Coronavirus; enteropathy; feces; fluorescence microscopy; human; isolation and purification; methodology; sensitivity and specificity; virology; virus infection; Acute Disease; Cells, Cultured; Child; Coronavirus; Coronavirus Infections; Feces; Fluorescent Dyes; Humans; Immune Sera; Intestinal Diseases; Microscopy, Fluorescence; Pyridinium Compounds; Sensitivity and Specificity",,"Smelianskaia, M.V.",,,10280987,,,"9410400","Russian","Mikrobiol. Z.",Article,"Final",,Scopus,2-s2.0-0031136889
"De Vries A.A.F., Horzinek M.C., Rottier P.J.M., De Groot R.J.","7202909794;7102624836;7006145490;7103077066;","The genome organization of the nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses",1997,"Seminars in Virology","8","1",,"33","47",,203,"10.1006/smvy.1997.0104","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030861788&doi=10.1006%2fsmvy.1997.0104&partnerID=40&md5=0eceb1f0de54430797dbb914bfdb4a13","Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","De Vries, A.A.F., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Groot, R.J., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonsegmented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organization and expression of their genomes, and sequence conservation among the polymerase polyproteins strongly suggests that they have a common ancestry. On this basis, the International Committee on Taxonomy of Viruses recently established a new order, Nidovirales, to contain the two families. 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Biol., 224, pp. 575-587; Meulenberg, J.J.M., Petersen-Den Besten, A., De Kluyver, E.P., Moorman, R.J.M., Schaaper, W.M.M., Wensvoort, G., Characterization of proteins encoded by ORFs 2 to 7 of Lelystad virus (1995) Virology, 206, pp. 155-163; Meulenberg, J.J.M., Petersen-Den Besten, A., Identification and characterization of a sixth structural protein of Lelystad virus: The glycoprotein GP2 encoded by ORF2 is incorporated in virus particles (1996) Virology, 225, pp. 44-51; Van Nieuwstadt, A.P., Meulenberg, J.J.M., Van Essen-Zandbergen, A., Petersen-Den Besten, A., Bende, R.J., Moormann, R.J.M., Wensvoort, G., Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus (Arteriviridae) are structural proteins of the virion (1996) J. Virol., 70, pp. 4767-4772; Wieczorek-Krohmer, M., Weiland, F., Conzelmann, K., Kohl, D., Visser, N., Van Woensel, P., Thiel, H.-J., Weiland, E., Porcine reproductive and respiratory syndrome virus (PRRSV): Monoclonal antibodies detect common epitopes on two viral proteins of European and U.S. isolates (1996) Vet. Microbiol., 51, pp. 257-266; Snijder, E.J., Den Boon, J.A., Spaan, W.J.M., Verjans, G.M.G.M., Horzinek, M.C., Identification and primary structure of the gene encoding the Berne virus nucleocapsid protein (1989) J. Gen. Virol., 70, pp. 3363-3370; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J.M., Sequence analysis of the 3′ end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., Spaan, W.J.M., Identification and stability of a 30-kDa nonstructural protein encoded by mRNA2 of mouse hepatitis virus in infected cells (1990) Virology, 175, pp. 303-306; Cox, G.J., Parker, M.D., Babiuk, L.A., Bovine coronavirus nonstructural protein ns2 is a phosphoprotein (1991) Virology, 185, pp. 509-512; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Schwarz, B., Routledge, E., Siddell, S.G., Murine coronavirus nonstructural protein ns2 is not essential for virus replication in transformed cells (1990) J. Virol., 64, pp. 4784-4791; Weiss, S.R., Zoltick, P.W., Leibowit, J.L., The ns4 gene of mouse hepatitis virus (MHV) strain A59 contains two ORFs and thus differs from ns4 of the JHM and S strains (1993) Arch. Virol, 129, pp. 301-309; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol., 66, pp. 6143-6154; Le, S.-Y., Sonenberg, N., Maizel J.V., Jr., Distinct structural elements and internal entry of ribosomes in mRNA3 encoded by infectious bronchitis virus (1994) Virology, 198, pp. 405-411; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5 (1994) J. Gen. Virol., 75, pp. 3041-3046; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene of bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Zimmern, D., (1987) RNA Genetics, pp. 211-240. , Holland, J. J., Domingo, E., and Ahlquist, P., Eds., CRC Press, Boca Raton, FL; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Jarvis, T.C., Kirkegaard, K., The polymerase in its labyrinth: Mechanisms and implications of RNA recombination (1991) Trends Genet., 7, pp. 186-191; Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Chao, L., Fitness of RNA virus decreased by Muller's ratchet (1990) Nature, 348, pp. 454-455; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Practice, 23, pp. 40-44; Dolja, V.V., Karasev, A.V., Koonin, E.V., Molecular biology and evolution of closteroviruses: Sophisticated build-up of large RNA genomes (1994) Annu. Rev. Phytopathol., 32, pp. 261-285; Agranovsky, A.A., Principles of molecular organization, expression, and evolution of closteroviruses: Over the barriers (1996) Adv. Virus Res., 47, pp. 119-158; De Zanotto, P.M.A., Gibbs, M.J., Gould, E.A., Holmes, E.C., A reevaluation of the higher taxonomy of viruses based on RNA polymerases (1996) J. Virol., 70, pp. 6083-6096; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charité Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary- structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Cornelissen, L.A.H.M., Wierda, C.M.H., Van Der Meer, F.J., Herrewegh, A.A.P.M., Horzinek, M.C., Egberink, H.F., De Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J. Virol., 71 (7). , in press; Kusters, J.G., Jager, E., Niesters, H.G.M., Van Der Zeijst, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996","de Groot, R.J.; Virology Unit, Department of Infectious Diseases, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,"Academic Press Inc.",10445773,,SEVIE,,"English","SEMIN. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0030861788
"Wege H., Schluesener H., Meyermann R., Lassmann H.","7005516649;7006032773;55796798200;35420677900;","Coronavirus infection and demyelination: Development of inflammatory lesions in Lewis rats",1997,"Immunobiology","197","2-4",,"298","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030746997&partnerID=40&md5=0691fbbbfa36d84694d55c3e2247836b","Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany","Wege, H., Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany; Schluesener, H., Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany; Meyermann, R., Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany; Lassmann, H., Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany",[No abstract available],,"chemoattractant; cytokine; gamma interferon; nitric oxide synthase; protein S 100; tumor necrosis factor alpha; animal cell; animal experiment; animal model; conference paper; Coronavirus; demyelination; experimental model; in situ hybridization; inflammation; nonhuman; priority journal; protein expression; rat; virus infection",,"Wege, H.; Institute of Diagnostic Virology, Federal Res. Ctr. Virus Dis. Animals, Friedrich-Loeffler-Institutes, Isle of Riems, Germany",,"Elsevier GmbH",01712985,,ZIMMD,,"English","IMMUNOBIOLOGY",Conference Paper,"Final",,Scopus,2-s2.0-0030746997
"Lai M.M., Cavanagh D.","7401808497;26642890500;","The molecular biology of coronaviruses.",1997,"Advances in virus research","48",,,"1","100",,593,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030633479&partnerID=40&md5=d22179d8e9e9f25a2eb1f9c21841e869","Department of Molecular Microbiology and Immunology, Howard Hughes Medical Institute, University of Southern California School of Medicine, Angeles, Los90033-1054, United States","Lai, M.M., Department of Molecular Microbiology and Immunology, Howard Hughes Medical Institute, University of Southern California School of Medicine, Angeles, Los90033-1054, United States; Cavanagh, D., Department of Molecular Microbiology and Immunology, Howard Hughes Medical Institute, University of Southern California School of Medicine, Angeles, Los90033-1054, United States",[No abstract available],,"virus RNA; animal; Coronavirus; genetics; human; physiology; review; virion; virus replication; Animals; Coronavirus; Humans; RNA, Viral; Virion; Virus Replication",,"Lai, M.M.",,,00653527,,,"9233431","English","Adv. Virus Res.",Review,"Final",,Scopus,2-s2.0-0030633479
"Homberger F.R.","7003348988;","Enterotropic mouse hepatitis virus",1997,"Laboratory Animals","31","2",,"97","115",,47,"10.1258/002367797780600189","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030994929&doi=10.1258%2f002367797780600189&partnerID=40&md5=d26b408ec004b288dc86cc3952c3f107","Institute of Laboratory Animal Science, University of Zurich, Switzerland; Institute of Laboratory Animal Science, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland","Homberger, F.R., Institute of Laboratory Animal Science, University of Zurich, Switzerland, Institute of Laboratory Animal Science, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland","Mouse hepatitis virus (MHV), the coronavirus of the mouse, is the most common viral pathogen in contemporary laboratory mouse colonies throughout the world. It is highly contagious with variable clinical manifestations. The majority of infections are subclinical, but can still significantly influence biological responses, thus interfering with research, mainly in the field of immunology. MHV has been intensively studied from a number of research perspectives and has become the prototype for studying the molecular biology of coronaviruses. MHV contains a single-stranded, positive-sense RNA genome ranging from 27 to 31 kb, which is divided into seven genes. Virions consist of four to five structural proteins. There are many MHV strains that vary in virulence, organotropism and cell tropism, and are constantly evolving by naturally occurring mutation and recombination. Based on pathogenesis studies MHV strains are usually grouped according to their primary tissue tropism into two biotypes: polytropic and enterotropic. Enterotropic strains of MHV replicate in the intestinal mucosa and only rarely spread to other tissues. No morphological structure of the virion has as yet been identified that is responsible for enterotropism. The course of an MHV infection is dependent on the virus strain and host factors. Generally, MHV causes an acute, self-limiting infection which is inapparent in adult mice. Neonates are highly susceptible to disease and show high mortality. In an enzootically infected colony, however, they are protected by maternally derived passive immunity. Detection of MHV infections depends on serological screening of colonies. MHV is controlled by culling and rederivation of the affected colony using hysterectomy or embryo transfer or by elimination through cessation of breeding.","Coronavirus; Enterotropic; Mouse; Mouse hepatitis virus","structural protein; animal welfare; breeding; Coronavirus; embryo transfer; host; hysterectomy; immunity; infection control; intestine mucosa; laboratory; molecular biology; mortality; mouse; Murine hepatitis coronavirus; nonhuman; review; virion; virus genome; virus infection; virus replication; virus strain; virus virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Adami, C., Pooley, J., Glomb, J., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Akimaru, K., Stuhlmiller, G.M., Seigler, H.F., Influence of mouse hepatitis virus on the growth of human melanoma in the peritoneal cavity of the athymic mouse (1981) Journal of Surgical Oncology, 17, pp. 327-339; Asanaka, M., Lai, M.M., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selective pressure (1991) Virology, 185, pp. 441-445; Barthold, S.W., Research complications and state of knowledge of rodent coronaviruses (1986) Complications of Viral and Mycoplasmal Infections in Rodents to Toxicology Research Testing, pp. 53-89. , (Hamm TF, ed). Washington: Hemisphere; Barthold, S.W., Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infection of Laboratory Rodents: Effects on Biomedical Research, pp. 571-601. , (Bhatt PN, Jacoby RO, Morse AC III, New AE, eds). Orlando: Academic Press; Barthold, S.W., Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Laboratory Animal Science, 37, pp. 36-40; Barthold, S.W., Smith, A.L., Mouse hepatitis virus S in weanling Swiss mice following intranasal inoculation (1983) Laboratory Animal Science, 33, pp. 103-112; Barthold, S.W., Smith, A.L., Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice (1984) Archives of Virology, 81, pp. 103-112; Barthold, S.W., Smith, A.L., Response of genetically susceptible and resistant mice to intranasal inoculation with mouse hepatitis virus (1987) Virus Research, 7, pp. 225-239; Barthold, S.W., Smith, A.L., Duration of challenge immunity to coronavirus JHM in mice (1989) Archives of Virology, 107, pp. 171-177; Barthold, S.W., Smith, A.L., Duration of mouse hepatitis virus infection: Studies in immunocompetent and chemically immunosuppressed mice (1990) Laboratory Animal Science, 40, pp. 133-137; Barthold, S.W., Smith, A.L., Lord, P.F.S., Bhatt, P.N., Jacoby, R.O., Main, A.J., Epizootic coronaviral typhlocolitis in suckling mice (1982) Laboratory Animal Science, 32, pp. 376-383; Barthold, S.W., Smith, A.L., Povar, M.L., Enterotropic mouse hepatitis virus infection in nude mice (1985) Laboratory Animal Science, 35, pp. 613-618; Barthold, S.W., Beck, D.S., Smith, A.L., Mouse hepatitis virus and host determinants of vertical transmission and maternally-derived passive immunity in mice (1988) Archives of Virology, 100, pp. 171-183; Barthold, S.W., Beck, D.S., Smith, A.L., Enterotropic coronavirus (mouse hepatitis virus) in mice: Influence of host age and strain on infection and disease (1993) Laboratory Animal Science, 43, pp. 276-284; Biggers, D.C., Kraft, L.M., Sprinz, H., Lethal intestinal virus infection of mice (LIVIM) (1964) American Journal of Pathology, 45, pp. 413-422; Boorman, G.A., Luster, M.I., Dean, J.H., Peritoneal and macrophage alterations caused by naturally occurring mouse hepatitis virus (1982) American Journal of Pathology, 106, pp. 110-117; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Braunsteiner, H., Friend, C., Viral hepatitis associated with transplantable mouse leukemia. I. Acute hepatic manifestations following treatment with urethane or methylformamide (1954) Journal of Experimental Medicine, 100, pp. 665-677; Braunwald, J., Nonnenmacher, H., Pereira, C.A., Kirn, A., Increased susceptibility to mouse hepatitis virus type 3 (MHV3) infection induced by a hypercholesterolaemic diet with increased adsorption of MHV3 to primary hepatocyte cultures (1991) Research in Virology, 142, pp. 5-15; Brownstein, D.G., Barthold, S.W., Mouse hepatitis virus immunofluorescence in formalin- Or Bouin's-fixed tissue using trypsin digestion (1982) Laboratory Animal Science, 32, pp. 37-39; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) Journal of Virology, 53, pp. 834-840; Byrd, L.G., McDonald, A.H., Gold, L.G., Potter, M., Specific pathogen-free BALB/cAn mice are refractory to plasmacytoma induction by pristane (1991) Journal of Immunology, 147, pp. 3632-3637; Carrano, V., Barthold, S.W., Beck, D.L., Smith, A.L., Alteration of viral respiratory infections of mice by prior infection with mouse hepatitis virus (1984) Laboratory Animal Science, 34, pp. 573-576; Carthew, P., Lethal intestinal virus of infant mice is mouse hepatitis virus (1977) Veterinary Record, 101, p. 465; Carthew, P., Inhibition of the mitotic response in regenerating mouse liver during viral hepatitis (1981) Infection and Immunity, 33, pp. 641-642; Carthew, P., Wood, M.J., Kirby, C., Pathogenicity of mouse hepatitis virus for preimplantation mouse embryo (1985) Journal of Reproduction and Fertility, 73, pp. 207-213; Casebolt, D.B., Spalding, D.M., Schoeb, T.R., Lindsey, J.R., Suppression of immune response induction in Peyer's patch lymphoid cells from mice infected with mouse hepatitis virus (1987) Cellular Immunology, 109, pp. 97-103; Casebolt, D.B., Stephensen, C.B., Monoclonal antibody solution hybridization assay for detection of mouse hepatitis virus infection (1992) Journal of Clinical Microbiology, 30, pp. 608-612; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin. I. Isolation and biological properties of the virus (1949) Journal of Experimental Medicine, 90, pp. 181-194; Collins, M.J., Parker, J.C., Murine virus contaminants of leukemia viruses and transplantable tumors (1972) Journal of the National Cancer Institute, 49, pp. 1139-1143; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Compton, S.R., Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors (1994) Virology, 203, pp. 197-201; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Laboratory Animal Science, 43, pp. 15-28; Compton, S.R., Winograd, D.F., Gaertner, D.J., Optimization of in vitro growth conditions for enterotropic murine coronavirus strains (1995) Journal of Virological Methods, 52, pp. 301-307; Cook-Mills, J.M., Munshi, H.G., Perlman, R.L., Chambers, D.A., Mouse hepatitis virus infection suppresses modulation of mouse spleen T-cell activation (1992) Immunology, 75, pp. 542-545; Coutelier, J.P., Van Der Logt, J.T., Heessen, F.W., IgG subclass distribution of primary and secondary immune responses concomitant with viral infection (1991) Journal of Immunology, 147, pp. 1383-1386; Cray, C., Mateo, M.O., Altman, N.H., In vitro and long-term in vivo immune dysfunction after infection of BALB/c mice with mouse hepatitis virus strain A59 (1993) Laboratory Animal Science, 43, pp. 169-174; David-Ferreira, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) Journal of Cell Biology, 24, pp. 57-78; Dempsey, W.L., Smith, A.L., Morahan, P.S., Effect of inapparent murine hepatitis virus infections on macrophages and host resistance (1986) Journal of Leukocyte Biology, 39, pp. 559-565; De Souza, M.S., Smith, A.L., Comparison of isolation in cell cultures with conventional and modified mouse antibody production tests for detection of murine viruses (1989) Journal of Clinical Microbiology, 27, pp. 185-187; Dick, G.W.A., Nivenand, J.S.F., Gledhill, A.W., Virus related to that causing hepatitis in mice (MHV) (1956) British Journal of Experimental Pathology, 37, pp. 90-98; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) Journal of Virology, 65, pp. 6881-6891; Fallon, M.T., Benjamin Jr., W.H., Schoeb, T.R., Briles, D.E., Mouse hepatitis virus strain UAB infection enhances resistance to Salmonella typhimurium in mice by inducing suppression of bacterial growth (1991) Infection and Immunity, 59, pp. 852-856; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Fox, J.G., Murphy, J.C., Igras, V.E., Adverse effects of mouse hepatitis virus on ascites myeloma passage in the BALB/c mouse (1977) Laboratory Animal Science, 27, pp. 173-179; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) Journal of Virology, 64, pp. 731-741","Homberger, F.R.; Institute Laboratory Animal Science, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland; email: frhom@ltk.unizh.ch",,"SAGE Publications Ltd",00236772,,LBANA,"9175007","English","LAB. ANIM.",Review,"Final",Open Access,Scopus,2-s2.0-0030994929
"Brown T.P., Garcia A.P., Kelley L.","7404319500;57201080947;7102317869;","Spiking mortality of turkey poults: 1. Experimental reproduction in isolation facilities",1997,"Avian Diseases","41","3",,"604","609",,22,"10.2307/1592151","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031194794&doi=10.2307%2f1592151&partnerID=40&md5=1d408b4e121962f0f6bb5bbf6da91809","Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States","Brown, T.P., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Garcia, A.P., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States; Kelley, L., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States","Spiking mortality of turkeys (SMT) is an infectious disease of 5-to-25-day-old turkey poults characterized by acute enteritis and bursal and thymic atrophy. Brooding 1-day-old poults on litter taken from naturally occurring cases successfully reproduced SMT 5 days postexposure. Oral exposure to an organ homogenate made of tissue samples from naturally occurring cases successfully reproduced SMT 5 days postinoculation. Coronaviruses were present in intestinal and bursal contents taken from poults with naturally occurring SMT. They were also present 5 days after exposure in the experimentally reproduced disease. Severe intestinal villus atrophy, bursal follicular lymphoid depletion, and thymic cortical atrophy were present histologically in naturally occurring SMT and in SMT reproduced by either experimental method.",,"Animalia; Aves; Coronavirus; Meleagris gallopavo","Brown, T.P., Glisson, J.R., Villegas, P.V., Acute enteritis as a cause of ""spiking mortality"" in young turkey poults (1992) Proc. 3rd Eli Lilly Turkey Technical Seminar, pp. 20-29. , Nashville, TN. May 8-10; Brown, T.P., Gobble, H., Williams, M.E., Lesions induced in sentinel birds placed in turkey flocks affected with acute enteritis/immunosuppression syndrome (1993) Proc. SmithKline Beecham Pacesetter Conference and National Turkey Federation Annual Meeting, , Newport Beach, CA. January 11-13; Brown, T.P., Howell, D.R., Garcia, A.P., Adult cattle as inapparent carriers of spiking mortality of turkeys (1996) 133rd Annual Meeting of American Veterinary Medical Association, p. 373. , Louisville, KY; Brown, T.P., Howell, D.R., Garcia, A.P., Villegas, P., Histologic lesions of spiking mortality of turkeys: Comparison of lesions induced by SMT organ suspension and cell culture (1996) 133rd Annual Meeting of American Veterinary Medical Association, p. 373. , Louisville, KY; Dea, S., Tijssen, P., Viral agents associated with outbreaks of diarrhea in turkey flocks in Quebec, Canada (1988) J. Vet. Res., 52, pp. 53-57; Dea, S., Verbeek, A., Tijssen, P., Transmissible enteritis of turkeys: Experimental inoculation studies with tissue-culture-adapted turkey and bovine coronaviruses (1991) Avian Dis., 35, pp. 767-777; Ficken, M.D., Wages, D.P., Guy, J.S., Quinn, J.A., Emory, W.H., High mortality of domestic turkeys associated with Highlands J virus and eastern equine encephalitis virus (1993) Avian Dis., 37, pp. 585-590; Garcia, A.P., Brown, T.P., Villegas, P.N., Steffens, W.L., Turkey enteric coronaviruses: Ultrastructural changes and indirect immunofluorescence in HRT-18 cells (1996) 133rd Annual Meeting of American Veterinary Medical Association, p. 372. , Louisville, KY; Gonder, E., Patel, B.L., Pomeroy, B.S., Scanning, light, and immunofluorescent microscopy of coronaviral enteritis of turkeys (bluecomb) Am. J. Vet. Res., 37, pp. 1435-1439; Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis/spiking mortality (1995) Avian Pathol., 24, pp. 497-505; Naqi, S.A., Panigrahy, B., Hall, C.F., Bursa of Fabricius, a source of bluecomb infectious agent (1972) Avian Dis., 16, pp. 937-939; Patel, B.L., Gonder, E., Pomeroy, B.S., Detection of turkey coronaviral enteritis (bluecomb) in field epiornithics, using the direct and indirect fluorescent antibody tests (1977) Am. J. Vet. Res., 38, pp. 1407-1411; Perry, R.W., Rowland, G.N., Glisson, J.R., Poult malabsorption syndrome. I. Malabsorption in poult enteritis (1991) Avian Dis., 35, pp. 685-693; Reynolds, D.L., Saif, Y.M., Theil, K.W., A survey of enteric viruses of turkey poults (1987) Avian Dis., 31, pp. 89-98; Ritchie, A.E., Deshmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of corona-virus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; Yason, C.V., Summers, B.A., Schat, K.A., Pathogenesis of rotavirus infection in various age groups of chickens and turkeys: Pathology (1987) Am. J. Vet. Res., 48, pp. 927-938","Brown, T.P.; Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA 30602, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"9356706","English","AVIAN DIS.",Article,"Final",,Scopus,2-s2.0-0031194794
"Kohara J., Hirai T., Mori K., Ishizaki H., Tsunemitsu H.","8667530400;7402768699;55470482600;57213510422;7004628959;","Enhancement of Passive Immunity with Maternal Vaccine against Newborn Calf Diarrhea",1997,"Journal of Veterinary Medical Science","59","11",,"1023","1025",,19,"10.1292/jvms.59.1023","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031262438&doi=10.1292%2fjvms.59.1023&partnerID=40&md5=7d799a13216f43829763e6195a93a234","Shintoku Anim. Husbandary Exp. Stn., Shintoku, Hokkaido 081, Japan; Dept. of Veterinary Microbiology, Obihiro Univ. Agric. and Vet. Med., Inada-cho, Obihiro, Hokkaido 080, Japan; Hokkaido Research Station, National Institute of Animal Health, Hitsujigaoka 4, Toyohira, Sapporo, Hokkaido 062, Japan; Animal Hygiene Laboratory, Department of Grazing Production, Natl. Grassland Research Institute, Nishinasuno, Tochigi 329-27, Japan","Kohara, J., Shintoku Anim. Husbandary Exp. Stn., Shintoku, Hokkaido 081, Japan; Hirai, T., Shintoku Anim. Husbandary Exp. Stn., Shintoku, Hokkaido 081, Japan; Mori, K., Shintoku Anim. Husbandary Exp. Stn., Shintoku, Hokkaido 081, Japan; Ishizaki, H., Dept. of Veterinary Microbiology, Obihiro Univ. Agric. and Vet. Med., Inada-cho, Obihiro, Hokkaido 080, Japan, Animal Hygiene Laboratory, Department of Grazing Production, Natl. Grassland Research Institute, Nishinasuno, Tochigi 329-27, Japan; Tsunemitsu, H., Hokkaido Research Station, National Institute of Animal Health, Hitsujigaoka 4, Toyohira, Sapporo, Hokkaido 062, Japan","The effects of a maternal vaccine against newborn calf diarrhea associated with group A bovine rotavirus (BRV), bovine coronavirus (BCV), bovine parvovirus and K99 Escherichia coli (E.coli) were examined on a beef cow-calf herd. After vaccination, serum or colostrum antibody titers to BRV, BCV and E. coli K99 in the vaccinated cows were significantly higher than those in unvaccinated control cows. Serum antibody titers to BRV, BCV and E. coli K99 in calves from the vaccinated cows were also significantly higher than those in calves from the control cows for 3-4 weeks after birth. These results suggested that the immunization of cows with the maternal vaccine enhanced the passive immunity levels in calves against BRV, BCV and K99 E. coli.","Bovine coronavirus; Bovine rolavirus; K99 Escherichia coli","bacterium antibody; virus antibody; animal; animal disease; article; cattle; cattle disease; colostrum; diarrhea; Enterobacter infection; female; immunology; newborn; passive immunization; pregnancy; serodiagnosis; virus infection; Animals; Animals, Newborn; Antibodies, Bacterial; Antibodies, Viral; Cattle; Cattle Diseases; Colostrum; Coronavirus Infections; Diarrhea; Escherichia coli Infections; Female; Immunity, Maternally-Acquired; Immunization, Passive; Neutralization Tests; Parvoviridae Infections; Pregnancy; Rotavirus Infections","Acres, S.D., Isaacson, R.E., Babiuk, L.A., Kapitany, R.A., (1979) Infect. Immun., 25, pp. 121-126; Durham, P.J.K., Hassard, L.E., Norman, G.R., Yemen, R.L., (1989) Can. Vet. J., 30, pp. 876-881; House, J.A., (1978) J. Am. Vet. Med. Assoc., 173, pp. 573-576; Ishizaki, H., Sakai, T., Shirahata, T., Taniguchi, K., Urasawa, T., Urasawa, S., Goto, H., (1996) Vet. Microbiol., 48, pp. 367-372; Mebus, C.A., White, R.G., Bass, E.P., Twiehaus, M.J., (1973) J. Am. Vet. Med. Assoc., 163, pp. 880-883; Moon, H.W., McClurkin, A.W., Isaacson, R.E., Pohlenz, J., Skartvedt, S.M., Gillette, K.G., Baetz, A.L., (1978) J. Am. Vet. Med. Assoc, 173, pp. 577-583; Myers, L.L., Snodgrass, D.R., (1982) J. Am. Vet. Med. Assoc., 181, pp. 486-488; Ohashi, S., Shiba, F., Haga, Y., Ajito, T., Yamada, Y., Nemoto, H., Motoyoshi, S., (1990) Bull. Nippon Vet. Zootech. Coll., 39, pp. 40-49; Ojeh, C.K., Jiang, B.M., Tsunemitsu, H., Kang, S.Y., Weilnau, P.A., Saif, L.J., (1991) J. Clin. Microbiol., 29, pp. 2051-2055; Saif, L., Redman, D.R., Smith, K.L., Theil, K.W., (1983) Infect. Immun., 41, pp. 1118-1131; Saif, L.J., Smith, K.L., Landmeier, B.J., Bohl, E.H., Theil, K.W., (1984) Am. J. Vet. Res., 45, pp. 49-58; Saif, L.J., Smith, K.L., (1985) J. Dairy Sci., 68, pp. 206-228; Snodgrass, D.R., Wells, P.W., (1978) J. Am. Vet. Med. Assoc., 173, pp. 565-568; Snodgrass, D.R., (1982) Res. Vet. Sci., 32, pp. 70-73; Spahn, G.J., Mohanty, S.B., Hetrick, F.M., (1966) Cornell Vet., 56, pp. 377-386; Suzuki, Y., Sanekata, T., Sato, M., Tajima, K., Matsuda, Y., Nakagomi, O., (1993) J. Clin. Microbiol., 31, pp. 3046-3049; Thunber, E.T., Bass, E.P., Beckenhauer, W.H., (1977) Can. J. Camp. Med., 41, pp. 131-136; Tsunemitsu, H., Shimizu, M., Hirai, T., Yonemichi, H., Kudo, T., Mori, K., Onoe, S., (1988) Jpn. J. Vet. Sci., 51, pp. 300-308; Tsunemitsu, H., Yonemichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., (1991) J. Vet. Med. Sci., 53, pp. 433-437; Wieda, J., Bengelsdorff, H.J., Hungerer, K.D., (1987) J. Vet. Med. B, 34, pp. 495-503; Woode, G.N., Jones, J., Bridger, J., (1975) Vet. Rec., 97, pp. 148-149","Kohara, J.; Shintoku Anim. Husbandary Exp. Stn., Shintoku, Hokkaido 081, Japan",,"Maruzen Co. Ltd.",09167250,,,"9409518","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0031262438
"Jacas J.A., Budia F., Rodríguez-Cerezo E., Viñuela E.","7004032401;6603185865;57205071504;7006098374;","Virus-like particles in the poison gland of the parasitic wasp Opius concolor",1997,"Annals of Applied Biology","130","3",,"587","592",,21,"10.1111/j.1744-7348.1997.tb07685.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030821777&doi=10.1111%2fj.1744-7348.1997.tb07685.x&partnerID=40&md5=748e45661f7b09d436500b03476d363f","U. de Protectión de Cultivas, ETSI Agrónomos, Univ. Politécnica de Madrid, E-28040 Madrid, Spain; Ctro. Natl. de Biotecnología, CSIC, E-28049 Canto Blanco, Spain; Dept. de Proteccio Veg. i B., Inst. Valencia d'Investigacions A., E-46113 Montcada, Spain","Jacas, J.A., U. de Protectión de Cultivas, ETSI Agrónomos, Univ. Politécnica de Madrid, E-28040 Madrid, Spain, Dept. de Proteccio Veg. i B., Inst. Valencia d'Investigacions A., E-46113 Montcada, Spain; Budia, F., U. de Protectión de Cultivas, ETSI Agrónomos, Univ. Politécnica de Madrid, E-28040 Madrid, Spain; Rodríguez-Cerezo, E., Ctro. Natl. de Biotecnología, CSIC, E-28049 Canto Blanco, Spain; Viñuela, E., U. de Protectión de Cultivas, ETSI Agrónomos, Univ. Politécnica de Madrid, E-28040 Madrid, Spain","Virus-like particles (VLP's) have been found in the poison glands of adult females of the parasitic wasp Opius concolor Szepl. (Hymenoptera, Braconidae). These VLP's are found in the secretory cells either free in the cytoplasm or within cytoplasmic vesicles, sometimes associated to a secretory apparatus. Negative staining of these VLP's has revealed the occurrence of two different particles. The first type exhibits icosahedral symmetry (diameter around 70 nm) and hollow surface spikes, this morphology being typical of the genus Cypovirus (Reoviridae). The other type is pleomorphic and presents an envelope with club-shaped projections (diameter ranging from 30 to 60 nm), as classical textbook examples of Coronaviruses, but smaller. Function and full characterisation of these particles are not yet known.","Braconidae; Corona-like virus; Opius concolor; Parasitoid virus; Poison gland; Reo-like virus","Braconidae; Cypovirus; Hymenoptera; Opius; Opius concolor; Opius concolor; Reoviridae; Reovirus sp.; Vespidae","Cavanagh, D., Brain, D.A., Brighton, M.A., Enjuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Coronaviridae (1995) Archives of Virology, 10 (SUPPL.), pp. 407-411. , Virus Taxonomy - 6th report of the International Committee on Taxonomy of Viruses. Eds F A Murphy, C M Fauquet, DHL Bishop, S A Ghabrial, A W Jarvis, G P Martelli, M A Mayo and M D Summers; Edson, K.M., Virus-like and membrane-bound particles in the venom apparatus of a parasitoid wasp (Hymenoptera: Braconidae) (1981) Proceedings of the 39th Annual Electron Microscopy Society of America, pp. 610-611. , Ed. G W Bailey. Baton Rouge, Los Angeles, USA: Claitors Publishing Division","Jacas, J.A.; DPVB, IVIA, E-46113 Montcada, Spain; email: jjacas@ivia.es",,"Blackwell Publishing Ltd",00034746,,AABIA,,"English","ANN. APP. BIOL.",Article,"Final",,Scopus,2-s2.0-0030821777
"Laurenson K., Van Heerden J., Stander P., Van Vuuren M.J.","6603505450;7201441435;6701669975;7004572625;","Seroepidemiological survey of sympatric domestic and wild dogs (Lycaon pictus) in Tsumkwe District, north-eastern Namibia",1997,"Onderstepoort Journal of Veterinary Research","64","4",,"313","316",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031317846&partnerID=40&md5=349aa7b00ea6c84d4d15d2b38de59ddb","Vet. Informatics and Epidemiology, Univ. of Glasgow Veterinary School, Bearsden Road, Glasgow G61 1QH, United Kingdom; Price Forbes Chair for Wildl. Dis., University of Pretoria, Faculty of Veterinary Science, Private Bag X4, Onderstepoort, 0110, South Africa; Ministry of Environment and Tourism, P.O. Box 6213, Windhoek, Namibia; Dept. of Vet. Tropical Diseases, University of Pretoria, Faculty of Veterinary Science, Private Bag X4, Onderstepoort, 0110, South Africa","Laurenson, K., Vet. Informatics and Epidemiology, Univ. of Glasgow Veterinary School, Bearsden Road, Glasgow G61 1QH, United Kingdom; Van Heerden, J., Price Forbes Chair for Wildl. Dis., University of Pretoria, Faculty of Veterinary Science, Private Bag X4, Onderstepoort, 0110, South Africa; Stander, P., Ministry of Environment and Tourism, P.O. Box 6213, Windhoek, Namibia; Van Vuuren, M.J., Dept. of Vet. Tropical Diseases, University of Pretoria, Faculty of Veterinary Science, Private Bag X4, Onderstepoort, 0110, South Africa","Disease is a potential threat to many endangered populations and may originate from sympatric domestic species. This paper describes a cross-sectional serological survey of canine pathogens carried out in domestic (n = 70) and wild dogs (Lycoan pictus) (n = 6), in Tsumkwe District, north-eastern Namibia. Evidence of past exposure to canine distemper virus, canine adenovirus and parainfluenza virus was evident in both wild and domestic dogs with this, the first, documented exposure of free-living wild dogs to canine distemper. Domestic dogs were also exposed to rabies virus, canine parvovirus and coronavirus. There was no pathogen to which wild dogs, but not domestic dogs, were exposed. With wild dogs known to be susceptible to rabies and canine distemper, these may be the greatest threat to this population of wild dogs, although some wild dogs can clearly survive infection with canine distemper.","Canine pathogens; Domestic dogs; Lycoan pictus; Seroepidemiological survey; Sympatric; Virus; Wild dogs","Adenoviridae; Canine adenovirus; Canine distemper virus; Canine parvovirus; Canis familiaris; Canis lupus; Coronavirus; distemper virus; Lycaon pictus; Rabies virus; virus antibody; Adenovirus; animal; animal disease; article; blood; Canine distemper morbillivirus; Carnivora; Coronavirus; cross-sectional study; dog; dog disease; epidemiology; isolation and purification; Namibia; Parvovirus; Rabies virus; Rotavirus; virology; virus infection; Adenoviruses, Canine; Animals; Antibodies, Viral; Carnivora; Coronavirus, Canine; Cross-Sectional Studies; Distemper Virus, Canine; Dog Diseases; Dogs; Namibia; Parvovirus, Canine; Rabies virus; Rotavirus; Seroepidemiologic Studies; Virus Diseases","Alexander, K.A., Smith, J.S., Macharia, M.J., King, A.A., Rabies in the Masai Mara, Kenya: Preliminary results (1993) Onderstepoort Journal of Veterinary Research, 60, pp. 411-414; Alexander, K.A., Appel, M.J.G., African wild dogs (Lycaon pictus) endangered by a canine distemper epizootic among domestic dogs near the Masasi Mara national reserve Kenya (1994) Journal of Wildlife Diseases, 30, pp. 481-485; Anderson, R.M., May, R.M., Population biology of infectious diseases. 1 (1979) Nature, 280, pp. 361-367; Cleaveland, Dye, Maintenance of a microparasite infecting several host species; rabies in the Serengeti (1995) Parasitology, 111, pp. S33-47; Creel, S., Creel, N.M., Matovelo, J.A., Mtambo, M.M.A., Batamuzi, E.K., Cooper, J.E., The effects of anthrax on endangered African wild dogs (Lycaon pictus) (1995) Journal of Zoology, 236, pp. 199-209. , London; Esterhuysen, J., Thomson, G.R., Prehaud, C., A liquid-phase blocking ELISA for the detection of antibodies to rabies virus (1995) Journal of Virological Methods, 51, pp. 31-42; Fanshawe, J.H., Frame, L.H., Ginsberg, J.R., The Africa wild dog; Africa's vanishing carnivore (1991) Oryx, 25, pp. 137-146; Gascoyne, S.C., Laurenson, M.K., Lelo, S., Borner, M., Rabies in African wild dogs (Lycaon pictus) in the Serengeti region, Tanzania (1993) Journal of Wildlife Diseases, 29, pp. 396-402; Laurenson, M.K., Esterhuysen, J., Stander, P., Van Heerden, J., Aspects of rabies epidemiology in Tsumkwe District, Namibia (1997) Onderstepoort Journal of Veterinary Research, 64, pp. 39-45; Malcolm, J.R., (1979) Social Organization and Communal Rearing in African Wild Dogs, , Ph.D. thesis. Harvard University; McCallum, H., Dobson, A.P., Detecting disease and parasite threats to endangered species and ecosystems (1995) Tree, 10, pp. 190-193; McCormick, A.E., Canine distemper in African hunting dogs (Lycaon pictus) - Possibly vaccine induced (1983) Journal of Zoo Animal Medicine, 14, pp. 66-71; Reich, A., An ounce of extinction (1979) African Wildlife, 33, pp. 29-31; Schaller, G.B., (1972) The Serengeti Lion: A Study of Predator-prey Relations, pp. 321-344. , Chicago, Illinois: University of Chicago Press; Stander, P., Tsusaba, D., Ghau, Txoma, Iui, I., Kaqece, Nisa, Haden, P., (1994) Ecology and Conservation of Large Carnivores and Some Ungulate Species in Bushmanland and Kaudom Game Reserve, Namibia, , Final Report, Ministry of Environment and Tourism, Namibia; Stander, P., Ghau, Tsisaba, D., Txoma, A new method of darting: Stepping back in time (1995) African Journal of Ecology, 34, pp. 48-53; Turnbull, P.C., Bell, R.H.V., Saigawa, K., Munyenyembem, F.H.C., Mulenga, C.K., Makal, L.H.C., Anthrax in wildlife in Luangwa Valley, Zambia (1991) Veterinary Record, 128, pp. 399-403; Van Heerden, J., Bainbridge, N., Burroughs, R.E.J., Kriek, N.P.J., Distemper-like disease and encephalitis in wild dogs (Lycaon pictus) (1989) Journal of Wildlife Diseases, 25, pp. 70-75","Laurenson, K.; Vet. Informatics and Epidemiology, Univ. of Glasgow Veterinary School, Bearsden Road, Glasgow G61 1QH, United Kingdom",,"AOSIS (pty) Ltd",00302465,,,"9551484","English","Onderstepoort J. Vet. Res.",Review,"Final",,Scopus,2-s2.0-0031317846
"Wang H.N., Wu Q.Z., Huang Y., Liu P.","57196433706;56284881000;57206438661;55038506500;","Isolation and identification of infectious bronchitis virus from chickens in Sichuan, China",1997,"Avian Diseases","41","2",,"279","282",,25,"10.2307/1592178","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031127406&doi=10.2307%2f1592178&partnerID=40&md5=4cbec2da78e73fef00065fea7d89a61f","Coll. of Anim. Sci. and Technology, Sichuan Agricultural University, Yaan, Sichuan, 625014, China","Wang, H.N., Coll. of Anim. Sci. and Technology, Sichuan Agricultural University, Yaan, Sichuan, 625014, China; Wu, Q.Z., Coll. of Anim. Sci. and Technology, Sichuan Agricultural University, Yaan, Sichuan, 625014, China; Huang, Y., Coll. of Anim. Sci. and Technology, Sichuan Agricultural University, Yaan, Sichuan, 625014, China; Liu, P., Coll. of Anim. Sci. and Technology, Sichuan Agricultural University, Yaan, Sichuan, 625014, China","A nonhemagglutinating virus was isolated from kidneys and lungs of chickens suspected of having infectious bronchitis infection. Specific-pathogen-free embryonated chicken eggs were used as the cultural system. With the use of the ciliary activity of chicken embryo tracheal organ cultures as indicator system, the physicochemical properties of one of the isolated strains (SAIB(i)) were shown to be similar to infectious bronchitis virus (IBV) strain M41 (standard strain); whereas electron microscopy of the isolate showed coronavirus particles. Virus-neutralization tests were performed in tracheal organ cultures to compare the serotypes of five IBV isolates and six known IBV strains on the basis of reciprocal neutralization titers and euclidean distance. The cross-neutralization pattern indicated that one isolate was of the T-strain IBV serotype, another of the M41 IBV serotype, while others had partial serotype relationship to M41 and T-strains of IBV.",,"Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Gallus gallus","Cavanagh, D., Davis, P.J., Cook, J.K.A., Infectious bronchitis virus: Evidence for recombination within the Massachusetts serocype (1992) Avian Pathol., 21, pp. 401-408; Cook, J.K., Darbyshire, J.H., The use of chicken tracheal organ cultures for the isolation and assay of avian infectious bronchitis virus (1976) Arch. Virol., 50, pp. 109-118; Darbyshire, J.H., Rowell, J.G., Cook, J.K.A., Peters, R.W., Taxonomic studies on strains of avian infectious bronchitis virus using neutralization test in tracheal organ cultures (1979) Arch. Virol., 61, pp. 227-238; King, D.J., Cavanagh, D., Infectious bronchitis (1991) Diseases of Poultry, 9th Ed., pp. 471-484. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoder, eds. Iowa State University Press, Ames, Iowa; Meulemans, G., Carlier, M.C., Gonze, M., Petit, P., Vandenbroeck, M., Incidence, characterization, and prophylaxis of nephropathogenic avian infectious bronchitis virus (1987) Vet. Rec., 120, pp. 205-206; Reed, L.J., Muench, H., A simple method of estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Schalk, A.F., Hawn, M.C., An apparently new respiratory disease of baby chicks (1931) J. Am. Vet. Med. Assoc., 78, pp. 413-422","Wang, H.N.; College of Animal Science/Technology, Sichuan Agricultural University, Yaan, Sichuan 625014, China",,"American Association of Avian Pathologists",00052086,,AVDIA,"9201388","English","AVIAN DIS.",Article,"Final",,Scopus,2-s2.0-0031127406
"Bouda J., Doubek J., Medina-Cruz M., Paasch M L., Candanosa A E., Dvořák R., Soška V.","7006191160;6701830711;7801548495;6504308554;6504444014;7006751036;7003895340;","Pathophysiology of severe diarrhoea and suggested intravenous fluid therapy in calves of different ages under field conditions",1997,"Acta Veterinaria Brno","66","2",,"87","94",,2,"10.2754/avb199766020087","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031488083&doi=10.2754%2favb199766020087&partnerID=40&md5=45abb3501ec92d1f4a1c17d41a9e380c","Department of Clinical Diagnosis, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Department of Pathophysiology, Univ. Vet. and Pharmaceutical Sci., 612 42, Brno, Czech Republic; Dept. of Dis. and Prod. of Ruminants, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Clinic of Ruminant Disease, Faculty of Veterinary Medicine, Univ. Vet. and Pharmaceutical Sci., 612 42, Brno, Czech Republic; Department of Clinical Biochemistry, University Hospital, Masaryk University Brno, Czech Republic","Bouda, J., Department of Clinical Diagnosis, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Doubek, J., Department of Pathophysiology, Univ. Vet. and Pharmaceutical Sci., 612 42, Brno, Czech Republic; Medina-Cruz, M., Dept. of Dis. and Prod. of Ruminants, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Paasch M, L., Department of Clinical Diagnosis, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Candanosa A, E., Department of Clinical Diagnosis, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico; Dvořák, R., Clinic of Ruminant Disease, Faculty of Veterinary Medicine, Univ. Vet. and Pharmaceutical Sci., 612 42, Brno, Czech Republic; Soška, V., Department of Clinical Biochemistry, University Hospital, Masaryk University Brno, Czech Republic","Selected clinical and biochemical variables were studied in 2 groups of severely dehydrated, diarrhoeic calves before and after fluid therapy. Group 1 (n = 10) included calves aged 2 to 7 d, Group 2 (n = 9) calves aged 8 to 14 d. Clinical examination and blood sampling for biochemical and haematological analyses were performed in each animal before and after fluid therapy. Samples of faeces for microbiological examination were taken before intravenous (IV) rehydration. Solutions used for IV rehydration contained salts of NaCl, NaHCO3, KCl and glucose in different quantities for calves in Groups 1 and 2. These rehydration solutions were infused IV at a volume of 41 to each calf during 3 hours and then followed by oral rehydration. In Group 1, rotavirus in faeces was diagnosed in 50.0% of all calves; combined infectious agents rotavirus and Cryptosporidium spp. occurred in 10.0%, none of the calves had in faeces coronavirus, enteretoxigenic E. coli K99 and Salmonella spp.; that means in 40% of calves of this group no infectious agents were isolated. In Group 2, coronavirus was found in 11.1%, combined infectious agents rotavirus and Cryptosporidium spp. were diagnosed in 55.5%, none of the calves had enterotoxigenic E. coli K99 or Salmonella spp in faeces. Before IV rehydration diarrhoeic calves in Group 2 presented mean blood values of pH 7.12, base excess (BE) -14.72 mmol/l, standard bicarbonate (SB) 9.86 mmol/l which were significantly lower (P&lt;0.05) than in calves in Group 1 before IV rehydration, where pH was 7.16, BE -11.68 mmol/l and SB 12.54 mmol/l. In both groups of calves before IV rehydration these low values of blood pH, BE, SB and normal value of pCO2, corresponded to partially compensated metabolic acidosis. The differences in blood values of pH, BE, SB, PCV, urea and K in both groups before and after rehydration were significant (P&lt;0.01). The metabolic acidosis together with hyperkalemia, prerenal uremia and haemoconcentration were restored after fluid therapy. Rehydration was successful in 79.0% of all diarrhoeic calves. Calves aged 8 d or older suffering from severe diarrhoea needed more bicarbonate for IV rehydration than diarrhoeic calves younger than 8 d. The suggested composition and volume of solutions for IV rehydration used in this study simplify fluid therapy in severely diarrhoeic calves of different ages in lateral or sternal recumbency without suckling reflex and under field conditions.","Calf; Dehydration; Fluid therapy; Hyperkalemia; Metabolic acidosis; Neonatal diarrhoea; Packed cell volume; Uremia",,"Acres, S.D., Enterotoxigenic Escherichia coli infection in newborn calves (1985) J. Dairy Sci., 68, pp. 229-256; Acres, S.D., Saunders, J., Radostits, O.M., Acute undifferentiated neonatal diarrhea of beef calves: The prevalence of enterotoxigenic E. coli, reo-like (rota) virus and other enteropathogens in cow-calf herds (1977) Can. Vet. J., 18, pp. 113-121; Argenzio, R.A., Pathophysiology of neonatal calf diarrhea (1985) Vet. Clin. North Am. (Food Anim. Pract), 1, pp. 461-469; Bouda, J., Doubek, J., Toth, J., Klimeš, J., Hrušková, M., Příspěvek k etiopatogenezi a léčbě průjmových onemocnění telat (1990) Veterinářství, 40, pp. 292-294; Bouda, J., Doubek, J., Toth, J., Průjmová onemocnění telat. Nové poznatky v rehydratační léčbě (1994) Veterinářství, 44, pp. 103-106; Bouda, J., Jagoš, P., Biochemical and hematological reference values in calves and their significance for health control (1984) Acta Vet. Brno, 53, pp. 137-142; Bouda, J., Jagoš, P., Disorders in the acid-base balance (1991) Metabolic Disorders and Their Prevention in Farm Animals, pp. 248-268. , Vrzgula L: Elsevier, Amsterdam; Bywater, R.J., Evaluation of an oral glucose-glycine-electrolyte formulation and amoxicillin for treatment of diarrhea in calves (1977) Am. J. Vet. Res., 38, pp. 1983-1987; Bywater, R.J., Logan, E.F., The site and characteristics of intestinal water and electrolyte loss in Escherichia coli-induced diarrhoea in calves (1974) J. Comp. Pathol., 84, pp. 599-610; Fromm, D., Gianella, R.A., Formal, S.B., Ion transport across isolated ileal mucosa invaded by Salmonella (1974) Gastroenterology, 66, pp. 215-225; Jagoš, P., Bouda, J., Přikrylová, J., Dynamika acidobazických změn venózní krve skotu in vitro v závislosti na čase (1977) Vet. Med., 22, pp. 257-260. , Praha; Kasari, T.R., Metabolic acidosis in diarrheic calves: The importance of alkalinizing agents in therapy (1990) Vet. Clin. North Am. (Food Anim Pract.), 6, pp. 29-43; Lewis, L.D., Phillips, R.W., Water and electrolyte losses in neonatal calves with acute diarrhea. A complete balance study (1972) Cornell Vet., 62, pp. 596-607; Mebus, C.A., Stair, E.L., Rhodes, M.B., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet. Pathol., 10, pp. 45-64; McGuirk, S.M., Neonatal calf management: A guide to disease investigation (1996) Proceedings of the XIXth World Buiatrics Congress, pp. 89-92. , Edinburgh; Medina, C.M., (1994) Medicina Productiva en la Crianza de Becerras Lecheras, 325p. , Limusa. D.F., México; Meltzer, R., Shpigel, N.Y., Etiologic and epidemiologic aspects of calf diarrhoea in Israeli dairy farms (1996) Proceedings of the XIXth World Buiatrics Congress, pp. 93-97. , Edinburgh; Michell, A.R., Bywater, R.J., Clarke, K.W., Hall, L.W., Waterman, A.E., (1989) Veterinary Fluid Therapy, 312p. , Blackwell Scientific Publications, Oxford; Moon, H.W., Mechanisms in the pathogenesis of diarrhea: A review (1978) J. Am. Vet. Med. Assoc., 172, pp. 443-448; Naylor, J.M., Severity and nature of acidosis in diarrheic calves over and under one week of age (1987) Can. Vet. J., 28, pp. 168-173; Naylor, J.M., Neonatal ruminant diarrhea (1996) Large Animal Internal Medicine, pp. 396-417. , Smith B. P.: Mosby, St. Louis; Radostits, O.M., Blood, D.C., Gay, C.C., (1994) Veterinary Medicine. A Textbook of the Diseases of Cattle, Sheep, Pigs, Goats and Horses. 8th Edition, , Baillière Tindall, London; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in Southern Britain (1986) Vet. Rec., 119, pp. 34-39; Roussel, A.J., Kasari, T.R., Using fluid and electrolyte replacement therapy to help diarrheic calves (1990) Vet. Med., 85, pp. 303-311; Salajka, E., Ulmann, L., Prospects of specific prevention and treatment of diarrhoeic E. coli infections in calves in the early postnatal period Acta Vet. Brno (Suppl. 2), 40, pp. 83-86; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Woode, G.N., Smith, C., Dennis, M.J., Intestinal damage in rotavirus infected calves assessed by D-xylose malabsorption (1978) Vet. Rec., 102, pp. 340-341","Bouda, J.; Department of Clinical Diagnosis, College of Veterinary Medicine, Natl. Autonomous Univ. of Mexico, 04510 Mexico, D. F., Mexico",,"University of Veterinary and Pharmaceutical Sciences",00017213,,,,"English","Acta Vet. Brno",Article,"Final",Open Access,Scopus,2-s2.0-0031488083
"Hansen A.K., Farlov H., Bollen P.","7401928543;13808137100;6603704522;","Microbiological monitoring of laboratory pigs",1997,"Laboratory Animals","31","3",,"193","200",,18,"10.1258/002367797780596248","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030759809&doi=10.1258%2f002367797780596248&partnerID=40&md5=4938639e6674041748e377652de66d93","Department of Experimental Medicine, University of Copenhagen, National University Hospital, Blegdamsvej 3B, DK-2200 Copenhagen N, Denmark; Ellegaard Göttingen Minipigs, Soro Landevej 302, DK-4261 Dalmose, Denmark","Hansen, A.K., Department of Experimental Medicine, University of Copenhagen, National University Hospital, Blegdamsvej 3B, DK-2200 Copenhagen N, Denmark; Farlov, H., Department of Experimental Medicine, University of Copenhagen, National University Hospital, Blegdamsvej 3B, DK-2200 Copenhagen N, Denmark; Bollen, P., Ellegaard Göttingen Minipigs, Soro Landevej 302, DK-4261 Dalmose, Denmark","Purpose-bred minipigs, are often used as the non-rodent species in toxicology. Infections may interfere with animal experiments, and there are no scientific reasons why the non-rodent species should be of a lower microbiological quality than the rodent species. Therefore, a system for health monitoring of pigs was developed in order to raise the quality of laboratory pigs to the level of laboratory rodents. This system, which includes screening for several viruses, bacteria and ecto- and endoparasites, was used for monitoring minipigs from a barrier unit with the same standards applied to rodents units. In these pigs only rotaviruses are found, which was shown by both serological antibody detection and by detection of rotaviral antigen in faeces. In minipigs from another unit with far less hygienic protection rotaviruses were also found along with certain influenza- and coronaviruses, as well as Pasteurella spp. It is concluded, that it is possible to raise pigs of a microbiological quality comparable to the quality of rats and mice, and that advanced microbiological monitoring in pigs will reveal useful information.","Bacteria; Health monitoring; Microbiology; Pig; Virus","antibody detection; article; experimental animal; feces analysis; health status; hygiene; infection prevention; microbiological examination; nonhuman; Rotavirus; screening; Animalia; Pasteurella; Rodentia; Rotavirus; Sus scrofa","Bisgaard, M., Comparative investigations of Pasteurella haemolytica sensu stricto and so-called P. haemolytica isolated from different pathological lesions in pigs (1984) APMIS, 92, pp. 201-207. , Sect B; Brown, I.H., Done, S., Hannam, D., Higgins, R.J., Machie, S.C., Courtenay, A., Outbreak of influenza in pigs (1992) Veterinary Record, 130 (8), p. 166; Chang, G.N., Chang, T.C., Lin, S.C., Tsai, S.S., Chern, R.S., Isolation and identification of hemagglutinating encephalomyelitis virus from pigs in Taiwan (1993) Journal of the Chinese Society of Veterinary Medicine, 19 (3), pp. 147-158; Betingelser for Deklareret Kontrol Med Svinedysenteri; Betingelser for Deklareret Kontrol Med Skab; Betingelser for Deklareret Kontrol Med Ondartet Lungesyge (Hp2); Betingelser for Deklareret Kontrol Med Smitsom Nysesyge (1987) Conditions for Declared Monitoring of Porcine Dysenteria; Conditions for Declared Monitoring of Scabies; Conditions for Declared Monitoring of Evil Lung Disease (Hp2); Conditions for Declared Monitoring of Infectious Cough, , Danske Slagterier, Copenhagen; Ellegaard, L., Hansen, A.K., Produktion von mikrobiologisch definierten Miniatur-Schweinen mit Rücksicht auf die Verbesserung des Wissenschaftlichen Standards von Schweineversuchen (Production of microbiologically defined minipigs in order to improve the scientific standard of experiments involving pigs) (1994) Der Tierschutzbeauftragte, 1, pp. 31-35; Farrell, D., Meyers, M.J., Hinton, D.M., Evaluation of the miniature swine for use in immunotoxicity testing. (Abstracts of the 32nd annual meeting) (1993) The Toxicologists, 13 (1), p. 326; Foster, H.L., A procedure for obtaining nucleus-stock for a pathogen-free animal colony (1959) Proceedings of Animal Care, 9, pp. 135-142; Foster, H.L., Establishment and operation of SPF colonies (1962) The Problems of Laboratory Animal Disease, pp. 249-259. , (Harris RJC, ed). New York: Academic Press; (1985) Complications of Viral and Mycoplasma Infections in Rodents to Toxicology Research, , Hamm Jr TE (ed.) Washington DC: Hemisphere Press; Hansen, A.K., Health status and the effect of microbial organisms on animal experiments (1994) Handbook of Laboratory Animal Science, , (Svendsen P, Hau J, eds). Boca Raton: CRC Press, chap 11; Hansen, A.K., Dagnæs-Hansen, F., Mollegaard-Hansen, K.E., Correlation between megaloileitis and antibodies to Bacillus piliformis in laboratory rat colonies (1992) Laboratory Animal Science, 42 (5), pp. 449-453; Hansen, A.K., Skovgaard-Jensen, H.J., Experience from sentinel health monitoring in units containing rats and mice in experiments (1995) Scandinavian Journal of Laboratory Animal Science, 22 (1), pp. 1-9; Hem, A., Hansen, A.K., Rehbinder, C., Voipio, H.M., Engh, E., Recommendations for health monitoring of pig, cat, dog and gerbil breeding colonies (1994) Scandinavian Journal of Laboratory Animal Science, 21 (3), pp. 97-115. , Report of the Scandinavian Federation for Laboratory Animal Science (Scand-LAS) Working Group of Animal Health; Jestin, A., Madec, F., Popoff, M.R., Le Syndome de la diarrhée récurrente dans les porcheries d'engraissement, Seconde partie: Étude microbiologique (The syndrome of recurrent diarrhoea in fattening pig units. II. Microbiological study) (1987) Bulletin D'Information des Laboratoires des Services Vétérinaires, 25, pp. 35-44; Kapil, S., Goyal, S.M., Trent, A.M., Cellular immune status of coronavirus-infected neonatal calves (1994) Comparative Immunology, Microbiology and Infectious Diseases, 17 (2), pp. 133-138; Lussier, G., Potential detrimental effects of rodent viral infections on long-term experiments (1988) Veterinary Research Communications, 12, pp. 199-217; Mims, C., Virus-related immunomodulation (1986) Viral and Mycoplasmal Infections, , (Bhat PN, Jacoby RO, Morse III HC, New AE, eds). Orlando: Academic Press, chap 28; (1995) Annual Report, , Ministry of Agriculture, Copenhagen Århus Kalvehave; Notkins, A.L., Mergenhagen, S.E., Howard, J.R., Effect of virus infections on the function of the immune system (1970) Annual Review of Microbiology, 24, pp. 525-538; Roder, B.L., (1973) Substrathåndbogen (Handbook of Substrates), , Statens Seruminstitut, Copenhagen; Skirrow, M.B., Campylobacter enteritis: A 'new' disease (1977) British Medical Journal, 2, pp. 9-11; Svensmark, B., (1984) Diarrhé Hos Grise. Epidemiologiske Undersogelser i Intensive Sobesætninger Med Særligt Henblik På Rotavirus-associeret Diarré (Diarrhoea in Pigs. Epidemiological Studies in Intensive Sow Herds with Special Attention to Rotavirus Associated Diarrhoea), , PhD thesis, Institute of Internal Medicine, Royal Veterinary and Agricultural University, Copenhagen; Van Netten, P., Perales, I., Van De Moos Dijk, A., Curtis, G.D.W., Mossel, D.A.A., Liquid and solid selective differential media for the detection and enumeration of L. monocytogenes and other Listezia spp (1989) International Journal of Food Microbiology, 8, pp. 299-316; Weisbroth, S.H., Scher, S., The establishment of a specific pathogen-free breeding colony. II. Monitoring for disease and health statistics (1969) Laboratory Animal Care, 19 (6), pp. 795-799","Hansen, A.K.; Department of Experimental Medicine, University of Copenhagen, The Panum Institute, Blegdamsvej 3B, DK-2200 Copenhagen N, Denmark",,"SAGE Publications Ltd",00236772,,LBANA,"9230498","English","LAB. ANIM.",Article,"Final",Open Access,Scopus,2-s2.0-0030759809
"Lamontagne L., Massicotte E., Page C.","7005766206;36973328000;7202916107;","Mouse hepatitis viral infection induces an extrathymic differentiation of the specific intrahepatic αβ-TCR(intermediate) LFA-1(high) T-cell population",1997,"Immunology","90","3",,"402","411",,9,"10.1111/j.1365-2567.1997.00402.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031048376&doi=10.1111%2fj.1365-2567.1997.00402.x&partnerID=40&md5=8a2ab50eb6866ec362d5799ed6407302","Dept. des Sciences Biologiques, Univ. du Quebec a Montreal, Canada; Dépt. Sciences Biologiques, Univ. du Quebec a Montreal, Succ. A. Centre-Ville, Montréal, Que. H3C 3P8, Canada","Lamontagne, L., Dept. des Sciences Biologiques, Univ. du Quebec a Montreal, Canada, Dépt. Sciences Biologiques, Univ. du Quebec a Montreal, Succ. A. Centre-Ville, Montréal, Que. H3C 3P8, Canada; Massicotte, E., Dept. des Sciences Biologiques, Univ. du Quebec a Montreal, Canada; Page, C., Dept. des Sciences Biologiques, Univ. du Quebec a Montreal, Canada","Mouse hepatitis virus type 3 (MHV3), a coronavirus, is an excellent model for the study of thymic and extrathymic T-cell subpopulation disorders induced during viral hepatitis. It was recently reported that, in addition to the intrathymic T-cell differentiation pathway, an extrathymic differentiation pathway of αβ-T-cell receptor (TCR) T lymphocytes exists in the liver, and becomes important under pathological situations such as autoimmune diseases, malignancies or hepatic bacterial infections. In the present study, we compared the phenotypes of resident hepatic, splenic or thymic T-cell subpopulations during the acute viral hepatitis induced by MHV3 in susceptible C57BL/6 mice. The number of liver-resident mononuclear cells (MNC) increased during the viral infection, while cellularity decreased. Single positive (SP) CD4+ cells strongly increased in both the liver and thymus, while double positive (DP) (CD4+CD8+) cells, present in the liver and thymus of mock-infected mice, decreased in C57BL/6 mice during the viral infection. A shift of αβ-TCR(intermediate) T cells toward αβ-TCR(high) was evidenced in the liver and thymus of infected mice, but not in the spleen. The few αβ-TCR(int) double negative (DN) (CD4-CD8-) cells also decreased following viral infection. αβ-TCR(int or high) lymphocytes expressing high levels of leucocyte function antigen-1 (LFA-1) increased in the liver of MHV3-infected mice. In addition, liver-resident T cells expressed strongly the CD44 (Pgp-1) activation marker, suggesting that they were either activated or antigen experienced during the viral infection. No significant change in T-cell subpopulations was detected in the spleen, suggesting that MHV3 infection could induce an early in situ differentiation of resident hepatic T cells rather than a recruitment of lymphocytes from peripheral lymphoid organs.",,"CD4 antigen; CD8 antigen; Hermes antigen; lymphocyte function associated antigen 1; T lymphocyte receptor; animal experiment; animal model; article; controlled study; flow cytometry; lymphocyte differentiation; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; T lymphocyte subpopulation; thymus; virus hepatitis","Byrne, J.A., Oldstone, M.B.A., Biology of cloned cytotoxic T lymphocytes specific for lymphocytic choriomeningitis virus: Clearance of virus in vivo (1984) J Virol, 51, p. 682; Fung-Leung, W.P., Kundig, T.M., Zingernakel, R.M., Mak, T.W., Immune response against lymphocytic choriomeningitis virus infection without CD8 expression (1991) J Exp Med, 174, p. 1425; Reddehase, M.J., Mutter, W., Munch, K., Burhing, H.J., Koszinowski, U.H., CD8-positive T lymphocytes specific for murine cytomegalovirus immediate-early antigens mediate protective immunity (1987) J Virol, 61, p. 3102; Raff, M.C., Owen, J.J.T., Thymus-derived lymphocytes: Their distribution and role in the development of peripheral lymphoid tissues in the mouse (1971) Eur J Immunol, 1, p. 27; Pham, B.N., Mosnier, J.F., Walker, F., Flowcytometry CD4 +/CD8+ ratio of liver-derived lymphocyte correlates with viral replication in chronic hepatitis B (1994) Clin Exp Immunol, 97, p. 403; Pham, B.N., Martinot-Peignoux, M., Mosnier, J.F., CD4+/CD8+ ratio of liver-derived lymphocytes is related to viraemia and not to hepatitis C virus genotypes in chronic hepatitis C (1995) Clin Exp Immunol, 102, p. 320; Wege, H., Siddell, S., Sturm, M., Termeulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Topics Microbiol Immunol, 99, p. 165; Sturman, L.S., Holmes, K.V., The molecular biology of coronavirus (1983) Adv Virus Res, 28, p. 35; Barthold, S.W., Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab Anim Sci, 37, p. 36; Le Prévost, C., Levy-Leblond, B., Virelizier, J.L., Dupuy, J.M., Immunopathology of mouse hepatitis virus type 3 infection. 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Dindzans, V.J., Skamene, E., Levy, G.A., Susceptibility/resistance to murine hepatitis virus (MHV-3) and monocyte procoagulant activity (MPCA) are genetically linked and controlled by 2 non-H-2 linked genes (1986) J Immunol, 137, p. 2355; Levy, G.A., Abecassis, M., Activation of the immune coagulation system by murine hepatitis virus strain 3 (1989) Rev Infect Dis, 11, p. 712; Jolicoeur, P., Lamontagne, L., Mouse hepatitis virus 3 pathogenicity expressed by a lytic viral infection in bone marrow 14·8+ μ+ B lymphocyte subpopulations (1989) J Immunol, 143, p. 3722; Lamontagne, L., Jolicoeur, P., Mouse hepatitis virus 3 thymic cell interactions correlating with viral pathogenicity (1991) J Immunol, 146, p. 3152; Seki, S., Abo, T., Ohteki, T., Sugiura, K., Kumagai, K., Unusual αβ-T cells expanded in autoimmune lpr mice are probably a counterpart of normal T cells in the liver (1991) J Immunol, 147, p. 1214; Ohteki, T., Okuyama, R., Seki, S., Age-dependent increase in extrathymic T cells in the liver and their appearance in the periphery of older mice (1992) J Immunol, 149, p. 1562; Watanabe, H., Ohtsuka, K., Kimura, M., Details of an isolation method for hepatic lymphocytes in mice (1992) J Immunol Methods, 146, p. 145; Ohtsuka, K., Itai, T., Watanabe, H., Similarities and differences between extrathymic T cells residing in mouse liver and intestine (1994) Cell Immunol, 153, p. 52; Ohteki, T., Seki, S., Abo, T., Kumagai, K., Liver is a possible site for the proliferation of abnormal CD3 + 4- 8- double negative lymphocytes in autoimmune MRL-lpr/lpr mice (1990) J Exp Med, 172, p. 7; Seki, S., Abo, T., Sugiura, K., Reciprocal T cell response in the liver and thymus of mice injected with syngeneic tumor cells (1991) Cell Immunol, 137, p. 4; Abo, T., Ohteki, T., Seki, S., The appearance of T cells bearing self-reactive T cell receptor in the liver of mice injected with bacteria (1991) J Exp Med, 174, p. 417; Dupuy, J.M., Rodrigue, D., Heterogeneity in evolutive pattern of inbred mice infected with a cloned substrain of mouse hepatitis virus type 3 (1981) Intervirology, 16, p. 116; Garvy, B.A., Telford, W.O., King, L.E., Fraker, P.J., Glucocorticoids and irradiation-induced apoptosis in normal murine bone marrow B-lineage lymphocytes as determined by flow cytometry (1993) Immunology, 79, p. 270; Springer, T.A., Dustin, M.L., Kishimoto, T.K., Marlin, S.D., The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: Cell adhesion receptors of the immune system (1987) Annu Rev Immunol, 5, p. 223; Kishimoto, T.K., Larson, R.S., Corbi, A.L., Dustin, M.L., Stauton, D.E., Springer, T.A., The leukocytes integrins (1989) Adv Immunol, 46, p. 149; Matsumoto, Y., Emoto, M., Usami, J., Mazda, K., Yoshikai, Y., A protective role of extrathymic αβ TcR cells in the liver in primary murine salmonellosis (1994) Immunology, 81, p. 8; Huang, L., Soldevila, G., Leeker, M., Flavell, R., Crispe, I.N., The liver eliminates T cells undergoing antigen-triggered apoptosis in vivo (1994) Immunity, 1, p. 741; Huang, L., Sye, K., Crispe, N., Proliferation and apoptosis of B220+ CD4-CD8-TCRαβintermediate T cells in the liver of normal adult mice: Implication for lpr pathogenesis (1994) Int Immunol, 6, p. 553; Von Boehmer, H., Developmental biology of T cells in T cell-receptor transgenic mice (1990) Ann Rev Immunol, 8, p. 531; Sprent, J., Lifespans of naive, memory and effector lymphocytes (1993) Curr Opin Immunol, 5, p. 433; Lucas, B., Vasseur, F., Petit, C., Production, selection, and maturation of thymocytes with high surface density of TCR (1994) J Immunol, 153, p. 53; Lucas, B., Vasseur, F., Petit, C., The normal sequence of phenotypic transitions in one cohort of BrdUrd-pulse labeled thymocytes: Correlation with T cell receptor expression (1993) J Immunol, 151, p. 4574; Fine, J.S., Kruisbeek, A.M., The role of LFA-1/ICAM-1 interactions during murine T lymphocyte development (1991) J Immunol, 147, p. 2852; Decimo, D., Boespflug, O., Meunier-Rotival, M., Hadchouel, M., Tardieu, M., Genetic restriction of murine hepatitis virus type 3 expression in liver and brain: Comparative study in Balb/C and C3H mice by immunochemistry and hybridization in situ (1990) Arch Virol, 130, p. 269; Volpes, R., Van Den Oord, J.J., Desmet, V.J., Immunohistochemical study of adhesion molecules in liver inflammation (1990) Hepatology, 12, p. 59; Sugama, Y., Tiruppathi, C., Janakidevi, K., Andersen, T.T., Fenton, H.J.W., Malik, A.B., Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: A mechanism for stabilizing neutrophil adhesion (1992) J Cell Biol, 119, p. 935; Conrad, P., Rothman, B.L., Kelley, K.A., Blue, M.L., Mechanism of peripheral T cell activation by coengagement of CD44 and CD2 (1992) J Immunol, 149, p. 1833; Shimizu, Y., Newman, W., Tanaka, Y., Shaw, S., Lymphocyte interactions with endothelial cells (1992) Immunol Today, 13, p. 106; Pope, M., Chung, S.W., Mosmann, T., Leibowitz, J.L., Gorczinski, M., Levy, G.A., Resistance of naive mice to murine hepatitis virus strain 3 requires development of a Th1, but not a Th2, response, whereas pre-existing antibody partially protects against primary infection (1996) J Immunol, 156, p. 3342; Chung, S., Gorczynski, R., Cruz, B., A Th1 cell line (3E9·1) from resistant A/J mice inhibits induction of macrophage procoagulant activity in vitro and protects against MHV3 (1994) Immunology, 83, p. 353; Cook-Mills, J.M., Munshi, H.G., Perlman, R.L., Chambers, D.A., Mouse hepatitis virus infection suppresses modulation of mouse spleen T-cell activation (1992) Immunology, 75, p. 542; Dustin, M.L., Springer, T.A., T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1 (1989) Nature, 341, p. 619","Lamontagne, L.; Dept. Sciences Biologiques, Universite du Quebec a Montreal, CP 8888 Succ. A, Centre-Ville, Montreal, QUE. H3C 3P8, Canada",,"Blackwell Publishing Ltd",00192805,,IMMUA,"9155648","English","IMMUNOLOGY",Article,"Final",,Scopus,2-s2.0-0031048376
"Wickham L.A., Huang Z., Lambert R.W., Sullivan D.A.","7004680594;15026684300;7403115333;35508908800;","Effect of sialodacryoadenitis virus exposure on acinar epithelial cells from the rat lacrimal gland",1997,"Ocular Immunology and Inflammation","5","3",,"181","195",,10,"10.3109/09273949709116893","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030873909&doi=10.3109%2f09273949709116893&partnerID=40&md5=768a4aa0fc2d72db9dc8a6f98906060f","Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA, United States; Schepens Eye Research Institute, 20 Staniford, Street, Boston, MA 02114, United States","Wickham, L.A., Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA, United States; Huang, Z., Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA, United States; Lambert, R.W., Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA, United States; Sullivan, D.A., Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, MA, United States, Schepens Eye Research Institute, 20 Staniford, Street, Boston, MA 02114, United States","Sialodacryoadenitis virus (SDAV), a RNA coronavirus, induces degenerative, necrotic and atrophic alterations in acinar epithelial cells of the rat lacrimal gland. To begin to explore the underlying mechanism(s) of this viral effect, we sought in the present study to: (1) determine whether SDAV invades and replicates in lacrimal gland acinar cells in vitro; and (2) assess whether short-term SDAV challenge interferes with the viability or function of acinar cells in vitro. For comparison we also evaluated the relative infectivity of SDAV in acinar epithelial cells from lacrimal, submandibular and parotid glands, given that salivary tissues are known to be highly susceptible to SDAV infection in vivo. Acinar epithelial cells from lacrimal, submandibular or parotid glands were isolated from male rats, exposed briefly to SDAV or control cell antigen and then cultured for four, eight or twelve days. At experimental termination, SDAV titers in both media and sonicated cell extracts were evaluated by plaque assay titration on mouse L2 cell monolayers. To evaluate functional aspects of lacrimal gland acinar cells, SDAV-infected cells were incubated in the presence or absence of dihydrotestosterone and culture media were analyzed by RIA to measure the extent of the androgen-induced increase in secretory component (SC) production. Our results showed that: (1) SDAV invades and replicates in lacrimal gland acinar cells. Viral challenge resulted in a significant, time-dependent increase in SDAV titers, that were primarily cell-associated and greatly exceeded amounts contained in the original inoculum; (2) SDAV infection did not compromise lacrimal acinar cell viability or prevent the cellular SC response to androgens. Viral presence, though, did often attenuate the magnitude of this hormone action; and (3) SDAV infects salivary acinar cells, but the kinetics and magnitude of viral replication in lacrimal, submandibular and parotid cells showed considerable variations. These findings demonstrate that SDAV invades and replicates in acinar epithelial cells from lacrimal and salivary glands. The resulting release of infectious progeny may play a role in the SDAV-induced pathology of exocrine tissues in vivo.","Epithelial cells; Lacrimal gland; Salivary gland; Secretory component; Sialodacryoadenitis virus","androgen; androstanolone; acinar cell; animal experiment; animal model; animal tissue; article; cell viability; controlled study; Coronavirus; culture medium; epithelium cell; exocrine gland; lacrimal gland disease; nonhuman; parotid gland; radioimmunoassay; rat; RNA virus infection; salivary gland; submandibular gland; virus infectivity; virus replication; virus titration","Sullivan, D.A., Ocular mucosal immunity (1994) Handbook of Mucosal Immunology, pp. 569-597. , Ogra PL, Mestecky J, Lamm ME, Strober W, McGhee J, Bienenstock J (editors). Orlando, FL: Academic Press; Mostov, K.E., Cardone, M.H., Regulation of protein traffic in polarized epithelial cells (1995) Bioessays, 17, pp. 129-138; Ogra, P.L., Mestecky, J., Lamm, M.E., Strober, W., McGhee, J., Bienenstock, J., (1994) Handbook of Mucosal Immunology, , Orlando, FL: Academic Press; Mestecky, J., Russell, M.W., Jackson, S., Michalek, S.M., Tlaskalová-Hogenová, H., Sterzl, J., Advances in Mucosal Immunology, Parts A and B (1995) Adv Exp Med Biol, 371; Montgomery, P.C., Whittum-Hudson, J., Mucosal immunity in the ocular system (1996) Mucosal Vaccines, pp. 403-423. , Kiyono H, Ogra PL, McGhee JR, (editors). Orlando, FL: Academic Press; Ridley Lathers, D., Gill, R.F., O'Sullivan, N.L., Montgomery, P.C., Inductive sites for rat IgA tear antibody response (1997) Adv Exp Med Biol, , in press; Bhatt, P.N., Percy, D.H., Jonas, A.M., Characterization of the virus of sialodacryoadenitis of rats: A member of the coronavirus group (1972) J Infect Dis, 126, pp. 123-130; Kunita, S., Mori, M., Terada, E., Sequence analysis of the nucleocapsid protein gene of rat coronavirus SDAV-681 (1993) Virology, 193, pp. 520-523; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Pathogenesis of sialodacryoadenitis in gnotobiotic rats (1975) Vet Pathol, 12, pp. 196-209; Lai, Y.-L., Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Keratoconjunctivitis associated with sialodacryoadenitis in rats (1976) Invest Ophthalmol, 15, pp. 538-541; Eisenbrandt, D.L., Hubbard, G.B., Schmidt, R., A subclinical epizootic of sialodacryoadenitis in rats (1982) Lab Anim Sci, 32, pp. 655-659; Percy, D.H., Hanna, P.E., Paturzo, F., Bhatt, P.N., Comparison of strain susceptibility to experimental sialodacryoadenitis in rats (1984) Lab Anim Sci, 34, pp. 255-260; Percy, D.H., Wojcinski, Z.W., Schunk, M.K., Sequential changes in the Harderian and exorbital lacrimal glands in Wistar rats infected with sialodacryoadenitis virus (1989) Vet Pathol, 26, pp. 238-245; Callow, K., Effect of specific humoral activity and some non-specific factors on resistance of volunteers to respiratory coronavirus infection (1985) J Hyg, 95, pp. 173-189. , Lond; Jonas, A.M., Craft, J., Black, C.L., Bhatt, P.N., Hilding, D., Sialodacryoadenitis in the rat. A light and electron microscopic study (1969) Arch Pathol, 88, pp. 613-622; Carthew, P., Slinger, R.P., Diagnosis of sialodacryoadenitis virus infection of rats in a virulent enzootic outbreak (1981) Lab Anim, 15, pp. 339-342; Bhatt, P.N., Jacoby, R.O., Epizootiological observations of natural and experimental infection with sialodacryoadenitis virus in rats (1985) Lab Anim Sci, 35, pp. 129-134; Lussier, G., Descoteaux, J.-P., Prevalence of natural virus infections in laboratory mice and rats used in Canada (1986) Lab Anim Sci, 36, pp. 145-148; Percy, D., Bond, S., MacInnes, J., Replication of sialodacryoadenitis virus in mouse L-2 cells (1989) Arch Virol, 104, pp. 323-333; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Jacoby, R.O., Susceptibility of rodent cell lines to rat coronaviruses and differential enhancement by trypsin or DEAE-dextran (1991) Arch Virol, 118, pp. 57-66; Wentworth, B.B., French, L., Plaque assay of cytomegalovirus strains of human origin (1970) Proc Soc Exp Biol Med, 135, pp. 253-258; Albrecht, T., Weller, T.H., Heterogeneous morphologic features of plaques induced by five strains of human cytomegalovirus (1980) Am J Clin Pathol, 73, pp. 648-654; Boyle, J.F., Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Black, J.W., Plaque assay, polypeptide composition and immunochemistry of feline infectious peritonitis virus and feline enteric coronavirus isolates (1984) Adv Exp Med Biol, 173, pp. 133-147; Hirano, N., Ono, K., Sada, Y., Inoue, A., Murakami, T., Takamaru, H., Replication of rat coronavirus in a rat cell line, LBC (1985) Arch Virol, 85, pp. 301-304; Hirano, N., Plaque assay and propagation in rat cell line LBC cells of rat coronavirus and 5 strains of sialodacryoadenitis virus (1990) J Vet Med B, 37, pp. 91-96; Gaertner, D.J., Winograd, D.F., Compton, S.R., Patuzo, F.X., Smith, A.L., Development and optimization of plaque assays for rat coronaviruses (1993) J Virol Meth, 43, pp. 53-64; Hann, L.E., Kelleher, R.S., Sullivan, D.A., Influence of culture conditions on the androgen control of secretory component production by acinar cells from the lacrimal gland (1991) Invest Ophthalmol Vis Sci, 32, pp. 2610-2621; Lambert, R.W., Kelleher, R.S., Wickham, L.A., Vaerman, J.P., Sullivan, D.A., Neuroendocrinimmune modulation of secretory component production by rat lacrimal, salivary and intestinal epithelial cells (1994) Invest Ophthalmol Vis Sci, 35, pp. 1192-1201; Sullivan, D.A., Wira, C.R., Variations in free secretory component levels in mucosal secretions of the rat (1983) J Immunology, 130, pp. 1330-1335; Fox, R.I., Sjögren's syndrome (1992) Rheum Dis Clin NA, 18; Homma, M., Sugai, S., Tojo, T., Miyasaka, N., Akizuki, M., (1994) Sjögren's Syndrome. State of the Art, , Amsterdam: Kugler Press; Fox, R.I., Saito, I., Sjögren's syndrome: Immunologic and neuroendocrine mechanisms (1994) Adv Exp Med Biol, 350, pp. 609-621; Sato, E.H., Ariga, H., Sullivan, D.A., Impact of androgen therapy in Sjögren's syndrome: Hormonal influence on lymphocyte populations and Ia expression in lacrimal glands of MRL/Mp-lpr/lpr mice (1992) Invest Ophthalmol Vis Sci, 33, pp. 2537-2545; Thrane, P.S., Sollid, L.M., Haanes, H.R., Brandtzaeg, P., Clustering of IgA-producing immunocytes related to HLA-DR-positive ducts in normal and inflamed salivary glands (1992) Scand J Immunol, 35, pp. 43-51; Fox, R.I., Bumol, T., Fantozzi, R., Bone, R., Schreiber, R., Expression of histocompatibility antigen HLA-DR by salivary gland epithelial cells in Sjögren's syndrome (1986) Arthritis Rheum, 29, pp. 1105-1111; Liu, S.H., Prendergast, R.A., Silverstein, A.M., Experimental autoimmune dacryoadenitis. I. Lacrimal gland disease in the rat (1987) Invest Ophthalmol Vis Sci, 28, pp. 270-275; Ohashi, Y., Simpson, K.S., Minasi, P.N., Tabbara, K.F., The presence of cytotoxic autoantibody to lacrimal gland cells in NZB/W mice (1985) Invest Ophthalmol Vis Sci, 26, pp. 214-219; Hanna, P.E., Percy, D.H., Paturzo, F., Bhatt, P.N., Sialodacryoadenitis in the rat: Effects of immunosuppression on the course of the disease (1984) Am J Vet Res, 45, pp. 2077-2083; Percy, D.H., Williams, K.L., Croy, B.A., Experimental Sialodacryoadenitis virus infection in severe combined immunodeficient mice (1991) Can J Vet Res, 55, pp. 89-90; Weir, E.C., Jacoby, R.O., Paturzo, F.X., Johnson, E.A., Ardito, R.B., Persistence of sialodacryoadenitis virus in athytnic rats (1990) Lab Anim Sci, 40, pp. 138-143; Huang, Z., Lambert, R.W., Wickham, A., Sullivan, D.A., Analysis of cytomegalovirus infection and replication in acinar epithelial cells of the rat lacrimal gland (1996) Invest Ophthalmol Vis Sci, 37, pp. 1174-1186; Mazanec, M.B., Kaetzel, C.S., Lamm, M.E., Fletcher, D., Peterra, J., Nedrud, J.G., Intracellular neutralization of Sendai and influenza viruses by IgA monoclonal antibodies (1993) Adv Exp Med Biol, 371 A, pp. 651-654; Sixbey, J.W., Yao, Q.F., Immunoglobulin A-induced shift of Epstein-Barr virus tissue tropism (1992) Science, 255, pp. 1578-1580; Bihun, C.G., Percy, D.H., Morphologic changes in the nasal cavity associated with sialodacryoadenitis virus infection in the Wistar rat (1995) Vet Pathol, 32, pp. 1-10; Wojcinski, Z.W., Percy, D.H., Sialodacryoadenitis virus-associated lesions in the lower respiratory tract of rats (1986) Vet Pathol, 23, pp. 278-286; Weir, E.C., Jacoby, R.O., Paturzo, F.X., Johnson, E.A., Infection of SDAV-immune rats with SDAV and rat coronavirus (1990) Lab Anim Sci, 40, pp. 363-366; Schunk, M.K., Percy, D.H., Rosendal, S., Effect of time of exposure to rat coronavirus and Mycoplasma pulmonis on respiratory tract lesions in the Wistar rat (1995) Can J Vet Res, 59, pp. 60-66; Fox, R.I., Saito, I., Sjögren's syndrome: Immunologic and neuroendocrine mechanisms (1994) Adv Exp Med Biol, 350, pp. 609-621; Percy, D.H., Scott, R.W., Coronavirus infection in the laboratory rat: Immunization trials using attenuated virus replicated in L-2 cells (1991) Can J Vet Res, 55, pp. 60-66; Percy, D.H., Bond, S.J., Paturzo, F.X., Bhatt, P.N., Duration of protection from reinfection following exposure to sialodacryoadenitis virus in Wistar rats (1990) Lab Anim Sci, 40, pp. 144-149","Sullivan, D.A.; Schepens Eye Research Institute, 20 Staniford Street, Boston, MA 02114, United States",,"Informa Healthcare",09273948,,OIINE,"9326763","English","OCUL. IMMUNOL. INFLAMM.",Article,"Final",,Scopus,2-s2.0-0030873909
"Sirinarumitr T., Paul P.S., Halbur P.G., Kluge J.P.","6602842923;7202714004;7005935318;7005760957;","Rapid in situ hybridization technique for the detection of ribonucleic acids in tissues using radiolabelled and flourescein-labelled riboprobes",1997,"Molecular and Cellular Probes","11","4",,"273","280",,6,"10.1006/mcpr.1997.0114","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030807295&doi=10.1006%2fmcpr.1997.0114&partnerID=40&md5=fe54ee513240205f6990f4a7d2b9d67a","Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Vet. Medical Research Institute, Dept. Microbiol. Immunol. Prev. Med., Iowa State University, Ames, IA 50011, United States; Veterinary Diagnostic Laboratory, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States","Sirinarumitr, T., Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Paul, P.S., Vet. Medical Research Institute, Dept. Microbiol. Immunol. Prev. Med., Iowa State University, Ames, IA 50011, United States; Halbur, P.G., Veterinary Diagnostic Laboratory, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Kluge, J.P., Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States","In situ hybridization (ISH) is a useful diagnostic and research tool but is also time consuming. This study was conducted to determine if a rate enhancement hybridization (REH) buffer, developed for membrane hybridization, could be used to decrease hybridization lime for ISH. Tissue from swine with an enteric disease produced by a swine coronavirus, transmissible gastroenteritis virus (TGEV), was used as a model to standardize hybridization conditions for a rapid ISH technique. Small intestinal sections from pigs experimentally and naturally infected with TGEV were hybridized for various times at 52°C and 70°C with a radiolabelled or a fluorescein-labelled RNA probe in a standard hybridization or a REH buffer. Viral RNA was detected in intestines from as early as 30 min of hybridization by using both buffers with the radiolabelled probe; however, the signal was stronger with the REH buffer. With the fluorescein-labelled probe, viral RNA was detected in virus-infected cells of the intestines after 30 min of hybridization by using the REH buffer. Signal intensity was greater with the REH buffer than with the standard hybridization buffer when compared at each hybridization time and hybridization temperature using both radiolabelled and fluorescein-labelled probes. With the REH buffer, hybridization signal intensity was greater at 70°C than at 52°C for both probes. The best results were obtained when small intestinal sections were hybridized at 70°C for 2 h using a radiolabelled or a fluorescein-labelled probe diluted in the REH buffer. The fluorescein-labelled RNA probe with REH buffer resulted in a minimal non-specific signal when compared with the radiolabelled probe. These studies demonstrated that the REH buffer can be used to decrease the time of ISH for the detection of viral RNA. This rapid ISH technique should have broad applications in the utilization of probe technology in diagnostics and research for the detection of target ribonucleic acids in situ.","Coronavirus; In situ hybridization; Nucleic acid; Rapid hybridization; Riboprobes; Swine; TGEV","fluorescein; RNA; virus RNA; animal tissue; article; autoradiography; controlled study; Coronavirus; fluorescence in situ hybridization; in situ hybridization; intermethod comparison; intestine infection; intestine villus; isotope labeling; nonhuman; priority journal; RNA analysis; RNA probe; swine; temperature sensitivity; tissue; virus infection; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Angerer, L.M., Angerer, R.C., In situIn situ hybridization: A Practical Approach. (1992) New York: Oxford University Press, pp. 15-32; Kohler, C.R., Nelsen, J.A., Technique for double-labelling virus infected cells. InAnimal Virus Pathogenesis a Practical Approach (1990) New York: Oxford University Press, pp. 67-86; Gibson, S.J., Polak, J.M., Principles and applications of complementary RNA probes. InIn situ Hybridization Principles and Practice (1990) New York: Oxford University Press, pp. 81-94; Wilcox, J.N., Fundamental principles ofin situ (1993) Journal of Histochemistry and Cyto- Chemistry, 41, pp. 1725-1733; Syrjänen, S.M., Viral gene detection byin situ (1992) New York: Oxford University Press, pp. 103-139; Morrell, J.I., Application ofin situ (1989) London: Academic Press, pp. 127-146; Musiani, M., Zerbini, M., Venturoli, S., Rapid diagnosis of cytomegalovirus encephalitis in patients with AIDS usingin situ (1994) Journal of Clinical Pathology, 47, pp. 886-891; Martinez-Montero, J.C., Herrington, C.S., Stickland, J., Model system for optimizing mRNA non-isotopic in situ hybridisation: Riboprobe detection of lysozyme mRNA in archival gut biopsy specimens (1991) Journal of Clinical Pathology, 44, pp. 835-839; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis. InDiseases of Swine (1992) Iowa: Iowa State University Press, pp. 362-386; Delmas, B., Gelfi, J., L'Haridon, R., Aminopeptidase N is a major receptor for the entero- pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Weingart, H., Derbyshire, J.B., Evidence for a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs (1994) Journal of Virology, 68, pp. 7253-7259; Thake, D.C., Jejunal epithelium in transmissible gastroenteritis of swine (an electron microscope and histochemical study (1968) American Journal of Pathology, 53, pp. 149-169; Pensaert, M.B., Haelterman, E.O., Hinsman, E.J., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions II. Electron microscopy of the epithelium in isolated jejunal loops (1970) Archiv fuer Die Gesamte Virusforschung, 31, pp. 335-351; Wagner, J.E., Beamer, P.D., Restic, M., Electron microscopy of intestinal epithelial cells of piglets infected with a transmissible gastroenteritis virus (1973) Canadian Journal of Comparative Medicine, 37, pp. 177-188; Paul, P.S., Halbur, P.G., Vaughn, E.M., Significance of porcine respiratory coronavirus infection (1994) Compendium on Continuing Education for the Practicing Veterinarian, 16, pp. 1223-1234; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveal heterogeneity in the S, 3, 3-1 genes (1995) Journal of Virology, 69, pp. 3176-3184; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Veterinary Micro- Biology, 36, pp. 333-347; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ (1996) Journal of Virological Methods, 56, pp. 149-160; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S gene deletions (1994) Journal of Clinical Microbiology, 32, pp. 1809-1812; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Research, 18, pp. 71-80; Vaughn, E.M., Halbur, P.G., Paul, P.S., Use of non-radioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates (1996) Journal of Veterinary Diagnostic Investigation, 8, pp. 241-244; Nuovo, G.F., In situPCR in situ Hybridization: Protocols and Applications (1994) New York: Raven Press, pp. 100-168","Paul, P.S.; Veterinary Med. Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States",,"Academic Press",08908508,,MCPRE,"9281413","English","MOL. CELL. PROBES",Article,"Final",,Scopus,2-s2.0-0030807295
"Yamada Y.K., Takimoto K., Yabe M., Taguchi F.","55471420900;7004647272;7005872003;7103209890;","Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein",1997,"Virology","227","1",,"215","219",,36,"10.1006/viro.1996.8313","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031555643&doi=10.1006%2fviro.1996.8313&partnerID=40&md5=8b8d79a999d7bde64b42072ea4e331f1","Div. of Experimental Animal Research, National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Yamada, Y.K., Div. of Experimental Animal Research, National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan; Takimoto, K., Div. of Experimental Animal Research, National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan; Yabe, M., Div. of Experimental Animal Research, National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","The spike (S) protein of a nonfusogenic murine coronavirus, MHV-2, was compared to the S protein of a variant with fusion activity, MHV-2f. Two amino acids differed between the S proteins of these viruses; one was located in the signal sequence and the other was in the putative cleavage site. The amino acid at position 12 in the signal sequence was S in MHV-2 and C in MHV-2f. The amino acid sequence of the cleavage site of MHV-2 was HRARS, while that of MHV-2f was HRARR, showing one amino acid replacement at position 757. In DBT cells infected with MHV-2, the S protein was not cleaved, while the S protein of MHV-2f was cleaved. The S protein of MHV-2f expressed in a transient vaccinia virus expression system was cleaved and was fusogenic in contrast to the nonfusogenic activity of uncleaved MHV-2 S protein. Because the signal sequence is assumed to be removed from the mature S protein soon after synthesis, and because the S protein of MHV-2 was expressed on the cell surface in the same way as the S protein of MHV-2f, the difference in the signal sequence seemed to have had little effect on the transportation and the fusion activity of the S protein. These results showed that MHV-2 does not fuse cells due to the lack of cleavage of its S protein. This conclusion differs from studies on the activity of syncytium formation by the S proteins of fusogenic MHV-JHM and -A59 strains. Possible reasons for these differences in fusion activity are discussed.",,"virus protein; amino acid sequence; article; cell fusion; controlled study; Coronavirus; nonhuman; priority journal; protein degradation; virus strain; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus","Siddell, S., Wege, H., Ter Meulen, V., (1983) J. Gen. Virol., 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., (1988) J. Gen. Virol., 69, pp. 2939-2952; Lai, M.M.C., (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Holmes, K.V., Lai, M.M.C., (1996) ""Fields Virology,"" 3rd Ed., pp. 1075-1093. , B. N. Fields, D. M. Knipe, P. M. Howley, et al., Eds. Lippincott-Raven, Philadelphia; Sturman, L.S., Ricard, C.S., Holmes, K.V., (1985) J. Virol., 56, pp. 904-911; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., (1982) Virology, 119, pp. 358-371; Frana, M.F., Behnke, J.M., Sturman, L.S., Holmes, K.V., (1985) J. Virol., 56, pp. 912-920; White, J.M., (1990) Annu. Rev. Physiol., 52, pp. 675-697; Taguchi, F.J., (1993) Virol., 67, pp. 1195-1202; Stauber, R., Pfleiderera, M., Siddell, S., (1993) J. Gen. Virol., 74, pp. 183-191; Gombold, J.L., Hingley, S.T., Weiss, S.R., (1993) J. Virol., 67, pp. 4504-4512; Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., (1995) Virology, 214, pp. 453-463; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., (1974) Arch. Gesamte Virusforsch., 44, pp. 298-307; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M.C., (1988) J. Virol., 62, pp. 1989-1998; Taguchi, F., Yamada, A., Fujiwara, K., (1980) Infect. Immun., 29, pp. 42-49; Yamada, Y.K., Yabe, M., Yamada, A., Taguchi, F., (1993) Lab. Anim. Sci., 43, pp. 285-290; Suzuki, H., Taguchi, F., (1996) J. Virol., 70, pp. 2632-2636; Taguchi, F., Ikeda, T., Shida, H., (1992) J. Gen. Virol., 73, pp. 1065-1072; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., (1989) Virology, 173, pp. 664-673; Banner, L.R., Keck, J.G., Lai, M.M.C., (1990) Virology, 175, pp. 548-555; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., (1987) Virology, 161, pp. 479-487; Schmidt, I., Skinner, M., Siddell, S., (1987) J. Gen. Virol., 68, pp. 47-65; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., (1990) J. Virol., 64, pp. 731-741; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., (1991) J. Virol., 65, pp. 1916-1928; Skinner, M.A., Siddell, S.G., (1983) Nucleic Acids Res., 11, pp. 5045-5054; Kubo, H., Yamada, Y.K., Taguchi, F., (1994) J. Virol., 68, pp. 5403-5410","Yamada, Y.K.; Div. of Experimental Animal Research, National Institute of Health, 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan",,"Academic Press Inc.",00426822,,VIRLA,"9007076","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0031555643
"Ballesteros M.L., Sánchez C.M., Enjuanes L.","7006110601;57193985365;7006565392;","Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism",1997,"Virology","227","2",,"378","388",,118,"10.1006/viro.1996.8344","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031579245&doi=10.1006%2fviro.1996.8344&partnerID=40&md5=05f3fcea5c159b0e96a2059b73927f84","CSIC, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Ballesteros, M.L., CSIC, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sánchez, C.M., CSIC, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., CSIC, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","To study the molecular basis of TGEV tropism, a collection of recombinants between the PUR46-MAD strain of transmissible gastroenteritis coronavirus (TGEV) infecting the enteric and respiratory tracts and the PTV strain, which only infects the respiratory tract, was generated. The recombinant isolation frequency was about 10-9 recombinants per nucleotide and was 3.7-fold higher at the 5'-end of the S gene than in other areas of the genome. Thirty recombinants were plaque purified and characterized phenotypically and genetically. All recombinant viruses had a single crossover and had inherited the 5'- and 3'-halves of their genome from the enteric and respiratory parents, respectively. Recombinant viruses were classified into three groups, named 1 to 3, according to the location of the crossover. Group 1 recombinants had the crossover in the S gene, while in Groups 2 and 3 the crossovers were located in ORF1b and ORF1a, respectively. The tropism of the recombinants was studied. Recombinants of Group 1 had enteric and respiratory tropism, while Group 2 recombinants infected the respiratory, but not the enteric, tract. Viruses of both groups differed by two nucleotide changes at positions 214 and 655. Both changes may be in principle responsible for the loss of enteric tropism but only the change in nucleotide 655 was specifically found in the respiratory isolates and most likely this single nucleotide change, which leads to a substitution in amino acid 219 of the S protein, was responsible for the loss of enteric tropism in the closely related PUR46 isolates. The available data indicate that in order to infect enteric tract cells with TGEV, two different domains of the S protein, mapping between amino acids 522 and 744 and around amino acid 219, respectively, are involved. The first domain binds to porcine aminopeptidase N, the cellular receptor for TGEV. In the other domain maps a second factor of undefined nature but which may be the binding site for a coreceptor essential for the enteric tropism of TGEV.",,"virus protein; animal cell; article; cell invasion; controlled study; Coronavirus; gastroenteritis; gene mutation; nonhuman; priority journal; protein domain; radioimmunoassay; spike; virus cell interaction; virus recombinant; Animalia; Coronavirus; Peru tomato mosaic virus; Suidae; Transmissible gastroenteritis virus","Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J. Gen. Virol., 76, pp. 2235-2241; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronaries: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Britton, P., Page, K.W., Mawditt, K., Pocock, D.H., Sequence comparison of porcine transmissible gastroenteritis virus (TGEV) with porcine respiratory coronavirus (1990) VIIIth International Congress of Virology, pp. P6-018. , IUMS, Berlin; Callebaut, P., Correa, I., Pensaert, M., Jiménez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J Gen. Virol., 69, pp. 1725-1730; Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K.V., Lai, M.M.C., Laude, H., Siddell, S.G., Talbot, P., Revision of the taxonomy of the Coronavirus, Torovirus, and Arterivirus genera (1994) Arch. Virol., 135, pp. 227-237; Cavanagh, D., Davis, P.J., Derbyshire, J.H., Peters, R.W., Coronavirus IBV: Virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or haemagglutination-inhibiting antibody, or induce chicken tracheal protection (1986) J. Gen. Virol., 67, pp. 1435-1442; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-94; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Deng, H., Liu, R., Ellmeier, W., Choe, S., Unutmaz, D., Burkhart, M., Di Marzio, P., Landau, N.R., Identification of a major co-receptor for primary isolates of HIV-1 (1996) Nature, 381, pp. 661-666; Dragic, T., Litwin, V., Allaway, G.P., Martin, S.R., Huang, Y., Nagashima, K.A., Cayanan, C., Paxton, W.A., HIV-1 entry into CD4 cells is mediated by the chemokine receptor CC-CKR-5 (1996) Nature, 381, pp. 667-673; Eleouet, J.R., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology (1995) The Coronaviridae, pp. 337-376. , (S. G. Siddell, Ed.). Plenum, New York; Feng, Y., Broder, C.C., Kennedy, P.E., Berger, E.A., HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor (1996) Science, 272, pp. 872-877; Fichot, O., Girard, M., An improved method for sequencing of RNA templates (1990) Nucleic Acids Res., 18, p. 6162; Fu, K., Baric, R.S., Map locations of mouse hepatitis virus temperature-sensitive mutants: Confirmation of variable rates of recombination (1994) J. Virol., 68, pp. 7458-7466; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Holmes, K.V., Williams, R.K., Stephensen, C.B., Compton, L.R., Cardellichio, C.B., Hay, C.M., Knobler, R.L., Boyle, J.F., Coronavirus receptors (1989) Cell Biology of Virus Entry, Replication, and Pathogenesis, pp. 85-94. , (R. W. Compans, A. Helenius, and M. B. A. Oldstone, Eds.). A. R. Liss, New York; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Kenny, A.J., Maroux, S., Topology of microvillar membrane hydrolases of kidney and intestine (1982) Physiol. Rev., 62, pp. 91-128; Lai, M.M.C., Coronavirus-organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Laude, H., Vanreeth, K., Pensaert, M., Porcine respiratory coronavirus-molecular features and virus host interactions (1993) Vet. Res., 24, pp. 125-150; Lunney, J.K., Pescovitz, M.D., Sachs, D.H., The swine major histocompatibility complex: Its structure and function (1986) Swine in Biomedical Research, pp. 1821-1836. , (M. E. Tumbleson, Ed.). Plenum, New York; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci., 30, pp. 190-198; McKittrick, S.P., Georgalis, A.M., Atchison, B.A., Efficient extraction of viral RNA for PCR amplification (1993) BioTechniques, 15, pp. 802-805; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Norén, Q., Sjöström, H., Danielsen, E.M., Cowell, G.M., Skovbjerg, H., (1986) The Enzymes of the Enterocyte Plasma Membrane, , Elsevier/North-Holland, Amsterdam; Pensaert, M., Callebaut, P., Hooyberghs, J., Transmissible gastroenteritis virus in swine: Old and news (1986) 9th Int. Pig Vet. Soc. Cong. 1986, pp. 40-45. , Barcelona, Spain; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochemie, 69, pp. 591-600; Robb, J.A., Bond, C.W., Leibowitz, J.L., Pathogenic murine coronaviruses. III. Biological and biochemical characterization of temperature-sensitive mutants of JHMV (1979) Virology, 94, pp. 385-399; Sachs, D., Leight, G., Cone, J., Schwarz, S., Stuart, L., Rosemberg, S., Transplantation in miniature swine. I. Fixation of the major histocompatibility complex (1976) Transplantation, 22, pp. 559-567; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , (A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor, Eds.). Wolfe, Ames, Iowa; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Semenza, G., Anchoring and biosynthesis of stalked brush border membrane proteins: Glycosidases and peptidases of enterocytes and renal tubuli (1986) Annu. Rev. Cell Biol., 2, pp. 225-313; Shepley, M.P., Racaniello, V.R., A monoclonal antibody that blocks poliovirus attachment recognizes the lymphocyte homing receptor CD44 (1994) J. Virol., 68, pp. 1301-1308; Siddell, S.G., (1995) The Coronaviridae, , Plenum, New York; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 36-112; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike protein (1996) J. Virol., 70, pp. 2632-2636; Takeuchi, Y., Akutsu, M., Murayama, K., Shimizu, N., Hoshino, H., Host range mutant of human immunodeficiency virus type 1: Modification of cell tropism by a single point mutation at the neutralization epitope in the env gene (1991) J. Virol., 65, pp. 1710-1718; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56","Enjuanes, L.; Centro Nacional de Biotecnologia, CSIC, Department of Molecular/Cell Biology, Cantoblanco, 28049 Madrid, Spain",,"Academic Press Inc.",00426822,,VIRLA,"9018137","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0031579245
"Chen D.S., Asanaka M., Chen F.S., Shively J.E., Lai M.M.C.","55628577597;6602256485;57190676149;7101837298;7401808497;","Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors",1997,"Journal of Virology","71","2",,"1688","1691",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031031924&partnerID=40&md5=a347b8a20046314018b63dc3ae1cab0d","DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States","Chen, D.S., DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States; Asanaka, M., DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States; Chen, F.S., DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States; Shively, J.E., DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States; Lai, M.M.C., DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States","Receptors for murine coronavirus mouse hepatitis virus (MHV) are members of the murine carcinoembryonic antigen (CEA) gene family. Since MHV can also infect primates and cause central nervous system lesions (G. F. Cabirac et al., Microb. Pathog. 16:349-357, 1994; R. S. Murray et al., Virology 188:274- 284, 1992), we examined whether human CEA-related molecules can be used by MHV as potential receptors. Transfection of plasmids expressing human carcinoembryonic antigen (hCEA) and human biliary glycoprotein into COS-7 cells, which lack a functional MHV receptor, conferred susceptibility to two MHV strains, A59 and MHV-2. Domain exchange experiments between human and murine CEA-related molecules identified the immunoglobulin-like loop I of hCEA as the region conferring the virus-binding specificity. This finding expands the potential MHV receptors to primate species.",,"carcinoembryonic antigen; complementary dna; glycoprotein; virus receptor; animal cell; article; cell line; controlled study; fluorescence activated cell sorter; gene expression; genetic transfection; immunofluorescence; molecular cloning; murine hepatitis coronavirus; nonhuman; plasmid; priority journal; virus strain; Amino Acid Sequence; Animals; Carcinoembryonic Antigen; COS Cells; Glycoproteins; Humans; Mice; Molecular Sequence Data; Murine hepatitis virus; Receptors, Virus; Sequence Alignment; Transfection",,"Lai, M.M.C.; DMMI, USC School of Medicine, 2011 Zonal Ave., Los Angeles, CA 90033-1054, United States; email: michlai@hsc.usc.edu",,,0022538X,,JOVIA,"8995701","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031031924
"Der Vartanian M., Girardeau J.-P., Martin C., Rousset E., Chavarot M., Laude H., Contrepois M.","6602094816;7005791284;57212178599;57212564412;6603223848;7006652624;7004249567;","An Escherichia coli CS31A fibrillum chimera capable of inducing memory antibodies in outbred mice following booster immunization with the entero-pathogenic coronavirus transmissible gastroenteritis virus",1997,"Vaccine","15","2",,"111","120",,12,"10.1016/S0264-410X(96)00172-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031081784&doi=10.1016%2fS0264-410X%2896%2900172-7&partnerID=40&md5=fb91cfdb3679f6aebb438197fbb7c641","Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France; U. de Virologie/Immunol. M., Inst. Natl. de la Rech. Agronomique, Domaine de Vilvert, 78352 Jouy-en-Josas, Cédex, France; Grp. de Rech. sur les Maladies I., Faculty of Veterinary Medicine, University of Montreal, Saint-Hyacinthe, Que., Canada","Der Vartanian, M., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France; Girardeau, J.-P., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France; Martin, C., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France; Rousset, E., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France, U. de Virologie/Immunol. M., Inst. Natl. de la Rech. Agronomique, Domaine de Vilvert, 78352 Jouy-en-Josas, Cédex, France; Chavarot, M., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France; Laude, H., Grp. de Rech. sur les Maladies I., Faculty of Veterinary Medicine, University of Montreal, Saint-Hyacinthe, Que., Canada; Contrepois, M., Laboratoire de Microbiologie, Inst. Natl. de la Rech. Agronomique, Ctr. de Rech. de Clermont-Ferrand-T., 63122 Saint-Genès-Champanelle, France","CS31A fibrillae are thin, flexible, heteropolymeric proteinaceous appendages exposed as a capsule-like material around the cell surface of certain Escherichia coli strains. Two antigenic peptides of the S spike glycoprotein (TGEV-S) amino acids (aa) 363-371 and 521-531 of the transmissible gastroenteritis virus (TGEV) were tandemly introduced in the loop-structured, variable region aa 202-218 of the major ClpG subunit protein composing the bulk of CS31A. The resulting hybrid fibrillae with a 25 aa heterologous peptide were produced at the cell surface. Using a monoclonal antibody (Mab) specific for the TGEV epitopes, purified hybrid fibrillae were analysed in Western blotting under native conditions, which showed that the two viral epitopes were recognized immunologically as an integral part of the hybrid fibrillae, and therefore that they were antigenically active. The immunogenicity of the fusion construct was evaluated with live recombinant bacteria, purified hybrid ClpG monomers, and purified chimeric CS31A polymers. Whatever the form of hybrid used as antigen, intraperitoneally immunized outbred mice elicited serum anti-TGEV peptides antibodies (Abs) with significant titres and capable of recognizing native TGEV particles, indicating that the epitopes are exposed in an immunogenic conformation in all cases. However, virus neutralization titres were only obtained after immunization with either purified polymers or monomers. Furthermore, 4 months after an ultimate immunization with 20 μg of hybrid fibrillae mice developed a strong anamnestic Ab response against the two TGEV peptides following booster inoculation with virions. We conclude that CS31A fibrillae carrying a combination of TGEV epitopes as insert can induce an immunological memory in outbred animals infected with TGEV, and therefore that hybrid CS31A fibrillae may prove efficient as components of a subunit vaccine.","Carrier-delivery system; CS31A fibrillae; Immune response; Recombinant DNA; TGEV coronavirus","chimeric protein; monoclonal antibody; recombinant dna; vaccine; animal experiment; antibody response; article; coronavirus; dna sequence; enzyme linked immunosorbent assay; escherichia coli; gastroenteritis; immunization; immunogenicity; immunological memory; intraperitoneal drug administration; mouse; nonhuman; priority journal; Adhesins, Escherichia coli; Amino Acid Sequence; Animals; Antibodies, Viral; Antigens, Bacterial; Bacterial Proteins; Base Sequence; Escherichia coli Proteins; Fimbriae, Bacterial; Haplotypes; Immunization, Secondary; Immunologic Memory; Mice; Mice, Inbred C57BL; Mice, Inbred CBA; Mice, Inbred DBA; Molecular Sequence Data; Recombinant Fusion Proteins; Transmissible gastroenteritis virus","Girardeau, J.P., Der Vartanian, M., Ollier, J.L., Contrepois, M., CS31A, a new K88 related fimbrial antigen on bovine enterotoxigenic and septicemic Escherichia coli strains (1988) Infect. Immun., 56, pp. 2180-2188; Contrepois, M., Fairbrother, J.M., Kaura, Y.K., Girardeau, J.P., Prevalence of CS31A and F16S surface antigens in Escherichia coli isolates from animals in France, Canada and India (1989) FEMS Microbiol. Lett., 59, pp. 319-324; Chérifi, A., Contrepois, M., Picard, P., Factors and marker of virulence in Escherichia coli from human septicemia (1990) FEMS Microbiol. Lett., 70, pp. 279-284; Méchin, M.C., Bertin, Y., Girardeau, J.P., Hydrophobic cluster analysis and secondary structure predictions revealed that major and minor structural subunits of K88-related adhesins of Escherichia coli share a common overall fold and differ structurally from other fimbrial subunits (1995) FEBS Lett., 364, pp. 319-324; Bousquet, F., Martin, C., Girardeau, J.P., CS31A capsule-like antigen as an exposure vector for heterologous antigenic determinants (1994) Infect. Immun., 62, pp. 2553-2561; Saif, L.J., Bohl, E.H., Transmissible gastroenteritis (1986) Diseases of Swine, pp. 255-274. , (Eds Leman A.D., Glock R.D., Mengeling W.K., Penny R.H.C., Scholl E. and Straw, B.). Iowa State University Press, Ames; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Suñé, C., Jimenez, G., Correa, I., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Saif, L.J., Van Cott, J.L., Brim, T.A., Immunity to transmissible gastroenteritis virus and porcine respiratory coronavirus infections in swine (1994) Vet. Immun. 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Pathog., 10, pp. 429-442; Takeshïta, S., Sato, M., Toba, M., Masahashi, W., Hashimoto, T., High-copy number and low-copy number plasmid vector for lacZ a-complementation and chloramphenicol or kanamycin resistance selection (1987) Gene, 61, pp. 63-74; Girardeau, J.P., Bertin, Y., Martin, C., Der Vartanian, M., Boeuf, C., Sequence analysis of the clpG gene, which codes for surface antigen CS31A subunit: Evidence of an evolutionary relationship between CS31A, K88 and F41 subunit genes (1991) J. Bacteriol., 173, pp. 7676-7683; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, New York; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl Acad. Sci. U.S.A., 74, pp. 5463-5467; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl Acad. Sci U.S.A., 76, pp. 4350-4354; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I - Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Hockney, R.C., Recent developments in heterologous protein production in Escherichia coli (1994) TIBTECH, 12, pp. 456-463; Van Der Zee, A., Noordegraaf, C.V., Van Den Bosch, H., P-fimbriae of Escherichia coli as carriers for gonadotropin releasing hormone: Development of a recombinant contraceptive vaccine (1995) Vaccine, 13, pp. 753-758; Broeckhuysen, M.P., Van Rijn, J.M.M., Blom, A.J.M., Fusion proteins with multiple copies of the major antigenic determinant of foot-and-mouth disease virus protect both the natural host and laboratory animals (1987) J. Gen. Virol., 68, pp. 31-37; Krogfelt, K.A., Bacterial adhesion: Genetics, biogenesis, and role in pathogenesis of fimbrial adhesins of Escherichia coli (1991) Rev. Infect. Dis., 13, pp. 721-735; Leclerc, C., Sedlik, C., Lo-Man, R., Charlot, B., Rojas, M., Deriaud, E., Stimulation of a memory B cell response does not require primed helper T cells (1995) Eur. J. Immun., 25, pp. 2533-2538","Der Vartanian, M.; Laboratoire de Microbiologie, Inst. Nat. de Recherche Agronomique, Ctr. Rech. de Clermont-Ferrand-Theix, 63122 Saint-Genes-Champanelle, France",,,0264410X,,VACCD,"9066025","English","VACCINE",Article,"Final",Open Access,Scopus,2-s2.0-0031081784
"Bonilla P.J., Hughes S.A., Weiss S.R.","7004225518;22956252200;57203567044;","Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59",1997,"Journal of Virology","71","2",,"900","909",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031028291&partnerID=40&md5=ffc034efc341b66545378f960a0d93a6","Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States; Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Inst. de Rech. Cliniques de Montreal, Montreal, Que. H2W-1R7, Canada","Bonilla, P.J., Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States, Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Hughes, S.A., Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States, Inst. de Rech. Cliniques de Montreal, Montreal, Que. H2W-1R7, Canada; Weiss, S.R., Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States","The 21.7-kb replicase locus of mouse hepatitis virus strain A59 (MHV- A59) encodes several putative functional domains, including three proteinase domains. Encoded closest to the 5' terminus of this locus is the first papain-like proteinase (PLP-1) (S. C. Baker et al., J. Virol. 67:6056-6063, 1993; H.-J. Lee et al., Virology 180:567-582, 1991). This cysteine proteinase is responsible for the in vitro cleavage of p28, a polypeptide that is also present in MHV-A59-infected cells. Cleavage at a second site was recently reported fur this proteinase (P. J. Bonilla et al., Virology 209:489-497, 1995). This new cleavage site maps to the same region as the predicted site of the C terminus of p65, a viral polypeptide detected in infected cells. In this study, microsequencing analysis of the radiolabeled downstream cleavage product and deletion mutagenesis analysis were used to identify the scissile bond of the second cleavage site to between Ala832 and Gly833. The effects of mutations between the P5 and P2' positions on the processing at the second cleavage site were analyzed. Most substitutions at the P4, P3, P2, and P2' positions were permissive for cleavage. With the exceptions of a conservative P1 mutation, Ala832Gly, and a conservative P5 mutation, Arg828Lys, substitutions at the P5, P1, and P1' positions severely diminished second- site proteolysis. Mutants in which the p28 cleavage site (Gly247 ↓ Val248) was replaced by the Ala832 ↓ Gly833 cleavage site and vice versa were found to retain processing activity. Contrary to previous reports, we determined that the PLP-1 has the ability to process in trans at either the p28 site or both cleavage sites, depending on the choice of substrate. The results from this study suggest a greater role by the PLP-1 in the processing of the replicase locus in vivo.",,"proteinase; article; enzyme activity; gene locus; gene mapping; murine hepatitis coronavirus; nonhuman; priority journal; protein degradation; Amino Acid Sequence; Animals; DNA, Viral; Endopeptidases; Gene Deletion; Genes, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Transcription, Genetic","Agranovsky, A.A., Koonin, E.V., Boyko, V.P., Maiss, E., Frötschl, R., Lunina, N.A., Atabekov, J.G., Beet yellows closterovirus: Complete genome structure and identification of a leader papain-like thiol protease (1994) Virology, 198, pp. 311-324; Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Pinón, J.D., Weiss, S.R., Characterization of the leader papain-like protcinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bransom, K.L., Wallace, S.E., Dreher, T.W., Identification of the cleavage site recognized by the turnip yellow mosaic virus protease (1996) Virology, 217, pp. 404-406; Bredenbeek, P.J., Pachuck, C.J., Noten, A.F.H., Charité, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Carrington, J.C., Cary, S.M., Parks, T.D., Dougherty, W.G., A second proteinase encoded by a plant potyvirus genome (1989) EMBO J., 8, pp. 365-370; Chen, J.-P., Strauss, J.H., Strauss, E.G., Frey, T.K., Characterization of the rubella virus nonstructural protease domain and its cleavage site (1996) J. 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Virol., 65, pp. 3076-3082; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kb) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS Lett., 288, pp. 201-205; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kadaré, G., Rozanov, M., Haenni, A.L., Expression of the turnip yellow mosaic virus proteinase in Escherichia coli and determination of the cleavage site within the 206 kDa protein (1995) J. Gen. Virol., 76, pp. 2853-2857; Khouri, H.E., Vernet, T., Ménard, R., Parlati, F., Laflamme, P., Tessier, D.C., Gour-Salin, B., Storer, A.C., Engineering of papain: Selective alteration of substrate specificity by site-directed mutagenesis (1991) Biochemistry, 30, pp. 8929-8936; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d (1995) Virology, 208, pp. 1-8; Kirchweger, R., Ziegler, E., Lamphear, B.J., Waters, D., Liebig, H.-D., Sommergruber, W., Sobrino, F., Skern, T., Foot-and-mouth disease virus leader proteinase: Purification of the Lb form and determination of the cleavage site on eTF-4γ (1994) J. Virol., 68, pp. 5677-5684; Lawrence, D.M., Rozanov, M.N., Hillman, B.I., Autocatalylic processing of the 223-kDa protein of blueberry scorch carlavirus by a papain-like proteinase (1995) Virology, 207, pp. 127-135; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Brown, T.D.K., Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Rozanov, M.N., Schiff, L.A., Weiss, S.R., Unpublished data; Shapira, R., Nuss, D.L., Gene expression by a hypovirulence-associated virus of the chestnut blight fungus involves two papain-like protease activities (1991) J. Biol. Chem., 266, pp. 19419-19425; Snijder, E.J., Wassenaar, A.L., Spaan, W.J.M., The 5′ end of the equine arteritis virus replicasc gene encodes a papainlike cysteine protease (1992) J. Virol., 66, pp. 7040-7048; Strauss, J.H., Strauss, E.G., The alphaviruses: Gene expression, replication, and evolution (1994) Microbiol. Rev., 58, pp. 491-562; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Weiss, S.R., Hughes, S.A., Bonilla, P.J., Turner, J.D., Leibowitz, J.L., Denison, M.R., Coronavirus polyprotein processing (1994) Arch. Virol., 9 (SUPPL.), pp. 349-358; Yoo, D., Parker, M.D., Cox, G.J., Babiuk, L.A., Zinc-binding of the cysteine-rich domain encoded in the open reading frame 1b of the RNA polymerase gene of coronavirus (1995) Adv. Exp. Med. Biol., 380, pp. 437-442; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Weiss, S.R.; Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"8995606","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031028291
"Luytjes W., Gerritsma H., Bos E., Spaan W.","6701683324;6507424618;7005778356;7007172944;","Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein",1997,"Journal of Virology","71","2",,"949","955",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031015207&partnerID=40&md5=95bf4b8750a2597dad7e21071f53a65b","Department of Virology, Leiden University, 2333 AA Leiden, Netherlands; Department of Virology, Leiden University, Albinusdreef 2, 2333 AA Leiden, Netherlands","Luytjes, W., Department of Virology, Leiden University, 2333 AA Leiden, Netherlands, Department of Virology, Leiden University, Albinusdreef 2, 2333 AA Leiden, Netherlands; Gerritsma, H., Department of Virology, Leiden University, 2333 AA Leiden, Netherlands; Bos, E., Department of Virology, Leiden University, 2333 AA Leiden, Netherlands; Spaan, W., Department of Virology, Leiden University, 2333 AA Leiden, Netherlands","Two temperature-sensitive (ts) mutants of mouse hepatitis virus strain A59, ts43 and ts379, have been described previously to be ts in infectivity but unaffected in RNA synthesis (M. J. M. Koolen, A. D. M. E. Osterhaus, G. van Steenis, M. C. Horzinek, and B. A.M. van der Zeijst, Virology 125:393- 402, 1983). We present a detailed analysis of the protein synthesis of the mutant viruses at the permissive (31°C) and nonpermissive (39.5°C) temperatures. It was found that synthesis of the nucleocapsid protein N and the membrane protein M of both viruses was insensitive to temperature. However, the surface protein S of both viruses was retained in the endoplasmic reticulum at the nonpermissive temperature. This was shown first by analysis of endoglycosidase H-treated and immunoprecipitated labeled S proteins. The mature Golgi form of S was not present at the nonpermissive temperature for the ts viruses, in contrast to wild-type (wt) virus. Second, gradient purification of immunoprecipitated S after pulse-chase labeling showed that only wt virus S was oligomerized. We conclude that the lack of oligomerization causes the retention of the ts S proteins in the endoplasmic reticulum. As a result, ts virus particles that were devoid of S were produced at the nonpermissive temperature. This result could be confirmed by biochemical analysis of purified virus particles and by electron microscopy.",,"virus protein; animal cell; article; murine hepatitis coronavirus; nonhuman; priority journal; protein synthesis; rna synthesis; temperature sensitivity; virion; virus strain; Animals; Genome, Viral; Mice; Murine hepatitis virus; Mutation; RNA, Viral; Temperature; Viral Structural Proteins","Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effeet on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Bos, E.C.W., Luytjes, W., Van Der Meulen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Carleton, M., Brown, D.T., Events in the endopiasmic reticulum abrogate the temperature sensitivity of Sindbis virus mutant ts23 (1996) J. 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Cell Biol., 131, pp. 339-349; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Ricard, C.S., Koetzner, C.A., Sturman, L.S., Masters, P.S., A conditional-lethal murine coronavirus mutant that tails to incorporate the spike glycoprotein into assembled virions (1996) Virus Res., 39, pp. 261-276; Rothman, J.E., Wieland, F.T., Protein sorting by transport vesicles (1996) Science, 272, pp. 227-234; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Rottier, P.J., Horzinek, M.C., Van Der Zeijst, B.A., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Sambrook, J., Rodgers, L., White, J., Gething, M.J., Lines of BPV-transformed murine cells that constitutively express influenza virus hemagglutinin (1985) EMBO J., 4, pp. 91-103; Siddell, S.G., The small-membrane protein (1995) The Coronaviridae, pp. 181-189. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Spaan, W.J.M., Rottier, P.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Sturman, L.S., Holmes, K.V., The novel glycoproteins of coronaviruses (1985) Trends Biochem. Sci., 10, pp. 17-20; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac-cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Vennema, H., Rottier, P.J.M., Heijnen, L., Godeke, G.J., Horzinek, M.C., Spaan, W.J.M., Biosynthesis and function of the eoronavirus spike protein (1990) Adv. Exp. Med. Biol., 276, pp. 9-19; Whitt, M.A., Zagouras, P., Crise, B., Rose, J.K., A fusion-defective mutant of the vesicular stomatitis virus glycoprotein (1990) J. Virol., 64, pp. 4907-4913; Whitt, M.A., Chong, L., Rose, J.K., Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant (1989) J. Virol., 63, pp. 3569-3578","Luytjes, W.; Department of Virology, Leiden University, Albinusdreef 2, 2333 AA Leiden, Netherlands; email: luytjes@virology.azl.nl",,,0022538X,,JOVIA,"8995612","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031015207
"Fischer F., Peng D., Hingley S.T., Weiss S.R., Masters P.S.","7202883540;7202530662;6701491322;57203567044;7006234572;","The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication",1997,"Journal of Virology","71","2",,"996","1003",,69,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031026431&partnerID=40&md5=545cde1fd46aa10ab987b85cb70259ad","Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; Mem. Sloan Kettering Cancer Center, New York, NY 10021, United States; Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States","Fischer, F., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Peng, D., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States, Mem. Sloan Kettering Cancer Center, New York, NY 10021, United States; Hingley, S.T., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States, Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States; Masters, P.S., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","The coronavirus mouse hepatitis virus (MHV) contains a large open reading frame embedded entirely within the 5' half of its nucleocapsid (N) gene. This internal gene (designated 1) is in the +1 reading frame with respect to the N gene, and it encodes a mostly hydrophobic 23-kDa polypeptide. We have found that this protein is expressed in MHV-infected cells and that it is a previously unrecognized structural protein of the virion. To analyze the potential biological importance of the I gene, we disrupted its expression by site-directed mutagenesis using targeted RNA recombination. The start codon for I was replaced by a threonine codon, and a stop codon was introduced at a short interval downstream. Both alterations created silent changes in the N reading frame. In vitro translation studies showed that these mutations completely abolished synthesis of I protein, and immunological analysis of infected cell lysates confirmed this conclusion. The MHV I mutant was viable and grew to high titer. However, the I mutant had a reduced plaque size in comparison with its isogenic wild-type counterpart, suggesting that expression of I confers some minor growth advantage to the virus. The engineered mutations were stable during the course of experimental infection in mice, and the I mutant showed no significant differences from wild type in its ability to replicate in the brains or livers of infected animals. These results demonstrate that I protein is not essential for the replication of MHV either in tissue culture or in its natural host.",,"animal cell; article; mouse; murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; protein expression; virus gene; virus replication; Animals; Gene Expression Regulation, Viral; Mice; Murine hepatitis virus; Nucleocapsid; Open Reading Frames; Viral Structural Proteins; Virus Replication","Chamberlain, J.P., Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate (1979) Anal. Biochem., 98, pp. 132-135; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Décimo, D., Philippe, H., Hadchouel, M., Tardieu, M., Meunier-Rotival, M., The gene encoding the nucleocapsid protein: Sequence analysis in murine hepatitis virus type 3 and evolution in Coronaviridae (1993) Arch. Virol., 130, pp. 279-288; Ernst, H., Shatkin, A.J., Reovirus hemagglutinini mRNA codes for two polypeptides in overlapping reading frames (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 48-52; Fichot, O., Girard, M., An improved method for sequencing of RNA templates (1990) Nucleic Acids Res., 18, p. 6162; Frolov, I., Schlesinger, S., Translation of Sindbis virus mRNA: Effects of sequences downstream of the initiating codon (1994) J. Virol., 68, pp. 8111-8117; Giorgi, C., Blumberg, B.M., Kolakofsky, D., Sendai virus contains overlapping genes expressed from a single mRNA (1983) Cell, 35, pp. 829-836; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Homberger, F.R., Sequence analysis of the nucleoprotein genes of three enterotropic strains of murine coronavirus (1995) Arch. Virol., 140, pp. 571-579; Horton, R.M., Pease, L.R., Recombination and mutagenesis of DNA sequences using PCR (1991) Directed Mutagenesis, a Practical Approach, , M. J. McPherson (ed.), IRL Press, New York, N.Y; Jacobs, B.L., Samuel, C.E., Biosynthesis of reovirus-specified polypeptides: The reovirus s1 mRNA encodes two primary translation products (1985) Virology, 143, pp. 63-74; Kingsman, S.M., Samuel, C.E., Mechanism of Interferon action. Interferon-mediated inhibition of simian virus-40 early KNA accumulation (1980) Virology, 101, pp. 458-465; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Kozak, M., Bifunctional messenger RNAs in eukaryotes (1986) Cell, 47, pp. 481-483; Kozak, M., The scanning model for translation: An update (1989) J. Cell Biol., 108, pp. 229-241; Kunita, S., Mori, M., Terada, E., Sequence analysis of the nucleocapsid protein gene of rat coronavirus SDAV-681 (1993) Virology, 193, pp. 520-523; Kunita, S., Terada, E., Goto, K., Kagiyama, N., Sequence analysis and molecular detection of mouse hepatitis virus using the polymerase chain reaction (1992) Lab. Anim. Sci., 42, pp. 593-598; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-688; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Arch. Virol., 125, pp. 141-160; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Radecke, F., Billeter, M.A., The nonstruclural C protein is not essential for multiplication of Edmonston B measles virus in cultured cells (1996) Virology, 217, pp. 418-421; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Samuel, C.E., Polycistronic animal virus mRNAs (1989) Prog. Nucleic Acid Res. Mol. Biol., 37, pp. 127-153; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schwarz, B., Routledge, E., Siddell, S.G., Murine nonstructural protein ns2 is not essential for virus replication in transformed cells (1990) J. Virol., 64, pp. 4784-4791; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene of bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Shaw, M.W., Choppin, P.W., Lamb, R.A., A previously unrecognized influenza B virus glycoprotein from a bicistronic mRNA that also encodes the viral neuraminidase (1983) Proc. Natl. Acad. Sci. USA, 80, pp. 4879-11883; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York; Skinner, M.A., Siddell, S.G., Coronavirus JHM: Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acids Res., 11, pp. 5045-5054; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-111; Weiner, R.S., Andersen, T.T., Dias, J.A., Topographic analysis of the alpha-subunit of human follicle-stimulating hormone using site-specific antipeptide antisera (1990) Endocrinology, 127, pp. 573-579; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns 4 gene of mouse hepatitis virus (MHV), strain A59 contains two ORFs and thus differs from ns 4 of the JHM and S strains (1993) Arch. Virol., 129, pp. 301-309; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Masters, P.S.; Wadsworth Center, David Axelrod Institute, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States",,,0022538X,,JOVIA,"8995618","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031026431
"Liu D.X., Xu H.Y., Brown T.D.K.","8972667300;55703819800;56248391000;","Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites",1997,"Journal of Virology","71","3",,"1814","1820",,48,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031058476&partnerID=40&md5=bd55879edae14327df792001c147c1b6","Institute of Molecular Agrobiology, National University of Singapore, Singapore 118240, Singapore; Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom; Institute of Molecular Agrobiology, National University of Singapore, 59A the Fleming, 1 Science Park Dr., Singapore 118240, Singapore","Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, Singapore 118240, Singapore, Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom, Institute of Molecular Agrobiology, National University of Singapore, 59A the Fleming, 1 Science Park Dr., Singapore 118240, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, National University of Singapore, Singapore 118240, Singapore; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom","Proteolytic processing of the polyprotein encoded by mRNA 1 is an essential step in coronavirus RNA replication and gene expression. We have previously reported that an open reading frame (ORF) 1a-specific proteinase of the picornavirus 3C proteinase group is involved in processing of the coronavirus infectious bronchitis virus (IBV) 1a/1b polyprotein, leading to the formation of a mature viral protein of 100 kDa. We report here the identification of a novel 10-kDa polypeptide and the involvement of the 3C- like proteinase in processing of the ORF 1a polyprotein to produce the 10- kDa protein species. By using a region-specific antiserum, V47, raised against a bacterial-vital fusion protein containing IBV sequence encoded between nucleotides 11488 and 12600, the 10-kDa polypeptide was detected in lysates from both IBV-infected and plasmid DNA-transfected Vero cells. Coexpression, deletion, and mutagenesis studies showed that this novel polypeptide was encoded by ORF 1a from nucleotide 11545 to 11878 and was cleaved from the 1a polyprotein by the 3C-like proteinase domain. Evidence presented suggested that a previously predicted Q-S (Q3783S3784) dipeptide bond encoded by ORF 1a between nucleotides 11875 and 11880 was responsible for the release of the C terminus of the 10-kDa polypeptide and that a novel Q-N (Q3672N3673) dipeptide bond encoded between nucleotides 11542 and 11547 was responsible for the release of the N terminus of the 10-kDa polypeptide.",,"messenger rna; virus protein; animal cell; article; avian infectious bronchitis virus; controlled study; coronavirus; gene expression; nonhuman; open reading frame; priority journal; protein degradation; protein domain; site directed mutagenesis; vero cell; virus gene; virus replication; Animals; Binding Sites; Cercopithecus aethiops; Cysteine Endopeptidases; DNA Mutational Analysis; Infectious bronchitis virus; Peptides; Plasmids; Protein Precursors; Protein Processing, Post-Translational; Recombinant Fusion Proteins; Sequence Deletion; Vero Cells; Viral Proteins","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO. J., 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus rihosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Carroll, A.R., Rowlands, D.J., Clarke, B.E., The complete nucleotide sequence of the RNA coding for the primary translation product of foot-and-mouth disease virus (1984) Nucleic Acids Res., 12, pp. 2461-2472; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.Y., Donchenko, A.P., Nov, V.M., Coronavirus genome: Prediction of putative functional domain the non-structural polyprotein by comparative amino acid sequence annuals (1989) Nucleic Acids Res., 17, pp. 4847-4860; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Lai, C.J., Zhao, B., Hori, H., Bray, M., Infectious RNA transcribed from stably cloned full-length cDNA of dengue type-4 virus (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5139-5143; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF-1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3C protein with the virion envelope (1991) Virology, 185, pp. 911-917; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression and processing of an 87 kDa polypeptide encoded by ORF1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Unpublished observations; MacFarlane, S.A., Wallis, C.V., Taylor, S.C., Goulden, M.G., Wood, K.R., Davies, J.W., Construction and analysis of infectious transcripts synthesized from full-length clones of both genomic RNAs of pea early browning virus (1991) Virology, 182, pp. 124-129; Palmenberg, A.C., Proteolytic processing of picornaviral polyprotein (1990) Annu. Rev. Microbiol., 44, pp. 603-623; Parks, G.D., Baker, J.C., Palmenberg, A.C., Proteolytic cleavage of encephalomyocarditis viral capsid region substrates by precursors to the 3C enzyme (1989) J. Virol., 63, pp. 1054-1058; Quillet, L., Guilley, H., Jonard, G., Richards, K., In vitro synthesis of biologically active beet necrotic yellow vein virus RNA (1989) Virology, 172, pp. 293-301; Rice, C.M., Grakoui, A., Galler, R., Chambers, T.J., Transcription of infectious yellow fever RNA from full-length cDNA templates produced by in vitro ligation (1989) New Biol., 1, pp. 285-296; Skotnicki, M.L., Ding, S.W., Mackenzie, A.M., Gibbs, A.J., Infectious eggplant mosaic tymovirus and ononis yellow mosaic tymovirus from cloned cDNA (1993) Arch. Virol., 131, pp. 47-60; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Location of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol., 50, pp. 22-29; Sumiyoshi, H., Hoke, C.H., Trent, D.W., Infectious Japanese encephalitis virus RNA can be synthesized from in vitro-tigated cDNA templates (1992) J. Virol., 66, pp. 5425-5431; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930","Liu, D.X.; Institute of Molecular Agrobiology, National University of Singapore, 1 Science Park Dr., Singapore 118240, Singapore; email: imaliudx@lconis.nus.sg",,,0022538X,,JOVIA,"9032311","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031058476
"Gamble D.A., Lobbiani A., Gramegna M., Moore L.E., Colucci G.","7005559322;6602922948;6603580181;57202840812;55238541100;","Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens",1997,"Journal of Clinical Microbiology","35","3",,"673","675",,35,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031056199&partnerID=40&md5=299213bca5eb48958f24680efdb7c3da","Animal Medical Center, New York, NY, United States; Clonit SpA, Milan, Italy; Fondazione Ctro. Studi Patol. M., Milan, Italy; Fondazione Ctro. Studi Patol. M., via Pace 9, 20122 Milan, Italy","Gamble, D.A., Animal Medical Center, New York, NY, United States; Lobbiani, A., Clonit SpA, Milan, Italy; Gramegna, M., Clonit SpA, Milan, Italy; Moore, L.E., Animal Medical Center, New York, NY, United States; Colucci, G., Fondazione Ctro. Studi Patol. M., Milan, Italy, Fondazione Ctro. Studi Patol. M., via Pace 9, 20122 Milan, Italy","A diagnostic test for feline infectious peritonitis virus (FIPV) infection based on a nested PCR (nPCR) assay was developed and tested with FIPV, feline enteric coronavirus (FECV), canine coronavirus (CCV), and transmissible gastroenteritis virus (TGEV) and clinical fluid samples from cats with effusive feline infectious peritonitis (FIP). The target sequence for the assay is in the S1 region of the peplomer protein E2 gene. A vaccine strain of FIPV and two wild-type FIPV strains tested positive, but FECV, TGEV, and CCV tested negative. Preliminary tests with 12 cats with clinical evidence of effusive FIP and 11 cats with an illness associated with effusions, but attributed to other causes, were performed. Eleven of the 12 cats with effusive FIP tested positive, while 1 was negative. Ten of the 11 cats ill from other causes tested negative, while 1 was positive. On the basis of clinical laboratory and histopathologic criteria, the preliminary sensitivity and specificity of the assay were 91.6 and 94%, respectively.",,"article; cat disease; coronavirus; diagnostic accuracy; diagnostic value; nonhuman; polymerase chain reaction; priority journal; serodiagnosis; viremia; virus detection; virus strain; Animals; Base Sequence; Cats; Coronavirus; Coronavirus, Canine; Coronavirus, Feline; Diagnostic Errors; DNA Primers; DNA, Viral; Dogs; Feline Infectious Peritonitis; Polymerase Chain Reaction; Sensitivity and Specificity; Transmissible gastroenteritis virus; Canine coronavirus; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; Felis catus; Transmissible gastroenteritis virus","Barlough, J.E., Cats, coronaviruses and coronavirus antibody tests (1985) J. Small Anim. Pract., 26, pp. 353-362; Bohl, E.H., Gupta, R.K., Olquin, M.V., Saif, L., Antibody responses in serum, colostrum, and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect. Immun., 6, pp. 289-301; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A., Spaan, W.J., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J. Gen. Virol., 68, pp. 2639-2646; Erlich, H.A., Gelfand, D., Sninsky, J.J., Recent advances in the polymerase chain reaction (1991) Science, 252, pp. 1643-1651; Evermann, J.F., Baumgartener, L., Ott, R.L., Davis, E.V., McKeirman, A.J., Characterization of a feline infectious peritonitis virus isolate (1981) Vet. Pathol., 18, pp. 256-265; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavires isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Gerstman, B.B., Cappucci, D.T., Evaluating the reliability of diagnostic test results (1986) J. Am. Vet. Med. Assoc., 88, pp. 248-251; Herreweg, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissue, and body fluid of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Horzinek, M.C., Osterhaus, A.D.M.E., The virology and pathogenesis of feline infectious peritonitis (1979) Arch Virol., 59, pp. 1-15; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical, and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Maniatis, T., Fritsch, E.F., Sambrook, J., Agarose gel electrophoresis (1982) Molecular Cloning: A Laboratory Manual, pp. 150-163. , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infections peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens utilizing feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 2580-2585; Pedersen, N.C., Everman, J.F., McKeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Pedersen, N.C., Virologie and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Porter-Jordan, K., Rosenberg, E.I., Keiser, J.F., Gross, J.D., Ross, A.M., Nasim, S., Garrett, T., Nested polymerase chain reaction assay for the detection of cytomegalovirus overcomes false positives caused by contamination with fragmented DNA (1990) J. Med. Virol., 30, pp. 85-91; Shelly, S.M., Scarlett-Kranz, J., Blue, J.T., Protein electrophoresis on effusions from cats as a diagnostic test for feline infectious peritonitis (1988) JAAHA, 24, pp. 495-500; Weiss, R.C., Feline infectious peritonitis and other coronaviruses (1989) The Cat: Diseases and Clinical Managements, pp. 333-355. , R. G. Sherding (ed.), Churchill Livingstone, New York, N.Y","Colucci, G.; FCSPMAC, via Pace 9, 20122 Milan, Italy",,,00951137,,JCMID,"9041410","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0031056199
"Lane T.E., Paoletti A.D., Buchmeier M.J.","24722465300;7102074961;7006201704;","Disassociation between the in vitro and in vivo effects of nitric oxide on a neurotropic murine coronavirus",1997,"Journal of Virology","71","3",,"2202","2210",,77,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031046897&partnerID=40&md5=0ba818df0d1445f5f262e797f3594d60","Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States; Scripps Research Institute, vCVN 8, 10666 N. Torrey Pines Rd., San Diego, CA 92037, United States","Lane, T.E., Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States; Paoletti, A.D., Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States; Buchmeier, M.J., Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States, Scripps Research Institute, vCVN 8, 10666 N. Torrey Pines Rd., San Diego, CA 92037, United States","Intranasal inoculation of the neuroattenuated OBLV60 strain of mouse hepatitis virus results in infection of mitral neurons in the olfactory bulb, followed by spread along olfactory and limbic pathways to the brain. Immunocompetent BALB/c mice were able to clear virus by 11 days postinfection (p.i.). Gamma interferon (IFN-γ) may play a role in clearance of OBLV60 from infected immunocompetent BALB/c mice through a nonlytic mechanism. Among the variety of immunomodulatory activities of IFN-γ is the induction of expression of inducible nitric oxide synthase (iNOS), an enzyme responsible for the production of nitric oxide (NO). Studies were undertaken to investigate the role of IFN-γ and NO in host defense and clearance of OBLV60 from the central nervous system (CNS). Exposure of OBLV60-infected OBL21a cells, a mouse neuronal cell line, to the NO-generating compound S-nitroso- L-acetyl penicillamine resulted in a significant decrease in viral replication, indicating that NO interfered with viral replication. Furthermore, infection of IFN-γ knockout (GKO) mice and athymic nude mice with OBLV60 resulted in low-level expression of iNOS mRNA and protein in the brains compared to that of OBLV60-infected BALB/c mice. Nude mice were unable to clear virus and eventually died between days 11 and 14 p.i. (B. D. Pearce, M. V. Hobbs, T. S. McGraw, and M. J. Buchmeier, J. Virol. 68:5483-5495, 1994); however, GKO mice survived infection and cleared virus by day 18 p.i. These data suggest that IFN-γ production in the olfactory bulb contributed to but may not be essential for clearance of OBLV60 from the brain. In addition, treatment of OBLV60-infected BALB/c mice with aminoguanidine, a selective inhibitor of iNOS activity, did not result in any increase in mortality, and the mice cleared the virus by 11 days p.i. These data suggest that although NO was able to block replication of virus in vitro, expression of iNOS with NO release in vivo did not appear to be the determinant factor in clearance of OBLV60 from CNS neurons.",,"aminoguanidine; gamma interferon; nitric oxide; nitric oxide synthase; animal cell; animal experiment; animal model; article; controlled study; host resistance; immunomodulation; mouse; murine hepatitis coronavirus; nonhuman; nude mouse; olfactory bulb; priority journal; virus replication; Animals; Cell Line; Coronavirus Infections; Enzyme Inhibitors; In Situ Hybridization; Interferon Type II; Mice; Mice, Inbred BALB C; Mice, Knockout; Mice, Nude; Murine hepatitis virus; Nitric Oxide; Nitric Oxide Synthase; Penicillamine; RNA, Messenger; RNA, Viral; S-Nitroso-N-Acetylpenicillamine; Time Factors; Tumor Cells, Cultured; Virus Replication","Akarid, K., Sinet, M., Desforges, B., Gougerot-Pocidalo, M., Inhibitory effect of nitric oxide on the replication of a murine retrovirus in vitro and in vivo (1995) J. 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"Baric R.S., Yount B., Hensley L., Peel S.A., Chen W.","7004350435;6603564156;55303564700;15722521700;7409646434;","Episodic evolution mediates interspecies transfer of a murine coronavirus",1997,"Journal of Virology","71","3",,"1946","1955",,66,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031041457&partnerID=40&md5=840d831965783cca650f6bf48cd1b40a","Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States; Dept. of Microbiology and Immunology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599, United States; Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States","Baric, R.S., Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States, Dept. of Microbiology and Immunology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599, United States, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States; Yount, B., Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States; Hensley, L., Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States; Peel, S.A., Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States; Chen, W., Program in Infectious Diseases, Department of Epidemiology, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States","Molecular mechanisms permitting the establishment and dissemination of a virus within a newly adopted host species are poorly understood. Mouse hepatitis virus (MHV) strains (MHV-A59, MHV-JHM, and MHV-A59/MHV-JHM) were passaged in mixed cultures containing progressively increasing concentrations of non-permissive Syrian baby hamster kidney (BHK) cells and decreasing concentrations of permissive murine DBT cells. From MHV-A59/MHV-JHM mixed infection, variant viruses (MHV-H1 and MHV-H2) which replicated efficiently in BHK cells were isolated. Under identical treatment conditions, the parental MHV-A59 or MHV-JHM strains failed to produce infectious virus or transcribe detectable levels of viral RNA or protein. The MHV-H isolates were polytrophic, replicating efficiently in normally nonpermissive Syrian hamster smooth muscle (DDT-1), Chinese hamster ovary (CHO), human adenocarcinoma (HRT), primate kidney (Vero), and murine 17Cl-1 cell lines. Little if any virus replication was detected in feline kidney (CRFK) and porcine testicular (ST) cell lines. The variant virus, MHV-H2, transcribed seven mRNAs equivalent in relative abundance and size to those synthesized by the parental virus strains. MHV-H2 was an RNA recombinant virus containing a crossover site in the S glycoprotein gene. At the molecular level, episodic evolution and positive Darwinian natural selection were apparent within the MHV-H2 S and HE glycoprotein genes. These findings differ from the hypothesis that neutral changes are the predominant feature of molecular evolution and argue thai changing ecologies actuate episodic evolution in the MHV spike glycoprotein genes that govern interspecies transfer and spread into alternative hosts.",,"virus protein; virus rna; animal cell; article; cat; cell strain bhk; cho cell; controlled study; evolution; human; human cell; mouse; murine hepatitis coronavirus; natural selection; nonhuman; priority journal; species; swine; vero cell; virus cell interaction; virus recombinant; virus replication; Animals; Cats; Cell Line; Cercopithecus aethiops; CHO Cells; Cricetinae; Evolution; Genome, Viral; Humans; Mesocricetus; Mice; Murine hepatitis virus; Rats; RNA, Viral; Swine; Transcription, Genetic; Tumor Cells, Cultured; Vero Cells","Allan, J.S., Viral evolution and AIDS (1992) J. 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Dis., 2, pp. 64-70; Morse, S.S., Schluederberg, A., Emerging viruses: The evolution of viruses and viral diseases (1990) J. Infect. Dis., 162, pp. 1-15; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence of O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus (1993) J. Gen. Virol., 74, pp. 1981-1989; Murphy, F.A., New emerging and reemerging infectious diseases (1994) Adv. Virus Res., 43, pp. 1-52; Murray, K., Selleck, P., Hooper, P., Hyatt, A., Gould, A., Gleeson, L., Westbury, H., Ketterer, P., A morbillivirus that caused fatal disease in horses and humans (1995) Science, 268, pp. 94-97; Murray, M.G., Bradley, J., Yang, X.-F., Wimmer, E., Moss, E.G., Racaniello, V.R., Poliovirus host range is determined by a short amino acid sequence in neutralization antigenic site I (1988) Science, 241, pp. 213-215; Murray, R.S., Brown, B., Brian, D., Gabirac, G.F., Detection of coronavirus-RNA and antigen in multiple sclerosis brain (1992) Ann. Neurol., 31, pp. 525-533; Murray, R.S., Cal, G.-Y., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in the primate central nervous system (1992) Virology, 188, pp. 274-284; Nichol, S.T., Rowe, J.D., Fitch, W.M., Punctuated equilibrium and positive Darwinian evolution in vesicular stomatitis virus (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 10424-10428; Ohta, T., Synonymous and nonsynonymous substitutions in mammalian genes and the nearly neutral theory (1995) J. Mol. Evol., 40, pp. 56-63; Parish, C.R., The emergence and evolution of canine parvovirus - An example of recent host range mutation (1994) Semin. Virology, 5, pp. 121-132; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucteocapsid protein (1990) Virology, 179, pp. 463-468; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Schmidt, I., Skinner, M.A., Siddell, S.G., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Scholtissek, C., Koennecke, I., Rott, R., Host range recombinants of fowl plaque (influenza A) virus (1978) Virology, 91, pp. 79-85; Shope, R.E., Swine influenza. III. Filtration experiments and etiology (1931) J. Exp. Med., 54, pp. 373-380; Shope, R.E., Swine influenza (1958) Diseases of Swine, 1st Ed., pp. 81-91. , H. W. Dunne (ed.), Iowa State University Press, Ames; Skinner, M.A., Ebner, D., Siddell, S.G., Coronavirus MHV-JHM mRNA 5 has a sequence arrangement which potentially allows translation of a second, downstream open reading frame (1985) J. Gen. Virol., 66, pp. 581-592; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Subbarao, E.K., London, W., Murphy, B.R., A single amino acid in the PB2 gene of influenza a virus is a determinant of host range (1993) J. Virol., 67, pp. 1761-1764; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Tian, S.-F., Buckler-White, A.J., London, W.T., Reck, L.J., Chanock, R.M., Murphy, B.R., Nucleoprotein and membrane protein genes are associated with restriction of replication of influenza A/Mallard?NY/78 virus and its reassortants in squirrel monkey respiratory tract (1985) J. Virol., 53, pp. 771-775; Truyen, U., Evermann, J.F., Vieler, E., Parrish, C.R., Evolution of canine parvovirus involved loss and gain of feline host range (1996) Virology, 215, pp. 186-189; Vlasak, R., Luytjes, W., Spaan, W.J.M., Palese, P., Human and bovine coronaviruses recognize sialic acid containing receptors similar to those of influenza viruses (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 4526-4529; Weaver, S.C., Scott, T.W., Rico-Hesse, R., Molecular evolution of eastern equine encephalomyelitis virus in North America (1991) Virology, 182, pp. 774-781; Webster, R.G., Geraci, J.R., Petursson, G., Skirnmission, K., Conjunctivitis in human beings caused by influenza a virus of seals (1981) N. Engl. J. Med., 304, pp. 911-914; Wimmer, E., Cellular receptors for viruses (1994) Cellular Receptors for Viruses, pp. 1-14. , E. Wimmer (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y; Yin, F.H., Lomax, N.B., Host range mutants of human rhinoviruses in which nonstructural genes are altered (1983) J. Virol., 48, pp. 410-418; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Yokomori, K., Banner, L.R., Lai, M.M.C., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin gene of human coronavirus OC43: Phylogenetic relationships to bovine and murine coronaviruses and influenza C virus (1992) Virology, 180, pp. 221-228","Baric, R.S.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States",,,0022538X,,JOVIA,"9032326","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031041457
"Erhard M.H., Schmidt P., Hofmann A., Bergmann J., Mittermeier P., Kaufmann P., Wiesmüller K.-H., Bessler W.G., Lösch U.","7006079567;57199317244;7401495002;7203025536;6504232571;7201921488;7006478708;57212403148;7003644748;","The Lipopeptide, Pam3Cys-Ser-(Lys)4: An Alternative Adjuvant to Freund's Adjuvant for the Immunisation of Chicken to Produce Egg Yolk Antibodies",1997,"ATLA Alternatives to Laboratory Animals","25","2",,"173","181",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2542571188&partnerID=40&md5=cd6286b9bab0105afcbf6de45fcd825f","Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Institut für Tierpathologie, Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; NMI, Universität Reutlingen, Gustav-Werner-Strasse 3, 72762 Reutlingen, Germany; Institut für Immunbiologie, Universität Freiburg, Stefan-Meier-Strasse 8, 79104 Freiburg, Germany","Erhard, M.H., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Schmidt, P., Institut für Tierpathologie, Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Hofmann, A., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Bergmann, J., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Mittermeier, P., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Kaufmann, P., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany; Wiesmüller, K.-H., NMI, Universität Reutlingen, Gustav-Werner-Strasse 3, 72762 Reutlingen, Germany; Bessler, W.G., Institut für Immunbiologie, Universität Freiburg, Stefan-Meier-Strasse 8, 79104 Freiburg, Germany; Lösch, U., Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany","This study describes an alternative adjuvant for the immunisation of chicken. The lipopeptide, Pam3Cys-Ser-(Lys)4 (PCSL), has been demonstrated to be a very potent adjuvant, by immunisation with the hapten methyl phosphonic acid paraaminophenyl 1,2,2-trimethylpropyl diester, with coronavirus, with rotavirus and with the Escherichia coli K99 pilus antigen. The antibody titres in chickens that received PCSL were compared with those in animals that received Freund's complete adjuvant/Freund's incomplete adjuvant (FCA/FIA). Antigen-dependent differences in antibody titres could be shown The optimal dosage for PCSL was 250μg per injection. Whereas injection of FCA/FIA. resulted in chronic inflammatory alterations, mostly accompanied with granulomatous reactions, no long-term tissue damage could be found with PCSL. When PCSL was used as the adjuvant, the total immunoglobulin Y (IgY) levels in chicken sera were constant during the immunisation period (20.2mg/ml, SD ± 1.3), and were significantly different (p &lt; 0.0001) from those in chickens given FCA as adjuvant (26.6mg/ml, SD ± 4.9). IgY concentrations in the egg yolks showed no significant differences in both groups (PCSL - 13.7mg/ml, SD ± 3.7; FCA -13.5mg/ml, SD ± 4.2), and were significantly lower (p &lt; 0.0001) than the IgY serum levels.","Adjuvant; Antibody titre; Chicken egg yolk antibodies; Freund's adjuvant; Histopathology; IgY levels; Immunoglobulin Y (IgY); Lipopeptide",,"Bar-Joseph, M., Malkinson, M., Hen egg yolk as a source of antiviral antibodies in the enzyme-linked immunosorbent assay (ELISA); a comparison of two plant viruses (1980) Journal of Virological Methods, 1, pp. 179-183; Gottstein, B., Hemmeler, E., Egg yolk immunoglobulin Y as an alternative antibody in the serology of ecchinococcosis (1985) Zeitschrift für Parasitenkunde, 71, pp. 273-276; Larsson, A., Karlsson-Parra, A., Sjöquist, J., Use of chicken antibodies in enzyme immunoassays to avoid interference by rheumatoid factors (1991) Clinical Chemistry, 37, pp. 411-414; Ntakarutimana, V., Demedts, P., Van Sande, M., A simple and economical strategy for downstream processing of specific antibodies to human transferrin from egg yolk (1992) Journal of Immunological Methods, 153, pp. 133-140; Sturmer, A.M., Driscoll, D.P., Jackson-Matthews, D.E., A quantitative immunoassay usíng chicken antibodies for detection of native and recombinant α-amidating enzyme (1992) Journal of Immunological Methods, 146, pp. 105-110; Larsson, A., Lindahl, T., Chicken antiprotein G for the detection of small amounts of protein G (1993) Hybridoma, 12, pp. 143-147; Wiedemann, V., Linckh, E., Kühlmann, R., Schmidt, P., Losch, U., Chicken egg antibodies for prophylaxis and therapy of infectious intestinal diseases. V. in vivo studies on protective effects against Escherichia coli diarrhoea in pigs (1991) Journal of Veterinary Medicine Series B, 38, pp. 283-291; Ikemori, Y., Kuroki, M., Peralta, R., Yokoyama, Y., Protection of neonatal calves against fatal enteric colibacillosis by administration of egg powder from hens immunized with K99-pilated enterotoxic Escherichia coli (1992) American Journal of Veterinary Research, 53, pp. 2005-2008; Yokoyama, H.R., Peralta, R.C., Diaz, R., Sendo, S., Ikemori, Y., Kodama, Y., Passive protection effect of chicken egg yolk immunoglobins against experimental enterotoxic Escherichia coli infection in neonatal piglets (1992) Infectious Immunity, 60, pp. 998-1007; Erhard, M.H., Kellner, J., Eichelberger, J., Lösch, U., New aspects in oral immunoprophylaxis for the prevention of infectious diarrhoea of newborn calves: A field study with specific antibodies (1993) Berliner und Münchner Tierärztliche Wochenschrift, 106, pp. 383-387; Kellner, J., Erhard, M.H., Renner, M., Lösch, U., A field trial of the treatment of diarrhoea in piglets with specific antibodies (1994) Tierärztliche Unschau, 49, pp. 31-34; Ozpinar, H., Erhard, M.H., Aytug, N., Ozpinar, A., Baklaci, C., Karamüptüglu, S., Hofmann, A., Lösch, U., Dose-dependent effects of specific egg-yolk antibodies on diarrhoea of newborn calves (1996) Preventive Veterinary Medicine, 27, pp. 67-73; Erhard, M.H., Bergmann, J., Renner, M., Hofmann, A., Heinrïtzi, K., Prophylactic effect of specific egg yolk antibodies in diarrhoea of weaned piglets caused by Escherichia coli K88 [F4] (1996) Journal of Veterinary Medicine Series A, 43, pp. 217-223; Freund, J., McDermott, K., Sensitisation to horse serum by means of adjuvants (1942) Proceedings of the Society for Experimental Biology and Medicine, 49, pp. 548-553; Hillemann, M.R., Critical appraisal of emulsified oil adjuvants applied to viral vaccines (1966) Progress in Medical Virology, 8, pp. 131-182; Murray, R., Cohen, P., Hardegree, M.C., Mineral oil adjuvants: Biological and chemical studies (1972) Annals of Allergy, 30, pp. 146-151; Altmann, A., Dixon, F.J., Immunomodifiers in vaccines (1989) Advanced Veterinary Science of Comparative Medicine, 33, pp. 301-343; Wiedemann, F., Link, R., Pumpe, K., Jacobshagen, U., Schaefer, H.E., Wiesmüller, K.-H., Hummel, R.-P., Böltz, T., Histopathological studies on the local reactions induced by complete Freund's adjuvant (CFA), bacterial lipopolysaccharide (LPS), and synthetic lipopeptide (P3C) conjugates (1991) Journal of Pathology, 164, pp. 265-271; Wanke, R., Schmidt, P., Erhard, M.H., Sprick-Sanjose Messing, A., Stangassinger, M., Schmahl, W., Hermanns, W., Freunds complete adjuvant in the chicken: Efficient immunostimulation but severe local inflammation (1996) Journal of Veterinary Medicine Series A, 43, pp. 243-253; Wiesmüller, K.-H., Bessler, W.G., Jung, G., Synthesis of the mitogenic S-(2,3-bis[palmitolyloxy]propyl)N-palmitoyl-pentapeptide from Escherichia coli lipoprotein (1983) Zeitschrift für Physiologische Chemie, Hoppe-Seyler, 364, pp. 593-606; Reitermann, A., Metzger, J., Wiesmüller, K.-H., Jung, G., Bessler, W.G., Lipopeptide derivates of bacterial lipoprotein constitute potent immune adjuvants combined or covalently coupled to antigen or hapten (1989) Biological Chemistry, Hoppe-Seyler, 370, pp. 343-352; Kellner, J., Erhard, M.H., Schranner, I., Lösch, U., The influence of various adjuvants on antibody synthesis following immunization with an hapten (1992) Biological Chemistry, Hoppe-Seyler, 373, pp. 51-55; Suttnar, J., Hrkal, Z., Vodrazka, Z., Affinity chromatography of serum haemopexin (1977) Journal of Chromatography, 131, pp. 453-457; Suter, M., A modified ELISA technique for anti-hapten antibodies (1982) Journal of Immunological Methods, 78, pp. 173-190; Schmidt, P., Kühlmann, R., Lösch, U., A competitive enzyme immunoassay for detection and quantification of organophosphorus compounds (1988) Zeitschrift für Naturforschung, 46, pp. C167-C172; Erhard, M.H., Von Quistorp, I., Schranner, I., Jüngling, A., Kaspers, B., Schmidt, P., Kühlmann, R., Development of specific enzyme-linked immunosorbent antibody systems for the detection of chicken immunoglobulins G, M and A using monoclonal antibodies (1992) Poultry Science, 71, pp. 302-310; Kowalczyk, K., Daiss, J., Halpern, J., Roth, T.F., Quantification of maternal-fetal IgG transport in the chicken (1985) Immunology, 54, pp. 755-762; Schade, R., Staak, C., Hendriksen, C., Erhard, M.H., Hugl, H., Koch, G., Larsson, A., Straughan, D., The production of avian (egg yolk) antibodies: IgY. The report and recommendations of ECVAM workshop 21 (1996) ATLA, 24, pp. 925-934","Erhard, M.H.; Inst. F. Physiol., Physiologische C., Tierärztliche Fakultät, Universität München, Veterinärstrasse 13, 80539 München, Germany",,,02611929,,AALAD,,"English","ATLA Altern. Lab. Anim.",Article,"Final",,Scopus,2-s2.0-2542571188
"Rao P.V., Kumari S., Gallagher T.M.","36868545200;57197190107;7202310503;","Identification of a contiguous 6-residue determinant in the MHV receptor that controls the level of virion binding to cells",1997,"Virology","229","2",,"336","348",,38,"10.1006/viro.1997.8446","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031575821&doi=10.1006%2fviro.1997.8446&partnerID=40&md5=168e94c98d58c9b4bdc0f062be94068c","Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153, United States","Rao, P.V., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153, United States; Kumari, S., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153, United States; Gallagher, T.M., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153, United States","Murine carcinoembryonic antigens serve as receptors for the binding and entry of the enveloped coronavirus mouse hepatitis virus (MHV) into cells. Numerous receptor isoforms are now known, and each has extensive differences in its amino terminal immunoglobulin-like domain (NTD) to which MHV binds via its protruding spike proteins. Some of these receptor alterations may affect the ability to bind viral spikes. To identify individual residues controlling virus binding differences, we have used plasmid and vaccinia virus vectors to express two forms of MHV receptor differing only in their NTD. The two receptors, designated biliary glycoproteins (Bgp) 1a and 1(NTD)b, varied by 29 residues in the 107 amino acid NTD. When expressed from cDNAs in receptor-negative HeLa cells, these two Bgp molecules were displayed on cell surfaces to equivalent levels, as both were equally modified by a membrane-impermeant biotinylation reagent. Infectious center assays revealed that the 1a isoform was 10 to 100 times more effective than 1(NTD)b in its ability to confer sensitivity to MHV (strain A59) infection. Bgp1a was also more effective than BgP1(NTD)b in comparative virus adsorption assays, binding 6 times more MHV (strain A59) and 2.5 times more MHV (strain JHMX). Bgp1a was similarly more effective in promoting the capacity of viral spikes to mediate intercellular membrane fusion as judged by quantitation of syncytia following cocultivation of spike and receptor-bearing cells. To identify residues influencing these differences, we inserted varying numbers of 1b residues into the Bgp1a background via restriction fragment exchange and site-directed mutagenesis. Analysis of the resulting chimeric receptors showed that residues 38 to 43 of the NTD were key determinants of the binding and fusion differences between the two receptors. These residues map to an exposed loop (C-C' loop) in a structural model of the closely related human carcinoembryonic antigen.",,"carcinoembryonic antigen; membrane receptor; amino acid sequence; article; cell invasion; controlled study; Coronavirus; Murine hepatitis coronavirus; nonhuman; priority journal; virus cell interaction; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus","Aiyar, A., Leis, J., (1993) Modification of the Megaprimer Method of PCR Mutagenesis: Improved Amplification of the Final Product, 14, p. 366. , 368; Aoki, J., Koike, S., Ise, I., Yoshida, Y.S., Nomoto, A., Amino acid residues on human poliovirus receptor involved in interaction with poliovirus (1994) J. Biol. Chem., 269, pp. 8431-8438; Barthold, S.W., Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab. Anim. Sci., 37, pp. 36-40; Barthold, S.W., Beck, D.S., Smith, A.L., Mouse hepatitis virus nasoencephalopathy is dependent upon virus strain and host genotype (1986) Arch. Virol., 91, pp. 247-256; Bates, P.A., Luo, J., Sternberg, M.J.E., A predicted three-dimensional structure of the carcinoembryonic antigen (CEA) (1992) FEBS Lett., 301, pp. 207-214; Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Boyle, J.F., Weismiller, D.G., Homes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. Virol., 61, pp. 185-189; Broder, C.C., Kennedy, P.E., Michaels, F., Berger, E.A., Expression of foreign genes in cultured human primary macrophages using recombinant vaccinia virus vectors (1994) Gene, 142, pp. 167-174; Chen, D.S., Asanaka, M., Yokomori, K., Wang, F.-I., Hwang, S.B., Li, H.P., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Chen, W., Baric, R.S., Molecular anatomy of mouse hepatitis virus persistence: Coevolution of increased host cell resistance and virus virulence (1996) J. Virol., 70, pp. 3947-3960; Choe, H.R., Sodroski, J., Contribution of charged amino acids in the CDR2 region of CD4 to HIV-1 gp120 binding (1992) J. Acquired Immune Defic. Syndr., 5, pp. 204-210; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Compton, S.R., Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors (1994) Virology, 203, pp. 197-201; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.-S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Dveksler, G.S., Basile, A.A., Cardellichio, C.B., Holmes, K.V., Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain (1995) J. Virol., 69, pp. 543-546; Elroy-Stein, O., Moss, B., Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6743-6747; Falkner, F.G., Moss, B., Escherichia coli (1988) J. Virol., 62, pp. 1849-1854; Felgner, P.L., Gadek, T.R., Holm, M., Roman, R., Chan, H.W., Wenz, M., Northrop, J.P., Danielsen, M., Lipofection: A highly efficient, lipid-mediated DNA-transfection procedure (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 7413-7417; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. 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Virol., 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56","Gallagher, T.M.; Dept. of Microbiology/Immunology, Loyola University Medical Center, 2160 South First Avenue, Maywood, IL 60153, United States; email: tgallag@luc.edu",,"Academic Press Inc.",00426822,,VIRLA,"9126247","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0031575821
"Zhang L., Homberger F., Spaan W., Luytjes W.","15039884400;7003348988;7007172944;6701683324;","Recombinant genomic RNA of coronavirus MHV-A59 after coreplication with a DI RNA containing the MHV-RI spike gene",1997,"Virology","230","1",,"93","102",,5,"10.1006/viro.1997.8460","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031592616&doi=10.1006%2fviro.1997.8460&partnerID=40&md5=f3def11444c9f47cb80c7c154082751a","Department of Virology, Leiden University, Leiden, Netherlands; Inst. of Laboratory Animal Science, University of Zurich, Zurich, Switzerland","Zhang, L., Department of Virology, Leiden University, Leiden, Netherlands, Inst. of Laboratory Animal Science, University of Zurich, Zurich, Switzerland; Homberger, F., Inst. of Laboratory Animal Science, University of Zurich, Zurich, Switzerland; Spaan, W., Department of Virology, Leiden University, Leiden, Netherlands; Luytjes, W., Department of Virology, Leiden University, Leiden, Netherlands","A strategy for targeted RNA recombination between the spike gene on the genomic RNA of MHV-A59 and a synthetic DI RNA containing the MHV-RI spike gene is described. The MHV-RI spike gene contains several nucleotide differences from the MHV-A59 spike gene that could be used as genetic markers, including a stretch of 156 additional nucleotides starting at nucleotide 1497. The MHV-RI S gene cDNA (from nucleotide 277-termination codon) was inserted in frame into pMIDI, a full-length cDNA clone of an MHV-A59 DI, yielding pDPRIS. Using the vaccinia vTF7.3 system, RNA was transcribed from pDPRIS upon transfection into MHV-A59-infected L cells. DPRIS RNA was shown to be replicated and passaged efficiently. MHV-A59 and the DPRIS DI particle were copassaged several times. Using a highly specific and sensitive RT-PCR, recombinant genomic RNA was detected in intracellular RNA from total lysates of pDPRIS-transfected and MHV-A59 infected cells and among genomic RNA that was agarose gel-purified from these lysates. More significantly, specific PCR products were found in virion RNA from progeny virus. PCR products were absent in control mixes of intracellular RNA from MHV-A59-infected cells and in vitro-transcribed DPRIS RNA. PCR products from intracellular RNA and virion RNA were cloned and 11 independent clones were sequenced. Crossovers between A59 and RI RNA were found upstream of nucleotide 1497 and had occurred between 106 nucleotides from the 5'-border and 73 nucleotides from the 3'-border of sequence homologous between A59 and RI S genes. We conclude that homologous RNA recombination took place between the genomic RNA template and the synthetic DI RNA template at different locations, generating a series of MHV recombinant genomes with chimeric S genes.",,"recombinant RNA; animal cell; article; controlled study; Coronavirus; DNA sequence; mouse; nonhuman; priority journal; reverse transcription polymerase chain reaction; virus recombination; virus replication; Animalia; Coronavirus; Murine hepatitis virus; Vaccinia","Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Barthold, S.W., Mouse hepatitis virus biology and epizootiology (1986) Viral and Mycoplasmal Infections of Laboratory Rodents, , New York: Academic Press. p. 571-601; Barthold, S.W., Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab. 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Virol., 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 13, pp. 3375-3381; Van Der Most, R.G., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98","Luytjes, W.; Department of Virology, Leiden University, Leiden, Netherlands; email: luytjes@virology.azl.nl",,"Academic Press Inc.",00426822,,VIRLA,"9126265","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0031592616
"Gallagher T.M.","7202310503;","A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor",1997,"Journal of Virology","71","4",,"3129","3137",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030896673&partnerID=40&md5=8c512189d80c247ee4f990ba94867020","Dept. of Microbiology and Immunology, Loyola University, Medical Center, Maywood, IL 60153, United States; Dept. of Microbiology and Immunology, Loyola University, Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States","Gallagher, T.M., Dept. of Microbiology and Immunology, Loyola University, Medical Center, Maywood, IL 60153, United States, Dept. of Microbiology and Immunology, Loyola University, Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States","Murine hepatitis virus (MHV), a coronavirus, initiates infection by binding to its cellular receptor (MHVR) via spike (S) proteins projecting from the virion membrane. The structures of these S proteins vary considerably among MHV strains, and this variation is generally considered to be important in determining the strain-specific pathologies of MHV infection, perhaps by affecting the interaction between MHV and the MHVR. To address the relationships between S variation and receptor binding, assays capable of measuring interactions between MHV and MHVR were developed. The assays made use of a novel soluble form of the MHVR, sMHVR-Ig, which comprised the virus- binding immunoglobulin-like domain of MHVR fused to the Fc portion of human immunoglobulin GL sMHVR-Ig was stably expressed as a disulfide-linked dimer in human 293 EBNA cells and was immobilized to Sepharose-protein G via the Fc domain. The resulting Sepharose beads were used to adsorb radiolabelled MHV particles. At 4°C, the beads specifically adsorbed two prototype MHV strains, MHV JHM (strain 4) and a tissue culture-adapted mutant of MHV JHM, the JHMX strain. A shift to 37°C resulted in elution of JHM but not JHMX. This in vitro observation of JHM (but not JHMX) elution from its receptor at 37°C was paralleled by a corresponding 37°C elution of receptor-associated JHM (but not JHMX) from tissue culture cells. The basis for this difference in maintenance of receptor association was correlated with a large deletion mutation present within the JHMX S protein, as sMHVR-Ig exhibited relatively thermostable binding to vaccinia virus-expressed S proteins containing the deletion. These results indicate that naturally occurring mutations in the coronavirus S protein affect the stability of the initial interaction with the host cell and thus contribute to the likelihood of successful infection by incoming virions. These changes in virus entry features may result in coronaviruses with novel pathogenic properties.",,"immunoglobulin fc fragment; immunoglobulin g1; virus protein; virus receptor; animal cell; article; controlled study; hela cell; human; human cell; mouse; murine hepatitis coronavirus; nonhuman; point mutation; priority journal; protein domain; receptor binding; vaccinia virus; virion; virus adsorption; virus cell interaction; virus particle; Animals; Cell Line; Evolution, Molecular; Glycoproteins; Hela Cells; Humans; Immunoglobulin Fc Fragments; Immunoglobulin G; Membrane Glycoproteins; Mice; Murine hepatitis virus; Receptors, Virus; Recombinant Fusion Proteins; Species Specificity; Temperature; Variation (Genetics); Viral Envelope Proteins; Virion","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of MHV during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Asanaka, M., Lai, M.M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Banner, L.R., Keck, J.G., Lai, M.M., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Barnett, E., Cassell, M., Perlman, S., Two neurotropic viruses, herpes simplex virus type 1 and mouse hepatitis virus, spread along different neural pathways from the main olfactory bulb (1993) Neuroscience, 157, pp. 1007-1025; Bates, P.A., Luo, J., Sternberg, M.J.E., A predicted three-dimensional structure for the carcinoembryonic antigen (CEA) (1992) FEBS Lett., 301, pp. 207-214; Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Castro, R., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J. 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Sci. USA, 74, pp. 5463-5467; Sawicki, S.G., Lu, J.-H., Holmes, K.V., Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from the epigenetic expression of the MHV receptor (1995) J. Virol., 69, pp. 5535-5543; Siddell, S.G., The small membrane protein (1995) The Coronaviridae, pp. 181-189. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect. Immun., 6, pp. 501-507; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. 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Cell Biol., 33, pp. 281-293; Vennema, H., Heignen, L., Zijderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol., 28, pp. 298-303; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938","Gallagher, T.M.; Microbiology/Immunology Department, Loyola University Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States; email: tgallag@luc.edu",,,0022538X,,JOVIA,"9060676","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030896673
"Krempl C., Schultze B., Laude H., Herrler G.","6602462665;7006104520;7006652624;7006339246;","Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus",1997,"Journal of Virology","71","4",,"3285","3287",,91,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030893578&partnerID=40&md5=a25d5527c38c92b6865896bc385f0b3a","Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany","Krempl, C., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany; Schultze, B., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany; Laude, H., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany; Herrler, G., Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany","Enteropathogenic transmissible gastroenteritis virus (TGEV), a porcine coronavirus, is able to agglutinate erythrocytes because of sialic acid binding activity. Competitive inhibitors that may mask the sialic acid binding activity can be inactivated by sialidase treatment of virions. Here, we show that TGEV virions with efficient hemagglutinating activity were also obtained when cells were treated with sialidase prior to infection. This method was used to analyze TGEV mutants for hemagglutinating activity. Recently, mutants with strongly reduced enteropathogenicity that have point mutations or a deletion of four amino acids within residues 145 to 155 of the S protein have been described. Here, we show that in addition to their reduced pathogenicity, these mutants also have lost hemagglutinating activity. These results connect sialic acid binding activity with the enteropathogenicity of TGEV.",,"sialic acid; sialidase; vitronectin; article; binding affinity; coronavirus; hemagglutination; nonhuman; point mutation; priority journal; virus mutant; virus pathogenesis; Animals; Cell Line; Chickens; Hemagglutinins; LLC-PK1 Cells; Male; Membrane Glycoproteins; Neuraminidase; Point Mutation; Receptors, Virus; Sialic Acids; Swine; Transmissible gastroenteritis virus; Viral Envelope Proteins",,"Herrler, G.; Institut fur Virologie, Philipps-Universitat Marburg, Robert-Koch-Str. 17, 35037 Marburg, Germany; email: herrler@mailer.uni-marburg.de",,,0022538X,,JOVIA,"9060696","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030893578
"Cristallo A., Gambaro F., Biamonti G., Ferrante P., Battaglia M., Cereda P.M.","6603250884;6506375719;7007029268;7006479718;7201908369;7003845258;","Human coronavirus polyadenylated RNA sequences in cerebrospinal fluid from multiple sclerosis patients",1997,"New Microbiologica","20","2",,"105","114",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031115531&partnerID=40&md5=83bf7bf2c689998cf2d0097029624227","Institute of Biochemistry, University of Pavia, V.le Taramelli 3B, 27100 Pavia, Italy; Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy; Pharmacia Biotech, via A. Volta 16/C, 20093 Cologno Monzese (Milano), Italy; Inst. of Biochem. and Evol. Genetics, CNR, via Abbuiategrasso 207, 27100 Pavia, Italy; Don Carlo Gnocchi Foundation, via Capecelatro 66, 20148 Milano, Italy; Institute of Experimental Medicine, CNR, via Marx 15-43, 00137 Roma, Italy","Cristallo, A., Institute of Biochemistry, University of Pavia, V.le Taramelli 3B, 27100 Pavia, Italy, Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy; Gambaro, F., Pharmacia Biotech, via A. Volta 16/C, 20093 Cologno Monzese (Milano), Italy; Biamonti, G., Inst. of Biochem. and Evol. Genetics, CNR, via Abbuiategrasso 207, 27100 Pavia, Italy; Ferrante, P., Don Carlo Gnocchi Foundation, via Capecelatro 66, 20148 Milano, Italy; Battaglia, M., Institute of Experimental Medicine, CNR, via Marx 15-43, 00137 Roma, Italy; Cereda, P.M., Institute of Microbiology, University of Pavia, via Brambilla 74, 27100 Pavia, Italy",[No abstract available],,"virus RNA; article; cerebrospinal fluid; Coronavirus; genetics; human; isolation and purification; molecular genetics; multiple sclerosis; neurologic disease; nucleic acid hybridization; open reading frame; polymerase chain reaction; virology; virus infection; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus OC43, Human; Humans; Molecular Sequence Data; Multiple Sclerosis; Nervous System Diseases; Nucleic Acid Hybridization; Open Reading Frames; Polymerase Chain Reaction; RNA, Viral","Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) Journal of Virology, 48, pp. 633-640; 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Eds, Springer-Verlag KG, Heidelberg; Stone, T.W., Connick, J.H., Quinolinic acid and other kynurenines in the central nervous system (1985) Neuroscience, 15, pp. 597-617; Talbot, P.J., Paquette, J.S., Ciurli, C., Antel, J.P., Quellet, F., Myelin basic pro-tein and human coronavirus 229E cross-reactive T cells in multiple sclerosis (1996) Annals of Neurology, 39, pp. 233-240; Tanaka, R., Iwasaki, Y., Koprowski, H., Intracisternal virus-like particles in brain of a multiple sclerosis patient (1976) Journal of the Neurological Sciences, 28, pp. 121-126; Thompson, J.A., Pande, H., Paxton, R.J., Shively, L., Padma, A., Simmer, R.L., Tood, C.W., Shively, J.E., Molecular cloning of a gene belonging to the carcinoembryonic antigen gene family and discussion of a domain model (1987) Proceedings of the National Academy of Sciences, USA, 84, pp. 2965-2969; Weimer, L.P., Herdon, R.M., Narayan, O., Johnson, R.T., Further studies of simian virus- 40-like virus isolated from human brain (1972) Journal of Virology, 10, pp. 147-152; Wigdahl, B., Kunsch, C., Human immunodeficiency virus infection and neurologic dysfunction (1990) Progress in Medical Virology, 37, pp. 1-46; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV resistant SJL/J mice (1990) Journal of Virology, 64, pp. 3817-3823; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proceedings of the National Academy of Sciences, USA, 88, pp. 5533-5536; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Cristallo, A.; Institute of Biochemistry, University of Pavia, V.le Taramelli 3B, 27100 Pavia, Italy",,,11217138,,,"9208420","English","New Microbiol.",Article,"Final",,Scopus,2-s2.0-0031115531
"Rowe C.L., Baker S.C., Nathan M.J., Fleming J.O.","7103076229;7403307881;7102650902;7401457370;","Evolution of mouse hepatitis virus: Detection and characterization of spike deletion variants during persistent infection",1997,"Journal of Virology","71","4",,"2959","2969",,57,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030941096&partnerID=40&md5=eae86b9833b3b45e751bb3fc8675537e","Dept. Microbiol./Immunol. Molec. B., Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Depts. Neurol. and Med. Microbiol., University of Wisconsin, William S. Middleton Vet. Hospital, Madison, WI 53792, United States","Rowe, C.L., Dept. Microbiol./Immunol. Molec. B., Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Baker, S.C., Dept. Microbiol./Immunol. Molec. B., Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Nathan, M.J., Depts. Neurol. and Med. Microbiol., University of Wisconsin, William S. Middleton Vet. Hospital, Madison, WI 53792, United States; Fleming, J.O., Depts. Neurol. and Med. Microbiol., University of Wisconsin, William S. Middleton Vet. Hospital, Madison, WI 53792, United States","High-frequency RNA recombination has been proposed as an important mechanism for generating viral deletion variants of murine coronavirus. Indeed, a number of variants with deletions in the spike glycoprotein have been isolated from persistently infected animals. However, the significance of generating and potentially accumulating deletion variants in the persisting viral RNA population is unclear. To study this issue, we evaluated the evolution of spike variants by examining the population of spike RNA sequences detected in the brains and spinal cords of mice inoculated with coronavirus and sacrificed at 4, 42, or 100 days postinoculation. We focused on the S1 hypervariable region since previous investigators had shown that this region is subject to recombination and deletion. RNA isolated from the brains or spinal cords of infected mice was rescued by reverse transcription- PCR, and the amplified products were cloned and used in differential colony hybridizations to identify individual isolates with deletions. We found that 11 of 20 persistently infected mice harbored spike deletion variants (SDVs), indicating that deletions are common but not required for persistent infection. To determine if a specific type of SDV accumulated during persistence, we sequenced 106 of the deletion isolates. We identified 23 distinct patterns of SDVs, including 5 double-deletion variants. Furthermore, we found that each mouse harbored distinct variants in its central nervous system (CNS), suggesting that SDVs are generated during viral replication in the CNS. Interestingly, mice with the most severe and persisting neurological disease harbored the most prevalent and diverse quasispecies of SDVs. Overall, these findings illustrate the complexity of the population of persisting viral RNAs which may contribute to chronic disease.",,"animal cell; article; chronic disease; coronavirus; dna sequence; gene deletion; hepatitis virus; hybridization; infection risk; molecular cloning; mouse; nonhuman; priority journal; reverse transcription polymerase chain reaction; rna sequence; virus detection; virus replication; Animals; Brain; Cell Line; Coronavirus Infections; Evolution, Molecular; Gene Deletion; Male; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Nervous System Diseases; Spinal Cord; Time Factors; Variation (Genetics); Viral Envelope Proteins; Virus Latency","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific D-b-restricted cytotoxic T cell response (1996) J. Gen. Virol., 77, pp. 315-325; Bertoletti, A., Sette, A., Chisari, F.V., Penna, A., Levrero, M., De Carli, M., Fiaccadori, F., Ferrari, C., Natural variants of cytotoxic epitopes are T-cell receptor are antagonists for antiviral cytotoxic T cells (1994) Nature, 369, pp. 407-410; Cascone, P.J., Haydar, T.F., Simon, A.E., Sequences and structures required for recombination between virus-associated RNAs (1993) Science, 260, pp. 801-805; Castro, R.F., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J. 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Plenum Press, New York, N.Y; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Domingo, E., Escarmis, C., Martinex, M.A., Martinez-Salas, E., Mateau, M.G., Foot-and-mouth disease virus populations are quasispecies (1992) Curr. Top. Microbiol. Immunol., 176, pp. 33-47; Duarte, E.A., Novella, I.S., Weaver, S.C., Domingo, E., Wain-Hobson, S., Clarke, D.K., Moya, A., Holland, J.J., RNA virus quasispecies: Significance for viral disease and epidemiology (1994) Infect. Agents Dis., 3, pp. 201-214; Eigen, M., The origin of genetic information: Viruses as models (1993) Gene, 135, pp. 37-117; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fazakerley, J.K., Buchmeier, M.J., Pathogenesis of virus-induced demyelination (1993) Adv. Virus Res., 42, pp. 249-324; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Fleming, J.O., Trousdale, M.D., Bradbury, J., Stohlman, S.A., Weiner, L.P., Experimental demyelination induced by coronavirus JHM (MHV-4): Molecular identification of a viral determinant of paralytic disease (1987) Microb. Pathog., 3, pp. 9-20; Fleming, J.O., Pen, L.B., Measurement of the concentration of murine IgG monoclonal antibody in hybridoma supernatants and ascites in absolute units by sensitive and reliable enzyme-linked immunosorbent assay (ELISA) (1988) J. Immunol. Methods, 110, pp. 8-11; Fleming, J.O., Wang, F.I., Trousdale, M.D., Hinton, D.R., Stohlman, S.A., Interaction of immune and central nervous systems: Contribution of antiviral Thy-1+ cells to demelination induced by coronavirus JHM (1993) Reg. Immunol., 5, pp. 37-43; Fleming, J.O., Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Baker, S.C., Mutations associated with viral sequences isolated from mice persistently infected with MHV-JHM (1995) Adv. Exp. Med. Biol., 380, pp. 591-595; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. 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Virol., 62, pp. 1810-1813; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Klenerman, P., Rowland-Jones, S., McAdam, S., Edwards, J., Daenke, S., Lalloo, D., Koppe, B., McMichael, A.J., Cytotoxic T-cell activity antagonized by naturally occurring HIV-1 gag variants (1994) Nature, 369, pp. 403-407; Kodama, T., Mori, K., Kawahara, T., Ringler, D.J., Desrosiers, R.C., Analysis of simian immunodeficiency virus sequence variation in tissues of rhesus macaques with simian AIDS (1993) J. Virol., 67, pp. 6522-6534; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbioi. Rev., 56, pp. 61-79; La Monica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, pp. 883-888; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., The organ tropism of mouse hepatitis virus A59 in mice is dependent on dose and route of inoculation (1986) Lab. Anim. Sci., 36, pp. 130-135; Li, Y., Ball, L.A., Nonhomologous RNA recombination during negative-strand synthesis of flock house virus RNA (1993) J. Virol., 67, pp. 3854-3860; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeust, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Makino, S., Taguchi, F., Hayami, M., Fujiwara, K., Characterization of small plaque mutants of mouse hepatitis virus, JHM strain (1983) Microbiol. Immunol., 27, pp. 445-454; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Martell, M., Esteban, J.I., Quer, J., Genesca, J., Weiner, A., Esteban, R., Guardia, J., Gomez, J., Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution (1992) J. Virol., 66, pp. 3225-3229; Morris, V.L., Tieszer, C., Mackinnon, J., Percy, D., Characterization of coronavirus JHM variants isolated from Wistar Furth rats with a viral-induced demyelinating disease (1989) Virology, 169, pp. 127-136; Moskophidis, D., Zinkernagel, R.M., Immunobiology of cytotoxic T-cell escape mutants of lymphocytic choriomeningitis virus (1995) J. Virol., 69, pp. 2187-2193; Nowak, M.A., May, R.M., Phillips, R.E., Rowland-Jones, S., Lalloo, D.G., McAdam, S., Klenerman, P., McMichael, A.J., Antigenic oscillations and shifting immunodominance in HIV-1 infections (1995) Nature, 375, pp. 606-611; Parker, S., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Pewe, L., Wu, G.F., Barnett, E.M., Castro, R.F., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Saiki, R.K., Gelfand, D.H., Stoffel, S., Scharf, S.J., Higuchi, R., Horn, G.T., Mullis, K.B., Erlich, H.A., Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase (1988) Science, 239, pp. 487-491; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: a Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schmidt, I., Skinner, M., Siddell, S., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Siddell, S.G., The coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-9. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activitv of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; Taguchi, F., Kubo, H., Takahasni, H., Suzuki, H., Localization of neurovirulence determinant for rats on the Sl subunit of murine coronavirus JHMV (1995) Virology, 208, pp. 67-74; Wang, F.-I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, H., Koga, M., Watanabe, R., Nagashima, K., Ter Meulen, V., Neurovirulence of murine coronavirus JHM temperature-sensitive mutants in rats (1983) Infect. Immun., 39, pp. 1316-1324; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98","Fleming, J.O.; DNMM, W. S. Middleton Veterans Hospital, University of Winconsin, Madison, WI 53792, United States; email: fleming@neurology.wisc.edu",,,0022538X,,JOVIA,"9060655","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030941096
"Meulenberg J.J.M., Petersen Den Besten A., De Kluyver E., Van Nieuwstadt A., Wensvoort G., Moormann R.J.M.","7003598565;6508098506;6602784924;7004907176;7004683225;7006536560;","Molecular characterization of Lelystad virus",1997,"Veterinary Microbiology","55","1-4",,"197","202",,80,"10.1016/S0378-1135(96)01335-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343924632&doi=10.1016%2fS0378-1135%2896%2901335-1&partnerID=40&md5=88e3a1a9f85380d8c9475eaa307d65ae","Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands","Meulenberg, J.J.M., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands; Petersen Den Besten, A., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands; De Kluyver, E., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands; Van Nieuwstadt, A., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands; Wensvoort, G., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands; Moormann, R.J.M., Inst. for Animal Science and Health, P. O. Box 365, NL 8200 AJ Lelystad, Netherlands","Lelystad virus (LV), the prototype of porcine reproductive respiratory syndrome virus, is a small enveloped virus, containing a positive strand RNA genome of 15 kb. LV is tentatively classified in the family Arteriviridae, which consists of lactate dehydrogenase-elevating virus (LDV), equine arteritis virus (EAV) and simian hemorrhagic fever virus (SHFV). These viruses have a similar genome organization and replication strategy as coronaviruses, but the size of the genome is much smaller (12-15 kb) and they have different morphological and physicochemical properties. The genome of LV contains eight open reading frames (ORFs) that encode the replicase genes (ORFs la and lb), envelope proteins (ORFs 2 to 6) and the nucleocapsid protein (ORF7). Genomic comparison of European and North American isolates has shown that the structural proteins encoded by ORFs 2 to 7 vary widely. The amino acid sequences of ORFs 2 to 7 of North American strains share only 55 to 79% identical amino acids with those of European strains. Using polyvalent porcine anti-LV serum, gene specific anti-peptide sera and monoclonal antibodies, we have identified six structural proteins of LV and their corresponding genes. These are: the 15 kDa unglycosylated nucleocapsid protein (N) encoded by ORF7, an 18 kDa unglycosylated integral membrane protein M encoded by ORF6, a 25 kDa N-glycosylated protein encoded by ORF5, a 31-35 kDa N-glycosylated protein encoded by ORF4, a 45-50 kDa N-glycosylated protein encoded by ORF3 and a 29-30 kDa N-glycosylated protein encoded by ORF2. A nomenclature for these structural proteins is proposed.","Genome organization; Lelystad virus; Molecular characterization; Nomenclature; Sequence comparisons","arterivirus; conference paper; gene sequence; nonhuman; open reading frame; swine disease; virus gene; virus genome; Animals; Arterivirus; Europe; Genome, Viral; North America; Nucleocapsid; Open Reading Frames; Porcine Reproductive and Respiratory Syndrome; Porcine respiratory and reproductive syndrome virus; Swine; Viral Envelope Proteins; Viral Structural Proteins; Arteriviridae; Arterivirus; Equidae; Equine arteritis virus; Lactate dehydrogenase-elevating virus; Lelystad virus; Simiae; Simian hemorrhagic fever virus; Suidae; Sus scrofa","Chen, Z., Kuo, L., Rowland, R.R.R., Even, C., Faaberg, K.S., Plagemann, P.G.W., Sequences of 3′ end of genome and of 5′ end of open reading frame 1a of lactate dehydrogenase-elevating virus and common junction motifs between 5′ leader and bodies of seven sugenomic mRNAs (1993) J. Gen. Virol., 74, pp. 643-660; Collins, J.E., Benfield, D.A., Christianson, W.T., Harris, L., Hennings, J.C., Shaw, D.P., Goyal, S.M., Chladek, D.W., Isolation of swine infertility and respiratory syndrome virus (Isolate ATCC-VR-2332) in North America and experimental reproduction of the disease in gnotobiotic pigs (1992) J. Vet. Diagn. Invest., 4, pp. 117-126; Conzelmann, K.K., Visser, N., Van Woensel, P.A., Tiel, H.J., Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the Arterivirus group (1993) Virology, 193, pp. 329-339; Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togavirus but belongs to the coronavirus superfamily (1991) J. Virol., 65, pp. 2910-2920; De Vries, A.A.F., Chinside, E.D., Horzinek, M.C., Rottier, P.J.M., Structural proteins of equine arteritis virus (1992) J. Virol., 66, pp. 6294-6303; Drew, T.W., Meulenberg, J.J.M., Sands, J.J., Paton, D.J., Production, characterisation and reactivity of monoclonal antibodies to porcine reproductive and respiratory syndrome (PRRSV) (1995) J. Gen. Virol., 76, pp. 1361-1369; Faaberg, K.S., Even, C., Palmer, G.A., Plagemann, P.G.W., Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity (1995) J. Virol., 69, pp. 613-617; Godeny, E.K., Chen, L., Kumar, S.N., Methven, S.L., Koonin, E.V., Brinton, M.A., Complete genomic sequence and phylogenetic analysis of the lactate-dehydrogenase-elevating virus (LDV) (1993) Virology, 194, pp. 585-596; Mardassi, H., Mounir, S., Dea, S., Identification of major differences in the nucleocapsid protein genes of a Quebec strain and European strains of porcine reproductive respiratory syndrome virus (1994) J. Gen. Virol., 75, pp. 681-685; Meng, X.-J., Paul, P.S., Halbur, P.G., Molecular cloning and nucleotide sequencing of the 3′-terminal genomic RNA of the porcine reproductive and respiratory syndrome virus (1994) J. Gen. Virol., 75, pp. 1795-1801; Meulenberg, J.J.M., Hulst, M.M., De Meijer, E.J., Moonen, P.L.J.M., Den Besten, A., De Kluyver, E.P., Wensvoort, G., Moormann, R.J.M., Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS) is related to LDV and EAV (1993) Virology, 192, pp. 62-74; Meulenberg, J.J.M., De Meijer, Moormann, R.J.M., Subgenomic RNAs of Lelystad virus contain a conserved junction sequence (1993) J. Gen. Virol., 74, pp. 1697-1701; Meulenberg, J.J.M., Petersen-Den Besten, A., De Kluyver, E.P., Moormann, R.J.M., Wensvoort, G., Characterization of proteins encoded by ORFs 2 to 7 of Lelystad virus (1995) Virology, 206, pp. 155-163; Murtaugh, M.P., Elam, M., Kakach, L., Comparison of the structural protein coding sequences of Lelystad virus and VR2332 strains of the PRRS virus (1993) 9th Int. Congr. Virol. Abstr., 132. , Bros, Norwich; Nelson, E.A., Christopher-Hennings, J., Drew, T., Wensvoort, G., Collins, J.E., Benfield, D.A., Differentiation of United States and European isolates of porcine reproductive and respiratory syndrome virus by monoclonal antibodies (1993) J. Clin. Microbiol., 31, pp. 3184-3189; Ohlinger, V.F., Weiland, F., Haas, B., Visser, N., Ahl, R., Mettenleiter, T.C., Weiland, E., Straub, O.C., Der seuchenhafte spätabort beim schwein: Ein beitrag zur ätiologie des porcine reproductive and respiratory syndrome (PRRS) (1991) Tieraerzl. Umsch., 46, pp. 703-708; Plagemann, P.G.W., Moennig, V., Lactate dehydrogenase-elevating virus, equine arteritis virus and simian hemorrhagic fever virus: A new group of positive-strand RNA viruses (1991) Adv. Virus Res., 41, pp. 99-192; Nieuwstadt, A.P., Meulenberg, J.J.M., Van Essen-Zandbergen, A., Petersen-Den Besten, A., Bende, R.J., Moormann, R.J.M., Wensvoort, G., Proteins encoded by ORFs 2 and 4 of the genome of Lelystad virus (A teriviridae) are structural proteins of the virion (1996) J. Virol., 70, pp. 4767-4772; Wensvoort, G., De Kluyver, E.P., Luijtze, E.A., Den Besten, A., Harris, L., Collins, J.E., Christianson, W.T., Chladek, D., Antigenic comparison of Lelystad virus and swine infertility and respiratory syndrome (SIRS) virus (1992) J. Vet. Diagn. Invest., 4, pp. 134-138; Wensvoort, G., Terpstra, C., Pol, J.M.A., Ter Laak, E.A., Bloemraad, M., De Kluyver, E.P., Kragten, C., Braamskamp, J., Mystery swine disease in the Netherlands: The isolation of Lelystad virus (1991) Vet. Q., 13, pp. 121-130","Meulenberg, J.J.M.; Institute for Animal Science/Health, P.O. Box 365, NL 8200 AJ Lelystad, Netherlands; email: j.j.m.meulenberg@id.dlo.nl",,,03781135,,VMICD,"9220614","English","VET. MICROBIOL.",Conference Paper,"Final",,Scopus,2-s2.0-0343924632
"Lu Y., Denison M.R.","47661483000;7101971810;","Determinants of mouse hepatitis virus 3C-like proteinase activity",1997,"Virology","230","2",,"335","342",,30,"10.1006/viro.1997.8479","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030988810&doi=10.1006%2fviro.1997.8479&partnerID=40&md5=d340eac2903c14e9cbb6381fa7282388","Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States; Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States","Lu, Y., Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States; Denison, M.R., Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States, Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States","The coronavirus, mouse hepatitis virus strain A59 (MHV), expresses a chymotrypsin-like cysteine proteinase (3CLpro) within the gene 1 polyprotein. The MHV 3CLpro is similar to the picornavirus 3C proteinases in the relative location of confirmed catalytic histidine and cysteine residues and in the predicted use of Q/(S, A, G) dipeptide cleavage sites. However, less is known concerning the participation of aspartic acid or glutamic acid residues in catalysis by the coronavirus 3C-like proteinases or of the precise coding sequence of 3CLpro within the gene 1 polyprotein. In this study, aspartic acid residues in MHV 3CLpro were mutated and the mutant proteinases were tested for activity in an in vitro trans cleavage assay. MHV 3CLpro was not inactivated by substitutions at Asp3386 (D53) or Asp3398 (D65), demonstrating that they were not catalytic residues. MHV 3CLpro was able to cleave at a glutamine-glycine (QG3607-8) dipeptide within the 3CLpro domain upstream from the predicted carboxy-terminal QS3635-6 cleavage site of 3CLpro. The predicted full-length 3CLpro (S3334 to Q3635) had an apparent mass of 27 kDa, identical to the p27 3CLpro in cells, whereas the truncated proteinase (S3334 to C3607) had an apparent mass of 24 kDa. This 28-amino-acid carboxy-terminal truncation of 3CLpro rendered it inactive in a trans cleavage assay. Thus, MHV 3CLpro was able to cleave at a site within the putative full-length proteinase, but the entire predicted 3CLpro domain was required for activity. These studies suggest that the coronavirus 3CL-proteinases may have a substantially different structure and catalytic mechanism than other 3C-like proteinases.",,"proteinase; amino acid sequence; article; controlled study; enzyme activity; enzyme structure; Murine hepatitis coronavirus; nonhuman; priority journal; protein domain; site directed mutagenesis; Coronavirus; Murinae; Murine hepatitis virus; Picornaviridae","Allaire, M., Chernala, M.M., Malcolm, B.A., James, N.G., Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature, 369, pp. 72-76; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Boursnell, M.F.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Breedenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerse gene of the coronavirus MHV-A59; A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Gorbalenya, A., Koonin, E., Comparative analysis of amino-acid sequences of key enzymes of replication and expression of positive-strand RNA viruses: Validity of approach and functional and evolutionary implications (1993) Sov. Sci. Rev. D Physiochem. Biol., 11, pp. 1-81; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Hammerle, T., Molla, A., Wimmer, E., Mutational analysis of the proposed FG look of poliovirus proteinase 3C identifies amino acids that are necessary for 3CD cleavage and might be determinants of a function distinct from proteolytic activity (1992) J. Virol., 66, pp. 6028-6034; Herold, J., Raabe, T., Schelle, P.B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Raabe, T., Siddell, S.G., Characterization of the human coronavirus 229E (HCV 229E) gene 1 (1993) Adv. Exp. Med. Biol., 342, pp. 75-79; Lawson, M.R., Semler, B.L., Alternate poliovirus nonstructural protein processing cascades generated by primary sites of 3C proteinase cleavage (1992) Virology, 191, pp. 309-320; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadhzyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Lu, X., Lu, Y., Denison, M.R., Intracellular andin vitro (1996) Virology, 222, pp. 375-382; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Martinez-Salas, E., Domingo, E., Effect of expression of the aphthovirus protease 3C on viral infection and gene expression (1995) Virology, 212, pp. 111-120; Matthews, D.A., Smith, W.W., Ferre, R.A., Condon, B., Budahazi, G., Sisson, W., Villafranca, J.E., Worland, S., Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein (1994) Cell, 77, pp. 761-771; Tibbles, K.W., Brierley, I., Cavanaugh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Denison, M.R.; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States",,"Academic Press Inc.",00426822,,VIRLA,"9143289","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030988810
"Piñón J.D., Mayreddy R.R., Turner J.D., Khan F.S., Bonilla P.J., Weiss S.R.","35870444000;6508359456;7404250580;7402008289;7004225518;57203567044;","Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes",1997,"Virology","230","2",,"309","322",,24,"10.1006/viro.1997.8503","https://www.scopus.com/inward/record.uri?eid=2-s2.0-18244432238&doi=10.1006%2fviro.1997.8503&partnerID=40&md5=9626435c50e5de9cb942cda41c981c77","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","Piñón, J.D., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Mayreddy, R.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Turner, J.D., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Khan, F.S., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Bonilla, P.J., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","The replicase gene of the coronavirus MHV-A59 encodes a serine-like proteinase similar to the 3C proteinases of picornaviruses. This proteinase domain is flanked on both sides by hydrophobic, potentially membrane-spanning, regions. Cell-free expression of a plasmid encoding only the 3C-like proteinase (3CLpro) resulted in the synthesis of a 29-kDa protein that was specifically recognized by an antibody directed against the carboxy-terminal region of the proteinase. A protein of identical mobility was detected in MHV-A59-infected cell lysates. In vitro expression of a plasmid encoding the 3CLpro and portions of the two flanking hydrophobic regions resulted in inefficient processing of the 29-kDa protein. However, the efficiency of this processing event was enhanced by the addition of canine pancreatic microsomes to the translation reaction, or removal of one of the flanking hydrophobic domains. Proteolysis was inhibited in the presence of N-ethylmaleimide (NEM) or by mutagenesis of the catalytic cysteine residue of the proteinase, indicating that the 3CLpro is responsible for its autoproteolytic cleavage from the flanking domains. Microsomal membranes were unable to enhance the trans processing of a precursor containing the inactive proteinase domain and both hydrophobic regions by a recombinant 3CLpro expressed from Escherichia coli. Membrane association assays demonstrated that the 29-kDa 3CLpro was present in the soluble fraction of the reticulocyte lysates, while polypeptides containing the hydrophobic domains associated with the membrane pellets. With the help of a viral epitope tag, we identified a 22-kDa membrane-associated polypeptide as the proteolytic product containing the amino-terminal hydrophobic domain.",,"epitope; proteinase; replicase; unclassified drug; animal cell; article; chemical structure; controlled study; Coronavirus; hydrophobicity; microsome membrane; nonhuman; priority journal; protein domain; protein processing; Animalia; Coronavirus; Escherichia coli; Murine hepatitis virus","Baker, S.C., La Monica, N., Shieh, C.K., Lai, M.M., Murine coronavirus gene 1 polyprotein contains an autoproteolytic activity (1990) Adv. Exp. Med. Biol., 276, pp. 283-289; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Bi, W., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., Intracellular localization of polypeptides encoded in mouse hepatitis virus open reading frame 1a (1995) Adv. Exp. Med. Biol., 380, pp. 251-258; Bienz, K., Egger, D., Pfister, T., Characteristics of the poliovirus replication complex (1994) Arch. Virol. - Supplementum, 9, pp. 147-157; Bienz, K., Egger, D., Pfister, T., Troxler, M., Structural and functional characterization of the poliovirus replication complex (1992) J. Virol., 66, pp. 2740-2747; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Piñón, J.D., Weiss, S.R., Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus MHV-A59 (1997) J. Virol., 71, pp. 900-909; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Chambers, T.J., Hahn, C.S., Galler, R., Rice, C.M., Flavivirus genome organization, expression, and replication. [Review] (1990) Annu. Rev. Microbiol., 44, pp. 649-688; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De, V.A.A., Horzinek, M.C., Spaan, W.J., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol., 65, pp. 2910-2920; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59 (1991) J. Virol., 65, pp. 3076-3082; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes. [Review] (1993) Microbiol. Rev., 57, pp. 781-822; Echeverri, A.C., Dasgupta, A., Amino terminal regions of poliovirus 2C protein mediate membrane binding (1995) Virology, 208, pp. 540-553; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kb) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes (1988) J. Cell. Biol., 107, pp. 2075-2086; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Grotzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d (1995) Virology, 208, pp. 1-8; Kolodziej, P.A., Young, R.A., Epitope tagging and protein surveillance (1991) Methods Enzymol., 194, pp. 508-519; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La, M.N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 222, pp. 375-382; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Mostov, K.E., Defoor, P., Fleischer, S., Blobel, G., Co-translational membrane integration of calcium pump protein without signal sequence cleavage (1981) Nature, 292, pp. 87-88; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Snijder, E.J., Wassenaar, A.L., Spaan, W.J., Proteolytic processing of the replicase ORF1a protein of equine arteritis virus (1994) J. Virol., 68, pp. 5755-5764; Snijder, E.J., Wassenaar, A.L., Van, D.L.C., Spaan, W.J., Gorbalenya, A.E., The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases (1996) J. Biol. Chem., 271, pp. 4864-4871; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Van Dinten, L.C., Wassenaar, A.L., Gorbalenya, A.E., Spaan, W.J., Snijder, E.J., Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) J. Virol., 70, pp. 6625-6633; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Weiss, S.R.; Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"9143287","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-18244432238
"Foley J.E., Poland A., Carlson J., Pedersen N.C.","7402872921;7006803895;57198852456;7202299909;","Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus",1997,"Journal of the American Veterinary Medical Association","210","9",,"1313","1318",,73,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031133784&partnerID=40&md5=4ee80f5b17ea83e10dc8601bd6ea8daa","Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Foley, J.E., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Poland, A., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Carlson, J., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Objective - To determine what risk factors, other than genetic predisposition, contribute to the incidence of feline infectious peritonitis (FIP) in private breeding catteries and animal shelters. Design - Cats from 7 catteries and a shelter were observed monthly for 1 year. At each visit, cats were examined, fecal samples were collected for determination of feline coronavirus shedding, and blood samples were collected for determination of coronavirus antibody titers. Diagnostic tests were performed on all cats that died of FIP. Animals - 275 purebred or random-bred cats that were kept by private breeder-owners in homes. Results - 24 cats died of FIP during the study. Development of FIP was not associated with cattery, mean cat number, mean age, sex, cattery median coronavirus antibody titer, husbandry and quarantine practices, caging and breeding practices, or prevalence of concurrent diseases. However, risk factors for FIP included individual cat age, individual cat coronavirus titer, overall frequency of fecal coronavirus shedding, and the proportion of cats in the cattery that were chronic coronavirus shedders. Deaths from FIP were more frequent in fall and winter, and on the basis of analysis of cattery records, the number of deaths varied yearly. Epidemics (> 10% mortality rate) were reported at least once in 5 years in 4 catteries. Clinical Implications - Elimination of FIP from a cattery is only possible by total elimination of endemic feline enteric coronavirus (FECV) infection. The most important procedure to reduce FECV from catteries is elimination of chronic FECV shedders.",,"virus antibody; age; animal; animal disease; animal housing; animal husbandry; article; blood; case control study; cat; cat disease; Coronavirus; feces; female; immunology; incidence; infection control; isolation and purification; male; population density; prevalence; risk factor; season; vaccination; virology; virus infection; virus shedding; Age Factors; Animal Husbandry; Animals; Antibodies, Viral; Case-Control Studies; Cats; Coronavirus; Coronavirus Infections; Feces; Feline Infectious Peritonitis; Female; Housing, Animal; Incidence; Male; Population Density; Prevalence; Quarantine; Risk Factors; Seasons; Vaccination; Virus Shedding","Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-22; Vennema, H., Poland, A., Hawkins, K.F., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-46; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., The sites of early viral replication in feline infectious peritonitis (1988) Vet Microbiol, 18, pp. 259-271; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus FIPV-UCD2, FIPV-UCD3,andFIPV-UCD4 (1985) Compend Contin Educ Pract Vet, 7, pp. 1001-1011; Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Pract, 24, pp. 14-22; Foley, J.E., Poland, A., Carlson, J., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J Am Vet Med Assoc, 210, pp. 1307-1312; Lutz, H., Pedersen, N.C., Durbin, R., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) J Immunol Methods, 56, pp. 209-220; Yamamoto, J.K., Hansen, H., Ho, E.W., Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission (1989) J Am Vet Med Assoc, 194, pp. 213-220; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am J Vet Res, 37, pp. 1449-1453; Chomel, B., Abbott, R.C., Casten, R.W., Bartonella henselae prevalence in domestic cats in California. Risk factors and association between bacteremia and antibody titers (1995) J CHn Microbiol, 33, pp. 2445-2450; Zar, J.H., (1984) Biostatistical Analysis, , Englewood Cliffs, NJ: Prentice-Hall Inc; Reubel, G.H., Hoffman, D.E., Pedersen, N.C., Acute and chronic faucitis of domestic cats. A feline calicivirus-induced disease (1992) Vet Clin North Am Small Anim Pract, 22, pp. 1347-1360; Poland, A., Vennema, H., Foley, J.E., Two independent mutant feline infectious peritonitis virus (FIPV) strains isolated from immunocompromised cats infected with feline enteric coronavirus (FECV) (1996) J Clin Microbiol, 32, pp. 3180-3184; Potkay, S., Bacher, J.D., Pitts, T.W., Feline infectious peritonitis in a closed breeding colony (1974) Lab Anim Sci, 24, pp. 279-289; Cotter, S.M., Gilmore, C.E., Rollins, C., Multiple cases of feline leukemia and feline infectious peritonitis in a household (1973) J Am Vet Med Assoc, 162, pp. 1054-1058; McKiernan, A.J., Evermann, J.F., Hargis, A., Isolation of feline coronaviruses from two cats with diverse disease manifestations (1981) Feline Pract, 11, pp. 16-21; Foley, J.E., Hirsch, D.C., Pedersen, N.C., An outbreak of Clostridium perfringens enteritis in a cattery of Bengal cats and experimental transmission to specific-pathogen-free cats (1996) Feline Pract, 24, pp. 31-35; Hickman, A., Morris, J.G., Rogers, Q.R., Elimination of feline coronavirus from a large experimental specific-pathogen-free cat breeding colony by serologic testing and isolation (1995) Feline Pract, 23, pp. 96-102; Pedersen, N.C., Black, J.W., Boyle, J.F., Pathogenic differences between various feline coronavirus isolates (1983) Adv Exp Med Biol, 173, pp. 365-380; Pedersen, N.C., (1988) Feline Infectious Diseases, pp. 45-60. , Goleta, Calif: American Veterinary Publications Inc; Kass, P.H., Dent, T.H., The epidemiology of feline infectious peritonitis in catteries (1995) Feline Pract, 23, pp. 27-33; Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet Rec, 130, pp. 133-137; Fehr, D., Holznagel, E., Bolla, S., Evaluation of the safety and efficacy of a modified live FIPV vaccine under field conditions (1995) Feline Pract, 23, pp. 83-88; Hethcote, H.W., Qualitative analyses of communicable disease models (1976) Math Biosci, 28, pp. 335-356","Foley, J.E.; Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States",,,00031488,,JAVMA,"9143536","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0031133784
"Ziebuhr J., Heusipp G., Siddell S.G.","7003783935;6603559110;7005260816;","Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase",1997,"Journal of Virology","71","5",,"3992","3997",,68,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030970783&partnerID=40&md5=520a80288aecbd9bcb562e3a3227964e","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Ziebuhr, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Heusipp, G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Coronavirus gene expression involves proteolytic processing of the gene 1-encoded polyprotein(s), and a key enzyme in this process is the viral 3C- like proteinase. In this report, we describe the biosynthesis of the human coronavirus 229E 3C-like proteinase in Escherichia coli and the enzymatic properties, inhibitor profile, and substrate specificity of the purified protein. Furthermore, we have introduced single amino acid substitutions and carboxyl-terminal deletions into the recombinant protein and determined the ability of these mutant 3C-like proteinases to catalyze the cleavage of a peptide substrate. Using this approach, we have identified the residues Cys- 3109 and His-3006 as being indispensable for catalytic activity. Our results also support the involvement of His-3127 in substrate recognition, and they confirm the requirement of the carboxyl-terminal extension found in coronavirus 3C-like proteinases for enzymatic activity. These data provide experimental evidence for the relationship of coronavirus 3C-like proteinases to other viral chymotrypsin-like enzymes, but they also show that the coronavirus proteinase has additional, unique properties.",,"proteinase; synthetic peptide; virus enzyme; article; coronavirus; enzyme activity; enzyme purification; enzyme structure; enzyme synthesis; escherichia coli; nonhuman; priority journal; structure activity relation; Amino Acid Sequence; Chymotrypsin; Coronavirus; Coronavirus 229E, Human; Endopeptidases; Humans; Molecular Sequence Data; Recombinant Proteins; Serine Endopeptidases; Structure-Activity Relationship; Substrate Specificity","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N.G., Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature, 369, pp. 72-76; Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1940) Virology, 177, pp. 646-656; Bazan, J.F., Fletterick, R.J., Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 7872-7876; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. 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A distinct protein superfamily with a common structural fold (1989) FEBS Lett., 243, pp. 103-114; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Süss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Siddell, S.G., An 'elaborated' pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275, pp. 68-89; Johnston, S., Holgate, S., Epidemiology of viral respiratory tract infections (1996) Viral and Other Infections of the Human Respiratory Tract, pp. 1-38. , S. 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Virol., 70, pp. 1923-1930; Yao, Z., Jones, D.H., Grose, C., Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction (1992) PCR Methods Appl., 1, pp. 205-207; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J. Med. Virol., 44, pp. 152-161; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Unpublished data","Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,,0022538X,,JOVIA,"9094676","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030970783
"Foley J.E., Poland A., Carlson J., Pedersen N.C.","7402872921;7006803895;57198852456;7202299909;","Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments",1997,"Journal of the American Veterinary Medical Association","210","9",,"1307","1312",,78,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031136088&partnerID=40&md5=abc8f971910e724a2cb5c6739a78e18f","Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Foley, J.E., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Poland, A., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Carlson, J., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Objective - To determine, by use of a reverse transcriptase-polymerase chain reaction (RT-PCR) test, patterns of fecal shedding of feline coronavirus among cats. Design - Prospective observational study. Animals - 275 purebred cats from 6 private catteries and 40 specific-pathogen-free (SPF) laboratory-reared cats. Procedure - 40 SPF cats were experimentally inoculated with crude fecal extract containing feline enteric coronavirus (FECV). Fecal and plasma samples were collected every 4 days and evaluated by use of RT-PCR and indirect immunofluorescence assays, respectively, to correlate RT-PCR results with fecal infectivity and to determine patterns of FECV shedding and anti-FECV IgG production in acutely infected cats. The 275 cats in private catteries were monitored for 1 year. Fecal and blood samples were collected every 1 to 3 months and assayed by use of RT-PCR and serologic tests to determine patterns of coronavirus shedding and cofactors for high frequency shedding. Results - Results of the RT-PCR test in SPF cats were directly correlated with fecal extract infectivity. Overall, 370 of 894 (41%) fecal samples collected from cattery and shelter cats contained infectious levels of coronavirus. Of 121 cats from which multiple samples were collected, 11 never shed virus and 35, 65, and 10, respectively, shed virus with low, moderate, and high frequency. High frequency shedding was associated with age and cattery of origin, but not with sex or concurrent disease. Stress associated with parturition and lactation did not induce shedding in queens. Kittens did not shed coronavirus before they were 10 weeks old, even when nursed by shedding mothers. Clinical Implications - A large proportion of cats in multiple-cat environments shed coronavirus at any given time, but most undergo cycles of infection and shedding, recovery, and reinfection. Infection is acquired from chronically shedding cats and from infectious cats undergoing transient primary infection. Chronically shedding cats cannot be identified on the basis of antibody titer or signalment, but must be identified on the basis of the results of serial fecal RT-PCR tests.",,"virus antibody; virus DNA; virus RNA; animal; animal disease; article; blood; cat; cat disease; chronic disease; Coronavirus; disease transmission; feces; genetics; germfree animal; immunology; isolation and purification; physiology; polymerase chain reaction; population density; prospective study; recurrent disease; risk factor; virology; virus infection; virus shedding; Animals; Antibodies, Viral; Cat Diseases; Cats; Chronic Disease; Coronavirus; Coronavirus Infections; Disease Transmission, Vertical; DNA, Viral; Feces; Polymerase Chain Reaction; Population Density; Prospective Studies; Recurrence; Risk Factors; RNA, Viral; Specific Pathogen-Free Organisms; Virus Shedding","Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-22; Loeffler, D.G., Ott, R.L., Evermann, J.F., The incidence of naturally occurring antibodies against feline infectious peritonitis in selected cat populations (1978) Feline Pract, 8, pp. 43-47; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am J Vet Res, 37, pp. 1449-1453; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Coronavirus serology in healthy pedigree cats (1992) Vet Rec, 131, pp. 35-36; Pedersen, N.C., Boyle, J.F., Floyd, K., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am J Vet Res, 42, pp. 368-377; Pedersen, N.C., (1988) Feline Infectious Diseases, pp. 45-60. , Goleta, Calif: American Veterinary Publications Inc; Hickman, A., Morris, J.G., Rogers, Q.R., Elimination of feline coronavirus from a large experimental specific-pathogen-free cat breeding colony by serologic testing and isolation (1995) Feline Pract, 23, pp. 96-102; Poland, A., Vennema, H., Foley, J.E., Feline infectious peritonitis is caused by simple mutants of feline enteric coronavirus (FECV) that arise frequently during the course of primary FECV infection (1996) J Clin Microbiol, 34, pp. 3180-3184; Vennema, H., Poland, A., Hawkins, K.F., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-46; Pedersen, N.C., Black, J.W., Boyle, J.F., Pathogenic differences between various feline coronavirus isolates (1983) Adv Exp Med Biol, 173, pp. 365-380; Pedersen, N.C., Evermann, J.F., McKiernan, A.J., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am J Vet Res, 45, pp. 2580-2585; Herrewegh, A.P.M., DeGroot, R.J., Cepica, A., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Lutz, H., Pedersen, N.C., Durbin, R., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) J Immunol Methods, 56, pp. 209-220; Yamamoto, J.K., Hansen, H., Ho, E.W., Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission (1989) J Am Vet Med Assoc, 194, pp. 213-220; Cheung, R.C., Matsui, S.M., Greenberg, H.B., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) J Clin Microbiol, 32, pp. 2593-2597; Pedersen, N.C., The history and interpretation of feline coronavirus serology (1995) Feline Pract, 23, pp. 46-52; Zar, J.H., (1984) Biostatistical Analysis, , Englewood Cliffs, NJ: Prentice-Hall Inc; Bliss, C.I., (1967) Statistics in Biology, 1. , New York: McGraw-Hill Book Co; Foley, J.E., Hirsch, D.C., Pedersen, N.C., An outbreak of Clostridium perfringens enteritis in a cattery of Bengal cats and inadvertent experimental transmission to specific pathogen free cats (1996) Feline Pract, 24, pp. 31-35; Hickman, M.A., Reubel, G.H., Pedersen, N.C., An epizootic of feline herpesvirus, type 1 in a large specific-pathogen free cat colony and attempts to eradicate the infection by identification of carriers (1994) Lab Anim, 28, pp. 320-329; Weir, E.C., Bhatt, P.N., Barthold, S.W., Elimination of mouse hepatitis virus from a breeding colony by temporary cessation of breeding (1987) Lab Anim Sci, 37, pp. 455-458; Addie, D.D., Jarrett, O., Control of feline coronavirus infections in breeding catteries by serotesting, isolation, and early weaning (1995) Feline Pract, 23, pp. 92-95; Kraft, V., Meyer, B., Seromonitoring in small laboratory animal colonies. A five year survey: 1984-1988 (1990) Z Versuchstierkd, 33, pp. 29-35; Hornberger, F.R., Thomann, P.E., Transmission of murine viruses and mycoplasma in laboratory mouse colonies with respect to housing conditions (1993) Lab Anim, 28, pp. 113-120; Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infection in kittens (1992) Vet Rec, 130, pp. 133-137; Keep, J.M., A survey of Microsporum canis infection in cats in Sydney (1963) Aust Vet J, 39, pp. 330-332; Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Pract, 24, pp. 14-22; Kermack, W.O., McKendrick, A.G., Contributions to the mathematical theory of epidemics (1927) R Stat Soc J, 115, pp. 700-721; Hethcote, H.W., Yorke, J.A., Nold, A., Gonorrhea modeling: A comparison of control methods (1992) Math Biosci, 58, pp. 93-109; Jacquez, J., Simon, C., Koopman, J., Core groups and the R0s for subgroups in heterogeneous SIS and SI models (1995) Epidemiologic Models: Their Structure and Relation to Data, pp. 279-301. , Mollison D, ed. Cambridge, England: Cambridge University Press","Foley, J.E.; Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, CA 95616, United States",,,00031488,,JAVMA,"9143535","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0031136088
"Kim K.H., Narayanan K., Makino S.","7409323179;7101933409;7403067550;","Assembled coronavirus from complementation of two defective interfering RNAs",1997,"Journal of Virology","71","5",,"3922","3931",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842291501&partnerID=40&md5=30425b54230056f9e4719344ec73c8be","Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States; Division of Biology, California Institute of Technology, Pasadena, CA 91125, United States","Kim, K.H., Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States, Division of Biology, California Institute of Technology, Pasadena, CA 91125, United States; Narayanan, K., Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States","In the presence of an RNA- temperature-sensitive (ts) mutant helper virus, two coronavirus mouse hepatitis virus (MHV) defective interfering (DI) RNAs complemented each other, resulting in the assembly of MHV particles; we used this ability to complement as a means to study coronavirus assembly. One of the two DI RNAs was DIssA, a naturally occurring self-replicating DI RNA encoding N protein and the gene 1 proteins that encode RNA polymerase function; DIssA supports the replication and transcription of other non- self-replicating DI RNAs. The other DI was a genetically engineered DI RNA that encoded sM and M proteins. Coinfection of these two DIs at the nonpermissive temperature for the ts helper virus resulted in replication and transcription of both DI RNAs but not in synthesis of the helper virus RNAs. MHV particles containing DI RNAs, N protein, and M protein, all of which were exclusively derived from the two DI RNAs, were released from the coinfected cells; the amount of sM protein was below the limits of detection. 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Virol., 65, pp. 3219-3226; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Xiong, C., Levis, R., Shen, P., Schlesinger, S., Rice, C.M., Huang, H.V., Sindbis virus: An efficient, broad host range vector for gene expression in animal cells (1989) Science, 243, pp. 1188-1191; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Yu, X., Weizhen, B., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion protein (1994) Virology, 202, pp. 1018-1023","Makino, S.; Department of Microbiology, University of Texas, Austin, TX 78712, United States; email: makino@mail.utexas.edu",,,0022538X,,JOVIA,"9094669","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-1842291501
"Wolf A.M.","7403174132;","Feline infectious peritonitis, part 2",1997,"Feline Practice","25","3",,"24","28",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-21744454479&partnerID=40&md5=8951fde6ec5945324dae0babd78d5e8f","Department of Small Animal Medicine and Surgery, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843-4474, United States","Wolf, A.M., Department of Small Animal Medicine and Surgery, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843-4474, United States","Feline infectious peritonitis (FIP) is a biologically complex and usually fatal disease of cats. FIP is primarily a problem in high population density multiple cat environments and catteries. The outcome of infection and symptoms of disease exhibited by each individual cat are determined by its immune status. Definitive antemortem diagnosis of FIP may be difficult because clinical signs are often vague and the results of routine laboratory tests are often nonspecific. The serologic and PCR tests currently available cannot differentiate cats infected with FIP coronavirus from those infected with nonpathogenic coronaviruses. FIP infection can be effectively prevented in cattery populations with specific husbandry and management procedures. A commercial FIP vaccine is available but its use is controversial.",,,"Barlough, J.E., Stoddart, C.A., Cats and Coronaviruses (1988) JAVMA, 193 (7), pp. 796-800; Mochizuki, M., Furukawa, H., An Enzyme-Linked Immunosorbent Assay Using Canine Coronavirus-Infected CRFK Cells as Antigen for Detection of Anti-Coronavirus Antibody in Cat (1989) Comp Immun Microbiol Infect Dis, 12 (4), pp. 139-146; Stoddart, C.A., Scott, F.W., Intrinsic Resistance of Feline Peritoneal Macrophages to Coronavirus Infection Correlates with in vivo Virulence (1989) J Virol, 63, pp. 436-440; Pedersen, N.C., Virologic and Immunologic Aspects of Feline Infectious Peritonitis Virus Infection (1987) Adv Exp Med Biol, 218, pp. 529-550; Pedersen, N.C., Animal Virus Infections That Defy Vaccination. Equine Infectious Anemia, Caprine Arthritis-Encephalitis, Maedi-visna, and Feline Infectious Peritonitis (1989) Adv Vet Sci Comp Med, 33, pp. 413-428; Pedersen, N.C., Personal Communication; Vennema, H., DeGroot, R.J., Harbour, D.A., Early Death after Feline Infectious Peritonitis Virus Challenge due to Recombinant Vaccinia Virus Immunization (1990) J Virol, 64 (3), pp. 1407-1409; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., The Sites of Early Viral Replication in Feline Infectious Peritonitis (1988) Vet Microbiol, 18, pp. 259-271; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Virus Shedding and Immune Responses in Cats Inoculated with Cell Culture-Adapted Feline Infectious Peritonitis Virus (1988) Vet Microbiol, 16, pp. 145-158; Scott, F.W., The Immune Response to FIP in Cats (1989) Feline Health Topics, 3 (4), pp. 1-3; August, J.R., Proceedings. Coronavirus Infections in Cats: An Internist's Perspective (1989) Proceedings: Feline Infectious Peritonitis: Current Concepts, pp. 4-13; Pedersen, N.C., Black, J.W., Attempted Immunization of Cats Against Feline Infectious Peritonitis, Using a Virulent Live Virus or Sublethal Amounts of Virulent Virus (1983) Am J Vet Res, 44 (2), pp. 229-234; Ingersoll, J.D., Wylie, D.E., Identification of Viral Antigens That Induce Antibody Responses on Exposure to Coronaviruses (1988) Am J Vet Res, 49 (9), pp. 1467-1471; Reinacher, M., Diseases Associated with Spontaneous Feline Leukemia Virus (FeLV) Infection in Cats (1989) Vet Immunol Immunopathol, 21, pp. 85-95; Vacirca, G., Mantelli, F., Ferro, E., Pericardial Effusion with Feline Infectious Peritonitis (1989) Comp Anim Pract, 19 (8-9), pp. 25-27; Tamke, P.G., Petersen, M.G., Dietze, A.M., Acquired Hydrocephalus and Hydromyelia in a Cat with Feline Infectious Peritonitis: A Case Report and Brief Review (1988) Can Vet J, 29, pp. 997-1000; Luttgen, P.J., Neurologic Aspects of Feline Infectious Disease (1989) Vet Med Reports, 1 (2), pp. 204-208; Sparkes, A.H., Gruffyd-Jones, T.J., Harbour, D.A., An Appraisal of the Value of Laboratory Tests in the Diagnosis of Feline Infectious Peritonitis (1994) JAAHA, 30, pp. 345-350; Stoddart, M.E., Whicher, J.T., Harbour, D.A., Cats Inoculated with Feline Infectious Peritonitis Virus Exhibit a Biphasic Acute Phase Plasma Protein Response (1988) Vet Rec, 123, pp. 621-624; Shelly, S.M., Scarlett-Kranz, J., Blue, J.T., Protein Electrophoresis on Effusions from Cats as a Diagnostic Test for Feline Infectious Peritonitis (1988) JAAHA, 24, pp. 495-500; Kline, K.L., Joseph, R.J., Averill Jr., D.A., Feline Infectious Peritonitis with Neurologic Involvement: Clinical and Pathologic Findings in 24 Cats (1994) JAAHA, 30, pp. 111-118; Ingersoll, J.D., Wylie, D.E., Comparison of Serologic Assays for Measurement of Antibody Response to Coronavirus in Cats (1988) Am J Vet Res, 49 (9), pp. 1472-1479; Sparkes, A.J., Gruffydd-Jones, T.J., Howard, P.E., Coronavirus Serology in Healthy Pedigree Cats (1992) Vet Rec, 131, pp. 35-36; Hök, K., Demonstration of Feline Corona Virus (FCV) Antigen in Organs of Cats Suspected of Feline Infectious Peritonitis (FIP) Disease (1990) APMIS, 98, pp. 659-664; Hök, K., Demonstration of Feline Infectious Peritonitis Virus in Conjunctival Epithelial Cells from Cats (1989) APMIS, 97, pp. 820-824; Weiss, R.C., A Virologist's Approach to Treatment of Feline Infectious Peritonitis (1989) Proceedings: Feline Infectious Peritonitis: Current Concepts, pp. 14-19; Weiss, R.C., Tiovio-Kinnucan, M., Inhibition of Feline Infectious Peritonitis Replication by Recombinant Human Leukocyte (α) Interferon and Feline Fibroblastic (β) Interferon (1988) Am J Vet Res, 49 (8), pp. 1329-1335; Weiss, R.C., Oostrom-Ram, T., Inhibitory Effects of Fibavirin Alone or Combined with Human Alpha Interferon on Feline Infectious Peritonitis Virus Replication in vitro (1989) Vet Microbiol, 20, pp. 255-265; Barlough, J.E., Scott, F.W., Effectiveness of Three Antiviral Agents Against FIP Virus in vitro (1990) Vet Rec, 126, pp. 556-558; Weiss, R.C., Cox, N.R., Oostrom-Ram, T., Effect of Interferon or Propionibacterium acnes on the Course of Experimentally Induced Feline Infectious Peritonitis in Specific-Pathogen Free and Random Source Cats (1990) Am J Vet Res, 51 (5), pp. 726-733; Addie, D.D., Jarrett, O., A Study of Naturally Occurring Feline Coronavirus Infections in Kittens (1992) Vet Rec, 130, p. 133; Gerber, J.D., New Approaches to Feline Infectious Peritonitis Prevention (1989) Proceedings: Feline Infectious Peritonitis: Current Concepts, pp. 20-23; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Characterization of a Temperature Sensitive Feline Infectious Peritonitis Coronavirus (1989) Arch Virol, 109, pp. 185-196; Scott, F.W., Corapi, W.V., Olsen, C.W., Evaluation of the Safety and Efficacy of Primucell-FIP Vaccine (1992) Feline Health Topics, 7 (3), pp. 6-8; Postorino-Reeves, N., Coyne, M.J., Herman, J.G., Evaluation of the Field Efficacy of a Temperature-Sensitive Feline Infectious Peritonitis Vaccine (1994) ACVIM Proc 12th Annual Forum, p. 1004; Hoskins, J.D., Taylor, H.W., Lomax, T.L., Challenge Trial of a Temperature-Sensitive Feline Infectious Peritonitis Vaccine (1994) ACVIM Proc 12th Annual Forum, p. 1005","Wolf, A.M.; Department of Small Animal Medicine and Surgery, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843-4474, United States",,,10576614,,,,"English",,Article,"Final",,Scopus,2-s2.0-21744454479
"Stohlman S.A., Lin M., Parra B., Bergmann C.C., Hinton D.R.","35502534500;7404816683;6701803000;35449739000;7202351155;","Immune regulation of coronavirus-induced demyelinating encephalomyelitis",1997,"Journal of NeuroVirology","3","SUPPL. 1",,"S56","S57",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030920658&partnerID=40&md5=8a99240739b5f9fb44abda9293bf81cb","Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Department of Molecular Microbiology and Immunology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Department of Pathology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States","Stohlman, S.A., Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States, Department of Molecular Microbiology and Immunology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Lin, M., Department of Pathology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Parra, B., Department of Molecular Microbiology and Immunology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Bergmann, C.C., Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States, Department of Molecular Microbiology and Immunology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Hinton, D.R., Department of Neurology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States, Department of Pathology, University of Southern California, School of Medicine, Los Angeles, CA 90033, United States",[No abstract available],"Coronavirus; Demyelination; Encephalitis; Interferon gamma; Perforin","interleukin 10; interleukin 4; tumor necrosis factor alpha; animal cell; animal experiment; animal model; central nervous system infection; conference paper; controlled study; coronavirus; demyelinating disease; demyelination; immunoregulation; mouse; nonhuman; priority journal; virus encephalitis; Adoptive Transfer; Animals; CD4-Positive T-Lymphocytes; Coronavirus Infections; Cytokines; Demyelinating Diseases; Encephalomyelitis; Mice; Murine hepatitis virus; Transcription, Genetic; Tumor Necrosis Factor-alpha","Lin, M.T., Stohlman, S.A., Hinton, D.R., Mouse hepatitis virus is cleared from the central nervous systems of mice lacking perforin-mediated cytolysis (1997) J Virol, 71, pp. 383-391; Parra, B., Hinton, D., Lin, M., Cua, D., Stohlman, S., (1997) Kinetics of Cytokine MRNA in the Central Nervous System Following Lethal and Nonlethal Coronavirus Induced Encephalomyelitis, , Submitted; Stohlman, S.A., Hinton, D.R., Cua, D., Dimacali, E., Sensintaffar, J., Hofman, F.M., Tahara, S.M., Yao, Q., Tumor necrosis factor expression during mouse hepatitis virus-induced demyelinating encephalomyelitis (1995) J Virol, 69, pp. 684-694","Stohlman, S.A.; Department of Neurology, School of Medicine, University of Southern California, Los Angeles, CA 90033, United States",,,13550284,,JNVIF,"9179796","English","J. NEUROVIROL.",Conference Paper,"Final",,Scopus,2-s2.0-0030920658
"Steiner L., Busato A., Burnens A., Gaillard C.","9269993300;7006678871;7006802781;8236359900;","Frequency and etiology of calf losses and calf diseases before weaning in cow-calf farms. II. Microbiological and parasitological diagnoses in diarrhoic calves [Häufigkeiten und ursachen von kälberverlusten und kälberkrankheiten in mutterkuhbetrieben. II. Mikrobiologische und parasitologische diagnosen bei kälbern mit durchfall]",1997,"Deutsche Tierarztliche Wochenschrift","104","5",,"169","173",,14,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031137654&partnerID=40&md5=05d7c7be6ad13a3236abf57f91a5762b","Institut für Tierzucht, Universität Bern, Switzerland; Institut für Tierzucht, Bremgartenstr. 109a, CH-3012 Bern, Switzerland","Steiner, L., Institut für Tierzucht, Universität Bern, Switzerland, Institut für Tierzucht, Bremgartenstr. 109a, CH-3012 Bern, Switzerland; Busato, A., Institut für Tierzucht, Universität Bern, Switzerland, Institut für Tierzucht, Bremgartenstr. 109a, CH-3012 Bern, Switzerland; Burnens, A., Institut für Tierzucht, Universität Bern, Switzerland; Gaillard, C., Institut für Tierzucht, Universität Bern, Switzerland","Diarrhea is the most frequently diagnosed disease in Swiss cow-calf farms. During an longitudinal study conducted in 105 cow-calf farms in Switzerland in 1993-95, blood and fecal samples were collected from diarrheic calves and from calves that died because of diarrhea. Campylobacter spp. were detected in 42%, E. coli (VTEC) in 32%, rotavirus in 33%, coronavirus in 13%, coccidia in 43% and helminths in 8% of the cases. In some samples Yersinia pseudotuberculosis were isolated. The BVD-virus antigen was not detected in any of the calves examined. In most cases concurrent infection with several enteropathogens was diagnosed. Specific causes of diarrhea were therefore difficult to establish. The bacteriological findings of this study have implications for food safety: VTEC, Campylobacter spp. Yersinia spp. and cryptosporidia are considered as potential causes of zoonoses.",,"animal; animal disease; animal parasitosis; article; bacterial infection; cattle; cattle disease; diarrhea; female; microbiology; mortality; parasitology; parasitosis; Switzerland; virus infection; Animals; Bacterial Infections; Cattle; Cattle Diseases; Diarrhea; Female; Parasitic Diseases; Parasitic Diseases, Animal; Switzerland; Virus Diseases","Al-Mashat, R.R., Taylor, D.J., Production of diarrhea and dysentery in experimental calves by feeding pure cultures of Campylobacters fetus subspecies jejuni (1980) Vet. Rec., 107, pp. 459-464; Al-Mashat, R.R., Taylor, D.J., Bacteria in enteric lesions in cattle (1983) Vet. Rec., 112, pp. 5-10; Altenkruse, S.F., Hunt, J.M., Tollefson, L.K., Madden, J.M., Food and animal sources of human Campylobacter jejuni infection (1994) J. Am. Vet. Med. Assoc., 204, pp. 57-61; Assmus, G., Frerking, H., Glässer, H., Meermann, A., Rosenberger, G., (1985) Buiatrik, Band II Rinderkrankheiten. 4. Auflage, 2. , Verlag M. & H. Schaper, Hannover; Bauer, G., Bachmann, P.A., Nachweis enteropathogener Escherichia coli - Stämme und Rotaviren in Kotproben von Kälbern mit Diarrhoe (1980) Zbl. Vet. Med. B, 27, pp. 608-615; Battaglia, M., Lutz, H., Wyler, R., Serologische Übersichtsuntersuchung über die Verbreitung des bovinen Coronavirus in der Schweiz (1986) Schweiz. Arch. Tierheilk., 128, pp. 213-218; Behymer, D.E., Riemann, H.P., Utterback, W., D-Elmi, C., Franti, C.E., Mass screening of cattle sera against 14 infectious agents, using an ELISA system for monitoring health in livestock (1991) Am. J. Vet. Res., 52, pp. 1699-1705; Berchtold, M., Zaremba, W., Grunert, E., Kälberkrankheiten (1990) Neugeborenen- und Säuglingskunde der Tiere, pp. 304-315. , Walser K., Bostedt H. (Hrsg.): Ferdinand Enke Verlag Stuttgart; Behra, G.D., Garg, D.N., Batra, H.V., Chandiramani, N.K., Isolation of Yersinia pseudotuberculosis from bovine calves with enteric disorders (1984) Microbiol. Immunol., 28, pp. 237-241; Borman-Eby, H.C., McEwen, S.A., Clarke, R.C., McNab, W.B., Rahn, K., Valdivieso-Garcia, A., The sero-prevalence of verocytotoxin-producing Escherichia coli in Ontario dairy cows and associations with production and management (1993) Prev. Vet. Med., 15, pp. 261-274; Boss, P., Monckton, P.P., Nicolet, J., Burnens, A.P., Nachweis von Toxigenen verschiedener E. coli Pathotypen beim Schwein mit nichtradioaktiv markierten Sonden (1992) Schweiz. Arch. Tierheilk., 134, pp. 31-37; Brown, C.G., Davis, F.N., Yersinia pseudotuberculosis enteritis in four calves (1989) J. Comp. Path., 101, pp. 463-466; Buogo, C., Burnens, A.P., Perrin, J., Nicolet, J., Présence de Campylobacter spp., Clostridium difficile, C. perfringens et salmonelles dans des nichées de chiots et chez des chiens adultes d'un refuge (1995) Schweiz. Arch. Tierheilk., 137, pp. 165-171; Burnens, A.P., Frey, A., Lior, H., Nicolet, J., Prevalence and clinical significance of Vero-cytotoxin-producing Escherichia coli (VTEC) isolated from cattle in herds with and without calf diarrhoea (1995) J. Vet. Med. B, 42, pp. 311-318; Busato, A., Steiner, L., Tontis, A., Gaillard, C., Häufigkeiten und Ursachen von Kälberverlusten und Kälberkrankheiten in Mutterkuhbetrieben. I Methoden der Datenerhebung, Kälbermortalität, Kälbermorbidität (1997) Dtsch. Tierärztl. Wschr., 104, pp. 131-135; Callinan, R.B., Cook, R.W., Boulton, J.G., Fraser, G.C., Unger, D.B., Enterocolitis in cattle associated with Yersinia pseudotuberculosis infection (1988) Austr. Vet. J., 65 (1), pp. 8-11; Cornelissen, A.W.C.A., Verstegen, R., Van Den Brand, H., Perie, N.M., Eysker, M., Lam, T.J.G.M., Pijpers, A., An observational study of Eimeria species in housed cattle on Dutch dairy farms (1995) Vet. Parasitol., 56, pp. 7-16; De Rycke, J., Bernard, S., Laporte, J., Naciri, M., Popoff, M.R., Rodolakis, A., Prevalence of various enteropathogens in the feces of diarrheic and healthy calves (1986) Ann. Rech. Vet., 17, pp. 159-168; Diker, K.S., Diker, S., Özlem, M.B., Bovine diarrhea associated with Campylobacter hyointestinalis (1990) J. Vet. Med. B, 37, pp. 158-160; Eckert, J., Kutzer, E., Rommel, M., Bürger, H.-J., Körting, W., (1992) Veterinärmedizinische Parasitologie. 4. Auflage, , Verlag Paul Parey Berlin und Hamburg, begründet von; Boch, J., Supperer, R., Ernst, J.V., Ciordia, H., Stuedemann, J.A., Coccidia in cows and calves on pasture in north Georgia (U. S. A.) (1984) Vet. Parasitol., 15, pp. 213-221; Fukushima, H., Saito, K., Tsubokura, M., Otsuki, K., Kawoaoka, Y., Isolation of Yersinia spp. from bovine feces (1983) J. Clin. Microbiol., 18, pp. 981-982; Ganaba, R., Bélanger, D., Dea, S., Bigras-Poulin, M., A seroepidemiological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from Northwestern Quebec (1995) Can. J. Vet. Res., 59, pp. 26-33; Garcia, M.M., Eaglesome, M.D., Rigby, C., Campylobacters important in veterinary medicine (1983) Vet. Bull., 53, pp. 793-818; Hess, R.G., Bachmann, P.A., Baljer, G., Mayr, A., Pospischil, A., Schmied, G., Synergism in experimental mixed infections of newborn colostrum-deprived calves with bovine rotavirus and enterotoxigenic Escherichia coli (ETEC) (1994) Zbl. Vet. Med., 31, pp. 585-596; Hoffer, M.A., Bovine campylobacteriosis: A review (1981) Can. Vet. J., 22, pp. 327-330; House, J.A., Economic impact of rotavirus and other neonatal disease agents of animals (1978) J. Am. Vet. Med. Ass., 173, pp. 573-576; Jactel, B., Espinasse, J., Viso, M., Valiergue, H., An epidemiological study of winter dysentery in fifteen herds in France (1990) Vet. Res. Comm., 14, pp. 367-379; Jones, F.S., Little, R.B., Orcutt, M., A continuation of the study of the etiology of infectious diarrhea (winter scours) in cattle (1932) Proc. Am. Vet. Med. Ass., , Atlanta, 1932; Juranek, D., Cryptosporidiosis sources of infection and guidelines for prevention (1995) Clin. Infect. Dis., 21 (1 SUPPL.), pp. 57-61; Kirckpatrick, C.E., (1985) Cryptosporidium Infection as a Cause of Calf Diarrhea, 1, pp. 515-528. , The Veterinary Clinics of North America, Saunders Company West Washington Square Philadelphia PA; Kodituwakku, S.N., Harbour, D.A., Persistent excretion of rotavirus by pregnant cows (1990) Vet. Rec., 126, pp. 547-549; Lynch, J., Improved Yersinia isolation from enteric specimens (1986) Can. Vet. J., 27, p. 154; Messerli, J., Yersinia pseudotuberculosis, Erreger einer Mastitis beim Rind (1972) Zbl. Bakt. Hyg., 222, pp. 280-282; Myers, L.L., Firehammer, B.D., Border, M.M., Shoop, D.S., Prevalence of enteric pathogens in the feces of healthy beef calves (1984) Am. J. Vet. Res., 45, pp. 1544-1548; Nicolet, J., (1985) Kompendium der Veterinärmedizinischen Bakteriologie, , Pareys Studientexte, Verlag Paul Parey, Berlin Hamburg; Nillo, L., Bovine coccidiosis in Canada (1970) Can. Vet. J., 11, pp. 91-98; Ostroff, S.M., Tarr, P.I., Neill, M.A., Lewis, J.H., Hargrett-Bean, N., Kobayashi, J.M., Toxin genotypes and plasmid profiles as determinants of systemic sequelae in Escherichia coli O157:H7 infections (1989) J. Infect. Dis., 6, pp. 994-998; Pivont, P., Antoine, H., L'infestation intestinale à cryptosporidies chez le veau nouveau-né: Une revue (1982) Ann. Méd. Vét., 126, pp. 189-203; Radostits, O.M., Blood, D.C., Gay, C.C., Arundel, J.H., Ikede, B.O., Mckenzie, R.A., Tremblay, R.R.M., (1994) Veterinary Medicine. A Textbook of the Diseases of Cattle, Sheep, Goats and Horses. 8th Ed., , Baillière Tindall, London, Philadelphia, Sydney, Tokyo, Toronto; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimental induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am. J. Vet. Res., 47, pp. 1426-1432; Saif, L.J., Theil, K.W., (1989) Viral Diarrheas of Man and Animals, pp. 220-222. , CRC Press, Boca Raton, Florida; Saif, L., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved (1990) Cornell Vet., 80, pp. 303-311; Schulze, F., Campylobacter als Diarrhöerreger beim Kalb (1992) Dtsch. Tierärztl. Wschr., 99, pp. 458-461; Sinell, H.-J., (1985) Einführung in die Lebensmittelhygiene. 2. Überarbeitete Auflage, , Verlag Paul Parey, Berlin Hamburg; Skirrow, M.B., Diseases due to Campylobacter, Helicobacter and related bacteria (1994) J. Comp. Path., 111, pp. 113-149; Slee, K.J., Brigthling, P., Seiler, R.J., Enteritis in cattle due to Yersinia pseudotuberculosis infection (1988) Austr. Vet. J., 65, pp. 271-275; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Stewart, T.B., Stone, W.M., Marti, O.G., Strongyloides ransomi: Prenatal and transmammary infection of pigs of sequential litters from dams experimentally exposed as weanlings (1976) Am. J. Vet. Res., 37, pp. 541-544; Strasser, M., Vogt, H.R., Pfister, H., Gerber, H., Peterhans, E., Detection of bovine virus diarrhea virus (BVDV) in peripheral blood, cell cultures and tissue using a monoclonal antigen-capture ELISA. Immunobiology of Viral Infections (1995) Proc 3rd Congress Europ. Soc. Vet. Virol., pp. 311-316; Tzipori, S., The aetiology and diagnosis of calf diarrhoea (1981) Vet. Rec., 108, pp. 510-514; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Adv. Vet. Sc. Comp. Med., 29, pp. 104-175; Warner, D.P., Bryner, J.H., Beran, G.W., Epidemiologic study of campylobacteriosis in Iowa cattle and the possible role of unpasteurized milk as a vehicle of infection (1986) Am. J. Res., 47, pp. 254-258; Weber, A., Bergmann, I., Bauer, K., Nachweis von Campylobacter jejuni in Kotproben von Kälbern mit und ohne Enteritiden (1984) Berl. Münch. Tierärztl. Wschr., 97, pp. 10-13; Wieler, L.H., Bauerfeind, R., Bauer, G., Characterization of shiga-like toxin producing Escherichia coli (SL-TEC) isolated from calves with and without diarrhea (1992) Zbl. Bakt., 276, pp. 243-253; Wilson, J.B., McEwen, S.A., Clarke, R.C., Leslie, K.E., Waltner-Toews, D., Carlton, L.G., A case-control study of selected pathogens including verocytotoxigenic Escherichia coli in Calf diarrhea on an Ontario veal farm (1992) Can. Vet. Res., 56, pp. 184-188; Wilson, J.B., McEwen, S.A., Clarke, R.C., Leslie, K.E., Wilson, R.A., Waltner-Toews, D., Gyles, C.L., Distribution and characteristics of verocytotoxigenic Escherichia coli isolated from Ontario dairy cattle (1992) Epidemiol. Infect., 108, pp. 423-439","Steiner, L.; Institut für Tierzucht, Bremgartenstr. 109a, CH-3012 Bern, Switzerland",,,03416593,,DTTIA,"9289401","German","Dtsch. Tierarztl. Wochenschr.",Article,"Final",,Scopus,2-s2.0-0031137654
"Monceyron C., Grinde B., Jonassen T.Ø.","17534864200;36932251300;7005250658;","Molecular characterisation of the 3'-end of the astrovirus genome",1997,"Archives of Virology","142","4",,"699","706",,51,"10.1007/s007050050112","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030981902&doi=10.1007%2fs007050050112&partnerID=40&md5=d9ef7bd9f3a8e3fe1d957366bffc4071","Department of Virology, National Institute of Public Health, Oslo, Norway; Department of Virology, National Institute of Public Health, P. O. Box 4404, Torshov, N-0403 Oslo, Norway","Monceyron, C., Department of Virology, National Institute of Public Health, Oslo, Norway; Grinde, B., Department of Virology, National Institute of Public Health, Oslo, Norway; Jonassen, T.Ø., Department of Virology, National Institute of Public Health, Oslo, Norway, Department of Virology, National Institute of Public Health, P. O. Box 4404, Torshov, N-0403 Oslo, Norway","We have sequenced the 3'-end of the RNA genomes of 14 serotyped and 12 untyped isolates of human astrovirus. The sequences, which include all 8 serotypes, were used to predict secondary structures, postulate possible functional domains, reveal conserved regions suitable for nucleic acid amplification and perform phylogenetic analysis. The final nucleotides of the capsid protein precursor gene and the adjacent 3'-noncoding region were highly conserved and, except for 35 nucleotides with homology to a sequence in the 3'-end of a coronavirus RNA genome, unique to astrovirus family. This confirms that the 3'-end is a suitable target for universal and specific detection of astrovirus RNA. For the deduced 72 C-terminal amino acids of the capsid protein precursor, distances between the serotypes were found to vary from 0.1 substitution per site between serotypes 3 and 7 to more than one substitution per site between serotype 4 and the other serotypes. Different isolates of the same serotype were closely related, which indicates that the presently used type-specific antibodies differentiate between phylogenetically distinct groups. RNA secondary structures with minimal free energy were predicted using computer programs. Comparative sequence analysis verified the significance of certain of the predicted structural elements.",,"complementary DNA; virus RNA; article; chemistry; classification; conformation; genetics; Mamastrovirus; molecular genetics; nucleotide sequence; phylogeny; sequence homology; virus genome; Base Sequence; DNA, Complementary; Genome, Viral; Mamastrovirus; Molecular Sequence Data; Nucleic Acid Conformation; Phylogeny; RNA, Viral; Sequence Homology, Nucleic Acid; Astroviridae; Coronavirus; Human astrovirus; Miridae","Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J Gen Virol, 66, pp. 573-580; Gait, M.J., Karn, J., RNA recognition by the human immunodeficiency virus Tat and Rev proteins (1993) Trends Biochem Sci, 18, pp. 255-259; James, B.D., Olsen, G.J., Pace, N.R., Phylogenetic comparative analysis of RNA secondary structure (1989) Methods Enzymol, 180, pp. 227-239; Jiang, B., Monroe, S.S., Koonin, E.V., Stine, S.E., Glass, R.I., RNA sequence of astroviruses: Distinctive genomic organization and a putative retrovirus-like ribosomal frameshifting signal that directs the viral replicase synthesis (1993) Proc Natl Acad Sci USA, 90, pp. 10539-10543; Jonassen, T.Ø., Kjeldsberg, E., Grinde, B., Detection of human astrovirus serotype 1 by the polymerase chain reaction (1993) J Virol Methods, 44, pp. 83-88; Jonassen, T.Ø., Monceyron, C., Lee, T.W., Kurtz, J.B., Grinde, B., Detection of all serotypes of human astrovirus by the polymerase chain reaction (1995) J Virol Methods, 52, pp. 327-334; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Lee, T.W., Kurtz, J.B., Prevalence of human astrovirus serotypes in the Oxford region 1976-92: With evidence for two new serotypes (1994) Epidemiol Infect, 112, pp. 187-193; Lewis, T.L., Greenberg, H.B., Herrmann, J.E., Smith, L.S., Matsui, S.M., Analysis of astrovirus serotype 1 RNA, identification of the viral RNA-dependent RNA polymerase motif, and expression of a viral structural protein (1994) J Virol, 68, pp. 77-83; Madeley, C.R., Cosgrove, B.P., 28 nm particles in faeces in infantile gastroenteritis (1975) Lancet, 2, pp. 451-452; Major, M.E., Eglin, R.P., Easton, A.J., 3′ terminal nucleotide sequence of human astrovirus type 1 and routine detection of astrovirus nucleic acid and antigens (1992) J Virol Methods, 39, pp. 217-225; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M., High-frequency RNA recombination of murine coronaviruses (1986) J Virol, 57, pp. 729-737; Monroe, S.S., Jiang, B., Stine, S.E., Koopmans, M., Glass, R.I., Subgenomic RNA sequence of human astrovirus supports classification of astroviridae as a new family of RNA viruses (1993) J Virol, 67, pp. 3611-3614; Monroe, S.S., Stine, S.E., Gorelkin, L., Herrmann, J.E., Blacklow, N.R., Glass, R.I., Temporal synthesis of proteins and RNAs during human astrovirus infection of cultured cells (1991) J Virol, 65, pp. 641-648; Noel, J.S., Lee, T.W., Kurtz, J.B., Glass, R.I., Monroe, S.S., Typing of human astroviruses from clinical isolates by enzyme immunoassay and nucleotide sequencing (1995) J Clin Microbiol, 33, pp. 797-801; Pilipenko, E.V., Maslova, S.A., Sinyakov, A.N., Agol, V.I., Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: A proposal for the existence of tRNA-like terminal structures (1992) Nucleic Acids Res, 20, pp. 1739-1745; Willcocks, M.M., Brown, T.D.K., Madeley, C.R., Carter, M.J., The complete sequence of a human astrovirus (1994) J Gen Virol, 75, pp. 1785-1788; Willcocks, M.M., Carter, M.J., The 3′ terminal sequence of a human astrovirus (1992) Arch Virol, 124, pp. 279-289","Jonassen, T.O.; Department of Virology, National Institute of Public Health, P.O. Box 4404, Torshov, N-0403 Oslo, Norway",,,03048608,,ARVID,"9170498","English","ARCH. VIROL.",Article,"Final",,Scopus,2-s2.0-0030981902
"Ieven M., Goossens H.","8760308500;7101668890;","Relevance of nucleic acid amplification techniques for diagnosis of respiratory tract infections in the clinical laboratory",1997,"Clinical Microbiology Reviews","10","2",,"242","256",,143,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030908033&partnerID=40&md5=f4cd4b6eea47519af6e6a60ce8d65f42","Department of Microbiology, University Hospital, Antwerp, Belgium; Department of Microbiology, University Hospital Antwerp, Wilrijkstraat 10, B-2650 Antwerp, Belgium","Ieven, M., Department of Microbiology, University Hospital, Antwerp, Belgium, Department of Microbiology, University Hospital Antwerp, Wilrijkstraat 10, B-2650 Antwerp, Belgium; Goossens, H., Department of Microbiology, University Hospital, Antwerp, Belgium","Clinical laboratories are increasingly receiving requests to perform nucleic acid amplification tests for the detection of a wide variety of infectious agents. In this paper, the efficiency of nucleic acid amplification techniques for the diagnosis of respiratory tract infections is reviewed. In general, these techniques should be applied only for the detection of microorganisms for which available diagnostic techniques are markedly insensitive or nonexistent or when turnaround times for existing tests (e.g., viral culture) are much longer than those expected with amplification. This is the case for rhinoviruses, coronaviruses, and hantaviruses causing a pulmonary syndrome, Bordetella pertussis, Chlamydia pneumoniae, Mycoplasma pneumoniae, and Coxiella burnetii. For Legionella spp. and fungi, contamination originating from the environment is a limiting factor in interpretation of results, as is the difficulty in differentiating colonization and infection. Detection of these agents in urine or blood by amplification techniques remains to be evaluated. In the clinical setting, there is no need for molecular diagnostic tests for the diagnosis of Pneumocystis carinii. At present, amplification methods for Mycobacterium tuberculosis cannot replace the classical diagnostic techniques, due to their lack of sensitivity and the absence of specific internal controls for the detection of inhibitors of the reaction. Also, the results of interlaboratory comparisons are unsatisfactory. Furthermore, isolates are needed for susceptibility studies. Additional work remains to be done on sample preparation methods, comparison between different amplification methods, and analysis of results. The techniques can be useful for the rapid identification of M. tuberculosis in particular circumstances, as well as the rapid detection of most rifampin-resistant isolates. The introduction of diagnostic amplification techniques into a clinical laboratory implies a level of proficiency for excluding false-positive and false-negative results.",,"bacterial infection; gene amplification; human; mycosis; pneumocystis carinii; respiratory tract infection; review; sputum analysis; virus infection; Bacterial Infections; Humans; Molecular Biology; Mycoses; Pneumocystis Infections; Respiratory Tract Infections; Virus Diseases; Bacteria (microorganisms); Bordetella pertussis; Chlamydia; Chlamydophila pneumoniae; Coxiella burnetii; Fungi; Legionella; Mycobacterium; Mycobacterium tuberculosis; Mycoplasma pneumoniae; Pneumocystis carinii; Rhinovirus","Abe, C., Hirano, K., Wada, M., Kazumi, Y., Takahashi, M., Fukasawa, Y., Yoshimura, T., Goto, S., Detection of Mycobacterium tuberculosis in clinical specimens by polymeyase chain reaction and Gen-Probe amplified Mycobacterium tuberculosis direct test (1993) J. Clin. 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Virol., 70, pp. 3111-3116; Ulrich, P.P., Romeo, J.M., Daniel, L.J., Vyas, G.N., An improved method for the detection of hepatitis C virus in plasma utilizing heminested primers and internal control RNA (1993) PCR Methods Applic., 2, pp. 241-249; Ursi, J.P., Ursi, D., Leven, M., Pattyn, S.R., Utility of an internal control for the polymerase chain reaction: Application to detection of Mycoplasma pneumoniae in clinical specimens (1992) APMIS, 100, pp. 635-639; Van der Zee, A., Agterberg, C., Peeters, M., Schellekens, J., Mooi, F.R., Polymerase chain reaction assay for pertussis: Simultaneous detection and discrimination of Bordetella pertussis and Bordetella parapertussis (1993) J. Clin. Microbiol., 31, pp. 2134-2140; Van Deventer, A.J., Goessens, W.H., Van Belkum, A., Van Vliet, H.J., Van Etten, E.W., Verbrugh, H.A., Improved detection of Candida albicans by PCR in blood of neutropenic mice with systemic candidiasis (1995) J. Clin. 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Microbiol., 33, pp. 2699-2703; Von Eiff, M., Roos, N., Fegeler, W., Von Eiff, C., Zühlsdorf, M., Glaser, J., Van de Loo, J., Pulmonary fungal infections in immunocompromised patients: Incidence and risk factors (1994) Mycoses, 37, pp. 329-335; Vuorinen, P., Miettinen, A., Vuento, R., Hallstrom, O., Direct detection of Mycobacterium tuberculosis complex in respiratory specimens by GenProbe amplified Mycobacterium tuberculosis Direct Test and Roche Amplicor Mycobacterium tuberculosis test (1995) J. Clin. Microbiol., 33, pp. 1856-1859; Wadowsky, R.M., Yee, R.B., Mezmar, L., Wing, E.J., Dowling, J.N., Hot water systems as sources of Legionella pneumophila in hospital and nonhospital plumbing fixtures (1982) Appl. Environ. Microbiol., 43, pp. 1104-1110; Wadowsky, R.M., Laus, S., Libert, T., States, S.J., Ehrlich, G.D., Inhibition of PCR-based assay for Bordetella pertussis by using calcium alginate fiber and aluminum shaft components of a nasopharyngeal swab (1994) J. Clin. Microbiol., 32, pp. 1054-1057; Walker, D.A., Taylor, I.K., Mitchell, D.M., Shaw, R.J., Comparison of polymerase chain reaction amplification of two mycobacterial DNA sequences, IS 6110 and the 65 kDa antigen gene, in the diagnosis of tuberculosis (1992) Thorax, 47, pp. 690-694; Walker, G.T., Nadeau, J.G., Spears, P.A., Schram, J.L., Nycz, C.M., Shank, D.D., Multiplex strand displacement amplification (SDA) and detection of DNA sequences from Mycobacterium tuberculosis and other mycobacteria (1994) Nucleic Acids Res., 22, pp. 2670-2676; Watson, M.W., Lambden, P.R., Clarke, I.N., Genetic diversity and identification by amplification of the chlamydial 60-kilodalton cysteinerich outer membrane protein gene (1991) J. Clin, Microbiol., 29, pp. 1188-1193; Whelen, A.C., Felmlee, T.A., Hunt, J.M., Williams, D.L., Roberts, G.D., Stockman, L., Persing, D.H., Direct genotypic detection of Mycobacterium tuberculosis rifampin resistance in clinical specimens by using single-tube heminested PCR (1995) J. Clin. Microbiol., 33, pp. 556-561; Williams, D.L., Waguespack, C., Eisenach, K., Crawford, J.T., Portaels, F., Characterization of rifampin resistance in pathogenic mycobacteria (1994) Antimicrob. Agents Chemother., 38, pp. 2380-2386; Wilson, S.M., McNerney, R., Nye, P.M., Godfrey-Faussett, P.D., Stoker, N.G., Voller, A., Progress toward a simplified polymerase chain reaction and its application to diagnosis of tuberculosis (1993) J. Clin. Microbiol., 31, pp. 776-782; Wobeser, W., Krajden, M., Conly, J., Simpson, H., Yim, B., D'Costa, M., Fuksa, M., Krayden, S., Evaluation of Roche amplicor PCR assay for Mycobacterium tuberculosis (1996) J. Clin. Microbiol., 34, pp. 134-139; Wollcott, M.J., Advances in nucleic acid based detection methods (1992) Clin. Microbiol. Rev., 5, pp. 370-386; Wu, D.Y., Wallace, R.B., The ligase amplification reaction (LAR)-ampIification of specific DNA sequences using sequential rounds of template-dependent ligation (1989) Genomics, 4, pp. 560-569; Yajko, D.M., Wagner, C., Tavere, V.J., Kacogöz, T., Hadley, W.K., Chambers, H.F., Quantitative culture of Mycobacterium tuberculosis from clinical sputum specimens and dilution endpoint of its detection by the amplicor PCR assay (1995) J. Clin. Microbiol., 33, pp. 1944-1947; Yuen, K.Y., Chan, K.S., Chan, C.M., Ho, B.S.W., Dal, L.K., Chan, P.Y., Ng, M.H., Use of PCR in routine diagnosis of treated and untreated pulmonary tuberculosis (1993) J. Clin. Pathol., 46, pp. 318-322; Yuen, L.K.W., Ross, B.C., Jackson, K.M., Dwyer, B., Characterization of Mycobacterium tuberculosis from Vietnamese patients by Southern blot hybridization (1993) J. Clin. Microbiol., 31, pp. 1615-1618; Zambardi, G., Roure, C., Boujaafar, N., Fouque, B., Freney, J., Fleurette, J., Comparison of three primer sets for the detection of Mycobacterium tuberculosis in clinical samples by polymerase chain reaction (1993) Ann. Biol. Clin. Paris, 51, pp. 893-897","Ieven, M.; Department of Microbiology, University Hospital Antwerp, Wilrijkstraat 10, B-2650 Antwerp, Belgium",,,08938512,,CMIRE,"9105753","English","CLIN. MICROBIOL. REV.",Review,"Final",,Scopus,2-s2.0-0030908033
"Lai M.M.C.","7401808497;","RNA-protein interactions in the regulation of coronavirus RNA replication and transcription",1997,"Biological Chemistry","378","6",,"477","481",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030754480&partnerID=40&md5=56bda818306c0176fda15e49851101bb","Howard Hughes Medical Institute, Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Lai, M.M.C., Howard Hughes Medical Institute, Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Coronavirus, with a 31-kb RNA genome, replicates its own RNA and transcribes subgenomic mRNAs by complex mechanisms. Viral RNA synthesis is regulated by multiple RNA regions, which appear to interact either directly or indirectly. Multiple cellular proteins bind to these regions and may undergo additional protein-protein interactions. These findings suggest that coronavirus RNA synthesis is carried out on a ribonucleoprotein via a mechanism that involves both viral and cellular proteins associated with viral RNA, similar to DNA-dependent RNA transcription. This mode of RNA synthesis may be applicable to most RNA viruses.","hnRNPA1; Mouse hepatitis virus; Transcription complex; UV cross-linking","cell protein; messenger rna; ribonucleoprotein; virus rna; coronavirus; nonhuman; priority journal; protein protein interaction; protein rna binding; review; rna replication; rna synthesis; rna transcription; rna virus; Animals; Coronavirus; Humans; RNA, Viral; Transcription, Genetic; Viral Proteins; Coronavirus; Murine hepatitis virus; RNA viruses","Andino, R., Rieckhof, G.E., Baltimore, D., A functional ribonucleoprotein complex forms around the 5́-end of poliovirus RNA (1990) Cell, 63, pp. 369-380; Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., Poliovirus RNA synthesis utilizes an RNP complex formed around the 5́-end of viral RNA (1993) EMBO J., 12, pp. 3587-3598; Burd, C.G., Dreyfuss, G., RNA binding specificity of hnRNP A1: Significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing (1994) EMBO J., 13, pp. 1197-1204; Danthinne, X., Seurinck, J., Meulewaeter, F., Van Montagu, M., Cornelissen, M., The 3′ untranslated region of satellite tobacco necrosis virus RNA stimulates translation in vitro (1993) Mol. Cell. Biol., 13, pp. 3340-3349; Den Boon, J.A., Spaan, W.J., Snijder, E.J., Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies (1995) Virology, 213, pp. 364-372; Dreyfuss, G., Matunis, M.J., Pinol-Roma, S., Burd, C.G., hnRNP proteins and the biogenesis of mRNA (1993) Ann. Rev. Biochem., 62, pp. 289-321; Furuya, T., Lai, M.M.C., Three different cellular proteins bind to the complementary sites on the 5′-end positive- and 3′-end negative-strands of mouse hepatitis virus RNA (1993) J. Virol., 67, pp. 7215-7222; Haynes, R.J., Buck, K.W., Complete replication of a eukaryotic virus RNA in vitro by purified RNA-dependent RNA polymerase (1990) Cell, 63, pp. 363-368; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kumar, A., Wilson, S.H., Studies of the strand-annealing activity of a mammalian hnRNA complex protein A1 (1990) Biochemistry, 29, pp. 10717-10722; Kwon, Y.K., Hecht, N.B., Binding of a phosphoprotein to the 3′ untranslated region of the mouse protamine 2 mRNA temporally represses its translation (1993) Mol. Cell. Biol., 13, pp. 6547-6557; Lahser, F.C., Marsh, L.E., Hall, T.C., Contributions of the brome mosaic virus RNA-3 3′-nontranslated region to replication and translation (1993) J. Virol., 67, pp. 3295-3303; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Ann. Rev. Microb., 44, pp. 303-333; Leathers, V., Tanguay, R., Kobayashi, M., Gallie, D.R., A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation (1993) Mol. Cell. Biol., 13, pp. 5331-5347; Liao, C.-L., Lai, M.M.C., Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J. Virol., 68, pp. 4727-4737; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.-J., Liao, C.L., Lai, M.M.C., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Lin, Y.-J., Zhang, X.M., Wu, R.-C., Lai, M.M.C., The 3′ untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA (1996) J. Virol., 70, pp. 7236-7240; Luo, G., Luytjes, W., Enami, M., Palese, P., The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure (1991) J. Virol., 65, pp. 2861-2867; Makino, S., Lai, M.M.C., Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective-interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; McBride, A.E., Schlegel, A., Kirkegaard, K., Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 2296-2301; Pardigon, N., Strauss, J.H., Mosquito homolog of the la autoantigen binds to Sindbis virus RNA (1996) J. Virol., 70, pp. 1173-1181; Quadt, R., Kao, C.C., Browning, K.S., Hershberger, R.P., Ahlquist, P., Characterization of a host protein associated with brome mosaic virus RNA-dependent RNA polymerase (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1498-1502; Singh, N.K., Atreya, C.D., Nakhasi, H.L., Identification of calreticulin as a rubella virus RNA binding protein (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 12770-12774; Wertz, G.W., Whelan, S., LeGrone, A., Ball, L.A., Extent of terminal complementarity modulates the balance between transcription and replication of vesicular stomatitis virus RNA (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 8587-8591; Yokomori, K., Banner, L.R., Lai, M.M.C., Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic length template (1992) J. Virol., 66, pp. 4671-4678; Yu, W., Leibowitz, J.L., A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology, 214, pp. 128-138; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′-end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Zhang, X., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirius leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Lai, M.M.C.; Howard Hughes Medical Institute, Dept. Mol. Microbiology Immunology, Univ. Southern CA School of Medicine, Los Angeles, CA 90033-1054, United States",,,14316730,,BICHF,"9224926","English","BIOL. CHEM.",Review,"Final",,Scopus,2-s2.0-0030754480
"Heusipp G., Harms U., Siddell S.G., Ziebuhr J.","6603559110;7006641137;7005260816;7003783935;","Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E",1997,"Journal of Virology","71","7",,"5631","5634",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030922564&partnerID=40&md5=84e21529383ec01c245d0841fdf87db0","Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany","Heusipp, G., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; Harms, U., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; Siddell, S.G., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; Ziebuhr, J., Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany","Human coronavirus 229E gene expression involves proteolytic processing of the gene 1-encoded polyproteins pp1a and pp1ab. In this study, we have detected a 71-kDa polypeptide in virus-infected cells that is released from pp1ab by the virus-encoded 3C-like proteinase and that has been predicted to contain both metal-binding and helicase domains. The polypeptide encompasses amino acids Ala-4996 to Gln-5592 of pp1ab and exhibits nucleic acid- stimulated ATPase activity when expressed as a fusion protein with the Escherichia coli maltose-binding protein. These data provide the first identification of a coronavirus open reading frame 1b-encoded enzymatic activity.",,"adenosine triphosphatase; helicase; hybrid protein; maltose binding protein; proteinase; article; coronavirus; enzyme activity; enzyme analysis; gene expression; human; human cell; metal binding; prediction; priority journal; protein degradation; virus infectivity; Adenosine Triphosphatases; Adenosine Triphosphate; Binding Sites; Cell Line; Coronavirus; Coronavirus 229E, Human; Cysteine Endopeptidases; Humans; Peptides; Recombinant Fusion Proteins; Viral Proteins",,"Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,,0022538X,,JOVIA,"9188639","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030922564
"Bos E.C.W., Dobbie J.C., Luytjes W., Spaan W.J.M.","7005778356;7005866936;6701683324;7007172944;","A subgenomic mRNA transcript of the coronavirus mouse hepatitis virus strain A59 defective interfering (DI) RNA is packaged when it contains the DI packaging signal",1997,"Journal of Virology","71","7",,"5684","5687",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031007372&partnerID=40&md5=fcf5c8a557b808fcfb1da8332ac7ce64","Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands","Bos, E.C.W., Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; Dobbie, J.C., Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; Luytjes, W., Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands","In injected cells, only the genomic RNA of the coronavirus mouse hepatitis virus strain A59 (MHY-A59) is packaged into the virions. In this study, we show that a subgenomic (sg) defective interfering (DI) RNA can be packaged into virions when it contains the DI RNA packaging signal (DI RNA- Ps). However, the sg DI RNA is packaged less efficiently than the DI genomic RNA. Thus, while specificity of packaging of RNAs into MHV-A59 virions is determined by the DI RNA-Ps, efficiency of packaging is determined by additional factors.",,"virus rna; animal cell; animal tissue; article; coronavirus; hepatitis virus; mouse; nonhuman; priority journal; quantitative diagnosis; rna analysis; signal processing; strain difference; virus capsid; Animals; Defective Viruses; L Cells (Cell Line); Mice; Murine hepatitis virus; RNA, Messenger; RNA, Viral; Virus Assembly",,"Spaan, W.J.M.; Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; email: spaan@virology.azl.nl",,,0022538X,,JOVIA,"9188649","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031007372
"Paton D., Ibata G., Sands J., McGoldrick A.","7103157927;6601944887;7101642578;6603456332;","Detection of transmissible gastroenteritis virus by RT-PCR and differentiation from porcine respiratory coronavirus",1997,"Journal of Virological Methods","66","2",,"303","309",,35,"10.1016/S0166-0934(97)00055-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030829309&doi=10.1016%2fS0166-0934%2897%2900055-4&partnerID=40&md5=0fb500a63b42913effad7de682b73ff9","Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom","Paton, D., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom; Ibata, G., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom; Sands, J., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom; McGoldrick, A., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom","An RT-PCR method was developed that amplified genetic material from the 5' end of the S protein gene of both transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), but discriminated between the two by the size of the product generated. A number of restriction endonuclease enzymes were assessed for recognition of the amplicons so produced. The assay was shown to detect viral RNA from all of the 26 different TGEV and PRCV isolates examined, covering a period from 1946 to 1996. Detection of TGEV in clinical specimens was possible using a spin column method to extract RNA and sensitivity was compared to virus isolation and antigen detection ELISA. The method could provide a means of confirming positive results from immunological screening tests such as FAT and ELISA, reducing the need for virus isolation and convalescent serology.","Gastroenteritis virus; Respiratory coronavirus; Transmissible gastroenteritis","animal cell; antigen detection; article; binding affinity; cell differentiation; coronavirus; enteritis; gene targeting; nonhuman; nucleotide sequence; oligonucleotide probe; priority journal; reverse transcription polymerase chain reaction; swine; virus detection; virus isolation; virus transmission; Animals; Coronavirus; Coronavirus Infections; Diagnosis, Differential; Feces; Gastroenteritis, Transmissible, of Swine; Intestine, Small; Membrane Glycoproteins; Molecular Sequence Data; Polymerase Chain Reaction; RNA, Viral; Sensitivity and Specificity; Serial Passage; Swine; Transmissible gastroenteritis virus; Viral Envelope Proteins; Animalia; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Bae, I., Jackwood, D.J., Benfield, D.A., Saif, L.J., Wesley, R.D., Hill, H., Differentiation of transmissible gastroenteritis virus from porcine respiratory coronavirus and other antigenically related coronaviruses by using cDNA probes specific for the 5′ region of the S glycoprotein gene (1991) J. Clin. Microbiol., 29, pp. 215-218; Bernard, S., Lantier, I., Laude, H., Aynaud, J.M., Detection of transmissible gastroenteritis coronavirus antigens by a sandwich enzyme-linked immunosorbent assay technique (1986) Amer. J. Vet. Res., 47, pp. 2441-2444; Callebaut, P., Correa, I., Pensaert, M., Jimenez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis of swine and a related porcine respiratory coronavirus (1988) J. Gen. Virol., 69, pp. 1725-1730; Cartwright, S.F., Harris, H.M., Blandford, T.B., Fincham, I., Gitter, M., A cytopathic virus causing a transmissible gastroenteritis in swine. I. Isolation and properties (1965) J. Comp. Path., 75, pp. 387-396; Garwes, D.J., Stewart, F., Elleman, C.J., Identification of epitopes of immunological importance on the peplomer of porcine transmissible gastroenteritis virus (1987) Coronaviruses, Advances in Experimental Medicine and Biology, (218), pp. 509-515. , Lai, M.M.C., Stohlman, S.A. (Eds.); Garwes, D.J., Stewart, F., Cartwright, S.F., Brown, I., Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet. Rec., 122, pp. 86-87; Harada, K., Kumagai, T., Sasahara, J., Cytopathogenicity of transmissible gastroenteritis virus in pigs (1963) Nat. Inst. Anim. Hlth. Quart., 3, pp. 166-167; Holm Jensen, M., Detection of antibodies against hog cholera virus and bovine viral diarrhoea virus in porcine serum. A comparative examination using CF, PLA and NPLA assays (1981) Acta Vet. Scand., 22, pp. 85-98; Honda, E., Takahashi, H., Okazaki, K., Minetoma, T., Kumagai, T., The multiplication of transmissible gastroenteritis viruses in several cell lines originated from porcine kidney and effects of trypsin on the growth of the viruses (1990) Jap. J. Vet. Sci., 52, pp. 217-224; Jackwood, D.J., Kwon, H.M., Saif, L.J., Molecular differentiation of transmissible gastroenteritis virus and porcine respiratory coronavirus strains (1995) Adv. Exp. Med. 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Diagn. Invest., 3, pp. 29-32","Paton, D.; Virology Department, Centr. Veterinary Lab. (Weybridge), Veterinary Laboratories Agency, Addlestone, Surrey KT15 3NB, United Kingdom; email: dpaton.wood.cvl@gtnet.gov.uk",,,01660934,,JVMED,"9255741","English","J. VIROL. METHODS",Article,"Final",Open Access,Scopus,2-s2.0-0030829309
"Fischer F., Stegen C.F., Koetzner C.A., Masters P.S.","7202883540;6602557632;6602982748;7006234572;","Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription",1997,"Journal of Virology","71","7",,"5148","5160",,76,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031010131&partnerID=40&md5=fa9ffc5150515ceac732b2703e448bae","Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Department of Biological Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Fischer, F., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Stegen, C.F., Department of Biological Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States; Koetzner, C.A., Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Masters, P.S., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12237, United States, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","We have inserted heterologous genetic material into the nonessential gene 4 of the coronavirus mouse hepatitis virus (MHV) in order to test the applicability of targeted RNA recombination for site-directed mutagenesis of the MHV genome upstream of the nucleocapsid (N) gene and to develop further genetic tools for site-directed mutagenesis of structural genes other than N. Initially, a 19-nucleotide tag was inserted into the start of gene 4a of MHV strain A59 with the N gene deletion mutant AIb4 as the recipient virus. In further work, the entire gene for the green fluorescent protein (GFP) was inserted in place of gene 4, creating the currently largest known RNA virus. The expression of GFP was demonstrated by Western blot analysis of infected cell lysates; however, the level of GFP expression was not sufficient to allow detection of fluorescence of viral plaques. Northern blot analysis of transcripts of GFP recombinants showed the expected alteration of the pattern of the nested MHV subgenomic mRNAs. Surprisingly, though, GFP recombinants also produced an RNA species that was the same size as wild-type mRNA4. Analysis of the 5' end of this species revealed that it was actually a collection of mRNAs originating from 10 different genomic fusion sites, none possessing a canonical intergenic sequence. The finding of these aberrant mRNAs suggests that long-range RNA or the ribonucleoprotein structure of the MHV genome can sometimes be the sole determinant of the site of initiation of transcription.",,"green fluorescent protein; recombinant rna; animal cell; article; controlled study; mouse; murine hepatitis coronavirus; nonhuman; priority journal; site directed mutagenesis; structural gene; virus gene; virus recombinant; virus transcription; Animals; Cell Line; Coronavirus; Gene Expression; Genetic Vectors; Green Fluorescent Proteins; L Cells (Cell Line); Luminescent Proteins; Mice; Murine hepatitis virus; Mutagenesis, Insertional; Recombination, Genetic; RNA, Messenger; RNA, Viral; Transcription, Genetic; Virus Replication","Aoki, T., Takahashi, Y., Koch, K.S., Leffert, H.L., Watabe, H., Construction of a fusion protein between protein A and green fluorescent protein and its application to western blotting (1996) FEBS Lett., 384, pp. 193-197; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bredenbeek, P.J., Rice, C.M., Animal RNA virus expression systems (1992) Semin. Virol., 3, pp. 297-310; Budzilowicz, C.J., Weiss, S.R., In vitro synthesis of two polypeptides from a nonstructural gene of coronavirus mouse hepatitis virus strain A59 (1987) Virology, 157, pp. 509-515; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Bukreyev, A., Camargo, E., Collins, P.L., Recovery of infectious respiratory syncytial virus expressing an additional, foreign gene (1996) J. Virol., 70, pp. 6634-6641; Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W., Prasher, D.C., Green fluorescent protein as a marker for gene expression (1994) Science, 263, pp. 802-805; Chang, R.-Y., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. 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Virol., 70, pp. 4646-4654","Masters, P.S.; David Axelrod Institute, Wadsworthrt Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States",,,0022538X,,JOVIA,"9188582","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0031010131
"Castilla J., Sola I., Enjuanes L.","8851950500;7003336781;7006565392;","Interference of coronavirus infection by expression of immunoglobulin G (IgG) or IgA virus-neutralizing antibodies",1997,"Journal of Virology","71","7",,"5251","5258",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030910843&partnerID=40&md5=25a995c049367c9d2f18edd01340fbf5","Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Castilla, J., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Immunoglobulin gene fragments encoding the variable modules of the heavy and light chains of a transmissible gastroenteritis coronavirus (TGEV)- neutralizing monoclonal antibody (MAb) have been cloned and sequenced. The selected MAb recognizes a highly conserved viral epitope and does not lead to the selection of neutralization escape mutants. The sequences of MAb 6A.C3 kappa and gamma 1 modules were identified as subgroup V and subgroup IIIC, respectively. The chimeric immunoglobulin genes encoding the variable modules from the murine MAb and constant modules of human gamma 1 and kappa chains were constructed by reverse transcriptase PCR. Chimeric immunoglobulins were stably or transiently expressed in murine myelomas or COS cells, respectively. The secreted recombinant antibodies had radioimmunoassay titers (i.e., the highest dilution giving a threefold increase over the background) higher than 10-3 and reduced the infectious virus more than 104-fold. Recombinant dimeric immunoglobulin A (IgA) showed a 50-fold enhanced neutralization of TGEV relative to a recombinant monomeric IgG1 which contained the identical antigen binding site. Stably transformed epithelial cell lines which expressed either recombinant IgG or IgA TGEV-neutralizing antibodies reduced virus production by &gt; 105-fold after infection with homologous virus, although a residual level of virus production (&lt;102 PFU/ml) remained in less than 0.1% of the cells. This low-level persistent infection was shown not to be due to the selection of neutralization escape mutants. The implications of these findings for somatic gene therapy with recombinant antibodies are discussed.",,"immunoglobulin a antibody; immunoglobulin g antibody; animal tissue; antibody titer; antigen binding; antigen recognition; article; binding site; coronavirus; epithelium cell; gene therapy; immunoglobulin gene; nonhuman; priority journal; swine; virus expression; virus infection; virus interference; virus neutralization; Animals; Antibodies, Monoclonal; Antibodies, Viral; Base Sequence; Cell Line, Transformed; COS Cells; DNA, Complementary; Humans; Immunoglobulin A; Immunoglobulin G; Immunoglobulin Variable Region; Mice; Molecular Sequence Data; Neutralization Tests; Recombinant Fusion Proteins; Transmissible gastroenteritis virus; Tumor Cells, Cultured; Viral Interference","Antón, I.M., Suñé, C., Meloen, R.H., Borrás-Cuesta, F., Enjuanes, L., A transmissible gastroenteritis coronavirus nucleoprotein epitope elicits T helper cells that collaborate in the in vitro antibody synthesis of the three major structural viral proteins (1995) Virology, 212, pp. 746-751; Armstrong, S.J., Outlaw, M.C., Dimmock, N.J., Morphological studies of neutralization of influenza virus by IgM (1990) J. 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Virol., 64, pp. 5367-5375; Dimmock, N.J., (1993) Neutralization of Animal Viruses, , Springer-Verlag, Heidelberg, Germany; Duan, L., Bagasra, O., Laughlin, M.A., Oakes, J.W., Pomerantz, R.J., Potent inhibition of human immunodeficiency virus type 1 replication by an intracellular anti-Rev single-chain antibody (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 5075-5079; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, pp. 337-364. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Fichot, O., Girard, M., An improved method for sequencing of RNA templates (1990) Nucleic Acids Res., 18, p. 6162; Fujinami, R.S., Oldstone, M.B.A., Antibody initiates virus persistence: Immune modulation and measles virus infection (1984) Concepts in Viral Pathogenesis, pp. 187-193. , A. L. Notkins and M. B. A. Oldstone (ed.), Springer-Verlag, New York, N.Y; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Goodman, J.W., Donch, J.J., Phage-neutralizing activity in light polypeptide chains of rabbit antibody (1965) Immunochemistry, 2, pp. 351-357; Jiang, W., Venugopal, K., Gould, E.A., Intracellular interference of tick-borne flavivirus infection by using a single-chain antibody (1995) J. Virol., 69, pp. 1044-1049; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Kabat, E.A., Antibody diversity versus antibody complementarity (1982) Pharmacol. Rev., 34, pp. 23-38; Lamm, M.E., Nedrud, J.G., Kaetzel, C.S., Mazanec, M.B., IgA and mucosal defense (1995) APMIS, 103, pp. 241-246; Liew, F.Y., Russell, S.M., Appleyard, G., Brand, C.M., Beale, J., Cross-protection in mice infected with influenza A virus by the respiratory route is correlated with local IgA antibody rather than serum antibody or cytotoxic T cell reactivity (1984) Eur. J. Immunol., 14, pp. 350-356; Liu, Y.A., Mack, W.P., Champion, C.I., Robinson, R.R., Expression of mouse: Human immunoglobulin heavy chain cDNA in lymphoid cells (1987) Gene, 54, pp. 33-40; Marasco, W.A., Haseltine, W.A., Chen, S., Design, intracellular expression, and activity of a human anti-human immunodeficiency virus type 1 gp120 single-chain antibody (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 7889-7893; Mazanec, M.B., Coudret, C.L., Fletcher, D.R., Intracellular neutralization of influenza virus by immunoglobulin A anti-hemagglutinin monoclonal antibodies (1995) J. Virol., 69, pp. 1339-1343; Mazanec, M.B., Kaetzel, C.S., Lamm, M.E., Fletcher, D., Nedrud, J.G., Intracellular neutralization of virus by immunoglobulin A antibodies (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 6901-6905; Mazanec, M.B., Nedrud, J.G., Kaetzel, C.S., Lamm, M.E., A three-tiered view of the role of IgA in mucosal defense (1993) Immunol. Today, 14, pp. 430-434; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Med. Vet. Sci., 30, pp. 190-198; McGhee, J.R., Mestecky, J., Elson, C.O., Kiyono, H., Regulation of IgA synthesis and immune response by T cells and interleukins (1989) J. Clin. Immunol., 9, pp. 175-199; Mestecky, J., McGhee, J.R., Immunoglobulin A (IgA): Molecular and cellular interactions involved in IgA biosynthesis and immune response (1987) Adv. Immunol., 40, pp. 153-245; Outlaw, M.C., Dimmock, N.J., Mechanisms of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the viral haemagglutinin (1990) J. Gen. Virol., 71, pp. 69-76; Potter, H., Weir, L., Leder, P., Enhancer-dependent expression of human k immunoglobulin genes introduced into mouse pre-B lymphocytes by electroporation (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 7161-7165; Richardson, J.H., Marasco, W.A., Intracellular antibodies: Development and therapeutic potential (1995) Trends Biotechnol., 13, pp. 306-310; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor (ed.), Wolfe Publishing Ltd, Ames, Iowa; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Sola, I., Castilla, J., Pintado, B., Sánchez-Morgado, J.M., Whitelaw, B., Clark, J., Enjuanes, L., High Level Expression of Enteric Coronavirus Neutralizing Antibody in the Milk of Transgenic Mice Using the CDNA Encoding Chimeric IgA under β-Lactoglobulin Promoter, , Submitted for publication; Staats, H.F., Jackson, R.J., Marinaro, M., Takahashi, I., Kiyono, H., McGhee, J.R., Mucosal immunity to infection with implications for vaccine development (1994) Curr. Opin. Immunol., 6, pp. 572-583; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG, and IgM(A) to protect neonatal pigs against the coronavirus transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Taylor, H.P., Dimmock, N.J., Mechanism of neutralization of influenza-virus by secretory IgA is different from that of monomeric IgA or IgG (1985) J. Exp. Med., 161, pp. 198-209; Torres, J.M., Alonso, C., Ortega, A., Mittal, S., Graham, F., Enjuanes, L., Tropism of human adenovirus type 5-based vectors in swine and their ability to protect against transmissible gastroenteritis coronavirus (1996) J. Virol., 70, pp. 3770-3780; Torres, J.M., Sanchez, C., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; VanCott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Weidle, U.H., Borgya, A., Mattes, R., Lenz, H., Buckel, P., Reconstitution of functionally active antibody directed against creatine kinase from separately expressed heavy and light chains in non-lymphoid cells (1987) Gene, 51, pp. 21-29; Weidle, U.H., Koch, S., Buckel, P., Expression of antibody cDNA in murine myeloma cells: Possible involvement of additional regulatory elements in transcription of immunoglobulin genes (1987) Gene, 60, pp. 205-216; Wesley, R.D., Woods, R.D., Immunization of pregnant gilts with PRCV induces lactogenic immunity for protection of nursing piglets from challenge with TGEV (1993) Vet. Microbiol., 38, pp. 31-40; Xoma Co. May 1987. Patent WO 87/02671","Enjuanes, L.; Dept. of Molecular and Cell Biology, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; email: l.enjuanes@cnb.uam.es",,,0022538X,,JOVIA,"9188593","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030910843
"Denis F., Barrière E., Venot C., Ranger-Rogez S., Durepaire N., Martin C., Ploy M.C.","35414314000;6603600879;13607681600;7003600376;6507055798;35242677700;7004029822;","Virus associated with the gastrointestinal tract [Virus et infections gastro-intestinales]",1997,"Annales de Biologie Clinique","55","4",,"275","287",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030811847&partnerID=40&md5=41c62122919ac41f9afefe87753c3adc","Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France","Denis, F., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Barrière, E., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Venot, C., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Ranger-Rogez, S., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Durepaire, N., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Martin, C., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France; Ploy, M.C., Dept. de Bacteriol.-Virologie-Hyg., CHU Dupuytren, 2, avenue Martin-Luther-King, 87042 Limoges Cedex, France","Numerous viruses found in the gut are not associated with primary infection or disease of the gastrointestinal tract. Other groups or viruses are not classically associated with infection of the gut but can infect the gastrointestinal tract in immunocompromised individuals (herpes simplex virus, cytomegalovirus, papillomavirus...). The viruses associated with gastroenteritis represent a large number of taxonomic group. Because these viruses have in general been difficult to cultivate, most members of this group were firstly detected by electron microscopic examination (adenovirus, astrovirus, calicivirus, coronavirus, rotavirus...). The most widely used diagnostic techniques for adenovirus (40/41), rotavirus and astrovirus detection in faecal samples include immunoassays such as Elisa and latex agglutination. Nucleic acid hybridization techniques have generally not proven to be substantially sensitive and the more sensitive techniques recently developed use the polymerase chain reaction (adenovirus) or the reverse transcription/polymerase chain reaction (astrovirus, calicivirus, coronavirus, rotavirus). Special efforts have been made in the search for efficient procedures to extract viral nucleic acids, and to establish the optimal conditions for the amplification and identification of PCR products but the candidat viruses were very different,, consensus procedures were not determined, and amplification kits were not actually commercialized.","Adenovirus; Astrovirus; Calicivirus; Gastrointestinal tract; Rotavirus; Viruses","adenovirus; astrovirus; calicivirus; coronavirus; enzyme linked immunosorbent assay; feces analysis; gastrointestinal infection; human; latex agglutination test; nonhuman; polymerase chain reaction; reverse transcription polymerase chain reaction; review; rotavirus; virus detection; virus infection; Gastroenteritis; Humans; Laboratory Techniques and Procedures; Virus Diseases; Viruses; Adenoviridae; Astroviridae; Caliciviridae; Coronavirus; Cytomegalovirus; Herpes; Papillomavirus; Rotavirus; Simplexvirus","Blacklow, N.R., Greenberg, H.B., Viral gastroenteritis (1991) N Engl J Med, 325, pp. 252-264; Durepaire, N., Pradie, M.P., Ploy, M.C., Mounier, M., Ranger-Rogez, S., Martin, Ch., Les adénovirus dans les prélèvements de selles en milieu hospitalier: Comparaison avec les principaux agents des gastroentérites (rotavirus, Campylobacter, Salmonella) (1995) Pathol Biol, 43, pp. 601-610; Conner, M.E., Ramig, R.F., Viral Enteric Diseases (1997) Viral Pathogenesis, pp. 713-743. , Nathanson N, et al. Philadelphia, Ed. Lippincott. Publishers; Liu, B.L., Clarke, J.N., Caul, E.O., Lambden, P.R., Human enteric caliciviruses have a unique genome structure and are distinct from the Norwalk-like viruses (1995) Arch Virol, 140, pp. 1345-1356; Bishop, R., Lund, J., Cipriani, E., Unicomb, L., Barnes, G., Clinical serological and intestinal immune responses to rotavirus infection in humans (1990) Medical Virology, pp. 85-109. , de la Maza LM, Peterson EM. New York: Plenum Press; Garbag-Chenon, A., Gastroentérites virales (1993) Virologie Médicale, pp. 289-298. , Crainic R, Nicolas JC. Cachan: Ed. Editions Médicales Internationales; Kapikian, A.Z., Chanock, R.M., Viral gastroenteritis (1989) Viral Infections of Humans Epidemiology and Control, pp. 293-340. , Evans AS, Ed. Plenum Medical Book, Co. New York and London, Chapter II (third Ed.); Madeley, C.R., Viruses associated with acute diarrhoeal disease (1994) Principles and Practice of Clinical Virology (Third Edition), pp. 189-227. , Zuckermann AJ, Banatvala JE, Pattison JR. Ed. John Wiley and Sons Ltd, Chichester; Mammette, A., (1992) Virologie Médicale à l'usage des Étudiants et des Praticiens, , La Madeleine, Editions C et R; Monroe, S.S., Glass, R.I., Noah, N., Flewett, T.H., Caul, O., Ashton, C.I., Electron microscopic reporting of gatrointestinal viruses in the United Kingdom, 1985-1987 (1991) J Med Virol, 33, pp. 193-198; Ackermann, H.W., Berthiaume, L., (1995) Atlas of Virus Diagrams, , Boca Raton, CRC Press; Kohli, E., Pothier, P., Denis, F., Freymuth, F., Goudeau, A., Multicenter evaluation of a new commercial latex agglutination test using a monoclonal antibody for rotavirus detection (1989) Eur J Clin Microbiol Infect Dis, 8, pp. 251-253; Wilde, J., Yolken, R., Willoughby, R., Eiden, J., Improved detection of rotavirus shedding by polymerase chain reaction (1991) Lancet, 337, pp. 323-326","Denis, F.; Dept Bacteriologie-virologie-hygiene, CHU Dupuytren, 2 avenue Martin-Luther-King, 87042 Limoges cedex, France",,,00033898,,ABCLA,"9309226","French","ANN. BIOL. CLIN.",Review,"Final",,Scopus,2-s2.0-0030811847
"Pitkäranta A., Arruda E., Malmberg H., Hayden F.G.","7003331729;7004935664;7003601862;7103233446;","Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR",1997,"Journal of Clinical Microbiology","35","7",,"1791","1793",,145,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842335103&partnerID=40&md5=2d033ed3a4944b320a7106515e7409ea","Depts. of Int. Med. and Pathology, University of Virginia, Charlottesville, VA 22908, United States; Department of Otolaryngology, Helsinki University Hospital, FIN-00290 Helsinki, Finland; Faculty of Medicine, University of Sao Paulo, Ribeirão Preto, SP 14049-900, Brazil; University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Pitkäranta, A., Depts. of Int. Med. and Pathology, University of Virginia, Charlottesville, VA 22908, United States, Department of Otolaryngology, Helsinki University Hospital, FIN-00290 Helsinki, Finland; Arruda, E., Depts. of Int. Med. and Pathology, University of Virginia, Charlottesville, VA 22908, United States, Faculty of Medicine, University of Sao Paulo, Ribeirão Preto, SP 14049-900, Brazil; Malmberg, H., Department of Otolaryngology, Helsinki University Hospital, FIN-00290 Helsinki, Finland; Hayden, F.G., Depts. of Int. Med. and Pathology, University of Virginia, Charlottesville, VA 22908, United States, University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Of 20 adults with acute community-acquired sinusitis (ACAS), rhinovirus was detected in specimens from 10 (50%) patients, including maxillary aspirates from 8 (40%) patients and nasal swabs from 9 (45%) patients, by reverse transcription-PCR (RT-PCR). Human coronavirus was detected by RT-PCR in nasal swabs from 3 of 20 patients but in no sinus secretions. These findings suggest that rhinovirus is an important cause of ACAS and that viral invasion of the sinus cavity itself may be a common event during the disease.",,"article; clinical article; cytodiagnosis; human; nonhuman; nose smear; priority journal; reverse transcription polymerase chain reaction; rhinovirus; sinusitis; virus characterization; Adult; Aged; Community-Acquired Infections; Female; Humans; Male; Middle Aged; Picornaviridae Infections; Polymerase Chain Reaction; Rhinovirus; Sinusitis","Arola, M., Ziegler, T., Ruuskanen, O., Respiratory virus infection as a cause of prolonged symptoms in acute otitis media (1990) J. Pediatr., 116, pp. 697-701; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings by PCR (1993) Mol. Cell. Probes, 7, pp. 373-379; Arruda, E., Crump, C.E., Rollins, B.S., Ohlin, A., Hayden, F.G., Comparative susceptibilities of human embryonic fibroblasts and HeLa cells for isolation of human rhinoviruses (1996) J. Clin. Microbiol., 34, pp. 1277-1279; Boni, J., Schupbach, J., Sensitive and quantitative detection of PCR-amplified HIV-1 DNA products by an enzyme linked immunoassay following solution hybridization with two differently labelled oligonucleotide probes (1993) Mol. Cell. Probes, 7, pp. 361-371; Evans, F.O., Sydnor, J.B., Moore, W.E.C., Moore, G.R., Manwaring, J.L., Brill, A.H., Jackson, R.J., Gwaltney, J.M., Sinusitis of the maxillary antrum (1975) N. Engl. J. Med., 293, pp. 735-739; Gwaltney Jr., J.M., Rueckert, R.R., Rhinovirus (1997) Clinical Virology, pp. 1025-1047. , D. D. Richman, R. J. Whitley, and F. G. Havden (ed.). Churchill Livingstone, New York, N.Y; Gwaltney Jr., J.M., Phillips, C.G., Miller, R.D., Riker, D.K., Computed tomographic study of the common cold (1994) N. Engl. J. Med., 330, pp. 25-30; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypiä, T., Hurskainen, P., Pallansch, M., Detection of enteroviruses and rhinoviruses in clinical specimens by PCR and liquid-phase hybridization (1995) J. Clin. Microbiol., 33, pp. 648-653; Hamory, B.H., Sande, M.A., Sydnor Jr., A., Seale, D.L., Gwaltney Jr., J.M., Etiology and antimicrobial therapy of acute maxillary sinusitis (1979) J. Infect. Dis., 139, pp. 197-201; Hyypiä, T., Auvinen, P., Maaronen, M., Polymerase chain reaction for human picornaviruses (1989) J. Gen. Virol., 70, pp. 3261-3268; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Lambden, P.R., Holgate, S.T., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J. Clin. Microbiol., 31, pp. 111-117; Kamahora, T., Soe, L.H., Lai, M.M.L., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Myint, S., Harmsen, D., Raabe, T., Siddell, S.G., Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) J. Med. Virol., 31, pp. 165-172; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell. Probes, 8, pp. 357-364; Myint, S.H., Human coronaviruses: A brief review (1994) Rev. Med. Virol., 4, pp. 35-46; Sung, B.S., Chonmaitree, T., Broemeling, L.D., Owen, M.J., Patel, J.A., Hedgpeth, D.C., Howie, V.M., Association of rhinovirus infection with poor bacteriologic outcome of bacterial-viral otitis media (1993) Clin. Infect. Dis., 17, pp. 38-42; Turner, B.W., Cail, W.S., Hendley, J.O., Hayden, F.G., Doyle, W.J., Sorrentino, J.V., Gwaltney Jr., J.M., Physiologic abnormalities in the paranasal sinuses during experimental colds (1992) J. Allergy Clin. Immunol., 90, pp. 474-478; Vesanen, M., Piiparinen, H., Kallio, A., Vaheri, A., Detection of herpes simplex virus DNA in cerebrospinal fluid samples using the polymerase chain reaction and microplate hybridization (1996) J. Virol. Methods, 59, pp. 1-11","Hayden, F.G.; University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States",,,00951137,,JCMID,"9196195","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-1842335103
"Fehr D., Holznagel E., Bolla S., Hauser B., Herrewegh A.A.P.M., Horzinek M.C., Lutz H.","7004257478;6603125837;6602952093;34770826600;6602355430;7102624836;57202819852;","Placebo-controlled evaluation of a modified life virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions",1997,"Vaccine","15","10",,"1101","1109",,34,"10.1016/S0264-410X(97)00006-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030747658&doi=10.1016%2fS0264-410X%2897%2900006-6&partnerID=40&md5=bfe9736623e477cafb8112140ba09691","Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland; Department of Veterinary Pathology, University of Berne, Berne, Switzerland; Department of Veterinary Pathology, University of Zurich, Zurich, Switzerland; Department of Veterinary Virology, Utrecht University, Utrecht, Netherlands","Fehr, D., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland; Holznagel, E., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland, Department of Veterinary Pathology, University of Berne, Berne, Switzerland; Bolla, S., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland; Hauser, B., Department of Veterinary Pathology, University of Zurich, Zurich, Switzerland; Herrewegh, A.A.P.M., Department of Veterinary Virology, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Department of Veterinary Virology, Utrecht University, Utrecht, Netherlands; Lutz, H., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland","A modified live virus vaccine against feline infectious peritonitis (FIP) was evaluated in a double blind, placebo-controlled field trial in two high-risk populations. The vaccine was found to be safe and efficacious in one population of cats that had low antibody titre against feline coronavirus (FCoV) at the time of vaccination. Although clinically healthy at the time of vaccination, retrospectively some vaccinees that later came down with FIP were found to be RT-PCR positive for FCoV in plasma and showed changes in blood parameters consistent with early stage of FIP. It is concluded that vaccination can protect cats with no or low FCoV antibody titres and that in some cats vaccine failure was probably due to pre-existing infection.","Coronavirus; FIP; Vaccine","virus vaccine; animal cell; animal tissue; antibody titer; article; cat; coronavirus; diarrhea; drug efficacy; drug safety; fatigue; female; male; nonhuman; peritonitis; population risk; priority journal; sneezing; vaccination; Animals; Antibodies, Viral; Cats; Coronavirus, Feline; Double-Blind Method; Feline Infectious Peritonitis; Female; Male; Polymerase Chain Reaction; Safety; Viral Vaccines; Viremia","Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, p. 165; Sanchez, C.M., Jimenez, G., Laviada, M.D., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, p. 410; Lutz, H., Lehmann, R., Winkler, G., Das feline Immunschwächevirus in der schweiz: Klinik und Epidemiologie im Vergleich mit dem Leukämie- und dem Coronavirus (1990) Schweiz. Arch. Tierheilkd., 132, p. 217; Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, p. 133; Rohrer, C., Suter, P.F., Lutz, H., Die diagnostik der felinen infektioesen Peritonitis (FIP): Retrospektive und prospektive Untersuchungen (1993) Kleintierpraxis, 38, p. 379; Evermann, J.F., Roelke, M.E., Briggs, M.B., Feline coronavirus infections of cheetaha (1986) Feline Pract., 16, p. 21; Fanton, R.W., Field safety studies of an intranasal FIPV vaccine (1991) Proceedings of the Symposium on New Perspectives on Prevention of Feline Infectious Peritonitis, p. 47. , Orlando; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, p. 1449; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonisis (1981) Am. J. Vet. 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B, 35, p. 773; Holznagel, E., Hofmann-Lehmann, R., Niederer, E., Lutz, H., Improved Method for Flow Cytometry Analysis of Feline Leukocytes, , In preparation; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, p. 684; Sachs, L., (1984) Angewandte Statistik, , Springer, Berlin; Mosmann, T.R., Cherwinski, H., Bond, M.W., Gieldin, M.A., Coffman, R.L., Two types of murine helper T cell clones. I. Definition according to profiles of lymphokine activities and secreted proteins (1986) J. Immunol., 136, p. 2348; Mosmann, T.R., Cofman, R.L., Th1 and Th2 cells: Different patterns of lymphokine secretion lead to different functional properties (1989) A. Rev. Immunol., 7, p. 145; Postorino Reeves, N.C., Vaccination against naturally occurring FIP in a single large cat shelter (1995) Feline Pract., 23, p. 81; Hoskins, J.D., Henk, W.G., Storz, J., Kearney, M.T., The potential use of a modified live FIPV vaccine to prevent experimental FECV infection (1995) Feline Pract., 23, p. 89; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Comp. Contin. Educ. Pract. Vet., 7, p. 1001","Fehr, D.; Clinical Laboratory, Dept. of Internal Veterinary Med., University of Zurich, Winterthurerstrasse 260, CH 8057 Zurich, Switzerland",,,0264410X,,VACCD,"9269053","English","VACCINE",Article,"Final",,Scopus,2-s2.0-0030747658
"Cornelissen L.A.H.M., Wierda C.M.H., Van Der Meer F.J., Herrewegh A.A.P.M., Horzinek M.C., Egberink H.F., De Groot R.J.","57200893222;8112395100;57208372494;6602355430;7102624836;7004767057;7103077066;","Hemagglutinin-esterase, a novel structural protein of torovirus",1997,"Journal of Virology","71","7",,"5277","5286",,51,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030971073&partnerID=40&md5=4c1a4ad3c591618630fa94f9f0e19311","Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Dept. of Large Anim. Med. and Nutr., Veterinary Faculty, Utrecht University, 3584 CL Utrecht, Netherlands","Cornelissen, L.A.H.M., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands, Dept. of Large Anim. Med. and Nutr., Veterinary Faculty, Utrecht University, 3584 CL Utrecht, Netherlands; Wierda, C.M.H., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Van Der Meer, F.J., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Herrewegh, A.A.P.M., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Egberink, H.F., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; De Groot, R.J., Virology Unit, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands","We have characterized the 3'-most 3 kb of the genome of bovine torovirus (BoTV) strain Breda. A novel 1.2-kb gene, located between the genes for the membrane and nucleocapsid proteins, was identified. This gene, the 3'-most 0.5 kb of which is also present in the genome of the equine torovirus isolate Berne virus (BEV), codes for a class I membrane protein displaying 30% sequence identity with the hemagglutinin-esterases (HEs) of coronaviruses and influenza C viruses. Heterologous expression of the BoTV HE gene yielded a 65,000-molecular weight N-glycosylated protein displaying acetylesterase activity. Serologic evidence indicates that the HE homolog is expressed during the natural infection and represents a prominent antigen. By using an antiserum raised against residues 13 to 130 of HE, the HE protein was detected in radioiodinated, sucrose gradient-purified BoTV preparations. Formal evidence that HE is a structural protein was provided by immunoelectron microscopy. In addition to the large, 17- to 20-nm spikes, BoTV virions possess shorter surface projections (6 nm on average). We postulate that these surface projections, which are absent from the BEV virion, are composed of the BoTV HE homolog. The HE gene, which has now been demonstrated in three different virus genera, is a showpiece example of modular evolution.",,"esterase; hemagglutinin; structural protein; animal cell; article; genetic organization; genetic recombination; glycosylation; immunoelectron microscopy; nonhuman; priority journal; torovirus; virus genome; virus isolation; virus morphology; virus nucleocapsid; virus replication; Amino Acid Sequence; Animals; Base Sequence; Cattle; Cell Line; Cricetinae; DNA, Complementary; Genome, Viral; Hemagglutinins, Viral; Molecular Sequence Data; Sequence Homology, Amino Acid; Torovirus; Viral Fusion Proteins; Viral Proteins; Viral Structural Proteins","Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995) The Coronaviridae, pp. 165-179. , S. G. 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"Paul P.S., Vaughn E.M., Halbur P.G.","7202714004;7007145803;7005935318;","Pathogenicity and sequence analysis studies suggest potential role of gene 3 in virulence of swine enteric and respiratory coronaviruses",1997,"Advances in Experimental Medicine and Biology","412",,,"317","321",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030901874&partnerID=40&md5=086a04f8e2e385f1ad0a3f02aafe3cda","Iowa State University, College of Veterinary Medicine, Ames, IA 50011, United States","Paul, P.S., Iowa State University, College of Veterinary Medicine, Ames, IA 50011, United States; Vaughn, E.M., Iowa State University, College of Veterinary Medicine, Ames, IA 50011, United States; Halbur, P.G., Iowa State University, College of Veterinary Medicine, Ames, IA 50011, United States","Coronaviruses have been commonly associated with enteric and respiratory diseases. Two of the swine coronaviruses, namely transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) have been extensively studied. TGEV replicates in both the enteric and respiratory tracts and causes enteric disease, whereas, PRCV replicates in the respiratory tract with limited to no replication in the enteric tract. We have isolated PRCV from swine herds with respiratory disease and have reproduced moderate pneumonia in gnotobiotic and conventionally reared pigs with two of the PRCV isolates. We have also identified two PRCV isolates with low virulence. One consistent difference that we have observed between PRCV isolates of different pathogenicities is in gene 3. The gene 3 is intact in the two virulent PRCV isolates, whereas gene 3 is altered in the two low virulence isolates. A similar observation has been reported for TGEV as a nonpathogenic TGEV mutant with a small plaque morphology had a deletion in gene 3. We have also observed that one of the low virulence PRCV isolates, IA1894, which has a deletion in gene 3, replicates poorly in cell cultures. Collectively these studies suggest that gene 3 may be an important determinant for in vivo virulence and in vitro replication of coronaviruses.",,"animal cell; animal model; animal tissue; article; controlled study; coronavirus; enteric virus; gene deletion; gene sequence; gnotobiotics; nonhuman; nucleotide sequence; priority journal; swine; swine disease; virus gene; virus isolation; virus pathogenesis; virus replication; virus virulence; Animals; Antigens, Viral; Coronavirus; Genes, Viral; Intestines; Sequence Deletion; Swine; Swine Diseases; Tissue Distribution; Transmissible gastroenteritis virus; Viral Structural Proteins; Animalia; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J. Vet. Diagn. Invest., 5, pp. 184-188; Halbur, P.G., Paul, P.S., Vaughn, E.M., Virulent porcine respiratory coronavirus isolates exist in the United States (1994) Proc Inter Pig Vet Soc Congr. Bangkok, p. 70. , Thailand; Hill, H., Biwer, J., Wood, R., Wesley, R., Porcine respiratory coronavirus isolated from two U.S. swine herds (1990) Proc. Am. Assoc. Swine Practitioners., pp. 333-335; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Page, K.W., Mawditt, K.L., Britton, P., Sequence comparison of the 5' end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J. Gen. Virol., 72, pp. 579-587; Paul, P.S., Vaughn, E.M., Halbur, P.G., Characterization and pathogenicity of a new porcine respiratory coronavirus strain AR310 (1992) Proc. Int. Pig Vet. Soc. Congr., 12, p. 92; Paul, P.S., Halbur, P.G., Vaughn, E.M., Significance of Porcine Respiratory Coronavirus Infection (1994) The Compendium of Continuing Education for Practicing Veterinarians, 16, pp. 1223-1245; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Quarterly., 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virology., 190, pp. 92-105; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three porcine respiratory coronavirus isolates with varying sizes of S gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence Comparison of Porcine Respiratory Coronavirus Isolates Reveal Heterogeneity in S, 3, and 3-1 Genes (1995) J. Virol., 69, pp. 3176-3184; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Woods, R.D., Small plaque variant transmissible gastroenteritis virus (1978) J. Am. Vet. Med. Assoc., 173, pp. 643-647. , 1978","Paul, P.S.; Iowa State University, College of Veterinary Medicine, Ames, IA 50011, United States",,,00652598,,AEMBA,"9192036","English","ADV. EXP. MED. BIOL.",Article,"Final",,Scopus,2-s2.0-0030901874
"Sirinarumitr T., Paul P.S., Halbur P.G., Kluge J.P.","6602842923;7202714004;7005935318;7005760957;","An overview of immunological and genetic methods for detecting swine coronaviruses, transmissible gastroenteritis virus, and porcine respiratory coronavirus in tissues",1997,"Advances in Experimental Medicine and Biology","412",,,"37","46",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031004448&partnerID=40&md5=441f818155042b7f09ba9cba24a8de11","Iowa State University, College of Veterinary Medicine, Vet. Medical Research Institute, Ames, IA 50011, United States; Iowa State University, College of Veterinary Medicine, Veterinary Diagnostic Laboratory, Ames, IA 50011, United States; Iowa State University, College of Veterinary Medicine, Veterinary Pathology, Ames, IA 50011, United States","Sirinarumitr, T., Iowa State University, College of Veterinary Medicine, Vet. Medical Research Institute, Ames, IA 50011, United States, Iowa State University, College of Veterinary Medicine, Veterinary Pathology, Ames, IA 50011, United States; Paul, P.S., Iowa State University, College of Veterinary Medicine, Vet. Medical Research Institute, Ames, IA 50011, United States; Halbur, P.G., Iowa State University, College of Veterinary Medicine, Veterinary Diagnostic Laboratory, Ames, IA 50011, United States; Kluge, J.P., Iowa State University, College of Veterinary Medicine, Veterinary Pathology, Ames, IA 50011, United States","Transmissible gastroenteritis (TGE) is an enteric disease of swine caused by a coronavirus, designated as transmissible gastroenteritis virus (TGEV). Commonly used methods for TGEV detection include viral isolation and detection of the viral antigen by indirect immunofluorescence (IFA), immunoperoxidase, and immunogold silver staining. Each of these techniques has some advantages and disadvantages. In general IFA and immunohistochemistry are preferred over viral isolation as TGEV isolation is not very reliable because not all field isolates replicate in cell cultures. The diagnosis of TGEV has become more complicated since the emergence of porcine respiratory coronavirus (PRCV). PRCV is believed to be a TGEV mutant, and can not be easily differentiated from TGEV by immunological tests. Nucleic acid probes and polymerase chain reaction (PCR) have successfully been used to detect and differentiate these viruses. These techniques can detect vital nucleic acids in the specimen but do not provide information on the cell types infected by these viruses. Recently we have developed isotopic and nonisotopic in situ hybridization techniques (ISH) for the detection of these viral nucleic acids in formalin-fixed paraffin-embedded tissues. Furthermore, this procedure can differentiate between TGEV-and PRCV-infected cells. By ISH, TGEV is detected in the mature absorptive enterocytes of tissues infected by TGEV and the crypt epithelial cells are also infected but to a lesser extent. For PRCV, the main infected cells are epithelial cells of the bronchioles, type II pneumocytes, and alveolar and septal macrophages. ISH is an excellent tool for studying molecular pathogenesis of these two viruses especially when used in combination with immunohistochemistry.",,"cell receptor; complementary dna; diaminobenzidine; dna polymerase; ethidium bromide; fluorescein; guanidine; hydrogen peroxide; messenger rna; microsomal aminopeptidase; nucleic acid; nucleotide; peroxidase; proteinase k; rna; rna directed dna polymerase; streptavidin; virus antibody; virus antigen; agar gel electrophoresis; article; autoradiography; coronavirus; dot hybridization; gastroenteritis; gene; immunofluorescence test; immunogold staining; immunohistochemistry; immunoperoxidase staining; in situ hybridization; nonhuman; polymerase chain reaction; priority journal; reverse transcription polymerase chain reaction; rna probe; virus isolation; X ray film; Animals; Antigens, Viral; Coronavirus; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Immunologic Techniques; In Situ Hybridization; RNA, Viral; Swine; Swine Diseases; Transmissible gastroenteritis virus; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Bohl, E.H., Pensaert, M.B., Transmissible gastroenteritis virus (classical enteric variant) and transmissible gastroenteritis virus (respiratory variant) (1989) Virus Infections of Porcines, pp. 139-165. , M. B. Pensaert (Ed), Elsevier Science Publishers B.N., Amsterdam; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res., 18, pp. 71-80; Callebaut, P., Correa, I., Pensaert, M., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J. Gen. Virol., 69, pp. 1725-1730; Chu, R.M., Li, N.J., Glock, R.D., Ross, R.F., Application of peroxidase-antiperoxidase staining technique for detection of transmissible gastroenteritis virus in pigs (1982) Am. J. Vet. 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Invest., 5, pp. 184-188; Halbur, P.G., Andrews, J.J., Huffman, E.L., Development of a streptavidin-biotin immunoperoxidase for the detection of porcine reproductive and respiratory syndrome virus antigen in porcine lung (1994) J. Vet. Diagn. Invest., 6, pp. 254-257; Hill, H.T., Biwer, J.D., Woods, R.D., Wesley, R.D., Porcine respiratory coronavirus isolated from two U.S. swine herds (1989) Proc. Am. Assoc. Swine. Pract., pp. 333-335; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structure polypeptides of porcine, feline, and canine coronaviruses (1982) Infect. Immun., 37, pp. 1148-1155; Jackwood, D.J., Bae, I., Jackwood, R.J., Transmissible gastroenteritis virus and porcine respiratory coronavirus molecular characterization of the S gene using cDNA probes and nucleotide sequence analysis (1993) Adv. Exp. Med. Biol., 342, pp. 43-48; Jin, L., Hemperly, J.J., Lloyd, R.V., Expression of neural cell adhesion molecule in normal and neoplastic human neuroendocrine tissues (1991) Am. J. Pathol., 138, pp. 961-969; La Bonnardiere, C., Laude, H., Interferon induction in rotavirus and coronavirus infections: A review of recent results (1983) Ann. Rech. Vet., 14, pp. 507-511; Larochelle, R., Mogar, R., The application of immunogold silver staining (IGSS) for the detection of the transmissible gastroenteritis virus in fixed tissue (1993) J. Vet. Diagn. Invest., 5, pp. 16-20; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Morin, M., Morehouse, L.G., Solorzano, R.F., Olsen, L.D., Transmissible gastroenteritis in feeder swine: Clinical, immunofluorescence and histopathological observations (1973) Can. J. Comp. Med., 37, pp. 239-248; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with 'pneumotropic' porcine respiratory coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Paul, P.S., Halbur, P.G., Vaughn, E.M., Significance of porcine respiratory coronavirus infection (1994) Compend. Cont. Educ. Pract. Vet., 16, pp. 1223-1234; Paul, P.S., Vaughn, E.M., Halbur, P.G., Characterization and pathogenicity of a new porcine respiratory coronavirus strain AR310 (1992) Proc. Int. Pig. Vet. Soc. Congr., 12, p. 92; Pensaert, M.B., Callebaut, P., Vergote, J., Isolation of a porcine respiratory non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Quart., 8, pp. 257-261; Pensaert, M.B., Haelterman, E.O., Hinsman, E.J., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions. II. Electron microscopy of the epithelium in isolated jejunal loops (1970) Arch. Gesamte. 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Iowa State University Press, Ames, IA; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virol., 190, pp. 92-105; Sherpherd, R.W., Butler, D.G., Cutz, E., Gall, D.G., The mucosal lesion in viral enteritis: Extent and dynamics of the epithelial response to virus invasion in transmissible gastroenteritis of piglets (1979) Gastroenterology, 76, pp. 770-777; Shockley, L.J., Kapke, P.A., Lapps, W., Brian, D.A., Diagnosis of porcine and bovine enteric coronavirus infections using cloned cDNA probes (1987) J. Clin. Micro., 25, pp. 1591-1596; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in the formalin-fixed paraffin-embedded tissues (1996) J. Virol. Methods., 56, pp. 149-160; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Thake, D.C., Jejunal epithelium in transmissible gastroenteritis of swine (an electron microscopic and histochemical study) (1968) Am. J. Pathol., 53, pp. 149-168; Van Nieustadt, A.P., Pol, J.M.A., Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pig (1989) Vet. Rec., 124, pp. 43-44; Vaughn, E.M., Halbur, P.G., Paul, P.S., The use of nonradioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates (1996) J. Vet. Diagn. Invest.; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, 3-1 genes (1995) J. Virol., 69, pp. 3176-3184; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol, 69, pp. 1809-1812; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet. Microbiol., 36, pp. 333-347; Wagner, J.E., Beamer, P.D., Restic, M., Electron microscopy of intestinal epithelial cells of piglets infected with a transmissible gastroenteritis virus (1973) Can. J. Comp. Med., 37, pp. 177-188; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a respiratory coronavirus antigenically similar to transmissible gastroenteritis in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1991) J. Virol., 64, pp. 4761-4768; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J. Vet. Diagn. Invest., 3, pp. 29-32; Weingartl, H., Derbyshire, J.B., Evidence of a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs (1994) J. Virol., 68, pp. 7253-7259; Weingartl, H., Derbyshire, J.B., Binding of porcine transmissible gastroenteritis virus by enterocytes from newborn and weaned piglets (1993) Vet. Microbiol., 35, pp. 1163-1169; Woods, R.D., Cheville, N.F., Gallagher, J.E., Lesions in the small intestines of newborn pigs inoculated with porcine, feline, and canine coronavirus (1981) Am. J. Vet. Res., 42, pp. 1163-1169","Sirinarumitr, T.; Iowa State University, College of Veterinary Medicine, Veterinary Med. Research Institute, Ames, IA 50011, United States",,,00652598,,AEMBA,"9191988","English","ADV. EXP. MED. BIOL.",Article,"Final",,Scopus,2-s2.0-0031004448
"Holmes K.V., Tresnan D.B., Zelus B.D.","7201657724;6602328481;6602571243;","Virus-receptor interactions in the enteric tract: Virus-receptor interactions",1997,"Advances in Experimental Medicine and Biology","412",,,"125","133",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031005737&partnerID=40&md5=4d522b0d096cdad764e4e71cc3d52362","Department of Microbiology, University of Colorado, Health Sciences Center, 4200 East 9th Avenue, Denver, CO 80262, United States","Holmes, K.V., Department of Microbiology, University of Colorado, Health Sciences Center, 4200 East 9th Avenue, Denver, CO 80262, United States; Tresnan, D.B., Department of Microbiology, University of Colorado, Health Sciences Center, 4200 East 9th Avenue, Denver, CO 80262, United States; Zelus, B.D., Department of Microbiology, University of Colorado, Health Sciences Center, 4200 East 9th Avenue, Denver, CO 80262, United States","Expression of specific virus receptors on the surface of intestinal epithelial cells or M cells can determine whether or not a animal is susceptible to infection with an enterotropic virus. Receptors for many animal viruses have been identified. The specificity of virus-receptor interactions clearly affects the species specificity of virus infection, and in some instances may be an important determinant of viral tissue tropism. In this paper, the specificity of coronavirus-receptor interactions is summarized. Porcine and human coronaviruses utilize aminopeptidase N as their receptors, but in a species-specific manner. Mouse hepatitis virus uses several rodent glycoproteins in the carcinoembryonic antigen family as receptors. In addition, some coronaviruses can interact with carbohydrate moieties on the cell surface. Understanding the molecular mechanisms of virus-receptor interactions may lead to development of novel strategies for the control of enteric vital diseases.",,"amino acid; capsid protein; carbohydrate; carcinoembryonic antigen; cell protein; complementary dna; envelope protein; glycolipid; glycoprotein; glycosyltransferase; metalloproteinase; microsomal aminopeptidase; monoclonal antibody; neuraminic acid; proteinase; receptor; transcription factor; virus receptor; article; binding affinity; coronavirus; diarrhea; intestine epithelium cell; nonhuman; priority journal; virus infection; Animals; Antigens, CD; Antigens, CD13; Cell Adhesion Molecules; Coronavirus; Coronavirus Infections; Glycoproteins; Humans; Intestinal Diseases; Mice; Receptors, Virus; Structure-Activity Relationship; Swine; Animalia; Coronavirus; Miridae; Murine hepatitis virus; Rodentia; Suidae","Bergelson, J.M., Chan, M., Solomon, K.R., St.john, N.F., Lin, H., Finberg, R.W., Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses (1994) Proc. 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Hematol., 16, pp. 1-31; Chen, D.S., Asanaka, M., Yokomori, K., Wang, F.-I., Hwang, S.B., Li, H.-P., Lai, M.M.C., A pregnancyspecific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Clarkson, N.A., Kaufman, R., Lublin, D.M., Ward, T., Pipkin, P.A., Minor, P.D., Evans, D.J., Almond, J.W., Characterization of the echovirus 7 receptor: Domains of CD55 critical for virus binding (1995) J. Virol., 69, pp. 5497-5501; Colston, E., Racaniello, V.R., Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor (1994) EMBO J., 13, pp. 5855-5862; Compton, S.R., Stephensen, C.B., Snyder, S.W., Weismiller, D.G., Holmes, K.V., Coronavirus species specificity: Murine coronavirus binds to a mouse-specific epitope on its carcinoembryonic antigen-related receptor glycoprotein (1992) J. Virol., 66, pp. 7420-7428; Compton, T., Nowlin, D.M., Cooper, N.R., Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate (1993) Urology, 193, pp. 834-841; Coutelier, J.-P., Godfraind, C., Dveksler, G.S., Wysocka, M., Cardellichio, C.B., Noel, H., Holmes, K.V., B lymphocyte and macrophage expression of carcinoembryonic antigen-related adhesion molecules that serve as receptors for murine coronavirus (1994) Europ. J. Immunol., 24, pp. 1383-1390; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norën, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Lande, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5367-5375; Dveksler, G.S., Basile, A.B., Cardellichio, C.B., Holmes, K.V., Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain (1995) J. Virol., 69, pp. 543-546; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Bcauchemin, N., Holmes, K.V., Several members of the mouse CEA-related glycoprotein family are functional receptors for murine coronavirus MHV-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci U. S. A., 90, pp. 1716-1720; Fenner, F., Woodroofe, B.M., Changes in the virulence and antigenic structure of strains of myxoma virus recovered from Australian wild rabbits between 1950 and 1964 (1965) Aust. J. Exp. Biol. Med. Sci., 43, p. 359; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus (1995) Lab. Invest., 73, pp. 615-627; Holmes, K.V., Lai, M.M.C., Coronaviridae and their replication (1996) Virology, Edition, 3, pp. 1075-1093. , Fields, B.N., ed., Raven Press, New York; Huang, J.Q., Turbide, C., Daniels, E., Jothy, S., Beauchemin, N., Spatiotemporal expression of murine carcinoembryonic antigen (CEA) gene family members during mouse embryogenesis (1990) Development, 110, pp. 573-588; Koike, S., Horie, H., Ise, I., Okitsu, A., Yoshida, M., Iizuka, N., Takeuchi, K., Nomoto, A., The poliovirus receptor protein is produced both as membrane- Bound and secreted forms (1990) EMBO J., 9, pp. 3217-3224; Mendelsohn, C.L., Wimmer, E., Racaniello, V.R., Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily (1989) Cell, 56, pp. 855-865; Nedellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. 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A., 85, pp. 4526-4529; Ward, T., Pipkin, P.A., Clarkson, N.A., Stone, D.M., Minor, P.D., Almond, J.W., Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS. a rapid immuno-focal cloning method (1994) EMBO J., 13, pp. 5070-5074; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV- Resistant SJL/J mice (1990) J. Virol, 64, pp. 3817-3823; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. U. S. A., 88, pp. 5533-5536; Wykes, M.N., Shellam, G.R., McCluskey, J., Kast, W.M., Dallas, P.B., Price, P., Murine cytomegalovirus interacts with major histocompatibility complex class 1 molecules to establish cellular infection (1993) J. Virol., 67, pp. 4182-4189; Xu, R., Mohanty, J.G., Crowell, R.L., Receptor proteins on newborn Balb/c mouse brain cells for coxsackievirus B3 are immunologically distinct from those on HeLa cells (1995) Virus. Res., 35, pp. 323-340; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56; Yokomori, K., Lai, M.M., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yokomori, K., Stohlman, S.A., Lai, M.M., The detection and characterization of multiple hemagglutininesterase (HE)-defective viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178","Holmes, K.V.; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States",,,00652598,,AEMBA,"9192004","English","ADV. EXP. MED. BIOL.",Article,"Final",,Scopus,2-s2.0-0031005737
"Baca-Estrada M.E., Babiuk L.A., Yoo D.","7004011163;35427029400;7103242554;","Hemagglutinin-esterase glycoprotein gene of bovine coronavirus delivered by adenovirus vector induces mucosal immunity in cotton rats",1997,"Advances in Experimental Medicine and Biology","412",,,"431","433",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030912817&partnerID=40&md5=475faa0d7804841298adaa78df1e1b21","Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask., Canada","Baca-Estrada, M.E., Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask., Canada; Babiuk, L.A., Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask., Canada; Yoo, D., Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask., Canada",[No abstract available],,"esterase; immunoglobulin A antibody; immunoglobulin G antibody; neutralizing antibody; virus glycoprotein; virus hemagglutinin; virus vector; Adenovirus; animal experiment; animal tissue; antibody production; antibody titer; article; cattle; controlled study; Coronavirus; gene targeting; immunization; intraduodenal drug administration; intranasal drug administration; mesentery lymph node; mucosal immunity; nonhuman; oral drug administration; priority journal; rat; virus gene; virus recombinant; Adenoviridae; Animals; Coronavirus, Bovine; Genetic Vectors; Hemagglutinins, Viral; Immunity, Mucosal; Immunoglobulin A; Sigmodontinae; Vaccines, Synthetic; Viral Fusion Proteins; Viral Proteins; Adenoviridae; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; Gossypium hirsutum; Sigmodon","Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, p. 410; Pacini, D.L., Dubovi, E., Clyde Jr., W.A., A new animal model for human respiratory tract disease due to adenovirus (1984) J. Infec. Dis., 150, p. 92; Yoo, D., Graham, L., Prevec, L., Parker, M.D., Benko, M., Zamb, T., Babiuk, L.A., Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus (1992) J. Gen. Virol., 73, p. 2591","Baca-Estrada, M.E.; Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask., Canada",,,00652598,,AEMBA,"9192051","English","ADV. EXP. MED. BIOL.",Article,"Final",,Scopus,2-s2.0-0030912817
"Zhang X., Hinton D.R., Cua D.J., Stohlman S.A., Lai M.M.C.","55715175900;7202351155;6701471337;35502534500;7401808497;","Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity",1997,"Virology","233","2",,"327","338",,30,"10.1006/viro.1997.8598","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030875194&doi=10.1006%2fviro.1997.8598&partnerID=40&md5=acaa87ffe66042dc1bd89d8158e9ce23","Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Department of Neurology, Univ. of S. California Sch. of Med., HMR-401, 2011 Zonal Avenue, Los Angeles, CA 90033, United States; Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Howard Hughes Medical Institute, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","Zhang, X., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Department of Neurology, Univ. of S. California Sch. of Med., HMR-401, 2011 Zonal Avenue, Los Angeles, CA 90033, United States; Hinton, D.R., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Cua, D.J., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Stohlman, S.A., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States; Lai, M.M.C., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States, Howard Hughes Medical Institute, Univ. of S. California Sch. of Med., Los Angeles, CA 90033-1054, United States","A defective-interfering (DI) RNA of the murine coronavirus mouse hepatitis virus (MHV) was developed as a vector for expressing interferon-γ (IFN-γ). The murine IFN-γ gene was cloned into the DI vector under the control of an MHV transcriptional promoter and transfected into MHV-infected cells IFN-γ was secreted into culture medium as early as 6 hr posttransfection and reached a peak level (up to 180 U/ml) at 12 hr posttransfection. The DI-expressed IFN-γ (DE-IFN-γ) exhibited an antiviral activity comparable to that of recombinant IFN-γ and was blocked by a neutralizing monoclonal antibody against IFN-γ. Treatment of macrophages with DE-IFN-γ selectively induced the expression of the cellular inducible nitric oxide synthase and the IFN-γ-inducing factor (IGIF) but did not affect the amounts of the MHV receptor mRNA. Antiviral activity was detected only when cells were pretreated with IFN-γ for 24 hr prior to infection; no inhibition of virus replication was detected when cells were treated with IFN-γ during or after infection. Furthermore, addition of IFN-γ together with MHV did not prevent infection, but appeared to prevent subsequent viral spread. MHV variants with different degrees of neurovirulence in mice had correspondingly different levels of sensitivities to IFN-γ treatment in vitro, with the most virulent strain being most resistant to IFN-γ treatment. Infection of susceptible mice with DE-IFN-γ-containing virus caused significantly milder disease, accompanied by more pronounced mononuclear cell infiltrates into the CNS and less virus replication, than that caused by virus containing a control DI vector. This study thus demonstrates the feasibility and usefulness of this MHV DI vector for expressing cytokines and may provide a model for studying the role of cytokines in MHV pathogenesis.",,"gamma interferon; virus vector; animal cell; article; molecular cloning; mouse; Murine hepatitis coronavirus; nonhuman; pathogenesis; priority journal; virus replication; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Benveniste, E., Inflammatory cytokines within the central nervous system: Sources, function, and mechanism of action (1992) Am. J. Physiol., 263, pp. 1-16; Bianzani, F., Autonelli, G., Physiological mechanisms of production and action of interferons in response to viral infections (1989) Adv. Exp. Med. 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Natl. Acad. Sci. USA, 88, pp. 5533-5536; Wong, G.H.W., Goeddel, D.V., Tumour necrosis factor α and β inhibit virus replication and synergize with interferons (1986) Nature, 323, pp. 819-822; Zhang, X.M., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Zhang, X.; Department of Neurology, University of Southern California, School of Medicine, 2011 Zonal Avenue, Los Angeles, CA 90033, United States",,"Academic Press Inc.",00426822,,VIRLA,"9217056","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0030875194
"Parra B., Hinton D.R., Lin M.T., Cua D.J., Stohlman S.A.","6701803000;7202351155;7404816683;6701471337;35502534500;","Kinetics of cytokine mRNA expression in the central nervous system following lethal and nonlethal coronavirus-induced acute encephalomyelitis",1997,"Virology","233","2",,"260","270",,70,"10.1006/viro.1997.8613","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030787902&doi=10.1006%2fviro.1997.8613&partnerID=40&md5=42bed29b572f5d1bc22ff7cbfc4b844e","Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States","Parra, B., Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Hinton, D.R., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Lin, M.T., Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Cua, D.J., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Stohlman, S.A., Dept. Molec. Microbiol. and Immunol., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States","The potential role(s) of cytokines in the reduction of infectious virus and persistent viral infection in the central nervous system was examined by determining the kinetics of cytokine mRNA expression following infection with the neurotropic JHM strain of mouse hepatitis virus. Mice were infected with an antibody escape variant which produces a nonlethal encephalomyelitis and compared to a clonal virus population which produces a fulminant fatal encephalomyelitis. Infection with both viruses induced the accumulation of mRNAs associated with Th1- and Th2-type cytokines, including IFN-γ, IL-4 and IL-10 Peak mRNA accumulations were coincident with the clearance of virus and there was no obvious differences between lethally and nonlethally infected mice. TNF-α mRNA was induced more rapidly in lethally infected mice compared to mice undergoing a nonfatal encephalomyelitis. Rapid transient increases in the mRNAs encoding IL-12, iNOS, IL-1α, IL-1β, and IL-6 occurred following infection. Nonlethal infections were associated with increased IL-12, IL- 1β, and earlier expression of IL-6, while lethal infections were associated with increased INOS and IL-α mRNA. These data suggest a rapid but differential response within the central nervous system cells to infection by different JHMV variants. However, neither the accumulation nor kinetics of induction provide evidence to distinguish lethal infections from nonlethal infections leading to a persistent infection. 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"Brierley I., Meredith M.R., Bloys A.J., Hagervall T.G.","7004639098;16407831900;6507341759;6603606235;","Expression of a coronavirus ribosomal frameshift signal in Escherichia coli: Influence of tRNA anticodon modification on frameshifting",1997,"Journal of Molecular Biology","270","3",,"360","373",,62,"10.1006/jmbi.1997.1134","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031577333&doi=10.1006%2fjmbi.1997.1134&partnerID=40&md5=6c89b594926395db0d12d58802bb7f4b","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Department of Microbiology, University of Umeå, S-90187, Umeå, Sweden; Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR, United Kingdom","Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Meredith, M.R., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom, Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR, United Kingdom; Bloys, A.J., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Hagervall, T.G., Department of Microbiology, University of Umeå, S-90187, Umeå, Sweden","Eukaryotic ribosomal frameshift signals generally contain two elements, a heptanucleotide slippery sequence (XXXYYYN) and an RNA secondary structure, often an RNA pseudoknot, located downstream. Frameshifting takes place at the slippery sequence by simultaneous slippage of two ribosome-bound tRNAs. All of the tRNAs that are predicted to decode frameshift sites in the ribosomal A-site (XXXYYYN) possess a hypermodified base in the anticodon-loop and it is conceivable that these modifications play a role in the frameshift process. To test this, we expressed slippery sequence variants of the coronavirus IBV frameshift signal in strains of Escherichira coli unable to modify fully either tRNA(Lys) or tRNA(Asn). At the slippery sequences UUUAAAC and UUUAAAU (underlined codon decoded by tRNA(Asn), anticodon 5' QUU 3'), frameshifting was very inefficient (2 to 3%) and in strains deficient in the biosynthesis of Q base, was increased (AAU) or decreased (AAC) only two-fold. In E. coli, therefore, hypomodification of tRNA(Asn) had little effect on frameshifting. The situation with the efficient slippery sequences UUUAAAA (15%) and UUUAAAG (40%) (underlined codon decoded by tRNA(Lys), anticodon 5' mnm5s2UUU 3') was more complex, since the wobble base of tRNA(Lys) is modified at two positions. Of four available mutants, only trmE (s2UUU) had a marked influence on frameshifting, increasing the efficiency of the process at the slippery sequence UUUAAAA. No effect on frameshifting was seen in trmC1 (cmnm5s2UUU) or trmC2 (nm5s2UUU) strains and only a very small reduction (at UUUAAAG) was observed in an asuE (mnm5UUU) strain. The slipperiness of tRNA(Lys), therefore, cannot be ascribed to a single modification site on the base. However, the data support a role for the amino group of the mnm5 substitution in shaping the anticodon structure. Whether these conclusions can be extended to eukaryotic translation systems is uncertain. Although E. coli ribosomes changed frame at the IBV signal (UUUAAAG) with an efficiency similar to that measured in reticulocyte lysates (40%), there were important qualitative differences. Frameshifting of prokaryotic ribosomes was pseudoknot-independent (although secondary structure dependent) and appeared to require slippage of only a single tRNA.","Lysyl-tRNA; Q base; Ribosomal frameshifting; RNA pseudoknot; tRNA anticodon modification","queuine; ribosome RNA; transfer RNA; anticodon; article; controlled study; Coronavirus; Escherichia coli; gene expression; molecular genetics; nonhuman; nucleotide sequence; priority journal; ribosomal frameshifting; RNA sequence; RNA structure; Avian infectious bronchitis virus; Coronavirus; Escherichia coli; Eukaryota; Prokaryota","Agris, P.F., The importance of being modified: Roles of modified nucleosides and Mg2+ (1996) Prog. Nucl. Acid Res. Mol. 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Acids Res., 19, pp. 2457-2462; Tsuchihashi, Z., Brown, P.O., Sequence requirements for efficient translational frameshifting in theEscherichia coli dnaXLys (1992) Genes Dev., 6, pp. 511-519; Tsuchihashi, Z., Kornberg, A., Translational frameshifting generates the gamma subunit of DNA polymerase III holenzyme (1990) Proc. Natl Acad. Sci. USA, 87, pp. 2516-2520; Vögele, K., Schwartz, E., Welz, C., Schiltz, E., Rak, B., High level ribosomal frameshifting directs the synthesis of IS150 gene products (1991) Nucl. Acids Res., 19, pp. 4377-4385; Watanabe, K., Hayashi, N., Oyama, A., Nishikawa, K., Ueda, T., Miura, K., Unusual anticodon loop structure found in E. coli (1993) Nucl. Acids Res., 22, pp. 79-87; Weiss, R.B., Dunn, D.M., Shuh, M., Atkins, J.F., Gesteland, R.F., E. coli (1989) Nature New. Biol., 1, pp. 159-169; Wittwer, A.J., Ching, W.-M., Selenium containing tRNAGluLysEscherichia coli (1989) Biofactors, 2, pp. 27-34; Wittwer, A.J., Stadtman, T.C., Biosynthesis of 5-methylaminomethyl-2-selenouridine, a natural occurring nucleoside in E. coli (1986) Arch. Biochem. Biophys., 248, pp. 540-550; Yokoyama, S., Nishimura, S., Modified nucleosides and codon recognition (1995) TRNA: Structure, Biosynthesis and Function, , D. Söll, & U.L. RajBhandary. Washington: ASM Press; Yokoyama, S., Watanabe, T., Murao, K., Ishikura, H., Yamaizumi, Z., Nishimura, S., Miyazawa, T., Molecular mechanism of codon recognition by tRNA species with modified uridine in the first position of the anticodon (1985) Proc. Natl Acad. Sci. USA, 82, pp. 4905-4909; Young, J.F., Desselberger, U., Graves, P., Palese, P., Shatzman, A., Rosenberg, M., Cloning and expression of influenza virus genes (1983) The Origin of Pandemic Influenza Viruses, , W.G. Laver. Amsterdam: Elsevier Science","Brierley, L.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom",,"Academic Press",00222836,,JMOBA,"9237903","English","J. MOL. BIOL.",Article,"Final",Open Access,Scopus,2-s2.0-0031577333
"Lappin M.R., Dow S.W., Reif J.S., Chavkin M.J.","7006475173;7005959709;7102293315;6602227209;","Elevated interleukin 6 activity in aqueous humor of cats with uveitis",1997,"Veterinary Immunology and Immunopathology","58","1",,"17","26",,12,"10.1016/S0165-2427(96)05766-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030826272&doi=10.1016%2fS0165-2427%2896%2905766-2&partnerID=40&md5=ab79cafdefa137cc3d3f0fa0820b8dc0","Departments of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States; Department of Pathology, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States; Department of Environmental Health, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States","Lappin, M.R., Departments of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States; Dow, S.W., Department of Pathology, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States; Reif, J.S., Department of Pathology, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States; Chavkin, M.J., Department of Environmental Health, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO 80523, United States","The purpose of this study was to assess the role of interleukin 6 (IL- 6) in feline uveitis by measuring IL-6 activity in the serum and aqueous humor of cats. Serum and aqueous humor was collected from clinically normal, random source eats (n = 10); clinically normal, specific-pathogen free cats experimentally inoculated with Toxoplasma gondii strain ME49 and sampled sequentially for 20 months (n = 4); and client-owned cats with uveitis (n = 27). Interleukin 6 activity was measured in each sample. Client-owned cats with uveitis were also evaluated for evidence of present or prior exposure to T. gondii, feline leukemia virus, feline immunodeficiency virus, and feline coronaviruses. Interleukin 6 activity was non-detectable or low in serum from cats of each group. Interleukin 6 activity was not detected in aqueous humor of clinically normal cats. Interleukin 6 activity was detected in 22/27 (81.5%) aqueous humor samples from cats with uveitis, with a range of 28.9 U ml-1-15 702.9 U ml-1 (mean = 1911.9 U ml-1 SD = 3946.7 U ml-1). Serologic evidence of exposure to T gondii, feline immunodeficiency virus, feline leukemia virus, or a coronavirus was present in 21/27 (77.8%) cats with uveitis. Interleukin 6 was detected in the aqueous humor of 18/21 (85.7%) and 3/6 (50%) of the cats with and without serologic evidence of exposure to one to the infectious diseases, respectively. Statistically significant increases in mean IL-6 activity in aqueous humor were found for cats with any evidence of infection with T. gondii, for eats with T. gondii antigen in aqueous humor and for cats with coronavirus antibody titers ≤ 1:100. Aqueous humor IL-6 activity was greater than corresponding serum IL-6 activity in 21/27 cats. These results show that IL-6 is produced intraocularly in some cats with uveitis and that IL-6 may be a mediator of uveitis in cats.","Feline; Interleukin 6; Toxoplasma gondii; Toxoplasmosis; Uveitis","immunoglobulin g; immunoglobulin m; interleukin 6; animal cell; animal disease; animal model; antibody titer; aqueous humor; article; cat; coronavirus; feline immunodeficiency virus; feline leukemia virus; nonhuman; serum; toxoplasma gondii; toxoplasmosis; uveitis; Animals; Antibodies, Protozoan; Antibodies, Viral; Aqueous Humor; Cat Diseases; Cats; Chorioretinitis; Coronavirus; Immunodeficiency Virus, Feline; Interleukin-6; Leukemia Virus, Feline; Toxoplasma; Toxoplasmosis, Animal; Toxoplasmosis, Ocular; Uveitis; Uveitis, Anterior; Animalia; Coronavirus; Felidae; Feline immunodeficiency virus; Feline leukemia virus; Felis catus; Toxoplasma gondii","Beaman, M.H., Hunter, C.A., Remington, J.S., Enhancement of intracellular replication of Toxoplasma gondii by IL-6: Interactions with IFN-gamma and TNF-alpha (1994) J. Immunol., 153, pp. 4583-4587; Chardes, T., Veige-Roussel, F., Merelee, P., Merelee, M.N., Buzoina-Gatel, D., Bout, D., Mucosal and systemic cellular immune responses induced by Toxoplasma gondii antigens in cyst orally infected mice (1993) Immunology, 78, pp. 421-429; Charkin, M.J., Lappin, M.R., Poweli, C.C., Roberts, S.M., Parshall, C.J., Reif, J.S., Seroepidemiologic and clinical observations of 93 cases of uveitis in cats (1992) Prog. Vet. Comp. Ophthalmol., 2, pp. 29-36; Chavkin, M.J., Lappin, M.R., Powell, C.C., Cooper, C.M., Munana, K.R., Toxoplasma gondii-specific antibodies in the aqueous humor of cats with toxoplasmosis (1994) Am. J. Vet. Res., 55, pp. 1244-1249; Davidson, M.G., Nasisse, M.P., English, R.V., Wilcock, B.P., Jamieson, V.E., Feline anterior uveitis: A study of 53 cases (1990) J. Am. Anim. Hosp. Assoc., 27, pp. 77-83; De Vos, A.F., Hoekzema, R., Kijlstra, A., Cytokines and uveitis, a review (1992) Curr. Eye Res., 6, pp. 581-597; De Vos, A.F., Van Haren, M.A.C., Verhagen, C., Hoekzema, R., Kijlstra, A., Kinetics of intraocular tumor necrosis factor and interleukin-6 in endotoxin-induced uveitis in the rat (1994) Invest. Ophthalmol. Vis. Sci., 35, pp. 1100-1106; Dubey, J.P., Carpenter, J.L., Histologically confirmed clinical toxoplasmosis in cats: 100 cases (1952-1990) (1993) J. Am. Vet. Med. Assoc., 203, pp. 1556-1566; Elmslie, R.E., Ogilvie, G.K., Dow, S.W., Evaluation of a biologic response modifier derived from Serratia marcescens: Effects on feline macrophages and usefulness for the prevention and treatment of viremia in feline leukemia virus-infected cats (1991) Mol. Biother., 3, pp. 231-238; English, R.V., Davidson, M.G., Nasisse, M.R., Jamieson, V.E., Lappin, M.R., Intraocular disease associated with feline immunodeficiency virus infection in cats (1990) J. Am. Vet. Med. Assoc., 196, p. 1116; Gilgor, T., Andus, T., Klapproth, J., Hirano, T., Kishimoto, T., Heinrich, P.C., Induction of rat acute-phase proteins by interleukin 6 in vivo (1988) Eur. J. Immunol., 18, pp. 717-721; Goitsuka, R., Ohashi, T., Ono, K., Yasukawa, K., Doishibara, Y., Fukui, H., Ohsugi, Y., Hasegawa, A., IL-6 activity in feline infectious peritonitis (1990) J. Immunol., 144, pp. 2599-2603; Hansen, M.B., Nielson, S.E., Berg, K., Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill (1989) J. Immunol. Methods, 119, pp. 203-206; Hoekzema, R., Murray, P.I., Van Haren, M.A.C., Helle, M., Kijlstra, A., Analysis of interleukin-6 in endotoxin-induced uveitis (1991) Invest. Ophthalmol. Vis. Sci., 32, pp. 88-95; Hunter, C.A., Roberts, C.W., Murray, M., Alexander, J.A., Detection of cytokine mRNA in the brains of mice with toxoplasmic encephalitis (1992) Parasite Immunol., 14, pp. 405-413; Hunter, C.A., Roberts, C.W., Alexander, J., Kinetics of cytokine mRNA production in the brains of mice with progressive toxoplasmic encephalitis (1992) Eur. J. Immunol., 22, pp. 2317-2322; Kauffmann, D.J.H., Van Meurs, J.C., Mertens, D.A.E., Peperkamp, E., Master, C., Gerritsen, M.E., Cytokines in vitreous humor: Interleukin-6 is elevated in proliferative vitreoretinopathy (1994) Invest. Ophthalmol. Vis. Sci., 35, pp. 900-906; Kishimoto, T., The biology of interleukin-6 (1989) Blood, 74, pp. 1-10; Kunimoto, D.Y., Nordan, R.P., Strober, W., IL-6 is a potent cofactor of IL-1 in IgM synthesis and of IL-5 in IgA synthesis (1989) J. Immunol., 143, pp. 2230-2235; Lappin, M.R., Roberts, S.M., Davidson, M.G., Powell, C.C., Reif, J.S., Enzyme-linked immunosorbent assays for the detection of Toxoplasma gondii-specific antibodies and antigens in the aqueous humor of cats (1992) J. Am. Vet. Med. Assoc., 201, pp. 1010-1016; Lappin, M.R., Gasper, P.W., Rose, B.J., Powell, C.C., Effect of primary phase feline immunodeficiency virus infection on cats with chronic toxoplasmosis (1992) Vet. Immunol. Immunopathol., 35, pp. 121-131; Murray, P.I., Hoekzema, R., Van Haren, M.A.C., De Hon, F.D., Kijlstra, A., Aqueous humor tnterleukin-6 levels in uveitis (1990) Invest. Ophthalmol. Vis. Sci., 31, pp. 917-920; Norose, K., Yano, A., Wang, X.C., Dominance of activated T cells and interleukin-6 in aqueous humor in Vogt-Koyanagi-Harada disease (1994) Invest. Ophthalmol. Vis. Sci., 35, pp. 33-39; Peiffer, R.L., Wilcock, B.P., Histopathologic study of uveitis in cats: 139 cases (1978-1988) (1991) J. Am. Vet. Med. Assoc., 198, pp. 135-138; Post, I.E., Wellenstein, R.C., Clarke, R.D., Serologic tests for feline infectious peritonitis using TGE virus antigen (1978) Proceedings, 21st Ann. Meet. Am. Assoc. Vet. Lab. Diagnost., pp. 427-436; Schluter, D., Deckert-Schluter, M., Schwendemann, G., Brunner, H., Hof, H., Expression of major histocompatibility complex class II antigens and levels of interferongamma, tumour necrosis factor, and interleukin-6 in cerebrospinal fluid and serum in Toxoplasma gondii-infected SCID and immunocompetent C.B-17 mice (1993) Immunology, 78, pp. 430-435; Van Der Lelij, A., Rothova, A., De Vries, J.P., Vetter, J.C.M., Van Haren, M.A.C., Stilma, J.S., Kijlstra, A., Analysis of aqueous humour in ocular onchocerciasis (1991) Current Eye Res., 10, pp. 169-175; Van Snick, J., Cayphass, Umik, A., Purification of NH2-terminal amino acid sequence of a T-cell derived cytokine with growth factor activity for B-cell hybridomas (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 9679-9683; Williams, D., Local and systemic implications of feline ocular disease: Iridal lesions (1994) Fel. Pract., 22, pp. 22-30","Lappin, M.R.; Department of Clinical Sciences, Colorado State University, Fort Collins, CO 80523, United States",,,01652427,,VIIMD,"9343336","English","VET. IMMUNOL. IMMUNOPATHOL.",Article,"Final",,Scopus,2-s2.0-0030826272
"Pardo M.C., Bauman J.E., Mackowiak M.","8274159300;7102784569;18341153900;","Protection of dogs against canine distemper by vaccination with a canarypox virus recombinant expressing canine distemper virus fusion and hemagglutinin glycoproteins",1997,"American Journal of Veterinary Research","58","8",,"833","836",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031201457&partnerID=40&md5=8b7ac661fceecb4bd60ca89d4eae5f46","Biol. R. and D. Department, Rhône Mérieux Inc., 115 Transtech Dr, Athens, GA 30601, United States","Pardo, M.C., Biol. R. and D. Department, Rhône Mérieux Inc., 115 Transtech Dr, Athens, GA 30601, United States; Bauman, J.E., Biol. R. and D. Department, Rhône Mérieux Inc., 115 Transtech Dr, Athens, GA 30601, United States; Mackowiak, M., Biol. R. and D. Department, Rhône Mérieux Inc., 115 Transtech Dr, Athens, GA 30601, United States","Objectives - To evaluate the safety and efficacy of a live canarypox virus recombinant-canine distemper virus (CDV) combination vaccine against virulent CDV challenge exposure, and to document lack of interference among the other modified-live virus (MLV) components. Animals - 33 specific-pathogen-free (SPF) Beagle pups (7 to 10 weeks old). Procedure - A canarypox virus recombinant-CDV combination vaccine was tested for safety and efficacy along with MLV components (canine adenovirus type 2, canine coronavirus, canine parainfluenza virus, and canine parvovirus) in 26 SPF Beagle pups. The combination vaccine was rehydrated with either Leptospira canicola-L icterohaemorrhagiae combination bacterin (vaccine 1) or sterile diluent (vaccine 2). An additional group of 7 seronegative SPF pups received the control MLV components devoid of the combination vaccine (vaccine 3). Two vaccinations were administered 21 days apart, either IM or SC. The dose of the combination vaccine used to inoculate these pups was 40 times lower than the recommended commercial dose. At 21 days after the booster vaccination, all pups were challenge exposed with a virulent CDV strain, then were observed for 21 days to record morbidity and mortality. Results - Adverse local or generalized reactions were not induced by vaccinations. All vaccinates seroconverted to CDV. Serum antibody titers to MLV components were not different, with or without inclusion of the combination vaccine. After challenge exposure, morbidity and mortality in vaccinates were 0% (0/26); in control dogs, values were 100% morbidity and 86% mortality (6/7). Brain impression smear slides made from all dogs that did not survive challenge exposure were CDV positive by use of a direct fluorescein isothiocyanate method. Conclusions - The canarypox virus-CDV combination vaccine, administered SC or IM, is a safe product that elicits CDV seroconversion, does not interfere with other vaccine components, and protects vaccinated pups against virulent CDV challenge exposure.",,"hybrid protein; recombinant vaccine; virus antibody; virus hemagglutinin; virus vaccine; animal; article; blood; Canine distemper morbillivirus; dog; dog disease; female; Fowlpox virus; immunology; incidence; male; morbidity; mortality; Animals; Antibodies, Viral; Avipoxvirus; Distemper; Distemper Virus, Canine; Dogs; Female; Hemagglutinins, Viral; Incidence; Male; Morbidity; Recombinant Fusion Proteins; Vaccines, Synthetic; Viral Vaccines","Appel, M.J.G., Yates, R.A., Foley, A.L., Canine distemper virus epizootic in lions, tigers, and leopards in North America (1994) J Vet Diagn Invest, 6, pp. 277-288; Harder, T.C., Kenter, M., Vos, H., Canine distemper virus from diseased large felids: Biological properties and phylogenetic relationships (1996) J Gen Virol, 77, pp. 397-405; Greene, C.E., (1990) Infectious Disease of the Dog and Cat, pp. 226-241. , Greene CE, ed. Philadelphia: WB Saunders Co; Norrby, E., Utter, G., Orvell, C., Protection against CDV in dogs after immunization with isolated F glycoprotein (1986) J Virol, 58, pp. 536-541; De Vries, T.C., Vytdenhaag, F.G.C., Osterhaus, A., CDV iscoms, but not measles virus iscoms protect dogs against CDV infection (1986) J Gen Virol, 69, pp. 536-541; Dudley, J.M., Nixon, A., Mumford, A.M., Distemper and measles vaccine-a comparative trial (1978) J Small Anim Pract, 19, pp. 463-468; Stephensen, C.B., Welter, J., Thaker, S.R., Ferrets as a model for Morbillivirus infections and vaccination with ALVAC and NYVAC-based CDV recombinants expressing the CDV HA and F glycoproteins (1997) J Virol, 71, pp. 1506-1513; Paoletti, E., Taylor, J., Meignier, B., Highly attenuated poxvirus vector; NYVAC, ALVAC, and TROVAC (1995) Dev Biol Stand, pp. 159-163; Pincus, S., Tartaglia, J., Paoletti, E., Poxvirus-based vector as vaccine candidates (1995) Biologicals, 23, pp. 159-164; Taylor, J., Weinberg, R., Tartaglia, J., Non-replicating viral vectors as potential vaccines: Recombinant canarypox virus expressing measles fusion (F) and hemagglutinin (HA) glycoproteins (1992) Virology, 187, pp. 321-328; Wild, F.P., Giraudon, D., Spehner, R., Fowlpox virus recombinant encoding the measles virus fusion protein: Protection of mice against fatal measles encephalitis (1990) Vaccine, 8, pp. 441-446; Pardo, M.C., Mackowiak, M., Canine distemper immunization by recombinant vaccines (1994) Proceedings. IBC Intern Symp; Appel, M.J.G., Robson, D.S., A micro-neutralization test for CDV (1973) Am J Vet Res, 34, pp. 1459-1463; Pialoux, G., Excler, J.L., Riviere, Y., A prime-boost approach to HIV preventive vaccine using a recombinant canarypox virus expressing glycoprotein 160 (MN) followed by a recombinant glycoprotein 160 (MN/LAI) (1995) AIDS Res Hum Retrovirus, 11, pp. 373-381; Egan, M.A., Pavlat, W.A., Tartaglia, J., Induction of HIV-1-specific cytolytic T lymphocyte responses in seronegative adults by non-replicating, host-range-restricted canarypox vector (ALVAC) carrying the HIV-1MN env gene (1995) J Infect Dis, 171, pp. 1623-1627; Franchini, G., Tartaglia, J., Markham, P., Highly attenuated HTLV type 1 env poxvirus vaccines induce protection against a cell-associated HTLV type 1 challenge in rabbits (1995) AIDS Res Hum Retrovirus, 11, pp. 307-313; Tartaglia, J., Jarret, O., Neil, J.C., Protection of cats against feline leukemia virus by vaccination with a canarypox virus recombinant, ALVAC-FL (1995) J Virol, 67, pp. 2370-2375; Cox, W.I., Tartaglia, J., Paoletti, E., Induction of cytotoxic T lymphocytes by recombinant canarypox (ALVAC) and attenuated vaccinia (NYVAC) viruses expressing the HIV-1 envelope glycoprotein (1993) Virology, 195, pp. 845-850; Plotkin, S.A., Cadoz, M., Meignier, B., The safety and use of canarypox vectored vaccines (1995) Dev Biol Stan, 84, pp. 164-170; Cornwell, H.J.C., Thompson, H., McCandish, I.A.P., Encephalitis in dogs associated with a batch of canine distemper (Rockborn) vaccine (1988) Vet Rec, 16, pp. 54-59; Pearce, K.S., Mitchell, W.J., Summers, B.A., Virulent and attenuatted canine distemper virus infects multiple dog brain cell types in vitro (1991) Glia, 4, pp. 408-416; Hartley, W.J., A post-vaccinal inclusion body encephalitis (1974) Vet Pathol, 11, pp. 301-312; Cadoz, M., Strady, A., Meignier, B., Immunization with canarypox virus expressing rabies glycoprotein (1992) Lancet, 339, pp. 1429-1432","Pardo, M.C.; Biol. R. and D. Department, Rhône Mérieux Inc., 115 Transtech Dr, Athens, GA 30601, United States",,,00029645,,AJVRA,"9256965","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0031201457
"Rowe C.L., Fleming J.O., Nathan M.J., Sgro J.-Y., Palmenberg A.C., Baker S.C.","7103076229;7401457370;7102650902;7004544310;7003937294;7403307881;","Generation of coronavirus spike deletion variants by high-frequency recombination at regions of predicted RNA secondary structure",1997,"Journal of Virology","71","8",,"6183","6190",,23,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030737704&partnerID=40&md5=894c4c8fb51635d6402650dc36c37b0f","Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States","Rowe, C.L., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; Fleming, J.O., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; Nathan, M.J., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; Sgro, J.-Y., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; Palmenberg, A.C., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; Baker, S.C., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States","Coronavirus RNA evolves in the central nervous systems (CNS) of mice during persistent infection. This evolution can be monitored by detection of a viral quasispecies of spike deletion variants (SDVs) (C. L. Rowe, S.C. Baker, M. J. Nathan, and J. O. Fleming, J. Virol. 71:2959-2969, 1997). We and others have found that the deletions cluster in the region from 1,200 to 1,800 nucleotides from the 5' end of the spike gene sequence, termed the 'hypervariable' region. To address how SDVs might arise, we generated the predicted folding structures of the positive- and negative-strand senses of the entire 4,139-nt spike RNA sequence. We found that a prominent, isolated stem-loop structure is coincident with the hypervariable region in each structure. To determine if this predicted stem-loop is a 'hot spot' for RNA recombination, we assessed whether this region of the spike is more frequently deleted than three other selected regions of the spike sequence in a population of viral sequences isolated from the CNS of acutely and persistently infected mice. Using differential colony hybridization of cloned spike reverse transcription-PCR products, we detected SDVs in which the hot spot was deleted but did not detect SDVs in which other regions of the spike sequence were exclusively deleted. Furthermore, sequence analysis and mapping of the crossover sites of 25 distinct patterns of SDVs showed that the majority of crossover sites clustered to two regions at the base of the isolated stem-loop, which we designated as high-frequency recombination sites 1 and 2. Interestingly, the majority of the left and right crossover sites of the SDVs were directly across from or proximal to one another, suggesting that these SDVs are likely generated by intramolecular recombination. Overall, our results are consistent with there being an important role for the spike RNA secondary structure as a contributing factor in the generation of SDVs during persistent infection.",,"virus rna; article; coronavirus; deletion mutant; nonhuman; priority journal; protein secondary structure; rna sequence; virus mutation; virus recombination; Base Sequence; DNA, Viral; Gene Deletion; Molecular Sequence Data; Murine hepatitis virus; Recombination, Genetic",,"Baker, S.C.; Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, United States; email: sbakerl@luc.edu",,,0022538X,,JOVIA,"9223514","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030737704
"Karasev A.V., Hilf M.E., Garnsey S.M., Dawson W.O.","7005975794;6701699420;6603913334;7102401975;","Transcriptional strategy of closteroviruses: Mapping the 5' termini of the citrus tristeza virus subgenomic RNAs",1997,"Journal of Virology","71","8",,"6233","6236",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030740649&partnerID=40&md5=7f84d01292f1529ed98fc29e7688f15a","Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States","Karasev, A.V., Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States; Hilf, M.E., Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States; Garnsey, S.M., Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States; Dawson, W.O., Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States","Citrus tristeza virus (CTV) induces formation of nested set of at least nine 3' coterminal subgenomic RNAs (sgRNAs) in infected tissue. The organization and expression of the 19,296-nucleotide (nt) CTV genome resembles that of coronaviruses, with polyprotein processing, translational frameshifting, and multiple sgRNA formation, but phylogenetically the CTV polymerase, like polymerases of other closteroviruses, belongs to the Sindbis virus-like lineage of RNA virus polymerases. Both positive-strand RNA virus supergroups, coronaviruses and Sindbis-like viruses, utilize different mechanisms of transcription. To address the mechanism of CTV transcription, 5' termini for the two most abundant sgRNAs, 1.5 and 0.9 kb, respectively, were mapped by runoff reverse transcription. The two sgRNAs were demonstrated to have 48- and 38-nt 5' untranslated regions (5'-UTRs), respectively. The 5'-UTR for the 1.5-kb RNA was cloned, sequenced, and demonstrated to be colinear with the 48-nt genomic sequence upstream of the initiator codon of the respective open reading frame 10, i.e., to be of continuous template origin. The data obtained suggest that the sgRNA transcription of CTV is dissimilar from the coronavirus transcription and consistent with the transcriptional mechanism of other Sindbis-like viruses. Thus, the Sindbis virus-like mechanism of transcription of the positive-strand RNA genomes might he successfully utilized by the closterovirus genome of up to 19.3 kb with multiple sgRNAs.",,"animal cell; article; carboxy terminal sequence; closterovirus; gene expression regulation; gene mapping; nonhuman; open reading frame; phylogeny; priority journal; protein processing; reverse transcription; ribosomal frameshifting; start codon; virus genome; virus transcription; Base Sequence; Closterovirus; Genome, Viral; Molecular Sequence Data; Open Reading Frames; RNA, Viral; Transcription, Genetic",,"Karasev, A.V.; Citrus Research and Education Center, University of Florida, 700 Experiment Station Rd., Lake Alfred, FL 33850-2299, United States",,,0022538X,,JOVIA,"9223524","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030740649
"Herrewegh A.A.P.M., Mähler M., Hedrich H.J., Haagmans B.L., Egberink H.F., Horzinek M.C., Rottier P.J.M., De Groot R.J.","6602355430;56935953600;7005734225;6701371301;7004767057;7102624836;7006145490;7103077066;","Persistence and evolution of feline coronavirus in a closed cat-breeding colony",1997,"Virology","234","2",,"349","363",,97,"10.1006/viro.1997.8663","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342460564&doi=10.1006%2fviro.1997.8663&partnerID=40&md5=8e53fdc43451850ffaa6af5dbc24e38b","Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; Inst. Lab. Anim. Sci. Ctrl. Lab. A., Medical School Hannover, Hannover, 30625, Germany","Herrewegh, A.A.P.M., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; Mähler, M., Inst. Lab. Anim. Sci. Ctrl. Lab. A., Medical School Hannover, Hannover, 30625, Germany; Hedrich, H.J., Inst. Lab. Anim. Sci. Ctrl. Lab. A., Medical School Hannover, Hannover, 30625, Germany; Haagmans, B.L., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; Egberink, H.F., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; Rottier, P.J.M., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands; De Groot, R.J., Virology Unit, Dept. Infect. Dis. Immunol., Fac. V., Utrecht University, 3584 CL, Utrecht, Netherlands","Feline coronavirus (FCoV) persistence and evolution were studied in a closed cat-breeding facility with an endemic serotype 1 FCoV infection. Viral RNA was detected by reverse transcriptase polymerase chain reaction (RT-PCR) in the faces and/or plasma of 36 of 42 cats (86%) tested. Of 6 cats, identified as FCoV shedders during the initial survey, 4 had detectable viral RNA in the feces when tested 111 days later. To determine whether this was due to continuous reinfection or to viral persistence, 2 cats were placed in strict isolation and virus shedding in the faces was monitored every 2-4 days. In 1 of the cats, virus shedding continued for up to 7 months. The other animal was sacrificed after 124 days of continuous virus shedding in order to identify the sites of viral replication. Viral mRNA was detected only in the ileum, colon, and rectum. Also in these tissues, FCoV-infected cells were identified by immunohistochemistry. These findings provide the first formal evidence that FCoV causes chronic enteric infections. To assess FCoV heterogeneity in the breeding facility and to study viral evolution during chronic infection, FCoV quasispecies sampled from individual cats were characterized by RT-PCR amplification of selected regions of the viral genome followed by sequence analysis. Phylogenetic comparison of nucleotides 7-146 of ORF7b to corresponding sequences obtained for independent European aria American isolates indicated that the viruses in the breeding facility form a clade and are likely to have originated from a single founder infection. Comparative consensus sequence analysis of the more variable region formed by residues 79-478 of the S gene revealed that each eat harbored a distinct FCoV quasispecies. Moreover, FCoV appeared to De subject to immune selection during chronic infection. The combined data support a model in which the endemic infection is maintained by chronically infected carriers. Virtually every cat born to the breeding facility becomes infected, indicating that FCoV is sprees very efficiently. FCoV-infected cats, however, appear to resist superinfection by closely related FCoVs.",,"virus RNA; animal disease; animal model; antibody detection; article; cat; chronic disease; Coronavirus; gastrointestinal tract; nonhuman; nucleotide sequence; persistent virus infection; priority journal; reverse transcription polymerase chain reaction; serotype; virus detection; virus replication; Animalia; Aria; Coronavirus; Felidae; Feline coronavirus; Felis catus","Addie, D.D., Jarrett, J.O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; Addie, D.D., Toth, S., Herrewegh, A.A.P.M., Jarrett, O., Feline coronavirus in the intestinal contents of cats with feline infectious peritonitis (1996) Vet. Rec., 139, pp. 522-523; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, , New York: Plenum. p. 73-113; Chen, C.M., Cavanagh, D., Britton, P., Cloning and sequencing of a 8.4-kb region from the 3′-end of a Taiwanese virulent isolate of the coronavirus transmissible gastroenteritis virus (1995) Virus Res., 38, pp. 83-89; Dayhoff, M.O., Atlas of protein sequence and structure (1979) Natl. Biomed. Res. Found., 5; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J.M., Sequence analysis of the 3′-end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-309. , S.G. Siddell. 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Virol., 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs): Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol., 28, pp. 13-24; Holland, J.J., De La Torre, J.C., Steinhauer, D.A., (1992) Genetic Diversity of RNA Viruses, pp. 1-20. , J.J. Holland. Berlin/Heidelberg/New York: Springer-Verlag; Holmes, E.C., Zhang, L.Q., Simmonds, P., Ludlam, C.A., Leigh Brown, A.J., Convergent and divergent sequence evolution in the surface envelope glycoprotein of human immunodeficiency virus type 1 within a single infected patient (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 4835-4839; Holmes, K.V., Behnke, J.N., Evolution of coronavirus during persistent infection in vitro (1981) Biochemistry and Biology of Coronavirus, pp. 287-299. , V. ter Meulen, S. Siddell, & H. Wege. 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Zeijst, W.J.M. Spaan, & M.C. Horzinek. New York: Plenum; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens utilizing feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 363-367; Perlman, S., Jacobsen, G., Moore, S., Regional localization of virus in the central nervous system of mice persistently infected with murine coronavirus JHM (1988) Virology, 166, pp. 328-338; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34, pp. 3180-3184; Rigby, M.A., Holmes, E.C., Pistello, M., MacKay, A., Brown, A.J., Neil, J.C., Evolution of structural proteins of feline immunodeficiency virus: Molecular epidemiology and evidence of selection for change (1993) J. Gen. 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Virol., 75, pp. 1789-1794","De Groot, R.J.; Dept. of Infectious Dis./Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; email: groot@vetmic.dgk.ruu.nl",,"Academic Press Inc.",00426822,,VIRLA,"9268167","English","VIROLOGY",Article,"Final",Open Access,Scopus,2-s2.0-0342460564
"Abdou S., Collomb J., Sallas F., Marsura A., Finance C.","6701908596;6603051487;6507092685;7003763370;6701554638;","Beta-cyclodextrin derivatives as carriers to enhance the antiviral activity of an antisense oligonucleotide directed toward a coronavirus intergenic consensus sequence",1997,"Archives of Virology","142","8",,"1585","1602",,45,"10.1007/s007050050182","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030849802&doi=10.1007%2fs007050050182&partnerID=40&md5=1540c25403731d94f04af6ff7f0efc14","GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France; GEVSM, Univ. H. Poincaré, Faculté de Pharmacie, B.P. 403, F-54001 Nancy Cedex, France","Abdou, S., GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France; Collomb, J., GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France; Sallas, F., GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France; Marsura, A., GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France; Finance, C., GEVSM, Univ. Henri Poincare - Nancy 1, Faculté de Pharmacie, Nancy, France, GEVSM, Univ. H. Poincaré, Faculté de Pharmacie, B.P. 403, F-54001 Nancy Cedex, France","The ability of cyclodextrins to enhance the antiviral activity of a phosphodiester oligodeoxynucleotide has been investigated. A 18-mer oligodeoxynucleotide complementary to the initiation region of the mRNA coding for the spike protein and containing the intergenic consensus sequence of an enteric coronavirus has been tested for antiviral action against virus growth in human adenocarcinoma cells. The phosphodiester oligodeoxynucleotide only showed a limited effect on virus growth rate (from 12 to 34% viral inhibition in cells treated with 7.5 to 25 μM oligodeoxynucleotide, respectively, at a multiplicity of infection of 0.1 infectious particle per cell). In the same conditions, the phosphorothioate analogue exhibited stronger antiviral activity, the inhibition increased from 56 to 90%. The inhibitory effect of this analogue was antisense and sequence-specific. Northern blot analysis showed that the sequence-dependent mechanism of action appears to be the inhibition of mRNA transcription. We conclude that the coronavirus intergenic consensus sequence is a good target for an antisense oligonucleotide antiviral action. The properties of the phosphodiester oligonucleotide was improved after its complexation with cyclodextrins. The most important increase of the antiviral activity (90% inhibition) was obtained with only 7.5 μM oligonucleotide complexed to a cyclodextrin derivative, 6-deoxy-6-S-β-D-galactopyranosyl-6-thio-cyclomaltoheptaose in a molar ratio of 1:100. These studies suggest that the use of cyclodextrin derivatives as carrier for phosphodiester oligonucleotides delivery may be an effective method for increasing the therapeutic potential of these compounds in viral infections.",,"antisense oligonucleotide; beta cyclodextrin; beta cyclodextrin derivative; cyclodextrin; drug carrier; virus RNA; article; cell culture; consensus sequence; Coronavirus; drug effect; genetics; intron; physiology; virus replication; beta-Cyclodextrins; Cells, Cultured; Consensus Sequence; Coronavirus; Cyclodextrins; Drug Carriers; Introns; Oligonucleotides, Antisense; RNA, Viral; Virus Replication; Coronavirus; Enteric coronavirus","Agrawal, S., Lyer, R.P., Modified oligonucleotides as therapeutic and diagnostic agents (1995) Curr Opin Biotechnol, 6, pp. 9-12; Agrawal, S., Antisense oligonucleotides: Towards clinical trials (1996) Trends Biotechnol, 14, pp. 376-387; Archambault, D., Stein, C.A., Cohen, J.S., Phosphorothioate oligonucleotides inhibit the replication of lentiviruses and type D retroviruses, but not that of type C retroviruses (1994) Arch Virol, 139, pp. 97-100; 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Les colloques de l'INSERM (1979) Viral Enteritis, 90, pp. 99-102; Leiter, J.M.E., Agrawal, S., Palese, P., Zamecnik, P.C., Inhibition of influenza virus replication by phophorothioate oligodeoxynucleotides (1990) Proc Natl Acad Sci USA, 87, pp. 3430-3434; Lisziewicz, J., Sun, D., Klotman, M., Agrawal, S., Zamecnik, P., Robert, G., Specific inhibition of human immunodeficiency virus type 1 replication by antisense oligonucleotides: An in vitro model for treatment (1992) Proc Natl Acad Sci USA, 89, pp. 11209-11213; Loke, S.L., Stein, C., Zhang, Xh., Mori, K., Nakanishi, M., Subasinghe, C., Cohen, J.S., Neckers, L.M., Characterization of oligonucleotide transport into living cells (1989) Proc Natl Acad Sci USA, 86, pp. 3474-3478; Lund, O.S., Nielsen, J.O., Hansen, J.E., Inhibition of HIV-1 in vitro by C-5 propyne phosphorothioate antisense to rev (1995) Antiviral Res, 28, pp. 81-91; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J Virol, 67, pp. 3304-3311; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA results from intergenic site insertion (1991) J Virol, 65, pp. 6031-6041; Manzoni, G.C., Zamfferrani, C., Granella, F., Piroxicam β-cyclodextrin in the symptomatic treatment of primary headache (1989) Meeting of the Interdisciplinare di Cardiologia e Neurologia Selecta Neurologia, pp. 449-453; Matsui, Y., Yokoi, T., Mochida, K., Catalytic Properties of Cu (II) complex with a modified cyclodextrin (1976) Chem Lett, 1, pp. 037-1040; Nakada, Y., Fattal, E., Foulquier, M., Couvreur, P., Pharmacokinetics and biodistribution of oligonucleotide adsorbed onto poly (isobutylcyanoacrylate) nano particles after intravenous administration in mice (1996) Pharm Res, 13, pp. 38-43; Onisk, D.V., Srikumaran, S., Kelling, C.L., Frey, M.L., Bovine viral diarrhoea virus-specific bovine monoclonal antibody (1991) Arch Virol, 121, pp. 219-225; Otake, T., Schols, M., Witvouw, L., Naesens, L., Nakashima, H., Moriya, T., Kurita, H., De Clercq, E., Modified cyclodextrin sulphates (mCDS11) have potent inhibitory activity against HIV and high oral bioavailability (1994) Antivir Chem Chemother, 5, pp. 155-161; Pari, G.S., Kirkfield, A., Smith, J., Potent antiviral activity of an antisense oligonucleotide complementary to the intron-exon boundary of human cytomegalovirus genes UL 36 and UL 37 (1995) Antimicrob Agents Chemother, 39, pp. 1157-1161; Phillips, N.C., Emili, A., Immunogenicity of immunoliposomes (1991) Immunol Lett, 30, pp. 291-296; Potgieter, L.N.D., McCrachen, M.D., Hopkins, F.M., Walker, R.D., Guy, J.S., Experimental production of bovine respiratory tract disease with bovine diarrhea virus (1984) Am J Vet Res, 45, pp. 1582-1585; Sands, H., Gorey-Feret, L.J., Cocuzza, A.J., Hobbs, F.W., Chidester, D., Trainor, G.L., Biodistribution and metabolism of internally 3H-labelled oligonucleotides. Comparison of a phosphodiester and phosphorothioate (1994) Mol Pharmacol, 45, pp. 932-943; Savoysky, E., Boireau, P., Finance, C., Laporte, J., Sequence and analysis of BECV F15 matrix protein (1990) Res Virol, 141, pp. 411-425; Sawiki, S.G., Sawiki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J Virol, 64, pp. 1050-1056; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNA contain anti-leaders (1991) J Virol, 65, pp. 320-325; Shien, C.K., Soe, L.H., Makino, S., Chang, M.F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genome implications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Simpkins, J.W., Solubilization of ovine growth hormone with 2-hydroxypropyl-β-cyclodextrin (1991) J Parent Sci Technol, 45, pp. 266-269; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronavirus: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Stein, C.A., Matsukura, M., Subasinghe, C., Broder, S., Cohen, J.S., Phosphorothioate oligodeoxynucleotides are potent sequence non-specific inhibitors of de novo infection by HIV (1989) Aids Res Hum Retroviruses, 5, pp. 639-645; Stein, C.A., Does antisense exist? (1995) Nature Med, 1, pp. 1119-1121; Stein, C.A., Phosphorothioate antisense oligodeoxynucleotides: Questions of specificity (1996) Trends Biotechnol, 14, pp. 147-149; Stern, D.F., Kennedy, S.I.T., Coronavirus multiplication strategy. II. Mapping the avian infectious bronchitis virus intracellular RNA species to the genome (1980) J Virol, 36, pp. 440-449; Stewart, A.J., Canitrot, Y., Barrachini, E., Dean, N.N., Daly, R.G., Cole, S.P.C., Reduction of expression of the multidrug resistance protein (MRP) in human tumor cells by antisense phosphorothioate oligonucleotides (1996) Biochem Pharmacol, 51, pp. 461-469; Sturman, L.S., Holmes, K., The molecular biology of coronaviruses (1983) Adv Virus Res, 28, pp. 35-112; Temsamani, J., Tang, J.Y., Padimapriya, A., Kubert, M., Agrawal, S., Pharmacokinetics, biodistribution and stability of capped oligodeoxynucleotide phosphorothioates in mice (1993) Antisense Res Dev, 3, pp. 277-284; Tonkinson, J.L., Stein, C.A., Antisense nucleic-acids. Prospects for antiviral intervention (1993) Antivir Chem Chemother, 4, pp. 193-200; Vautherot, J.F., Plaque assay for titration of bovine enteric coronavirus (1981) J Gen Virol, 56, pp. 451-455; Vlassov, V.V., Balakireva, L.A., Yakubov, L.A., Transport of oligonucleotides across natural and model membranes (1994) Biochem Biophys Acta, 1197, pp. 95-108; Weiner, D.B., Williams, W.V., Weisz, P.B., Greene, M.I., Synthetic cyclodextrin derivatives inhibit HIV infection in vitro (1992) Pathobiology, 60, pp. 206-212; Wenz, G., Cyclodextrin as building blocks for supramolecular structures and functional units (1994) Angew Chem Int Edit, 33, pp. 803-822; Zhao, Q., Temsamani, J., Agrawal, S., Use of cyclodextrins and its derivatives as carriers for oligonucleotide delivery (1995) Antisense Res Dev, 5, pp. 185-192","Finance, C.; GEVSM, EA 1123, Univ. H. Poincare, Faculte de Pharmacie, B.P. 403, F-54001 Nancy Cedex, France",,,03048608,,ARVID,"9672621","English","ARCH. VIROL.",Article,"Final",Open Access,Scopus,2-s2.0-0030849802
"González P., Sánches A., Rivera P., Jiménez C., Hernández F.","7202330734;6602527043;14632286800;57210402191;57197480243;","Rotavirus and coronavirus outbreak: Etiology of annual diarrhea in Costa Rican children",1997,"Revista de Biologia Tropical","45","3",,"989","991",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031216855&partnerID=40&md5=2671b3b2b4e3c1ae68aa1053640c8869","Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica; Servicio de Patología, Hospital Nacional de Niños, San José, Costa Rica; Prog. Invest. en Enferm. Tropicales, Escuela de Medicina Veterinaria, Universidad Nacional, Heredia, Costa Rica","González, P.; Sánches, A., Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica; Rivera, P., Servicio de Patología, Hospital Nacional de Niños, San José, Costa Rica; Jiménez, C., Prog. Invest. en Enferm. Tropicales, Escuela de Medicina Veterinaria, Universidad Nacional, Heredia, Costa Rica; Hernández, F., Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica","In Costa Rica, an annual outbreak of infant diarrheal disease (December and January) was reported since 1976, and rotavirus was incriminated later as the main etiological agent (1976-1981). Apparently the disease has not been systematically studied in Costa Rica after 1981. For that reason the occurence of the outbreak was retrospectively documented for 1993-1995 and etiology was studied in 48 children treated for diarrhea at the Nacional Children Hospital (capital city of San Jose) during December, 1994 and January, 1995. Rotavirus (33%) and coronavirus (27%) were the main agents. To our knowledge, this is the first time that these viruses are incriminated in an outbreak of diarrhea.","Coronavirus; Diarrhea; Diarrheal disease outbreak; Rotavirus","article; child; Costa Rica; epidemic; human; infant; infantile diarrhea; prevalence; retrospective study; virology; virus infection; Child; Coronavirus Infections; Costa Rica; Diarrhea, Infantile; Disease Outbreaks; Humans; Infant; Prevalence; Retrospective Studies; Rotavirus Infections","Bishop, R.F.G.P.D., Holmes, I.H., Ruck, B.J., Virus particles in epithelial cells of duodenal mucosa from children with acute non-bacterial gastroentiritis (1973) Lancet, 2, pp. 1228-1283; Christensen, M.L., Human viral gastroenteritis (1989) Clin. Microbiol. Rev., 2, pp. 51-89; Flewett, T.H.A.S.B., Davis, H., Virus particles in gastroenteritis (1973) Lancet, 2, p. 1497; Germa, G.N.P., Cereda, P.M., Battaglia, M., Antigenic relatedness of human enteric coronavirus strains to human coronavirus OC43: A preliminary report (1985) J. Infect. Dis., 150, pp. 618-619; Jiménez, C., (1990) Vergleichende Labordianostische Untersuechungen Von Kotproben (EM. Virusisolierung, Immunologische Verfahren) Zum Nachweis Einer Bovine Coronavirus Infection Bei Durchfallkranken Kalberm Vet. Med. Diss, 170p. , Justus-Liebig- Universitat, Giessen, Germany; Hernández, F.L.M., Lizano, C., Mohs, E., Prevalencia de rotavirus y descripción de una epidemiade diarrea por ese agente en Costa Rica (1977) Acta Méd. Cost., 20, pp. 297-304; Hernández, F.L.M., Villalobos, V.H., Análisis electroforético del ácido ribonucleico de rotavirus de Costa Rica: Implicaciones epidemiológicas Rev (1980) Hosp. Nal. Niños, 15, pp. 21-30; Hernández, F.R.M.A., Oviedo, M.T., Epizotiología de las diarreas bovinas en Costa Rica (1987) Rev. Latinoamer. Microbiol., 29, pp. 113-117; Mata, L.C.L., Hernández, F., Mohs, E., Herrero, L., Peñaranda, M.E., Gamboa, F., León, J., Agentes infecciosos en la diarrea del niño hospitalizado (1977) Bol. Méd. Hosp. Infant., 34, pp. 955-969; Mata, L.A.S., Padilla, R., Gamboa, M.M., Vargas, G., Hernández, F., Mohs, E., Lizano, C., Diarrhea associated with rotaviruses, enterotoxigenic Escherichia coli, Campylobacter, and other agents in Costa Rican children, 1976-1981 (1983) Am. J. Trop. Med. Hyg., 32, pp. 146-153; Mortesen, M.L.C.G.R., Payne, C.M., Friedman, A.D., Minnich, L.L., Rousseau, C., Coronaviruslike particles in human gastrointestinal disease (1985) Am. J. Dis. Child., 139, pp. 928-934; Odio, C.F.H., Ruiz, M.A., Padilla, R., Mohs, E., Rotavirus en un servicio de neonatología. Descripción de una epidemia (1980) Rev. Hosp. Nal. Niños, 15, pp. 159-172; Simhon, A.S.A., Hernández, F., Yolken, R.H., Mata, L., Diagnóstico de rotavirus por microscopia electrónica y el ensayo inmunosorbente enzima conjugada (ELISA) (1979) Bol.Of.Sanit.Panam., 86, pp. 391-397; Zheng, B.J.R.X.C., Ma, G.Z., Xie, J.M., Liu, Q., Liang, X.R., Ng, M.H., Rotavirus infections of the orophariynx and respiratory tract in young children (1991) J. Med. Virol., 34, pp. 29-37","Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica",,,00347744,,,"9611302","English","Rev. Biol. Trop.",Article,"Final",,Scopus,2-s2.0-0031216855
"Paton D., Lowings P.","7103157927;6603497710;","Discrimination between transmissible gastroenteritis virus isolates brief report: Brief Report",1997,"Archives of Virology","142","8",,"1703","1711",,7,"10.1007/s007050050191","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030750659&doi=10.1007%2fs007050050191&partnerID=40&md5=accebe06b4c1ed2e1248b2a7f1bb3966","Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey, United Kingdom; Central Veterinary Laboratory, Woodham Lane, Addlestone, Surrey KT15 3NB, United Kingdom","Paton, D., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey, United Kingdom, Central Veterinary Laboratory, Woodham Lane, Addlestone, Surrey KT15 3NB, United Kingdom; Lowings, P., Virology Department, Central Veterinary Laboratory, Veterinary Laboratories Agency, Addlestone, Surrey, United Kingdom","Twenty TGEV isolates were compared by sequencing a 393-414 nucleotide stretch near the 5' end of the S gene, after amplification by RT-PCR. This part of the S gene is known to show considerable variation between porcine, canine and feline coronaviruses and is completely deleted from porcine respiratory coronaviruses. The discrimination achieved by nucleotide sequence analysis was compared with that obtained by monoclonal antibody typing. The viruses could be split into several clusters, and recent isolates of TGEV from England, The Netherlands and Belgium showed the greatest differences compared to earlier reference types. However, not all viruses with unique isolation histories were distinct, suggesting either genetic stability over many years, laboratory cross-contaminations or repeated introductions of similar viruses into the field. Firm conclusions on evolutionary trends cannot be drawn without obtaining a larger number of isolates, preferably from outbreaks with known epidemiological links. The sequences of some field isolates from the 1980s contained both nucleotide deletions and insertions. The latter included a short sequence of fourteen nucleotides with identity to a region of the TGEV polymerase gene.",,"article; classification; genetics; molecular genetics; nucleotide sequence; phylogeny; sequence alignment; sequence homology; serotyping; Transmissible gastroenteritis virus; virus gene; Base Sequence; Genes, Viral; Molecular Sequence Data; Phylogeny; Sequence Alignment; Sequence Homology, Nucleic Acid; Serotyping; Transmissible gastroenteritis virus; Felidae; Suidae; Transmissible gastroenteritis virus","Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res, 18, pp. 71-80; Chen, C.-M., Cavanagh, D., Britton, P., Cloning and sequencing of a 8.4-kb region from the 3′-end of a Taiwanese virulent isolate of the coronavirus transmissible gastroenteritis virus (1995) Virus Res, 38, pp. 83-89; Correa, I.G., Jimenez, C., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res, 10, pp. 77-94; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Res, 12, pp. 387-395; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Felsenstein, J., PHYLIP: Phylogenetic inference package (version 3.2) (1989) Cladistics, 5, pp. 164-166; Garwes, D.J., Stewart, F., Elleman, C.J., Identification of epitopes of immunological importance on the peplomer of procine transmissible gastroenteritis virus (1987) Adv Exp Med Biol, 218, pp. 509-515; Garwes, D.J., Stewart, F., Cartwright, S.F., Brown, I., Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet Rec, 122, pp. 86-87; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sanchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Holm Jensen, M., Detection of antibodies against hog cholera virus and bovine viral diarrhoea virus in procine serum. A comparative examination using CF, PLA and NPLA assays (1981) Acta Vet Scand, 22, pp. 85-98; Jimenez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J Virol, 60, pp. 131-139; Jones, T.O., Paton, D.J., Classical transmissible gastroenteritis returns (1996) Vet Rec, 138, pp. 166-167; Lai, M.M., Genetic recombination in RNA viruses (1992) Curr Top Microbiol Immunol, 176, pp. 21-32; Laude, H., Van Reeth, K., Pensaert, M., Procine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Paton, D., Ibata, G., Sands, J., McGoldrick, A., Detection of transmissible gastroenteritis virus by RT-PCR and differentiation from porcine respiratory coronavirus (1997) J Virol Methods, , in press; Sanchez, C.M., Gebauer, F., Suñé, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virology, 190, pp. 92-105; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine. 7th Ed., pp. 362-386. , Leman AD, Straw BE, Mengeling WL, Allaire D'S, Taylor DJ (ed), Iowa State University Press, Ames; Stallcup, M.R., Washington, L.D., Region-specific initiation of mouse mammary tumour virus RNA synthesis by endogenous RNA polymerase II in preparations of cell nuclei (1983) J Biol Chem, 258, pp. 2802-2807; Van Nieuwstadt, A.P., Boonstra, J., Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus, using monoclonal antibodies to antigenic sites a and X of the S glycoprotein (1992) Am J Vet Res, 53, pp. 184-190","Paton, D.; Central Veterinary Laboratory, Woodham Lane, Addlestone, Surrey KT15 3NB, United Kingdom",,,03048608,,ARVID,"9672630","English","ARCH. VIROL.",Article,"Final",,Scopus,2-s2.0-0030750659
"McReynolds C., Macy D.","36939415700;7004037423;","Feline infectious peritonitis. Part I. Etiology and diagnosis",1997,"Compendium on Continuing Education for the Practicing Veterinarian","19","9",,"1007","1016",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042903881&partnerID=40&md5=d73e12c19201e43c9a0112a1cbeadc78","Colorado State University, United States; Department of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO, United States; Amer. Coll. of Vet. Int. Medicine, United States","McReynolds, C., Colorado State University, United States, Department of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO, United States; Macy, D., Colorado State University, United States, Department of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO, United States, Amer. Coll. of Vet. Int. Medicine, United States","Feline infectious peritonitis (FIP) is a generally lethal disease of domestic and wild felines. It occurs when an enteritis-producing strain of feline coronavirus (FoCV) mutates and develops the ability to replicate inside macrophages. If the cat fails to mount a cell-mediated immune response, complement-mediated vasculitis leads to serosal cavity effusions or pyogranulomatous foci in multiple organs. Both the virulence of the viral strain and the ability of the cat to mount a cell-mediated response dictate whether the cat will clear the infection or FIP will occur. Most cases occur in cats between 3 months and 3 years of age. Cats in multicat households are at high risk for several reasons. The disease rarely strikes cats from one- or two-cat households. The antemortem diagnosis of FIP is presumptive and is based on a group of findings that individually have little predictive significance. Cats with FCoV antibody do not necessarily have FIP, but cats without FCoV antibody probably do not have FIP. The presumptive diagnosis is based on a triad of laboratory findings in a cat with suggestive clinical signs: lymphopenia (&lt; 1.5 × 10 3 cells/μl), FCoV antibody titer (≥1:160), and hyperglobulinemia (&gt; 5.1 g/dl). The gold standard for antemortem diagnosis is histopathologic examination of biopsy specimens. Laboratory analysis of a sample of exudate can also help confirm or rule out the diagnosis. Part II of this two-part presentation will discuss treatment and prevention of FIP.",,"Coronavirus; Felidae; Feline coronavirus; Felis catus","Holzworth, J., Some important disorders of cats (1973) Cornell Vet, 53, pp. 157-160; Fowler, M.E., Felidae (1986) Zoo and Wildlife Medicine, Ed 2, pp. 831-841. , Fowler ME (ed): Philadelphia, WB Saunders Co; Ward, J.M., Morphogenesis of a virus in cats with experimental feline infectious peritonitis (1970) Virology, 41, pp. 191-194; Pedersen, N.C., Boyle, J.F., Floyd, K., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am J Vet Res, 42, pp. 368-373; Horzinek, M.C., Lutz, H., Pederson, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect Immun, 37, pp. 148-154; McArdle, F., Bennett, M., Gaskell, R.M., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am J Vet Res, 53, pp. 1500-1506; Hohdatsu, T., Okada, S., Ishizuka, Y., The prevalence of types I and II feline coronavirus infection in cats (1992) J Vet Med Sci, 54, pp. 557-562; Vennema, H., Poland, A., Hawkins, K.F., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23 (3), pp. 40-45; Poland, A.M., Vennema, H., Foley, J.E., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with feline enteric coronavirus (1996) J Clin Microbiol, 34, pp. 3180-3184; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Compend Contin Educ Pract Vet, 7 (12), pp. 1001-1010; Laude, H., Van, R.K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab Anim Sci, 43, pp. 15-28; Addie, D.D., Toth, S., Murray, G.D., Risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) Am J Vet Res, 56, pp. 429-434; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23 (3), pp. 7-20; Reeves, N., Vaccination against naturally occurring FIP in a single large cat shelter (1995) Feline Pract, 23 (3), pp. 81-82; Kass, P.H., Dent, T.H., The epidemiology of feline infectious peritonitis in catteries (1995) Feline Pract, 23 (3), pp. 27-33; Scott, F.W., Update on FIP (1988) Proc Kal Kan Symp, 12, pp. 43-47; McKiernan, A.J., Evermann, J.F., Hargis, A., Isolation of feline coronaviruses from two cats with diverse disease manifestations (1981) Feline Pract, 11 (3), pp. 16-20; Foley, J.E., Pedersen, N.C., The inheritance susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Pract, 24 (1), pp. 14-22; Pederson, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am J Vet Res, 41, pp. 363-367; Fehr, D., Holznagel, E., Bolla, S., Evaluation of the safety and efficacy of a modified live FIPV vaccine under field conditions (1995) Feline Pract, 23 (3), pp. 83-88; Pedersen, N.C., Feline infectious peritonitis: Something old, something new (1976) Feline Pract, 6 (3), pp. 42-51; Lutz, H., Fehr, D., Risk factors for FIP in natural exposure, epidemiology and natural occurrence patterns, clues in the real world of catteries (1995) Proc Feline Infect Dis Symp, pp. 43-46; Kline, K.L., Joseph, R.J., Averill, D.R., Feline infectious peritonitis with neurologic involvement: Clinical and pathological findings in 24 cats (1994) JAAHA, 30, pp. 111-118; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) JAVMA, 209, pp. 1117-1120; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., An appraisal of the value of laboratory tests in the diagnosis of feline infectious peritonitis (1994) JAAHA, 30, pp. 345-350; Herrewegh, A.A.P.M., Egberink, H.F., Horzinek, M.C., Polymerase chain reaction (PCR) for the diagnosis of naturally occurring feline coronavirus infections (1995) Feline Pract, 23 (3), pp. 56-61; Shelly, S., Scarlett-Kranz, J., Blue, J., Protein electrophoresis on effusions from cats as a diagnostic test for feline infectious peritonitis (1988) JAAHA, 24, pp. 495-501","McReynolds, C.; Department of Clinical Sciences, Coll. of Vet. Med. and Biomed. Sci., Colorado State University, Fort Collins, CO, United States",,,01931903,,,,"English","Compend. Contin. Educ. Pract. Vet.",Review,"Final",,Scopus,2-s2.0-3042903881
"Zimmer K., Zimmermann Th., Heß R.G.","7101896015;7103341490;57197694325;","Causes of death in swine [Todesursachen bei schweinen]",1997,"Praktische Tierarzt","78","9",,"772","780",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342325266&partnerID=40&md5=05d94ad2393d397caf8e8ed5aca1f618","Landesveterinäruntersuchungsamt Rheinland-Pfalz, Koblenz, Germany; Landesveterinäruntersuchungsamt Rheinland-Pfalz, Blücherstr. 34, 56073 Koblenz, Germany","Zimmer, K., Landesveterinäruntersuchungsamt Rheinland-Pfalz, Koblenz, Germany, Landesveterinäruntersuchungsamt Rheinland-Pfalz, Blücherstr. 34, 56073 Koblenz, Germany; Zimmermann, Th., Landesveterinäruntersuchungsamt Rheinland-Pfalz, Koblenz, Germany; Heß, R.G., Landesveterinäruntersuchungsamt Rheinland-Pfalz, Koblenz, Germany","The present study is based upon post mortem findings on 4663 pigs at the Federal State Veterinary Investigation Centre of Rhineland-Palatinate from 1980 to 1995. The decline of farms (-76.5 %) and swine (-42.9 %) in the province does not correlate with the number of animals annually investigated. 55.6 per cent of the swine under investigation were suckling piglets. Aujeszky's disease was found in 5.6 per cent of the swine, suckling piglets (8.9 %) being most often affected. Swine fever was proven in 2.9 per cent of the animals; weaners (7.8 %), breeding (7.4 %) and fattening pigs (7.3 %) being predominantly affected. 29.4 per cent of the fattening and 21.6 per cent of the breeding pigs were found to have cardiovascular disorders. 75.0 per cent of the diseases of the respiratory system were found to be pneumonias caused by bacteria, predominantly Pasteurella (29.5 %), Mycoplasma (23.1 %) and Streptococcus (11.6 %) species. Weaners (33.1 %) were most often affected. 71.0 per cent of the diseases of the alimentary system were enteritis induced by bacteria, 91.5 per cent of which were due to Escherichia coli-infection. From 1991 to 1995 colonization factor antigens (predominantly F4- and F41-antigen) were detected in 27.2 per cent of the Eschericha coli-strains isolated from piglets with enteritis. Salmonella species were found in 2.4 per cent of the animals, fattening pigs (7.3 %) being most often affected. Viral infections, predominantly coronaviruses, were detected by electron microscopic investigation in 12.7 per cent of piglets with enteritis from 1992 to 1995. Diseases of the alimentary system were most often encountered in weaned (59.3 %) and suckling (49.9 %) piglets. (Poly-)Serositis was most often found in suckling piglets (8.9 %). Diseases of the urinary and reproductive system were most often encountered in breeding pigs (16.5 %). No cause of death was found in 6.7 per cent of the animals under investigation. © Schlütersche GmbH & Co. KG, Verlag und Druckerei.","Causes of death; Swine",,"Appel, G., Schütte, A., Untersuchungsergebnisse der diagnostischen Pathologie (1990) Prakt. Tierarzt, 71, pp. 22-34; Bergmann, V., Das Verhalten der Schweinekrankheiten in den Jahren 1959-1964 nach den Sektionsergebnissen (1965) Monatsh. Veterinärmed., 20, pp. 882-889; Dyck, G.W., Swierstra, E.E., Causes of piglet death from birth to weaning (1987) Can. J. Anim. Sci., 76, pp. 543-547; Häni, H., Luginbühl, H., König, H., Brändli, A., Vorkommen und Bedeutung von Schweinekrankheiten: Analyse eines Sektionsgutes (1971-1973). I. Einleitung, Literatur, Material, Methoden, Problematik (1975) Schweiz. Arch. Tierheilk., 117, pp. 517-528; Häni, H., Brändli, A., Luginbühl, H., König, H., Vorkommen und Bedeutung von Schweinekrankheiten: Analyse eines Sektionsgutes (1971-1973). II. Krankheits- und Todesursachen in verschienenen Altersgruppen (1976) Schweiz. Arch. Tierheilk., 118, pp. 1-11; Hellmers, B., (1986) Todesursachen bei Schweinen. Auswertung der im Tiergesundheitsamt der Landwirtschaftskammer Hannover Erhobenen Sektionsbefunde der Jahre 1976-1985, , Vet. med. Diss. Hannover; Ikes, D., (1976) Auswertung der von 1959-1975 im Tiergesundheitsamt der Landwirtschaftskammer Hannover bei Schweinen Erhobenen Sektionsbefunde, , Vet. med. Diss. Hannover; Nielsen, N.C., Christensen, K., Bille, N., Larsen, I.L., Preweaning Mortality in Pigs. I. Herd Investigations (1974) Nord. Vet. Med., 26, pp. 138-150; Rolle, M., Mayr, A., (1993) Medizinische Mikrobiologie, Infektions- und Seuchenlehre, , Ferdinand Enke Verlag Stuttgart; STATISTISCHES LANDESAMT RHEINLAND-PFALZ: Viehzählung 1980; STATISTISCHES LANDESAMT RHEINLAND-PFALZ: Viehzählung 1995; TIERSEUCHENBERICHTE des BMELF 1980-1995; Zimmermann, T.H., (1994) Todesursachen bei Schweinen. Auswertung der Am Landesveterinäruntersuchungsamt Rheinland-Pfalz Erhobenen Untersuchungsbefunde der Jahre 1980 Bis 1991, , Vet. med. Diss. Hannover","Zimmer, K.; Landesveterinäruntersuchungsamt Rheinland-Pfalz, Blücherstr. 34, 56073 Koblenz, Germany",,,0032681X,,,,"German","Prakt. Tierarzt",Article,"Final",,Scopus,2-s2.0-0342325266
"Hsue B., Masters P.S.","7801347035;7006234572;","A bulged stem-loop structure in the 3' untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication",1997,"Journal of Virology","71","10",,"7567","7578",,75,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030768788&partnerID=40&md5=5a6149312cab80cfac2dbc406a3ecaac","Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Wadworth Ctr. for Labs. and Research, New York State Department of Health, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Hsue, B., Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Masters, P.S., Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States, Wadworth Ctr. for Labs. and Research, New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","The 3' untranslated region (UTR) of the positive-sense RNA genome of the coronavirus mouse hepatitis virus (MHV) contains sequences that are necessary for the synthesis of negative-strand vital RNA as well as sequences that may be crucial for both genomic and subgenomic positive-strand RNA synthesis. We have found that the entire 3' UTR of MHV could be replaced by the 3' UTR of bovine coronavirus (BCV), which diverges overall by 31% in nucleotide sequence. This exchange between two viruses that are separated by a species barrier was carried out by targeted RNA recombination. Our results define regions of the two 3' UTRs that are functionally equivalent despite having substantial sequence substitutions, deletions, or insertions with respect to each other. More significantly, our attempts to generate an unallowed substitution of a particular portion of the BCV 3' UTR for the corresponding region of the MHV 3' UTR led to the discovery of a bulged stem-loop RNA secondary structure, adjacent to the stop codon of the nucleocapsid gene, that is essential for MHV viral RNA replication.",,"amino acid substitution; article; coronavirus; deletion mutant; genetic recombination; hepatitis virus; nonhuman; nucleotide sequence; priority journal; protein secondary structure; rna sequence; rna translation; virus genome; virus replication; virus transcription; Animals; Base Composition; Base Sequence; Cattle; Coronavirus, Bovine; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Nucleic Acid Conformation; Recombination, Genetic; Restriction Mapping; RNA, Viral; Transcription, Genetic; Virus Replication","Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Cruciere, C., Laporte, J., Sequence and analysis of bovine enteritic coronavirus (F15) genome. I. Sequence of the gene coding for the nucleocapsid protein: Analysis of the predicted protein (1988) Ann. Inst. Pasteur Virol., 139, pp. 123-138; De Groot, R.J., Van der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased hy nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5898-5905; Fichot, O., Girard, M., An improved method for sequencing of RNA templates (1990) Nucleic Acids Res., 18, p. 6162; Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; (1996) Program Manual for the Wisconsin Package. Version 9.0, , Genetics Computer Group, Madison, Wis; Haenni, A.-L., Joshi, S., Chapeville, F., TRNA-like structures in the genomes of RNA viruses (1982) Prog. Nucleic Acid Res. Mol. Biol., 27, pp. 85-104; Hofmann, M.A., Brian, D.A., The 5′ end of coronavirus minusstrand RNAs contains a short poly(U) tract (1991) J. Virol., 65, pp. 6331-6333; Hofmann, M.A., Senanayake, S.D., Brian, D.A., A translation-attenuating intraleader open reading frame is selected on coronavirus mRNAs during persistent infection (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 11733-11737; Jacobson, S.J., Konings, D.A.M., Sarnow, P., Biochemical and genetic evidence for a pseudoknot structure at the 3′ terminus of the polio-virus RNA genome and its role in viral RNA amplification (1993) J. Virol., 67, pp. 2961-2971; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res, 12, pp. 1-9; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.-N., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Kingsman, S.M., Samuel, C.E., Mechanism of interferon action. Interferon-mcdiated inhibition of simian virus-40 early RNA accumulation (1980) Virology, 101, pp. 458-465; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.-J., Liao, C.-L., Lai, M.M.C., Identification of the cu-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Lin, Y.-J., Zhang, X., Wu, R.-C., Lai, M.M.C., The 3′ untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA (1996) J. Virol., 70, pp. 7236-7240; Liu, Q., Yu, W., Leibowitz, J.L., A specific host cellular protein binding element near the 3′ end of mouse hepatitis virus genomic RNA (1997) Virology, 232, pp. 74-85; Luytjes, W., Gerritsma, H., Spaan, W.J.M., Replication of synthetic interfering RNAs derived from coronavirus mouse hepatitis virus-A59 (1996) Virology, 216, pp. 174-183; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol., 54, pp. 329-336; Makino, S., Shieh, C.-K., Keck, J.G., Lai, M.M.C., Defective interfering particles of murine coronavirus: Mechanism of synthesis of defectivc viral RNAs (1988) Virology, 163, pp. 104-111; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, p. 495507; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revenants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Penzes, Z., Tibbies, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: a Laboratory Manual. 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shi, P.-Y., Brinton, M.A., Veal, J.M., Zhong, Y.Y., Wilson, W.D., Evidence for the existence of a pseudoknot structure at the 3′ terminus of the flavivirus genomic RNA (1996) Biochemistry, 35, pp. 4222-4230; Siddell, S.G., The Coronaviridae: An introduction p (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Stemmer, W.P.C., Rapid evolution of a protein in vitro by DNA shuffling (1994) Nature, 370, pp. 389-391; Stemmer, W.P.C., DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 10747-10751; Todd, S., Semler, B.L., Structure-infectivity analysis of the human rhinovirus genomic RNA 3′ non-coding region (1996) Nucleic Acids Res., 24, pp. 2133-2142; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Van der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Weiner, A.M., Maizels, N., TRNA-like structures tag the 3′ ends of genomic RNA molecules for replication: Implications for the origin of protein synthesis (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 7383-7387; Williams, G.D., Chang, R.-Y., Brian, D.A., Evidence for a pseudoknot in the 3′ untranslated region of the bovine coronavirus genome: Corona and related viruses (1995) Adv. Exp. Med. Biol., 380, pp. 511-514; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′ end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Yu, W., Leibowitz, J.L., A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology, 214, pp. 128-138","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States",,,0022538X,,JOVIA,"9311837","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030768788
"Sethna P.B., Brian D.A.","7003358474;7006460232;","Coronavirus genomic and subgenomic minus-strand rnas copartition in membrane-protected replication complexes",1997,"Journal of Virology","71","10",,"7744","7749",,32,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030866422&partnerID=40&md5=2b02a97ad3ae83d0198c55ab084b8dbd","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Glaxo Wellcome Inc., Research Triangle Park, NC 27709, United States","Sethna, P.B., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Glaxo Wellcome Inc., Research Triangle Park, NC 27709, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","The majority of porcine transmissible gastroenteritis coronavirus plus- strand RNAs (genome and sub-genomic mRNAs), at the time of peak RNA synthesis (5 h postinfection), were not found in membrane-protected complexes in lysates of cells prepared by Dounce homogenization but were found to be susceptible to micrococcal nuclease (85%) or to sediment to a pellet in a cesium chloride gradient (61%). They therefore are probably free molecules in solution or components of easily dissociable complexes. By contrast, the majority of minus-strand RNAs (genome length and subgenomic mRNA length) were found to be resistant to micrococcal nuclease (69%) or to remain suspended in association with membrane-protected complexes following isopycnic sedimentation in a cesium chloride gradient (85%). Furthermore, 35% of the suspended minus strands were in a dense complex (1.20 to 1.24 g/ml) that contained an RNA plus-to-minus-strand molar ratio of approximately 8:1 and viral structural proteins S, M, and N, and 65% were in a light complex (1.15 to 1.17 g/ml) that contained nearly equimolar amounts of plus- and minus- strand RNAs and only trace amounts of proteins M and N. In no instance during fractionation were genome-length minus strands found segregated from sub- genome-length minus strands. These results indicate that all minus-strand species are components of similarly structured membrane-associated replication complexes and support the concept that all are active in the synthesis of plus-strand RNAs.",,"messenger rna; virus rna; article; coronavirus; nonhuman; priority journal; protein analysis; rna analysis; rna structure; viral genetics; virus genome; virus replication; Animals; Cell Fractionation; Cells, Cultured; Centrifugation, Density Gradient; Genome, Viral; Male; RNA, Viral; RNA-Directed DNA Polymerase; Swine; Testis; Transmissible gastroenteritis virus; Viral Structural Proteins; Virus Replication","Barton, D.J., Flanegan, J.B., Coupled translation and replication of poliovirus RNA in vitro: Synthesis of functional 3D polymerase and infectious virus (1993) J. Virol., 67, pp. 822-831; Barton, D.J., Sawieki, S.G., Sawicki, D.L., Solubilization and immunoprecipitation of alphavirus replication complexes (1991) J. Virol., 65, pp. 1496-1506; Bi, W., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., Intracellular localization of polypeptides encoded in mouse hepatitis virus open reading frame 1A (1995) Adv. Exp. Med. Biol., 380, pp. 251-258; Bienz, K., Egger, D., Pfister, T., Troxler, M., Structural and functional characterization of the poliovirus replication complex (1992) J. Virol., 66, pp. 2740-2747; Brayton, P.R., Stohlman, S.A., Lai, M.M.C., Further characterization of mouse hepatitis virus RNA-depcndcnt RNA polymerase (1984) Virology, 133, pp. 197-201; Brian, D.A., Dennis, D.E., Guy, J.S., Genome of porcine trans missible gastroenteritis virus (1980) J. Virol., 34, pp. 410-415; Brian, D.A., Chang, R.-Y., Sethna, P.B., Hofmann, M.A., Role of subgenomic minus-strand RNA in coronavirus replication (1994) Arch. Virol. Suppl., 9, pp. 173-180; Chang, R.-Y., Brian, D.A., Cis requirement for N-specitic protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Chang, R.-Y., Krishnan, R., Brian, D.A., The UCUAAAC Promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. Virol., 70, pp. 2720-2729; David-Kerriera, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) J. Cell Biol., 24, pp. 57-78; Dennis, D.E., Brian, D.A., RNA-dependent RNA polymerase activity in coronavirus-infected cells (1982) J. Virol., 42, pp. 153-164; Dubois-Dakcq, M., Holmes, K.V., Rentier, B., Assembly of coronaviruses (1984) Assembly of Enveloped RNA Viruses, pp. 100-117. , D. W. Kingsbury (ed.), Springer-Verlag, New York, N.Y; Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes (1988) J. Cell Biol., 107, pp. 2075-2086; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Hofmann, M.A., Brian, D.A., The 5-prime end of coronavirus minus-strand RNAs contains a short poly(U) tract (1991) J. Virol., 65, pp. 6331-6333; Hofmann, M.A., Sethna, P.B., Brian, D.A., Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture (1990) J. Virol., 64, pp. 4108-4114; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Kapke, P.A., Tung, F.Y.T., Hogue, B.G., Brian, D.A., Woods, R.D., Wesley, R., The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation (1988) Virology, 165, pp. 367-376; Lai, M.M.C., Coronavirus: Organization, replication, and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Mahy, B.W.J., Siddell, S., Wege, H., Ter Meulen, V., RNA-dependent RNA polymerase activity in murine coronavirus-infected cells (1983) J. Gen. Virol., 64, pp. 103-111; Miller, W.A., Hall, T.C., Use of micrococcal nuclease in the purification of highly template dependent RNA-dependent RNA polymerase from brome mosaic virus-infected barley (1983) Virology, 125, pp. 236-241; Moreau, K., Brian, D., Unpublished data; Morimoto, T., Arpin, M., Gaetani, S., Use of proteases for the study of membrane insertion (1983) Methods Enzymol., 96, pp. 121-150; Naito, S., Ishihama, A., Function and structure of RNA polymerase of vesicular stomatitis virus (1976) J. Biol. Chem., 251, pp. 4307-4314; Parvin, J.D., Palese, P., Honda, A., Ishihama, A., Krystal, M., Promoter analysis of influenza virus RNA polymerase (1989) J. Virol., 63, pp. 5142-5152; Penman, S., Greenberg, H., Willems, M., Preparation of polyribosomes from cells grown in tissue culture (1968) Fundamental Techniques in Virology, pp. 49-58. , K. Habel and N. P. Salzman (ed.), Academic Press, New York, N.Y; Pons, M.W., Schulze, I.T., Hirst, G.K., Hauser, R., Isolation and characterization of the ribonucleoprotein of influenza virus (1969) Virology, 39, pp. 250-259; Raju, R., Raju, L., Hacker, D., Garcin, D., Compans, R., Kolakofsky, D., Nontemplated bases at the 5′ ends of Tacaribe virus mRNAs (1990) Virology, 174, pp. 53-59; Sachs, A.B., Lenchitz, B., Noble, R.L., Hess, G.P., A convenient large-scale method for the isolation of membrane vesicles permeable to a specific inorganic ion: Isolation and characterization of functional acetylcholine receptor-containing vesicles from the electric organ of Electrophorus electricus (1982) Anal. Biochem., 124, pp. 185-190; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., Coronavirus use discontinuous extension for synthesis of subgenome-length negative strands (1995) Adv. Exp. Med. Biol., 380, pp. 499-506; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating Coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNA and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 25-112; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of Coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.-L., Sethna, P.B., Hogue, B.G., Brian, D.A., The 9.1 kilodalton protein hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane associated (1992) Virology, 186, pp. 676-683; Wu, S.-X., Ahlquist, P., Kaesberg, P., Active complete in vitro replication of nodavirus RNA requires glycerophosphofipid (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 11136-11140; Wu, S.-X., Kaesberg, P., Synthesis of template-sense, single-strand flockhouse virus RNA in a cell-free replication system (1991) Virology, 183, pp. 392-396","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,,0022538X,,JOVIA,"9311859","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030866422
"Pewe L., Xue S., Perlman S.","6603143496;7202791284;7102708317;","Cytotoxic T-cell-resistant variants arise at early times after infection in C57BL/6 but not in SCID mice infected with a neurotropic coronavirus",1997,"Journal of Virology","71","10",,"7640","7647",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030768760&partnerID=40&md5=a1c0cef96f7c1cd8ea49830aac699e7f","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Medical Laboratories 225, Towa City, IA 52242, United States","Pewe, L., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Xue, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Medical Laboratories 225, Towa City, IA 52242, United States","Under certain conditions, C57BL/6 mice persistently infected with mouse hepatitis virus strain JHM (MHV-JHM) develop clinical disease and histological evidence of demyelination several weeks after inoculation with virus. In a previous report, we showed that mutations in the RNA encoding an immunodominant CD8 T-cell epitope within the surface glycoprotein (epitope S- 510-518) were present in all persistently infected animals and that these mutations abrogated recognition by virus-specific cytotoxic T cells (CTLs) in direct ex vivo cytotoxicity assays. To obtain further evidence that these mutations were necessary for the development of clinical disease, the temporal course of their appearance was determined. Mutations in the epitope were identified by 10 to 12 days after inoculation, and in some mice, virus containing mutated epitope was the dominant species detected by 15 days. In addition, most mice that remain asymptomatic at 80 days after inoculation, a time after which clinical disease almost never develops, were infected with only wild-type virus. Finally, analysis of virus isolated from mice with severe combined immunodeficiency (SCID) revealed the presence only of wild- type epitope S-510-518. These results, by showing that mutations are not selected in SCID mice and occur at early times after inoculation in C57BL/6 mice, support the view that they result from immune pressure and contribute to virus persistence and demyelination in mice infected persistently with MHV-JHM.",,"animal cell; antibody specificity; article; combined immunodeficiency; coronavirus; cytotoxic t lymphocyte; demyelination; gene mutation; lymphocytic infiltration; molecular recognition; mouse; nonhuman; priority journal; scid mouse; virus infection; virus virulence; Amino Acid Sequence; Animals; Brain; CD8-Positive T-Lymphocytes; Coronavirus Infections; Mice; Mice, Inbred C57BL; Mice, SCID; Murine hepatitis virus; Mutation; Point Mutation; RNA, Viral; Sequence Deletion; Species Specificity; Spinal Cord; T-Lymphocytes, Cytotoxic; Time Factors; Variation (Genetics)","Adami, C., Pooley, J., Glomb, J., Stecker, E., Eazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecics nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted CTL response (1996) J. Gen. Virol., 77, pp. 315-325; Bertoletti, A., Costanzo, A., Chisari, F.V., Levrero, M., Artini, M., Seite, A., Penna, A., Ferrari, C., Cytotoxic T lymphocyte response to a wild type hepatitis B virus epitope in patients chronically infected by variant viruses carrying substitutions within the epitope (1994) J. Exp. Med., 180, pp. 933-943; Bertoletti, A., Sette, A., Chisari, F.V., Penna, A., Levrero, M., De Carli, M., Fiaccadori, F., Ferrari, C., Natural variants of cytotoxic epitopes are T-cell receptor antagonists for antiviral cytotoxic T cells (1994) Nature, 369, pp. 407-410; Bureau, J.-F., Montagutelli, X., Bihl, F., Lefebvre, S., Guenet, J.-L., Brahic, M., Mapping loci influencing the persistence of Theiler's virus in the murine central nervous system (1993) Nat. Genet., 5, pp. 87-91; Castro, R.F., Evans, G.D., Jaszewski, A., Perlman, S., Coronavirus- Induced demyelination occurs in the presence of virus-specific cytotoxic T cells (1994) Virology, 200, pp. 733-743; Castro, R.F., Perlman, A.S., CD8+ T cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenic ity (1995) J. Virol., 69, pp. 8127-8131; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmtier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Falk, K., Rötzschke, A.O., Consensus motifs and peptide ligands of MHC class I molecules (1993) Semin. Immunol., 5, pp. 81-94; Franco, A., Ferrari, C., Sette, A., Chisari, F.V., Viral mutations, TCR antagonism and escape from the immune response (1995) Curr. Opin. Immunol., 7, pp. 524-531; Gallagher, T., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenially immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Jacobsen, G., Perlman, S., Localization of virus and antibody response in mice infected persistently with MHV-JHM (1990) Adv. Exp. Med. Biol., 276, pp. 573-578; Klenerman, P., Rowland-Jones, S., McAdam, S., Edwards, J., Daenke, S., Lalloo, D., Koppe, B., McMichael, A.J., Cytotoxic T-cell activity antagonized by naturally occurring HIV-1 gag variants (1994) Nature, 369, pp. 403-407; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Lamonica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, pp. 883-888; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol., 5, pp. 9-14; Lewicki, H., Von Herrath, M., Evans, C., Whitton, J.L., Oldstone, M., CTL escape viral variants. II. Biologic activity in vivo (1995) Virology, 211, pp. 443-450; Meyerhans, A., Cheynier, R., Albert, J., Seth, M., Kwok, S., Sninsky, J., Morfeldt-Manson, A.L.B., Wain-Hobson, S., Temporal fluctuations HIV quasispecies in vivo are not reflected by sequential HIV isolations (1989) Cell, 58, pp. 901-910; Moskophidis, D., Zinkernagel, R.M., Immunobiology of cytotoxic T-cell escape mutants of lymphocytic choriomeningitis virus (1995) J. Virol., 69, pp. 2187-2193; Nonoyama, S., Smith, F.O., Bernstein, I.D., Ochs, H.D., Strain-dependent leakiness of mice with severe combined immune deficiency (1993) J. Immunol., 150, pp. 3817-3824; Nowak, M.A., Bangham, C.R.M., Population dynamics of immune responses to persistent viruses (1996) Science, 272, pp. 74-79; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol., 68, pp. 5483-5495; Perlman, S., Jacobsen, G., Afifi, A., Spread of a neurotropic murine coronavirus into the CNS via the trigeminal and olfactory nerves (1989) Virology, 170, pp. 556-560; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating enccphalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog., 2, pp. 185-194; Pewe, L., Wu, G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Phillips, R.E., Rowland-Jones, S., Nixon, D.F., Gotch, F.M., Edwards, J.P., Ogunlesi, A.O., Elvin, J.G., McMichael, A.J., Human immunodeficiency virus genetic variation that can escape cytotoxic T cell recognition (1991) Nature, 354, pp. 453-459; Pircher, H., Moskophidis, D., Rohrer, U., Burki, K., Hengartner, H., Zinkernagel, R., Viral escape by selection of cytotoxic T cell-resistant virus variants in vivo (1990) Nature, 346, pp. 629-633; Rehermann, B., Pasquinelli, C., Mosier, S., Chisari, F., Hepatitis B virus (HBV) sequence variation in cytotoxic T lymphocyte epitopes is not common in patients with chronic HBV infection (1995) J. Clin. Invest., 96, pp. 1527-1534; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterization of S1 deletion vanants during persistent infection (1997) J. Virol., 71, pp. 2959-2967; Stevenson, P.G., Hawke, S., Sloan, D.J., Bangham, C.R.M., The immunogenicity of intraccrebral virus infection depends on anatomical site (1997) J. Virol., 71, pp. 145-151; Stohlman, S.A., Kyuwa, S., Cohen, M., Bergmann, C., Polo, J.M., Yeh, J., Anthony, R., Keck, J.G., Mouse hepatitis virus nucleocapsid protein- Specific cytotoxic T lymphocytes are Ld-restricted and specific for the carboxy terminus (1992) Virology, 189, pp. 217-224; Stohlman, S.A., Kyuwa, S., Polo, J.M., Brady, D., Lai, M.M.C., Bergmann, C.C., Characterization of mouse hepatitis virus-specific cytotoxic T cells derived from the central nervous system of mice infected with the JHM strain (1993) J. Virol., 67, pp. 7050-7059; Sun, N., Grzybicki, D., Castro, R., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Vollmer, T.L., Multiple sclerosis: New approaches to immunotherapy (1996) Neuroscientist, 2, pp. 127-136; Wang, F., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Weidt, G., Deppert, W., Utermohlen, O., Heukeshoven, J., Lehmann-Grube, F., Emergence of virus escape mutants after immunization with epitope vaccine (1995) J. Virol., 69, pp. 7147-7151; Williamson, J.S., Sykes, K.C., Stohlman, S.A., Characterization of brain-infiltrating mononuclear cells during infection with mouse hepatitis virus strain JHM (1991) J. Neuroimmunol., 32, pp. 199-207; Wolinsky, S.M., Korber, B., Neumann, A.U., Daniels, M., Kunsttnan, K., Whetsell, A., Furtado, M., Koup, R., Adaptive evolution of human immunodeficiency virus-type 1 during ihe natural course of infection (1996) Science, 272, pp. 537-542; Young, A., Zhang, W., Sacchettini, J., Nathenson, S., The three-dimensional structure of H-2D at 2.4 (1994) A Resolution: Implications for Antigen-determinant Selection. Cell, 76, pp. 39-50; Zinkernagel, R.M., Immunology taught by viruses (1996) Science, 271, pp. 173-178","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 225, Iowa City, IA 52242, United States; email: stanley-perlman@uiowa.edu",,,0022538X,,JOVIA,"9311846","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030768760
"Lin X., O'Reilly K.L., Storz J.","36768282000;7103313844;7006694594;","Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny",1997,"American Journal of Veterinary Research","58","10",,"1120","1124",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031253694&partnerID=40&md5=333a8829694d29553dd7f445082f3e31","Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Lin, X., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; O'Reilly, K.L., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Storz, J., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Objective - To investigate the susceptibility of polarized epithelioid human rectal tumor (HRT-18G) cells to bovine coronaviruses (BCV) isolated from enteric (EBCV) and respiratory (RBCV) tract infections. Procedure - Cells of the G clone of HRT-18 were grown to confluent monolayers on permeable supports, and were directionally infected at the apical and basolateral domains with 3 wild-type BCV strains, RBCV-LSU-94LSS-051-2, RBCV-OK-0514-3, and EBCV-LY138-2, and 1 cell culture-adapted strain, EBCV-L9-80. Sequential cytopathic changes were microscopically monitored. Medium samples for titration of hemagglutinins and viral infectivity were collected directionally from both domains of the infected cell cultures at various intervals. Results - Polarized epithelioid HRT-18G cells from apical domains had maximal susceptibility to infection with the EBCV and RBCV strains, and those from basolateral surfaces had minimal susceptibility. Titers of hemagglutinins and infective progeny BCV reached 1,280 hemagglutinin units and 4.2 × 108 plaque-forming units/ml for apical samples, but were minimal for basolateral samples. Asymmetric virus release occurred through the apical surfaces of the HRT-18G cells by 12 hours after infection when cell fusion as a sign of cytopathic changes began. When cells were infected basolaterally, progeny virions released from apical surfaces reinfected the target cells from the apical domains and induced cytopathic changes were delayed about 12 hours, compared with changes detectable in apically exposed cultures. Conclusions - EBCV and RBCV, isolated from cattle, had marked tropism for polarized epithelioid HRT-18G cells. Entry of BCV into the polarized HRT-18G cells was effected maximally through the apical domains and minimally through the basolateral domains. Release of progeny BCV occurred preferentially from the apical domains.",,"virus hemagglutinin; adenocarcinoma; animal; animal disease; article; cattle; cattle disease; cell culture; cell membrane; Coronavirus; diarrhea; digestive system; epithelium cell; human; isolation and purification; metabolism; methodology; microvillus; pathology; physiology; rectum tumor; respiratory system; respiratory tract infection; scanning electron microscopy; ultrastructure; virology; virus infection; virus replication; Adenocarcinoma; Animals; Cattle; Cattle Diseases; Cell Membrane; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Digestive System; Epithelial Cells; Hemagglutinins, Viral; Humans; Microscopy, Electron, Scanning; Microvilli; Rectal Neoplasms; Respiratory System; Respiratory Tract Infections; Tumor Cells, Cultured; Virus Replication","Mebus, C.A., Stair, E.L., Rhodes, M.B., Neonatal calf diarrhea: Propagation, attenuation and characteristics of coronavirus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronaviruses in the feces (1988) Vet Rec, 123, pp. 300-301; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses, structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2953; Cavanagh, D., Brian, D.A., Enjuanes, L., Recommendations of the coronavirus study group for the nomenclature of the structural proteins, mRNAs, and genes of coronaviruses (1990) Virology, 176, pp. 306-307; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Laporte, J., L'Haridon, R., Bobulesco, P., In vitro culture of bovine enteric coronavirus (BEC) (1979) Inst Nat Sante Tech Med Colloq, 90, pp. 99-102; St. Cyr-Coats, K., Storz, J., Bovine coronavirus-induced cytopathic expression and plaque formation: Host cell and virus strain determine trypsin dependence (1988) Zentralbl Veterinarmed [B], 35, pp. 48-56; Tompkins, W.A.F., Watrach, A.M., Schmale, J.D., Cultural and antigenic properties of newly established cell strains from adenocarcinomas of human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 101-106; Doughri, A.M., Storz, J., Light and ultrastructural pathological changes in intestinal coronavirus infection of newborn calves (1977) Zentralbl Veterinarmed [B], 24, pp. 367-385; Payne, H.R., Storz, J., Scanning electron microscopic characterization of bovine coronavirus plaques in HRT cells (1990) Zentralbl Veterinarmed [B], 37, pp. 501-508; Murphy, J.S., Bang, F.B., Observations with electron microscope on cells of chick chorioallantoic membrane infected with influenza virus (1952) J Exp Med, 95, pp. 259-268; Jones, L.V., Compans, R.W., Davis, A.R., Surface expression of influenza virus neuraminidase, an amino-terminal anchored viral membrane glycoprotein, in polarized epithelial cells (1985) Mol Cell B, 5, pp. 2182-2189; Rodriguez-Boulan, E., Sabatini, D.D., Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity (1978) Proc Natl Acad Sci USA, 75, pp. 5071-5075; Roth, M.G., Compans, R.W., Giusti, L., Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA (1983) Cell, 33, pp. 435-443; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Tucker, S.P., Compans, R.W., Virus infection of polarized epithelial cells (1993) Adv Virus Res, 42, pp. 187-247; Doughri, A.M., Storz, J., Hajer, I., Morphology and morphogenesis of a coronavirus infecting intestinal epithelial cells of newborn calves (1976) Exp Mol Pathol, 25, pp. 355-370; Schultz, B., Herrler, G., Polarized entry of bovine coronavirus in epithelial cells (1995) Corona and Related Viruses - Current Concepts in Molecular Biology and Pathogenesis, pp. 375-378. , Talbot PJ, Levy GA, eds. New York: Plenum Press; Fuller, S., Von Bonsdorff, C.-H., Simons, K., Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line MDCK (1984) Cell, 38, pp. 65-77; Misfeldt, D.S., Hamamoto, S.T., Pitelka, D.R., Transepithelial transport in cell culture (1976) Proc Natl Acad Sci U S A, 73, pp. 1212-1216; Cereijido, M., Robbins, E.S., Donlan, W.J., Polarized monolayers formed by epithelial cells on a permeable and translucent support (1978) J Cell Biol, 77, pp. 853-880; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Coronaviruses in polarized epithelial cells (1995) Corona and Related Viruses - Current Concepts in Molecular Biology and Pathogenesis, pp. 135-138. , Talbot PJ, Levy GA, eds. New York: Plenum Press; Stephens, E.B., Compans, R.W., Nonpolarized expression of a secreted murine leukemia virus glycoprotein in polarized epithelial cells (1986) Cell, 47, pp. 1053-1059","Storz, J.; Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",,,00029645,,AJVRA,"9328665","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0031253694
"Riffault S., Carrat C., Besnardeau L., La Bonnardière C., Charley B.","6603556292;6603249904;6602382869;7003503325;55246691600;","In vivo induction of interferon-α in pig by non-infectious coronavirus: Tissue localization and in situ phenotypic characterization of interferon-α-producing cells",1997,"Journal of General Virology","78","10",,"2483","2487",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030773726&partnerID=40&md5=2d18e2310ced2111672404b6e90a2e8b","U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France","Riffault, S., U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France; Carrat, C., U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France; Besnardeau, L., U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France; La Bonnardière, C., U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France; Charley, B., U. Virologie Immunol. Moleculaires, INRA, 78352 Jouy-en-Josas Cedex, France","A low frequency peripheral blood mononuclear cell (PBMC) subpopulation, referred to as natural interferon-producing (NIP) cells, is described as producing interferon-α (IFN-α) following contact with non-infectious viral structures, namely viral glycoproteins. These cells are characterized in vitro as non-T, non-B, MHC class II+ and CD4+ cells. In this study, NIP cells were analysed in vivo after an intravenous injection of UV-inactivated transmissible gastroenteritis virus in newborn piglets, which resulted in strong serum IFN-α production. Splenocytes, but not PBMC, were the IFN-α producers in vivo. Using double immunohistochemical labelling for both IFN-α and leukocyte markers, we established that splenic NIP cells were not T or B cells. The majority were MHC class II+ and only a minority expressed a macrophage marker. NIP cells were localized in contact with MHC class II-expressing cells and T cells, which suggested that NIP cells might modulate the antiviral immune response.",,"alpha interferon; cell marker; major histocompatibility antigen class 2; animal cell; animal experiment; animal tissue; antigen expression; article; b lymphocyte; cell subpopulation; coronavirus; interferon production; macrophage; mononuclear cell; newborn; nonhuman; phenotype; priority journal; protein induction; spleen cell; swine; t lymphocyte; tissue distribution; Animals; Antibodies, Monoclonal; Antigens, Differentiation, Myelomonocytic; CD4-Positive T-Lymphocytes; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Indirect; Histocompatibility Antigens Class II; Interferon-alpha; Lymphocyte Subsets; Spleen; Swine; Time Factors; Transmissible gastroenteritis virus; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Artursson, K., Lindersson, M., Varela, N., Scheynius, A., Alm, G.V., Interferon-α production and tissue localization of interferon-α/β producing cells after intradermal administration of Aujeszky's disease virus-infected cells in pigs (1995) Scandinavian Journal of Immunology, 41, pp. 121-129; Belardelli, F., Gresser, I., The neglected role of type I interferon in the T-cell response: Implications for its clinical use (1996) Immunology Today, 17, pp. 369-372; Bhuiya, T.A., Shodell, M., Fitzgerald-Bocarsly, P.A., Murasko, D., Shah, K., Drake, D., Siegal, F.P., Interferon-α generation in mice responding to challenge with UV-inactivated herpes simplex virus (1994) Journal of Interferon Research, 14, pp. 17-24; Cederblad, B., Alm, G.V., Infrequent but highly efficient interferon-α producing human mononuclear leukocytes induced by herpes simplex virus in vitro studied by immuno-plaque and limiting dilution assays (1990) Journal of Interferon Research, 10, pp. 65-73; Charley, B., Laude, H., Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of a transmembrane glycoprotein E1 (1988) Journal of Virology, 62, pp. 8-11; De Diaz Arce, H., Artursson, K., L'Haridon, R., Perers, A., La Bonnardière, C., Alm, G.V., A sensitive immunoassay for porcine interferon-α (1992) Veterinary Immunology and Immunopathology, 30, pp. 319-327; Eloranta, M.-L., Sandberg, K., Alm, G.V., The interferon-α/β responses of mice to herpes simplex virus studied at the blood and tissue level in vitro and in vivo (1996) Scandinavian Journal of Immunology, 43, pp. 355-360; Ferbas, J.J., Toso, J.F., Logar, A.J., Navratil, J.S., Rinaldo Jr., C.R., CD4+ blood dendritic cells are potent producers of IFN-α in response to in vitro HIV-1 infection (1994) Journal of Immunology, 152, pp. 4649-4662; Fitzgerald-Bocarsly, P., Human natural interferon-α producing cells (1993) Pharmacology and Therapeutics, 60, pp. 39-62; Francis, M.L., Meltzer, M.S., Induction of IFN-α by HIV-1 in monocyte-enriched PBMC requires gp120-CD4 interaction but not virus replication (1993) Journal of Immunology, 151, pp. 2208-2216; Gobl, A.E., Funa, K., Alm, G.V., Different induction patterns of mRNA for IFN-α and IFN-β in human mononuclear leukocytes after in vitro stimulation with herpes simplex virus-infected fibroblasts and Sendai virus (1988) Journal of Immunology, 140, pp. 3605-3609; Grage-Griebenow, E., Flad, H.-D., Ernst, M., Fcγ receptor I (CD64)-negative human monocytes are potent accessory cells in viral antigen-induced T cell activation and exhibit high IFN-α-producing capacity (1996) Journal of Leukocyte Biology, 60, pp. 389-396; Hammerberg, C., Schurig, G.G., Characterization of monoclonal antibodies directed against swine leucocytes (1986) Veterinary Immunology and Immunopathology, 11, pp. 107-121; Kaeffer, B., Bottreau, E., Marcon, D., Olivier, M., Lantier, I., Salmon, H., Histocompatible miniature pig (d/d haplotype): Generation of hybridomas secreting A or M monoclonal antibody (1991) Hybridoma, 10, pp. 731-744; La Bonnardière, C., Laude, H., High interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infection and Immunity, 32, pp. 28-31; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus (1992) Journal of Virology, 66, pp. 743-749; Lefèvre, F., L'Haridon, R., Borras-Cuesta, F., La Bonnardière, C., Production, purification and biological properties of an Escherichia coli-derived recombinant porcine alpha interferon (1990) Journal of General Virology, 71, pp. 1057-1063; Nowacki, W., Charley, B., Enrichment of coronavirus-induced interferon-producing blood leukocytes increases the interferon yield per cell: A study with pig leukocytes (1993) Research in Immunology, 144, pp. 111-120; Nowacki, W., Cederblad, B., Renard, C., La Bonnardière, C., Charley, B., Age-related increase of porcine natural interferon α producing cell frequency and of interferon yield per cell (1993) Veterinary Immunology and Immunopathology, 37, pp. 113-122; Pescovitz, M.D., Lunney, J.K., Sachs, D.H., Preparation and characterization of monoclonal antibodies reactive with porcine PBL (1984) Journal of Immunology, 133, pp. 368-375; Riffault, S., Eloranta, M.-L., Carrat, C., Sandberg, K., Charley, B., Alm, G., Herpes simplex virus induces appearance of interferon-α/β producing cells and partially interferon-α/β-dependent accumulation of leukocytes in murine regional lymph nodes (1996) Journal of Interferon and Cytokine Research, 16, pp. 1007-1014; Riffault, S., Grosclaude, J., Vayssier, M., Laude, H., Charley, B., Reconstituted coronavirus TGEV virosomes lose the virus ability to induce porcine interferon-alpha production (1997) Veterinary Research, 28, pp. 105-114; Sandberg, K., Eloranta, M.L., Johannisson, A., Alm, G.V., Flow cytometric analysis of natural interferon-α producing cells (1991) Scandinavian Journal of Immunology, 34, pp. 565-576; Sandberg, K., Eloranta, M.-L., Campbell, I.L., Expression of alpha/beta interferons (IFN-α/β) and their relationship to IFN-α/β-induced genes in lymphocytic choriomeningitis (1994) Journal of Virology, 68, pp. 7358-7366; Splichal, I., Rehakova, Z., Sinkora, J., Charley, B., Sinkora, M., Interferon alpha secreting cells in hematopoietic organs of pig fetuses after in vivo stimulation by coronavirus TGEV (1995) Scandinavian Journal of Immunology, 41, p. 642; Svensson, H., Johannisson, A., Nikkilä, T., Alm, G.V., Cederblad, B., The cell surface phenotype of human natural IFN-α producing cells as determined by flow cytometry (1996) Scandinavian Journal of Immunology, 44, pp. 164-172; Van Den Broek, M.F., Müller, U., Huang, S., Zinkernagel, R.M., Aguet, M., Immune defence in mice lacking type I and/or type II interferon receptors (1995) Immunological Reviews, 148, pp. 5-18; Yang, H., Parkhouse, R.M.E., Phenotypic classification of porcine lymphocyte subpopulations in blood and lymphoid tissues (1996) Immunology, 89, pp. 76-83","Riffault, S.; Unite Virologie Immunol. Moleculaire, INRA, 78352 Jouy-en-Josas cedex, France; email: riffault@biotec.jouy.inra.fr",,,00221317,,JGVIA,"9349468","English","J. GEN. VIROL.",Article,"Final",,Scopus,2-s2.0-0030773726
"Thiel V., Rashtchian A., Herold J., Schuster D.M., Guan N., Siddell S.G.","35238592100;6701774018;7006838690;35910570200;36728900800;7005260816;","Effective amplification of 20-kb DNA by reverse transcription PCR",1997,"Analytical Biochemistry","252","1",,"62","70",,26,"10.1006/abio.1997.2307","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031260478&doi=10.1006%2fabio.1997.2307&partnerID=40&md5=146fcfb93c679e894711ba4108d786ab","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Life Technologies Inc., 9800 Medical Center Drive, Rockville, MD 20850, United States; Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Thiel, V., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Rashtchian, A., Life Technologies Inc., 9800 Medical Center Drive, Rockville, MD 20850, United States; Herold, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Schuster, D.M., Life Technologies Inc., 9800 Medical Center Drive, Rockville, MD 20850, United States; Guan, N., Life Technologies Inc., 9800 Medical Center Drive, Rockville, MD 20850, United States; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Polymerase chain reaction has been applied to the amplification of long DNA fragments from a variety of sources, including genomic, mitochondrial, and vital DNAs. However, polymerase chain reaction amplification from cDNA templates produced by reverse transcription has generally been restricted to products of less than 10 kilobases. In this paper, we report a system to effectively amplify fragments up to 20 kilobases from human coronavirus 229E genomic RNA. We demonstrate that the integrity of the RNA template and the prevention of false priming events during reverse transcription are the critical parameters to achieve the synthesis of long cDNAs. The optimization of the polymerase chain reaction conditions enabled us to improve the specificity and yield of product but they were not definitive. Finally, we have shown that the same reverse transcription polymerase chain reaction technology can be used for the amplification of extended regions of the dystrophin mRNA, a cellular RNA of relatively low abundance.",,"complementary DNA; DNA fragment; dystrophin; messenger RNA; polyadenylated RNA; virus RNA; article; Coronavirus; DNA template; gene amplification; human; human cell; human tissue; priority journal; reverse transcription polymerase chain reaction; Coronavirus; human coronavirus; Human coronavirus 229E","Barnes, W.M., (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 2216-2220; Cheng, S., Fockler, C., Barnes, W.M., Higuchi, R., (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 5695-5699; Cheng, S., Chang, S.Y., Gravitt, P., Respess, R., (1994) Nature, 369, pp. 684-685; Cheng, S., Higuchi, R., Stoneking, M., (1994) Nature Genet., 7, pp. 350-351; Cheng, S., Chen, Y., Monforte, J.A., Higuchi, R., Van Houten, B., (1995) PCR Methods Appl., 4, pp. 294-298; Tellier, R., Bukh, J., Emerson, S.U., Purcell, R.H., (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 4370-4373; Martinez, J.M., Breidenbach, H.H., Cawthon, R., (1996) Genome Res., 6, pp. 58-66; Chumakov, K.M., (1996) J. Virol., 70, pp. 7331-7334; Fakhfakh, H., Vilaine, F., Makni, M., Robaglia, C., (1996) J. Gen. Virol., 77, pp. 519-523; Nathan, M., Mertz, L.M., Fox, D.K., (1995) Focus, 17, pp. 78-80; Herold, J., Raabe, T., Siddell, S., (1993) Arch. Virol., 7 (SUPPL.), pp. 63-74; Raabe, T., Schelle-Prinz, B., Siddell, S.G., (1990) J. Gen. Virol., 71, pp. 1065-1073; Siddell, S., (1983) J. Gen. Virol., 64, pp. 113-125; Meinkoth, J., Wahl, G., (1984) Anal. Biochem., 138, pp. 267-284; Gerard, G.F., Schmidt, B.J., Kotewicz, M.L., Campbell, J.H., (1992) Focus, 14, pp. 91-93; Koenig, M., Hoffmann, E.P., Bertelson, C.J., Monaco, A.P., Feener, C., Kunkel, L.M., (1987) Cell, 50, pp. 509-517; Hoffman, E.P., Monaco, A.P., Feener, C.C., Kunkel, L.M., (1987) Science, 238, pp. 347-350; Tennyson, C.N., Shi, Q., Worton, R.G., (1996) Nucleic Acids Res., 24, pp. 3059-3064; Racaniello, V.R., Baltimore, D., (1981) Science, 214, pp. 916-919; Rice, C.M., Levis, R., Strauss, J.H., Huang, H.V., (1987) J. Virol., 61, pp. 3809-3819; Rice, C.M., Grakoui, A., Galler, R., Chambers, T.J., (1989) New Biol., 1, pp. 285-296; Sumiyoshi, H., Hoke, C.H., Trent, D.W., (1992) J. Virol., 66, pp. 5425-5431","Thiel, V.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany; email: v.thiel@rzbox.uniwuerzburg.de",,"Academic Press Inc.",00032697,,ANBCA,"9324942","English","ANAL. BIOCHEM.",Article,"Final",,Scopus,2-s2.0-0031260478
"Majhdi F., Minocha H.C., Kapil S.","7801417122;7003283136;7003293348;","Isolation and characterization of a coronavirus from elk calves with diarrhea",1997,"Journal of Clinical Microbiology","35","11",,"2937","2942",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030833381&partnerID=40&md5=e2f8e9e8243fc752c9b37fb11e432c66","Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Majhdi, F., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Minocha, H.C., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Kapil, S., Dept. of Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","This is the first report of the isolation of a coronavirus from elk calves. Two fecal samples from elk calves with diarrhea were shown to be positive for coronavirus-like particles by electron microscopy, and the particles were propagated in the human rectal tumor-18 cell line. After 24 h, syncytia were observed, and cell culture supernatants from both samples showed hemagglutinating activity with mouse erythrocytes. Cells infected with both elk coronavirus (ECV) isolates reacted with Z3A5, a monoclonal antibody against the spike protein of bovine coronavirus (BCV), on an indirect fluorescent antibody test. The protein profiles of both ECV isolates were similar to that of BCV as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. On Northern blot analysis, the transcriptional pattern of ECV was typical of coronaviruses, with a nested set of transcripts with common 3' end sequences. Based on a published nucleoprotein gene sequence for BCV (Mebus isolate), we arbitrarily designed two primers for amplification by PCR. After cloning, the nucleoprotein was sequenced and a high degree of homology (99%) between the nucleoprotein gene sequences of ECV and BCV was observed. Thus, ECV is closely related genetically and antigenically to BCV and will be a new member of antigenic group 2 of the mammalian coronaviruses, which possess hemagglutinin-esterase protein.",,"animal cell; animal tissue; article; bacterium isolation; cattle; coronavirus; diarrhea; electron microscopy; feces analysis; hemagglutination; nonhuman; phylogeny; priority journal; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Base Sequence; Blotting, Northern; Cattle; Cloning, Molecular; Coronavirus; Coronavirus Infections; Coronavirus, Bovine; Deer; Diarrhea; Erythrocytes; Feces; Fluorescent Antibody Technique, Indirect; Genes, Viral; Hemagglutination Tests; Humans; Male; Membrane Glycoproteins; Mice; Molecular Sequence Data; Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Transcription, Genetic; Tumor Cells, Cultured; Viral Envelope Proteins; Viral Structural Proteins; Animalia; Bacteria (microorganisms); Bos taurus; Bovinae; Bovine coronavirus; Cervus elaphus; Coronavirus; Mammalia","Chasey, D., Reynolds, D.J., Bridges, J.C., Debney, T.G., Scott, A.C., Identification of coronaviruses in exotic species of bovidae (1984) Vet. Rec., 115, pp. 602-603; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Crouch, C.F., Bielefeldtohmann, H., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J. Gen. Virol., 66, pp. 1489-1500; Elazhary, M.A.S.Y., Frechette, J.L., Silim, A., Roy, R.S., Serological evidence of some bovine viruses in caribou (Rangifer tarandus caribou) in Quebec (1981) J. Wildl. Dis., 17, pp. 609-612; Feng, D.F., Doolittle, R.F., Progressive sequence alignment as a prerequisite to correct phylogenetic trees (1987) J. Mol. Evol., 25, pp. 351-360; Guy, J.S., Brian, D.A., Bovine coronavirus genome (1979) J. Virol., 29, pp. 293-300; Kapil, S., Pomeroy, K.A., Goyal, S.M., Trent, A.M., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J. Vet. Diagn. Invest., 3, pp. 88-89; Kapil, S., Chard-Bergstrom, C., Bolin, P., Landers, D., Plaque variations in clinical isolates of bovine coronavirus (1995) J. Vet. Diagn. Invest., 7, pp. 538-539; Kapil, S., Richardson, K.L., Radi, C., Chard-Bergstrom, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J. Vet. Diagn. Invest., 8, pp. 96-99; King, B., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein (1982) J. Mol. Biol., 157, pp. 105-132; Munoz, M., Alvarez, M., Lanza, I., Carmens, P., Role of enteric pathogens in the etiology of neonatal diarrhea in lambs and goat kids in Spain Epidemiol (1996) Infect., 117, pp. 203-211; Pass, D.A., Penhale, W.J., Wilcox, G.E., Batey, R.G., Intestinal coronavirus-like particles in sheep with diarrhea (1982) Vet. Rec., 111, pp. 106-107; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet., 80, pp. 303-311; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am. J. Vet. Res., 37, pp. 1031-1041; Smits, J.E.G., Elk diseases survey in western Canada and northwestern United States (1992) The Biology of Deer, pp. 101-106. , R. D. Brown (ed.), Springer-Verlag, New York, N.Y; Stair, E.L., Rhodes, M.B., White, R., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am. J. Vet. Res., 33, pp. 1147-1156; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Reed, H.H., Saif, L.J., Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J. Clin. Microbiol., 33, pp. 3264-3269; Zhang, Z., Maag, T.R., Xue, W., Muenzenberger, M.M., Minocha, H.C., Kapil, S., Development, characterization, and application of monoclonal antibodies specific for spike glycoprotein of bovine coronavirus (1995) Conference of Research Workers in Animal Diseases, p. 240. , Iowa State University Press, Ames","Kapil, S.; Diagnostic Med./Pathobiology Dept., College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,00951137,,JCMID,"9350763","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0030833381
"Zhang Z., Andrews G.A., Chard-Bergstrom C., Minocha H.C., Kapil S.","55721882200;7202160819;6602711643;7003283136;7003293348;","Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalin-fixed intestines",1997,"Journal of Clinical Microbiology","35","11",,"2964","2965",,14,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030827110&partnerID=40&md5=c426bfb9a2c534e50fe04d35ab96ea8c","DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Zhang, Z., DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Andrews, G.A., DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Chard-Bergstrom, C., DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Minocha, H.C., DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Kapil, S., DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","A monoclonal antibody (MAh) (Z3AS) against spike protein subunit of bovine coronavirus (BCV) reacted with the virus in formalin-fixed intestines in an immunoperoxidase test. We found an 88% correlation between immunohistochemistry with Z3A5 and in situ hybridization with a BCV nucleoprotein cDNA probe. MAb Z3A5 reacted with 90 BCV isolates from the United States and was an effective reagent for the diagnosis of BCV.",,"monoclonal antibody; protein subunit; virus protein; animal cell; animal experiment; animal model; animal tissue; article; cattle disease; coronavirus; diarrhea; dna probe; dysentery; in situ hybridization; mouse; nonhuman; priority journal; virus detection; virus infection; virus isolation; Animals; Antibodies, Monoclonal; Cattle; Cattle Diseases; Colon; Coronavirus Infections; Coronavirus, Bovine; DNA Probes; Immunohistochemistry; In Situ Hybridization; Intestinal Mucosa; Membrane Glycoproteins; Necrosis; Paraffin; Reproducibility of Results; United States; Viral Envelope Proteins; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus",,"Kapil, S.; DDMPD, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,00951137,,JCMID,"9350768","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0030827110
"Ikemori Y., Ohta M., Umeda K., Icatlo Jr. F.C., Kuroki M., Yokoyama H., Kodama Y.","6701880616;7402949202;7102144610;6602748645;57216061484;36958373000;7203085451;","Passive protection of neonatal calves against bovine coronavirus-induced diarrhea by administration of egg yolk or colostrum antibody powder",1997,"Veterinary Microbiology","58","2-4",,"105","111",,60,"10.1016/S0378-1135(97)00144-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031458280&doi=10.1016%2fS0378-1135%2897%2900144-2&partnerID=40&md5=f16af27b91062e5dfbbf0f852f4e6e86","Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan","Ikemori, Y., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Ohta, M., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Umeda, K., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Icatlo Jr., F.C., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Kuroki, M., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Yokoyama, H., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan; Kodama, Y., Ghen Corp. Immunol. Res. Institute, 839-1 Sano, Gifu City, 501-11, Japan","The protective effect of egg yolk and colostrum powders prepared from hens and cows vaccinated with inactivated bovine coronavirus (BCV) antigen was evaluated in a challenge model with a virulent BCV strain. Twenty three calves from BCV-free herds were randomly divided into control and several treatment groups. All calves were orally challenged with 1 x 109 TCID50 of the virulent Kakegawa strain of BCV at 24 to 36 h after birth. Calves in treatment groups received either egg yolk powder or cow colostrum containing BCV specific antibodies. Daily treatment with these antibody preparations started 6 h until 7 days post-challenge. Control calves which received no antibody had severe diarrhea and all died within 6 days after infection. In contrast, calves fed milk containing egg yolk or colostrum with neutralization titers of 1:2560 or 1:10,240 respectively all survived and had positive weight gain unlike the other treatment groups. These results indicate that the orally administered egg yolk and colostrum powders protected against BCV-induced diarrhea in neonatal calves and that the egg yolk used provided a higher degree of protection compared to colostrum powder on a titer basis. Treatment with whole egg yolk from immunized hens therefore provides a more efficacious alternative to the existing methods of specific passive protection against BCV.","Bovine coronavirus; Cattle-viruses; Colostrum; Egg yolk; Immunology; Passive immunization","maternal antibody; virus antigen; animal experiment; animal tissue; antibody titer; article; cattle; chicken; colostrum; controlled study; coronavirus; diarrhea; egg yolk; female; immunization; intramuscular drug administration; nonhuman; oral drug administration; passive immunization; Animals; Antibodies, Viral; Antibody Specificity; Cattle; Cattle Diseases; Colostrum; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Egg Yolk; Immunization, Passive; Neutralization Tests","Heckert, R.A., Saif, L.J., Mengel, J.P., Myers, G.W., Mucosal and systemic antibody responses to bovine coronavirus structural proteins in experimentally challenge-exposed calves fed low or high amounts of colostral antibodies (1991) Am. J. Vet. Res., 52, pp. 700-708; Heckert, R.A., Saif, L.J., Myers, G.W., Mucosal and systemic isotype-specific antibody responses to bovine coronavirus structural proteins in naturally infected dairy calves (1991) Am. J. Vet. Res., 52, pp. 852-857; Heckert, R.A., Saif, L.J., Myers, G.W., Agnes, A.G., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am. J. Vet. Res., 52, pp. 845-851; Ikemori, Y., Kuroki, M., Peralta, R.C., Yokoyama, H., Kodama, Y., Protection of neonatal calves against fatal enteric colibacillosis by administration of egg yolk powder from hens immunized with K99-piliated enterotoxigenic Escherichia coli (1992) Am. J. Vet. Res., 53, pp. 2005-11008; Ikemori, Y., Peralta, R.C., Kuroki, M., Yokoyama, H., Kodama, Y., Research note: Avidity of chicken yolk antibodies to enterotoxigenic Escherichia coli fimbriae (1993) Poultry Sci., 72, pp. 2361-2365; Kapil, S., Trent, A.M., Goyal, S.M., Excretion and persistence of bovine coronavirus in neonatal calves (1990) Arch. Virol., 115, pp. 127-132; Kuroki, M., Ikemori, Y., Yokoyama, H., Peralta, R.C., Icatlo F.C., Jr., Kodama, Y., Passive protection against bovine rotavirus-induced diarrhea in murine model by specific immunoglobulins from chicken egg yolk (1993) Vet. Microbiol., 37, pp. 135-146; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.F., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Shimizu, M., Nagashima, H., Sano, K., Hashimoto, K., Ozeki, M., Tsuda, K., Hatta, H., Molecular stability of chicken and rabbit immunoglobulin g (1992) Biosci. Biotech. Biochem., 56, pp. 270-274; Tsunemitsu, H., Yonemichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J. Vet. Med. Sci., 53, pp. 433-437","Ikemori, Y.; Ghen Corporation Immunology Research, 839-1 Sano, Gifu City 501-11, Japan",,,03781135,,VMICD,"9453122","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0031458280
"Arruda E., Pitkäranta A., Witek Jr. T.J., Doyle C.A., Hayden F.G.","7004935664;7003331729;35548933600;57213614919;7103233446;","Frequency and natural history of rhinovirus infections in adults during autumn",1997,"Journal of Clinical Microbiology","35","11",,"2864","2868",,224,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842292104&partnerID=40&md5=f77884e49f806688fb4cf12d71b1b8d8","Department of Internal Medicine, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States; Department of Pathology, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States; Boehringer Ingelheim Pharmaceut., I., Ridgefield, CT 06877, United States; University of Sao Paulo, School of Medicine, Ribeirao Preto, Sao Paulo 14049-900, Brazil; University Hospital of Helsinki, Helsinki, Finland; University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Arruda, E., Department of Internal Medicine, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States, Department of Pathology, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto, Sao Paulo 14049-900, Brazil; Pitkäranta, A., Department of Internal Medicine, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States, University Hospital of Helsinki, Helsinki, Finland; Witek Jr., T.J., Boehringer Ingelheim Pharmaceut., I., Ridgefield, CT 06877, United States; Doyle, C.A., Boehringer Ingelheim Pharmaceut., I., Ridgefield, CT 06877, United States; Hayden, F.G., Department of Internal Medicine, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States, Department of Pathology, University of Virginia, School of Medicine, Charlottesville, VA 22908, United States, University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Human rhinovirus (HRV) accounts for a significant portion of common- cold illness, with the peak incidence being in the early fall. Three hundred forty-six adults who had self-diagnosed colds of 48 h or less were enrolled in a study during September and October 1994 to determine the frequency and clinical course of HRV infections. Nasal wash specimens for viral culture and reverse transcription-PCR (RT-PCR) for HRV RNA and human coronavirus OC43 and 229E RNA detection were collected on enrollment, and participants recorded their symptoms twice daily for 14 days. Middle ear pressure (MEP) was measured with a digital tympanometer on days 1 and 7. Picornaviruses (224 HRV and 7 enterovirus isolates) were detected by culture in 67% (231 of 346) of the subjects. Among 114 samples negative by culture, HRV was detected by RT- PCR in 52 (46%) for an overall picornavirus infection rate of 82% (283 of 346 subjects). Among the remaining 62 negative samples, human coronavirus RNA was detected by RT-PCR in 5 patients, so that 288 (83%) of patients had documented viral infection. The first symptom noticed most often was sore throat (40%) in HRV culture- or PCR-positive patients and stuffy nose in HRV- negative patients (27%). No differences in symptom scores over time or in the presence of individual symptoms were noted between groups. The median duration of the cold episodes was 11 days in HRV culture-positive patients, 9.5 days in HRV RT-PCR-positive patients, and 11.5 days in HRV-negative patients. On enrollment, abnormal MEPs (≤-100 or ≤+100 mm of H2O) were found for 21% of HRV culture-positive patients, 14% of HRV RT-PCR-positive patients, and 10% of HRV-negative patients. No important differences in the clinical course of HRV culture-positive, HRV culture-negative and RT-PCR- positive, or HRV-negative colds were found. These results represent the highest frequency of virologically confirmed natural colds to date and document the importance of rhinoviruses as the cause of colds during fall months.",,"adult; article; female; history; human; human cell; human tissue; incidence; infection rate; major clinical study; male; picornavirus; priority journal; rhinovirus; seasonal variation; virus culture; virus infection; Adolescent; Adult; Common Cold; Female; Humans; Incidence; Male; Middle Aged; Pharyngitis; Polymerase Chain Reaction; Retrospective Studies; Rhinitis; Rhinovirus; Seasons; Smoking; Sneezing; Time Factors; Virginia; Coronavirus; Enterovirus; human coronavirus; Human rhinovirus sp.; Rhinovirus","Arruda, E., Hayden, F.G., McAuliffe, J.F., Sota, M.A., Mota, S.B., McAuliffe, M.I., Geist, F.G., Gwaltney Jr., J.M., Acute respiratory viral infections in ambulatory children in urban northeast Brazil (1991) J. Infect. Dis., 164, pp. 1261-1268; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings by PCR (1993) Mol. Cell. Probes, 7, pp. 373-379; Arruda, E., Crump, C.E., Rollins, B.S., Ohlin, A., Hayden, F.G., Comparative susceptibility of human embryonic fibroblasts and HeLa cells for isolation of human rhinoviruses (1996) J. Clin. Microbiol., 34, pp. 1277-1279; Arruda, E., Rakes, G.P., Heymann, P.W., Hayden, F.G., Detection of human rhinovirus (HRV) in nasal washes (NW) by RT-PCR and non-isotopic in solution hybridization Abstracts of the 95th General Meeting of the American Society for Microbiology 1995, p. 41. , abstr. C-236, American Society for Microbiology, Washington, D.C; Boni, J., Schupbach, J., Sensitive and quantitative detection of PCR-amplified HIV-1 DNA products by an enzyme linked immunoassay following solution hybridization with two differently labelled oligonucleotide probes (1993) Mol. Cell. Probes, 7, pp. 361-371; Doyle, W.J., McBride, T.P., Swarts, J.D., Hayden, F.G., Gwaltney Jr., J.M., The response of the nasal airway, middle ear, and eustachian tube to experimental rhinovirus infection (1988) Am. J. Rhinol., 2, pp. 149-154; Doyle, W.J., McBride, T.P., Skoner, D.P., Maddern, B.R., Gwaltney Jr., J.M., Uhrin, M., A double-blind, placebo-controlled clinical trial of the effect of chlorpheniramine on challenge (1988) Pediatr. Infect. Dis. J., 7, pp. 215-242; Elkhatieb, A., Hipskind, G., Woerner, D., Hayden, F.G., Middle ear abnormalities during natural rhinovirus colds in adults (1993) J. Infect. Dis., 168, pp. 618-621; Gwaltney Jr., J.M., Hendley, J.O., Simon, G., Jordan, W.S., Rhinovirus infections in an industrial population. I. The occurrence of illness (1967) N. Engl. J. Med., 275, pp. 1261-1268; Gwaltney Jr., J.M., The Jeremiah Metzger Lecture: Climatology and the common cold (1984) Trans. Am. Clin. Climatol. Assoc., 96, pp. 159-175; Gwaltney Jr., J.M., Rhinoviruses (1989) Viral Infections of Human, pp. 593-615. , A. S. Evans (ed.), Plenum Medical Book Co., New York, N.Y; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypiä, T., Hurskainen, P., Pallansch, M., Detection of enteroviruses and rhinoviruses in clinical specimens by polymerase chain reaction and liquid-phase hybridization (1995) J. Clin. Microbiol., 33, pp. 648-653; Harris, J.M., Gwaltney, J.M., Incubation periods of experimental rhinovirus infection and illness (1996) Clin. Infect. Dis., 23, pp. 1287-1290; Hayden, F.G., Kaiser, D.L., Albrecht, J.K., Intranasal recombinant alfa-2b interferon treatment of naturally occurring common colds (1988) Antimicrob. Agents Chemother., 32, pp. 224-230; Hayden, F.G., Hipskind, G.J., Woerner, D.H., Eisen, G.F., Janssens, M., Janssen, P.A.J., Andries, K., Intranasal pirodavir (R77, 975) treatment of rhinovirus colds (1995) Antimicrob. Agents Chemother., 39, pp. 290-294; Hyypiä, T., Auvinen, P., Maaronen, M., Polymerase chain reaction for human picornaviruses (1989) J. Gen. Virol., 70, pp. 3261-3268; Ireland, D.C., Kent, J., Nicholson, K.G., Improved detection of rhinoviruses in nasal and throat swabs by semi-nested RT-PCR (1993) J. Med. Virol., 40, pp. 96-101; Johnston, S.L., Sanderson, G., Pattermore, P.K., Smith, S., Bardin, P.G., Pruce, C.B., Lambden, P.R., Holgate, S.T., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J. Clin. Microbiol., 31, pp. 111-117; McBride, T.P., Doyle, W.J., Hayden, F.G., Gwaltney Jr., J.M., Alterations of the eustachian tube, middle ear, and nose in rhinovirus infection (1989) Arch. Otolaryngol. Head Neck Surg., 115, pp. 1054-1059; Myint, S., Harmsen, D., Raabe, T., Siddell, S.G., Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) J. Med. Virol., 31, pp. 165-172; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell. Probes, 8, pp. 357-364; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) Br. Med. J., 307, pp. 982-986; Pitkäranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus by reverse transcription PCR in sinus brushings of patients with acute community acquired sinusitis (1997) J. Clin. Microbiol., 35, pp. 1791-1793; Rao, S.S., Hendley, J.O., Hayden, F.G., Gwaltney Jr., J.M., Symptom expression in natural and experimental rhinovirus colds (1995) Am. J. Rhinol., 9, pp. 49-52; Vesanen, M., Piiparinen, H., Kallio, A., Vaheri, A., Detection of herpes simples virus DNA in cerebrospinal fluid samples using the polymerase chain reaction and microplate hybridization (1996) J. Virol. Methods, 59, pp. 1-11","Hayden, F.G.; Univ. of Virginia Hlth. Sci. Center, Box 473, Charlottesville, VA 22908, United States",,,00951137,,JCMID,"9350748","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-1842292104
"Glaus T., Hofmann-Lehmann R., Greene C., Glaus B., Wolfensberger C., Lutz H.","7005084886;7003867023;35425243500;57199629501;6701759869;35480426400;","Seroprevalence of Bartonella henselae infection and correlation with disease status in cats in Switzerland",1997,"Journal of Clinical Microbiology","35","11",,"2883","2885",,91,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030760603&partnerID=40&md5=122bfce5cfe3854b2364060d2b0ab8f4","Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland; Department of Small Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Dept. of Vet. Internal Medicine, University of Zurich, Winterthurerstr. 260, CH-8057 Zurich, Switzerland","Glaus, T., Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland, Dept. of Vet. Internal Medicine, University of Zurich, Winterthurerstr. 260, CH-8057 Zurich, Switzerland; Hofmann-Lehmann, R., Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland; Greene, C., Department of Small Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Glaus, B., Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland; Wolfensberger, C., Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland; Lutz, H., Dept. of Vet. Internal Medicine, University of Zurich, Zurich, Switzerland","The prevalence of infection with Bartonella henselae was investigated in cats from different areas of Switzerland. Serum samples of 728 cats were examined for antibodies to B. henselae by immunofluorescent antibody testing, and the results were analyzed with a view to a possible correlation between a positive titer and signalment, clinical signs, infection with feline leukemia virus (FeLV), feline immunodeficiency virus (FIV), feline coronavirus (FCoV), or feline spumavirus (FeSFV), and the living environments of the cats. The seroprevalence in all cats was 8.3%. No significantly different prevalence was found in sick versus healthy cats (9.2 versus 7.2%); however, in sick cats seropositive for B. henselae, there was an increased frequency of stomatitis and a variety of diseases of the kidneys and the urinary tract. There was an increased prevalence of B. henselae in cats positive for FCoV (P = 0.0185) or FeSFV (P = 0.0235) and no statistically significant increased prevalence in cats infected with FeLV or FIV. There was no correlation between a positive titer and sex or breed. The same prevalence of B. henselae antibodies was found in cats with and without access to the outdoors and in cats from single- and multicat households. The seroprevalence was increased in cats living south of the Alps (12.1%); however, this difference was not significant (P = 0.0616).",,"animal cell; animal model; animal tissue; article; bartonella henselae; cat; cat scratch disease; controlled study; geographic distribution; nonhuman; prevalence; priority journal; serodiagnosis; switzerland; Age Factors; Animals; Bartonella henselae; Cat Diseases; Cat-Scratch Disease; Cats; Coronavirus Infections; Cross-Sectional Studies; Feline Acquired Immunodeficiency Syndrome; Leukemia Virus, Feline; Leukemia, Feline; Retroviridae Infections; Spumavirus; Switzerland; Animalia; Bartonella henselae; Coronavirus; Felidae; Feline coronavirus; Feline immunodeficiency virus; Feline leukemia virus; Felis catus; Spumavirus","Allerberger, F., Schönbauer, M., Regnery, R.L., Dierich, M.P., Prävalenz von Rochalimaea henselae-Antikörpern bei Katzen in Oesterreich (1995) Wien. Tierärztl. Monschr., 82, pp. 40-43; Childs, J.E., Olson, J.G., Wolf, A., Cohen, N., Fakile, Y., Rooney, J.A., Bacellar, F., Regnery, R.L., Prevalence of antibodies to Rochalimaea species (cat scratch disease agent) in cats (1995) Vet. Rec., 136, pp. 519-520; Chomel, B.B., Abbott, R.C., Kasten, R.W., Floyd-Hawkins, K.A., Kass, P.H., Glaser, C.A., Pedersen, N.C., Koehler, J.E., Bartonella henselae prevalence in domestic cats in California: Risk factors and association between bacteremia and antibody titers (1995) J. Clin. Microbiol., 33, pp. 2445-2450; Chomel, B.B., Gurfield, A.N., Boulois, H.H., Kasten, R.W., Piemont, Y., Cat as a source of Bartonella henselae, the infectious agent of cat-scratch disease - Preliminary study in Paris (France) (1995) Recl. Med. Vet., 171, pp. 841-845; Chomel, B.B., Kasten, R.W., Floyd-Hawkins, K., Chi, B., Yamamoto, K., Roberts-Wilson, J., Gurfield, A.N., Koehler, J.E., Experimental transmission of Bartonella henselae by the cat flea (1996) J. Clin. Microbiol., 34, pp. 1952-1956; Dolan, M.J., Wong, M.T., Regnery, R.L., Jorgensen, J.H., Garcia, M., Peters, J., Drehner, D., Syndrome of Rochalimaea henselae adenitis suggesting cat scratch disease (1993) Ann. Intern. Med., 118, pp. 331-336; Greene, C.E., McDermott, M., Jameson, P.H., Atkins, C.L., Marks, A.M., Bartonella henselae infection in cats: Evaluation during primary infection, treatment, and rechallenge infection (1996) J. Clin. Microbiol., 34, pp. 1682-1685; Hadfield, T.L., Warren, R., Kass, M., Brun, E., Levy, C., Endocarditis caused by Rochalimaea henselae (1993) Hum. Pathol., 24, pp. 1140-1141; Higgins, J.A., Radulovic, S., Jaworski, D.C., Azad, A.F., Acquisition of the cat scratch disease agent Bartonella henselae by cat fleas (1996) J. Med. Entomol., 33, pp. 490-495; Hofmann-Lehmann, R., Holznagel, E., Ossent, P., Lutz, H., Parameters of disease progression in long-term experimental feline retrovirus (feline immunodeficiency virus and feline leukemia virus) infections: Hematology, clinical chemistry, and lymphocyte subsets (1997) Clin. Diagn. Lab. Immunol., 4, pp. 33-42; Jameson, P., Greene, C., Regnery, R., Dryden, M., Marks, A., Brown, J., Cooper, J., Greene, R., Prevalence of Bartonella henselae antibodies in pet cats throughout regions of North America (1995) J. Infect. Dis., 172, pp. 1145-1149; Koehler, J.E., Glaser, C.A., Tappero, J.W., Rochalimaea henselae infection: A new zoonosis with the domestic cat as reservoir (1994) JAMA, 271, pp. 531-535; Koehler, J.E., Quinn, F.D., Berger, T.G., LeBoit, P.E., Tappero, J.W., Isolation of Rochalimaea species from cutaneous and osseous lesions of bacillary angiomatosis (1992) N. Engl. J. Med., 327, pp. 1625-1631; Kölbl, S., Lutz, H., Die Infektion mit felinem Spumavirus (FeSFV): Häufigkeit bei Katzen in Oesterreich und Beziehung zur Infektion mit dem felinem Immunschwächevirus (FIV) (1992) Kleintierpraxis, 37, pp. 307-318; Lutz, H., Arnold, P., Hubscher, U., Egberink, H., Pedersen, N., Horzinek, M.C., Specificity assessment of feline T-lymphotropic lentivirus serology (1988) Zentralbl. Veterinaermed. Reihe B, 35, pp. 773-778; Lutz, H., Hauser, B., Horzinek, M., Die Diagnostik der felinen infektiösen Peritonitis mittels der Serologie (1984) Prakt. Tierarzt, 5, pp. 406-407; Lutz, H., Lehmann, R., Winkler, G., Kottwitz, B., Dittmer, A., Wolfensberger, C., Arnold, P., Das feline Immunschwächevirus in der Schweiz: Klinik und Epidemiologie im Vergleich mit dem Leukämie- Und dem Coronavirus (1990) Schweiz. Arch. Tierheilkd., 132, pp. 217-225; Lutz, H., Pedersen, N., Durbin, R., Theilen, G.H., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) J. Immunol. Methods, 56, pp. 209-220; Pedersen, N.C., Feline syncytium-forming virus infection (1986) Diseases of the Cat, pp. 268-272. , J. Holzworth (ed.), W. B. Saunders Co., Philadelphia, Pa; Pedersen, N.C., Boyle, D.F., Floyd, K., Infection studies in kittens using feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 363-367; Regnery, R.L., Olson, J.G., Perkins, B.A., Bibb, W., Serological response to ""Rochalimaea henselae"" antigen in suspected cat-scratch disease (1992) Lancet, 339, pp. 1443-1445; Regnery, R.L., Rooney, J.A., Johnson, A.M., Nesby, S.L., Manzewitsch, P., Beaver, K., Olson, J.G., Experimentally induced Bartonella henselae infections followed by challenge exposure and antimicrobial therapy in cats (1996) Am. J. Vet. Res., 57, pp. 1714-1719; Swiss Metereological Institute. Zurich, Switzerland; Tappero, J.W., Mohle-Boetani, J., Koehler, J.E., Swaminathan, B., Berger, T.G., LeBoit, P.E., Smith, L.L., Reingold, A.L., The epidemiology of bacillary angiomatosis and bacillary peliosis (1993) JAMA, 269, pp. 770-775; Ueno, H., Hohdatsu, T., Muramatsu, Y., Koyama, H., Morita, C., Does coinfection of Bartonella henselae and FIV induce clinical disorders in cats? (1996) Microbiol. Immunol., 40, pp. 617-620; Welch, D.F., Pickett, D.A., Slater, L.N., Steigerwalt, A.G., Brenner, D.J., Rochalimaea henselae sp. nov., a cause of septicemia, bacillary angiomatosis, and parenchymal bacillary peliosis (1992) J. Clin. Microbiol., 30, pp. 275-280; Zangwill, K.M., Hamilton, D.H., Perkins, B.A., Regnery, R.L., Plikaytis, B.D., Hadler, J.L., Cartter, M.L., Wenger, J.D., Cat scratch disease in Connecticut: Epidemiology, risk factors, and evaluation of a new diagnostic test (1993) N. Engl. J. Med., 329, pp. 8-13","Glaus, T.; Dept. of Veterinary Internal Med., University of Zurich, Winterthurerstr. 260, CH-8057 Zurich, Switzerland",,,00951137,,JCMID,"9350752","English","J. CLIN. MICROBIOL.",Article,"Final",,Scopus,2-s2.0-0030760603
"Nicholson K.G., Kent J., Hammersley V., Cancio E.","7103216939;57197399234;6603613082;16938383300;","Acute viral infections of upper respiratory tract in elderly people living in the community: Comparative, prospective, population based study of disease burden",1997,"British Medical Journal","315","7115",,"1060","1064",,264,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030710196&partnerID=40&md5=4788f00ffe6e55008a27c58dcb0c8ad5","Leicester University, School of Medicine, Dept. of Microbiology and Immunology, Leicester LE1 9HN, United Kingdom","Nicholson, K.G., Leicester University, School of Medicine, Dept. of Microbiology and Immunology, Leicester LE1 9HN, United Kingdom; Kent, J., Leicester University, School of Medicine, Dept. of Microbiology and Immunology, Leicester LE1 9HN, United Kingdom; Hammersley, V., Leicester University, School of Medicine, Dept. of Microbiology and Immunology, Leicester LE1 9HN, United Kingdom; Cancio, E., Leicester University, School of Medicine, Dept. of Microbiology and Immunology, Leicester LE1 9HN, United Kingdom","Objective: To evaluate the disease burden of upper respiratory infections in elderly people living at home. Design: Prospective surveillance of elderly people. Intervention: None. Setting: Leicestershire, England. Subjects: 533 subjects 60 to 90 years of age. Main outcome measures: Pathogens, symptoms, restriction of activity, duration of illness, medical consultations, interval between onset of illness and medical consultation, antibiotic use, admission to hospital, and death. Results: 231 pathogens were identified for 211 (43%) of 497 episodes for which diagnostic specimens were available: 121 (52%) were rhinoviruses, 59 (26%) were coronaviruses, 22 (9.5%) were influenza A or B, 17 (7%) were respiratory syncytial virus, 7 (3%) were parainfluenza viruses, and 3 (1%) were Chlamydia species; an adenovirus and Mycoplasma pneumoniae caused one infection each. Infections occurred at a rate of 1.2 episodes per person per annum (95% confidence interval 1.0 to 1.7; range 0-10) and were clinically indistinguishable. Lower respiratory tract symptoms complicated 65% of upper respiratory infections and increased the medical consultation rate 2.4-fold (χ2 test P &lt; 0.001). The median interval between onset of illness and medical consultation was 3 days for influenza and 5 days for other infections. Rhinoviruses caused the greatest disease burden overall followed by episodes of unknown aetiology, coronaviruses, influenza A and B, and respiratory syncytial virus. Conclusions: Respiratory viruses cause substantial morbidity in elderly people. Although respiratory syncytial virus and influenza cause considerable individual morbidity, the burden of disease from rhinovirus infections and infections of unknown aetiology seems greater overall. The interval between onset of illness and consultation together with diagnostic difficulties raises concern regarding the role of antiviral drugs in treating influenza.",,"antibiotic agent; antivirus agent; adenovirus; adult; aged; article; chlamydiaceae; clinical trial; comparative study; consultation; death; hospital admission; human; influenza virus a; influenza virus b; major clinical study; morbidity; mycoplasma pneumoniae; parainfluenza virus; priority journal; respiratory syncytial pneumovirus; rhinovirus; statistics; united kingdom; upper respiratory tract infection; virus infection; Aged; Aged, 80 and over; Anti-Bacterial Agents; Cost of Illness; England; Female; Hospitalization; Humans; Male; Middle Aged; Patient Acceptance of Health Care; Prospective Studies; Respiratory Tract Infections; Virus Diseases","Nicholson, K.G., Impact of influenza and respiratory syncytial virus on mortality in England and Wales from January 1975 to December 1990 (1996) Epidemiol Infect, 116, pp. 51-63; Nicholson, K.G., Baker, D.J., Farquhar, A., Hurd, D., Kent, J., Smith, S.H., Acute upper respiratory tract viral illness and influenza immunisation in homes for the elderly (1990) Epidemiol Infect, 105, pp. 609-618; Nicholson, K.G., Kent, J., Hammersley, V., Cancio, E., Risk factors for lower respiratory complications of rhinovirus infections in the community dwelling elderly: A prospective cohort study (1996) BMJ, 313, pp. 1119-1123; Monto, A.S., Bryan, E.R., Ohmit, S., Rhinovirus infections in Tecumseh, Michigan: Frequency of illness and number of serotypes (1987) J Infect Dis, 156, pp. 43-49; (1992) Immunisation Against Infectious Disease, , London: HMSO; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) BMJ, 307, pp. 982-986; Ireland, D.C., Kent, J., Nicholson, K.G., Improved detection of rhinovirus in nasal and throat swabs by semi-nested RT-PCR (1993) J Med Virol, 40, pp. 96-101; (1985) New Vaccine Development: Establishing Priorities. Vol I. Disease of Importance in the United States, 1, p. 51. , Washington DC: National Academy Press; Falsey, A.R., McCann, R.M., Hall, W.J., Tanner, M.A., Criddle, M.M., Formica, M.A., Acute respiratory tract infection in daycare centers for older persons (1995) J Am Geriatr Soc, 43, pp. 30-36; Monto, A.S., Ullman, B.M., Acute respiratory illness in an American community (1974) JAMA, 227, pp. 164-169; Monto, A.S., Cavallaro, J.J., The Tecumseh study of respiratory illness. II. Patterns of occurrence of infection with respiratory pathogens, 1965-1969 (1971) Am J Epidemiol, 94, pp. 280-289; Monto, A.S., Sullivan, K.M., Acute respiratory illness in the community. Frequency of illness and the agents involved (1993) Epidemiol Infect, 110, pp. 145-160; Kellner, G., Popow-Kraupp, T., Kundi, M., Binder, C., Kunz, C., Clinical manifestations of respiratory tract infections due to respiratory syncytial virus and rhinoviruses in hospitalized children (1989) Acta Paed Scand, 78, pp. 390-394; Horn, M.E.C., Brain, E., Gregg, I., Yealland, S., Inglis, J.M., Respiratory viral infection in childhood. A survey in general practice, Roehampton 1967-1972 (1975) J Hyg Camb, 74, pp. 157-168; Tannock, G.A., Reid, A.L.A., Gillett, S.M., Herd, R., Gillett, R.S., Hensley, M.J., A study of respiratory infections in a healthy adult population during the 1987 Australian winter (1993) Fam Pract, 10, pp. 378-385; Tyrrell, D.A.J., Cohen, S., Schlarb, J.E., Symptoms and signs in common colds (1993) Epidemiol Infect, 111, pp. 143-156; Falsey, A.R., Treanor, J.J., Betts, R.F., Walsh, E.E., Viral respiratory infections in the institutionalized elderly: Clinical and epidemiological findings (1992) J Am Geriatr Soc, 40, pp. 115-119; Thompson, J., Fleet, W., Lawrence, E., Pierce, E., Morris, L., Wright, P., A comparison of acetominophen and rimantadine in the treatment of influenza A infection in children (1987) J Med Virol, 21, pp. 249-255; Hall, C.B., Dolin, R., Gala, C.L., Makovitz, D.M., Zhang, Y.Q., Madore, P.H., Children with influenza A infection: Treatment with rimantadine (1987) Pediatrics, 80, pp. 275-282; Wingfield, W.L., Pollack, D., Grunert, R.R., Therapeutic efficacy of amantadine HCI and rimantadine HCI in naturally occurring influenza A2 respiratory illness in man (1969) N Engl J Med, 281, pp. 579-584; Galbraith, A.W., Oxford, J.S., Schild, G.C., Watson, G.I., Study of 1-adamantanamine hydrochloride used prophylactically during the Hong Kong influenza epidemic in the family environment (1969) Bull WHO, 41, pp. 677-682; Falsey, A.R., Cunningham, C.K., Barker, W.H., Kouides, R.W., Yuen, J.B., Menegus, M., Respiratory syncytial virus and influenza A infections in hospitalized elderly J Infect Dis, 172, pp. 389-394. , 995; Fleming, D.M., Cross, K.W., Crombie, D.L., Lancashire, R.J., Respiratory illness and mortality in England and Wales (1993) Eur J Epidemiol, 9, pp. 571-576","Nicholson, K.G.; Leicester University School Medicine, Department Microbiology Immunology, Leicester LE1 9HN, United Kingdom",,,09598146,,BMJOA,"9366736","English","BR. MED. J.",Article,"Final",,Scopus,2-s2.0-0030710196
"Kraeft S.-K., Chen D.S., Li H.-P., Chen L.B., Lai M.M.C.","6701368674;16165697600;9276641400;7409435067;7401808497;","Mouse hepatitis virus infection induces an early, transient calcium influx in mouse astrocytoma cells",1997,"Experimental Cell Research","237","1",,"55","62",,3,"10.1006/excr.1997.3768","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031586613&doi=10.1006%2fexcr.1997.3768&partnerID=40&md5=4f90331f891ecdd778a4eef2af42ccd2","Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, United States; Howard Hughes Medical Institute, Los Angeles, CA 90033-1054, United States; Dept. of Molec. Microbiol. and I., School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Inst. of Clin. Chem. and P., University of Rostock, Ernst-Heydemann-Strasse 6, D-18055 Rostock, Germany; Dana-Farber Cancer Institute, Div. of Cell. and Molecular Biology, 44 Binney Street, Boston, MA 02115, United States","Kraeft, S.-K., Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, United States, Inst. of Clin. Chem. and P., University of Rostock, Ernst-Heydemann-Strasse 6, D-18055 Rostock, Germany; Chen, D.S., Dept. of Molec. Microbiol. and I., School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Li, H.-P., Dept. of Molec. Microbiol. and I., School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States; Chen, L.B., Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, United States, Dana-Farber Cancer Institute, Div. of Cell. and Molecular Biology, 44 Binney Street, Boston, MA 02115, United States; Lai, M.M.C., Howard Hughes Medical Institute, Los Angeles, CA 90033-1054, United States, Dept. of Molec. Microbiol. and I., School of Medicine, University of Southern California, Los Angeles, CA 90033-1054, United States","Mouse hepatitis virus (MHV), a murine coronavirus, utilizes murine carcinoembryonic antigens as receptors. The events that follow virus-receptor binding and eventually lead to virus entry are poorly understood. We studied the possible effects of MHV infection on intracellular calcium in a mouse astrocytoma cell line. Using the calcium-sensitive dye fluo-3 and confocal laser scanning microscopy, we found that MHV strain JHM induced an immediate (within 20 s) and transient (lasting no longer than 2 min) calcium increase in about 5% of the infected cells. The calcium increase was blocked by antibodies against the viral spike protein, suggesting that it was specifically triggered by the interaction of the viral spikes with cells. It was also inhibited by L-type calcium channel blockers and was not detected in calcium-free medium, suggesting that the calcium increase was caused by calcium influx from the extracellular medium. Studies of the kinetics of viral replication by immunofluorescence staining of the viral nucleocapsid protein revealed that at 3 h postinfection there was roughly the same percentage of cells (5%) that produced the viral protein as the percentage of cells that had responded with a calcium signal. This finding and the virus dilution studies together suggest that calcium responders may represent cells that had been infected with multiple viruses and undergone rapid vital replication. Furthermore, calcium channel blockers, including verapamil and cadmium chloride, and the calcium chelator EGTA inhibited virus infection. Therefore, the transient intracellular calcium increase reported here may be an early signaling event associated with virus infection.","Confocal laser scanning microscopy; Fluo-3; Immunofluorescence; Intracellular calcium; Mouse astrocytoma cells; Mouse hepatitis virus","cadmium chloride; calcium channel blocking agent; calcium ion; egtazic acid; verapamil; animal cell; article; astrocytoma cell; calcium transport; cell membrane transport; confocal laser microscopy; controlled study; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; transport kinetics; virus cell interaction; virus replication; Animalia; Coronavirus; Hepatitis virus A; Murinae; Murine hepatitis virus","Compton, S.R., Barthold, S.W., Smith, A.L., (1993) Lab. Anim. Sci., 43, pp. 15-28; Williams, R.K., Jiang, G., Holmes, K.V., (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Lai, M.M.C., (1992) J. Virol., 66, pp. 6931-6938; Nedellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., (1994) J. Virol., 68, pp. 4525-4537; Chen, D.S., Asanaka, M., Yokomori, K., Wang, F., Hwang, S.B., Li, H., Lai, M.M.C., (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Lai, M.M.C., Cananagh, D., (1997) Adv. Virus Res., 48, pp. 1-100; Dreyer, E.B., Kaiser, P.K., Offermann, J.T., Lipton, S.A., (1990) Science, 248, pp. 364-367; Lo, T.-M., Fallert, C.J., Piser, T.M., Thayer, S.A., (1992) Brain Res., 594, pp. 189-196; Hartshorn, K.L., Collamer, M., Auerbach, M., Myers, J.B., Pavlotsky, N., Tauber, A.I., (1988) J. Immunol., 141, pp. 1295-1301; Kornfeld, H., Cruikshank, W.W., Pyle, S.W., Berman, J.S., Center, D.M., (1988) Nature, 335, pp. 445-448; Dayanithi, G., Yani, N., Baghdiguian, S., Fantini, J., (1995) Cell Calcium, 18, pp. 9-18; Michelangeli, F., Liprandi, F., Chemello, M.E., Ciarlet, M., Ruitz, M.-C., (1995) J. Virol., 69, pp. 3838-3847; Irurzun, A., Arroyo, J., Alvarez, A., Carrasco, L., (1995) J. Virol., 69, pp. 5142-5146; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Stohlman, S.A., Brayton, P.R., Fleming, J.O., Weiner, L.P., Lai, M.M.C., (1982) J. Gen. Virol., 63, pp. 265-275; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., (1983) Virology, 131, pp. 296-307; Burnier, M., Centeno, G., Burki, E., Brunner, H.R., (1994) Am. J. Physiol., 266, pp. C1118-C1127; Grynkiewicz, G., Poenie, M., Tsien, R.Y., (1985) J. Biol. Chem., 260, pp. 3440-3450; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., (1986) J. Virol., 58, pp. 869-875; Huang, R.C., (1993) J. Neurophysiol., 70, pp. 1692-1703; Asanaka, M., Lai, M.M.C., (1993) Virology, 197, pp. 732-741; Coutelier, J.P., Godfraind, C., Dveksler, G.S., Wysocka, M., Cardellichio, C.B., Noel, H., Holmes, K.V., (1994) Eur. J. Immunol., 24, pp. 1383-1390; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., (1995) Lab. Invest., 73, pp. 615-627; Hallett, M.B., Fuchs, P., Campbell, A.K., (1982) Biochem. J., 206, pp. 671-674; Pace, J., Hayman, M.J., Galan, J.E., (1993) Cell, 72, pp. 505-514","Chen, L.B.; Dana-Farber Cancer Institute, Div. of Cell. and Molecular Biology, 44 Binney Street, Boston, MA 02115, United States",,"Academic Press Inc.",00144827,,ECREA,"9417866","English","EXP. CELL RES.",Article,"Final",,Scopus,2-s2.0-0031586613
"Lacheretz A., Jurin C.","6603464024;6506314275;","Canine coronavirus infection : Epidemiology and diagnosis as compared to canine parvovirus infection [La coronavirose canine : Comparaisons épidémiologiques et diagnostiques avec la parvovirose]",1997,"Revue de Medecine Veterinaire","148","7",,"621","626",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031524704&partnerID=40&md5=d1529f1ca5fd80744e144d51a85d4fca",,"Lacheretz, A.; Jurin, C.","Feacal and serum samples from 128 pet dogs with gastroenteritis were screened for parvovirus (CPV) and coronavirus (CCV) infections. Fifty per cent of feacal samples were positive for canine parvovirus, 24% of serum specimens possessed antibodies to parvovirus, 19,5% to coronavirus, 8% to both parvovirus and coronavirus. The decrease of canine coronavirus infection in France may be explained by the generalization of the disinfection of kennels against canine parvovirus and the fact that coronavirus is less resistant than parvovirus. In other hands, by indirect immunofluorescence, the raise of specific anti-CCV Ig G is later than that of specific anti-CPV Ig G. That difference must be known for diagnosis of both canine parvovirus and coronavirus infections.","Coronavirus; Diagnosis; Dog; Epidemiology; Immunofluorescence; Parvovirus",,"Chappuis, G., Apport de la sérologie dans le diagnostic des maladies infectieuses du chien (1994) Point Vét., 26, pp. 39-44; Difruscia, R., Chalifoux, A., Elazhary, Y., Infections entériques à parvovirus et à coronavirus chez le chien : Fréquence au Québec (1991) Méd.Vét.Québec, 21, pp. 16-19; Everman, J.F., Eugster, A.K., Solozano, R.F., Collins, J.K., Black, J.W., Kim, J.S., Update on canine coronavirus infection and interactions with other enteric pathogens of the dog (1989) Companion Animal Proctice, 19, pp. 6-12; Lacheretz, A., Jurin, C., Epidémiologie et diagnostic de la parvovirose canine (1997) Rev. Méd. Vét., , à paraître; Maris, P., Virucidal efficacy of eight disinfectants against pneumovirus, coronavirus and parvovirus (1990) Ann. Rech. Vét., 21, pp. 275-279; Moraillon, R., Actualité sur la parvovirose canine (1994) Point Vét., 25, pp. 19-24; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Tennant, B.S., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Vet. Rec., 132, pp. 7-11; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Vet. Microbiol., 42, pp. 255-259; Toma, B., Moraillon, A., Infection du chien par un virus antigéniquement apparenté au virus de la gastro-entérite transmissible du porc (1980) Rec. Méd. Vét., 156, pp. 464-470",,,,00351555,,RVMVA,,"French","Rev. Med. Vet.",Article,"Final",,Scopus,2-s2.0-0031524704
"Nguyen V.-P., Hogue B.G.","57199220079;7003393593;","Protein interactions during coronavirus assembly",1997,"Journal of Virology","71","12",,"9278","9284",,81,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030782149&partnerID=40&md5=8a865f799b66193d2346809a82b188b8","Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States; Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Nguyen, V.-P., Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Hogue, B.G., Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States, Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States, Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Coronaviruses assemble and obtain their envelope at membranes of the intermediate compartment between the endoplasmic reticulum and Golgi complex. Like other enveloped viruses, coronavirus assembly is presumably dependent on protein localization and protein-protein as well as protein-RNA interactions. We have used the bovine coronavirus (BCV) as a model to study interactions between the viral proteins in virus-infected cells that are important for coronavirus assembly. BCV is a prototype for the coronaviruses that express an additional major structural protein, the hemagglutinin esterase (HE), in addition to the spike(S) glycoprotein, membrane (M) glycoprotein, and nucleocapsid (N) protein. Complexes consisting of the M, S, and HE proteins were detected in virus-infected cells by coimmunoprecipitations. Kinetic analyses demonstrated that S protein and HE each quickly formed a complex with M protein after synthesis, whereas heterocomplexes consisting of all three proteins formed more slowly. The kinetics of HE biosynthesis revealed that the half-life of oligomerization was ~30 min, which correlated with the appearance of complexes consisting of M, HE, and S proteins, suggesting that oligomerization and/or conformational changes may be important for the S-M- HE protein complexes to form. Only HE dimers were found associated with the heterocomplexes consisting of all three proteins. S-M-HE protein complexes were detected prior to processing of the oligosaccharide chains on HE, indicating that these protein complexes formed in a premedial Golgi compartment before trimming of sugar chains. Transient coexpressions and double-labeling immunofluorescence demonstrated that HE and S proteins colocalized with M protein. This was further supported by coimmunoprecipitation of specific HE-M and S-M protein complexes from transfected cells, indicating that these proteins can form complexes in the absence of other viral proteins.",,"capsid protein; esterase; virus glycoprotein; animal cell; article; conformational transition; controlled study; coronavirus; endoplasmic reticulum; golgi complex; human; human cell; immunofluorescence; immunoprecipitation; nonhuman; priority journal; protein localization; protein protein interaction; protein rna binding; virus assembly; virus envelope; Animals; Cattle; Cell Compartmentation; Cell Line; Cercopithecus aethiops; Coronavirus, Bovine; Cricetinae; Dimerization; Glycoproteins; Hela Cells; Hemagglutinins, Viral; Humans; Kinetics; Membrane Glycoproteins; Nucleocapsid; Subcellular Fractions; Tumor Cells, Cultured; Viral Envelope Proteins; Viral Fusion Proteins; Viral Matrix Proteins; Viral Proteins; Virus Assembly","Bos, E.C.W., Luytjes, W., Meulen, H.V.D., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995) The Coronaviridae, pp. 165-179. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Cavanagb, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , S. G. Siddell (ed.). Plenum Press, New York. N.Y; Cologna, R., Hogue, B.G., Unpublished data; Copeland, C.S., Zimmer, K.-P., Wagner, K.R., Healey, G.A., Mellman, I., Helenius, A., Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin (1988) Cell, 53, pp. 197-209; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J. Gen. Virol., 68, pp. 2863-2877; Dubois-Dalcq, M., Holmes, K.V., Rentier, B., (1984) Assembly of Enveloped Viruses, p. 236. , Springer-Verlag, Vienna, Austria; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Godet, M., L'Haridon, R., Vautherot, J.-F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Griffiths, G., Rottier, P., Cell biology of viruses that assemble along the biosynthetic pathway (1992) Semin. Cell Biol., 3, pp. 367-381; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J. 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Microbiol., 42, pp. 489-516; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in Sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell. Biol., 33, pp. 281-293; Tooze, J., Tooze, S.A., Warren, G., Site of addition of ,V-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 (1988) J. Cell Biol., 106, pp. 1475-1487; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhour, W.F., Horrinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Hogue, B.G.; Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; email: bhogue@bcm.tmc.edu",,,0022538X,,JOVIA,"9371586","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030782149
"Woods R.D.","7401706916;","Development of PCR-Based Techniques to Identify Porcine Transmissible Gastroenteritis Coronavirus Isolates",1997,"Canadian Journal of Veterinary Research","61","3",,"167","172",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031179490&partnerID=40&md5=b1847909aecb3301e27300d9d5a74baa","Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States","Woods, R.D., Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States","Sixteen isolates of transmissible gastroenteritis virus and one isolate of porcine respiratory coronavirus were characterized using RT-PCR amplification of 4 antigenic subsites in the site A epitope on the TGEV spike gene. The PCR products were digested with restriction enzymes Sau3AI and SspI and the sizes of the fragments were determined. Three different digestion patterns were observed with each enzyme. The recognition site for Sau3AI was missing in 1 isolate, was present in 13 isolates and 3 isolates had 2 sites. PCR-products with a single site had 3 different fragment sizes and the other isolates produced 2 fragments with different sizes. The SspI recognition site was not present in 5 isolates and 12 isolates had a single site that produced 2 fragments of different sizes. Based on the restriction fragment sizes, the 17 isolates were separated into 7 groups. Direct sequencing of the 455 bp nested set fragments demonstrated greater than 96% sequence homology among the 16 isolates and 100% homology in the 4 antigenic subsites in the conserved site A epitope. The groups are discussed in relation to their sequence homology and virulence. In vitro procedures have been developed to identify several porcine enteric coronavirus isolates at the strain level.",,"DNA fragment; epitope; restriction endonuclease; virus DNA; agar gel electrophoresis; animal; animal disease; article; cell line; chemistry; Coronavirus; genetics; isolation and purification; methodology; nucleotide sequence; polymerase chain reaction; radioimmunoassay; sequence homology; serodiagnosis; swine; swine disease; Transmissible gastroenteritis virus; virus infection; Animals; Base Sequence; Cell Line; Coronavirus; Coronavirus Infections; DNA Fragmentation; DNA Restriction Enzymes; DNA, Viral; Electrophoresis, Agar Gel; Epitopes; Gastroenteritis, Transmissible, of Swine; Neutralization Tests; Polymerase Chain Reaction; Radioimmunoassay; Sequence Homology, Nucleic Acid; Swine; Swine Diseases; Transmissible gastroenteritis virus","Siddell, S.C., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, H.D., Macnaughton, M.R., Pensaert, M.B., Van der Zeijst, B.A.M., Coronaviridae (1983) Intervirol, 20, pp. 181-189; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infectious peritonitis virus to coronaviruses of other species (1978) Arch Virol, 58, pp. 45-58; Laude, H., Rasschaert, D., Delmas, B., Godet, M., Gelfi, J., Charley, B., Molecular biology of transmissible gastroenteritis virus (1990) Vet Microbiol, pp. 23147-23154; Saif, L.J., Wesley, R.D., Transmissible Gastroenteritis (1992) Diseases of Swine. 7th Ed., pp. 362-386. , Leman AD, Straw BE, Mengeling WL, D'Allaire S, Taylor DJ, eds. Ames. Iowa: Iowa State University Press; Woods, R.D., Cheville, N.F., Gallagher, J.E., Lesions in the small intestine of newborn pigs inoculated with porcine, feline, and canine coronaviruses (1981) Am J Vet Res, 42, pp. 1163-1169; Liou, P.P., In vitro differentiation of transmissible gastroenteritis virus strains by plaque sizes in swine testis cell culture (1983) J Chinese Soc Vet Sci, 9, pp. 161-166; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet Microbiol, 36, pp. 333-347; Flruuchi, S., Shimizu, Y., Kumagai, T., Comparison of properties between virulent and attenuated strains of transmissible gastroenteritis virus (1975) Nat Inst Anim Health Q, 15, pp. 159-164; Aynaud, J.M., Bottreal, E., Brun, A., Effect of stomach and gut juices on infectivity of low and high passaged strains of T.G.E. [transmissible gastroenteritis] coronavirus: Properties of a virus mutant resistant to inactivation by stomach juice obtained by cycles of survivor selection in tissue culture [Swine] (1984) Adv Exp Med Biol, 173, pp. 387-388; Hess, R.G., Bachmann, P.A., In vitro differentiation and pH sensitivity of field and cell culture-attenuated strains of transmissible gastroenteritis virus (1976) Infect Immunol, 13, pp. 1642-1646; Woods, R.D., Humoral and cellular responses in swine exposed to transmissible gastroenteritis virus (1979) Am J Vet Res, 40, pp. 108-110; Callebaut, P., Correa, I., Pensaert, M., Jimenez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J Gen Virol, 69, pp. 1725-1730; Saiki, R.K., Gelfand, D.H., Stoffel, S., Scharf, S.F., Higuchi, R., Horng, T., Mullis, K.B., Erlich, H.A., Primer directed enzymatic amplification of DNA with a thermostable DNA polymerase (1988) Science, 239, pp. 487-491; Homberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res, 31, pp. 49-56; Millane, G., Michaud, L., Dea, S., Biological and molecular differentiation between coronaviruses associated with neonatal calf diarrhoea and winter dysentery in adult cattle (1994) Adv Exp Biol Med, 380, pp. 29-33; Jackwood, D.J., Kwon, H.M., Saif, L.J., Molecular differentiation of transmissible gastroenteritis virus and porcine respiratory coronavirus strains (1994) Adv Exp Biol Med, 380, pp. 35-41; Lai, C.H., Welter, M.W., Welter, L.M., The use of ARMS PCR and RFLP analysis in identifying genetic profiles of virulent, attenuated or vaccine strains of TGEV and PRCV (1994) Adv Exp Biol Med, 380, pp. 243-250; Rasschaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J Gen Virol, 68, pp. 1883-1890; Mcclurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from TGE (1966) Can J Comp Med, 30, pp. 190-198; Kemeny, L.J., Antibody response in pigs inoculated with transmissible gastroenteritis virus and cross reactions among ten strains (1976) Can J Comp Mod, 40, pp. 209-214; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J Vet Diagn Invest, 3, pp. 29-32; Woods, R.D., Wesley, R.D., Neutralization of porcine transmissible gastroenteri- Tis virus by complement-dependent monoclonal antibodies (1988) Am J Vet Res, 49, pp. 300-304; Wesley, R.D., Woods, R., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet Microbiol, 18, pp. 197-208; Correa, I., Jimenez, G., Sune, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res, 10, pp. 77-93; Ridpath, J.F., Bolin, S.R., Dubov, E.J., Segregation of bovine diarrhea virus into genotypes (1994) Virol, 205, pp. 66-74; Van Nieuwstadt, A.P., Boonstra, J., Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus. using monoclonal antibodies to antigenic site A and X of the S glycoprotein (1992) An J Vet Res, 53, pp. 184-190; Gebauer, F., Posthumus, W.P.A., Correa, I., Sune, C., Smerdou, C., Sanchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virol, 183, pp. 225-238; Eleoquet, T., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virol, 206, pp. 817-822","Woods, R.D.; Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States",,,08309000,,CJVRE,"9242995","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0031179490
"Schickli J.H., Zelus B.D., Wentworth D.E., Sawicki S.G., Holmes K.V.","6603027057;6602571243;57203154014;7004118344;7201657724;","The murine coronavirus mouse hepatitis virus strain A59 from persistently infected murine cells exhibits an extended host range",1997,"Journal of Virology","71","12",,"9499","9507",,40,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030730238&partnerID=40&md5=84e764c42721020f8a3853fd67684b56","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States; Molecular Biology Program, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States; Department of Microbiology, Medical College of Ohio, Toledo, Ohio 43699, United States; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 E. 9th Ave., Denver, CO 80262, United States","Schickli, J.H., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States; Zelus, B.D., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States; Wentworth, D.E., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States; Sawicki, S.G., Department of Microbiology, Medical College of Ohio, Toledo, Ohio 43699, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States, Molecular Biology Program, Univ. of Colorado Hlth. Sci. Center, Denver, Colorado 80262, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 E. 9th Ave., Denver, CO 80262, United States","In murine 17 CI 1 cells persistently infected with murine coronavirus mouse hepatitis virus strain A59 (MHV-A59), expression of the virus receptor glycoprotein MHVR was markedly reduced (S. G. Sawicki, J. H. Lu, and K. V. Holmes, J. Virol. 69:5535-5543, 1995). Virus isolated from passage 600 of the persistently infected cells made smaller plaques on 17 CI 1 cells than did MHV-A59. Unlike the parental MHV-A59, this variant virus also infected the BHK-21 (BHK) line of hamster cells. Virus plaque purified on BHK cells (MHV/BHK) grew more slowly in murine cells than did MHV-A59, and the rate of viral RNA synthesis was lower and the development of the viral nucleocapsid (N) protein was slower than those of MHV-A59. M MHV/BHK was 100-fold more resistant to neutralization with the purified soluble recombinant MHV receptor glycoprotein (sMHVR) than was MHV-A59. Pretreatment of 17 CI 1 cells with anti-MHVR monoclonal antibody CC1 protected the cells from infection with MHV-A59 but only partially protected them from infection with MHV/BHK. Thus, although MHV/BHK could still utilize MHVR as a receptor, its interactions with the receptor were significantly different from those of MHV-A59. To determine whether a hemagglutinin esterase (HE) glycoprotein that could bind the virions to 9-O-acetylated neuraminic acid moieties on the cell surface was expressed by MHV/BHK, an in situ esterase assay was used. No expression of HE activity was detected in 17 CI 1 cells infected with MHV/BHK, suggesting that this virus, like MHV-A59, bound to cell membranes via its S glycoprotein. MHV/BHK was able to infect cell lines from many mammalian species, including murine (17 CI 1), hamster (BHK), feline (Fcwf), bovine (MDBK), rat (RIE), monkey (Vero), and human (L132 and HeLa) cell lines. MHV/BHK could not infect dog kidney (MDCK I) or swine testis (ST) cell lines. Thus, in persistently infected murine cell lines that express very low levels of virus receptor MHVR and which also have and may express alternative virus receptors of lesser efficiency, there is a strong selective advantage for virus with altered interactions with receptor (D. S. Chen, M. Asanaka, F. S. Chen, J. E. Shively, and M. M. C. Lai, J. Virol. 71:1688-1691, 1997; D. S. Chen, M. Asanaka, K. Yokomori, F.-I. Wang, S. B. Hwang, H.-P. Li, and M. M. C. Lai, Proc. Natl. Acad. Sci. USA 92:12095-12099, 1995; P. Nedellec, G. S. Dveksler, E. Daniels, C. Turbide, B. Chow, A. A. Basile, K. V. Holmes, and N. Beauchemin, J. Virol. 68:4525-4537, 1994). Possibly, in coronavirus infected animals, replication of the virus in tissues that express low levels of receptor might also select viruses with altered receptor recognition and extended host range.",,"esterase; hemagglutinin; virus receptor; animal cell; animal experiment; article; cell adhesion; coronavirus; enzyme activity; hepatitis virus; mouse; nonhuman; priority journal; protein analysis; rna synthesis; virus infection; virus nucleocapsid; virus replication; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, CD; Cats; Cattle; Cell Adhesion Molecules; Cell Line; Cell Line, Transformed; Cercopithecus aethiops; Cricetinae; Dogs; Glycoproteins; Hela Cells; Hemagglutinins, Viral; Humans; Mice; Murine hepatitis virus; Neutralization Tests; Nucleocapsid; Rats; Recombinant Proteins; RNA, Viral; Solubility; Swine; Time Factors; Vero Cells; Viral Fusion Proteins; Viral Proteins; Virus Latency","Ahmed, R., Hahn, C.S., Somasundaram, T., Villarete, L., Matloubian, M., Strauss, J.H., Molecular basis of organ-specific selection of viral variants during chronic infection (1991) J. Virol., 65, pp. 4242-4247; Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. Virol., 71, pp. 1946-1955; Barnett, T.R., Drake, L., Pickle II, W., Human biliary glycoprotein gene: Characterization of a family of novel alternatively spliced RNAs and their expressed proteins (1993) Mol. Cell. Biol., 13, pp. 1273-1282; Beushausen, S., Dales, S., In vivo and in vitro models of demyelinating disease. XI. Tropism and differentiation regulate the infectious process of coronaviruses in primary explants of the rat CNS (1985) Virology, 141, pp. 89-101; Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. 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Virol., 67, pp. 1-8; Dveksler, G.S., Gagneten, S.E., Scanga, C.A., Cardellichio, C.B., Holmes, K.V., Expression of the recombinant anchorless N-terminal domain of mouse hepatitis virus (MHV) receptor makes hamster or human cells susceptible to MHV infection (1996) J. Virol., 70, pp. 4142-4145; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Edlund, M., Gaardsvoll, H., Bock, E., Obrink, B., Different isoforms and stock-specific variants of the cell adhesion molecule C-CAM (cell-CAM 105) in rat liver (1993) Eur. J. Biochem., 213, pp. 1109-1116; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Freimuth, P., A human cell line selected for resistance to adenovirus infection has reduced levels of the virus receptor (1996) J. Virol., 70, pp. 4081-4085; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus (1995) Lab. Invest., 73, pp. 615-627; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Hirano, A., Yant, S., Iwata, K., Korte-Sarfaty, J., Seya, T., Nagasawa, S., Wong, T.C., Human cell receptor CD46 is down regulated through recognition of a membrane-proximal region of the cytoplasmic domain in persistent measles virus infection (1996) J. 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Virol., 71, pp. 2535-2539; McCuaig, K., Rosenberg, M., Nedellec, P., Turbide, C., Beauchemin, N., Expression of the Bgp gene and characterization of mouse colon biliary glycoprotein isoforms (1993) Gene, 127, pp. 173-183; Montali, R.J., Scanga, C.A., Pernikoff, D., Wessner, D.R., Ward, R., Holmes, K.V., A common-source outbreak of callitrichid hepatitis in captive tamarins and marmosets (1993) J. Infect. Dis., 167, pp. 946-950; Murray, R.S., Cai, G.Y., Hoel, K., Zhang, J.Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primate central nervous system (1992) Virology, 188, pp. 274-284; Nedellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; Nedellec, P., Turbide, C., Beauchemin, N., Characterization and transcriptional activity of the mouse biliary glycoprotein 1 gene, a carcinoembryonic antigen-related gene (1995) Eur. J. Biochem., 231, pp. 104-114; Rao, P.V., Kumari, S., Gallagher, T.M., Identification of a contiguous 6-residue determinant in the MHV receptor that controls the level of virion binding to cells (1997) Virology, 229, pp. 336-348; Sawa, H., Kamada, K., Sato, H., Sendo, S., Kondo, A., Saito, I., Edlund, M., Obrink, B., C-CAM expression in the developing rat central nervous system (1994) Dev. Brain Res., 78, pp. 35-43; Sawicki, S.G., Lu, J.H., Holmes, K.V., Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from the epigenetic expression of the MHV receptor (1995) J. Virol., 69, pp. 5535-5543; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect. Immun., 6, pp. 501-507; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J. Virol., 62, pp. 4686-4690; Wagaman, P.C., Spence, H.A., O'Callaghan, R.J., Detection of influenza C virus by using an in situ esterase assay (1989) J. Clin. Microbiol., 27, pp. 832-836; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Wessner, D.R., Shick, P.C., Lu, J.-H., Cardellichio, C.B., Gagneten, S.E., Beauchemin, N., Holmes, K.V., Dveksler, G.S., Mutational Analysis of the Virus and Monoclonal Antibody Binding Sites in MHVR, the Cellular Receptor of the Murine Coronavirus MHV-A59, , Submitted for publication; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Banner, L.R., Lai, M.M., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Yokomori, K., Lai, M.M., Mouse hepatitis virus receptors: More than a single carcinoembryonic antigen (1994) Arch. Virol. Suppl., 9, pp. 461-471; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Zelus, B.D., Tanner, F., Wessner, D., Dveksler, G., Holmes, K.V., Unpublished data","Holmes, K.V.; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Campus Box B-175, 4200 E. 9th Ave., Denver, CO 80262, United States; email: kathryn.holmes@uchsc.edu",,,0022538X,,JOVIA,"9371612","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030730238
"Lamarre A., Yu M.W.N., Chagnon F., Talbot P.J.","7004646746;16940438900;57196797991;7102670281;","A recombinant single chain antibody neutralizes coronavirus infectivity but only slightly delays lethal infection of mice",1997,"European Journal of Immunology","27","12",,"3447","3455",,13,"10.1002/eji.1830271245","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031474553&doi=10.1002%2feji.1830271245&partnerID=40&md5=2b0fe648db487d00e66d91f201fa95ff","Laboratory of Neuroimmunovirology, Virology Research Center, Université du Québec, Laval, Que., Canada; Institute of Experimental Immunology, Department of Pathology, University of Zürich, Zürich, Switzerland; Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Lamarre, A., Laboratory of Neuroimmunovirology, Virology Research Center, Université du Québec, Laval, Que., Canada, Institute of Experimental Immunology, Department of Pathology, University of Zürich, Zürich, Switzerland; Yu, M.W.N., Laboratory of Neuroimmunovirology, Virology Research Center, Université du Québec, Laval, Que., Canada; Chagnon, F., Laboratory of Neuroimmunovirology, Virology Research Center, Université du Québec, Laval, Que., Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Virology Research Center, Université du Québec, Laval, Que., Canada, Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","The variable region genes of a murine anti-coronavirus monoclonal antibody (mAb) were joined by assembly polymerase chain reaction and expressed in Escherichia coil in a single chain variable fragment (scFv) configuration. After induction of expression, the expected 32-kDa protein was identified by Western immunoblotting with specific rabbit anti-idiotype antibodies. The scFv fragments were purified from soluble cytoplasmic preparations by affinity chromatography on nickel agarose, which was possible with an N-terminal but not with a C-terminal histidine tag. Purified scFv fragments retained the antigen-binding properties of the parental antibody, could inhibit its binding to viral antigens with apparently higher efficiency than monovalent antigen-binding (Fab) fragments, but neutralized viral infectivity with lower efficiency (about sevenfold at a molar level). To evaluate the usefulness of these smaller and less immunogenic molecules in the treatment of viral diseases, mice were treated with purified recombinant scFv fragments and challenged with a lethal viral dose. A small delay in mortality was observed for the scFv-treated animals. Therefore, even though the scFv could neutralize viral infectivity in vitro, the same quantity of fragments that partially protected mice in the form of Fab only slightly delayed virus-induced lethality when injected as scFv fragments, probably because of a much faster in vivo clearance: the biologic half-life was estimated to be about 6 min. Since a scFv derived from a highly neutralizing and protective mAb is only marginally effective in the passive protection of mice from lethal viral infection, the use of such reagents for viral immunotherapy will require strategies to overcome stability limitations.","Antibody; Immunotherapy; In vivo animal model; Infectious immunity-virus; Rodent","idiotypic antibody; virus antibody; virus antigen; affinity chromatography; animal experiment; article; coronavirus; escherichia coli; female; immunoblotting; male; mouse; nonhuman; polymerase chain reaction; priority journal; virus infection; virus infectivity; Amino Acid Sequence; Animals; Antibodies, Viral; Base Sequence; Coronavirus; Coronavirus Infections; Escherichia coli; Immunoglobulin Variable Region; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Rabbits; Recombinant Proteins","Wege, H., Siddell, S., Ter Meulen, V., (1982) Curr. Top. Microbiol. Immunol., 99, p. 165; Spaan, W., Cavanagh, D., Horzinek, M.C., (1990) Immunochemistry of Viruses. The Basis for Serodiagnosis and Vaccines, 2, p. 359. , van Regenmortel, M. H. V. and Neurath, A. R. (Eds.), Elsevier Science Publishers B. V., Amsterdam; Siddell, S., Wege, H., Ter Meulen, V., (1983) J. Gen. Virol., 64, p. 761; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., (1984) Virology, 132, p. 261; Daniel, C., Talbot, P.J., (1990) Virology, 174, p. 87; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., (1989) Virology, 168, p. 162; Lecomte, J., Cainelli-Gebara, V., Mercier, G., Mansour, S., Talbot, P.J., Lussier, G., Oth, D., (1987) Arch. Virol., 97, p. 123; Yokomori, K., Baker, S.C., Stohlman, S.A., Lai, M.M.C., (1992) J. Virol., 66, p. 2865; Lamarre, A., Talbot, P.J., (1995) J. Immunol., 154, p. 3975; Mountain, A., Adair, J.R., (1992) Biotechnol. Genet. Eng. Rev., 10, p. 1; Lefranc, G., Lefranc, M.P., (1990) Biochimie, 72, p. 639; Ward, E.S., (1992) FASEB J., 6, p. 2422; Chanock, R.M., Crowe Jr., J.E., Murphy, B.R., Burton, D.R., (1993) Infect. Agents Dis., 2, p. 118; Daniel, C., Talbot, P.J., (1987) Arch. Virol., 96, p. 241; Mounir, S., Talbot, P.J., (1992) J. Gen. Virol., 73, p. 2731; Ward, E.S., Güssow, D., Griffiths, A.D., Jones, P.T., Winter, G., (1989) Nature, 341, p. 544; Orlandi, R., Güssow, D.H., Jones, P.T., Winter, G., (1989) Proc. Natl. Acad. Sci. USA, 86, p. 3833; Clackson, T., Hoogenboom, H.R., Griffiths, A.D., Winter, G., (1991) Nature, 352, p. 624; McCafferty, J., Griffiths, A.D., Winter, G., Chiswell, D.J., (1990) Nature, 348, p. 552; Sanger, F., Nicklen, S., Coulson, A.R., (1977) Proc. Natl. Acad. Sci. USA, 74, p. 5463; Laemmli, U.K., (1970) Nature, 227, p. 680; Lamarre, A., Lecomte, J., Talbot, P.J., (1991) J. Immunol., 147, p. 4256; Talbot, P.J., Salmi, A.A., Knobler, R.L., Buchmeier, M.J., (1984) Virology, 132, p. 250; Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K., Pease, L.R., (1977) Gene, 77, p. 61; Huston, J.S., Levinson, D., Mudgett-Hunter, M., Tai, M.S., Novotny, J., Margolies, M.N., Ridge, R.J., Oppermann, H., (1988) Proc. Natl. Acad. Sci. USA, 85, p. 5879; Winter, E., Radbruch, A., Krawinkel, U., (1985) EMBO J., 4, p. 2861; Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S., Foeller, C., (1991) Sequences of Proteins of Immunological Interest, 5th Ed., p. 2597. , National Institutes of Health, Bethesda; Lawler, A.M., Kearney, J.F., Kuehl, M., Gearhart, P.J., (1989) Proc. Natl. Acad. Sci. USA, 86, p. 6744; Avner, B., Swindell, L., Sharp, E., Liao, S.K., Ogden, J.R., Avner, B.P., Oldham, R.K., (1991) Mol. Biother., 3, p. 14; Barbas III, C.F., Björling, E., Chiodi, R., Dunlop, N., Cababa, D., Jones, T.M., Zebedee, S.L., Burton, D.R., (1992) Proc. Natl. Acad. Sci. USA, 89, p. 9339; Cheung, S.C., Dietzschold, B., Koprowski, H., Hotkins, A.L., Rando, R.F., (1992) J. Virol., 66, p. 6714; Barbas III, C.F., Crowe Jr., J.E., Cababa, D., Jones, T.M., Zebedee, S.L., Murphy, B.R., Chanock, R.M., Burton, D.R., (1992) Proc. Natl. Acad. Sci. USA, 89, p. 10164; Jiang, W., Bonnert, T.P., Venugopal, K., Gould, E.A., (1994) Virology, 200, p. 21; Lake, D.F., Lam, K.S., Peng, L., Hersh, E.M., (1994) Mol. Immunol., 31, p. 845; Colcher, D., Bird, R., Roselli, M., Hardman, K.D., Johnson, S., Pope, S., Dodd, S.W., Schlom, J., (1990) J. Natl. Cancer Inst., 82, p. 1191; Friedman, P.N., Chace, D.F., Trail, P.A., Siegall, C.B., (1993) J. Immunol., 150, p. 3054; Laroche, Y., Demaeyer, M., Stassen, J.M., Gansemans, Y., Demarsin, E., Matthyssens, G., Collen, D., Holvoet, P., (1991) J. Biol. Chem., 266, p. 16343; Reiter, Y., Pai, L.H., Brinkmann, U., Wang, Q.C., Pastan, I., (1994) Cancer Res., 54, p. 2714; Kalinke, U., Krebber, A., Krebber, C., Bucher, E., Plückthun, A., Zinkernagel, R.M., Hengartner, H., (1996) Eur. J. Immunol., 26, p. 2801; Cumber, A.J., Ward, E.S., Winter, G., Parnell, G.D., Wawrzynczak, E.J., (1992) J. Immunol., 149, p. 120; Benhar, I., Pastan, I., (1995) J. Biol. Chem., 270, p. 23373","Talbot, P.J.; Centre de recherche en virologie, Instutut Armand-Frappier, Universite du Quebec, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,,00142980,,EJIMA,"9464834","English","Eur. J. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0031474553
"Wang Y., Zhang J., Yu Z.-X., Detrick B., Hooks J.J.","56802808200;7601342242;57199729136;7003911483;7006661655;","Retinal apoptosis in virus - induced retinopathy is associated with the acute infectious disease and not with the late degenerative disease",1997,"Investigative Ophthalmology and Visual Science","38","4",,"","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749112619&partnerID=40&md5=2c545839d14efccd7cce1d382c691627","NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States","Wang, Y., NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States; Zhang, J., NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States; Yu, Z.-X., NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States; Detrick, B., NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States; Hooks, J.J., NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States","Purpose. Apoptosis occurs in JHM virus infected mouse retinas. In order to determine if apoptosis contributes to retinal degeneration, we evaluated the time and dose response of virus infection associated with apoptosis within the retinas of Iwo strains of mice and three virus permissive cell cultures. Methods. In vivo. BALB/c and CD-1 mice were inoculated with coronavirus. JHM strain, or media by the intravitreal route. In vitro, mouse macrophages, liver cells, and L2 cells were infected with JHM virus. At varying times after inoculation, mouse retinas and cells were assayed by terminal deoxynucleotidyl transferase conjugated-dUTP nick end labeling (TUNEL), double-staining. DNA laddering and electron microscopy (EM) to detect apoptosis. Results. Virus infection in BALB/c and CD-1 mice resulted in widespread apoptosis within the retina during the acute phase of the disease (day 1-10). Feu apoptotic cells were observed after 20 days, when infectious virus was absent and viral RNA persisted. Double-staining and EM demonstrated that the apoptotic cells were not macrophages, the predominant infiltrating cell, but rather resident retina cells within the outer nuclear layer. This finding correlated apoptosis with acute infection in a mouse strain that was retinal degeneration susceptible (BALB/c) and in a mouse strain that was retinal degeneration resistant (CD-1 ). Temporally related to retinal apoptosis was the presence of CDS+ T cells and the cytokine. TNF-a. both of which trigger apoptotic events. In vitro studies demonstrated that the munne coronavirus. JHM strain, did not induce apoptosis directly. This inability to induce apoptosis may correlate with the viruses ability to persist within the host. Conclusions. Retinal apoptosis appears to be an indirect result of coronavirus infection and is likely to reflect host mechanisms of virus-elimination within the retina. Furthermore, in this model system, induction of retinal apoptosis is insufficient, by itself, to trigger retinal degeneration.",,,,"Wang, Y.; NEI, NHLBI, National Institutes of Health, Bethesda, MD, United States",,,01460404,,IOVSD,,"English","Invest. Ophthalmol. Vis. Sci.",Article,"Final",,Scopus,2-s2.0-33749112619
"Dessau R.B.","6603866036;","Coronavirus hos patienter med dissemineret sklerose",1997,"Ugeskrift for Laeger","159","25",,"3973","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33748198706&partnerID=40&md5=ab4ddad87b017bcd6beb75896fae965b","Sauntesvej 31, 2820 Gentofte, Denmark","Dessau, R.B., Sauntesvej 31, 2820 Gentofte, Denmark",[No abstract available],,,,,,,00415782,,UGLAA,,"Danish","Ugeskr. Laeg.",Article,"Final",,Scopus,2-s2.0-33748198706
"Wesley R.D., Woods R.D., McKean J.D., Senn M.K., Elazhary Y.","7103154080;7401706916;7005834645;7007011972;7003751362;","Prevalence of Coronavirus Antibodies in Iowa Swine",1997,"Canadian Journal of Veterinary Research","61","4",,"305","308",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031243957&partnerID=40&md5=ad77271438cc916165a54fca06b30ad9","Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States; College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Faculty of Veterinary Medicine, University of Montreal, C.P. 5000, Saint-Hyacinthe, Que. J2S 7C6, Canada","Wesley, R.D., Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States; Woods, R.D., Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States; McKean, J.D., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Senn, M.K., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Elazhary, Y., Faculty of Veterinary Medicine, University of Montreal, C.P. 5000, Saint-Hyacinthe, Que. J2S 7C6, Canada","Three hundred and forty-seven serum samples from 22 Iowa swine herds were screened for TGEV/ PRCV neutralizing antibody. Ninety-one percent of the sera and all 22 herds were positive. These sera were then tested by the blocking ELISA test to distinguish TGEV and PRCV antibody. The ELISA test confirmed the high percentage of TGEV/PRCV positive sera. By the blocking ELISA test, 12 herds were PRCV positive, 6 herds were TGEV positive and 4 herds were mixed with sera either positive for TGEV or PRCV antibody. The results suggest a recent increase in TGEV/PRCV seroprevalence in Iowa swine most likely due to subclinical PRCV infections.",,"virus antibody; animal; animal disease; antibody specificity; article; blood; Coronavirus; enzyme linked immunosorbent assay; immunology; methodology; prevalence; swine; swine disease; United States; virus infection; Animals; Antibodies, Viral; Antibody Specificity; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Gastroenteritis, Transmissible, of Swine; Iowa; Prevalence; Swine; Swine Diseases","Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., pp. 362-386. , Leman A, Straw B, Mengeling W, D'Allaire S, Taylor D, eds. Ames, Iowa: Iowa State University Press; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373; Hill, H., Biwer, J., Woods, R., Wesley, R., Porcine respiratory coronavirus isolated from two U.S swine herds (1990) Proc Am Assoc Swine Practitioners, pp. 333-335; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; National Animal Health Monitoring System Survey (Data Collection: 1989-1990) (1991) Tech Rep USDA:APHIS:VS, , USDA:APHIS:VS; Egan, I.T., Harris, D.L., Hill, H.T., Prevalence of swine dysentery, transmissible gastroenteritis, and pseudorabies in Iowa, Illinois and Missouri swine (1982) Proc US Anim Health Assoc, 86, pp. 497-502; Callebaut, P., Correa, I., Pensaert, M., Jimenez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J Gen Virol, 69, pp. 1725-1730; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19; Jabrane, A., Elazhary, Y., Talbot, B.G., Ethier, R., Dubuc, C., Assaf, R., Porcine respiratory coronavirus in Quebec: Serological studies using a competitive inhibition enzyme-linked immunosorbent assay (1992) Can Vet J, 33, pp. 727-733; Senn, M.K., Mckean, J.D., Performance and economic evaluation of two treatment protocols in commingled segregated early weaned pigs (1996) Proc int Pig Vet Soc Congr, 14, p. 488; Elazhary, Y., Jabrane, A., Talbot, B.G., Porcine respiratory coronavirus isolated from young piglets in Quebec (1992) Vet Rec, 130, p. 500","Wesley, R.D.; Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States",,,08309000,,CJVRE,"9342456","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0031243957
"Saeki K., Ohtsuka N., Taguchi F.","36854828200;7005191275;7103209890;","Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor- resistant mutants",1997,"Journal of Virology","71","12",,"9024","9031",,61,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030780569&partnerID=40&md5=6ede7b3c494231b4a7cc3362b736e920","Div. of Anim. Models of Hum. Dis., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Saeki, K., Div. of Anim. Models of Hum. Dis., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Ohtsuka, N., Div. of Anim. Models of Hum. Dis., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Taguchi, F., Div. of Anim. Models of Hum. Dis., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","We previously demonstrated by site-directed mutagenesis analysis that the amino acid residues at positions 62 and 214 to 216 in the N-terminal region of mouse hepatitis virus (MHV) spike (S) protein are important for receptor-binding activity (H. Suzuki and F. Taguchi, J. Virol. 70:2632-2636, 1996). To further identify the residues responsible for the activity, we isolated the mutant viruses that were not neutralized with the soluble form of MHV receptor proteins, since such mutants were expected to have mutations in amino acids responsible for receptor-binding activity. Five soluble- receptor-resistant (srr) mutants isolated had mutations in a single amino acid at three different positions: one was at position 65 (Leu to His) (srr11) in the S1 subunit and three were at position 1114 (Leu to Phe) (srr3, srr4, and srr7) and one was at position 1163 (Cys to Phe) (srr18) in the S2 subunit. The receptor-binding activity examined by a virus overlay protein blot assay and by a coimmunoprecipitation assay showed that srr11 S protein had extremely reduced binding activity, while the srr7 and srr18 proteins had binding activity similar to that of wild-type c1-2 protein. However, when cell surface receptors were used for the binding assay, all srr mutants showed activity similar to that of the wild type or only slightly reduced activity. These results, together with our previous observations, suggest that amino acids located at positions 62 to 65 of S1, a region conserved among the MHV strains examined, are important for receptor-binding activity. We also discuss the mechanism by which srr mutants with a mutation in S2 showed high resistance to neutralization by a soluble receptor, despite their sufficient level of binding to soluble receptors.",,"receptor protein; spike protein; unclassified drug; virus protein; animal cell; article; cell strain bhk; murine hepatitis coronavirus; nonhuman; priority journal; receptor binding; virus mutant; virus neutralization; Animals; Binding Sites; Cell Line; Cricetinae; Glycoproteins; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutagenesis, Site-Directed; Precipitin Tests; Receptors, Virus; Solubility; Viral Envelope Proteins","Chen, D.S., Asanaka, M., Yokomori, K., Wang, F., Hwang, S.B., Li, H., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion (1982) Virology, 119, pp. 358-371; Colston, E., Racaniello, V.R., Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor (1994) EMBO J., 13, pp. 5855-5862; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van Der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike of coronaviruses (1987) J. Mol. Biol., 196, pp. 963-966; Dunning, A.M., Talmud, P., Humphries, S.E., Errors in the polymerase chain reaction (1988) Nucleic Acids Res., 16, p. 10393; Dveksler, G.S., Diffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G., Holmes, K.V., Diffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Diffenbach, C.W., Cardeilichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated and has a reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Flory, E., Pfleiderer, M., Stuhler, A., Wege, H., Induction of protective immunity against coronavirus-induced encephalomyelitis: Evidence for an important role of CD8+ T cells in vivo (1993) Eur. J. Immunol., 23, pp. 1757-1761; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Fuerst, T.R., Earl, P.L., Moss, B., Use of hybrid vaccinia virus-T7 RNA polymerase system for the expression of target genes (1987) Mol. Cell. Biol., 7, pp. 2538-2544; Gallagher, T.M., Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein (1996) J. Virol., 70, pp. 4683-4690; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J. Virol., 71, pp. 3129-3137; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Holmes, K.V., Doller, E.W., Behnke, J.N., Analysis of the function of coronavirus glycoprotein by differential inhibition of synthesis with tunicamycin (1981) Adv. Exp. Med. Biol., 142, pp. 133-142; Kaplan, G., Peters, D., Racaniello, V.R., Poliovirus mutants resistant to neutralization with soluble cell receptors (1990) Science, 250, pp. 1596-1599; Kubo, H., Takase, S.Y., Taguchi, F., Neutralization and fusion inhibition activities of monoclonal antibodies specific for the S1 subunit of the spike protein of neurovirulent murine coronavirus JHMV cl-2 variant (1993) J. Gen. Virol., 74, pp. 1421-1425; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus strain, JHM, in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Lai, M.M.C., Coronaviruses: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Matsubara, Y., Watanabe, R., Taguchi, F., Neurovirulence of six different murine coronavirus JHMV variants for rats (1991) Virus Res., 20, pp. 45-58; McCuaig, K., Rosenberg, M., Nedellec, P., Turbide, C., Beauchemin, N., Expression of the Bgp gene and characterization of mouse colon biliary glycoprotein isoforms (1993) Gene, 127, pp. 173-183; Nedellec, P., Dveksler, G.S., Daniels, E., Turbide, E., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; Ohtsuka, N., Yamada, Y.K., Taguchi, F., Difference in virus- Binding activity of two distinct receptor proteins for mouse hepatitis virus (1996) J. Gen. Virol., 77, pp. 1683-1692; Routledge, E., Stauber, R., Pfleiderer, M., Siddell, S.G., Analysis of murine coronavirus surface glycoprotein functions by using monoclonal antibodies (1991) J. Virol., 65, pp. 254-262; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Siddell, S.G., The coronaviridae, an introduction (1995) Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stauber, R., Pfleiderer, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Sturman, L.S., Holmes, K.V., Proteolytic cleavage of peplomer glycoprotein E2 of MHV yields two 90 K subunits and activates cell fusion (1984) Adv. Exp. Med. Biol., 173, pp. 25-35; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; Taguchi, F., Fleming, J.O., Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein (1989) Virology, 169, pp. 233-235; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; Taguchi, F., Yamada, A., Fujiwara, K., Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: Enhanced antiviral activity of macrophages (1980) Infect. Immun., 29, pp. 42-49; Vennema, H., Hejnen, L., Zijderfeld, A., Horziek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implication for virus assembly (1990) J. Virol., 64, pp. 339-346; Wang, F.-I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic site affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, H., Siddell, S.G., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; email: taguchi@ncnaxp.ncnp.go.jp",,,0022538X,,JOVIA,"9371559","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030780569
"Pohlenz J.","7005663687;","Observations on the diagnosis of the respiratory diseases of swine [A sertés légzoszervi megbetegedéseinek kórjelzéséhez]",1997,"Magyar Allatorvosok Lapja","119","8",,"464","466",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3342902984&partnerID=40&md5=a1674c5c521dcd888c0d1b182285f037","Institut für Pathologie, Tierarztlichen Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany","Pohlenz, J., Institut für Pathologie, Tierarztlichen Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany","Anatomical characteristics of the lungs of swine have been summarized together with the pathological and histopathological characteristics of certain respiratory diseases that promote the confirmation of the etiological diagnosis. Judgment of the pathological changes of the lungs has been highlighted. Of the virus infections in swine, respiratory changes caused by influenza-A, porcine coronavirus. Aujeszky's disease virus and arteri- (Lelystad-) virus have been detailed. Of the bacterial infections, pneumoniae caused by mycoplasmas, Actinobacillus pleuropneumoniae, bordetellosis, pasteurellosis and certain pyogenous bacteria have been reported. Frequent occurrence of mixed infections has been emphasized. Especially the virus infections and Mycoplasma byopneumoniae play as ""door openers"" and cause secondary complications with other bacteria present in the upper respiratory tract. Thus pathologist hardly never find pneumonia caused by one of the before mentioned pathogens. The author has referred also that under certain conditions parasitic (Metastrongyli and Ascaris larvae) infestation of porcine lungs has also occurred.",,,,"Pohlenz, J.; Institut für Pathologie, Tierarztlichen Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Article,"Final",,Scopus,2-s2.0-3342902984
"Aymard M., Lina B., Thouvenot D., Luciani J., Stagnara J.","55306003900;7006493939;7005288678;57198192269;56255271800;","A five year survey of respiratory syncytial virus infections in outpatients",1997,"Pediatric Pulmonology","24","SUPPL. 16",,"310","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33748575962&partnerID=40&md5=0bcb698184ef842e7b3f68b342635590","Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France; General Practitioners and Pediatricians, Rhône-Alpes, France","Aymard, M., Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France, General Practitioners and Pediatricians, Rhône-Alpes, France; Lina, B., Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France, General Practitioners and Pediatricians, Rhône-Alpes, France; Thouvenot, D., Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France, General Practitioners and Pediatricians, Rhône-Alpes, France; Luciani, J., Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France, General Practitioners and Pediatricians, Rhône-Alpes, France; Stagnara, J., Laboratory of Virology, National Influenza Reference Centre, CHU de Lyon, Lyon, France, General Practitioners and Pediatricians, Rhône-Alpes, France","The incidence of RSV in respiratory diseases observed in outpatients is less known than in hospitals. To evaluate its pathogenic role in communityacquired respiratory diseases, a network of surveillance is required. Such a network is already established in Rhône-Alpes, France since 1987, for the detection and isolation of Influenza strains. This network (Groupe Régional D'Observation de la Grippe or GROG) includes 50 general practitioners and 25 pediatricians and collects nasal swabs each year from October to April in patients suffering of an influenza-like disease (ILD). These swabs also allow detection and/or cultivation of respiratory viruses such as RSV, adenovirus, parainfluenza, rhinovirus and coronavirus. RSV was detected in clinical samples by an immunofluorescent assay or an ELISA test. During the last five years, 6254 swabs were collected, allowing to detect 367 isolates (annual mean: 73.4, range: 52-117). During each surveillance, a peak of isolation of RSV was clearly identified, varying in starting time, duration and intensity. During these peaks, RSV represented up to 68.5% of the isolates recovered from the swabs during a week. In pédiatrie practice, during the peak of incidence, RSV was detected in up to 30% of the samples. As for influenza, the variation in the percentage of positive swabs was well correlated to the criteria ILD/practician/week, but mostly to the number of bronchiolitis per ILD observed. In general practice, RSV infections were mainly detected in children below 5 years (77%), but were also observed in adults over 20 (14.2%). In outpatients, the more frequently reported clinical symptoms related to an RSV infection were: mild fever, clear nasal secretion, cough associated to bronchiolitis, but no or rare general symptoms such as headache, myalgia or asthenia. As other respiratory viruses were co-circulating, 5% of the RSV isolates were associated with other viruses (influenza, coronavirus, rhinovirus, adenovirus). The outpatients epidemic periods were compared to those occurring in hospital during the last 5 years. They did not regularly occur at the same time. During the last five years, the GROG was a satisfactory alert network for RSV, even if it was not specifically established for its surveillance. It allowed the comparison of successive annual epidemics. It could be of use for both implementation and evaluation of preventive therapy. Nevertheless, it would be necessary to fulfill epidemiological requirements as determining the denominator and the representativity of the sampling. © 1997 Wiley-Liss, Inc.",,,,"Aymard, M.; General Practitioners and Pediatricians, Rhône-Alpes, France",,,87556863,,PEPUE,,"English","Pediatr. Pulmonol.",Article,"Final",,Scopus,2-s2.0-33748575962
"Chanarin N., Miles J., Beasley R., Holgate S.T., Johnston S.L.","6602208370;57213874044;56666971400;7201795361;7401781716;","Seasonal distribution of episodes of acute severe asthma in adults",1997,"Thorax","52","SUPPL. 6",,"","",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0008250527&partnerID=40&md5=769f567b3aa923d98a7ed1c5de5d9311","University Medicine, Centre Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom; Department of Medicine, School of Medicine, P.O. Box 7343, Wellington South, New Zealand","Chanarin, N., University Medicine, Centre Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom; Miles, J., Department of Medicine, School of Medicine, P.O. Box 7343, Wellington South, New Zealand; Beasley, R., Department of Medicine, School of Medicine, P.O. Box 7343, Wellington South, New Zealand; Holgate, S.T., University Medicine, Centre Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom; Johnston, S.L., University Medicine, Centre Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom","The role of viruses as precipitants of acute severe asthma is well recognised. It might thus be expected that admissions with acute severe asthma would be highest in the winter months when viral infections are at their peak. We studied all young adults (16-45 years) admited with asthma at Southampton General Hospital, UK and Wellington, NZ. All subjects were asked about symptoms of recent or current infections and nasal aspirate was collected for viral isolation. Viral detection used PCR to detect the presence of human rhinovirus and coronaviruses 229E and OC43. The study ran for one year. 132 episodes of asthma were recorded, 43 UK and 89 NZ. The graph below shows a peak in admissions in late spring early summer. The peak was seen in both the UK and NZ and corresponded to the peak in reported subjective infections and in virus detection. (Graph Presented) The peak in admission occurred earlier than predicted if viral infection were the major factor in these exacerbation's. The peak corresponds to the seasonal peak seen in asthma death rates (Campbell M J et al. ""Age-specific seasonality of asthma deaths"" BMJ 1997(In Press)). The peak suggests that additional factors, including viral infection, are important in acute severe exacerbations of asthma in adults.",,,,"Chanarin, N.; University Medicine, Centre Block, Southampton General Hospital, Southampton SO16 6YD, United Kingdom",,,00406376,,THORA,,"English","Thorax",Article,"Final",,Scopus,2-s2.0-0008250527
"Couch R.B.","7102611225;","Respiratory viral infections in immunocompetent and immunocompromised persons",1997,"American Journal of Medicine","102","3A",,"2","9",,206,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031007965&partnerID=40&md5=2c4e4a40149d2de81df1f5653bd6f845","Department of Microbiology and Immunology, Baylor College of Medicine and Section of Infectious Diseases, University of Texas M.D. Anderson Cancer Center, Houston, TX, United States","Couch, R.B., Department of Microbiology and Immunology, Baylor College of Medicine and Section of Infectious Diseases, University of Texas M.D. Anderson Cancer Center, Houston, TX, United States","The acute respiratory illnesses are the most common type of acute illness in the United States today. The respiratory viruses - which include influenza viruses, parainfluenza viruses, respiratory syncytial virus (RSV), rhinoviruses, coronaviruses, and adenoviruses - cause the majority of these illnesses. Some of these viruses cause illness throughout the year, whereas others are most common in winter. All population groups experience these infections and illnesses. As the number of elderly persons and those with underlying disease increases, awareness is growing that these common infections can have serious consequences. This has recently been emphasized for immunocompromised persons. At the M.D. Anderson Cancer Center (MDACC), infection surveillance of mostly hospitalized adults with leukemia or a recent bone marrow transplant yielded a respiratory virus from 181 of 668 (27.1%) respiratory illness episodes. In descending order of frequency, infections with RSV, rhinoviruses, influenza viruses, parainfluenza viruses, and adenoviruses were detected in each of three surveillance years. High frequencies of nosocomial acquisition occurred, as has been noted in prior reports. Similarly, persistence of infection and high frequencies of pneumonia and death among infected patients occurred, which have also been noted earlier. At MDACC, pneumonia occurred in 58-78% of infected patients, and 22-44% died. The role of the virus infection in many cases of pneumonia is uncertain, but death from pure viral pneumonia is well documented. A number of immune deficiencies in this patient population and options for control of these infections have been described that can, respectively, account for the medical problem and provide ways to approach prevention and treatment. © 1997 by Excerpta Medica, Inc.",,"amantadine; antivirus agent; rimantadine; adenovirus; cancer patient; conference paper; coronavirus; death; hospital infection; human; immune deficiency; immunocompetence; influenza virus; inhalational drug administration; parainfluenza virus; priority journal; respiratory syncytial pneumovirus; respiratory tract infection; rhinovirus; virus infection; virus pneumonia; Bone Marrow Transplantation; Cross Infection; Humans; Immunocompetence; Immunocompromised Host; Incidence; Neoplasms; Respiratory Tract Infections; United States; Virus Diseases","Keitel, W.A., Cate, T.R., Couch, R.B., Efficacy of sequential annual vaccination with inactivated influenza virus vaccine (1988) Am J Epidemiol., 127, pp. 353-364; Lewis, V.A., Champlin, R., Englund, J., Respiratory disease due to parainfluenza virus in adult bone marrow transplant recipients (1996) Clin Infect Dis., 23, pp. 1033-1037","Couch, R.B.; Department of Microbiology and Immunology, Baylor College of Medicine and Section of Infectious Diseases, University of Texas M.D. Anderson Cancer Center, Houston, TX, United States",,,00029343,,AJMEA,"10868136","English","Am. J. Med.",Article,"Final",,Scopus,2-s2.0-0031007965
"Bos E.C.W., Luytjes W., Spaan W.J.M.","7005778356;6701683324;7007172944;","The function of the spike protein of mouse hepatitis virus strain A59 can be studied on virus-like particles: Cleavage is not required for infectivity",1997,"Journal of Virology","71","12",,"9427","9433",,29,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030774237&partnerID=40&md5=c388808d26333c356ec39d650a30bfb0","Department of Virology, Leiden University, 2300 RC Leiden, Netherlands; Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands","Bos, E.C.W., Department of Virology, Leiden University, 2300 RC Leiden, Netherlands; Luytjes, W., Department of Virology, Leiden University, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Leiden University, 2300 RC Leiden, Netherlands, Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands","The spike protein (S) of the murine coronavirus mouse hepatitis virus strain A59 (MHV-A59) induces both virus-to-cell fusion during infection and syncytium formation. Thus far, only syncytium formation could be studied after transient expression of S. We have recently described a system in which viral infectivity is mimicked by using virus-like particles (VLPs) and reporter defective-interfering (DI) RNAs (E. C. W. Bos, W. Luytjes, H. Van der Meulen, H. K. Koerten, and W. J. M. Spaan, Virology 218:52-60, 1996). Production of VLPs of MHV-A59 was shown to be dependent on the expression of M and E. We now show in several ways that the infectivity of VLPs is dependent on S. Infectivity was lost when spikeless VLPs were produced. Infectivity was blocked upon treatment of the VLPs with MHV-A59-neutralizing anti-S monoclonal antibody (MAb) A2.3 but not with nonneutralizing anti-S MAb A1.4. When the target cells were incubated with antireceptor MAb CC1, which blocks MHV-A59 infection, VLPs did not infect the target cells. Thus, S- mediated VLP infectivity resembles MHV-A59 infectivity. The system can be used to identify domains in S that are essential for infectivity. As a first application, we investigated the requirements of cleavage of S for the infectivity of MHV-A59. We inserted three mutant S proteins that were previously shown to be uncleaved (E. C. W. Bos, L. Heijnen, W. Luytjes, and W. J. M. Spaan, Virology 214:453-463, 1995) into the VLPs. Here we show that cleavage of the spike protein of MHV-A59 is not required for infectivity.",,"hybrid protein; monoclonal antibody; neutralizing antibody; vitronectin; amino terminal sequence; animal cell; animal experiment; animal tissue; article; cell fusion; gene expression; hepatitis virus; mouse; nonhuman; priority journal; protein analysis; target cell; virion; virus particle; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Viral; Cell Line; Helper Viruses; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Neutralization Tests; Polymerase Chain Reaction; Rabbits; Receptors, Virus; RNA, Viral; Viral Envelope Proteins","Blumberg, B.M., Giorgi, C., Rose, K., Kolakofski, D., Sequence determination of the Sendai virus fusion protein gene (1985) J. Gen. Virol., 66, pp. 317-331; Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Bos, E.C.W., Luytjes, W., Van Der Meulen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Bredenbeek, P., (1990) Nucleic Acid Domains and Proteins Involved in the Replication of Coronaviruses, , Ph.D. thesis. University of Utrecht, Utrecht, The Netherlands; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Dveksler, G.S., Pensiero, M.N., Cardelechio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardelechio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Freed, E.O., Myers, D.J., Risser, R., Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 4650-4654; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike protein (1991) J. Virol., 65, pp. 1916-1928; Gallagher, T.M., Buchmeier, M.J., Perlman, S., Cell receptor-independent infection by a neurotropic murine coronavirus (1992) Virology, 191, pp. 517-522; Gallagher, T.M., Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein (1996) J. Virol., 70, pp. 4683-4690; Gallaher, W.R., Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus (1987) Cell, 50, pp. 327-328; Garroff, H., Frischauf, A.-M., Simons, K., Lehrbach, H., Delius, H., Nucleotide sequence of cDNA coding for Semliki Forest virus membrane proteins (1980) Nature, 288, pp. 236-241; Gething, M.J., Doms, R.W., York, D., White, J., Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus (1986) J. Cell Biol., 102, pp. 11-23; Gilmore, W., Fleming, J.O., Stohlman, S.A., Weiner, L.P., Characterization of the structural proteins of the murine coronavirus strain A59 using monoclonal antibodies (1987) Proc. Soc. Exp. Biol. Med., 185, pp. 177-186; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike cleavage signal (1993) J. 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Rueckert (ed.), Alan R. Liss, Inc., New York, N.Y; Kim, K.H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J. Virol., 71, pp. 3922-3931; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Luytjes, W., Gerritsma, H., Bos, E., Spaan, W.J.M., Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein (1997) J. Virol., 71, pp. 949-955; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Meinkoth, J., Wahl, G., Hybridization of nucleic acids immobilized on solid supports (1984) Anal. Biochem., 138, pp. 267-284; Niemann, H., Klenk, H.D., Coronavirus glycoprotein E1, a new type of viral glycoprotein (1981) J. Mol. Biol., 153, pp. 993-1010; Opstelten, D.-J.E., De Groote, P., Horzinek, M.C., Vennema, H., Rottier, P.J.M., Disulfide bonds in folding and transport of mouse hepatitis coronavirus glycoproteins (1993) J. Virol., 67, pp. 7394-7401; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Ricard, C.S., Sturman, L.S., Isolation of the subunits of the coronavirus envelope glycoprotein by hydroxyapatite high-performance liquid chromatography (1985) J. Chromatogr., 326, pp. 191-197; Ricard, C.S., Koetzner, C.A., Sturman, L.S., Masters, P.S., A conditional-lethal coronavirus mutant that fails to incorporate the spike glycoprotein into assembled virions (1995) Virus Res., 39, pp. 261-276; Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Schmidt, M.F.G., Acylation of viral spike glycoproteins: A feature of enveloped RNa viruses (1982) Virology, 116, pp. 327-338; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., Proteolytic processing of the replicase ORF1a protein of equine arteritis virus (1994) J. Virol., 68, pp. 5755-5764; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Stauber, R., Pfleiderer, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion (1993) J. Gen. Virol., 74, pp. 183-191; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine cornavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHM variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Van Berlo, M.F., Van Den Brink, W.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells: Brief report (1987) Arch. Virol., 95, pp. 123-128; Van Most, D., Bredenbeek, R.G.P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for the encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M.C., Spaan, W.J.M., Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system with encephalomyocarditis virus 5′ untranslated region sequences (1991) Gene, 108, pp. 201-210; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Williams, R.K., Jiang, G.-S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a non-functional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219; Zhang, L., Luytjes, W., Homberger, F., Spaan, W.J.M., Recombinant genomic RNA of coronavirus MHV-A59 after coreplication with a DI RNA containing the MHV RI spike gene (1997) Virology, 230, pp. 93-102","Spaan, W.J.M.; Department of Virology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; email: spaan@virology.azl.nl",,,0022538X,,JOVIA,"9371603","English","J. VIROL.",Article,"Final",,Scopus,2-s2.0-0030774237
"Greenberg S.B., Atmar R.L., Glezen W.P.","7402294401;7005296248;7004510527;","Spectrum of clinical illnesses due to ""common cold"" viruses in hospitalized patients",1997,"Clinical Infectious Diseases","25","2",,"356","",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345114072&partnerID=40&md5=d0e893100d24eeafefa8c857236739c3","Baylor College of Medicine, Ben Taub General Hospital, Houston, TX, United States","Greenberg, S.B., Baylor College of Medicine, Ben Taub General Hospital, Houston, TX, United States; Atmar, R.L., Baylor College of Medicine, Ben Taub General Hospital, Houston, TX, United States; Glezen, W.P., Baylor College of Medicine, Ben Taub General Hospital, Houston, TX, United States","The ""common cold"" viruses, rhinoviruses (RHI) and coronaviruses (COR) are best known as causes of upper respiratory tract infections (URTI) but have been implicated in lower respiratory tract infections (LRTI) especially in infants and young children. A prospective study (1991-95) of acute respiratory viral infections in hospitalized patients was performed at both an urban community and a public hospital. Respiratory cultures (nasal wash and/or throat swab) were obtained in 1,030 illness episodes and placed on 4 different tissue cultures for virus isolation. Acute and convalescent sera were obtained on 403 of these acutely ill patients and assayed for COR OC43 and 229E antibody. Of 66 documented ""common cold"" virus infections, 49 were due to RHI and 17 to COR; these represent 18.5% of all documented respiratory viral illness episodes. No gender differences were identified. Clinical diagnoses differed by age of the patients: 14/22 (64%) less than 2 years of age had bronchiolitis or pneumonia; 17/21 (81%) 5-34 years of age had an asthma exacerbation; and 19/23 (83%) 35-75 years of age had COPD, CHF or pneumonia. Other diagnoses included R/O sepsis (5 patients), croup (1 patient), fever (2 patients), lung abscess (1 patient), and R/O myocardial infarction (1 patient). A diagnosis of pneumonia was made in 17/66 (26%) patients and 24/66 (36%) had an asthma exacerbation. Mean length of hospital stay was 3,2, and 6.4 days for ages 0-4 years, 5-34 years, and 35-75 years, respectively. Intensive care or intermediate care units were used in 30/66 (45%) patients. Infections were documented throughout the year without a seasonal peak. These cases suggest a more significant role than previously reported for ""common cold"" viruses in the hospitalisation of patients with underlying illnesses (e.g., asthma and COPD).",,,,"Greenberg, S.B.; Baylor College of Medicine, Ben Taub General Hospital, Houston, TX, United States",,,10584838,,CIDIE,,"English","Clin. Infect. Dis.",Article,"Final",,Scopus,2-s2.0-0345114072
"Molenkamp R., Spaan W.J.M.","6603227562;7007172944;","Identification of a specific interaction between the coronavirus mouse hepatitis virus A59 nucleocapsid protein and packaging signal",1997,"Virology","239","1",,"78","86",,42,"10.1006/viro.1997.8867","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031472878&doi=10.1006%2fviro.1997.8867&partnerID=40&md5=1ac202c072e7fb9ee3cf2535a391c86b","Department of Virology, Institute of Medical Microbiology, Leiden University, AZL-L4-Q, P.O. Box 9600, 2300 RC Leiden, Netherlands","Molenkamp, R., Department of Virology, Institute of Medical Microbiology, Leiden University, AZL-L4-Q, P.O. Box 9600, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Institute of Medical Microbiology, Leiden University, AZL-L4-Q, P.O. Box 9600, 2300 RC Leiden, Netherlands","The coronavirus mouse hepatitis virus (MHV) is an enveloped positive stranded RNA virus. In infected cells MHV produces a 3' coterminal nested set of subgenomic messenger RNAs. Only the genomic RNA, however, is encapsidated by the nucleocapsid protein and incorporated in infectious MHV virions. It is believed that an RNA packaging signal (Ps), present only in the genomic RNA, is responsible for this selectivity. Earlier studies mapped this signal to a 69-nt-stem-loop structure packaging signal with the nucleocapsid protein. In this study we demonstrate the in vitro interaction of the MHV-A59 nucleocapsid protein with the packaging signal of MHV using gel retardation and UV cross-linking assays. This interaction was observed not only with the nucleocapsid protein from infected cells but also with that from purified virions and from cells expressing a recombinant nucleocapsid protein. The specificity of the interaction was demonstrated by competition experiments with nonlabeled Ps containing RNAs, tRNA, and total cytoplasmic RNA. The results indicated that no virus specific modification of the N-protein or the presence of other viral proteins are required for this in vitro interaction. The assays described in this report provide us with a powerful tool for studying encapsidation (initiation) in more detail.",,"capsid protein; messenger RNA; recombinant protein; RNA; transfer RNA; virus protein; amino terminal sequence; animal cell; article; controlled study; cytoplasm; mouse; Murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; signal transduction; virion; virus genome; virus nucleocapsid; Animalia; Coronavirus; Miridae; Murinae; Murine hepatitis virus; RNA viruses","Aldovini, A., Young, R.A., Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus (1990) J. 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Bredenbeek, (1990) Nucleic Acid Domains and Proteins Involved in the Replication of Coronaviruses, , University of Utrecht, Utrecht, The Netherlands; Burd, C.G., Dreyfuss, G., Conserved structures and diversity of functions of RNA-binding proteins (1994) Science, 265, pp. 615-621; Dignam, J.D., Lebowitz, R.M., Roeder, R.G., Acurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei (1983) Nucleic Acids Res., 11, pp. 1475-1489; Draper, D.E., Protein-RNA recognition (1995) Annu. Rev. Biochem., 64, pp. 593-620; Dubois-Dalcq, M.E., Doller, E.W., Haspel, M.V., Holmes, K.V., Cell tropism and expression of mouse hepatitis viruses (MHV) in mouse spinal cord cultures (1982) Virology, 119, pp. 317-331; Dupraz, P., Spahr, P.F., Specificity of Rous sarcoma virus nucleocapsid protein in genomic RNA packaging (1992) J. 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Virol., 39, pp. 545-549; Mahondas, D.V., Dales, S., Endosomal association of a protein phosphatase with high dephosphorylation activity against a coronavirus nucleocapsid protein (1991) FEBS Lett., 282, pp. 419-424; Makino, S., Shieh, C., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 1-11; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Arch. Virol., 125, pp. 141-160; Most, R.G.V.D., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Murphy, F.A., Fauquet, C.M., Bishop, D.H.L., Ghabrial, S.A., Jarvis, A.W., Martinelli, G.P., Mayo, M.A., Summers, M.D., (1995) Virus Taxonomy, Classification and Nomenclature of Viruses, , New York: Springer-Verlag; Nelson, G.W., Stohlman, S.A., Localization of the RNA-binding domain of mouse hepatitis virus nucleocapsid protein (1993) J. Gen. Virol., 74, pp. 1975-1979; Owen, K.E., Kuhn, R.J., Identification of a region in the sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation (1996) J. Virol., 70, pp. 2757-2763; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Pugatsch, T., Stacey, D.W., Identification of a sequence likely to be required for avian retroviral packaging (1983) Virology, 128, pp. 505-511; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor: Cold Spring Harbor Laboratory Press; Schlesinger, S., Makino, S., Linial, M.L., Cistrans (1994) Semin. Virol., 5, pp. 39-49; Snijder, E.J., Wassenaar, A.L.M., Dinten, L.C.V., Spaan, W.J.M., Gorbalenya, A.E., The arterivirus Nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases (1996) J. Biol. Chem., 271, pp. 4864-4871; Sorge, J., Ricci, W., Hughes, S.H., Cis (1983) J. Virol., 48, pp. 667-675; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Spaan, W.J.M., Delius, H., Skinner, M.A., Armstrong, J., Rottier, P.J.M., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO. J., 2, pp. 1839-1844; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stohlman, S.A., Fleming, J.O., Patton, C.D., Lai, M.M.C., Synthesis and subcellular localization of the murine coronavirus nucleocapsid protein (1983) Virology, 130, pp. 527-532; Stohlman, S.A., Baric, R.S., Nelson, G.W., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Stohlman, S.A., Lai, M.M.C., Phosphoproteins of murine hepatitis viruses (1979) J. Virol., 32, pp. 672-675; Strauss, J.H., Strauss, E.G., The alphaviruses: Gene expression, replication, and evolution [published erratum appears inMicrobiol. Rev.,58 (1994) Microbiol. Rev., 58, pp. 491-562; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Talbot, P.J., Buchmeier, M.J., Antigenic variation among murine coronaviruses: Evidence for polymorphism on the peplomer glycoprotein, E2 (1985) Virus Res., 2, pp. 317-328; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten D.-J., E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Weis, B., Nitschko, H., Ghattas, I., Schlesinger, S., Evidence for specificity in the encapsidation of Sindbis virus RNAs (1989) J. Virol., 63, pp. 5310-5318; Witherell, G.W., Gott, J.M., Uhlenbeck, O.C., Specific interaction between RNA phage coat proteins and RNA (1991) Prog. Nucleic Acid Res. Mol. Biol., 40, pp. 185-220; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Zhang, Y., Barklis, E., Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation (1995) J. Virol., 69, pp. 5716-5722; Zhou, M., Williams, A.K., Chung, S., Wang, L., Collisson, E.W., The infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3′ terminus of the genome (1997) Virology, 217, pp. 191-199","Spaan, W.J.M.; Department of Virology, Institute of Medical Microbiology, Leiden University, P.O. Box 9600, 2300 RC Leiden, Netherlands; email: azruviro@virology.azl.nl",,"Academic Press Inc.",00426822,,VIRLA,"9426448","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0031472878
"Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.","57213052499;6701491322;7006092803;56142402000;7006986911;57203567044;","Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein",1997,"Virology","239","1",,"1","10",,52,"10.1006/viro.1997.8877","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031458312&doi=10.1006%2fviro.1997.8877&partnerID=40&md5=2673a403a4d5c8235bd441677af21b92","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Department of Pathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States","Leparc-Goffart, I., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Hingley, S.T., Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States; Chua, M.M., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Jiang, X., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Lavi, E., Department of Pathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States","C12, an attenuated, fusion delayed, very weakly hepatotropic mutant of mouse hepatitis virus strain A59 (MHV-A59) has been further characterized. We have previously shown that C12 has two amino acid substitutions relative to wild type virus in the spike protein, Q159L (within a region of S1 shown to bind to viral receptor in an in vitro assay) and H716D (in the proteolytic cleavage recognition site). We have sequenced the rest of the 31-kb genome of C12 and compared it to wild type virus. Only three additional amino acids substitutions were found, all encoded within the replicase gene. Analysis of C12 in vivo in C57BI/6 mice has shown that despite the fact that this virus replicates in the brain to titers at least as high as wild type and causes acute encephalitis similar to wild type, this virus causes a minimal level of demyelination and only at very high levels of virus inoculation. Thus acute encephalitis is not sufficient for the induction of demyelination by MHV- A59. Analysis of mutants isolated at earlier times from the same persistently infected glial cell culture as C12, as well as mutants isolated from a second independent culture of persistently infected glial cells, suggests that both the weakly demyelinating and the weakly hepatotropic phenotypes of C12 are associated with the Q159L amino acid substitution.",,"RNA directed RNA polymerase; virus protein; amino acid substitution; animal cell; animal experiment; animal model; animal tissue; article; controlled study; demyelination; glia cell; inoculation; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; virus encephalitis; virus gene; virus mutant; virus pathogenesis; virus replication; virus titration; virus virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Armstrong, J., Smeekens, S., Rottier, P., Sequence of the nucleocapsid gene of the murine coronavirus MHV-A59 (1983) Nucleic Acids Res., 11, pp. 883-891; Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature (London), 308, pp. 751-752; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59: A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Budzilowicz, C.J., Weiss, S.R., In vitro (1987) Virology, 157, pp. 509-515; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that it not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; Fleming, J.D., Trousdale, M.D., Bradbury, J., Stohlman, S.A., Weiner, L.P., Experimental demyelination induced by coronavirus JHM (MHV-4): Molecular identification of a viral determinant of paralytic disease (1987) Microbial Pathogenesis, 3, pp. 9-20; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Fleming, J.O., Wang, F.I., Trousdale, M.D., Hinton, D.R., Stohlman, S.A., Interaction of immune and central nervous systems: Contribution of Thy-1+ cells to demyelination induced by coronavirus JHM (1993) Reg. Immunol., 5, pp. 37-43; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization resistant variants of a neurotropic coronavirus are generated by deletions within the amino terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gombold, J.L., Sutherland, R.M., Lavi, E., Paterson, Y., Weiss, S.R., Mouse hepatitis virus A59-induced demyelination can occur in the absence of CD8+ T cells (1995) Microb. Pathog., 18, pp. 211-221; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., 7, pp. 5631-5634; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., Hepatitis mutants of mouse hepatitis virus strain A59 (1995) Adv. Exp. Med. Biol., 380, pp. 577-582; Holmes, K.V., Compton, S.R., Coronavirus receptors (1995) The Coronaviridae, , New York: Plenum. p. 55-71; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5404-5410; Kyuwa, S., Yamaguchi, K., Toyoda, Y., Fujiwara, K., Induction of self reactive T cells after murine coronavirus infection (1991) J. Virol., 65, pp. 1789-1795; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., Persistence of MHV-A59 RNA in a slow virus demyelinating infection in mice as detected byin situ (1984) J. Virol., 51, pp. 563-566; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Suzumura, A., Hirayama, M., Highkin, M.K., Dambach, D.M., Silberberg, D.H., Weiss, S.R., Coronavirus mouse hepatitis virus (MHV)-A59 causes a persistent, productive infection in primary glial cell cultures (1987) Microb. Pathog., 3, pp. 79-86; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence of the murine coronavirus gene 1 encoding the putative protease and RNA polymerase (1991) Virology, 180, pp. 567-582; Luytjes, W., Sturman, L., Bredenbeck, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Luytjes, W., Bredenbeek, P.J., Noten, A.F., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike protein (1996) J. Virol., 70, pp. 2632-2635; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription and RNA recombination (1995) The Coronaviradae, pp. 11-32. , S.G. Siddell. New York: Plenum; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns4 gene of mouse hepatitis virus (MHV), strain A59 contains two ORFs and thus differs from ns4 of the JHM and S strains (1993) Arch. Virol., 129, pp. 301-309; Zoltick, P.W., Leibowitz, J.L., Oleszak, E., Weiss, S.R., Mouse hepatitis virus ORF 2a is expressed in the cytosol of infected mouse fibroblasts (1990) Virology, 174, pp. 605-607","Weiss, S.R.; Department of Microbiology, Philadelphia, PA 19104, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"9426441","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0031458312
"Maceyka M., Machamer C.E.","6506957814;7004585797;","Ceramide accumulation uncovers a cycling pathway for the cis-Golgi network marker, infectious bronchitis virus M protein",1997,"Journal of Cell Biology","139","6",,"1411","1418",,29,"10.1083/jcb.139.6.1411","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031468115&doi=10.1083%2fjcb.139.6.1411&partnerID=40&md5=c4e5e857b3d1696cc01cc34775e0dbac","Dept. of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States; Dept. of Cell Biology and Anatomy, Johns Hopkins University, School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","Maceyka, M., Dept. of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States; Machamer, C.E., Dept. of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States, Dept. of Cell Biology and Anatomy, Johns Hopkins University, School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","The M glycoprotein from the avian coronavirus, infectious bronchitis virus (IBV), contains information for localization to the cis-Golgi network in its first transmembrane domain. We hypothesize that localization to the Golgi complex may depend in part on specific interactions between protein transmembrane domains and membrane lipids. Because the site of sphingolipid synthesis overlaps the localization of IBV M, we asked whether perturbation of sphingolipids affected localization of IBV M. Short-term treatment with two inhibitors of sphingolipid synthesis had no effect on localization of IBV M or other Golgi markers. Thus, ongoing synthesis of these lipids was not required for proper localization. Surprisingly, a third inhibitor, d,1- threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP), shifted the steady-state distribution of IBV M from the Golgi complex to the ER. This effect was rapid and reversible and was also observed for ERGIC-53 but not for Golgi stack proteins. At the concentration of PDMP used, conversion of ceramide into both glucosylceramide and sphingomyelin was inhibited. Pretreatment with upstream inhibitors partially reversed the effects of PDMP, suggesting that ceramide accumulation mediates the PDMP-induced alterations. Indeed, an increase in cellular ceramide was measured in PDMP-treated cells. We propose that IBV M is at least in part localized by retrieval mechanisms. Further, ceramide accumulation reveals this cycle by upsetting the balance of anterograde and retrograde traffic and/or disrupting retention by altering bilayer dynamics.",,"2 decanoylamino 3 morpholino 1 phenyl 1 propanol; ceramide; glucosylceramide; membrane lipid; sphingomyelin; virus protein; animal cell; article; avian infectious bronchitis virus; bilayer membrane; cell strain bhk; controlled study; endoplasmic reticulum; golgi complex; immunofluorescence microscopy; lipogenesis; nonhuman; priority journal; protein localization; vero cell; Animals; Biological Markers; Cell Line; Ceramides; Cricetinae; Endoplasmic Reticulum; Enzyme Inhibitors; Golgi Apparatus; Infectious bronchitis virus; Kidney; Kinetics; Models, Biological; Morpholines; Sphingolipids; Viral Matrix Proteins; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus","Abe, A., Wu, D., Shayman, J.A., Radin, N.S., Metabolic effects of short-chain ceramide and glucosylceramide on sphingolipids and protein kinase C (1992) Eur. 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Chem., 266, pp. 22968-22974; Sodeik, B., Doms, R.W., Ericsson, M., Hiller, G., Machamer, C.E., Van't Hof, W., Van Meer, G., Griffiths, G., Assembly of vaccinia virus: Role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks (1993) J. Cell Biol., 121, pp. 521-541; Swift, A.M., Machamer, C.E., A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein (1991) J. Cell Biol., 115, pp. 19-30; Uemura, K.-I., Sugiyama, E., Tamai, C., Hara, A., Taketomi, T., Radin, N.S., Effect of an inhibitor of glucosylceramide synthesis on cultured rabbit skin fibroblasts (1990) J. Biochem. (Tokyo), 108, pp. 525-530; Meer, G., Transport and sorting of membrane lipids (1993) Curr. Opin. Cell Biol., 5, pp. 661-673; Velasco, A., Hendricks, L., Moremen, K.W., Tulsiani, D.R.P., Touster, O., Farquhar, M.G., Cell type-dependent variations in the subcellular distribution of α-mannosidase I and II (1993) J. Cell Biol., 122, pp. 39-51; Vunnam, R.R., Radin, N.S., Analogs of ceramide that inhibit glucocerebroside synthetase in mouse brain (1980) Chem. Phys. Lipids, 26, pp. 265-278; Wang, E., Norred, W.P., Bacon, C.W., Riley, R.T., Merril Jr., A.H., Inhibition of sphingolipid biosynthesis by fumonisins: Implications for diseases associated with Fusarium moniliforme (1991) J. Biol. Chem., 266, pp. 14486-14490; Weisz, O.A., Swift, A.M., Machamer, C.E., Oligomerization of a membrane protein correlates with its retention in the Golgi complex (1993) J. Cell Biol., 122, pp. 1185-1196; Wolff, R.A., Dobrowsky, R.T., Bielawska, A., Obeid, L.M., Hannun, Y., Role of ceromide-activated protein phosphatase in ceramide-mediated signal transduction (1994) J. Biol. Chem., 269, pp. 19605-19609","Machamer, C.E.; Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States",,,00219525,,JCLBA,"9396747","English","J. Cell Biol.",Article,"Final",Open Access,Scopus,2-s2.0-0031468115
"Kipar A., Kremendahl J., Addie D.D., Leukert W., Grant C.K., Reinacher M.","7004576445;6507138764;7003910352;6506376559;7402511447;7003284148;","Fatal enteritis associated with coronavirus infection in cats",1998,"Journal of Comparative Pathology","119","1",,"1","14",,22,"10.1016/S0021-9975(98)80067-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031857797&doi=10.1016%2fS0021-9975%2898%2980067-4&partnerID=40&md5=4b98d4459519c7f64e7254d4117e6d14","Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany","Kipar, A., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany; Kremendahl, J., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany; Addie, D.D., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany; Leukert, W., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany; Grant, C.K., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany; Reinacher, M., Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany","This report describes five cases of naturally occurring feline coronavirus enteritis. The affected animals, aged 2 months to 7 years, had a clinical history of intestinal symptoms, including diarrhoea or vomiting, or both. They exhibited variable histological changes in the epithelium of the small intestine, ranging from degeneration of single cells and detachment of groups of cells from the villous tips to regenerative processes of the crypt epithelia. Post-mortem diagnosis was based on the immunohistochemical demonstration of coronavirus antigen within intestinal epithelial cells and on the electron microscopical demonstration of coronavirus particles in the faeces. In addition, one animal was immunohistochemically positive for antigens of feline leukaemia virus (FeLV) and exhibited intestinal changes consistent with FeLV-associated enteritis. Two cats were tested serologically for feline immunodeficiency antibodies, with negative results. The findings indicate that natural coronavirus infection is a potential cause of severe enteritis in juvenile and adult cats.",,"virus antigen; animal cell; animal tissue; article; cat; controlled study; Coronavirus; crypt cell; diarrhea; electron microscopy; enteritis; feces analysis; Feline leukemia virus; immunohistochemistry; intestine epithelium cell; intestine villus; male; nonhuman; small intestine mucosa; symptom; virus infection; vomiting; Animalia; Coronavirus; Felidae; Feline coronavirus; Feline leukemia virus; Felis catus; leukaemia virus",,"Kipar, A.; Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete-Blank-Strasse 4, 04103 Leipzig, Germany",,"W.B. Saunders Ltd",00219975,,JCVPA,"9717123","English","J. Comp. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0031857797
"Collins A.R., Grubb A.","24439435400;22943736600;","Cystatin D, a natural salivary cysteine protease inhibitor, inhibits coronavirus replication at its physiologic concentration",1998,"Oral Microbiology and Immunology","13","1",,"59","61",,41,"10.1111/j.1399-302X.1998.tb00753.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032007523&doi=10.1111%2fj.1399-302X.1998.tb00753.x&partnerID=40&md5=06af2a65c581db4ca977f87c44f905c9","State University of New York, Buffalo, NY, United States; University of Lund, Sweden; Department of Microbiology, State Univ. of New York at Buffalo, Buffalo, NY 14214, United States","Collins, A.R., State University of New York, Buffalo, NY, United States, Department of Microbiology, State Univ. of New York at Buffalo, Buffalo, NY 14214, United States; Grubb, A., University of Lund, Sweden","This study was conducted to examine the effect of cystatin D, a newly discovered salivary cysteine protease inhibitor, on human coronavirus replication. When MRC-5, human diploid lung cells, were incubated with dilutions of recombinant human cystatin D from 0.65-10 μM for 1 h prior to, during and after infection with coronavirus OC43 and 229e strains, a decrease in virus yield was observed resulting in an IC50 of 0.8 μM for both virus strains. This dose is within the normal concentration range of cystatin D, 0.12-1.9 μM found in saliva. When a single dose, 2.5 μM, was applied, cystatin inhibition of release of virus progeny was not overcome until three days post infection whereas inhibition by leupeptin, a serine and cysteine protease inhibitor, was completely abrogated by two days. When cellular toxicity was measured by 3H-thymidine uptake, cystatin D did not markedly affect cell proliferation below a 10 μM dose. The results demonstrate that cystatin D is a potent inhibitor of coronavirus replication.","Cystatins; Human coronavirus; Inhibition",,"Abrahamson, M., Barrett, A.J., Salvenson, G., Grubb, A., Isolation of six cysteine proteinase inhibitors from human urine. Their physiologic and enzyme kinetic properties and concentrations in biological fluids (1986) J Biol Chem, 261, pp. 11282-11289; Appleyard, G., Tisdale, M., Inhibition of the growth of human coronavirus 229e by leupeptin (1985) J Gen Virol, 66, pp. 363-366; Balbin, M., Hall, A., Grubb, A., Mason, R.W., Lopez-Otin, C., Abrahamson, M., Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases (1994) J Biol Chem, 269, pp. 23156-23162; Bjorck, L., Grubb, A., Kjellen, L., Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus (1990) J Virol, 64, pp. 941-943; Collins, A., Grubb, A., Inhibitory effects of recombinant human cystatin C on human coronaviruses (1991) Antimicrob Agents Chemother, 35, pp. 2444-2446; Freije, J.P., Balbin, M., Abrahamson, M., Human cystatin D. cDNA cloning, characterization of the Escherichia coli expressed inhibitor and identification of the native protein in saliva (1993) J Biol Chem, 268, pp. 15737-15744; Gu, M., Haraszthy, G., Collins, A.R., Bergey, J., Identification of salivary proteins inhibiting herpes simplex virus 1 replication (1995) Oral Microbiol Immunol, 10, pp. 54-59; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229e RNA polymerase locus (1993) Virology, 195, pp. 680-691; Katoh, I., Yasunaga, T., Ikawa, Y., Yohinaka, Y., Inhibition of retroviral protease activity by an aspartyl proteinase inhibitor (1987) Nature, 329, pp. 654-656; Korant, B., Brzin, J., Turk, V., Cystatin, a protein inhibitor of cysteine proteases alters viral protein cleavages in infected human cells (1985) Biochem Biophys Res Commun, 127, pp. 1072-1076; Myint, S.H., Human coronaviruses, a brief review (1994) Rev Med Virol, 4, pp. 35-46; Sadoul, R., Fernandez, P.A., Quiquerez, A.L., Involvement of the proteasome in the programmed cell death of NGF-deprived sympathetic neurons (1996) EMBO J., 15, pp. 3845-3852; Taugner, R., Buhrle, C.P., Nobiling, R., Kirschke, H., Coexistence of renin and cathepsin B in epitheloid cell secretory granules (1995) Histochemistry, 83, pp. 103-108; Schroder, E., Phillips, C., Garman, E., Harlos, K., Crawford, C., X-ray crystallographic structure of a papain-leupeptin complex (1993) FEBS Lett, 315, pp. 38-42","Collins, A.R.; Department of Microbiology, State University of New York, Buffalo, NY 14214, United States",,"Blackwell Publishing Ltd",09020055,,OMIME,"9573825","English","Oral Microbiol. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0032007523
"Rossen J.W.A., De Beer R., Godeke G.-J., Raamsman M.J.B., Horzinek M.C., Vennema H., Rottier P.J.M.","7005977394;7003474059;6603099700;6603137050;7102624836;7003697291;7006145490;","The viral spike protein is not involved in the polarized sorting of coronaviruses in epithelial cells",1998,"Journal of Virology","72","1",,"497","503",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031974773&partnerID=40&md5=da6955468e89adbcaf19d2690762e167","Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands","Rossen, J.W.A., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands, Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Beer, R., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Godeke, G.-J., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Raamsman, M.J.B., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Vennema, H., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, Utrecht, Netherlands","Coronavirus are assembled by budding into a pre-Golgi compartment from which they are transported along the secretory pathway to leave the cell. In cultured epithelial cells, they are released in a polarized fashion; depending on the virus and cell type, they are sorted preferentially either to the apical domain or to the basolateral plasma membrane domain. In this study, we investigated the role of the coronavirus spike protein, because of its prominent position in the virion the prime sorting candidate, in the directionality of virus release. Three independent approaches were taken. (i) The inhibition of N glycosylation by tunicamycin resulted in the synthesis of spikeless virions. The absence of spikes, however, did not influence the polarity in the release of virisons. Thus, murine hepatitis virus strain A59 (MHV-A59) was still secreted from the basolateral membrane of mTAL and LMR cells and from the apical sides of MDCK(MHVR) cells, whereas transmissible gastroenteritis virus (TGEV) was still released from the apical surfaces of LMR cells. (ii) Spikeless virions were also studied by using the MHV-A59 temperature-sensitive mutant Albany 18. When these virions were produced in infected LMR and MDCK(MHVR) cells at the nonpermissive temperature, they were again preferentially released from basolateral and apical membranes, respectively. (iii) We recently demonstrated that coronavirus-like particles resembling normal virions were assembled and released when the envelope proteins M and E were coexpressed in cells (H. Vennema, G.-J., J. W. A. Rossen, W. F. Voorhout, M. C. Horzinek, D.-J. E. Opstelten, and P. J. M. Rottier, EMBO J. 15:2020-2028, 1996). The spikeless particles produced in mTAL cells by using recombinant Semliki Forest viruses to express these two genes of MHV-A59 were specifically released from basolateral membranes, i.e., with the same polarity as that of wild-type MHV-A59. Our results thus consistently demonstrate that the spike protein is not involved in the directional sorting of coronaviruses in epithelial cells. In addition, our observations with tunicamycin show that contrary to the results with some secretory proteins, the N-linked oligosaccharides present on the viral M proteins of coronaviruses such as TGEV also play no role in viral sorting. The implications of these conclusions are discussed.",,"animal cell; article; cell selection; coronavirus; epithelium cell; nonhuman; priority journal; virus assembly; virus cell interaction; virus replication; Animals; Base Sequence; Cell Line; Cell Polarity; Coronavirus; DNA Primers; Dogs; Epithelial Cells; LLC-PK1 Cells; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutation; Swine; Temperature; Transmissible gastroenteritis virus; Tunicamycin; Viral Envelope Proteins; Viral Proteins; Virus Replication","Bredenbeek, P.J., Charité, J., Noten, J.F.H., Luytjes, W., Horzinek, M.C., Van Der Zeijst, B.A.M., Spaan, W.J.M., Sequences involved in the replication of coronaviruses (1987) Adv. Exp. Med. Biol., 218, pp. 65-72; Budzilowicz, C.J., Weiss, S.R., In vitro synthesis of two polypeptides from a nonstructural gene of coronavirus mouse hepatitis virus strain A59 (1987) Virology, 157, pp. 509-515; Chen, W., Madden, V.J., Bagnell Jr., C.R., Baric, R.S., Host-derived intracellular immunization against mouse hepatitis virus infection (1997) Virology, 228, pp. 318-332; Compans, R.W., Virus entry and release in polarized epithelial cells (1995) Curr. Top. Microbiol. Immunol., 202, pp. 209-219; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-26; Delmas, B., Kut, E., Gelfi, J., Laude, H., Overexpression of TGEV cell receptor impairs the production of virus particles (1995) Adv. Exp. Med. Biol., 380, pp. 379-385; Doyle, L.P., Hutchings, L.M.A., A transmissible gastroenteritis in pigs (1946) J. Am. Vet. Med. Assoc., 108, pp. 257-259; Eaton, S., Simons, K., Apical, basal, and lateral cues for epithelial polarization (1995) Cell, 82, pp. 5-8; Fiedler, K., Simons, K., The role of N-glycans in the secretory pathway (1995) Cell, 81, pp. 309-312; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M., Frelinger, J.A., Weiner, L.P., Antigcnic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Gagneten, S., Gout, O., Dubois Dalcq, M., Rottier, P.J.M., Rossen, J.W.A., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Gallagher, T.M., Overexpression of the MHV receptor. Effect on progeny virus secretion (1995) Adv. Exp. Med. Biol., 380, pp. 331-336; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV corona virus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Gonzáles, A., Nicovani, S., Juica, F., Apical secretion of hepatitis B surface antigen from transfected Madin-Darby canine kidney cells (1993) J. Biol. Chem., 268, pp. 6662-6667; Holmes, K.V., Doller, E.W., Sturman, L.S., Tunicamycin resistant alycosylation of coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein (1981) Virology, 115, pp. 334-344; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Virology, 1, pp. 1075-1093. , B. N. Fields, D. M. Knipe, P. M. Howley, K. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Lippincott-Raven Publishers, Philadelphia, Pa; Kawasaki, E.S., Wang, A.M., Detection of gene expression (1989) PCR Technology: Principles and Applications for DNA Amplification, pp. 89-97. , H. A. Erlich (ed.), Stockton Press, New York, N.Y; Kitagawa, Y., Sano, Y., Ueda, M., Higashio, K., Narita, H., Okano, M., Matsumoto, S.-I., Sasaki, R., N-glycosylation of crythropoietein is critical for apical secretion by Madin-Darby canine kidney cells (1994) Exp. Cell Res., 213, pp. 449-457; Klumperman, J., Krijnse Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Krijnse Locker, J., Ericsson, M., Rottier, P.J.M., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J. Cell Biol., 124, pp. 55-70; Liljeström, P., Garoff, H., A new generation of animal cell expression vectors based on the Semliki Forest virus replicon (1991) Bio/Technology, 9, pp. 1356-1361; Marzolo, M.P., Gonzáles, A., Glycosylation is not required for apical secretion of the hepatitis B surface antigen by MDCK and Fisher polarized epithelial cells (1995) Mol. Biol. Cell, 6 (SUPPL.), pp. 400a; Matter, K., Yamamoto, E.M., Mellman, I., Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells (1994) J. Cell Biol., 126, pp. 991-1004; Mays, R.W., Beck, K.A., Nelson, W.J., Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery (1994) Curr. Opin. Cell Biol., 6, pp. 16-24; McIntosh, K., Coronaviruses (1996) Virology, 1, pp. 1095-1103. , B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Lippincott-Raven Publishers, Philadelphia, Pa; Mostov, K.E., Cardone, M.H., Regulation of protein traffic in polarized epithelial cells (1995) Bioessays, 17, pp. 129-138; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Mustu, N.A., Polarized secretion of human corticosteroid binding globulin by MDCK and BeWo cells (1993) Exp. Cell Res., 209, pp. 271-276; Parczyk, K., Koch-Brandt, C., The role of carbohydrates in vectorial exocytosis: The secretion of the gp 80 glycoprotein complex in a ricin-resistant mutant of MDCK cells (1991) FEBS Lett., 278, pp. 267-270; Pensaert, M., Haelterman, E.O., Burnstein, T., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions. 1. Immunofluorescence, histopathology and virus production in the small intestine through the course of infection (1970) Arch. Gesamte Virusforsh., 31, pp. 321-334; Pensaert, M., Haelterman, E.O., Hinsman, E.J., Transmissible gastroenteritis of swine: Virus-intestinal cell interactions. 2. Electron microscopy of the epithelium in isolated jejunal loops (1970) Arch. Gesamte Virusforsh., 31, pp. 335-351; Raamsman, M.J.B., Rottier, P.J.M., Unpublished data; Ricard, C.S., Koetzner, C.A., Sturman, L.S., Masters, P.S., A conditional-lethal murine coronavirus mutant that fails to incorporate the spike glycoprotein into assembled virions (1995) Virus Res., 39, pp. 261-276; Risco, C., Antón, I.M., Suñé, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Rossen, J.W.A., Bekker, C.P.J., Strous, G.J.A.M., Horzinek, M.C., Dveksler, G.S., Holmes, K.V., Bottier, P.J.M., A murine and a porcine coronavirus are released from opposite surfaces of the same epithelial cells (1996) Virology, 224, pp. 345-351; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells (1994) J. Virol., 68, pp. 7966-7973; Rossen, J.W.A., Strous, G.J.A.M., Horzineck, M.C., Rottier, P.J.M., Mouse hepatitis virus strain A59 is released from opposite sides of different epithelial cell types (1997) J. Gen. Virol., 78, pp. 61-69; Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Van Der Ende, A., Strous, G.J.A.M., Rottier, P.J.M., MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally (1995) Virology, 210, pp. 54-66; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Rottier, P.J.M., Rose, J.K., Coronavirus E1 glycoprotein expressed from cloned cDNA localizes in the Golgi region (1987) J. Virol., 61, pp. 2042-2045; Rottier, P.J.M., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Translation of three mouse hepatitis virus strain A59 sub-genomic RNAs in Xenopus laevis oocytes (1981) J. Virol., 38, pp. 20-26; Scheiffele, P., Peränen, J., Simons, K., N-glycans as apical sorting signals in epithelial cells (1995) Nature, 378, pp. 96-98; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac cells: Determination of the first site of budding of progeny virions (1984) J. Clin. Microhiol., 19, pp. 388-393; Tooze, J., Tooze, S.A., Fuller, S.D., Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells (1987) J. Cell Biol., 105, pp. 1215-1226; Tucker, S.P., Compans, R.W., Virus infection of polarized epithelial cells (1993) Adv. Virus Res., 42, pp. 187-247; Urban, J., Parczvk, K., Leutz, A., Kayne, M., Konder-Koch, C., Constitutive apical secretion of an 80-kDa sulfated glycoprotein complex in the polarized epithelial Madin-Darby canine kidney cell line (1987) J. 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Cell Biol., 67, pp. 84-88; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Rossen, J.W.A.; Institute of Virology, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: J.Rossen@vetmic.dgk.ruu.nl",,,0022538X,,JOVIA,"9420251","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031974773
"Castilla J., Sola I., Pintado B., Sánchez-Morgado J.M., Enjuanes L.","8851950500;7003336781;6701776268;6602349176;7006565392;","Lactogenic immunity in transgenic mice producing recombinant antibodies neutralizing coronavirus",1998,"Advances in Experimental Medicine and Biology","440",,,"675","686",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754401&partnerID=40&md5=a558dbb94f10bb1bc232659cb96cb394","Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Canto Blanco 28049 Madrid, Spain; Department of Animal Reproduction, INIA, Carretera La Coruña km 5.9, 28040 Madrid, Spain","Castilla, J., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Canto Blanco 28049 Madrid, Spain; Sola, I., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Canto Blanco 28049 Madrid, Spain; Pintado, B., Department of Animal Reproduction, INIA, Carretera La Coruña km 5.9, 28040 Madrid, Spain; Sánchez-Morgado, J.M., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Canto Blanco 28049 Madrid, Spain; Enjuanes, L., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Canto Blanco 28049 Madrid, Spain","Protection against coronavirus infections can be provided by the oral administration of virus neutralizing antibodies. To provide lactogenic immunity, eighteen lines of transgenic mice secreting a recombinant IgG1 monoclonal antibody (rIgG1) and ten lines of transgenic mice secreting recombinant IgA monoclonal antibodies (rIgA) neutralizing transmissible gastroenteritis coronavirus (TGEV) into the milk were generated. Genes encoding the light and heavy chains of monoclonal antibody (MAb) 6A.C3 were expressed under the control of regulatory sequences derived from the mouse genomic DNA encoding the whey acidic protein (WAP) and beta-lactoglobulin (BLG), which are highly abundant milk proteins. The MAb 6A.C3 binds to a highly conserved epitope present in coronaviruses of several species. This MAb does not allow the selection of neutralization escaping virus mutants. The antibody was expressed in the milk of transgenic mice with titers of one million as determined by RIA, and neutralized TGEV infectivity by one million fold corresponding to immunoglobulin concentrations of 5 to 6 mg per ml. Matrix attachment regions (MAR) sequences were not essential for rIgG1 transgene expression, but co-microinjection of MAR and antibody genes led to a twenty to ten thousand-fold increase in the antibody titer in 50% of the rIgG1 transgenic animals generated. Co-microinjection of the genomic BLG gene with riga light and heavy chain genes led to the generation of transgenic mice carrying the three transgenes. The highest antibody titers were produced by transgenic mice that had integrated the antibody and BLG genes, although the number of transgenic animals generated does not allow a definitive conclusion on the enhancing effect of BLG co-integration. Antibody expression levels were transgene copy number independent and integration site dependent. The generation of transgenic animals producing virus neutralizing antibodies in the milk could be a general approach to provide protection against neonatal infections of the enteric tract.",,"beta lactoglobulin; immunoglobulin A; immunoglobulin G; neutralizing antibody; animal cell; animal model; antibody production; antibody titer; article; controlled study; Coronavirus; gene expression; immunity; milk production; mouse; nonhuman; priority journal; RNA virus infection; transgenic mouse; virus neutralization; Animalia; Coronavirus; Mus musculus; RNA viruses; Transmissible gastroenteritis virus","Bonifer, C., Vidal, M., Grosveld, F., Sippel, A.E., Tissue specific and protein position independent expression of the complete gene domain for chicken lysozyme in transgenic mice (1990) EMBO J., 9, pp. 2843-2848; Castilla, J., Pintado, B., Sola, I., Sánchez-Morgado, J.M., Hennighausen, L., Enjuanes, L., Engineering lactogenic immunity in transgenic mice secreting virus neutralizing antibodies in the milk (1998) Nat. Biotech., 16, pp. 349-353; Castilla, J., Sola, I., Enjuanes, L., Interference of coronavirus infection by expression of immunoglobulin G (IgG) or IgA virus-neutralizing antibodies (1997) J. Virol., 71, pp. 5251-5258; Clark, A.J., Archibald, A.L., McClenaghan, M., Simons, J.P., Wallace, R., Whitelaw, C.B.A., Enhancing the efficiency of transgene expression (1993) Transg. Res. Soc. Lond., 339, pp. 225-232; Clark, A.J., Cowper, A., Wallace, R., Wright, G., Simons, J.P., Rescuing transgene expression by co-integration (1992) Biotechnology, 10, pp. 1450-1454; Correa, I., Gebauer, F., Bullido, M.J., Suñé, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus (1990) J. Gen. Virol., 71, pp. 271-279; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus. Res., 10, pp. 77-94; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5367-5375; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , (S. G. Siddell, Ed.), Plenum Press, New York; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Hennighausen, L.G., Sippel, A.E., Mouse whey acidic protein is a novel member of the family of four-disulfide core proteins (1982) Nuc. Acid. Res., 10, pp. 2677-2684; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Mazanec, M.B., Huang, Y.T., Pimplikar, S.W., Lamm, M.E., Mechanisms of inactivation of respiratory viruses by IgA, including intraepithelial neutralization (1996) Sem. Virol., 7, pp. 285-292; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis. Seventh ed (1992) Diseases of Swine, pp. 362-386. , (A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor, Eds.), Wolfe Publishing Ltd, Ames. Iowa; Sanchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sola, I., Castilla, J., Pintado, B., Sánchez-Morgado, J.M., Whitelaw, B., Clark, J., Enjuanes, L., Transgenic mice secreting coronavirus neutralizing antibodies into the milk (1998) J. Virol., 72, pp. 3762-3772; Torres, J.M., Sanchez, C.M., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; Whitelaw, C.B.A., Archibald, A.L., Harris, S., McClenaghan, M., Simons, L.P., Clark, A.J., Targeting expression to the mammary gland: Intronic sequences can enhance the efficiency of gene expression in transgenic mice (1991) Transgenic Res., 1, pp. 3-13","Castilla, J.; Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Univ. Autonoma, Canto Blanco, 28049 Madrid, Spain",,"Springer New York LLC",00652598,,AEMBA,"9782344","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754401
"Risco C., Antón I.M., Muntión M., González J.M., Carrascosa J.L., Enjuanes L.","56251715300;57198264385;8114506300;57201828108;35481302900;7006565392;","Structure and intracellular assembly of the transmissible gastroenteritis coronavirus",1998,"Advances in Experimental Medicine and Biology","440",,,"341","346",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783433&partnerID=40&md5=4989b8e7d65279edfb06d3807af2a4bd","Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain","Risco, C., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Antón, I.M., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Muntión, M., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; González, J.M., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Carrascosa, J.L., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnología (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain","Coronaviruses have been described as pleomorphic, round particles with a helical nucleocapsid as the unique internal structure under the virion envelope. Our studies on the organization of the transmissible gastroenteritis coronavirus (TGEV) have shown that the structure of these viruses is more complex. Different electron microscopy techniques, including cryomicroscopy of vitrified viruses, revealed the existence of an internal core, most probably icosahedral, in TGEV virions. Disruption of these cores induced the release of elongated ribonucleoprotein complexes. Ultrastructural analysis of freeze-substituted TGEV-infected swine testis (ST) cells showed characteristic intracellular budding profiles as well as two types of virions. While large virions with an electron-dense internal periphery are seen at perinuclear regions, smaller viral particles exhibiting compact internal cores of poligonal contours are more abundant in areas closer to the plasma membrane of the cell. These data strongly suggest that maturation events following the budding process are responsible for the formation of the internal core shell, the new structural element that we have recently described in extracellular infectious TGEV virions.",,"ribonucleoprotein; virus protein; animal cell; article; controlled study; Coronavirus; cryoelectron microscopy; nonhuman; priority journal; swine; testis cell; virion; virus assembly; virus core; virus morphology; virus nucleocapsid; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Booy, F.P., Cryoelectron microscopy (1993) Viral Fusion Mechanisms, pp. 21-54. , J. Bentz, ed., CRC Press, Inc., Boca Raton, Fla; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Grief, C., Nermut, M.V., Hockley, D.J., A morphological study of freeze-substituted human and simian immunodeficiency viruses (1994) Micron., 25, pp. 119-128; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.P., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Krijnse-Locker, J., Ericsson, M., Rottier, P.J., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J. Cell Biol., 124, pp. 55-70; Risco, C., Anton, I.M., Suñé, C., Pedregosa, A.M., Martin-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of the transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Risco, C., Menéndez-Arias, L., Copeland, T.D., Pinto Da Suva, P., Oroszlan, S., Intracellular transport of the murine leukemia virus during acute infection of NIH 3T3 cells: Nuclear import of nucleocapsid protein and integrase (1995) J. Cell Sci., 108, pp. 3039-3050; Risco, C., Antón, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Rottier, J.M., The coronavirus membrane glycoprotein (1995) The Coronaviridae, pp. 115-139. , S.G. Sidell, ed., Plenum Press, New York and London","Risco, C.; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma, 28049 Madrid, Spain",,"Springer New York LLC",00652598,,AEMBA,"9782301","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783433
"Chagnon F., Lamarre A., Lachance C., Krakowski M., Owens T., Laliberté J.-F., Talbot P.J.","57196797991;7004646746;57210675095;7006751120;7101750869;7003676265;7102670281;","Characterization of the expression and immunogenicity of the ns4b protein of human coronavirus 229E",1998,"Canadian Journal of Microbiology","44","10",,"1012","1017",,,"10.1139/w98-089","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032447786&doi=10.1139%2fw98-089&partnerID=40&md5=7641c3fbb6e2eea13330bef54ec0f54e","Lab. of Neuroimmunovirology/H. H., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Neuroimmunology Unit, Montreal Neurological Institute, McGill University, 3801 University, Montréal, QC H3A 2B4, Canada; Microbiol. and Biotechnology Res. C., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada","Chagnon, F., Lab. of Neuroimmunovirology/H. H., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Lamarre, A., Lab. of Neuroimmunovirology/H. H., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Lachance, C., Lab. of Neuroimmunovirology/H. H., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Krakowski, M., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, 3801 University, Montréal, QC H3A 2B4, Canada; Owens, T., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, 3801 University, Montréal, QC H3A 2B4, Canada; Laliberté, J.-F., Microbiol. and Biotechnology Res. C., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada; Talbot, P.J., Lab. of Neuroimmunovirology/H. H., Institut Armand-Frappier, INRS, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada, Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531, boulevard des Prairies, Laval, QC H7V 1B7, Canada","Sequencing of complementary DNAs prepared from various coronaviruses has revealed open reading frames encoding putative proteins that are yet to be characterized and are so far only described as nonstructural (ns). As a first step in the elucidation of its function, we characterized the expression and immunogenicity of the ns4b gene product from strain 229E of human coronavirus (HCV-229E), a respiratory virus with a neurotropic potential. The gene was cloned and expressed in bacteria. A fusion protein of ns4b with maltose- binding protein was injected into rabbits to generate specific antibodies that were used to demonstrate the expression of ns4b in HCV-229E-infected cells using flow cytometry. Given a previously reported contiguous five amino acid shared region between ns4b and myelin basic protein, a purified recombinant histidine-tagged ns4b protein and (or) human myelin basic protein were injected into mice to evaluate whether myelin-viral protein cross- reactive antibody responses could be generated. Each immunogen induced specific but not cross-reactive antibodies. We conclude that ns4b is expressed in infected cells and is immunogenic, although this does not involve amino acids shared with a self protein, at least in the experimental conditions used.","Expression; Human coronavirus 229E; Immunogenicity; Nonstructural protein; Ns4b protein","virus protein; article; Coronavirus; cross reaction; DNA sequence; immunogenicity; molecular cloning; nonhuman; open reading frame; priority journal; protein analysis; protein expression; protein structure; Coronavirus; Hepatitis C virus; human coronavirus; Human coronavirus 229E; Oryctolagus cuniculus; RNA viruses","Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J., Rutter, W.J., Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease (1979) Biochemistry, 18, pp. 5294-5299; Daniel, C., Talbot, P.J., Protection from lethal coronavirus infection by affinity-purified spike glycoprotein of murine hepatitis virus, strain A59 (1990) Virology, 174, pp. 87-94; Fritz, R.B., McFarlin, D.E., Encephalitogenic epitopes of myelin basic protein (1989) Chem. Immunol., 46, pp. 101-125; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fields Virology. 3rd Ed., pp. 1075-1093. , Edited by B.N. Fields, D.M. Knipe, and P.M. Howley. Raven Press, Philadelphia; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M.C., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus 229E (1990) Virology, 174, pp. 608-612; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Krakowski, M., Owens, T., Interferon-gamma confers resistance to experimental allergic encephalomyelitis (1996) Eur. J. Immunol., 26, pp. 1641-1646; Liu, D.X., Inglis, S.C., Identification of two new polypeptides encoded by mRNA 5 of the coronavirus infectious bronchitis virus (1992) Virology, 186, pp. 342-347; McIntosh, K., Coronaviruses: A comparative review (1974) Curr. Top. Microbiol. Immunol., 63, pp. 85-129; Myint, S.H., Human coronaviruses: A brief review (1994) Rev. Med. Virol., 4, pp. 35-46; Raabe, T., Siddell, S.G., Nucleotide sequence of the membrane protein of human coronavirus 229E (1989) Arch. Virol., 107, pp. 323-328; Raabe, T., Siddell, S.G., Nucleotide sequence of the human coronavirus HCV-229E messenger RNA 4 and messenger RNA 5 unique regions (1989) Nucl. Acids Res., 17, p. 6387; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual. 2nd Ed., pp. 174-184. , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Schägger, H., Von Jagow, G., Tricine - Sodium dodecyl sulfate - Polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa (1987) Anal. Biochem., 166, pp. 368-379; Schreiber, S.S., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleoprotein protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Talbot, P.J., Paquette, J.-S., Ciurli, C., Antel, J.P., Ouellet, F., Myelin basic protein and human coronavirus 229E crossreactive T cells in multiple sclerosis (1996) Ann. Neurol., 39, pp. 233-240; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.-L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683","Talbot, P.J.; Laboratoire de neuroimmunovirologie, Institut Armand-Frappier, 531, boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,"National Research Council of Canada",00084166,,CJMIA,"9933919","English","Can. J. Microbiol.",Article,"Final",,Scopus,2-s2.0-0032447786
"Dar A.M., Kapil S., Goyal S.M.","8326657500;7003293348;7202441793;","Comparison of immunohistochemistry, electron microscopy, and direct fluorescent antibody test for the detection of bovine coronavirus",1998,"Journal of Veterinary Diagnostic Investigation","10","2",,"152","157",,12,"10.1177/104063879801000206","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032042131&doi=10.1177%2f104063879801000206&partnerID=40&md5=a7ce14e57745ca44c05330f3e952150e","Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States; Dept. Vet. Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Dar, A.M., Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States; Kapil, S., Dept. Vet. Diagn. Med./Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Goyal, S.M., Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States","Bovine coronavirus (BCV) is 1 of the major causes of calf diarrhea and has also been implicated in respiratory infections of young calves and winter dysentery of adult cattle. Currently, transmission electron microscopy (TEM), direct fluorescent antibody (DFA), and enzyme-linked immunosorbent assay (ELISA) techniques are considered standard methods for the diagnosis of BCV infection. However, these techniques are not useful if fresh tissues and intestinal contents are not available for examination. The detection of viral antigens in formalin-fixed, paraffin-embedded tissues using immunohistochemistry (IHC) is a suitable alternative. In the present study, 166 tissue specimens were tested by IHC for the presence of BCV. These tissues were from animals whose feces were positive for rotavirus and/or coronavirus by TEM. Some of these samples were also tested by DFA. Thus, TEM, DFA, and IHC were compared for the detection of BCV. There was 56% agreement among the 3 methods (overall kappa = 0.368). When IHC was compared with TEM, 78% agreement was observed (kappa = 0.475). Similarly, IHC and DFA had 64% agreement (kappa = 0.277). These kappa values indicate a moderate degree of agreement between IHC and TEM; agreement between IHC and DFA was fair. The results of this study indicate that IHC may be a suitable adjunct for the detection of BCV because of its simplicity, ease of use, and relatively close correlation with TEM results.",,"animal; animal disease; article; cat; cat disease; cattle; cattle disease; comparative study; Coronavirus; diarrhea; dog; dog disease; electron microscopy; feces; fluorescent antibody technique; immunohistochemistry; isolation and purification; reproducibility; swine; swine disease; virology; virus infection; Animals; Cat Diseases; Cats; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Dog Diseases; Dogs; Feces; Fluorescent Antibody Technique, Direct; Immunohistochemistry; Microscopy, Electron; Reproducibility of Results; Swine; Swine Diseases","Allan, G.M., McNulty, M.S., Bryson, D., Demonstration of bovine virus diarrhea virus antigen in formalin fixed paraffin embedded tissue using streptavidin/biotin technique (1989) Res Vet Sci, 46, pp. 416-418; Almeda, J.D., Craig, C.R., Hall, T.E., Multiple viruses present in the feces of a scouring calf (1978) Vet Rec, 102, pp. 170-171; (1983) Laboratory Methods for Detecting Calf Diarrhea Viruses, , Norden Laboratories, Lincoln, NE; Athanssious, R., Marsolais, G., Assaf, R., Detection of bovine coronavirus and type a rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can Vet J, 35, pp. 163-169; Barlow, R.M., Nettleton, P.F., Gardiner, A.C., Persistent bovine virus diarrhea infection in a bull (1986) Vet Rec, 118, pp. 321-324; Baszler, T.V., Evermann, J.F., Kaylor, P.S., Diagnosis of naturally occurring bovine viral diarrhea virus infections in ruminants using monoclonal antibody-based immunohistochemistry (1995) Vet Pathol, 32, pp. 609-618; Brown, C.C., Ojok, L., Immunohistochemical detection of rinderpest virus: Effect of autolysis and period of fixation (1996) Res Vet Sci, 60, pp. 182-184; Bryson, D.G., Cush, P.F., McNulty, M.S., An immunoperoxidase method of detecting respiratory syncytial virus antigen in paraffin sections of pneumonic bovine lungs (1988) Am J Vet Res, 49, pp. 1121-1126; Carman, P.S., Hazlett, M.J., Bovine coronavirus infection in Ontario 1990-91 (1992) Can Vet J, 33, pp. 812-814; El-kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Infection and cross protection studies of winter dysentry and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am J Vet Res, 57, pp. 48-53; Fleiss, J.L., (1981) Statistical Methods for Rates and Proportions, 2nd Ed., , Wiley, New York, NY; Flewett, T.H., Electron microscopy in the diagnosis of infectious diarrhea (1978) J Am Vet Med Assoc, 173, pp. 538-541; Giusti, A.M., Lavazza, A., Scanziani, E., Diagnosis of coronavirus enteritis in calves: Comparison of the ELISA, immunoelectron microscopy and immunohistochemistry (1994) Selezione Vet, 35, pp. 737-742; Goyal, S.M., Rademacher, R.A., Pomeroy, K.A., Comparison of electron microscopy with three commercial tests for the detection of rotavirus in animal feces (1987) Diagn Microbiol Infect Dis, 6, pp. 249-254; Haines, D.M., Chelack, B.J., Technical consideration for developing enzyme immunohistochemical staining procedures on formalin-fixed paraffin-embedded tissue for diagnostic pathology (1991) J Vet Diagn Invest, 3, pp. 101-112; Haines, D.M., Kendall, J.C., Remenda, B.W., Monoclonal and polyclonal antibodies for immunohistochemical detection of bovine parainfluenza type 3 in frozen and formalin-fixed paraffin-embedded tissues (1992) J Vet Diagn Invest, 4, pp. 393-399; Hardy Jr., W.D., Hirshaut, Y., Hess, P., Detection of feline leukemia virus and other mammalian oncoviruses by immunofluorescence (1973) Unifying Concepts of Leukemia, pp. 778-799. , ed. Dutcher RM, Chieco-Bianchi L, Karger, Basel, Switzerland; Hyatt, A.D., The application of electron microscopy to veterinary virus diagnosis (1989) Aust Vet J, 66, pp. 445-449; Jonson, L.G., Engstrom, B.E., Immunohistochemical detection of infectious bursal disease and infectious bronchitis virus antigen in fixed, paraffin embedded chicken tissue (1986) Avian Pathol, 15, pp. 385-393; Kapil, S., Pomeroy, K.A., Goyal, S.M., Trent, A.M., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J Vet Diagn Invest, 3, pp. 88-89; Kapil, S., Richardson, K.L., Radi, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J Vet Diagn Invest, 7, pp. 538-539; Landis, J., Koch, G., The measurement of observer agreement for categorical data (1977) Biometrics, 33, pp. 159-174; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am J Vet Res, 40, pp. 1476-1478; Lopez, J.W., Delpiero, F., Amyglaser, Immunoperoxidase histochemistry as a diagnostic tool for detection of equine arteritis virus antigen in formalin fixed tissues (1996) Equine Vet J, 28, pp. 77-79; Martin, S.W., The evaluation of test (1977) Can J Comp Med, 41, pp. 19-25; Miller, J.M., Van Der Maaten, J.M., Demonstration of infectious rhinotracheitis virus antigen in paraffin sections (1989) J Vet Diagn Invest, 1, pp. 105-109; Naeem, K., Goyal, S.M., Comparison of virus isolation, immunofluorescence and electron microscopy for diagnosis of animal viruses (1988) Microbiologica, 11, pp. 355-362; Ratafia, M., Genetically engineered vaccines: World business opportunities (1988) Am Clin Prod Rev, 7, pp. 18-21; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tract of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Introduction (1990) Viral Diarrheas of Man and Animals, pp. 3-6. , ed. Saif LJ, Theil KW, CRC Press, Boca Raton, FL; Saif, L.J., Brock, K.V., Redmen, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Heckert, R.A., Enteric coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 211-222. , ed. Saif LJ, Theil KW, CRC Press, Boca Raton, FL; Sato, M., Akashi, H., Detection of bovine coronavirus by enzyme-linked immunosorbent assay using monoclonal antibodies (1994) J Vet Med Sci, 55, pp. 771-774; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Storz, J., Stein, L., Leim, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Sueyoshi, M., Tsuda, T., Yamazaki, K., An immunohistochemical investigation of porcine epidemic diarrhoea (1995) J Comp Pathol, 113, pp. 59-67; Tahir, R.A., Pomeroy, K.A., Goyal, S.M., Evaluation of shell vial cell culture technique for the detection of bovine coronavirus (1995) J Vet Diagn Invest, 7, pp. 301-304; Torres-Medina, A., Schlafer, D.H., Mebus, C.A., Rotaviral and coronaviral diarrhea (1985) Vet Clin North Am Food Anim Pract, 1, pp. 471-493","Dar, A.M.; Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, St. Paul, MN 55108, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"9576342","English","J. Vet. Diagn. Invest.",Review,"Final",Open Access,Scopus,2-s2.0-0032042131
"Hohdatsu T., Yamada M., Tominaga R., Makino K., Kida K., Koyama H.","57197786893;35616061600;7005331040;7202528159;36965056800;7402164528;","Antibody-Dependent Enhancement of Feline Infectious Peritonitis Virus Infection in Feline Alveolar Macrophages and Human Monocyte Cell Line U937 by Serum of Cats Experimentally or Naturally Infected with Feline Coronavirus",1998,"Journal of Veterinary Medical Science","60","1",,"49","55",,26,"10.1292/jvms.60.49","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031607178&doi=10.1292%2fjvms.60.49&partnerID=40&md5=db1b075368e7c4e53336c2eea84d2157","Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan","Hohdatsu, T., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Yamada, M., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Tominaga, R., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Makino, K., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Kida, K., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Koyama, H., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan","Infection of the type II feline infectious peritonitis virus (FIPV) strain 79-1146 to primary feline alveolar macrophages and human monocyte cell line U937 was enhanced by the sera of cats experimentally infected with the 79-1146 strain, but not those of cats infected with KU-2 or UCD-1 strain of type I FIPV. The experiments using sera of cats with feline infectious peritonitis (FIP) and of cats naturally infected with feline coronavirus (FCoV) revealed that infection of the FIPV 79-1146 strain to the U937 cells was enhanced only by the sera of cats infected with type II FIPV or feline enteric coronavirus. The samples positive for antibody-dependent enhancement (ADE) activity had high neutralizing antibody titers against the FIPV 79-1146 strain and the samples negative for ADE activity had low neutralizing antibody titers. These findings support the previous results where a monoclonal antibody with neutralizing activity had high ADE activity, suggesting that there was a close relationship between the neutralization and enhancement sites. And then it is also suggested that ADE of infection is likely to be induced by re-infection with the same serotype of virus in type II FIPV infection. Furthermore, U937 cells are considered useful and can be substituted for the feline macrophages for determining ADE of FIPV-infection.","Antibody-dependent enhancement of infection; Feline infectious peritonitis virus; Feline macrophage; U937 cell","Coronavirus; Enteric coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus; monoclonal antibody; staphylococcus protein A; virus antibody; animal; animal disease; antibody dependent enhancement; article; blood; cat; cat disease; cell line; Coronavirus; drug effect; germfree animal; human; immunology; lung alveolus macrophage; monocyte; physiology; serodiagnosis; virology; virus infection; virus replication; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antibody-Dependent Enhancement; Cat Diseases; Cats; Cell Line; Coronavirus; Coronavirus Infections; Feline Infectious Peritonitis; Humans; Macrophages, Alveolar; Monocytes; Neutralization Tests; Specific Pathogen-Free Organisms; Staphylococcal Protein A; Virus Replication","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab. Anim. Sci., 34, pp. 592-597; Chanas, A.C., Gould, C.A., Clegg, J.C.S., Varma, M.G.R., Monoclonal antibodies to Sindbis virus glycoprotein E1 can neutralize, enhance infectivity, and independently inhibit haemagglutination or haemolysis (1982) J. Gen. Virol., 58, pp. 37-46; Corapi, W.V., Darteil, R.J., Audonnet, J.C., Chappuis, G.E., Localization of antigenic site of the S glycoprotein of feline infectious peritonitis virus involved in neutralization and antibody-dependent enhancement (1995) J. Virol., 69, pp. 2858-2862; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J. Virol., 66, pp. 6695-6705; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Plenum Press, New York and London; Halstead, S.B., Pathogenesis of dengue: Challenges to molecular biology (1988) Science, 239, pp. 476-481; Halstead, S.B., O'Rourke, E.J., Antibody-enhanced dengue virus infection in primate leukocytes (1977) Nature (Lond.), 265, pp. 739-741; Halstead, S.B., O'Rourke, E.J., Dengue viruses and mononuclear phagocytes. I. Infection enhancement by nonneutralizing antibody (1977) J. Exp. Med., 146, pp. 201-217; Halstead, S.B., Venkateshan, C.N., Gentry, M.K., Larsen, L.K., Heterogeneity of infection enhancement of dengue 2 strains by monoclonal antibodies (1984) J. Immunol., 132, pp. 1529-1532; Hohdatsu, T., Nakamura, M., Ishizuka, Y., Yamada, H., Koyama, H., A study on the mechanism of antibody-dependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies (1991) Arch. Virol., 120, pp. 207-217; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Tokunaga, J., Koyama, H., The role of IgG subclass of mouse monoclonal antibodies in antibody-dependent enhancement of feline infectious peritonitis virus infection of feline macrophages (1994) Arch. Virol., 139, pp. 273-285; Hohdatsu, T., Yamada, H., Ishizuka, Y., Koyama, H., Enhancement and neutralization of feline infectious peritonitis virus infection in feline macrophages by neutralizing monoclonal antibodies recognizing different epitopes (1993) Microbiol. Immunol., 37, pp. 499-504; Kimura, T., Ueba, N., Minekawa, Y., Studies on the mechanism of antibody-mediated enhancement of Getah virus infectivity (1981) Biken J., 24, pp. 39-45; Morens, D.M., Halstead, S.B., Measurement of antibody-dependent infection enhancement of four dengue virus serotypes by monoclonal and polyclonal antibodies (1990) J. Gen. Virol., 71, pp. 2909-2914; Morens, D.M., Venkateshan, C.N., Halstead, S.B., Dengue 4 virus monoclonal antibodies identify epitopes that mediate immune infection enhancement of dengue 2 viruses (1987) J. Gen. Virol., 68, pp. 91-98; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Olsen, C.W., Corapi, W.V., Jacobson, R.H., Simkins, R.A., Saif, L.J., Scott, F.W., Identification of antigenie sites mediating antibody-dependent enhancement of feline infectious peritonitis virus infectivity (1993) J. Gen. Virol., 74, pp. 745-749; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Pedersen, N.C., Black, W.B., Attempted immunization of cats against feline infectious peritonitis, using avirulent live virus or sublethal amounts of virulent virus (1983) Am. J. Vet. Res., 44, pp. 229-234; Pedersen, N.C., Black, J.W., Boyle, J.F., Everman, J.F., Mckeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Everman, J.F., Mckeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Peiris, J.S.M., Porterfield, J.S., Antibody-mediated enhancement of Flavivirus replication in macrophage-like cell lines (1979) Nature (Lond.), 282, pp. 509-511; Schlesinger, J.J., Brandriss, M.W., Growth of 17 D yellow fever virus in a macrophage-like cell line, U937: Role of Fc and viral receptors in antibody-mediated infection (1981) J. Immunol., 127, pp. 659-665; Stoddart, C.A., Barlough, J.E., Baldwin, C.A., Scott, F.W., Attempted immunisation of cats against feline infectious peritonitis using canine coronavirus (1988) Res. Vet. Sci., 45, pp. 383-388; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Pearson, G.R., The sites of early viral replication in feline infectious peritonitis (1988) Vet. Microbiol., 18, pp. 259-271; Takeda, A., Tuazon, C.V., Ennis, F.A., Antibody-enhanced infection by HIV-1 via Fc receptor-mediated entry (1988) Science, 242, pp. 580-583; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: Comparisons with dengue hemorrhagic fever (1981) Comp. Immunol. Microbiol. Infect. Dis., 4, pp. 175-189; Woods, R.D., Pedersen, N.C., Cross-protection studies between feline infectious peritonitis and porcine transmissible gastroenteritis viruses (1979) Vet. Microbiol., 4, pp. 11-16","Hohdatsu, T.; Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan",,"Maruzen Co. Ltd.",09167250,,,"9492360","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0031607178
"Sola I., Castilla J., Pintado B., Sánchez-Morgado J.M., Whitelaw C.B.A., Clark A.J., Enjuanes L.","7003336781;8851950500;6701776268;6602349176;7004304428;7404479867;7006565392;","Transgenic mice secreting coronavirus neutralizing antibodies into the milk",1998,"Journal of Virology","72","5",,"3762","3772",,45,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031980306&partnerID=40&md5=e798312d95f4966aaf86b64b96101001","Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Depto. de Reproducción Animal, Inst. Nac. de Invest. Agrarias, 28040 Madrid, Spain; Division of Molecular Biology, Roslin Institute, Midlothian EH25 9PS, United Kingdom","Sola, I., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Castilla, J., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Pintado, B., Depto. de Reproducción Animal, Inst. Nac. de Invest. Agrarias, 28040 Madrid, Spain; Sánchez-Morgado, J.M., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Whitelaw, C.B.A., Division of Molecular Biology, Roslin Institute, Midlothian EH25 9PS, United Kingdom; Clark, A.J., Division of Molecular Biology, Roslin Institute, Midlothian EH25 9PS, United Kingdom; Enjuanes, L., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Ten lines of transgenic mice secreting transmissible gastroenteritis coronavirus (TGEV) neutralizing recombinant monoclonal antibodies (rMAbs) into the milk were generated. The rMAb light- and heavy-chain genes were assembled by fusing the genes encoding the variable modules of the murine MAb 6A. C3, which binds an interspecies conserved coronavirus epitope essential for virus infectivity, and a constant module from a porcine myeloma with the immunoglobulin A (IgA) isotype. The chimeric antibody led to dimer formation in the presence of J chain. The neutralization specific activity of the recombinant antibody produced in transiently or stably transformed cells was 50-fold higher than that of a monomeric rMAb with the IgG1 isotype and an identical binding site. This rMAb had titers of up to 104 by radioimmunoassay (RIA) and neutralized virus infectivity up to 104- fold. Of 23 transgenic mice, 17 integrated both light and heavy chains, and at least 10 of them transmitted both genes to the progeny, leading to 100% of animals secreting functional TGEV neutralizing antibody during lactation. Selected mice produced milk with TGEV-specific antibody titers higher than 106 as determined by A, neutralized virus infectivity by 10-fold, and produced up to 6 mg of antibody per ml. Antibody expression levels were transgene copy number independent and integration site dependent. Comicroinjection of the genomic β-lactoglobulin gene with rMAb light and heavy-chain genes led to the generation of transgenic mice carrying the three transgenes. The highest antibody titers were produced by transgenic mice that had integrated the antibody and β-lactoglobulin genes, although the number of transgenic animals generated does not allow a definitive conclusion on the enhancing effect of β-lactoglobulin cointegration. This approach may lead to the generation of transgenic animals providing lactogenic immunity to their progeny against enteric pathogens.",,"immunoglobulin G1; monoclonal antibody; neutralizing antibody; virus antibody; animal experiment; antibody production; antibody titer; article; Coronavirus; gastroenteritis; host resistance; infection resistance; milk level; mouse; nonhuman; passive immunization; priority journal; progeny; radioimmunoassay; transgenic mouse","Ali, S., Clark, A.J., Characterization of the gene encoding ovine β-lactoglobulin (1988) J. Mol. 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Biol., 11, pp. 3070-3074; Clark, A.J., Archibald, A.L., McClenaghan, M., Simons, J.P., Wallace, R., Whitelaw, C.B.A., Enhancing the efficiency of transgene expression (1993) Transgenic Res. Soc. London, 339, pp. 225-232; Clark, A.J., Cowper, A., Wallace, R., Wright, G., Simons, J.P., Rescuing transgene expression by co-integration (1992) Bio/Technology, 10, pp. 1450-1454; Correa, I., Gebauer, F., Bullido, M.J., Suñé, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus (1990) J. Gen. Virol., 71, pp. 271-279; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-94; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. 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Immunol., 3, pp. 425-453; Lamm, M.E., Nedrud, J.G., Kaetzel, C.S., Mazanec, M.B., IgA and mucosal defense (1995) APMIS, 103, pp. 241-246; Lammers, B.M., Beaman, K.D., Kim, Y.B., Sequence analysis of porcine immunoglobulin light chain cDNAs (1991) Mol. Immunol., 28, pp. 877-880; Lee, K.F., DeMayo, J., Alice, S.H., Rosen, J.M., Tissue-specific expression of the rat β-casein gene in transgenic mice (1988) Nucleic Acids Res., 16, pp. 1027-1041; Lee, S.H., De Boer, H.A., Production of biomedical proteins in the milk of transgenic dairy cows: The state of the art (1994) J. Controlled Release, 29, pp. 213-221; Limonta, J., Pedraza, A., Rodríguez, A., Freyre, F.M., Barral, A.M., Castro, F.O., Lleonart, R., De La Fuente, J., Production of active anti-CD6 mouse-human chimeric antibodies in the milk of transgenic mice (1995) Immunotechnology, 1, pp. 107-113; Liu, A.Y., Mack, P.W., Champion, C.I., Robinson, R.R., Expression of mouse:human immunoglobulin heavy chain cDNA in lymphoid cells (1987) Gene, 54, pp. 33-40; Mazanec, M.B., Kaetzel, C.S., Lamm, M.E., Fletcher, D., Nedrud, J.G., Intracellular neutralization of virus by immunoglobulin A antibodies (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 6901-6905; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. 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USA, 81, pp. 7161-7165; Randall, T.D., Parkhouse, R.M.E., Corley, R.B., J chain synthesis and secretion of hexameric IgM is differentially regulated by lipopolysaccharide and interleukin 5 (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 962-966; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., pp. 362-386. , A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor (ed.), Wolfe Publishing Ltd, Ames, Iowa; Sanchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sauger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Simons, J.P., McClenaghan, M., Clark, A.J., Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice (1987) Nature, 328, pp. 530-532; Staats, H.F., Jackson, R.J., Marinaro, M., Takahashi, I., Kiyono, H., McGhee, J.R., Mucosal immunity to infection with implications for vaccine development (1994) Curr. Opin. Immunol., 6, pp. 572-583; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Torres, J.M., Sánchez, C.M., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; VanCott, J.L., Brim, T.A., Simkins, R.A., Sait, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Weidle, U.H., Koch, S., Buckel, P., Expression of antibody cDNA in murine myeloma cells: Possible involvement of additional regulatory elements in transcription of immunoglobulin genes (1987) Gene, 60, pp. 205-216; Weidle, U.H., Lenz, H., Brem, G., Genes encoding a mouse monoclonal antibody are expressed in transgenic mice, rabbits and pigs (1991) Gene, 98, pp. 185-191; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet. Microbiol., 18, pp. 197-208; Whitelaw, C.B.A., Archibald, A.L., Harris, S., McClenaghan, M., Simons, L.P., Clark, A.J., Targeting expression to the mammary gland: Intronic sequences can enhance the efficiency of gene expression in transgenic mice (1991) Transgenic Res., 1, pp. 3-13; Wright, G., Carver, A., Cottom, D., Reeves, D., Scott, A., Simons, P., Wilmut, I., Colman, A., High level expression of active human alpha-1-antitrypsin in the milk of transgenic sheep (1991) Bio/Technology, 9, pp. 830-834; Xoma Co. May 1987. U.S. Patent WO 87/02671; Zikan, J., Novotny, J., Trapane, T.L., Koshland, M.E., Urry, D.W., Bennett, J.C., Mestecky, J., Secondary structure of the immunoglobulin J chain (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 5905-5909","Enjuanes, L.; Centro Nacional de Biotecnologfa, CSIC, Department of Molecular/Cell Biology, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,"American Society for Microbiology",0022538X,,JOVIA,"9557658","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031980306
"Palmer-Densmore M.L., Johnson A.F., Sabara M.I.J.","36897518900;55696400500;6604020621;","Development and evaluation of an ELISA to measure antibody responses to both the nucleocapsid and spike proteins of canine coronavirus",1998,"Journal of Immunoassay","19","1",,"1","22",,8,"10.1080/01971529808005468","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031884388&doi=10.1080%2f01971529808005468&partnerID=40&md5=d353b7351fdf0dd0bf983aff0d48512c","Pfizer Inc., Central Research Division, 601 West Cornhusker Hwy., Lincoln, NE 68521-3596, United States; Pfizer Inc., 6601 Rexford Drive, Lincoln, NE 68506, United States","Palmer-Densmore, M.L., Pfizer Inc., Central Research Division, 601 West Cornhusker Hwy., Lincoln, NE 68521-3596, United States; Johnson, A.F., Pfizer Inc., Central Research Division, 601 West Cornhusker Hwy., Lincoln, NE 68521-3596, United States; Sabara, M.I.J., Pfizer Inc., Central Research Division, 601 West Cornhusker Hwy., Lincoln, NE 68521-3596, United States, Pfizer Inc., 6601 Rexford Drive, Lincoln, NE 68506, United States","A rapid and reproducible enzyme linked immunosorbent assay (ELISA) was developed for detection of canine coronavirus (CCV) specific antibodies directed to both the nucleocapsid (NC) and the spike (s) proteins. The coating antigen, a methanol-treated, S-protein enriched preparation, was produced by subjecting infected cells to Triton X-114 detergent followed by phase separation. The sensitivity of this assay was determined by following the course of infection in dogs experimentally infected with CCV. The specificity of the antibody response was determined by Western blot analysis and supported the increase magnitude of the ELISA response and the presence of serum neutralizing (SN) antibody. Due to the sensitivity and specificity of the IgG response detected by this assay it can be used to determine both virus exposure and vaccine efficacy.","CCV; Coating antigen preparation; Enzyme immunoassay; Methanol; Triton X- 114","neutralizing antibody; vaccine; virus protein; animal experiment; antibody detection; antibody response; article; Coronavirus; diagnostic accuracy; dog; enteritis; enzyme linked immunosorbent assay; fluorescent antibody technique; immunoblotting; nonhuman; vaccine production; virus detection; virus nucleocapsid","Appel, M., Canine coronavirus (1987) Virus Infections of Carnivores, pp. 115-122. , Ed M. Appel, New York, Elsevier; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhoea (1974) Proceedings of the 78th Meeting of the US Animal Health Association, pp. 359-366; Vandenberghe, J., Ducatelle, R., Debouck, P., Hoorens, J., Coronavirus infection in a litter of pups (1980) Vet. Quart., 2, pp. 136-141; Mostl, V.K., Buxbaum, A., Odorfer, G., Verbreitung und Bedeutung von Coronavirus-infektionen in heimishchen Hundepopulationen (1994) Wien. Tierarztl. Mschr., 81, pp. 355-361; Miller, J., Immunofluorescence test for canine coronavirus and parvovirus (1980) Western Vet., 18 (1), pp. 14-19; Heifer-Baker, C.J., Evermann, J.F., McKeirnan, A.J., Morrison, W.B., Serological studies on the incidence of canine enteritis viruses (1980) Can. Pract., 7, pp. 37-42; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H.A., UytdeHaag, F.G.C.M., Osterhaus, A.D.M.E., The use of enzyme-linked immunosorbent assay systems for serology and antigen detections in parvovirus, corornavirus and rotavirus infection in dogs in the Netherlands (1991) Vet. Microbiol., 25, pp. 25-40; Tuchiya, K., Horimoto, T., Azetaka, M., Takahashi, E., Konishi, S., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet. Microbiol., 26, pp. 41-51; Martin-Calvo, M., Marcotegui, M.A., Simarro, I., Canine-coronavirus (CCV) characterization in Spain epidemiological aspects (1994) J. Vet. Med., 41, pp. 249-256; Gaskell, R., Gaskel, C.J., Denis, D.E., Wooldridge, M.J.A., Efficacy of an inactivated feline calicivirus (FCV) vaccine against challenge with United Kingdom field strains and its interaction with the FCV carrier state (1982) Res. Vet. Sci., 32, pp. 23-26; Tuchiya, K., Kasaoka, T., Azetaka, M., Takahashi, E., Konishi, S., Plaque assay for canine coronavirus in CRFK cells (1987) Jpn. J. Vet. Sci., 49, pp. 571-573; Binn, L.N., Marchwicki, R.H., Stephenson, E.H., Establishment of a canine cell line: Derivation, characterization and viral spectrum (1980) Am. J. Vet. Res., 41, pp. 855-860; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Gaskell, C.J., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Garwes, D.J., Lucas, M.H., Higgins, D.A., Pike, B.V., Cartwright, S.F., Antigenicity of structural components from porcine transmissible gastroenteritis virus (1978) Vet. Microbiol., 3, pp. 179-183; Garwes, D.J., Reynolds, D.J., The polypeptide structure of canine coronavirus and its relationship to porcine-transmissible gastorenteritis virus (1981) J. Gen. Virol., 52, pp. 153-157; Cavanagh, D., Structural polypeptides of coronavirus IBV (1981) J. Gen. Virol., 53, pp. 93-103; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from gels to nitrocellulose sheets, procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354; Horzinek, M.C., Lutz, H., Pederson, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect. Immun., 37, pp. 1148-1151; Hasony, H.J., Macnaughton, M.R., Antigenicity of mouse hepatitis virus strain 3 subcomponents in C57 strain mice (1981) Arch. Virol., 69, pp. 33-41; Venema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Immunogenicity of recombinant feline infectious peritonitis virus spike protein in mice and kittens (1990) Coronaviruses and Their Diseases, pp. 217-222. , D. Cavanagh and T.D.K. Brown (Eds), Plenum Press, New York; De Diego, M., Laviada, M.D., Enjuanes, L., Escribano, J.M., Epitope specificity of protective lactogenic transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 6502-6508; Ricard, C.S., Sturman, L.S., Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite high-performance liquid chromatography (1985) J. Chrom., 326, pp. 191-197; Pryde, J.G., Triton X-114: A detergent that has come in from the cold (1986) TIBS, 11, pp. 160-163; Bordier, C., Phase separation of integral membrane proteins in Triton X-114 solution (1981) J. Biol. Chem., 256, pp. 1604-1607; Brusca, J.S., Radolf, J.D., Isolation of Integral membrane proteins by phase partitioning with Triton X-114 (1994) Meth. in Enzymol., 228, pp. 182-193; Helenius, A., Simons, K., Solubilization of membranes by detergents (1975) Biochim. Biophys. Acta, 415, pp. 29-79; Hooper, N.M., Bashir, A., Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X-114 (1991) Biochem. J., 280, pp. 745-751; Clemetson, K.J., Bienz, D., Zahno, M.-L., Luscher, E.F., Distribution of platelet glycoproteins and phosphoproteins in hydrophobic and hydrophilic phases in Triton X-114 phase partition (1984) Biochim. et Biophys. Acta, 778, pp. 463-469; Maher, P.A., Singer, S.J., Anomalous interaction of the acetylcholine receptor protein with the nonionic detergent Triton X-114 (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 958-962; Pryde, J.G., Phillips, J.H., Fractionation of membrane proteins by temperature-induced phase separation in Triton X-114 (1986) Biochem. J., 233, pp. 525-533; Lang, E., Szendrei, G.I., Lee, V.M.-Y., Otvos Jr., L., Spectroscopic evidence that monoclonal antibodies recognize the dominant conformation of medium-sized synthetic peptides (1994) J. Immunol. Meth., 170, pp. 103-115","Palmer-Densmore, M.L.; Pfizer Inc., Central Research Division, 601 West Cornhusker Hwy., Lincoln, NE 68521-3596, United States",,"Marcel Dekker Inc.",01971522,,JOUID,"9530608","English","J. Immunoassay",Article,"Final",Open Access,Scopus,2-s2.0-0031884388
"Fukai K., Sakai T., Fujita K., Abe S.","7006195783;7404832007;7404058999;7403335373;","Evaluation of serum neutralizing antibodies to bovine coronavirus in cows and their calves using Hmlu-1 cells",1998,"Indian Journal of Medical Research","107","JULY",,"8","11",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032109389&partnerID=40&md5=3dad6b426291410fb65dacb9c295acd9","Dept. of Prev. Veterinary Medicine, Nihon Univ. Sch. of Vet. Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan","Fukai, K., Dept. of Prev. Veterinary Medicine, Nihon Univ. Sch. of Vet. Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan; Sakai, T., Dept. of Prev. Veterinary Medicine, Nihon Univ. Sch. of Vet. Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan; Fujita, K., Dept. of Prev. Veterinary Medicine, Nihon Univ. Sch. of Vet. Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan; Abe, S., Dept. of Prev. Veterinary Medicine, Nihon Univ. Sch. of Vet. Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan","Between 1992 and 1993, 75 paired serum samples from Holstein dairy cows and their calves were collected from Aomori, Tochigi and Okinawa Prefectures, and the neutralizing antibody titres to bovine coronavirus (BCV) were determined using hamster lung (Hmlu)-1 cells. The anti-BCV antibody positive rate in the maternal serum samples was significantly lower (P < 0.001) in Okinawa (72%) than in Aomori (100%) or Tochigi (100%). The geometric mean titre (GMT) of anti-BCV neutralizing antibody was also significantly lower (P < 0.05) in maternal sera from Okinawa (89) than that of Aomori (229) or Tochigi (264). The anti-BCV neutralizing antibody titres in the sera of calves which had ingested the colostrum, significantly correlated with the antibody concentration of the maternal serum samples (P < 0.05). These results suggest an extensive BCV infection among the dairy cattle in these prefectures, with a varied pattern of distribution between the prefectures. Anti-BCV neutralizing antibody in the sera of newborn calves appeared to be transferred from their dams through colostrum.","Bovine coronavirus; Hmlu-1 cells; Neutralizing antibody; Seroepidemiology","neutralizing antibody; virus antibody; animal cell; animal experiment; animal tissue; antibody blood level; antibody titer; article; cattle; cattle disease; cell line; colostrum; controlled study; coronavirus; female; geographic distribution; hamster; japan; maternal serum; newborn; nonhuman; seroepidemiology; virus infection; virus transmission; animal; blood; cell culture; Coronavirus; immunology; serodiagnosis; Animals; Antibodies, Viral; Cattle; Cells, Cultured; Coronavirus, Bovine; Cricetinae; Female; Neutralization Tests","Akashi, H., Inaba, Y., Miura, Y., Tokuhisa, S., Sato, K., Satoda, K., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet Microbiol, 5, pp. 265-276; Mebus, C.A., Kono, M., Underdahl, N.R., Twiehaus, M.J., Cell culture propagation of neonatal calf diarrhea (scours) virus (1971) Can Vet J, 12, pp. 69-72; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am J Vet Res, 37, pp. 1031-1041; Stair, E.L., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am J Vet Res, 33, pp. 1147-1156; Takahashi, E., Inaba, Y., Sato, K., Ito, Y., Kurogi, H., Akashi, H., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase gene of human coronavirus strain OC43: Phylogenetic relationships to bovine and murine coronavirus and influenza C virus (1992) Virology, 186, pp. 318-323; Shiraishi, T., Harada, K., Takase, M., Itazaki, K., Kurihara, K., Hara, F., Outbreaks of diarrhea in cows by bovine coronavirus infection (1980) J Jpn Vet Med Assoc, 33, pp. 70-74; Taniguchi, S., Iwamoto, H., Fukuura, H., Ito, H., Kaigai, N., Nagato, T., Recurrence of bovine coronavirus infection in cows (1986) J Jpn Vet Med Assoc, 39, pp. 298-302; Tsunemitsu, H., Tonemichi, H., Hirai, T., Kubo, T., Ones, S., Mori, K., Isolation of bovine coronavirus from faeces and nasal swabs of calves with diarrhea (1991) J Vet Ned Sci, 53, pp. 433-437; Collins, J.K., Riegel, C.A., Olson, J.D., Fountain, A., Shedding of enteric coronavirus in adult cattle (1987) Am J Vet Res, 48, pp. 361-365; Crouch, C.F., Ohmann, H.B., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Gerna, G., Cereda, P.M., Revello, M.G., Cattaneo, E., Battaglia, M., Gerna, M.T., Antigenic and biological relationships between human coronavirus OC43 and neonatal calf diarrhoea coronavirus (1981) J Gen Virol, 54, pp. 91-102; Storz, J., Rott, R., Reactivity of antibodies in humans serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol (Berl), 169, pp. 169-178; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet Microbiol, 22, pp. 187-201; Abraham, G., Roeder, P.L., Zewdu, R., Agents associated with neonatal diarrhea in Ethiopian dairy calves (1992) Trop Anim Health Prod, 24, pp. 74-80; House, J.A., Economic impact of rotavirus and other neonatal disease agents of animals (1987) J Am Vet Med Assoc, 173, pp. 573-576; Moon, H.W., McClurkin, A.W., Issacson, R.E., Pohlenz, J., Slartvedt, S.M., Gillette, K.G., Pathogenic relationships of rotavirus, Escherichia coli and other agents in mixed infections in calves (1978) J am Vet Med Assoc, 173, pp. 577-583; Thorns, C.J., Bell, M.M., Chasey, D., Chesham, J., Roeder, P.L., Development of monoclonal antibody ELISA for simultaneous detection of bovine coronavirus, rotavirus serogroup A, and Escherichia coli K99 antigen in faeces of calves (1992) Am J Vet Res, 53, pp. 36-43; Caul, E.O., Paver, W.K., Clarke, S.K.R., Coronavirus particles in faeces from patients with gastroenteritis (1975) Lancet, 1, p. 1192; Caul, E.O., Clarke, S.K.R., Coronavirus propagated from patient with non-bacterial gastroenteritis (1975) Lancet, 2, pp. 953-954; Kate, H.S., Yarbrough, W.B., Reed, C.J., Calf diarrhoea coronavirus (1975) Lancet, 2, p. 509; Hogoue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J Virol, 51, pp. 384-388; Kunkel, F., Herrler, G., Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202","Sakai, T.; Dept Prev Veter Med Animal Health, Nihon University, School of Veterinary Medicine, 1866 Kameino, Fujisawa, Kanagawa 252-0813, Japan",,,09715916,,IMIRE,"9745212","English","Indian J. Med. Res.",Article,"Final",,Scopus,2-s2.0-0032109389
"Sola I., Castilla J., Enjuanes L.","7003336781;8851950500;7006565392;","Interference of coronavirus infection by expression of IgG or IgA virus neutralizing antibodies",1998,"Advances in Experimental Medicine and Biology","440",,,"665","674",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783282&partnerID=40&md5=539971e90b0e1d75ffeda094c57a5299","Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CSIC), Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain","Sola, I., Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CSIC), Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Castilla, J., Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CSIC), Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CSIC), Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain","Mouse immunoglobulin gene fragments encoding the variable modules of the heavy (VH) and light (VL) chains of a transmissible gastroenteritis coronavirus (TGEV) neutralizing monoclonal antibody (MAb) have been cloned and sequenced. The selected MAb recognizes a highly conserved viral epitope and does not lead to the selection of neutralization escape mutants. Chimeric immunoglobulin genes with the variable modules from the murine MAb and constant modules of human gamma I and kappa chains were constructed using RT- PCR. These chimeric immunoglobulins were stably or transiently expressed in murine myelomas and COS cells, respectively. The secreted recombinant antibodies had radioimmunoassay (RIA) titers higher than 103 and reduced the infectious virus more than 104-fold. Recombinant dimeric IgA showed a 50- fold enhanced neutralization of TGEV relative to a recombinant monomeric IgG1 which contained the identical antigen binding site. Epithelial cell lines stably-transformed with these constructs and expressing either recombinant IgG or IgA TGEV neutralizing antibodies reduced virus production by &gt;105- fold after infection with homologous virus, although a residual level of virus production (&lt;102 PFU/ml) remained in less than 0.1 % of the cells.",,"monoclonal antibody; neutralizing antibody; animal cell; antibody production; antibody titer; antigen binding; article; Coronavirus; gene sequence; immunofluorescence microscopy; molecular cloning; mouse; nonhuman; priority journal; reverse transcription polymerase chain reaction; RNA virus infection; virus inhibition; Animalia; Coronavirus; Murinae; RNA viruses; Transmissible gastroenteritis virus","Armstrong, S.J., Outlaw, M.C., Dimmock, N.J., Morphological studies of neutralization of influenza virus by IgM (1990) J. Gen. Virol., 71, pp. 2313-2319; Bullido, M.J., Correa, I., Jiménez, G., Suñé, C., Gebauer, F., Enjuanes, L., Induction of transmissible gastroenteritis coronavirus-neutralizing antibodies in vitro by virus-specific T helper cell hybridomas (1989) J. Gen. Virol., 70, pp. 659-672; Castilla, J., Sola, I., Enjuanes, L., Interference of coronavirus infection by expression of immunoglobulin G (IgG) or IgA virus-neutralizing antibodies (1997) J. Virol., 71, pp. 5251-5258; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus. Res., 10, pp. 77-94; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , (S. G. Siddell, eds.), Plenum Press, New York; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Marasco, W.A., Haseltine, W.A., Chen, S., Design, intracellular expression, and activity of a human anti-human immunodeficiency virus type 1 gp120 single-chain antibody (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 7889-7893; Mazanec, M.B., Coudret, C.L., Fletcher, D.R., Intracellular neutralization of influenza virus by immunoglobulin a anti-hemagglutinin monoclonal antibodies (1995) J. Virol., 69, pp. 1339-1343; Mazanec, M.B., Kaetzel, C.S., Lamm, M.E., Fletcher, D., Nedrud, J.G., Intracellular neutralization of virus by immunoglobulin A antibodies (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 6901-6905; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci., 30, pp. 190-198; McGhee, J.R., Mestecky, J., Elson, C.O., Kiyono, H., Regulation of IgA synthesis and immune response by T cells and interleukins (1989) J. Clin. Immunol., 9, pp. 175-199; Mestecky, J., McGhee, J.R., Immunoglobulin a (IgA): Molecular and cellular interactions involved in IgA biosynthesis and immune response (1987) Adv. Immunol., 40, pp. 153-245; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , (A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor, eds.), Wolfe Publishing Ltd, Ames. Iowa; Sanchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sola, I., Castilla, J., Pintado, B., Sánchez-Morgado, J.M., Whitelaw, B., Clark, J., Enjuanes, L., Transgenic mice secreting coronavirus neutralizing antibodies into the milk (1998) J. Virol., 72, pp. 3762-3772; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG, and IgM(A) to protect neonatal pigs against the coronavirus transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569","Sola, I.; Centro Nacional de Biotecnologia, Consejo Sup. de Invest. Cientificas, Dept. of Molecular and Cell Biology, 28049 Madrid, Spain",,"Springer New York LLC",00652598,,AEMBA,"9782343","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783282
"Pénzes Z., González J.M., Izeta A., Muntión M., Enjuanes L.","55761804900;57201828108;6602523425;8114506300;7006565392;","Progress towards the construction of a transmissible gastroenteritis coronavirus self-replicating RNA using a two-layer expression system",1998,"Advances in Experimental Medicine and Biology","440",,,"319","325",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753582&partnerID=40&md5=586790b707161a0c0be55f87c279d0fb","Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Pénzes, Z., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; González, J.M., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Muntión, M., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Three transmissible gastroenteritis coronavirus (TGEV) defective interfering RNAs of 21, 10.6 and 9.7 kb (DI-A, DI-B and DI-C, respectively) were isolated. Dilution experiments showed that the largest DI RNA, DI-A, is a self-replicating RNA (replicon), and thus codes for a functional RNA polymerase and all the necessary replication signals. In order to engineer a cDNA encoding the RNA replicon a strategy based on the cloning of DI-C cDNA, followed by the insertion of the sequences required to complete the DI-A sequence has been developed. A cDNA complementary to DI-C RNA was cloned under the control of the CMV promoter (pDI-C-CMV) and rescued with a helper virus. In the ORF 1a of polymerase gene pDI-C-CMV contained a 10 kb deletion and in ORF lb a 1.1 kb deletion. The consensus sequence corresponding to the deleted regions was cloned, and the deletions in pDI-C-CMV were replaced to yield a complete cDNA clone of DI-A, pDI-A-21-CMV, containing a full-length TGEV polymerase, driven by a CMV promoter. Expression of a functional TGEV polymerase is being investigated.",,"complementary DNA; virus RNA; article; Coronavirus; gastroenteritis; nonhuman; priority journal; promoter region; replicon; RNA replication; virus replication; virus transmission; Coronavirus; Cucumber mosaic virus; RNA viruses; Transmissible gastroenteritis virus","Dubensky, J., W., T., Driver, D.A., Polo, J.M., Belli, B.A., Latham, E.M., Ibanez, C.E., Chang, S.M.W., Sindbis virus DNA-based expression vectors: Utility for in vitro and in vivo gene transfer (1996) J. Virol., 70, pp. 508-519; Izeta, A., Smerdou, C., Mendez, A., Alonso, S., Pénzes, Z., Enjuanes, L., Replication and packaging of synthetic minigenomes derived from defective transmissible gastroenteritis coronavirus (1997) J. Virol., , Manuscript submitted; Makino, S., Shieh, C.K., Keck, J.G., Lai, M.M.C., Defective-interfering particles of murine coronaviruses: Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Ruggli, N., Tratschin, J.D., Mittelholzer, C., Hofmann, M.A., Nucleotide sequence of classical swine fever virus strain Alfort/187 and transcription of infectious RNA from stably cloned full-length cDNA (1996) J. Virol., 70, pp. 3478-3487; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory, Cold Spring Harbor, New York; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417","Penzes, Z.; Veterinary Med. Research Institute, Hungarian Academy of Sciences, Budapest, Hungary",,"Springer New York LLC",00652598,,AEMBA,"9782299","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753582
"Kwon H.M., Saif L.J., Jackwood D.J.","7401838151;7102226747;7005468303;","Field Isolates of Transmissible Gastroenteritis Virus Differ at the Molecular Level from the Miller and Purdue Virulent and Attenuated Strains and from Porcine Respiratory Coronaviruses",1998,"Journal of Veterinary Medical Science","60","5",,"589","597",,15,"10.1292/jvms.60.589","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032061957&doi=10.1292%2fjvms.60.589&partnerID=40&md5=1bf42a09a7ff746e3664b7da51b3b3c7","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Department of Veterinary Medicine, Kangwon National University, Chunchon 200-701, Kangwon-Do, South Korea","Kwon, H.M., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Department of Veterinary Medicine, Kangwon National University, Chunchon 200-701, Kangwon-Do, South Korea; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Jackwood, D.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States","The diversity in selected regions of the transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) genomes was analyzed among known TGEV and PRCV strains and field isolates. The N-terminal half of the spike (S) glycoprotein gene and open reading frames (ORF) 3, 3-1 and 4 were amplified by reverse transcriptase reaction and polymerase chain reaction (RT/PCR), and analyzed using restriction fragment length polymorphism (RFLP) patterns of the amplified DNA. Reference TGEV strains (Miller and Purdue) and a PRCV strain (ISU-I), and TGEV and PRCV field isolates were analyzed. Based on the size of the ORF 3, 3-1 and 4 RT/PCR products. TGEV and PRCV strains could be quickly and easily differentiated into three groups designated TGEV Miller, Purdue types and PRCV. By RFLP analysis of the N-terminal region of the S glycoprotein gene and ORFs 3, 3-1 and 4, TGEV and PRCV strains were differentiated into five groups using the restriction enzyme SauI. Sequence analysis of a PCR product in the ORFs 3, 3-1 and 4 from virulent and attenuated Miller strains demonstrated additional differences in that region which have been correlated with a change in virulence of TGEV isolates.","Coronavirus; PRCV; RT/PCR-RFLP analysis; TGEV","Acronicta leporina; Coronavirus; Porcine respiratory coronavirus; Suidae; Transmissible gastroenteritis virus; animal; animal disease; Arterivirus; article; cell culture; cytology; gene deletion; genetic variability; genetics; isolation and purification; male; molecular genetics; nucleotide sequence; open reading frame; polymerase chain reaction; restriction fragment length polymorphism; sequence homology; swine; swine disease; testis; Transmissible gastroenteritis virus; virology; virus genome; virus infection; Animals; Base Sequence; Cells, Cultured; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Genome, Viral; Male; Molecular Sequence Data; Open Reading Frames; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Porcine Reproductive and Respiratory Syndrome; Porcine respiratory and reproductive syndrome virus; Sequence Deletion; Sequence Homology, Nucleic Acid; Swine; Testis; Transmissible gastroenteritis virus; Variation (Genetics)","Bae, I., Jackwood, D.J., Benfield, D.A., Saif, L.J., Wesley, R.D., Hill, H., Differentiation of transmissible gastroenteritis virus from porcine respiratory coronavirus and other antigenically related coronaviruses by using cDNA probes specific for the 5' region of the S glycoprotein gene (1991) J. Clin. Microbiol., 29, pp. 215-218; Britton, P., Kottier, S., Chen, C.-M., Pocock, D.H., Salmon, H., Aynaud, J.M., The use of PCR genome mapping for the characterisation of TGEV strains (1994) Coronaviruses, , Laude, H. and Vautherot, J. F. eds., Plenum Press, New York; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein (1986) J. Gen. Virol., 67, pp. 1405-1418; Delmas, B., Laude, H., Carbohydrate-induced conformational changes strongly modulate the antigenicity of coronavirus TGEV glycoproteins S and M (1991) Virus Res., 20, pp. 107-120; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S (1990) J. Gen. Virol., 71, pp. 1313-1323; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch. Virol., 104, pp. 241-248; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Garwes, D.J., Lucas, M.H., Higging, D.A., Pike, B.V., Cratwright, S.F., Antigenicity of structural components from porcine transmissible gastroenteritis virus (1978) Vet. Microbiol., 3, pp. 179-190; Garwes, D.J., Pocock, D.H., The polypeptide structure of transmissible gastroenteritis virus (1975) J. Gen. Virol., 29, pp. 25-34; Garwes, D.J., Reynolds, D.J., The polypeptide structure of canine coronavirus and its relationship to protein transmissible gastroenteritis virus (1981) J. Gen. Virol., 52, pp. 153-157; Gelb Jr., J., Wolff, J.B., Moran, C.A., Variant serotypes of infectious bronchitis virus isolated from commercial layer and broiler chickens (1991) Avian Dts., 35, pp. 82-87; Godet, M., L'haridon, R., Vautherot, J.-F., Laude, H., TGEV corona virus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Godet, M., Rasschaert, D., Laude, H., Processing and antigenicity of entire and anchor-free spike glycoprotein S of coronavirus TGEV expressed by recombinant baculovirus (1991) Virology, 186, pp. 732-740; Halbur, G.H., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J. Vet. Diagn. Invest., 5, pp. 184-188; Have, P., Infection with a new porcine respiratory coronavirus in Denmark: Serologic differentiation from transmissible gastroenteritis virus using monoclonal antibodies (1990) Coronaviruses and Their Diseases, pp. 435-439. , (Cavanagh, D. and Brown, T. D. K. eds.), Plenum Press, New York; Hohdatsu, T., Eiguchi, Y., Tsuchimoto, M., Ide, S., Yamagishi, H., Matumoto, M., Antigenic variation of porcine transmissible gastroenteritis virus detected by monoclonal antibodies (1987) Vet. Microbiol., 14, pp. 115-124; Horzinek, M., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polpeptides of porcine, feline, and canine coronaviruses (1982) Inject. Immun., 37, pp. 1148-1155; Jacobs, L., Van Der Zeijst, B.A.M., Horzinek, M.C., Characterizatioin and translation of transmissible gastroenteritis virus mRNAs (1986) J. Virol., 57, pp. 1010-1015; Jimenez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Kemeny, L.J., Antibody response in pigs inoculated with transmissible gastroenteritis virus and cross reactions among ten isolates (1976) Can. J. Comp. Med., 40, pp. 209-214; Kwon, H.M., Jackwood, M.W., Gelb Jr., J., Differentiation of infectious bronchitis virus serotypes using the polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Dis., 37, pp. 194-202; Kusukawa, N., Uemori, T., Asada, K., Kato, I., Rapid and reliable protocol for direct sequencing of material amplified by the polymerase chain reaction (1990) BioTechniques, 9, pp. 66-72; Laude, H., Chapsal, J.-M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Laude, H., Rasschaert, D., Huet, J.C., Sequence and N-terminal processing of the membrane protein E1 of the coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1687-1693; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common 10 five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Med., 30, pp. 190-198; Page, K.W., Mawditt, K.L., Britton, P., Sequence comparison of the 5' end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J. Gen. Virol., 72, pp. 579-587; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA its organization and expression (1987) Biochimie, 69, pp. 591-600; Rasschaert, D., Laude, H., The predicted primary structure of the peplomer protein E2 of the porcine coronavirus transmissible gastroenteritis virus (1987) J. Gen. Virol., 68, pp. 1883-1890; Register, K.B., Wesley, R.D., Molecular characterization of attenuated vaccine strains of transmissible gastroenteritis virus (1994) J.Vet. Diagn. Invest., 6, pp. 16-22; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , Leman, A. D., Straw, B. E. and Mengeling, W. L. eds.. Iowa State University Press, Ames. IA; Sambrook, J., Frifsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual. 2nd Ed., , Cold Spring Harbor Laboratory Press, New York; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronavirus related 10 transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. U.S.A., 74, pp. 5463-5467; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RnAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. U S.A., 86, pp. 5626-5630; Siddle, S.G., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, D.H., Macnaughton, M.R., Pensaert, M., Van Der Zeijst, B.A.M., Coronaviridae (1983) Intervirology, 20, pp. 181-189; Simpkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavinis strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am. J. Vet. Res., 53, pp. 1253-1258; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Underdahl, N.R., Mebus, C.A., Stair, E.L., Rhodes, M.B., Mcgill, L.D., Twiehaus, M.J., Isolation of transmissible gastroenteritis virus from lungs of market-weight swine (1974) Am. J. Vet. Res., 35, pp. 1209-1216; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet. Microbiol., 36, pp. 333-347; Wesley, R.W., Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain) (1990) Coronaviruses and Their Diseases, pp. 301-306. , Cavanagh, D. and Brown, T. D. K. eds.. Plenum Press, New York; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J. Vet. Diagn. Invest., 3, pp. 29-32; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Woods, R.D., Small plaque variant transmissible gastroenteritis virus (1978) J. Am. Vet. Med. Assoc., 173, pp. 643-647; Zhu, X.-L., Paul, P.S., Vaughn, E., Morales, A., Characterization and reactivity of monoclonal antibodies to the Miller strain of transmissible gastroenteritis virus of swine (1990) Am. J. Vet. Res., 51, pp. 232-237","Jackwood, D.J.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States",,"Maruzen Co. Ltd.",09167250,,,"9637293","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0032061957
"Hansen G.H., Delmas B., Besnardeau L., Vogel L.K., Laude H., Sjöström H., Norén O.","7202191577;7003294168;6602382869;7102142452;7006652624;7005649072;7006675786;","The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment",1998,"Journal of Virology","72","1",,"527","534",,35,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031964681&partnerID=40&md5=f2c5640d338599279adcfbbff485ec1b","Biochemistry Laboratory C, Dept. of Med. Biochem. and Genetics, Panum Institute, DK-2200 Copenhagen N, Denmark; U. Virologie Immunol. Moleculaires, INRA, F-78350 Jouy-en-Josas, France; IMBG, Biochemistry Laboratory C, Panum Institute, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark","Hansen, G.H., Biochemistry Laboratory C, Dept. of Med. Biochem. and Genetics, Panum Institute, DK-2200 Copenhagen N, Denmark; Delmas, B., U. Virologie Immunol. Moleculaires, INRA, F-78350 Jouy-en-Josas, France; Besnardeau, L., U. Virologie Immunol. Moleculaires, INRA, F-78350 Jouy-en-Josas, France; Vogel, L.K., Biochemistry Laboratory C, Dept. of Med. Biochem. and Genetics, Panum Institute, DK-2200 Copenhagen N, Denmark; Laude, H., U. Virologie Immunol. Moleculaires, INRA, F-78350 Jouy-en-Josas, France; Sjöström, H., Biochemistry Laboratory C, Dept. of Med. Biochem. and Genetics, Panum Institute, DK-2200 Copenhagen N, Denmark; Norén, O., Biochemistry Laboratory C, Dept. of Med. Biochem. and Genetics, Panum Institute, DK-2200 Copenhagen N, Denmark, IMBG, Biochemistry Laboratory C, Panum Institute, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark","Aminopeptidase N is a species-specific receptor for transmissible gastroenteritis virus (TGEV), which infects piglets, and for the 229E virus, which infects humans. It is not known whether these coronaviruses are endocytosed before fusion with a membrane of the target cell, causing a productive infection, or whether they fuse directly with the plasma membrane. We have studied the interaction between TGEV and a cell line (MDCK) stably expressing recombinant pig aminopeptidase N (pAPN). By electron microscopy and flow cytometry, TGEV was found to be associated with the plasma membrane after adsorption to the pAPN-MDCK cells. TGEV was also observed in endocytic pits and apical vesicles after 3 to 10 min of incubation at 38°C. The number of pits and apical vesicles was increased by the TGEV incubation, indicating an increase in endocytosis. After 10 min of incubation, a distinct TGEV- pAPN-containing population of large intracellular vesicles, morphologically compatible with endosomes, was found. A higher density of pAPN receptors was observed in the pits beneath the virus particles than in the surrounding plasma membrane, indicating that TGEV recruits pAPN receptors before endocytosis. Ammonium chloride and bafilomycin A1 markedly inhibited the TGEV infection as judged from virus production and protein biosynthesis analyses but did so only when added early in the course of the infection, i.e., about 1 h after the start of endocytosis. Together our results point to an acid intracellular compartment as the site of fusion for TGEV.",,"animal cell; article; cell fusion; coronavirus; endocytosis; gastroenteritis; nonhuman; priority journal; virus cell interaction; virus transmission; Ammonium Chloride; Animals; Anti-Bacterial Agents; Antigens, CD13; Cell Compartmentation; Cell Line; Cell Membrane; Dogs; Endocytosis; Enzyme Inhibitors; Gastroenteritis, Transmissible, of Swine; Hydrogen-Ion Concentration; Lysosomes; Macrolides; Membrane Fusion; Microscopy, Electron; Proton Pumps; Receptors, Cell Surface; Swine; Transmissible gastroenteritis virus; Virus Replication","Asanaka, M., Lai, M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissble gastroenteritis virus (1997) J. 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Laude and J. F. Vautherot (ed.), Plenum Press, New York, N.Y; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus A59 (1993) J. Virol., 67, pp. 1-8; Gallagher, T., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Gaudin, Y., Tuffereau, C., Segretain, D., Knossow, M., Flamand, A., Reversible conformational changes and fusion activity of rabies virus glycoprotein (1991) J. Virol., 65, pp. 4853-4859; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Hansen, G.H., Wetterberg, L.-L., Sjöström, H., Norén, O., Immunogold labelling is a quantitative method as demonstrated by studies on aminopeptidase N in microvillar membrane vesicles (1992) Histochem. J., 24, pp. 132-136; Hansen, S.H., Casanova, J.E., Gs alpha stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A (1994) J. Cell Biol., 126, pp. 677-687; Hernandez, L.D., Hoffman, L.R., Wolfsberg, T.G., White, J.M., Virus-cell and cell-cell fusion (1996) Annu. Rev. Cell. Dev. Biol., 12, pp. 627-661; Holmes, K.V., Lai, M.C., Coronaviridae: The viruses and their replication (1996) Fields Virology 3rd Ed., pp. 1075-1093. , N. Fields, D. M. Knipe, P. Howley, et al. 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Res., 42, pp. 447-449; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Look, T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) J. Clin. Invest., 83, pp. 1299-1307; Marsh, M., Helenius, A., Virus entry into animal cells (1989) Adv. Virus Res., 36, pp. 107-151; Marsh, M., Pelchen-Matthews, A., The endocytic pathway and virus entry (1994) Cellular Receptors for Animal Viruses, pp. 215-240. , E. Wimmer (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Mizzen, L., Hilton, A., Cheley, S., Anderson, R., Attenuation of murine coronavirus infection by ammonium chloride (1985) Virology, 142, pp. 378-388; Okhuma, S., Poole, B., Fluorescence probe measurements of the intralysosomal pH in living cells and the perturbation of pH by various agents (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 3327-3331; Olsen, J., Cowell, G.M., Kønigshøfer, E., Danielsen, E.M., Møller, J., Laustsen, L., Hansen, O., Norén, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Lett., 238, pp. 307-314; Pensaert, M., Callebaut, P., Cox, E., Enteric coronaviruses of animals (1993) Viral Infections of the Gastrointestinal Tract, 2nd Ed., pp. 627-696. , A. Z. Kapikian (ed.), Marcel Dekker, New York, N.Y; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-12007; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van Der Ende, A., Rottier, P.J.M., Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells (1994) J. Virol., 68, pp. 7966-7973; Sawicki, S.G., Sawicki, D., Coronavirus minus strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Sjöström, H., Norén, O., Changes of the quaternary structure of microvillus aminopeptidase in the membrane (1982) Eur. J. Biochem., 122, pp. 245-250; Sturman, L.S., Richard, S., Holmes, K.V., Conformational changes of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canainc, porcine, and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Vogel, L.K., Spiess, M., Sjöström, H., Norén, O., Evidence for an apical sorting signal on the ectodomain of human aminopeptidase N (1992) J. Biol. Chem., 267, pp. 2794-2797; Vogel, L.K., Norén, O., Sjöström, H., Transcytosis of aminopeptidase N in Caco-2 cells is mediated by a non-cytoplasmic signal (1995) J. Biol. Chem., 270, pp. 22933-22938; Wessels, H.P., Hansen, G.H., Fuhrer, C., Look, A.T., Sjöström, H., Norén, O., Spiess, M., Aminopeptidase N is directly sorted to the apical domain in MDCK cells (1990) J. Cell Biol., 111, pp. 2923-2930; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K.Y., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Noren, O.; IMBG, Biochemistry Laboratory C, Panum Institute, Blegdamsvej 3, DK-2200 Copenhagen N, Denmark; email: noren@biobase.dk",,,0022538X,,JOVIA,"9420255","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031964681
"Pitkaranta A., Jero J., Arruda E., Virolainen A., Hayden F.G.","7003331729;7004052788;7004935664;6701758010;7103233446;","Polymerase chain reaction-based detection of rhinovirus, respiratory syncytial virus, and coronavirus in otitis media with effusion",1998,"Journal of Pediatrics","133","3",,"390","394",,57,"10.1016/S0022-3476(98)70276-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031687703&doi=10.1016%2fS0022-3476%2898%2970276-8&partnerID=40&md5=c1baa758df4317bdb3c738c22a807cd2","Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States","Pitkaranta, A., Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States; Jero, J., Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States; Arruda, E., Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States; Virolainen, A., Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States; Hayden, F.G., Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States","Objectives: To study the association of human rhinovirus (HRV), respiratory syncytial virus (RSV), and human coronavirus infections in children aged 6 months to 12 years with otitis media with effusion (OME). To determine how long HRV RNA can be detected after HRV infection. Methods: Middle ear effusion (MEE) samples collected at the time of tympanostomy tube placement from 100 children with OME were examined. Viral RNA was detected by reverse-transcriptase polymerase chain reaction. For HRV the results were compared with virus isolation in cell culture. In vitro studies of the persistence of HRV infectivity and RNA were conducted by combining ~105 median cell culture infectious doses of HRV with pooled MEE at 37°C and assaying serial samples for 12 weeks. Results: Virus RNA was detected in 30 children. HRV was detected by reverse-transcriptase polymerase chain reaction in 19 children with OME and by virus isolation in 5 children. RSV RNA was found in 8 and HCV in 3 children with OME. No dual vital infection was found. Bacterial pathogens were isolated from 35 MEE samples and were associated with vital RNA in 11 cases, most often with HRV (9 cases). Under in vitro conditions, HRV culture positivity declined rapidly (&lt;2 days), but RNA was detectable for up to 8 weeks. Conclusions: These results suggest that virus infection, particularly HRV infection, either alone or concurrent with bacteria, is present in a larger percentage of children with OME than previously suspected. It remains to be determined how often the presence of vital RNA in MEE represents persistent RNA, ongoing viral replication, or recurrent infection.",,"article; cell culture; child; clinical article; Coronavirus; diagnostic accuracy; female; human; infant; male; otitis media; polymerase chain reaction; priority journal; Respiratory syncytial pneumovirus; Rhinovirus; virus culture; virus detection; virus infectivity; virus replication",,"Hayden, F.G.; Univ. of Virginia Hlth. Sci. Center, Box 475, Charlottesville, VA 22908, United States",,"Mosby Inc.",00223476,,JOPDA,"9738723","English","J. Pediatr.",Article,"Final",Open Access,Scopus,2-s2.0-0031687703
"Hegyi A., Kolb A.F.","6603368848;7005622195;","Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N",1998,"Journal of General Virology","79","6",,"1387","1391",,21,"10.1099/0022-1317-79-6-1387","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031834946&doi=10.1099%2f0022-1317-79-6-1387&partnerID=40&md5=234d83f2b56abe9cabab4ca45571dce4","Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany; Hannah Research Institute, Ayr KA6 5HL, United Kingdom","Hegyi, A., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany; Kolb, A.F., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, 97078 Würzburg, Germany, Hannah Research Institute, Ayr KA6 5HL, United Kingdom","Feline aminopeptidase N (fAPN) is a major cell surface receptor for feline infectious peritonitis virus (FIPV), transmissible gastroenteritis virus (TGEV), human coronavirus 229E (HCV 229E) and canine coronavirus (CCV). By using chimeric molecules assembled from porcine, human and feline APN we have analysed the determinants involved in the coronavirus receptor function of fAPN. Our results show that amino acids 670-840 of fAPN are critically involved in its FIPV and TGEV receptor function whereas amino acids 135-297 are essential for the HCV 229E receptor function. We also demonstrate that a chimeric molecule assembled from human and porcine APN is able to act as a receptor for FIPV. This is surprising as neither human nor porcine APN by themselves mediate FIPV infection. These results suggest that different determinants in the APN protein are involved in mediating the coronavirus receptor function.",,"amino acid; cell surface receptor; microsomal aminopeptidase; virus receptor; article; Coronavirus; priority journal; Canine coronavirus; Coronavirus; Felidae; Feline infectious peritonitis virus; Hepatitis C virus; human coronavirus; Human coronavirus 229E; RNA viruses; Suidae; Transmissible gastroenteritis virus","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline enteric coronavirus isolates (1984) Laboratory Animal Science, 34, pp. 592-597; Barlough, J.E., Johnson-Lussenburg, C.M., Stoddart, C.A., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis virus (1985) Canadian Journal of Comparative Medicine, 49, pp. 303-307; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) Journal of Virology, 71, pp. 734-737; De Groot, R.J., Haar, R.T.J., Horzinek, M.C., Van Der Zeijst, B.A.M.V., Intracellular RNAs of the feline peritonitis coronavirus strain 79-1146 (1987) Journal of General Virology, 68, pp. 995-1002; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Advances in Experimental Medicine and Biology, 342, pp. 293-298; Delmas, B., Gelfi, J., Kut, E., Sjöström, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) Journal of Virology, 68, pp. 5216-5224; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline and canine coronaviruses (1982) Infection and Immunity, 37, pp. 1148-1155; Jacobse-Geels, H.E.L., Horzinek, M.C., Expression of feline infectious peritonitis coronavirus antigens on the surface of feline macrophage-like cells (1983) Journal of General Virology, 64, pp. 1859-1866; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) Journal of General Virology, 77, pp. 2515-2521; Kolb, A.F., Hegyi, A., Siddell, S.G., Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N (1997) Journal of General Virology, 78, pp. 2795-2802; Olsen, J., Cowell, G.M., Konigshofer, E., Danielsen, E.M., Moller, J., Laustsen, L., Hansen, O.C., Noren, O., Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA (1988) FEBS Letters, 238, pp. 307-314; Ringold, G., Yamamoto, K.R., Tomkins, G.M., Bishop, J.M., Varmus, H.E., Dexamethasone mediated induction of MMTV-RNA: A system for studying glucocorticoid action (1975) Cell, 6, pp. 299-305; Rost, B., PHD: Predicting one dimensional protein structure by profile based neural networks (1996) Methods in Enzymology, 266, pp. 525-539; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Suné, C., María, J.B., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Edited by S. G. Siddell. New York: Plenum Press; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) Journal of Virology, 70, pp. 8669-8674; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human amino-peptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Kolb, A.F.; Hannah Research Institute, Ayr KA6 5HL, United Kingdom; email: kolba@main.hri.sari.ac.uk",,"Microbiology Society",00221317,,JGVIA,"9634079","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0031834946
"Heggen C.L., Qureshi M.A., Edens F.W., Barnes H.J., Havenstein G.B.","6506912544;7202876162;7005975426;7102581732;7003539691;","Alterations in the lymphocytic and mononuclear phagocytic systems of turkey poults associated with exposure to poult enteritis and mortality syndrome",1998,"Avian Diseases","42","4",,"711","720",,14,"10.2307/1592706","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032193882&doi=10.2307%2f1592706&partnerID=40&md5=8b9b39e7e7f015ab07d1d80ebd99e794","Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States; Dept. Food, Anim., and Equine Med., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States","Heggen, C.L., Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States; Qureshi, M.A., Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States, Dept. Food, Anim., and Equine Med., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States; Edens, F.W., Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States; Barnes, H.J.; Havenstein, G.B., Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695-7608, United States","In vivo and in vitro mononuclear phagocytic system functions, expression of lymphocyte subset cell surface markers in the thymus and bursa of Fabricius, and lymphocyte subset dynamics during the course of poult enteritis and mortality syndrome (PEMS) were examined. PEMS is an acute, transmissible, infectious intestinal disease accompanied by high mortality and morbidity. The etiology of this multifactorial disease remains to be elucidated; however, turkey coronavirus was initially assumed to be one of the primary agents involved. Further investigation demonstrated that turkey coronavirus was not always detectable in poults exhibiting PEMS symptoms, and, thus, PEMS poults began to be identified as positive or negative for turkey coronavirus. In each trial, uninfected hatchmate controls were compared with turkey poults that were contact exposed to PEMS poults at 7 days of age. Following intravenous inoculation, control poults cleared Escherichia coli from their circulation by 60 min, whereas viable E. coli were still present in the circulation of PEMS poults at 60 min postinoculation. Inflammatory response measured by Sephadex-elicited abdominal exudate cell recruitment and the adherence potential of abdominal exudate cells was not significantly different between uninfected and PEMS poults. The percentage of glass-adherent abdominal exudate macrophages was higher in PEMS poults. However, the ability of these macrophages to phagocytize sheep red blood cells and the average number of sheep red blood cells per phagocytic macrophage were both lower compared with uninfected controls CD4+ expression in thymic tissue of PEMS poults at 9 days postinfection was significantly lower. The CD4+:CD8+ lymphocyte ratio in peripheral blood leukocytes from coronavirus-negative PEMS poults was lower than that from both uninfected and coronavirus-positive PEMS poults at 14 days postinfection. In the spleen, the CD4+:CD8+ lymphocyte ratio was higher in coronavirus-positive PEMS poults as compared with the other treatments. In conclusion, immune system dysfunction in PEMS is associated with impaired mononuclear phagocytic system function and alterations in lymphocyte populations.","Escherichia coli; Lymphocytes; Macrophage; Poult enteritis and mortality syndrome; Turkey","Animalia; Aves; Coronavirus; Escherichia coli; Fabricius; Meleagris gallopavo; Ovis aries; Turkey coronavirus","Axum Version 5.0, , Copyright (©) 1988-96, Mathsoft, Inc., Seattle, WA; Barnes, H.J., Guy, J.S., Spiking mortality of turkeys (SMT) and related disorders: An update (1995) Proc. 19th Annual NC Turkey Industry Days Conference, pp. 16-21. , NCSU, Raleigh, NC; Barnes, H.J., Guy, J.S., Brown, T.P., Edens, F.W., (1996) Poult Enteritis and Mortality Syndrome (""Spiking Mortality of Turkeys"") and Related Disorders - An Update and Overview, pp. 1-11. , Newsletter, College of Veterinary Medicine and College of Agriculture and Life Sciences, NCSU, October 29, 1996; Barnes, H.J., Guy, J.S., Weaver, J.T., Jennings, S.R., Turkey flocks with high spiking mortality that are negative for turkey coronavirus (1997) Proc. 134th Annual Convention of the American Veterinary Medical Association, p. 169. , Reno, NV July 19-24; Brian, A.A., Stimulation of B-cell proliferation by membrane-associated molecules from activated T cells (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 564-568; Brown, T.P., Howell, D.R., Garcia, A.P., Villegas, P., Histological lesions of spiking mortality of turkeys (SMT): Comparison of lesions induced by SMT organ suspension and cell culture (1996) J. Am. Vet. Med. Assoc., 209, p. 373; Chun, T.W., Chadwick, K., Margolick, J., Siliciano, R.F., Differential susceptibility of naive and memory CD4+ T cells to the cytopathic effects of infection with human immunodeficiency virus type 1 strain LAI (1997) J. Virol., 71, pp. 4436-4444; Edens, F.W., Parkhurst, C.R., Qureshi, M.A., Casas, I.A., Havenstein, G.B., Atypical Escherichia coli strains and their association with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 952-960; Edens, F.W., Qureshi, M.A., Parkhurst, C.R., Casas, I.A., Havenstein, G.B., Involvement of atypical Escherichia coli strains in turkey health (1997) 20th Technical Turkey Conference, pp. 1-39. , Cheshire, England. April 17-18; Ficken, M.D., Edwards, J.F., Lay, J.C., Induction, collection, and partial characterization of induced respiratory macrophages of the turkey (1986) Avian Dis., 30, pp. 766-771; Hala, K., Bock, G., Sgonc, R., Schulmannova, J., Tempelis, C.H., Vainio, O., Kemmler, G., Frequency of chicken CD4+ and CD8+ cells: Genetic control and effect of rous sarcoma virus infection (1992) Scand. J. Immunol., 35, pp. 237-245; Hu, L., Lucio, B., Schat, K.A., Depletion of CD4+ and CD8+ T lymphocyte subpopulations by CIA-1, a chicken infectious anemia virus (1993) Avian Dis., 37, pp. 492-500; Image Pro Plus, , Media Cybernetics, Silver Springs, MD; Kidd, M.T., Hagler Jr., W.M., Qureshi, M.A., Trichothecene mycotoxins depress the mononuclear-phagocytic system of young turkeys (1995) Immunopharmacol. Immunotoxicol., 17, pp. 385-398; Kidd, M.T., Qureshi, M.A., Ferket, P.R., Thomas, L.N., Blood clearance of Escherichia coli and evaluation of mononuclear-phagocytic system as influenced by supplemental dietary zinc methionine in young turkeys (1994) Poult. Sci., 73, pp. 1381-1389; Kuppers, R.C., Henney, C.S., Studies on the mechanism of lymphocyte-mediated cytolysis. IX. Relationships between antigen recognition and lytic expression in killer T cells (1977) J. Immunol., 118, pp. 71-76; Miller, L., Qureshi, M.A., Induction of heat-shock proteins and phagocytic function of chicken macrophage following in vitro heat exposure (1992) Vet. Immunol. Immunopathol., 30, pp. 179-191; Mogensen, S.C., Role of macrophages in natural resistance to virus infections (1979) Microbiol. Rev., 43, pp. 1-26; Nakamura, K., Imada, Y., Maeda, M., Lymphocytic depletion of bursa of Fabricius and thymus in chickens inoculated with Escherichia coli (1986) Vet. Pathol., 23, pp. 712-717; Neldon-Ortiz, D.L., Qureshi, M.A., Direct and microsomal activated aflatoxin b1 exposure and its effects on turkey peritoneal macrophage functions in vitro (1991) Toxicol. Appl. Pharmacol., 109, pp. 432-442; Parmentier, H.K., Kreukniet, M.B., Goeree, B., Davison, T.F., Jeurissen, S.H.M., Harmsen, E.G.M., Nieuwland, M.G.B., Differences in distribution of lymphocyte antigens in chicken lines divergently selected for antibody response to sheep red blood cells (1995) Vet. Immunol. Immunopathol., 48, pp. 155-168; Qureshi, M.A., Dietert, R.R., Bacterial uptake and killing by macrophages (1995) Methods in Immunotoxicology, 2, pp. 119-131; Qureshi, M.A., Dietert, R.R., Bacon, L.D., Genetic variation in the recruitment and activation of chicken peritoneal macrophages (1986) Proc. Soc. Exp. Biol. Med., 181, pp. 560-568; Qureshi, M.A., Edens, F.W., Havenstein, G.B., Immune system dysfunction during exposure to poult enteritis and mortality syndrome agents (1997) Poult. Sci., 76, pp. 564-569; Qureshi, M.A., Hagler Jr., W.M., Effect of fumonisin-b1 exposure on chicken macrophage functions in vitro (1992) Poult. Sci., 71, pp. 104-112; Rothwell, L., Gramzinski, R.A., Rose, M.E., Kaiser, P., Avian coccidiosis: Changes in intestinal lymphocyte populations associated with the development of immunity to Eimeria maxima (1995) Parasite Immunol., 17, pp. 525-533. , Oxf; Sabet, T., Hsia, W., Stanisz, M., El-Domeiri, A., Van Alten, P., A simple method for obtaining peritoneal macrophages from chickens (1977) J. Immunol. Methods, 14, pp. 103-110; (1995) SAS User's Guide: Statistics, Version 6.11 Ed., , SAS Institute, Inc., Cary, NC; Stout, R.D., Bottomly, K., Antigen-specific activation of effector macrophages by IFN-γ producing (Th1) T cell clones. Failure of IL-4 producing (Th2) T cell clones to activate effector function in macrophages (1989) J. Immunol., 142, pp. 760-765; Suresh, M., Sharma, J.M., Hemorrhagic enteritis virus induced changes in the lymphocyte subpopulations in turkeys and the effect of experimental immunodeficiency on viral pathogenesis (1995) Vet. Immunol. Immunopathol., 45, pp. 139-150; Suresh, M., Sharma, J.M., Belzer, S.W., Studies on lymphocyte subpopulations and the effect of age on immune competence in turkeys (1993) Dev. Comp. Immunol., 17, pp. 525-535","Qureshi, M.A.; Dept. of Food, Animal/Equine Med., North Carolina State University, Raleigh, NC 27695-7608, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"9876839","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0032193882
"Foley J.E., Lapointe J.M., Koblik P., Poland A., Pedersen N.C.","7402872921;35945061600;7003608863;7006803895;7202299909;","Diagnostic features of clinical neurologic feline infectious peritonitis.",1998,"Journal of veterinary internal medicine / American College of Veterinary Internal Medicine","12","6",,"415","423",,71,"10.1111/j.1939-1676.1998.tb02144.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032201344&doi=10.1111%2fj.1939-1676.1998.tb02144.x&partnerID=40&md5=8b62943d33240ffe8555bf8b55e1deb3","Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States","Foley, J.E., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States; Lapointe, J.M., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States; Koblik, P., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States; Poland, A., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California, Davis, 95616, United States","Feline infectious peritonitis (FIP) is a fatal Arthus-type immune response of cats to infection with FIP virus, a mutant of the ubiquitous feline enteric coronavirus (FECV). The disease may occur systemically or in any single organ system, and primary neurologic disease is a common subset of such manifestations. We examined 16 domestic cats with clinical neurologic FIP and 8 control cats with nonneurologic FIP, with the intention of identifying the ante- and postmortem diagnostic tests that most contribute to accurate diagnosis. Of the 16 cats with neurologic FIP, 15 were less than 2 years of age and all 16 originated from large multiple-cat households. The most useful antemortem indicators of disease were positive anti-coronavirus IgG titer in cerebrospinal fluid, high serum total protein concentration, and findings on magnetic resonance imaging suggesting periventricular contrast enhancement, ventricular dilatation, and hydrocephalus. Postmortem diagnosis was facilitated by FIP monoclonal antibody staining of affected tissue and coronavirus-specific polymerase chain reaction. Most cats with neurologic and ocular forms of FIP had patchy, focal lesions, suggesting that recently developed technologies described in this report may be useful for evaluation of cats with suspected FIP.",,"immunoglobulin G; plasma protein; virus antigen; virus RNA; agar gel electrophoresis; age; animal; animal disease; article; blood; brain; cat; cat disease; cerebrospinal fluid; Coronavirus; cytochemistry; female; genetics; germfree animal; immunology; male; neurologic disease; nuclear magnetic resonance imaging; pathology; protein cerebrospinal fluid level; reverse transcription polymerase chain reaction; virology; Age Factors; Animals; Antigens, Viral; Blood Proteins; Brain; Cats; Cerebrospinal Fluid Proteins; Coronavirus, Feline; Electrophoresis, Agar Gel; Feline Infectious Peritonitis; Female; Histocytochemistry; Immunoglobulin G; Magnetic Resonance Imaging; Male; Nervous System Diseases; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Specific Pathogen-Free Organisms",,"Foley, J.E.email: jefoley@ucadavis.edu",,,08916640,,,"9857333","English","J. Vet. Intern. Med.",Article,"Final",,Scopus,2-s2.0-0032201344
"Jonassen C.M., Jonassen T.Ø., Grinde B.","6506806313;7005250658;36932251300;","A common RNA motif in the 3' end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus",1998,"Journal of General Virology","79","4",,"715","718",,89,"10.1099/0022-1317-79-4-715","https://www.scopus.com/inward/record.uri?eid=2-s2.0-6844266251&doi=10.1099%2f0022-1317-79-4-715&partnerID=40&md5=6c8c753161c2ad356e8dbfc2c3192bfd","Department of Virology, National Institute of Public Health, PO Box 4404 Torshov, N-0403 Oslo, Norway","Jonassen, C.M., Department of Virology, National Institute of Public Health, PO Box 4404 Torshov, N-0403 Oslo, Norway; Jonassen, T.Ø., Department of Virology, National Institute of Public Health, PO Box 4404 Torshov, N-0403 Oslo, Norway; Grinde, B., Department of Virology, National Institute of Public Health, PO Box 4404 Torshov, N-0403 Oslo, Norway","In the 3' non-coding region of the genomes of infectious bronchitis virus, an avian coronavirus and the picornavirus equine rhinovirus serotype 2, there is a motif with remarkable similarity, both in sequence and folding, to the second RNA stem-loop from the 3' end of the genomes of human astroviruses. This motif was also found in astroviruses of sheep, pig and turkey, suggesting that it is a common feature of all astroviruses. The conserved nature of the motif indicates that there has been strong selection for its preservation. There is significant homology between the regions flanking this motif in infectious bronchitis virus and a continuous RNA sequence at the same distance from the 3' poly(A) tail in some related mammalian coronaviruses. These observations suggest that the presence of the motif in these three viral families is the result of at least two separate RNA recombination events.",,"recombinant RNA; virus RNA; article; Astrovirus; Avian infectious bronchitis virus; genome; priority journal; Rhinovirus; RNA sequence","Belliot, G., Laveran, H., Monroe, S.S., Detection and genetic differentiation of human astroviruses: Phylogenetic grouping varies by coding region (1997) Archives of Virology, 142, pp. 1323-1334; Chetverin, A.B., Chetverina, H.V., Demidenko, A.A., Ugarov, V.I., Nonhomologous RNA recombination in a cell-free system: Evidence for a transesterification mechanism guided by secondary structure (1997) Cell, 88, pp. 503-513; Koonin, E.V., Dolja, V.V., Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences (1993) Critical Reviews in Biochemistry and Molecular Biology, 28, pp. 375-430; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiological Reviews, 56, pp. 61-79; Madeley, C.R., Cosgrove, B.P., 28 nm particles in faeces in infantile gastroenteritis (1975) Lancet, 2, pp. 451-452; Monceyron, C., Grinde, B., Jonassen, T.Ø., Molecular characterisation of the 3′end of the astrovirus genome (1997) Archives of Virology, 142, pp. 99-706; Monroe, S.S., Jiang, B., Stine, S.E., Koopmans, M., Glass, R.I., Subgenomic RNA sequence of human astrovirus supports classification of Astroviridae as a new family of RNA viruses (1993) Journal of Virology, 67, pp. 3611-3614; Nagy, P.D., Simon, A.E., New insights into the mechanisms of RNA recombination (1997) Virology, 235, pp. 1-9; Saif, Y.M., Sait, L.J., Hofacre, C.L., Hayhow, C., Swayne, D.E., Dearth, R.N., A small round virus associated with enteritis in turkey poults (1990) Aman Diseases, 34, pp. 762-764; Shimizu, M., Shirai, J., Narita, M., Yamane, T., Cytopathic astrovirus isolated from porcine acute gastroenteritis in an established cell line derived from porcine embryonic kidney (1990) Journal of Clinical Microbiology, 28, pp. 201-206; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) Journal of General Virology, 64, pp. 761-776; Snodgrass, D.R., Gray, E.W., Detection and transcription of 30 nm virus particles (astroviruses) in faeces of iambs with diarrhoea (1977) Archives of Virology, 55, pp. 287-291; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Analysis of a hypervariable region in the 3′ non-coding end of the infectious bronchitis virus genome (1993) Virus Research, 28, pp. 19-27; Wutz, G., Auer, H., Nowotny, N., Skern, T., Keuchler, E., Equine rhinovirus serotypes 1 and 2: Relationships to each other and to aphthoviruses and cardioviruses (1996) Journal of General Virology, 77, pp. 1719-1730","Monceyron Jonassen, C.; Department of Virology, National Institute of Public Health, PO Box 4404 Torshov, N-0403 Oslo, Norway; email: christmj@embnet.uio.no",,"Microbiology Society",00221317,,JGVIA,"9568965","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-6844266251
"Pérez E., Kummeling A., Janssen M.M.H., Jiménez C., Alvarado R., Caballero M., Donado P., Dwinger R.H.","25925328700;6508167084;19534677800;57210402191;7005553744;7102935169;6506866069;7004655567;","Infectious agents associated with diarrhoea of calves in the canton of Tilarán, Costa Rica",1998,"Preventive Veterinary Medicine","33","1-4",,"195","205",,28,"10.1016/S0167-5877(97)00038-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041854537&doi=10.1016%2fS0167-5877%2897%2900038-X&partnerID=40&md5=ac18fd7cb6be61edafcd6102e9b8041c","University of Utrecht, Utrecht, Netherlands","Pérez, E.; Kummeling, A., University of Utrecht, Utrecht, Netherlands; Janssen, M.M.H., University of Utrecht, Utrecht, Netherlands; Jiménez, C.; Alvarado, R.; Caballero, M.; Donado, P.; Dwinger, R.H.","A case-control study of calves under 3 months of age was carried out by weekly visits to 15 farms in the canton of Tilarán, Costa Rica. Most farms were dedicated to beef or dual-purpose (DP) production. Faecal samples were collected over a 6-month period from a total of 194 calves with clinical signs and from 186 animals without clinical signs of diarrhoea as assessed by a scoring system. The samples were investigated for the presence of viruses, bacteria and parasites. Torovirus was detected for the first time in Costa Rica and was present in 14% of calves with diarrhoea and in 6% of the controls. Coronavirus and Rotavirus were less frequently encountered in either one of the groups (in 9 and 7% of scouring calves and in 1 and 2% of controls, respectively). Escherichia coli was detected in 94% of all the faecal samples, but isolates from only three samples from calves with diarrhoea contained the K99 antigen. Similarly, Salmonella was found only in scouring calves. Cryptosporidium oocysts were detected in animals with signs of diarrhoea, while other coccidia oocysts, Strongylida and Strongyloides eggs were frequently found in animals both with and without diarrhoea. A conditional logistic regression (CLR) analysis to compare healthy and scouring calves showed a significant difference with regard to the presence of Torovirus, Rotavirus and Coronavirus. © 1998 Elsevier Science B.V.","Case-control studies; Cattle-microbiological diseases; Diarrhoea; Mortality and morbidity; Torovirus","animal; animal disease; article; case control study; cattle; cattle disease; Coccidia; Coronavirus; Costa Rica; Cryptosporidium; diarrhea; Escherichia coli; feces; female; isolation and purification; male; microbiology; parasitology; prevalence; Rotavirus; Salmonella; statistical model; Strongyloides; Torovirus; tropic climate; Animals; Case-Control Studies; Cattle; Cattle Diseases; Coccidia; Coronavirus; Costa Rica; Cryptosporidium; Diarrhea; Escherichia coli; Feces; Female; Logistic Models; Male; Prevalence; Rotavirus; Salmonella; Strongyloides; Torovirus; Tropical Climate","Besser, T.E., Gay, C.C., Septicemic colibacillosis and failure of passive transfer of colostral immunoglobulin in calves (1985) Vet. Clin. North Am. (Food Anim. Pract.), 1, pp. 445-459; Breslow, N.E., Day, N.E., (1980) Statistical Methods in Cancer Research. Vol. 1 - The Case-control Studies, 1, p. 162. , Lyon IARC; Britney, J.B., Martin, S.W., Stone, J.B., Curtis, R.A., Analysis of early calfhood health status and subsequent dairy herd survivorship and productivity (1984) Prev. Vet. Med., 3, pp. 45-52; Cordero, R.R., Osorio, S.M.L., (1988) Factores de Riesgo Sobre Morbilidad y Mortalidad en Terneras Menores de Tres Meses en Tres Zonas Lecheras de Costa Rica, , Thesis, Escuela de Medicina Veterinaria, Universidad Nacional, Costa Rica, 78 pp; Crouch, C.F., Ohmann, H.B., Watts, T.C., Babiuk, L.A., Chronic enteric shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) Gen. Virol., 66, pp. 1489-1500; Debnath, N.C., Sil, B.K., Prodhan, M.A.M., Howlader, M.M.R., A retrospective study on calf mortality and morbidity on smallholder traditional farms in Bangladesh (1990) Prev. Vet. Med., 9, pp. 1-7; Dwinger, R.H., Cappella, E., Pérez, E., Baaijen, M., Müller, E., Application of a computerised herd management and production control program in Costa Rica (1994) Trop. Agric., 71, pp. 74-76. , Trinidad; Gordon, H.M., Whitlock, H.V., A new technique for counting nematode eggs in sheep faeces (1939) J. Council Sci. Industrial Res., 12, pp. 50-52. , Australia; Haggard, D.L., Bovine enteric colibacillosis (1985) Vet. Clin. North Am. (Food Anim. Pract.), 1, pp. 495-507; Heath, S.E., Neonatal diarrhoea in calves: Diagnosis and intervention in problem herds (1992) Comp. Cont. Educ. Pract. Vet., 14, pp. 995-1002; Hird, D., Pérez, E., Caballero, M., Rodríguez, L., Velázquez, J., Identification of selected disease agents from calves on Costa Rican tropical cloud-forest dairy farms (1990) Prev. Vet. Med., 9, pp. 221-231; Jiménez, C., (1990) Vergleichende Labordiagnostische Untersuchungen von Kotproben (EM, Virusisolierung, Immunologische Verfahren) zum Nachweis einer Bovinen Coronavirus-infektion bei Durchfallkranken Kälbern, , Vet. Med. Diss. Justus-Liebig-Universität Giessen, Germany, 170 pp; Koopmans, M., Van Den Boom, U., Woode, G., Horzinek, M.C., Seroepidemiology of Breda virus in cattle using ELISA (1989) Vet. Microbiol., 19, pp. 233-243; Liprandi, F., López, G., Rodríguez, I., Hidalgo, M., Ludert, J.E., Mattion, N., Monoclonal antibodies to the VP6 of porcine subgroup I rotaviruses reactive with subgroup I and non-subgroup I non-subgroup II strains (1990) Gen. Virol., 71, pp. 1395-1398; Mebus, C.A., Underdahl, N.R., Rhodes, M.B., Twiehaus, M.J., Calf diarrhoea (scours) reproduced with a virus from a field outbreak (1969) Univ. Nebr. Agric. Exp. Sta. Res. Bull., 233, pp. 1-16; Moerman, A., De Leeuw, P.W., Van Zijderveld, F.G., Baanvinger, T., Tiessink, J.W.A., Prevalence and significance of viral enteritis in Dutch dairy calves (1982) XII World Congress on Diseases of Cattle. The Netherlands. Proceedings, 1, pp. 228-234; Moon, H.W., McClurkin, A.W., Isaacson, R.E., Pohlenz, J., Skartvedt, S.M., Gillette, K.G., Baetz, A.L., Pathogenic relationships of Rotavirus, Escherichia coli, and other agents in mixed infections in calves (1978) J. Am. Vet. Med. Assoc., 173, pp. 577-583; Olson, T.A., Elzo, M.A., Koger, M., Butts, W.T., Adams, E.L., Direct and material genetic effects due to the introduction of Bos taurus alleles into Brahman cattle in Florida: 1. Reproduction and calf survival (1989) J. Anim. Sci., 68, pp. 317-323; Olsson, S.-O., Viring, S., Emanuelsson, U., Jacobsson, S.-O., Calf diseases and mortality in Swedish dairy herds (1993) Acta Vet. Scand., 34, pp. 263-269; Oviedo, M.T., Araya, L.N., Hernández, F., Agentes bacterianos, parasitarios y virales involucrados en la etiologia de la diarrea de terneros en Costa Rica (1987) Cienc. Vet. (Costa Rica), 9, pp. 29-35; Oxender, W.D., Newman, L.E., Morrow, D.A., Factors influencing dairy calf mortality in Michigan (1973) J. Am. Vet. Med. Assoc., 162, pp. 458-460; Ferez, E., (1994) Epidemiological Aspects of Morbidity, Mortality and Growth of Calves in Costa Rica, pp. 87-105. , PhD thesis. University of Utrecht, The Netherlands; Perez, E., Noordhuizen, J.P.T.M., Van Wuijkhuise, L.A., Stassen, E.N., Management factors related to calf morbidity and mortality rates (1990) Livest. Prod. Sci., 25, pp. 79-93; Pohjola, S., Oksanen, H., Neuvonen, E., Veijalainen, P., Henriksson, K., Certain enteropathogens in calves of Finnish dairy herds with recurrent outbreaks of diarrhoea (1986) Prev. Vet. Med., 3, pp. 547-558; Reynolds, D.J., Morgan, J.E., Chanter, N., Jones, P.W., Bridger, J.C., Debney, T.G., Bunch, K.J., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec., 119, pp. 34-39; Roberts, F.H.S., O'Sullivan, P.J., Methods for egg counts and larval cultures for strongyles infesting the gastro-intestinal tract of cattle (1950) Aust. J. Agric. Res., 1, pp. 99-102; Simpson, J.R., Conrad, J.H., Intensification of cattle production systems in Central America: Why and when (1993) J. Dairy Sci., 76, pp. 1744-1752; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Troncy, P.M., Helminths of livestock and poultry in tropical Africa (1989) Manual of Tropical Veterinary Parasitology, pp. 33-61. , CAB International, Wallingford; Tzipori, S., The aetiology and diagnosis of calf diarrhoea (1981) Vet. Rec., 108, pp. 510-514; Umoh, J.U., Relative survival in calves in an University herd in Zaria, Nigeria (1982) Br. Vet. J., 138, pp. 507-514; Vaccaro, L.P., Survival of European dairy breeds and their crossess with zebus in the tropics (1990) Anim. Bre. Abst., 58, pp. 475-494; Vanopdenbosch, E., Pohl, P., Infectieuze kalverdiarree: Therapie en preventiemogelijkheden op basis van etiologische, pathofysiologische en immunologische gegevens (1993) Tijdschr. Diergeneesk., 118, pp. 731-734; Vermunt, J.J., Rearing and management of diarrhoea in calves to weaning (1994) Aust. Vet. J., 71, pp. 33-41; Vogt, R.F., Phillips, D.L., Henderson, L.O., Whitfield, W., Spierto, F.W., Quantitative differences among various proteins as blocking agents for ELISA microtiter plates (1987) J. Immunol. Meth., 101, pp. 43-50; Voller, A., Bidwell, D., Enzyme-linked immunosorbent assay (1986) Manual of Clinical Laboratory Immunology, pp. 99-109. , Rose, N.R., Friedman, H., Fahey, J.L. (Eds.), American Society for Microbiology, Washington DC; Woode, G.N., Reed, D.E., Runnels, P.L., Herrig, M.A., Hill, H.T., Studies with an unclassified virus isolated from diarrhoeal calves (1982) Vet. Microbiol., 7, pp. 221-240",,,"Elsevier",01675877,,PVMEE,"9500174","English","Prev. Vet. Med.",Article,"Final",,Scopus,2-s2.0-0041854537
"Guy J.S.","7202723649;","Virus Infections of the Gastrointestinal Tract of Poultry",1998,"Poultry Science","77","8",,"1166","1175",,68,"10.1093/ps/77.8.1166","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032134607&doi=10.1093%2fps%2f77.8.1166&partnerID=40&md5=98588d27f64142c6c7a40b0b66323a17","Dept. Microbiol., Pathol. Parasitol., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","Guy, J.S., Dept. Microbiol., Pathol. Parasitol., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","Several different viruses have been identified as causes of gastrointestinal tract infections in poultry. These include rotaviruses, coronaviruses, enteroviruses, adenoviruses, astroviruses, and reoviruses. In addition, a number of other viruses of unknown importance have been associated with gastrointestinal diseases in poultry based on electron microscopic examination of feces and intestinal contents. Viral infections of the gastrointestinal tract of poultry are known to negatively impact poultry production, and they likely contribute to the development of other, extra-gastrointestinal diseases. Our current understanding of the viruses that cause gastrointestinal tract infections in poultry is reviewed, with emphasis given to those of greatest importance.","Enteritis; Gastrointestinal tract; Infection; Rotavirus; Virus","animal; animal disease; bird disease; Enterovirus infection; gastrointestinal disease; pathophysiology; poultry; review; virology; virus infection; Adenoviridae Infections; Animals; Coronavirus Infections; Enterovirus Infections; Gastrointestinal Diseases; Poultry; Poultry Diseases; Virus Diseases","Anderson, A.A., (1981) Comparative Diagnosis of Viral Diseases, pp. 4-66. , Academic Press, New York, NY; Andral, B., Toquin, D., Observations et isoelements de pseudopicornavirus a partir de dindonneaux malades (1984) Avian Pathol., 13, pp. 377-388; Barnes, H.J., (1997) Diseases of Poultry. 10th Ed., pp. 685-686. , Iowa State University Press, Ames, IA; Barnes, H.J., Guy, J.S., (1997) Diseases of Poultry. 10th Ed., pp. 1025-1031. , Iowa State University Press, Ames, IA; Benfield, D.A., (1990) Viral Diarrheas of Man and Animals, pp. 115-135. , CRC Press, Boca Raton, FL; Bergeland, M.E., McAdaragh, J.P., Stotz, I., Rotaviral enteritis in turkey poults (1977) Proceedings of the 26th Western Poultry Disease Conference, pp. 129-130; Berns, K.I., Parvovirus replication (1990) Micro. Rev., 54, pp. 316-329; Bridger, J.C., (1990) Viral Diarrheas of Man and Animals, pp. 161-182. , CRC Press, Boca Raton, FL; Cavanagh, D., Structural polypeptides of coronavirus IBV (1981) J. Gen. Virol., 53, pp. 93-103; Chooi, K.F., Chulan, U., Broiler runting/stunting syndrome in Malaysia (1985) Vet. Rec., 116, p. 354; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1986) Avian Dis., 30, pp. 319-326; Decaesstecker, M., Charlier, G., Meulemans, G., Significance of parvoviruses, entero-like viruses and reoviruses in the etiology of the chicken malabsorption syndrome (1986) Avian Pathol., 15, pp. 769-782; Engstrom, B.E., Fossum, O., Luthman, M., Blue wing disease: Experimental infection with a Swedish isolate of chicken anemia agent as an avian reovirus (1988) Avian Pathol., 17, pp. 33-50; Estes, M.K., (1990) Virology. 2nd Ed., pp. 1329-1352. , Raven Press, New York, NY; Fadly, A.M., Nazerian, K., Nagaraja, K., Below, G., Field vaccination against hemorrhagic enteritis of turkeys (1985) Avian Dis., 29, pp. 768-777; Goodwin, M.A., Adenovirus inclusion body ventriculitis in chickens and captive bobwhite quail (Colinus virginianus) (1993) Avian Dis., 37, pp. 568-571; Goodwin, M.A., Hill, D.L., Dekich, M.A., Putnam, M.R., Multisystemic adenovirus infection in broiler chicks with hypoglycemia and spiking mortality (1993) Avian Dis., 37, pp. 625-627; Guy, J.S., Levy, M.G., Ley, D.H., Barnes, H.J., Gerig, T.M., Experimental reproduction of enteritis in bobwhite quail (Colinus virginianus) with Cryptosporidium and reovirus (1987) Avian Dis., 31, pp. 713-722; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hayhow, C.S., Saif, Y.M., Kerr, K.M., Whitmoyer, R.E., Further observations on enterovirus infection in specific-pathogen-free turkey poults (1993) Avian Dis., 37, pp. 124-134; Hayhow, C.S., Saif, Y.M., Development of an antigen-capture enzyme-linked immunosorbent assay for detection of enterovirus in commercial turkeys (1993) Avian Dis., 37, pp. 375-379; Joklik, W.K., Structure and function of the reovirus genome (1981) Micro. Rev., 45, pp. 483-501; Jones, R.C., Islam, M.R., Kelly, D.F., Early pathogenesis of experimental reovirus infection in chickens (1989) Avian Pathol., 18, pp. 239-253; Kibenge, F.S.B., Gwaze, G.E., Jones, R.C., Chapman, A.F., Savage, C.E., Experimental reovirus infection in chickens: Observations on early viremia and virus distribution in bone marrow, liver, and enteric tissues (1985) Avian Pathol., 14, pp. 87-98; Kisary, J., Nagy, B., Bitay, Z., Presence of parvoviruses in the intestine of chickens showing stunting syndrome (1984) Avian Pathol., 13, pp. 339-343; Kisary, J., Experimental infection of chicken embryos and day-old chickens with parvovirus of chicken origin (1985) Avian Pathol., 14, pp. 1-7; Kisary, J., Indirect immunofluorescence as a diagnostic tool for parvovirus infection of chickens (1985) Avian Pathol., 14, pp. 269-273; Kisary, J., Avalosse, B., Miller-Faures, A., Rommelaere, J., The genome of a new chicken virus identifies it as a parvovirus (1985) J. Gen. Virol., 66, pp. 2259-2263; Kouwenhoven, B., Davelaar, F.G., Van Walsum, J., Infectious proventriculitis causing runting in broilers (1978) Avian Pathol., 7, pp. 183-187; McFerran, J.B., (1997) Diseases of Poultry. 10th Ed., pp. 607-620. , Iowa State University Press, Ames, IA; McNulty, M.S., (1997) Diseases of Poultry. 10th Ed., pp. 692-701. , Iowa State University Press, Ames, IA; McNulty, M.S., McFerran, J.B., (1993) Virus Infections of Vertebrates, 4, pp. 519-529. , Elsevier Science Publishers, New York, NY; McNulty, M.S., Guy, J.S., (1997) Diseases of Poultry. 10th Ed., pp. 706-710. , Iowa State University Press, Ames, IA; McNulty, M.S., Allan, G.M., Todd, D., McFerran, J.B., Isolation and cell culture propagation of rotaviruses from turkeys and chickens (1979) Arch. Virol., 61, pp. 13-21; McNulty, M.S., Curran, W.L., Todd, D., McFerran, J.B., Detection of viruses in avian feces by direct electron microscopy (1979) Avian Pathol., 8, pp. 239-247; McNulty, M.S., Curran, W.L., McFerran, J.B., Determination of astroviruses in turkey feces by direct electron microscopy (1980) Vet. Rec., 106, p. 561; McNulty, M.S., Allan, G.M., Todd, D., McFerran, J.B., McCracken, R.M., Isolation from chickens of a rotavirus lacking the rotavirus group antigen (1981) J. Gen. Virol., 55, pp. 405-413; McNulty, M.S., Allan, G.M., McCracken, R.M., Experimental infection of chickens with rotavirus: Clinical and virological findings (1983) Avian Pathol., 12, pp. 45-54; McNulty, M.S., Allan, G.M., McFerran, J.B., Isolation of a novel avian entero-like virus (1987) Avian Pathol., 16, pp. 331-337; Moon, H.W., Mechanisms in the pathogenesis of diarrhea: A review (1978) J. Am. Vet. Med. Assoc., 172, pp. 443-446; Nazerian, K., Fadly, A.M., Propagation of virulent and avirulent turkey hemorrhagic enteritis virus in cell culture (1982) Avian Dis., 26, pp. 816-827; Orr, J.P., Necrotizing enteritis in a calf infected with adenovirus (1984) Can. Vet. J., 25, p. 72; Panigrahy, B., Naqi, S.A., Hall, C.F., Isolation and characterization of viruses associated with transmissible enteritis (bluecomb) of turkeys (1973) Avian Dis., 17, pp. 430-438; Paradiso, P.R., Rhone, S.L., Singer, I.I., Canine parvovirus: A biochemical and ultrastructural characterization (1982) J. Gen. Virol., 62, pp. 113-125; Pierson, F.W., Domermuth, C.H., (1997) Diseases of Poultry. 10th Ed., pp. 624-633. , Iowa State University Press, Ames, IA; Pomeroy, B.S., Larsen, C.T., Deshmukh, D.R., Patel, B.L., Immunity to transmissible (coronaviral) enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 553-555; Pomeroy, B.S., Nagaraja, K.V., (1991) Diseases of Poultry. 9th Ed., pp. 621-627. , Iowa State University Press, Ames, IA; Reynolds, D.L., Saif, Y.M., Astrovirus: A cause of an enteric disease in turkey poults (1986) Avian Dis., 30, pp. 89-98; Reynolds, D.L., Saif, Y.M., Theil, K.W., A survey of enteric viruses of turkey poults (1987) Avian Dis., 31, pp. 89-98; Reynolds, D.L., (1997) Diseases of Poultry. 10th Ed., pp. 701-705. , Iowa State University Press, Ames, IA; Rinehart, C.L., Rosenberger, J.K., Effects of avian reoviruses on the immune responses of chickens (1983) Poultry Sci., 62, pp. 1488-1489; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; Rosenberger, J.K., Olson, N.O., (1997) Diseases of Poultry. 10th Ed., pp. 711-719. , Iowa State University Press, Ames, IA; Rosenberger, J.K., Fries, P.A., Cloud, S.S., Wilson, R.A., In vitro and in vivo characterization of avian Escherichia coli. II. Factors associated with pathogenicity (1985) Avian Dis., 29, pp. 1094-1107; Ruff, M.D., Rosenberger, J.K., Concurrent infections with reoviruses and coccidia in broilers (1985) Avian Dis., 33, pp. 535-544; Saif, L.J., Saif, Y.M., Theil, K.W., Enteric viruses in diarrheic turkey poults (1985) Avian Dis., 29, pp. 798-811; Saif, Y.M., Saif, L.J., Hofacre, C.L., Hayhow, C., Swayne, D.E., Dearth, R.N., A small round virus associated with enteritis in turkey poults (1989) Avian Dis., 34, pp. 762-764; Spackman, D., Gough, R.E., Collins, M.S., Lanning, D., Isolation of an enterovirus-like agent from the meconium of dead-in-shell chicken embryos (1984) Vet. Rec., 114, pp. 216-218; Swayne, D.E., Radin, M.J., Saif, Y.M., Enteric disease in specific-pathogen-free turkey poults inoculated with a small round turkey-origin enteric virus (1990) Avian Dis., 34, pp. 683-692; Theil, K.W., Saif, Y.M., Age-related infections with rotavirus, rotavirus-like virus, and atypical rotavirus in turkey flocks (1987) J. Clin. Microbiol., 25, pp. 333-337; Theil, K.W., Reynolds, D.L., Saif, Y.M., Comparison of immune electron microscopy and genome electropherotyping techniques for detection of turkey rotaviruses and rotavirus-like viruses in intestinal contents (1986) J. Clin. Microbiol., 23, pp. 695-699; Thorsen, J., Weninger, N., Weber, L., Van Dijk, C., Field trials of an immunization procedure against hemorrhagic enteritis of turkeys (1982) Avian Dis., 26, pp. 473-477; Trambel, D.W., Kinden, D.A., Solorzano, R.F., Stogsdill, P.L., Parvovirus-like enteropathy in Missouri turkeys (1982) Avian Dis., 27, pp. 49-54; Van Der Heide, L., Kalbac, M., Infectious tenosynovitis (viral arthritis): Influence of maternal antibodies on the development of tenosynovitis lesions after experimental infection by day old chickens with tenosynovitis virus (1975) Avian Dis., 20, pp. 641-648; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Wigand, R., Bartha, A., Dreizin, R.S., Esche, H., Ginsberg, H.S., Green, M., Hierholzer, J.C., Wadell, G., Adenoviridae: Second report (1982) Intervirol., 18, pp. 169-176; Wood, G.W., Nicholas, R.A.J., Hebert, C.N., Thornton, D.H., Serological comparisons of avian reoviruses (1980) J. Comp. Pathol., 90, pp. 29-38; Yason, C.V., Schat, K.A., Pathogenesis of rotavirus infection in turkey poults (1986) Avian Pathol., 15, pp. 421-435","Guy, J.S.; Dept. Microbiol., Pathol. Parasitol., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; email: jim_guy@ncsu.edu",,"Poultry Science Association",00325791,,,"9706084","English","Poult. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0032134607
"Kennedy M.A., Brenneman K., Millsaps R.K., Black J., Potgieter L.N.D.","7402308045;36838037500;8371157900;57212989992;7004094951;","Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis",1998,"Journal of Veterinary Diagnostic Investigation","10","1",,"93","97",,21,"10.1177/104063879801000119","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031608338&doi=10.1177%2f104063879801000119&partnerID=40&md5=31f2a339f9aae5ab418700584f0a8c66","Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Department of Pathology, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; American BioResearch, PO Box 584, Seymour, TN 37865-0584, United States","Kennedy, M.A., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Brenneman, K., Department of Pathology, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Millsaps, R.K., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Black, J., American BioResearch, PO Box 584, Seymour, TN 37865-0584, United States; Potgieter, L.N.D., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States",[No abstract available],,"agar gel electrophoresis; animal; animal disease; article; cat; cat disease; comparative study; Coronavirus; fluorescent antibody technique; genetics; isolation and purification; methodology; open reading frame; polymerase chain reaction; serology; virus genome; virus infection; Animals; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; Electrophoresis, Agar Gel; Feline Infectious Peritonitis; Fluorescent Antibody Technique, Indirect; Genome, Viral; Open Reading Frames; Polymerase Chain Reaction; Serologic Tests","Almeida, J.D., Practical aspects of diagnostic electron microscopy (1980) Yale J Biol Med, 53, pp. 5-18; Burleson, F.G., Chambers, T.M., Wiedbrauk, D.L., (1992) Virology: A Laboratory Manual, pp. 41-44. , Academic Press, San Diego, CA; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction (1987) Anal Biochem, 162, pp. 156-159; Fiscus, S.A., Rivoire, B.L., Teramoto, Y.A., Humoral immune response of cats to virulent and avirulent feline infectious peritonitis virus isolates (1987) Adv Exp Med Biol, 218, pp. 559-568; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., The molecular genetics of feline coronavirus: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Horzinek, M.C., Herrewegh, A., De Groot, R.J., Perspectives on feline coronavirus evolution (1995) Feline Pract, 23, pp. 34-39; Hoskins, J.D., Coronavirus infection in cats (1993) Vet Clin North Am Small Anim Pract, 23, pp. 1-16; Jubb, K.V.F., Kennedy, P.C., Palmer, N., (1993) Pathology of Domestic Animals, 4th Ed., pp. 438-441. , Academic Press, New York, NY; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet Microbiol, 42, pp. 65-77; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv Exp Med Biol, 218, pp. 529-550; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-20; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, pp. 8.11-8.20. , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Scott, F.W., Corapi, W.V., Olsen, C.W., Evaluation of the safety and efficacy of Primucell-FIP vaccine (1992) Feline Health Top, 7, pp. 6-8; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., Coronavirus serology in healthy pedigree cats (1992) Vet Rec, 131, pp. 35-36; Vennema, H., Poland, A., Hawkins, K.F., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-45; Vennema, H., Rossen, J.W.A., Wesseling, J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 91, pp. 134-140; Wolf, J., The impact of feline infectious peritonitis on catteries (1995) Feline Pract, 23, pp. 21-23","Kennedy, M.A.; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"9526870","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0031608338
"Winther B., Gwaltney Jr. J.M., Mygind N., Hendley J.O.","7003521735;7005905022;7102682582;7006491299;","Viral-induced rhinitis",1998,"American Journal of Rhinology","12","1",,"17","20",,44,"10.2500/105065898782102954","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031948413&doi=10.2500%2f105065898782102954&partnerID=40&md5=aa4433164d269207588b1cc44425c37a","Department of Otolaryngology, Head and Neck Surgery, University of Virginia, Health Sciences Center, Charlottesville, VA, United States; Department of Internal Medicine, University of Virginia, Health Sciences Center, Charlottesville, VA, United States; Department of Pediatrics, University of Virginia, Health Sciences Center, Charlottesville, VA, United States; Department of Respiratory Diseases, University of Aarhus, Denmark; Department of Otolaryngology, Head and Neck Surgery, University of Virginia, Health Sciences Center, PO Box 430, Charlottesville, VA 22908, United States","Winther, B., Department of Otolaryngology, Head and Neck Surgery, University of Virginia, Health Sciences Center, Charlottesville, VA, United States, Department of Otolaryngology, Head and Neck Surgery, University of Virginia, Health Sciences Center, PO Box 430, Charlottesville, VA 22908, United States; Gwaltney Jr., J.M., Department of Internal Medicine, University of Virginia, Health Sciences Center, Charlottesville, VA, United States; Mygind, N., Department of Pediatrics, University of Virginia, Health Sciences Center, Charlottesville, VA, United States; Hendley, J.O., Department of Respiratory Diseases, University of Aarhus, Denmark","Upper respiratory viruses cause self-limited illness characterized by acute rhinitis. In rhinovirus colds the symptoms are thought to be caused by the host response rather than viral damage of the nasal epithelium. Rhinovirus triggers an inflammatory cascade, evidenced by the presence of inflammatory mediators (e.g., IL-8) and proinflammatory cytokines (e.g., kinins) in nasal secretions, which results in symptomatic illness. In contrast to rhinovirus and coronavirus, which do not cause discernible epithelial damage, influenza virus and adenovirus do damage the nasal epithelium. Appropriate antiviral therapy will depend on the causative virus. Treatment of rhinovirus colds may require an antiviral agent (e.g., interferon α) in combination with antiinflammatory medication.",,"alpha adrenergic receptor stimulating agent; alpha interferon; antihistaminic agent; antiinflammatory agent; antivirus agent; corticosteroid; cytokine; interleukin 1beta; interleukin 6; interleukin 8; ipratropium bromide; naproxen; nonsteroid antiinflammatory agent; prednisone; tumor necrosis factor; Adenovirus; common cold; conference paper; Coronavirus; cytopathogenic effect; human; Human rhinovirus; Influenza virus; intranasal drug administration; nose mucosa; oral drug administration; rhinitis; topical drug administration; upper respiratory tract infection; virus infection; virus shedding","Rossman, M.G., Palmenberg, A.C., Conservation of the putative receptor attachment site in picornaviruses (1988) Virology, 64, pp. 373-382; Hendley, J.O., Gwaltney Jr., J.M., Mechanisms of transmission of rhinovirus infection (1988) Epidemiol Rev, 10, pp. 242-258; Hendley, J.O., Gwaltney Jr., J.M., Jordan Jr., W.S., Rhinovirus infections in an industrial population. IV. Infections within families of employees during two fall peaks of respiratory illness (1969) Am J Epidemiol, 89, pp. 184-196; Dingle, J.H., Badger, G.F., Jordan Jr., W.S., (1964) Illness in the Home. A Study of 25,000 Illnesses in a Group of Cleveland Families, , Cleveland: The Press of Western Reserve University; Winther, B., Gwaltney Jr., J.M., Mygind, N., Turner, R.B., Hendley, J.O., Sites of rhinovirus recovery after point-inoculation of the upper airway (1986) JAMA, 256, pp. 1763-1767; Winther, B., Gwaltney Jr., J.M., Hendley, J.O., Respiratory virus infection of monolayer cultures of human nasal epithelial cells (1990) Am Rev Resp Dis, 141, pp. 839-845; Hoorn, B., Tyrrell, D.A., Effects of some viruses on ciliated cells (1966) Am Rev Respir Dis, 93, pp. 156-161; Becker, S., Soukup, J., Yankaskas, J.R., Respiratory syncytial virus infection of human primary nasal and bronchial epithelial cell cultures and bronchoalveolar macrophages (1992) Am J Resp Cell Mol Biol, 6, pp. 369-374; Winther, B., Brofeldt, S., Christensen, B., Mygind, N., Light and scanning electron microscopy of nasal biopsy material from patients with naturally acquired common colds (1984) Acta Otolaryngol (Stockh), 97, pp. 309-318; Carson, J.L., Collier, A.M., Hu, S.S., Acquired ciliary defects in nasal epithelium of children with acute viral upper respiratory infections (1985) New Eng J Med, 312, pp. 463-468; Winther, B., Farr, B., Turner, R.B., Hendley, J.O., Gwaltney Jr., J.M., Mygind, N., Histopathologic examination and enumeration of polymorphonuclear leukocytes in the nasal mucosa during experimental rhinovirus colds (1984) Acta Otolaryngol Suppl, 413, pp. 19-24; Turner, R.B., Winther, B., Hendley, J.O., Mygind, N., Gwaltney, J.M., Sites of virus recovery and antigen detection in epithelial cells during experimental rhinovirus infection (1984) Acta Otolaryngol Suppl, 413, pp. 9-14; Bardin, P.G., Johnston, S.L., Sanderson, G., Detection of rhinovirus infection of the nasal mucosa by oligonucleotide in situ hybridization (1994) Am J Respir Cell Mol Biol, 10, pp. 207-213; Arruda, E., Boyle, T.R., Winther, B., Pevear, D.C., Gwaltney Jr., J.M., Hayden, F.G., Localization of human rhinovirus replication in the upper respiratory tract by in situ hybridization (1995) J Infect Dis, 171, pp. 1329-1333; Arruda, E., Mifflin, T.E., Gwaltney, J.M., Winther, B., Hayden, F.G., Localization of rhinovirus replication in vitro with in situ hybridization (1991) J Med Virol, 34, pp. 38-44; Winther, B., Greve, J.M., Gwaltney Jr., J.M., Innes, D.J., Eastman, R.J., McClelland, A., Hendley, J.O., Surface expression of ICAM-1 on epithelial cells in the human adenoid (1997) J Infect Dis, 176, pp. 523-525; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Immunohistochemical analysis of nasal biopsies during rhinovirus experimental colds (1994) Am J Respir Crit Care Med, 150, pp. 1130-1136; Naclerio, R.M., Proud, D., Lichtenstein, L.M., Kagey-Sobotka, A., Hendley, J.O., Sorrentino, J., Gwaltney Jr., J.M., Kinins are generated during experimental rhinovirus colds (1988) J Infect Dis, 157, pp. 133-142; Levandowski, R.A., Ou, D.W., Jackson, G.G., Acute-phase decrease of T-lymphocyte subsets in rhinovirus infection (1986) J Infect Dis, 153, pp. 743-748; Winther, B., Innes, D.F., Bratsch, J., Hayden, F.G., Lymphocyte subsets in the nasal nasal mucosa and peripheral blood during experimental rhinovirus infection (1992) Am J Rhinol, 6, pp. 149-156; Winther, B., The effect on the nasal mucosa of respiratory viruses (common cold) (1994) Danish Med Bull, 41, pp. 193-204; Turner, R.B., Rhinovirus infection of human embryonic lung fibroblast induces the production of a chemoattractant for polymorphonuclear leukocytes (1988) J Infect Dis, 157, pp. 346-350; Proud, D., Epithelial derived cytokines and the modulation by virus infection (1995) Proceedings I, XVI European Congress of Allergology and Clinical Immunology ECACI, pp. 357-362; Subauste, M.C., Jacoby, D.B., Richards, S.M., Proud, D., Infection of a human respiratory epithelial cell line with rhinovirus. Induction of cytokine release and modulation of susceptibility to infection by cytokine exposure (1995) J Clin Invest, 96, pp. 549-557; Noah, T.L., Becker, S., Respiratory syncytial virus-induced cytokine production by a human bronchial epithelial cell line (1993) Am J Physiol, 265, pp. L472-L478; Choi, A.M.K., Jacoby, D.B., Influenza virus A infection induces interleukin-8 gene expression in human airway epithelial cells (1992) FEBS Letters, 309, pp. 327-329; Becker, S., Koren, H.S., Henke, D.C., Interleukin-8 expression in normal nasal epithelium and its modulation by infection with respiratory syncytial virus and cytokines tumor necrosis gactor, Interleukin-1, and Interleukin-6 (1993) Am J Respir Cell Mol Biol, 8, pp. 20-27; Roseler, S., Holtappels, G., Wagenmann, M., Bachert, C., Elevated levels of interleukins IL-18, IL-6 a, IL-6, and IL-8 in naturally acquired viral rhinitis (1995) Eur Arch Otorhinolaryngol, 252 (SUPPL.), pp. S61-S63; Noah, T.L., Henderson, F.W., Wortman, I.A., Nasal cytokine production in viral acute upper respiratory infection of childhood (1995) J Infect Dis, 171, pp. 584-592; Kenney, J.S., Baker, C., Welch, M.R., Altman, L.C., Synthesis of interleukin-1, interleukin-6, and interleukin-8 by cultured human nasal epithelial cells (1994) J Allergy Clin Immunol, 93, pp. 1060-1067; Proud, D., Gwaltney Jr., J.M., Hendley, J.O., Increased levels of Interleukin-1 are detected in nasal secretions of volunteers during experimental rhinovirus colds (1994) J Infect Dis, 169, pp. 1007-1013; Zhu, Z., Tang, W., Ray, A., Wu, Y., Einarsson, O., Landry, M., Gwaltney Jr., J.M., Elias, J.A., Rhinovirus stimulation of Interleukin-6 in vivo and in vitro: Evidence for NF-κB-dependent transcriptional activation (1996) J Clin Invest, 97, pp. 421-430; Uyttenhove, C.J., Coulie, P.G., Van Snick, J., T cell growth and differentiation induced by interleukin HP1/IL-6, the murine hybridoma/plasmacytoma growth factor (1988) J Exp Med, 167, pp. 1417-1427; Muraguchi, A., Hirano, T., Tang, B., The essential role of B cell stimulatory factor 2 (BSF-2/IL-6) for the terminal differentiation of B cells (1988) J Exp Med, 167, pp. 332-344; Proud, D., Reynolds, C.J., Lacapra, S., Nasal provocation with bradykinin induces symptoms of rhinitis and a sore throat (1988) Am Rev Respir Dis, 137, pp. 613-616; Gwaltney Jr., J.M., Phillips, C.D., Miller, R.D., Riker, D.K., Computed tomographic study of the common cold (1994) N Engl J Med, 330, pp. 25-30; Hayden, F.G., Albrecht, J.K., Kaiser, D.L., Gwaltney Jr., J.M., Prevention of natural colds by contact prophylaxis with intranasal Alpha2-Interferon (1986) N Engl J Med, 314, p. 71; Hayden, F.G., Gwaltney Jr., J.M., Intranasal Interferon-α2 treatment of xxperimental rhinoviral colds (1984) J Infect Dis, 150, pp. 174-180; Gwaltney Jr., J.M., Combined antiviral and antimediator treatment of rhinovirus colds (1992) J Infect Dis, 166, pp. 776-782; Farr, B.M., Gwaltney Jr., J.M., Hendley, J.O., A randomized controlled trial of glucocorticoid prophylaxis against experimental rhinovirus infection (1990) J Infect Dis, 162, pp. 1173-1177; Gustafson, L.M., Proud, D., Hendley, J.O., Hayden, F.G., Gwaltney Jr., J.M., Oral prednisone therapy in experimental rhinovirus infections (1996) J Allergy Clin Immunol, 97, pp. 1009-1014; Gwaltney Jr., J.M., Park, J., Paul, R.A., Randomized controlled trial of clemastine fumarate for treatment of experimental rhinovirus colds (1996) Clin Infect Dis, 22, pp. 656-662; Sperber, S.J., Sorrentino, J.V., Riker, D.K., Hayden, F.G., Evaluation of an alpha agonist alone and in combination with a nonsteroidal anti-inflammatory agent in the treatment of experimental rhinovirus colds (1989) Bull N Y Acad Med, 65, pp. 145-160; Borum, P., Olsen, L., Winther, B., Mygind, N., Ipratropium nasal spray: A new treatment for rhinorrhea in the common cold (1981) Am Rev Respir Dis, 123, pp. 418-420; Østberg, B., Winther, B., Borum, P., Mygind, N., Common cold and high-dose ipratropium bromide: Use of anticholinergic medication as an indicator of reflex-mediated hypersecretion (1997) Rhinology, 35, pp. 58-62","Winther, B.; Department of Otolaryngology, Head and Neck Surgery, Univ. of Virginia Hlth. Sci. Center, PO Box 430, Charlottesville, VA 22908, United States",,"OceanSide Publications Inc.",10506586,,AJRHE,"9513654","English","Am. J. Rhinol.",Conference Paper,"Final",,Scopus,2-s2.0-0031948413
"Lubinski J., Nagashunmugam T., Friedman H.M.","7005557040;6603789573;57189210444;","Viral interference with antibody and complement",1998,"Seminars in Cell and Developmental Biology","9","3",,"329","337",,53,"10.1006/scdb.1998.0242","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032087482&doi=10.1006%2fscdb.1998.0242&partnerID=40&md5=fb8fda7c5efb57beb1934eba31a872e5","Division of Infectious Diseases, Department of Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6073, United States","Lubinski, J., Division of Infectious Diseases, Department of Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6073, United States; Nagashunmugam, T., Division of Infectious Diseases, Department of Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6073, United States; Friedman, H.M., Division of Infectious Diseases, Department of Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6073, United States","Viruses have evolved strategies to evade immunity mediated by antibody and complement. Herpesviruses and coronaviruses encode IgG Fc binding proteins that inhibit IgG activity, enabling the virus or infected cell to escape antibody attack. Herpesviruses, vaccinia virus and HIV-1 have the capacity to interfere with complement, either by incorporation of cellular complement regulatory proteins into the virion envelope or cell membrane, or by expression of viral molecules that mimic functions of complement regulatory proteins. The structure and biological activities of herpes simplex virus type 1 (HSV-1) glycoproteins gE, gI and gC are described. These glycoproteins protect HSV from immune attack; HSV-1 gE/gI form a complex that binds the Fc domain of IgG while gC is a C3b binding complement regulatory protein, providing a survival advantage to the virus in vitro and in vivo by inhibiting immune functions.","Complement; Complement regulatory proteins; Fc receptors; HSV-1; Immune evasion","Herpes; Human herpesvirus 1; Human immunodeficiency virus 1; Vaccinia; Vaccinia virus; Fc receptor; virus antibody; virus envelope protein; animal; biological model; complement classical pathway; Herpes simplex virus 1; human; immunology; review; virus; Animals; Antibodies, Viral; Complement Pathway, Classical; Herpesvirus 1, Human; Humans; Models, Immunological; Receptors, IgG; Viral Envelope Proteins; Viruses","Anderson, C.L., Looney, R.J., Human leukocyte IgG Fc receptors (1986) Immunol Today, 7, pp. 264-266; Kinet, J.-P., Antibody-cell interactions: Fc receptors (1989) Cell, 57, pp. 351-354; Ravetch, J.V., Fc receptors: Rubor redux (1994) Cell, 78, pp. 553-560; Watkins, J.F., Adsorption of sensitized sheep erythrocytes to Hela cells infected with herpes simplex virus (1964) Nature, 202, pp. 1364-1365; Westmoreland, D., Watkins, J.F., The IgG receptor induced by herpes simplex virus: Studies using radioiodinated IgG (1974) J Gen Virol, 24, pp. 167-178; Baucke, R.B., Spear, P.G., Membrane proteins specified by herpes simplex viruses. V. 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Friedman, H.M., Wang, L., Fishman, N.O., Lambris, J.D., Eisenberg, R.J., Cohen, G.H., Lubinski, J.M., Immune evasion properties of herpes simplex virus type 1 glycoprotein gC (1996) J Virol, 70, pp. 4253-4260; Herold, B.C., WuDunn, D., Soltys, N., Spear, P.G., Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity (1991) J Virol, 65, pp. 1090-1098; Tal-Singer, R., Peng, C., De Leon, M., Abrams, W.R., Banfield, B.W., Tufaro, F., Cohen, G.H., Eisenberg, R.J., The interaction of herpes simplex glycoprotein C with mammalian cell surface molecules (1995) J Virol, 69, pp. 4471-4483; Trybala, E., Bergstrom, T., Svennerholm, B., Jeansson, S., Glorioso, J.C., Olofsson, S., Localization of a functional site on herpes simplex virus type 1 glycoprotein C involved in binding to cell surface heparan sulfate (1994) J Gen Virol, 75, pp. 743-752; Friedman, H.M., Wang, L., Lambris, J., Eisenberg, R.J., Cohen, G.H., Burger, R., Frank, M.M., Lubinski, J., Immune evasion by HSV-1 glycoprotein gC (1997) 22nd International Herpesvirus Workshop, , San Diego, CA, Abstract 417","Lubinski, J.; Division of Infectious Diseases, Department of Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6073, United States",,"Elsevier Ltd",10849521,,SCDBF,"9665870","English","Semin. Cell. Dev. Biol.",Article,"Final",,Scopus,2-s2.0-0032087482
"Keeler Jr. C.L., Reed K.L., Nix W.A., Gelb Jr. J.","7006248739;57197379076;57196757385;57206493616;","Serotype identification of avian infectious bronchitis virus by RT-PCR of the peplomer (S-1) gene",1998,"Avian Diseases","42","2",,"275","284",,94,"10.2307/1592477","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345055303&doi=10.2307%2f1592477&partnerID=40&md5=77991f4f8a7e3daf59862b06a244b7d0","Dept. of Animal and Food Sciences, College of Agricultural Sciences, University of Delaware, Newark, DE 19717-1303, United States","Keeler Jr., C.L., Dept. of Animal and Food Sciences, College of Agricultural Sciences, University of Delaware, Newark, DE 19717-1303, United States; Reed, K.L., Dept. of Animal and Food Sciences, College of Agricultural Sciences, University of Delaware, Newark, DE 19717-1303, United States; Nix, W.A., Dept. of Animal and Food Sciences, College of Agricultural Sciences, University of Delaware, Newark, DE 19717-1303, United States; Gelb Jr., J., Dept. of Animal and Food Sciences, College of Agricultural Sciences, University of Delaware, Newark, DE 19717-1303, United States","The S-1 peplomer gene sequences of 3 l strains of avian coronavirus infectious bronchitis virus (IBV) from North America, Europe, and Australia were compared to identify common and unique regions for possible diagnostic applications. S-1 sequences that were conserved among serotypes and sequences that were variable between serotypes were identified. Based on conserved S-1 gene sequences, 'general' degenerate oligonucleotide primers were designed that amplified IBV genomic RNA by the reverse transcriptase polymerase chain reaction (RT-PCR) procedure regardless of serotype. Primers specific for IBV serotypes Massachusetts, Connecticut, Arkansas, JMK, Delaware (DE/072/92), and California (CA/633/85) were designed from regions of the S-1 gene exhibiting extensive sequence hypervariability. The ability to identify these six serotypes of IBV by RT-PCR was demonstrated by testing the serotype-specific primers on a panel of unknown samples that included 30 reference strains and field isolates previously characterized by virus neutralization (VN). The use of serotype-specific primers in RT-PCR provides a rapid and accurate means of identifying IBV.","Infectious bronchitis virus (BV); Reverse transcriptase polymerase chain reaction (RT-PCR); Serotype identification","Australia; Avian infectious bronchitis virus; degenerate oligonucleotide primer; Europe; genomic RNA; identification; infectivity; North America; peplomer gene; reverse transcription polymerase chain reaction; serotype; United States; virus neutralization; Aves; Avian infectious bronchitis virus; Coronavirus","Andreasen J.R., Jr., Jackwood, M.W., Hilt, D.H., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis., 35, pp. 216-220; Binns, M.M., Boursnell, M.E., Cavanagh, D., Pappin, D.J., Brown, T.D., Cloning and sequencing of the gene encoding the spike protein of coronavirus IBV (1985) J. Gen. 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Kendall/Hunt Publishing Co., Dubuque, IA; Gelb J., Jr., Keeler C.L., Jr., Nix, W.A., Rosenberger, J.K., Cloud, S.S., Antigenic and S-1 genomic characterization ol the Delaware variant serotype of infectious bronchitis virus (1997) Avian Dis., 41, pp. 661-669; Gelb J., Jr., Killian, S.L., Serum antibody responses of chickens following sequential inoculations with infectious bronchitis virus serotypes (1987) Avian Dis., 31, pp. 513-522; Gelb J., Jr., Perkins, B.E., Rosenberger, J.K., Allen, P.H., Serologic and cross-protection studies with several infectious bronchitis virus isolates from Delmarva-reared broiler chickens (1981) Avian Dis., 25, pp. 655-666; Gelb J., Jr., Wolff, J.B., Moran, C.A., Variant serotypes of infectious bronchitis virus isolated from commercial layer and broiler chickens (1991) Avian Dis., 35, pp. 82-87; Harless, D.D., Hobert, V.A., Donahoe, J.P., Daft, B.M., Serologic investigation of suspect variant bronchitis isolates from California (1987) Proceedings of the 36th Western Poultry Disease Conference, pp. 63-66. , Davis, CA; Higgins, D.G., Sharp, P.M., CLUSTAL: A package for performing multiple sequence alignment on a microcomputer (1988) Gene, 73, pp. 237-244; Hitchner, S.B., Serendipity in science - Discovery of the B-1 strain of Newcastle disease virus (1975) Avian Dis., 19, pp. 215-223; Homberger, F.R., Smith, A.L., Barthold, S.W., Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. 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Iowa State University Press, Ames, IA; Kusters, J.G., Jager, E.J., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Kusters, J.G., Niesters, H.G.M., Bleumink-Pluym, N.M.C., Davelaar, F.G., Horzinek, M.C., Van Der Zeijst, B.A.M., Molecular epidemiology of infectious bronchitis virus in the Netherlands (1987) J. Gen. Virol., 68, pp. 343-352; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Koch, G., Posthumus, W.P.A., Meloen, R.H., Van Der Zeijst, B.A.M., Analysis of an immunodominant region of infectious bronchitis virus (1989) J. Immunol., 143, pp. 2692-2698; Kwon, H.M., Jackwood, M.W., Gelb J., Jr., Differentiation of infectious bronchitis virus serotypes using the polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Dis., 37, pp. 194-202; Lin, Z., Kato, A., Kudou, Y., Ueda, S., A new typing method for the avian infectious bronchitis virus using polymerase chain reaction and restriction enzyme fragment length polymorphism (1991) Arch. Virol., 116, pp. 19-31; Myint, S.H., Human coronavirus infections (1995) The Coronaviridae, pp. 389-401. , S. G. Siddell, ed. Plenum Press, New York; Niesters, H.G.M., Lenstra, J.A., Spaan, W.J.M., Zijederveld, A.J., Bleumink-Pluym, N.M.C., Hong, F., Van Scharrenburg, G.J.M., Van Der Zeijst, B.A.M., The peplomer protein sequence of the M41 strain of corona virus IBV and its comparison with Beaudette strains (1986) Virus Res., 5, pp. 253-263; Rudd, K.H., Machado, G.V., Woodward, W.D., Cooperative investigation for the isolation of respiratory agents on problem cage layer operations (1989) Proceedings of the 38th Western Poultry Disease Conference, pp. 79-82. , Tempe, AZ","Keeler Jr., C.L.; Delaware Agric. Experiment Station, Dept. of Animal and Food Sciences, University of Delaware, 040 Townsend Hall, Newark, DE 19717-1303, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"9645318","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0345055303
"Els H.J., Josling D.","7004507813;6505822647;","Viruses and virus-like particles identified in ostrich gut contents",1998,"Journal of the South African Veterinary Association","69","3",,"74","80",,16,"10.4102/jsava.v69i3.821","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032149974&doi=10.4102%2fjsava.v69i3.821&partnerID=40&md5=758ab5f6163fddf1d541c5f7a72b158a","Electron Microscopy Unit, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort, 0110, South Africa","Els, H.J., Electron Microscopy Unit, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort, 0110, South Africa; Josling, D., Electron Microscopy Unit, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort, 0110, South Africa","Samples of either gut content from ostriches showing symptoms of enteritis, or allantoic fluid of eggs inoculated with ostrich isolates, were examined for the presence of viral agents by direct negative-contrast electron microscopy. Only a few virus types could be identified with certainty, namely a circovirus (1 sample), a coronavirus (1 sample), a member of either the toga- or bunyaviridae (1 sample), enterovirus (16 samples) and paramyxovirus (26 samples). A large number of samples contained structures resembling myxovirus particles that were interpreted as fringed membranous particles of non-viral origin. An unusual observation of probable single-strand nucleocapsid helices, possibly originating from digested plant material and which were identified in a number of small intestine samples, is reported. This is the 1st report of a spectrum of viruses and virus-like particles occurring in enteric samples from ostriches in South Africa. The low incidence and variety of viruses reported here contribute to the multifactorial origin and complexity of enteric disease in ostriches as well as in other birds and mammalian species.","Enteritis; Fringed membranous particles; Ostrich; Paramyxovirus","Aves; Bunyaviridae; Circovirus; Coronavirus; Enterovirus; Mammalia; Myxovirus; Paramyxoviridae; Struthio camelus; Struthioniformes; animal; animal disease; article; bird disease; electron microscopy; enteritis; isolation and purification; ostrich; Paramyxovirus; small intestine; virion; virology; Animals; Bird Diseases; Enteritis; Intestine, Small; Microscopy, Electron; Respirovirus; Struthioniformes; Virion","Allwright, D., Viruses encountered in intensively reared ostriches in southern Africa (1996) Proceedings International Congress: Improving Our Understanding of Ratites in a Farming Environment. University of Manchester, England, pp. 27-33. , Deeming D C (ed.), 27-29 March 1996; Arnott, H.J., Smith, K.M., Electron microscopic observations on the apparent replication in vivo of a plant virus (1968) Virology, 34, pp. 25-35; Edwardson, J.R., Purcifull, D.E., Christie, R.G., Structure of cytoplasmic inclusions in plants infected with rod-shaped viruses (1968) Virology, 34, pp. 250-263; Els, H.J., Josling, D., Procedures for the diagnosis of virus particles by electron microscopy (1998) Journal of the South African Veterinary Association, 69, pp. 2-3; Geyer, A., Steele, A.D., Peenze, I., Lecatsas, G., Astrovirus-like particles, adenoviruses and rotaviruses associated with diarrhoea in piglets (1994) Journal of the South African Veterinary Association, 65, pp. 164-166; Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis complex/ spiking mortality (1995) Avian Pathology, 24, pp. 497-505; Gough, R.E., Collins, M.S., Alexander, D.J., Cox, W.J., Viruses and virus-like particles detected in samples from diseased game birds in Great Britain during 1988 (1990) Avian Pathology, 19, pp. 331-342; Kushner, D.J., Self-assembly of biological structures (1969) Bacteriological Reviews, 33, pp. 302-345; Marcus, P.B., Glycocalyceal bodies and their role in tumour typing (1981) Journal of Submicroscopic Cytology, 13, pp. 483-500; Murti, K.G., Bean, W.J., Webster, R.G., Helical ribonucleoproteins of influenza virus: An electron microscopic analysis (1980) Virology, 104, pp. 224-229; Reece, R.L., Infectious stunting syndrome (1996) Poultry Diseases (4th Edn), pp. 375-388. , Jordan F T W, Pattison M (eds). W B Saunders, London; Schulze, I.T., Structure of influenza virion (1973) Advances in Virus Research, 18, pp. 1-55. , Lauffer M A, Bang F B, Maramorosch K, Smith K H (eds), Academic Press, London; Schnagl, R.D., Brookes, S., Medvedec, S., Morey, F., Characteristics of Australian human enteric coronavirus-like particles: Comparison with human respiratory coronavirus 229E and duodenal brush border vesicles (1987) Archives of Virology, 97, pp. 309-323","Els, H.J.; Electron Microscopy Unit, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort, 0110, South Africa",,"AOSIS (pty) Ltd",10199128,,JAVTA,"9850509","English","J. S. Afr. Vet. Assoc.",Article,"Final",Open Access,Scopus,2-s2.0-0032149974
"Wood A., Payne D.","57199004032;24562537000;","The action of three antiseptics/disinfectants against enveloped and non-enveloped viruses",1998,"Journal of Hospital Infection","38","4",,"283","295",,40,"10.1016/S0195-6701(98)90077-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031955937&doi=10.1016%2fS0195-6701%2898%2990077-9&partnerID=40&md5=683c7cc2b36278f9ccd4dd525069e24d","Reckitt and Colman Products Limited, Dansom Lane, Hull, HU8 7DS, United Kingdom","Wood, A.; Payne, D., Reckitt and Colman Products Limited, Dansom Lane, Hull, HU8 7DS, United Kingdom","The antiviral action of chloroxylenol, benzalkonium chloride and cetrimide/chlorhexidine was assessed against a range of enveloped and non-enveloped human viruses using a suspension test method. Viral suspensions of 106-107 pfu/TCID50 or sfu were prepared in each of the antiseptic/ disinfectant solutions in the presence of a bovine serum/yeast extract mixture to simulate 'dirty conditions'. During incubation, aliquots were removed at predetermined timepoints up to 10 min to assess the kinetics of inactivation. Results indicate that all products were effective in inactivating the enveloped viruses herpes simplex virus type 1 and human immunodeficiency virus type 1, whilst being ineffective in inactivating human coronavirus, also enveloped, and the non-enveloped viruses. The exception to this was the benzalkonium chloride-based product (Dettol Hospital Concentrate) which was active against the non-enveloped human coxsackie virus. Four antiseptic/disinfectant solutions with chloroxylenol, benzalkonium chloride, cetrimide/chlorhexidine and povidone-iodine were also assessed for antiviral effect against human immunodeficiency virus in the presence of whole human blood. All four solutions proved to be effective within 1 min despite the cytotoxic nature of the compounds to the detection system.","Antiseptic/disinfectant; Antiviral; Cetrimide/chlorhexidine enveloped; Chloroxylenol benzalkonium chloride; Non-enveloped viruses","antiinfective agent; benzalkonium chloride; cetrimide; chlorhexidine; chloroxylenol; disinfectant agent; povidone iodine; antiviral activity; article; Coronavirus; Coxsackie virus; Herpes simplex virus 1; Human immunodeficiency virus 1","Comments on the guidelines of BGA; German Federal Health Office and the DVV; German Association for the Control of Virus Diseases for Testing the Effectiveness of Chemical Disinfectants against Viruses. Official translation of the BGA and DVV (1983) Bundesgesundhbl., 26, pp. 413-415; Quinn, P.J., Virucidal activity of disinfectants (1992) Principles and Practice of Disinfection, Presentation and Sterilisation. 2nd Edn., pp. 150-171. , Russell AD et al., (eds). Oxford: Blackwell Scientific Publications; Chen, J.H.S., Koski, T.A., Methods of testing virucides (1983) Disinfection, Sterilisation and Preservation. 3rd Edn., pp. 981-997. , Block SS, (ed). Philadelphia: Lea & Febiger; Cremieux, A., Fleurette, J., Methods of testing disinfectants (1983) Disinfection, Sterilisation and Preservation. 3rd Edn., pp. 918-945. , Block SS, (ed). Philadelphia: Lea & Febiger; Klein, M., De Forest, A., Principles of viral inactivation (1983) Disinfection, Sterilisation and Preservation. 3rd Edn., pp. 422-434. , Block SS, (ed). Philadelphia: Lea & Febiger; Bailey, A., Longson, M., Viricidal activity of chlorhexidine on stains of Herpes virus hominis, poliovirus and adenovirus (1972) J Clin Path, 25, pp. 76-78; Tyler, R., Aycliffe, G.A.J., A surface test for virucidal activity of disinfectants: Preliminary study with herpes virus (1987) J Hosp Infect, 9, pp. 22-29; Resnick, L., Veren, K., Salahuddin, S.Z., Tondreau, S., Markham, P.D., Stability and inactivation of HTLVIII/LAV under clinical and laboratory environments (1986) J Amer Med Assoc, 255, pp. 1887-1891; Kaplan, J.C., Crawford, D.C., Durno, A.G., Schooley, R.T., Inactivation of human immunodeficiency virus by Betadine (1987) Infect Control, 8, pp. 412-414; Bloomfield, S.F., Smith-Burchnell, C.A., Dalgleish, A.G., Effect of hypochlorite-releasing disinfectants against the human immunodeficiency virus (1990) J Hosp Infect, 15, pp. 273-278; Narang, H.K., Codd, A.A., Action or commonly used disinfectants against enteroviruses (1983) J Hosp Infect, 4, pp. 209-212; Grossgebauer, K., (1970) Virus Disinfection in Disinfection, pp. 103-148. , Bernarde M, editor. New York: Marcel Dekker; British Pharmacopoeia, 1988, HMSO","Payne, D.; Reckitt and Colman Products Limited, Dansom Lane, Hull HU8 7DS, United Kingdom",,"W.B. Saunders Ltd",01956701,,JHIND,"9602977","English","J. Hosp. Infect.",Article,"Final",,Scopus,2-s2.0-0031955937
"Rabenau H., Knoll B., Allwinn R., Doerr H.W., Weber B.","7004984201;35916546100;6603600471;7102740671;57216111743;","Improvement of the specificity of enzyme immunoassays for the detection of rotavirus and adenovirus in fecal specimens",1998,"Intervirology","41","2-3",,"55","62",,17,"10.1159/000024915","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031732287&doi=10.1159%2f000024915&partnerID=40&md5=98cb8f7500d5d35a17e3fa254ec5279d","Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany; Laboratoires Reunis Kutter-L., Junglinster, Luxembourg; Laboratoires Reunis Kutter-L., Centre Langwies, L-6131 Junglinster, Luxembourg","Rabenau, H., Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany; Knoll, B., Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany; Allwinn, R., Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany; Doerr, H.W., Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany; Weber, B., Inst. F. Medizinische Virologie, Universitätskliniken Frankfurt, Germany, Laboratoires Reunis Kutter-L., Junglinster, Luxembourg, Laboratoires Reunis Kutter-L., Centre Langwies, L-6131 Junglinster, Luxembourg","A variable rate of false-positive results may be observed with commercial enzyme immunoassays (EIAs) for the detection of rotavirus and adenovirus antigen in stool specimens, depending on the quality of the reagents and the presence of potentially interfering substances in stool samples. The present study was performed in an attempt to improve the specificity of current commercial rotavirus and adenovirus EIAs without significant loss of sensitivity by optimizing the cut-off value. A collective of 174 stool samples obtained from children suffering from acute gastroenteritis was tested. Electron microscopy (EM) and PAGE were used as reference methods for rotavirus detection. For the evaluation of the adenovirus kits, virus isolation in cell culture and the polymerase chain reaction served as reference standards. The highest sensitivity for rotavirus and adenovirus detection was achieved by the Ridascreen® Rotavirus and Ridascreen® Adenovirus. However, the Ridascreen® Rotavirus and Ridascreen® Adenovirus produced the highest number of false-positive results (n = 9) for each rotavirus and adenovirus detection. Cross-reactivities to coronaviruses and reoviruses were observed with the rotavirus antigen EIAs. For Rotazyme II, Ridascreen Rotavirus and Ridascreen Adenovirus, the specificity could be markedly increased without loss of sensitivity by doubling the cut-off value. For the alternative immunoassays, which were overall more specific, it was not possible to significantly decrease the rate of false-positive results without impairment of sensitivity by raising the cut-off value. In conclusion, at least for some rotavirus and adenovirus antigen EIAs, the cut-off value set by the manufacturer may not permit an optimal differentiation between true-positive and -negative samples. By raising the cut-off value from 50 to 100%, the specificity of two rotavirus antigen and one adenovirus antigen EIA can be improved markedly without significant loss of sensitivity.","Coronavirus; Electron microscopy; PAGE; Reovirus","acute gastroenteritis; Adenovirus; analytical equipment; article; clinical trial; comparative study; Coronavirus; cross reaction; diagnostic value; electron microscopy; enzyme immunoassay; feces analysis; human; human cell; infant; laboratory diagnosis; newborn; polyacrylamide gel electrophoresis; preschool child; priority journal; Reovirus; Rotavirus; virus detection; Adenoviridae; Coronavirus; Orthoreovirus; Reovirus sp.; Rotavirus","Beards, G.M., Desselberger, U., Flewett, T.H., Temporal and geographical distributions of human rotavirus serotypes, 1983 to 1988 (1989) J Clin Microbiol, 27, pp. 2827-2833; Brandt, C.D., Kim, H.W., Rodriguez, W.J., Thomas, L., Yolken, R.H., Arrobio, J.O., Kapikian, A.Z., Chanok, R.M., Comparison of direct electron microscopy, immune electron microscopy, and rotavirus enzyme-linked immunosorbent assay for detection of gastroenteritis viruses in children (1981) J Clin Microbiol, 13, pp. 976-981; Dolan, K.T., Twist, E.M., Horton-Slight, P., Forrer, C., Bell, L.M., Plotkin, S.A., Clark, H.F., Epidemiology of rotavirus electrophoretypes determined by a simplified diagnostic technique with RNA analysis (1985) J Clin Microbiol, 21, pp. 753-758; Selb, B., Baumeister, H.G., Maass, G., Doerr, H.W., Detection of human rotavirus by nucleic acid analysis in comparison to enzyme-linked immunoassay and electron microscopy (1985) Eur J Clin Microbiol, 4, pp. 41-45; De Jong, J.C., Bijlsma, K., Wermenbol, A.G., Verweij-Uijterwaal, M.W., Van Der Avoort, H.G.A.M., Wood, D.J., Bailey, A.S., Osterhaus, A.D.M.E., Detection, typing, and subtyping of enteric adenoviruses 40 and 41 from fecal samples and observation of changing incidences of infections with these types and subtypes (1993) J Clin Microbiol, 31, pp. 1562-1569; Martin, A.L., Kudesia, G., Enzyme linked immunosorbent assay for detecting adenoviruses in stool specimens: Comparison with electron microscopy and isolation (1990) J Clin Pathol, 43, pp. 514-515; Arens, M., Swierkosz, E.M., Detection of rotavirus by hybridization with a nonradioactive synthetic DNA probe and comparison with commercial enzyme immunoassays and silver-stained polyacrylamide gels (1989) J Clin Microbiol, 27, pp. 1277-1279; Pacini, D.L., Brady, M.T., Budde, C.T., Connell, M.J., Hamparian, V.V., Hughes, J.H., Polyacrylamide gel electrophoresis of RNA compared with polyclonal- And monoclonal-antibody-based enzyme immunoassays for rotavirus (1988) J Clin Microbiol, 26, pp. 194-197; Dennehy, P.H., Gauntlett, D.R., Tente, W.E., Comparison of nine commercial immunoassays for the detection of rotavirus in fecal specimens (1988) J Clin Microbiol, 26, pp. 1630-1634; Weber, B., Harms, F., Selb, B., Doerr, H.W., Improvement of rotavirus isolation in the cell culture by immune peroxidase staining (1992) J Virol Methods, 38, pp. 187-194; Hierholzer, J.C., Halonen, P.E., Dahlen, P.O., Bingham, P.G., McDonough, M.M., Detection of adenovirus in clinical specimens by polymerase chain reaction and liquid-phase hybridization quantitated by time-resolved fluorometry (1993) J Clin Microbiol, 31, pp. 1886-1891; Yolken, R.H., Stopa, P.J., Analysis of nonspecific reactions in enzyme-linked immunosorbent assay testing for human rotaviruses (1979) J Clin Microbiol, 10, pp. 703-707; Dennehy, P.H., Gauntlett, D.R., Spangenberger, S.E., Choice of reference assay for the detection of rotavirus in fecal specimens: Electron microscopy versus enzyme immunoassay (1990) J Clin Microbiol, 28, pp. 1280-1283; Kapikian, A.Z., Chanock, R.M., Rotaviruses (1996) Fields Virology, Ed 3, pp. 1658-1708. , Fields BN, Knipe DM, Howley PM, et al (eds): Philadelphia. Lippincott-Raven Publishers; Keswick, B.H., Pickering, L.K., DuPont, H.L., Woodward, W.E., Survival and detection of rotaviruses on environmental surfaces in day care centers (1983) Appl Environ Microbiol, 46, pp. 813-816; Albert, S., Weber, B., Schäfer, V., Rosenthal, P., Simonsohn, M., Doerr, H.W., Six enteropathogens isolated from a case of acute gastroenteritis (1990) Infection, 18, pp. 381-382","Weber, B.; Lab. Reunis Kutter-Lieners-Hastert, Centre Langwies, L-6131 Junglinster, Luxembourg",,"S. Karger AG",03005526,,IVRYA,"9820838","English","Intervirology",Article,"Final",,Scopus,2-s2.0-0031732287
"Pizzichini M.M.M., Pizzichini E., Efthimiadis A., Chauhan A.J., Johnston S.L., Hussack P., Mahony J., Dolovich J., Hargreave F.E.","7005137660;6701464752;16635573800;57202492049;7401781716;6602325448;7102654582;7005059321;35392481400;","Asthma and natural colds. Inflammatory indices in induced sputum: A feasibility study",1998,"American Journal of Respiratory and Critical Care Medicine","158","4",,"1178","1184",,168,"10.1164/ajrccm.158.4.9712082","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031768355&doi=10.1164%2fajrccm.158.4.9712082&partnerID=40&md5=4e5af6faf3cf5642db927e06f5340ad4","McMaster University; Firestone Reg. Chest and Allerg. U., St. Joseph's Hospital, 50 Charlton Avenue East, Hamilton, Ont. L8N 4A6, Canada","Pizzichini, M.M.M., McMaster University; Pizzichini, E., McMaster University; Efthimiadis, A.; Chauhan, A.J.; Johnston, S.L.; Hussack, P.; Mahony, J.; Dolovich, J.; Hargreave, F.E., Firestone Reg. Chest and Allerg. U., St. Joseph's Hospital, 50 Charlton Avenue East, Hamilton, Ont. L8N 4A6, Canada","We examined the feasibility of using induced sputum to evaluate the airway inflammatory response to natural acute respiratory virus infections. We recruited eight asthmatics and nine healthy subjects on Day 4 of a cold. Viral infection was confirmed in six of the asthmatics (influenza A or B) and six of the healthy subjects (influenza A, rhinovirus, adenovirus, respiratory syncytial virus, and coronavirus). In the subjects with confirmed virus infection, five of the asthmatics had an objective exacerbation of asthma during the cold. Their sputum on Day 4 showed a high median total cell count of 19.7 x 106 cells/ml with a modest neutrophilia (58.5%) and high levels of interleukin-8 (IL-8) (16,000 pg/ml), eosinophilic cationic protein (ECP) (1,880 μg/L) and very high levels of fibrinogen (250 mg/L). In contrast, the proportion (1.3%) and absolute number of eosinophils was low. IL-2 levels were within the normal range, whereas IL-5 and interferon gamma were under the limit of detection of the assays. In the healthy subjects with a confirmed virus infection the sputum findings were qualitatively similar but significantly less prominent. Sputum IL-8 on Day 4 was strongly correlated with neutrophils (rs = 0.8, p &lt; 0.001). This correlation was also significant when each group was analyzed separately. On Day 21 there was a fall in the absolute number of neutrophils and in ECP and fibrinogen levels in both groups. Similar results were found in the two asthmatic and three healthy subjects with a cold of comparable severity but in whom vital infection was not confirmed. We conclude that induced sputum examination can be used to study the effects of natural colds and influenza on the airways of the lungs. The results also suggest that natural colds, on Day 4, cause neutrophilic lower airway inflammation that is greater in asthmatics than in healthy subjects. The greater inflammatory response in asthmatics may be due to the changes associated with trivial eosinophilia or to the different viruses involved.",,"eosinophil cationic protein; fibrinogen; gamma interferon; interleukin 2; interleukin 5; interleukin 8; adult; article; asthma; clinical article; common cold; controlled study; disease severity; eosinophilia; feasibility study; female; human; influenza; male; priority journal; respiratory tract infection; respiratory tract inflammation; sputum cytodiagnosis; sputum examination; virus infection","Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L.K., Symington, P., Holgate, S.T., Community study role of viral infections in exacerbations of asthma of asthma in 9-11 year old children (1995) B.M.J., 310, pp. 1225-1229; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Campbell, M.J., Josephs, L.K., Cunningham, A., Holgate, S.T., The relationship between upper respiratory infections and hospital admissions for asthma: A time-trend analysis (1996) Am. J. Respir. Crit. Crit. Med., 154, pp. 654-660; Busse, W.W., Gern, J.E., Viruses in asthma (1997) J. Allergy Clin. Immunol., 100, pp. 147-150; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airway inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Am. J. Respir. Crit. Care Med., 151, pp. 879-886; Grünberg, K., Smits, H.H., Timmers, M.C., Klerk, E.P.A., Dolhain, R.J.E.M., Hiemstra, P.S., Sterk, P.J., Experimental rhinovirus 16 infection: Effects on cell differentials and soluble markers in sputum of asthmatic subjects (1997) Am. J. Respir. Crit. Care Med., 156, pp. 609-616; Meschievitz, C.K., Shultz, S.B., Dick, E.C., A model for obtaining predictable natural transmission of rhinovirus in human volunteers (1984) J. Infect. Dis., 150, pp. 195-201; Calhoun, W.J., Dick, E.C., Schwartz, L.B., Busse, W.W., A common cold virus, rhinovirus 16, potentiates airway inflammation after segmental antigen bronchoprovocation in allergic subjects (1994) J. Clin. Invest., 94, pp. 2200-2208; Standardization of spirometry: 1987 Update (1987) Am. Rev. Respir. Dis., 136, pp. 1285-1298; Crapo, R.U., Morris, A.H., Gardner, R.M., Reference spirometric values using techniques and equipment that meets ATS recommendation (1981) Am. Rev. Respir. Dis., 123, pp. 659-694; Juniper, E.F., Cockcroft, D.W., Hargreave, F.E., (1994) Histamine and Methacholine Inhalation Tests: A Laboratory Tidal Breathing Protocol, 2nd Ed., , Astra Draco AB, Lund, Sweden; Pepys, J., Skin test in diagnosis (1975) Clinical Aspects of Immunology, 3rd Ed., pp. 55-80. , P. G. H. Gell, R. R. A. Coombs, and P. J. Lachmann, editors. Oxford: Blackwell Scientific Publications, Cambridge, MA; Pin, I., Gibson, P.G., Kolendowicz, R., Denburg, J.A., Hargreave, F.E., Dolovich, J., Use of induced sputum cell counts to investigate airway inflammation in asthma (1992) Thorax, 47, pp. 25-29; Pizzichini, M.M.M., Pizzichini, E., Clelland, L., Efthimiadis, A., Mahony, J., Dolovich, J., Hargreave, F.E., Sputum in severe exacerbations of asthma: Kinetics of inflammatory indices after prednisone treatment (1997) Am. J. Respir. Crit. Care Med., 155, pp. 1501-1508; Chauhan, A.J., Johnston, S.L., (1997) Advances in the Diagnosis Respiratory Viral Infections in Asthma and Respiratory Infections, , Marcel Decker, New York. (In press); Pizzichini, E., Pizzichini, M.M.M., Efthimiadis, A., Evans, S., Morris, M.M., Squillace, D., Gleich, G.J., Hargreave, F.E., Indices of airway inflammation in induced sputum: Reproducibility and validity of cell and fluid phase measurements (1996) Am. J. Respir. Crit. Care Med., 154, pp. 808-817; Naclerio, R.M., Proud, D., Lichtenstein, L.M., Sobotka, A.K., Hendley, J.O., Sorrentino, J., Gwaltney, J.M., Kinins are generated during experimental rhinovirus cold (1988) J. Infect. Dis., 1, pp. 133-142; Teran, L.M., Johnston, S.L., Schröder, J.M., Church, M.K., Holgate, S.T., Role of nasal interleukin-8 in neutrophil recruitment and activation in children with virus induced asthma (1997) Am. J. Respir. Crit. Care Med., 155, pp. 1362-1366; Greiff, L., Andersson, M., Akerlund, A., Wollmer, P., Svensson, C., Persson, C.O.A., Microvascular exudative hyperresponsiveness in human coronavirus-induced cold (1994) Thorax, 49, pp. 121-127; Trigg, C.G., Nicholson, K.G., Wang, J.H., Ireland, D.C., Jordan, S., Duddle, J.M., Hamilton, S., Davies, S.J., Bronchial inflammation and the common cold: A comparison of atopic and non-atopic individuals (1996) Clin. Exp. Allergy, 26, pp. 666-676; Bagglioni, M., Walz, A., Kunkel, S.L., Neutrophil activating peptide-1/interleukin-8, a novel cytokine that stimulates neutrophils (1989) J. Clin. Invest., 84, pp. 1045-1049; Matsukura, S., Kokuhu, F., Noda, H., Tokunaga, H., Adachi, M., Expression of IL-6, 1L-8, and RANTES of human bronchial epithelial cells, NCL-H292, induced by influenza virus A (1996) J. Allergy Clin. Immunol., 98, pp. 1080-1087; Mastronarde, J.G., He, B., Monick, M.M., Mukaida, N., Matsushima, K., Hunninghake, O.W., Induction of interleukin (IL)-8 gene expression by respiratory syncytial virus involves activation of nuclear factor (NF)-kappa B and NF-IL-6 (1996) Infect. Dis., 174, pp. 262-267; Subauste, M.C., Jacoby, D.B., Richards, S.M., Proud, D., Infection of a human respiratory epithelial cell line with rhinovirus: Induction of cytokine release and modulation of susceptibility to infection by cytokine exposure (1995) J. Clin. Invest., 96, pp. 549-557; Grünberg, K., Timmers, M.C., Smits, H.H., Klerk, E.P.A., Dick, E., Spaan, W.J.M., Dolhain, R.J.E.M., Sterk, P.J., Effects of experimental rhinovirus 16 colds on airway hyperresponsiveness to histamine and interleukin-8 in nasal lavage in asthmatic subjects in vivo (1995) Clin. Exp. Allergy, 156, pp. 609-616; Hennet, T., Ziltener, H.J., Frei, K., Peterhans, E., A kinetic study of immune mediators in the lungs of mice infected with influenza A virus (1992) J. Immunol., 149, pp. 932-939; Hsia, J., Goldstein, A.L., Simon, O.L., Sztein, M., Hayden, K.G., Peripheral blood mononuclear cell interleukin-2 and interferon-gamma production, cytotoxicity, and antigen-stimulated blastogenesis during experimental rhinovirus infection (1990) J. Infect. Dis., 162, pp. 591-597; Wimalasundera, S.S., Katz, D.R., Chain, B.M., Characterization of the T cell response to human rhinovirus in children: Implications for understanding the immunopathology of the common cold (1997) J. Infect. Dis., 176, pp. 755-759; Keatings, V.M., Barnes, P.G., Granulocyte activation markers in induced sputum: Comparison between chronic obstructive pulmonary disease, asthma and normal subjects (1996) Am. J. Respir. Crit. Care Med., 155, pp. 449-453; Pizzichini, M.M.M., Pizzichini, E., Efthimiadis, A., Berman, L., Parameswaran, K., Gleich, G.J., Jorgenson, R., Hargreave, F.E., Sputum eosinophil and neutrophil proteins in smokers with severe airflow limitation (1997) Eur. Respir. J., 10, pp. 183s; Sur, S., Glitz, D.G., Kita, H., Kujawa, S.M., Peterson, E.A., Weiler, D.A., Kephart, G.M., Leiferman, K.M., Localization of eosinophils-derived neurotoxin and eosinophil cationic protein in neutrophilic leukocytes (1998) J. Leukoc. Biol., 63, pp. 715-722; Folkerts, G., Busse, W.W., Nijkamp, F.P., Sorkness, R., Gern, J.E., Virus-induced airway hyperresponsiveness and asthma (1998) Am. J. Respir. Crit. Care Med., 157, pp. 1708-1720; Ackerlund, A., Greiff, L., Andersson, M., Bende, M., Alkner, U., Persson, C.G.A., Mucosal exudation of fibrinogen in coronavirus-induced common colds (1993) Acta. Otolaringol. (Stockh.), 113, pp. 642-648; Pizzichini, E., Pizzichini, M.M.M., Gibson, P., Berman, L., Parameswaran, K., Gleich, G.J., Dolovich, J., Hargreave, F.E., Sputum eosinophilia predicts benefit from prednisone in smokers with chronic obstructive bronchitis (1998) Am. J. Respir. Crit. Care Med., , In press; Doull, I.J.M., Lampe, F.C., Smith, S., Schreiber, J., Freezer, N.J., Holgate, S.T., Effect of inhaled corticosteroid on episodes of wheezing associated with viral infection in school age children: Randomized double blind placebo controlled trial (1997) B.M.J., 315, pp. 858-866","Hargreave, F.E.; Firestone Reg. Chest/Allergy Unit, St. Joseph's Hospital, 50 Charlton Avenue East, Hamilton, Ont. L8N 4A6, Canada",,"American Lung Association",1073449X,,AJCME,"9769279","English","Am. J. Respir. Crit. Care Med.",Article,"Final",,Scopus,2-s2.0-0031768355
"Sanchez A., Trappier S.G., Ströher U., Nichol S.T., Bowen M.D., Feldmann H.","35499296900;6602225376;6603000295;7007051048;26643513200;7202115850;","Variation in the glycoprotein and VP35 genes of Marburg virus strains",1998,"Virology","240","1",,"138","146",,49,"10.1006/viro.1997.8902","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032484488&doi=10.1006%2fviro.1997.8902&partnerID=40&md5=7b8281471200506c4037ce0e1f823737","Special Pathogens Branch, Div. of Viral and Rickettsial Dis., Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Institute of Virology, Philipps University, Marburg, Germany","Sanchez, A., Special Pathogens Branch, Div. of Viral and Rickettsial Dis., Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Trappier, S.G., Special Pathogens Branch, Div. of Viral and Rickettsial Dis., Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Ströher, U., Institute of Virology, Philipps University, Marburg, Germany; Nichol, S.T., Special Pathogens Branch, Div. of Viral and Rickettsial Dis., Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Bowen, M.D., Special Pathogens Branch, Div. of Viral and Rickettsial Dis., Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Feldmann, H., Institute of Virology, Philipps University, Marburg, Germany","Marburg virus, the prototype of the family Filoviridae, differs genetically, serologically, and morphologically from Ebola viruses. To better define the genetic variation within the species, VP35 and glycoprotein (GP) genes of representative human isolates from four known episodes of Marburg virus hemorrhagic fever were analyzed. The percentage nucleotide differences in the GP gene coding regions of Marburg viruses (0.1-21%) was nearly equal to the percentage amino acid changes (0-23%), while the percentage nucleotide differences in VP35 coding regions (0.3-20.9%) were higher than the percentage amino acid changes (0.9-6.1%), indicating a greater number of nonsynonymous changes occurring in the GP gene. The higher variation in the GP gene and the corresponding protein, especially those changes in the variable middle region of the GP, suggests that the variability may be the result of responses to natural host pressures. Analysis of the GP gene open reading frame shows a nonrandom distribution of nonsynonymous mutations that may indicate positive Darwinian selection is operating within the variable region. A heptad repeat region and an adjoining predicted fusion peptide are found in the C-terminal third of Marburg virus GPs, as has been previously shown for Ebola virus, and are similar to those found in transmembrane glycoproteins of retroviruses, paramyxoviruses, coronaviruses, and influenza viruses. Comparative analyses showed that there are two lineages within the Marburg virus species of filoviruses. The most recent isolate from Kenya (1987) represents a separate genetic lineage within the Marburg virus species (21-23% amino acid difference). However, this lineage likely does not represent a separate Marburg subtype, as the extent of divergence is less than that separating Ebola virus subtypes.",,"gene product; hybrid protein; virus glycoprotein; amino acid sequence; article; Coronavirus; Ebola virus; Filoviridae; genetic variability; Influenza virus; Marburg virus; nonhuman; nucleotide sequence; open reading frame; Paramyxovirus; priority journal; Retrovirus; virus hemorrhagic fever; Coronavirus; Darwinia; Ebola virus; Filoviridae; Influenza virus; Lake Victoria marburgvirus; Paramyxoviridae; RNA viruses; unidentified retrovirus","Bukreyev, A.A., Volchkov, V.E., Blinov, V.M., Dryga, S.A., Netesov, S.V., The complete nucleotide sequence of the Popp (1967) strain of Marburg virus: A comparison with the Musoke (1980) strain (1995) Arch. Virol., 140, pp. 1589-1600; (1993) Biosafety in Microbiological and Biomedical Laboratories, , Centers for Disease Control and Prevention and National Institutes of Health U. S. Department of Health and Human Services; Chambers, P., Pringle, C.R., Easton, A.J., Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins (1990) J. Gen. Virol., 71, pp. 3075-3080; Chan, D.C., Fass, D., Berger, J.M., Kim, P.S., Core structure of gp41 from the HIV envelope glycoprotein (1997) Cell, 89, pp. 263-273; Endo, T., Ikeo, K., Gojobori, T., Large-scale search for genes on which positive selection may operate (1996) Mol. Biol. Evol., 13, pp. 685-690; Feldmann, H., Will, C., Schikore, M., Slenczka, W., Klenk, H.-D., Glycosylation and oligomerization of the spike protein of Marburg virus (1991) Virology, 182, pp. 353-356; Feldmann, H., Mühlberger, E., Randolf, A., Will, C., Kiley, M.P., Sanchez, A., Klenk, H.-D., Marburg virus, a filovirus: Messenger RNAs, gene order, and regulatory elements of the replication cycle (1992) Virus Res., 24, pp. 1-19; Feldmann, H., Nichol, S.T., Klenk, H.-D., Peters, C.J., Sanchez, A., Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein (1994) Virology, 199, pp. 469-473; Feldmann, H., Klenk, H.-D., Marburg and Ebola viruses (1996) Adv. Virus Res., 47, pp. 1-52; Felsenstein, J., (1993) PHYLIP: Phylogeny Inference Package, , University of Washington, Seattle, WA; Fitch, W.M., Leiter, J.M.E.J.M., Li, X., Palese, P., Positive Darwinian evolution in human influenza A viruses (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 4270-4274; Gallaher, W.R., Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses (1996) Cell, 85, pp. 477-478; Gear, J.S.S., Cassel, G.A., Gear, A.J., Trappler, B., Clausen, L., Meyers, A.M., Kew, M.C., Gear, J.H.S., Outbreak of Marburg virus disease in Johannesburg (1975) Br. Med. J., 4, pp. 489-493; Geisbert, T.W., Jahrling, P.B., Differentiation of filoviruses by electron microscopy (1996) Virus Res., 39, pp. 129-150; Georges-Courbot, M.-C., Sanchez, A., Lu, C.-Y., Baize, S., Leroy, E., Lansout-Soukate, J., T'Nissan Georges, A.J., Ksiazek, T.G., Isolation and phylogenetic characterization of Ebola viruses causing different outbreaks in Gabon (1997) Emerg. Inf. Dis., 3, pp. 59-62; Jarhling, P.B., Kiley, M.P., Klenk, H.-D., Peters, C.J., Sanchez, A., Swanepoel, R., Family Filoviridae (1995) Arch. Virol., 10, pp. 289-292; Johnson, E.D., Kohnson, B.K., Silverstein, D., Tukei, P., Geisbert, T.W., Sanchez, A., Jahrling, P.B., Characterization of a new Marburg virus isolated from a 1987 fatal case in Kenya (1997) Arch. Virol., 11, pp. 101-114; Kiley, M.P., Cox, N.J., Elliott, L.H., Sanchez, A., Defries, R., Buchmeier, M.J., Richman, D.D., McCormick, J.B., Physicochemical properties of Marburg virus: Evidence for three distinct virus strains and their relationship to Ebola virus (1988) J. Gen. Virol., 69, pp. 1957-1967; Ksiazek, T.G., Rollin, P.E., Jahrling, P.B., Johnson, E., Dalgard, D.W., Peters, C.J., Enzyme immunosorbent assay for Ebola virus antigens in tissues of infected primates (1992) J. Clin. Microbiol., 30, pp. 947-950; Lambert, D.M., Barney, S., Lambert, A.L., Guthrie, K., Medinas, R., Davis, D.E., Bucy, T., Petteway S.R., Jr., Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 2186-2191; Peters, C.J., Johnson, E.D., Jahrling, P.B., Ksiazek, T.G., Rollin, P.E., White, J., Hall, W., Jaax, N., Filoviruses (1993) Emerging Viruses, pp. 159-175. , S. Morse. New York: Oxford Univ. Press; Peters, C.J., Sanchez, A., Rollin, P.E., Ksiazek, T.G., Murphy, F.A., Filoviridae: Marburg and Ebola viruses (1996) In, Fields Virology, 1, p. 1161. , B. N. FieldsD. M. KnipeP. M. Howleyet al, 1176, Lippincott-Raven Press, Philadelphia; Sanchez, A., Kiley, M.P., Identification and analysis of Ebola virus messenger RNA (1987) Virology, 157, pp. 414-420; Sanchez, A., Kiley, M.P., Holloway, B.P., McCormick, J.B., Auperin, D.D., The nucleoprotein gene of Ebola virus: Cloning, sequencing and in vitro expression (1989) Virology, 170, pp. 81-91; Sanchez, A., Kiley, M.P., Holloway, B.P., Auperin, D.D., Sequence analysis of the Ebola virus genome: Organization, genetic elements, and comparison with the genome of Marburg virus (1993) Virus Res., 29, pp. 215-240; Sanchez, A., Trappier, S.G., Mahy, B.W.J., Peters, C.J., Nichol, S.T., The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 3602-3607; Siegert, R., Shu, H.-L., Slenczka, W., Peters, D., Müller, G., Zur Äthiologie einer unbekannten von Affen ausgegangenen Infektionskrankheit (1967) Dtsch. Med. Wochenschr., 92, pp. 2341-2343; Smith, D.H., Johnson, B.K., Isaäcson, M., Swanapoel, R., Johnson, K.M., Bagshawe, A., Siongok, T., Keruga, W.K., Marburg-virus disease in Kenya (1982) Lancet, 1, pp. 816-820; Volchkov, V.E., Blinov, V.M., Netesov, S.V., The envelope glycoprotein of Ebola virus contains an immunosuppressive-like domain similar to oncogenic retroviruses (1992) FEBS Lett., 305, pp. 181-184; Volchkov, V.E., Becker, S., Volchkova, V.A., Ternovoj, V.A., Kotov, A.N., Netesov, S.V., Klenk, H.-D., GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases (1995) Virology, 214, pp. 421-430; Volchkov, V.E., Volchkova, V., Eckel, C., Klenk, H.-D., Bouloy, M., Leguenno, B., Feldmann, H., Emergence of subtype Zaire Ebola virus in Gabon (1997) Virology, 232, pp. 139-144; Will, C., Mühlberger, E., Linder, D., Slenczka, W., Klenk, H.-D., Feldmann, H., Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein (1993) J. Virol., 67, pp. 1203-1210; Yamaguchi, Y., Gojobori, T., Evolutionary mechanisms and population dynamics of the third variable envelope region of HIV within single hosts (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 1264-1269","Sanchez, A.; Building 15, Mail Stop G14, 1600 Clifton Road, Atlanta, GA 30333, United States; email: ans1@cdc.gov",,"Academic Press Inc.",00426822,,VIRLA,"9448698","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032484488
"Herold J., Gorbalenya A.E., Thiel V., Schelle B., Siddell S.G.","7006838690;7005626044;35238592100;6602866326;7005260816;","Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate",1998,"Journal of Virology","72","2",,"910","918",,49,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031907557&partnerID=40&md5=62bd9c9cb95eb7e273ee2f0eff520050","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; M. P. Chumakov Inst. P., Russian Academy of Medical Sciences, 142782 Moscow Region, Russian Federation; Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Institute of Virology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","Herold, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Gorbalenya, A.E., M. P. Chumakov Inst. P., Russian Academy of Medical Sciences, 142782 Moscow Region, Russian Federation, Department of Virology, Institute of Medical Microbiology, Leiden University, 2300 AH Leiden, Netherlands; Thiel, V., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Schelle, B., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Expression of the coronavirus gene 1-encoded polyproteins, pp1a and pp1ab, is linked to a series of proteolytic events involving virus-encoded proteinases. In this study, we used transfection and immunoprecipitation assays to show that the human coronavirus 229E-encoded papain-like cysteine proteinase, PCP1, is responsible for the release of an amino-terminal protein, p9, from the gene 1-encoded polyproteins. The same protein, p9, has also been identified in virus-infected cells. Furthermore, using an in vitro trans-cleavage assay, we defined the proteolytic cleavage site at the carboxyl terminus of p9 as pp1a-pp1ab amino acids Gly-111 and Asn-112. These results and a comparative sequence analysis suggest that substrate positions P1 and P5 seem to be the major determinants of the PCP1 cleavage site and that the latter can occupy a variable position at the amino terminus of the coronavirus pp1a and pp1ab polyproteins. By combining the trans-cleavage assay with deletion mutagenesis, we were also able to locate the boundaries of the active PCP1 domain between pp1a-pp1ab amino acids Gly-861-Glu-975 and Asn-1209-Gln-1285. Finally, codon mutagenesis was used to show that Cys-1054 and His-1205 are essential for PCP1 proteolytic activity, suggesting that these amino acids most likely have a catalytic function.",,"proteinase; amino terminal sequence; article; coronavirus; human; human cell; nonhuman; priority journal; protein degradation; protein processing; virus gene; Amino Acid Sequence; Coronavirus; Coronavirus 229E, Human; Genes, Viral; Hela Cells; Humans; Molecular Sequence Data; Papain; Proteins; Substrate Specificity; Viral Proteins","Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Pinon, J.D., Weiss, S.R., Characterization or the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. Virol., 71, pp. 900-909; Boursnell, M.E., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-67; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine-proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Gorbalenya, A.E., Unpublished data; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Süss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Henikoff, S., Henikoff, J.G., Amino acid substitution matrices from protein blocks (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 10915-10919; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275, pp. 68-69; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Heusipp, G., Grötzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and suhcellular localization of a 41 kDa, polyprotein lab processing product in human coronavirus 229E-infectcd cells J. Gen. Virol., , in press; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded by gene 1 of the human coronavirus 229E (1997) J. Virol., 71, pp. 5631-5634; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Johnston, S., Holgate, S., Epidemiology of viral respiratory tract infections (1996) Viral and Other Infections of the Human Respiratory Tract, pp. 1-38. , S. Myint and D. Taylor (ed.), Chapman & Hall, Ltd., London, United Kingdom; Karlin, S., Altschul, S.F., Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 2264-2268; Kräusslich, H.-G., Wimmer, E., Viral proteinases (1988) Annu. Rev. 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Siddell (ed.), Plenum Press, New York, N.Y; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Schuler, G.D., Altschul, S.F., Lipman, D.J., A workbench for multiple alignment construction and analysis (1991) Proteins, 9, pp. 180-190; Siddell, S.G., The coronaviridae - An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Sutter, G., Ohlmann, M., Erfle, V., Nonreplicating vaccinia vector efficiently expresses bacteriophage-T7 RNA-polymerase (1995) FEBS Lett., 371, pp. 9-12; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J. Med. Virol., 44, pp. 152-161; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Herold, J.; Institute of Virology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; email: viro008@mail.uni-wuerzburg.de",,,0022538X,,JOVIA,"9444982","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031907557
"Hingley S.T., Leparc-Goffart I., Weiss S.R.","6701491322;57213052499;57203567044;","The spike protein of murine coronavirus mouse hepatitis virus strain A59 is not cleaved in primary glial cells and primary hepatocytes",1998,"Journal of Virology","72","2",,"1606","1609",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031931227&partnerID=40&md5=d824a240e5926f1f1deebc842dff8b06","Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA, United States; Department of Microbiology, Universtiy of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States","Hingley, S.T., Dept. of Microbiology and Immunology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA, United States; Leparc-Goffart, I., Department of Microbiology, Universtiy of Pennsylvania, School of Medicine, Philadelphia, PA, United States, Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Weiss, S.R., Department of Microbiology, Universtiy of Pennsylvania, School of Medicine, Philadelphia, PA, United States, Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Mouse hepatitis virus strain A59 (MHV-A59) produces meningoencephalitis and severe hepatitis during acute infection. Infection of primary cells derived from the central nervous system (CNS) and liver was examined to analyze the interaction of virus with individual cell types derived from the two principal sites of viral replication in vivo. In glial cell cultures derived from C57BL/6 mice, MHV-A59 produces a productive but nonlytic infection, with no evidence of cell-to-cell fusion. In contrast, in continuously cultured cells, this virus produces a lytic infection with extensive formation of syncytia. The observation of few and delayed syncytia following MHV-A59 infection of hepatocytes more closely resembles infection of glial cells than that of continuously cultured cell lines. For MHV-A59, lack of syncytium formation correlates with lack of cleavage of the fusion glycoprotein, or spike (S) protein. The absence of cell-to-cell fusion following infection of both primary cell types prompted us to examine the cleavage of the spike protein. Cleavage of S protein was below the level of detection by Western blot analysis in MHV-A59-infected hepatocytes and glial cells. Furthermore, no cleavage of this protein was detected in liver homogenates from C57BL/6 mice infected with MHV-A59. Thus, cleavage of the spike protein does not seem to be essential for entry and spread of the virus in vivo, as well as for replication in vitro.",,"spike protein; unclassified drug; virus protein; animal cell; article; controlled study; glia cell; liver cell; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein degradation; syncytium; virus cell interaction; Animals; Liver; Membrane Glycoproteins; Mice; Murine hepatitis virus; Neuroglia; Viral Envelope Proteins; Virus Replication","Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell to cell fusion (1996) Virology, 214, pp. 453-463; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gombold, J.L., Weiss, S.R., Mouse hepatitis virus A59 increases steady state levels of MHC mRNAs in primary glial cell cultures and in the murine central nervous system (1992) Microb. Pathog., 13, pp. 493-505; Gotoh, B., Ohnishi, Y., Inocencio, N.M., Esaki, E., Nakayama, K., Barr, P.J., Thomas, G., Nagai, Y., Mammalian subtilisin-related proteinases in cleavage activation of the paramyxovirus fusion glycoprotein: Superiority of furin/PACE to PC2 or PC1/PC3 (1992) J. Virol., 66, pp. 6391-6397; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., Hepatitis mutants of mouse hepatitis virus strain A59 (1995) Adv. Exp. Med. Biol., 380, pp. 577-582; Joseph, J., Kim, R., Siebert, K., Lublin, F.D., Offenbach, C., Knobler, R.L., Organ specific endothelial cell heterogeneity influences differential replication and cytopathogenicity of MHV-3 and MHV-4 (1995) Adv. Exp. Med. Biol., 380, pp. 43-50; Kreamer, B.L., Staecker, J.L., Sawada, G.L., Sattler, G.L., Hsia, M.T.S., Pitot, H.C., Use of low speed, iso-density percoll centrifugation method to increase the viability of isolated rat hepatocyte preparations (1986) In Vitro Cell. Dev. Biol., 22, pp. 201-211; Lavi, E., Fishman, P.S., Highkin, M.K., Weiss, S.R., Limbic encephalitis after inhalation of a murine coronavirus (1988) Lab. Invest., 58, pp. 31-36; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M.C., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by rihonucleic acid-ribonucleic acid recombination (1990) Lab. Invest., 62, pp. 570-578; Lavi, E., Suzumura, A., Hirayama, M., Highkin, M.K., Dambach, D.M., Silberberg, D.H., Weiss, S.R., Coronavirus mouse hepatitis virus (MHV)-A59 causes a persistent, productive infection in primary glial cell cultures (1987) Microb. Pathog., 3, pp. 79-86; Luytjes, W., Sturman, L., Bredenbeck, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Martin, J.P., Chen, W., Koehren, F., Pereira, C.A., The virulence of mouse hepatitis virus 3, as evidenced by permissivity of cultured hepatic cells toward escape mutants (1994) Res. Virol., 145, pp. 297-302; Martin, J.P., Chen, W., Obert, G., Koehren, F., Characterization of attenuated mutants of MHV3: Importance of the E2 protein in organ tropism and infection of isolated liver cells (1990) Adv. Exp. Med. Biol., 276, pp. 403-410; Ohnishi, Y., Shioda, T., Nakayama, K., Iwata, S., Gotoh, B., Hamaguchi, M., Nagai, Y., A furin-defective cell line is able to process correctly the gp160 of human immunodeficiency virus type I (1994) J. Virol., 68, pp. 4075-4079; Schmidt, I., Skinner, M., Siddell, S., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Seglin, P.O., Preparation of isolated rat liver cells (1976) Methods Cell Biol., 13, pp. 29-83; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronaviruses. Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stauber, R., Pfleiderer, M., Siddell, S.G., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for infectivity (1993) J. Gen. Virol., 74, pp. 183-191; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania School of Med., 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"9445064","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031931227
"Mäkelä M.J., Puhakka T., Ruuskanen O., Leinonen M., Saikku P., Kimpimäki M., Blomqvist S., Hyypiä T., Arstila P.","35275175200;6701748112;55068112200;21534996000;7005686722;7801544108;7004588653;7005868381;6603884228;","Viruses and bacteria in the etiology of the common cold",1998,"Journal of Clinical Microbiology","36","2",,"539","542",,469,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2642614524&partnerID=40&md5=972bda20e0182b20355863c4c6b42df9","Department of Pediatrics, University of Turku, Turku, Finland; Dept. Pulmon. Dis. Clin. Allergol., University of Turku, Turku, Finland; National Public Health Institute, Oulu, Finland; Department of Virology, National Public Health Institute, Helsinki, Finland; Department of Virology, University of Turku, Turku, Finland; Department of Pediatrics, University of Turku, Kiinamyllynkatu 4-8, 20520 Turku, Finland; Department of Virology, Haartman Institute, University of Helsinki, FIN-00014, Finland","Mäkelä, M.J., Department of Pediatrics, University of Turku, Turku, Finland, Dept. Pulmon. Dis. Clin. Allergol., University of Turku, Turku, Finland, Department of Pediatrics, University of Turku, Kiinamyllynkatu 4-8, 20520 Turku, Finland; Puhakka, T., Department of Pediatrics, University of Turku, Turku, Finland; Ruuskanen, O., Department of Pediatrics, University of Turku, Turku, Finland; Leinonen, M., National Public Health Institute, Oulu, Finland; Saikku, P., National Public Health Institute, Oulu, Finland; Kimpimäki, M., Department of Virology, National Public Health Institute, Helsinki, Finland; Blomqvist, S., Department of Virology, National Public Health Institute, Helsinki, Finland; Hyypiä, T., Department of Virology, University of Turku, Turku, Finland, Department of Virology, Haartman Institute, University of Helsinki, FIN-00014, Finland; Arstila, P., Department of Virology, University of Turku, Turku, Finland","Two hundred young adults with common colds were studied during a 10- month period. Virus culture, antigen detection, PCR, and serology with paired samples were used to identify the infection. Viral etiology was established for 138 of the 200 patients (69%). Rhinoviruses were detected in 105 patients, coronavirus OC43 or 229E infection was detected in 17, influenza A or B virus was detected in 12, and single infections with parainfluenza virus, respiratory syncytial virus, adenovirus, and enterovirus were found in 14 patients. Evidence for bacterial infection was found in seven patients. Four patients had a rise in antibodies against Chlamydia pneumoniae, one had a rise in antibodies against Haemophilus influenzae, one had a rise in antibodies against Streptococcus pneumoniae, and one had immnnoglobulin M antibodies against Mycoplasma pneumoniae. The results show that although approximately 50% of episodes of the common cold were caused by rhinoviruses, the etiology can vary depending on the epidemiological situation with regard to circulating viruses. Bacterial infections were rare, supporting the concept that the common cold is almost exclusively a viral disease.",,"article; bacterium identification; bacterium isolation; Chlamydophila pneumoniae; common cold; controlled study; human; Influenza virus A; Influenza virus B; major clinical study; Mycoplasma pneumoniae; nonhuman; priority journal; Streptococcus pneumoniae; virus characterization; virus isolation; Adenovirus Infections, Human; Adult; Antibodies, Bacterial; Antibodies, Viral; Antigens, Viral; Bacterial Infections; Chlamydia Infections; Common Cold; Coronaviridae Infections; Enterovirus Infections; Female; Haemophilus Infections; Humans; Influenza, Human; Male; Mycoplasma Infections; Picornaviridae Infections; Pneumococcal Infections; Polymerase Chain Reaction; Respiratory Syncytial Virus Infections; Respirovirus Infections; Rhinovirus; RNA, Viral; Seroepidemiologic Studies; Virus Diseases; Adenoviridae; Bacteria (microorganisms); Chlamydia; Chlamydophila pneumoniae; Coronavirus; Enterovirus; Haemophilus influenzae; Influenza virus; Influenzavirus A; Influenzavirus B; Mycoplasma pneumoniae; Negibacteria; Posibacteria; Respiratory syncytial virus; Rhinovirus; RNA viruses; Streptococcus pneumoniae; Syncytial virus","Al-Nakib, W., Tyrrell, D.A.J., Picornaviridae: Rhinoviruses - Common cold viruses (1988) Laboratory Diagnosis of Infectious Diseases. Principle and Practice, pp. 723-742. , E. H. Lennette, P. Halonen, and F. A. Murphy (ed.), Springer-Verlag, New York, N.Y; Arason, V.A., Kristinsson, K.G., Sigurdsson, J.A., Stefansdottir, G., Molstad, S., Gudmundsson, S., Do antimicrobials increase the carriage rate of penicillin resistant pneumococci in children? Cross sectional prevalence study (1996) Br. Med. J., 313, pp. 387-391; Arola, A., Santti, J., Halonen, P., Ruuskanen, O., Hyypiä, T., Identification of enteroviruses in clinical specimens by competitive PCR followed by genetic typing using sequence analysis (1996) J. Clin. Microbiol., 34, pp. 313-318; Arruda, E., Pitkäranta, A., Witek Jr., T.J., Doyle, C.A., Hayden, F.G., Frequency and natural history of rhinovirus infections in adults during autumn (1997) J. Clin. Microbiol., 35, pp. 2864-2868; Arstila, P.P., Halonen, P.E., Direct antigen detection (1988) Laboratory Diagnosis of Infectious Diseases. Principle and Practice, pp. 60-75. , E. H. Lennette, P. Halonen, and F. A. Murphy (ed.), Springer-Verlag, New York, N.Y; Burman, L.A., Leinonen, M., Trollfors, B., Use of serology to diagnose pneumonia caused by nonencapsulated Haemophilus influenzae and Moraxella catarrhalis (1994) J. Infect. Dis., 170, pp. 220-222; Ekman, M.R., Leinonen, M., Syrjala, H., Linnanmaki, E., Kujala, P., Saikku, P., Evaluation of serological methods in the diagnosis of Chlamydia pneumoniae pneumonia during an epidemic in Finland (1993) Eur. J. Clin. Microbiol. Infect. Dis., 12, pp. 756-760; Englund, J.A., Piedra, P.A., Jewell, A., Patel, K., Baxter, B.B., Whimbey, E., Rapid diagnosis of respiratory syncytial virus infections in immunocompromised adults (1996) J. Clin. Microbiol., 34, pp. 1649-1653; Gwaltney Jr., J.M., Phillips, C.D., Miller, R.D., Riker, D.K., Computed tomographic study of the common cold (1994) N. Engl. J. Med., 330, pp. 25-30; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypia, T., Hurskainen, P., Pallansch, M., Detection of enteroviruses and rhinoviruses in clinical specimens by PCR and liquid-phase hybridization (1995) J. Clin. Microbiol., 33, pp. 648-653; Herzog, C., Berger, R., Fernex, M., Friesecke, K., Havas, L., Just, M., Dubach, U.C., Intranasal interferon (rIFN-alpha A, Ro 22-8181) for contact prophylaxis against common cold: A randomized, double-blind and placebo-controlled field study (1986) Antivir. Res., 6, pp. 171-176; Hietala, J., Uhari, M., Tuokko, H., Antigen detection in the diagnosis of viral infections (1988) Scand. J. Infect. Dis., 20, pp. 545-599; Hovi, T., Kainulainen, H., Ziola, B., Salmi, A., OC43 strain-related coronavirus antibodies in different age groups (1979) J. Med. Virol., 3, pp. 313-320; Huovinen, P., Lahtonen, R., Ziegler, T., Meurman, O., Hakkarainen, K., Miettinen, A., Arstila, P., Saikku, P., Pharyngitis in adults: The presence and coexistence of viruses and bacterial organisms (1989) Ann. Intern. Med., 110, pp. 612-616; Hyypia, T., Auvinen, P., Maaronen, M., Polymerase chain reaction for human picornaviruses (1989) J. Gen. Virol., 70, pp. 3261-3268; Hyypiä, T., Puhakka, T., Ruuskanen, O., Mäkelä, M.J., Arola, A., Arstila, P., Unpublished data; Jackson, G.G., Muldoon, R.L., Viruses causing common respiratory infections in man (1973) J. Infect. Dis., 127, pp. 328-355; Jalonen, E., Paton, J.C., Koskela, M., Kerttula, Y., Leinonen, M., Measurement of antibody responses to pneumolysin - A promising method for the presumptive aetiological diagnosis of pneumococcal pneumonia (1989) J. Infect., 19, pp. 127-134; Kaiser, L., Lew, D., Hirschel, B., Auckenthaler, R., Morabia, A., Heald, A., Benedict, P., Stalder, H., Effects of antibiotic treatment in the subset of common-cold patients who have bacteria in nasopharyngeal secretions (1996) Lancet, 347, pp. 1507-1510; Koskinen, P., Vuorinen, T., Meurman, O., Influenza A and B virus IgG and IgM serology by enzyme immunoassays (1987) Epidemiol. Infect., 99, pp. 55-64; Lehtomaki, K., Rapid etiological diagnosis of pneumonia in young men (1988) Scand. J. Infect. Dis. Suppl., 54, pp. 1-56; Mainous III, A.G., Hueston, W.J., Clak, J.R., Antibiotics and upper respiratory infection: Do some folks think there is a cure for the common cold? (1996) J. Fam. Pract., 42, pp. 357-361; Monto, A.S., Studies of the community and family: Acute respiratory illness and infection (1994) Epidemiol. Rev., 16, pp. 351-373; Monto, A.S., Bryan, E.R., Ohmit, S., Rhinovirus infections in Tecumseh, Michigan: Frequency of illness and number of serotypes (1987) J. Infect. Dis., 156, pp. 43-49; Mossad, S.B., Macknin, M.L., Medendorp, S.V., Mason, P., Zinc gluconate lozenges for treating the common cold. A randomized, double-blind, placebo-controlled study (1996) Ann. Intern. Med., 125, pp. 81-88; Popow Kraupp, T., Kern, G., Binder, C., Tuma, W., Kundi, M., Kunz, C., Detection of respiratory syncytial virus in nasopharyngeal secretions by enzyme-linked immunosorbent assay, indirect immunofluorescence, and virus isolation: A comparative study (1986) J. Med. Virol., 19, pp. 123-134; Putto, A., Ruuskanen, O., Meurman, O., Fever in respiratory virus infections (1986) Am. J. Dis. Child., 140, pp. 1159-1163; Ruuskanen, O., Nohynek, H., Ziegler, T., Capeding, R., Rikalainen, H., Huovinen, P., Leinonen, M., Pneumonia in childhood: Etiology and response to antimicrobial therapy (1992) Eur. J. Clin. Microbiol. Infect. Dis., 11, pp. 217-223; Saikku, P., Ruutu, P., Leinonen, M., Panelius, J., Tupasi, T.E., Grayston, J.T., Acute lower-respiratory-tract infection associated with chlamydial TWAR antibody in Filipino children (1988) J. Infect. Dis., 158, pp. 1095-1097; Van Buchem, F.L., Knottnerus, J.A., Schrijnemaekers, V.J.J., Peeters, F.M., Primary-care-based randomised placebo-controlled trial of antibiotic treatment in acute maxillary sinusitis (1997) Lancet, 349, pp. 683-687","Makela, M.J.; Department of Pediatrics, University of Turku, Kiinamyllynkatu 4-8, 20520 Turku, Finland; email: mika.makela@utu.fi",,,00951137,,JCMID,"9466772","English","J. Clin. Microbiol.",Article,"Final",,Scopus,2-s2.0-2642614524
"Godfraind C.","56877631600;","Morphological analysis of mouse hepatitis virus A59-induced pathology with regard to viral receptor expression",1998,"Histology and Histopathology","13","1",,"181","199",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031963264&partnerID=40&md5=19bd99898dfd1b89e977007b5adca9ac","Laboratory of Pathology, St Luc Hospital, UCL, Av. Hippocrate 10, B-1200 Bruxelles, Belgium","Godfraind, C., Laboratory of Pathology, St Luc Hospital, UCL, Av. Hippocrate 10, B-1200 Bruxelles, Belgium","Mouse hepatitis virus, strain A59 (MHV-A59), is a coronavirus that triggers in susceptible mice a wide variety of pathologies, including hepatitis, thymus involution, B lymphocyte polyclonal activation and, after intra-cerebral inoculation, transient demyelination. One receptor that mediates entry of the virus into target cells has been identified: it is a glycoprotein of the carcinoembryonic antigen family, called Bgp1a. The availability of antibodies recognizing this molecule permits the analysis of its cellular expression and of the relationship between receptor expression and pathology induced by the virus. Bgp1a is found on epithelial and endothelial cells as well as on B lymphocytes and macrophages. In the liver, Bgp1a expression correlates well with infection of hepatocytes and endothelial cells, leading to the development of hepatitis. However, other cells expressing this molecule, such as central nervous system endothelial cells, are not infected by the virus. This observation may explain how the blood-brain barrier prevents dissemination of MHV-A59 from the general circulation into the brain. Thymic atrophy results from apoptosis of immature double-positive T lymphocytes which might be caused indirectly by infection of a small proportion of thymus epithelial cells that express Bgp1a rather than by infection of T cells that do not express the receptor. Finally, polyclonal activation of B lymphocytes, leading to increased secretion of antibodies of the IgG2a isotype, involves a cascade of events, including cytokine secretion, that may result from the interaction of MHV-A59 with B cells and macrophages that express Bgp1a. Therefore, after viral infection, cellular expression of Bgp1a may have different results: cell lysis; alteration of cellular functions that may lead to indirect death of other cell types, or resistance to infection.","Biliary glycoprotein; Carcinoembryonic antigen; Mouse hepatitis virus; Viral pathogenicity; Viral receptor","carcinoembryonic antigen; cell receptor; cytokine; glycoprotein; immunoglobulin g2a; virus receptor; animal experiment; animal model; antibody production; apoptosis; b lymphocyte activation; blood brain barrier; cytolysis; hepatitis; mouse; murine hepatitis coronavirus; nonhuman; polyclonal activation; review; thymus atrophy; virus infection; Animals; Antigens, CD; Cell Adhesion Molecules; Coronavirus Infections; Glycoproteins; Mice; Models, Biological; Murine hepatitis virus; Receptors, Virus; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Almeida, J.D., Berry, D.M., Cunningham, C.H., Hamre, D., Hofstad, M.S., Mallucci, L., McIntosh, K., Tyrrell, D.A.J., Coronaviruses (1968) Nature, 220, p. 650; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembnyonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Wimmer, E., Harber, J.J., Bibb, J.A., Gromeier, M., Lu, H.-H., Bernhardt, G., Poliovirus receptors (1994) Cellular Receptors for Animal Viruses, pp. 101-127. , Wimmer E. (ed). Cold Spring Harbor Laboratory Press. Plainview; Woyciechowska, J.L., Trapp, B.D., Patrick, D.H., Shekarchi, I.C., Leinikki, P.O., Sever, J.L., Holmes, K.V., Acute and subacute demyelination induced by mouse hepatitis virus strain A59 in C3H mice (1984) J. Exp. Pathol., 1, pp. 295-306","Godfraind, C.; Laboratory of Pathology, St Luc Hospital, UCL, Av. Hippocrate 10, B-1200 Bruxelles, Belgium",,,02133911,,HIHIE,"9476648","English","Histol. Histopathol.",Review,"Final",,Scopus,2-s2.0-0031963264
"Wessner D.R., Shick P.C., Lu J.-H., Cardellichio C.B., Gagneten S.E., Beauchemin N., Holmes K.V., Dveksler G.S.","6603847933;57188621935;55701377800;6602071538;6602898805;7005461095;7201657724;6603790777;","Mutational analysis of the virus and monoclonal antibody binding sites in MHVR, the cellular receptor of the murine coronavirus mouse hepatitis virus strain A59",1998,"Journal of Virology","72","3",,"1941","1948",,40,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031885849&partnerID=40&md5=2d672f5c1627cfeae2735954febbfeb1","Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Lab. Hepat. Res., Food Drug Admin., Bethesda, MD 20892, United States","Wessner, D.R., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Shick, P.C., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Lu, J.-H., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Lab. Hepat. Res., Food Drug Admin., Bethesda, MD 20892, United States; Cardellichio, C.B., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Gagneten, S.E., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Lab. Hepat. Res., Food Drug Admin., Bethesda, MD 20892, United States; Beauchemin, N., McGill Cancer Centre, McGill University, Montreal, Que. H3G 1Y6, Canada; Holmes, K.V., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Dveksler, G.S., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States","The primary cellular receptor for mouse hepatitis virus (MHV), a murine coronavirus, is MHVR (also referred to as Bgp1a or C-CAM), a transmembrane glycoprotein with four immunoglobulin-like domains in the murine biliary glycoprotein (Bgp) subfamily of the carcinoembryonic antigen (CEA) family. Other murine glycoproteins in the Bgp subfamily, including Bgp1b and Bgp2, also can serve as MHV receptors when transfected into MHV-resistant cells. Previous studies have shown that the 108-amino-acid N-terminal domain of MHVR is essential for virus receptor activity and is the binding site for monoclonal antibody (MAb) CC1, an antireceptor MAb that blocks MHV infection in vivo and in vitro. To further elucidate the regions of MHVR required for virus receptor activity and MAb CC1 binding, we constructed chimeras between MHVR and other members of the CEA family and tested them for MHV strain A59 (MHV-A59) receptor activity and MAb CC1 binding activity. In addition, we used site-directed mutagenesis to introduce selected amino acid changes into the N-terminal domains of MHVR and these chimeras and tested the abilities of these mutant glycoproteins to bind MAb CC1 and to function as MHV receptors. Several recombinant glycoproteins exhibited virus receptor activity but did not bind MAb CC1, indicating that the virus and MAb binding sites on the N- terminal domain of MHVR are not identical. Analysis of the recombinant glycoproteins showed that a short region of MHVR, between amino acids 34 and 52, is critical for MHV-A59 receptor activity. Additional regions of the N- terminal variable domain and the constant domains, however, greatly affected receptor activity. Thus, the molecular context in which the amino acids critical for MHV-A59 receptor activity are found profoundly influences the virus receptor activity of the glycoprotein.",,"carcinoembryonic antigen; glycoprotein; monoclonal antibody; virus receptor; amino terminal sequence; animal cell; article; binding affinity; binding site; chimera; coronavirus; gene mutation; hepatitis virus; mouse; nonhuman; priority journal; site directed mutagenesis; virus strain; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antigens, CD; Binding Sites; Carcinoembryonic Antigen; Cell Adhesion Molecules; Cell Line; Cricetinae; Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Protein Conformation; Receptors, Virus","Arnheiter, H., Baechi, T., Haller, O., Adult mouse hepatocytes in primary monolayer culture express genetic resistance to mouse hepatitis virus type 3 (1982) J. 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"Zhang X., Hinton D.R., Park S., Parra B., Liao C.-L., Lai M.M.C., Stohlman S.A.","55715175900;7202351155;55717067600;6701803000;7401957370;7401808497;35502534500;","Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis",1998,"Virology","242","1",,"170","183",,22,"10.1006/viro.1997.8993","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032029766&doi=10.1006%2fviro.1997.8993&partnerID=40&md5=90a7058a0229aa85cde2b4464d765149","Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Howard Hughes Medical Institute, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Mail Slot 511, 4301 West Markham St., Little Rock, AR 72205-7199, United States; Dept. of Microbiology and Immunology, National Defense Medical Center, Taipai, Taiwan","Zhang, X., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Mail Slot 511, 4301 West Markham St., Little Rock, AR 72205-7199, United States; Hinton, D.R., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Department of Pathology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Park, S., Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Parra, B., Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Liao, C.-L., Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Dept. of Microbiology and Immunology, National Defense Medical Center, Taipai, Taiwan; Lai, M.M.C., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Howard Hughes Medical Institute, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States; Stohlman, S.A., Department of Neurology, Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States, Dept. of Molec. Microbiol. and I., Univ. of S. California Sch. of Med., Los Angeles, CA 90033, United States","A defective-interfering (DI) RNA of mouse hepatitis virus (MHV) was developed as a vector for expressing MHV hemagglutinin/esterase (HE) protein. The virus containing an expressed HE protein (A59-DE-HE) was generated by infecting cells with MHV-A59, which does not express HE, and transfecting the in vitro-transcribed DI RNA containing the HE gene. A similar virus (A59-DE- CAT) expressing the chloramphenicol acetyltransferase (CAT) was used as a control. These viruses were inoculated intracerebrally into mice, and the role of the HE protein in viral pathogenesis was evaluated. Results showed that all mice infected with parental A59 or A59-DE-CAT succumbed to infection by 9 days postinfection (p.i.), demonstrating that inclusion of the DI did not by itself alter pathogenesis. In contrast, 60% of mice infected with A59- DE-HE survived infection. HE- or CAT-specific subgenomic mRNAs were detected in the brains at days 1 and 2 p.i. but not later, indicating that the genes in the DI vector were expressed only in the early stage of viral infection. No significant difference in virus titer or viral antigen expression in brains was observed between A59-DE-HE and A59-DE-CAT-infected mice; suggesting that virus replication in brain was not affected by the expression of HE. However, at day 3 p.i. there was a slight increase in the extent of inflammatory cell infiltration in the brains of the A59-DE-HE-infected mice. Surprisingly, virus titers in the livers of A59-DE-HE-infected mice were 3 log10 lower than that of the A59-DE-CAT-infected mice at day 6 p.i. Also, substantially less necrosis and vital antigen were detected in the livers of the A59-DE-HE-infected mice. This may account for the reduced mortality of these mice. The possible contribution of the host immune system to this difference in pathogenesis was analyzed by comparing the expression of four cytokines. Results showed that both tumor necrosis factor-α and interleukin- 6 mRNAs increased in the brains of the A59-DE-HE-infected mice at day 2 p.i., whereas interferon-γ and interleukin-1α mRNAs were similar between A59-DE- HE- and A59-DE-CAT-infected mice. These data suggest that the transient expression of HE protein enhances an early innate immune response, possibly contributing to the eventual clearance of virus from the liver. This study indicates the feasibility of the DI expression system for studying roles of viral proteins during MHV infection.",,"esterase; hemagglutinin; animal model; animal tissue; antigen expression; article; histopathology; inflammatory infiltrate; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; RNA virus infection; virus expression; virus infectivity; virus pathogenesis; virus transcription; Animalia; Coronavirus; Felis catus; Murinae; Murine hepatitis virus; RNA viruses","Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response (1996) J. Gen. 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Virol., 68, pp. 4738-4746","Zhang, X.; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 West Markham St., Little Rock, AR 72205-7199, United States",,"Academic Press Inc.",00426822,,VIRLA,"9501044","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032029766
"Schiller J.J., Kanjanahaluethai A., Baker S.C.","56354099200;6603130302;7403307881;","Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a",1998,"Virology","242","2",,"288","302",,61,"10.1006/viro.1997.9010","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032520567&doi=10.1006%2fviro.1997.9010&partnerID=40&md5=5dee72a4301a300b454aa035f278bfad","Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States","Schiller, J.J., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States; Kanjanahaluethai, A., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States; Baker, S.C., Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States","The replicase of mouse hepatitis virus strain JHM (MHV-JHM) is encoded by two overlapping open reading frames, ORF1a and ORF1b, which are translated to produce a 750-kDa precursor polyprotein. The polyprotein is proposed to be processed by viral proteinases to generate the functional replicase complex. To date, only the MHV-JHM amino-terminal proteins p28 and p72, which is processed to p65, have been identified. To further elucidate the biogenesis of the MHV-JHM replicase, we cloned and expressed five regions of ORF1a in bacteria and prepared rabbit antisera to each region. Using the immune sera to immunoprecipitate radiolabeled proteins from MHV-JHM infected cells, we determined that the MHV-JHM ORF1a is initially processed to generate p28, p72, p250, and p150. Pulse-chase analysis revealed that these intermediates are further processed to generate p65, p210, p40, p27, the MHV 3C-like proteinase, and p15. A putative replicase complex consisting of p250, p210, p40, p150, and a large protein (>300 kDa) coprecipitate from infected cells disrupted with NP-40, indicating that these proteins are closely associated even after initial proteolytic processing. Immunofluorescence studies revealed punctate labeling of ORF1a proteins in the perinuclear region of infected cells, consistent with a membrane-association of the replicase complex. Furthermore, in vitro transcription/translation studies of the MHV- JHM 3Cpro and flanking hydrophobic domains confirm that 3C protease activity is significantly enhanced in the presence of canine microsomal membranes. Overall, our results demonstrate that the MHV-JHM ORF1a polyprotein: (1) is processed into more than 10 protein intermediates and products, (2) requires membranes for efficient biogenesis, and (3) is detected in discrete membranous regions in the cytoplasm of infected cells.",,"RNA directed RNA polymerase; virus protein; article; Coronavirus; nonhuman; open reading frame; priority journal; protein analysis; protein degradation; protein processing; Coronavirus; Murine hepatitis virus; Oryctolagus cuniculus; RNA viruses","Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. 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Virol., 70, pp. 6625-6633; Van Marle, G., Luytjes, W., Van Der Most, R.G., Van Der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Wassenaar, A.L.M., Spaan, W.J.M., Gorbalenya, A.E., Snijder, E.J., Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease (1997) J. Virol., 71, pp. 9313-9322; Zhang, X., Lai, M.M., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Baker, S.C.; Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Avenue, Maywood, IL 60153, United States; email: sbaker@luc.edu",,"Academic Press Inc.",00426822,,VIRLA,"9514967","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032520567
"An S., Makino S.","55107136200;7403067550;","Characterizations of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency",1998,"Virology","243","1",,"198","207",,17,"10.1006/viro.1998.9059","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032579771&doi=10.1006%2fviro.1998.9059&partnerID=40&md5=90efc4b342979189f20a502157b2d749","Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","An, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","Seven to eight species of viral subgenomic mRNAs are produced in coronavirus-infected cells. These mRNAs are produced in different quantities, and their molar ratios remain constant during viral replication. We studied RNA elements that affect coronavirus transcription efficiency by characterizing a series of cloned coronavirus mouse hepatitis virus (MHV) defective interfering (DI) RNAs containing an inserted intergenic sequence, from which subgenomic DI RNA is transcribed in MHV-infected cells. Certain combinations of upstream and downstream flanking sequences of the intergenic sequence suppressed subgenomic DI RNA transcription, yet changing one of the flanking sequences to a different sequence eliminated transcription suppression. The suppressive effect of certain combinations of flanking sequences, but not all combinations, could be counteracted by altering the intergenic sequence. Thus, the combination of intergenic sequence and flanking sequence affected transcription efficiency. We also characterized another set of DI RNAs designed to clarify which transcription step determines the relative molar ratios of coronavirus mRNAs. Our study indicated that if subgenomic mRNAs were exclusively synthesized from negative-strand genomic RNA, then the relative molar ratios of coronavirus mRNAs were most likely determined after synthesis of the genomic-sized template RNA. If negative-strand subgenomic RNAs were templates for subgenomic mRNAs, then the relative molar ratios of coronavirus mRNAs probably were determined after synthesis of the genomic-sized template RNA used for subgenomic-sized RNA transcription but prior to the completion of the synthesis of subgenomic-sized RNAs containing the leader sequence. The relative molar ratios of coronavirus mRNAs, therefore, seem to have been established prior to a putative replicon-type amplification of subgenomic mRNAs.",,"cis acting element; messenger RNA; virus RNA; animal cell; article; Coronavirus; nonhuman; priority journal; RNA analysis; RNA synthesis; RNA transcription; transcription regulation; virus transcription; Animalia; Coronavirus; Murine hepatitis virus; RNA viruses","Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. 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Virusforch., 44, pp. 298-302; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effect of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Jeong, Y.S., Repass, J.F., Kim, Y.-N., Hwang, S.M., Makino, S., Coronavirus transcription mediated by sequences flanking the transcription consensus sequence (1996) Virology, 217, pp. 311-322; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis ofcis (1993) Virology, 197, pp. 53-63; Kim, Y.-N., Makino, S., Characterization of a murine coronavirus defective interfering RNA internalcis (1995) J. Virol., 69, pp. 4963-4971; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. 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Virol., 63, pp. 5285-5292; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139, pp. 138-151; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shieh, C.-K., Lee, H.-J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcription initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol., 63, pp. 3729-3736; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1939-1944; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.M., (1994) Subgenomic RNa Synthesis Directed by a Synthetic Defective Interfering RNa of Mouse Hepatitis Virus: a Study of Coronavirus Transcription Initiation, 68, p. 3656. , 3666; Van Marle, G., Luytjes, W., Van Der Most, R.G., Van Der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Winship, P.R., An improved method for directly sequencing PCR material using dimethyl sulfoxide (1989) Nucleic Acids Res., 17, p. 1266; Zhang, X., Liao, C.J., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Makino, S.; Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas, Austin, TX 78712-1095, United States; email: makino@mail.utexas.edu",,"Academic Press Inc.",00426822,,VIRLA,"9527929","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032579771
"Vennema H., Poland A., Foley J., Pedersen N.C.","7003697291;7006803895;7402872921;7202299909;","Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses",1998,"Virology","243","1",,"150","157",,231,"10.1006/viro.1998.9045","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032579804&doi=10.1006%2fviro.1998.9045&partnerID=40&md5=b7579c0c145f32bd364c1e07ab230d46","Center for Companion Animal Health, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States; Dept. of Medicine and Epidemiology, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States","Vennema, H., Center for Companion Animal Health, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States; Poland, A., Center for Companion Animal Health, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States; Foley, J., Center for Companion Animal Health, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States; Pedersen, N.C., Center for Companion Animal Health, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States, Dept. of Medicine and Epidemiology, School of Veterinary Medicine, University of California at Davis, Davis, CA 95616, United States","Feline infectious peritonitis virus (FIPV) strains from six cats and three different geographic areas were compared genetically with feline enteric coronavirus (FECV) isolates obtained from cats inhabiting the same environments. Sequence comparisons were made from 1.2- to 8.9-kb segments on the 3' end of the genome. FECV/FIPV pairs from the same catteries or shelters were 97.3-99.5% related but were genetically distinct from FIPV and FECV strains obtained from cats living in geographically distinct environments. The high genetic similarity between FECVs and FIPVs from the same environment strongly suggested a common ancestry. Based on the presence of deletion mutations in the FIPVs and not in the FECVs, it was concluded that FIPVs evolved as mutants of FECVs. The mutations are deletions in the FIPVs and not insertions in the FECVs since similar sequences are present in other strains that have segregated earlier from a common ancestor. Therefore, the order of descent is from FECV tO FIPV. Mutations unique to FIPVs were found in open reading frames (ORFs) 3c in 4 of 6 isolates and/or 7b in 3 of 6 isolates. When the study was extended to include 7 additional FIPV isolates, 11/13 of the FIPVs sequenced were found to have mutated 30 ORFs.",,"adolescent; article; cat; Coronavirus; evolution; gene deletion; gene mutation; genetic variability; geography; nonhuman; priority journal; sequence homology; strain difference; virogenesis; Animalia; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; Felis catus; RNA viruses","Black, J.W., Recovery and in vitro cultivation of a coronavirus from laboratory-induced cases of feline infectious peritonitis (FIP) (1980) Vet. Med. Small Anim. Clin., 75, pp. 811-814; ChoMcZynski, P., Sacchi, N., Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J.M., Sequence analysis of the 3′ end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Res., 12, pp. 387-395; Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1995) Feline Pract., 24, pp. 14-22; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) J. Am. Vet. Med. Assoc., 210, pp. 1313-1318; Herrewegh, A.A., Vennema, H., Horzinek, M.C., Rottier, P.J., De, G.R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hickman, M.A., Morris, J.G., Rogers, Q.R., Pedersen, N.C., Elimination of feline coronavirus infection from a large experimental specific pathogen-free cat breeding colony by serologic testing and isolation (1995) Feline Pract., 23, pp. 96-102; Holzworth, J., Some important disorders of cats (1963) Cornell Vet., 53, pp. 157-160; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 66, pp. 6931-6938; Jacobs, L., Van-Der-Zeijst, B.A.M., Horzinek, M.C., Characterization and translation of transmissible gastroenteritis virus mRNAs (1986) J. Virol., 57, pp. 1010-1015; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M., RNA recombination of murine coronaviruses: Recombination between fusion-positive mouse hepatitis virus A59 and fusion-negative mouse hepatitis virus 2 (1988) J. Virol., 62, pp. 1989-1998; Kusters, J.G., Jager, E.J., Niesters, H.G., Van Der Zeijst, B.A., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-20; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 37-52; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens, using feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 363-367; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD3, and FIPV-UCD4 (1985) Compend. Contin. Educ. Pract. Vet., 7, pp. 1001-1011; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34, pp. 3180-3184; Postorino-Reeves, N., Vaccination against naturally occurring FIP in a single large cat shelter (1995) Feline Pract., 23, pp. 81-82; (1994) Program Manual for the Wisconsin Package Version 8, , Genetics Computer Group, 575 Science Drive, Madison, WI; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Heijnen, L., Rottier, P.J., Horzinek, M.C., Spaan, W.J., A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal (1992) J. Virol., 66, pp. 4951-4956; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Ward, J.M., Morphogenesis of a virus in cats with experimental feline infectious peritonitis (1970) Virology, 41, pp. 191-194; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Vennema, H.; Division of Virology, I and I, PO Box 80.165, 3508 TD Utrecht, Netherlands; email: H.Vennema@vetmic.dgk.ruu.nl",,"Academic Press Inc.",00426822,,VIRLA,"9527924","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032579804
"Castilla J., Pintado B., Sola I., Sánchez-Morgado J.M., Enjuanes L.","8851950500;6701776268;7003336781;6602349176;7006565392;","Engineering passive immunity in transgenic mice secreting virusneutralizing antibodies in milk",1998,"Nature Biotechnology","16","4",,"349","354",,54,"10.1038/nbt0498-349","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031981820&doi=10.1038%2fnbt0498-349&partnerID=40&md5=d6c7ed3c62c15962ba598646648975e0","Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Dept. Anim. Repro. Zoogenetic R., Inst. Nac. de Invest. Agrarias, Carretera La Coruña km 5.9, 28040 Madrid, Spain","Castilla, J., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Pintado, B., Dept. Anim. Repro. Zoogenetic R., Inst. Nac. de Invest. Agrarias, Carretera La Coruña km 5.9, 28040 Madrid, Spain; Sola, I., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sánchez-Morgado, J.M., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Protection against enteric infections can be provided by the oral administration of pathogen-neutralizing antibodies. To provide passive immunity, 18 lines of transgenic mica secreting a recombinant mono-clonal antibody (Mab) neutralizing transmissible gastroenteritis coronavirus (TGEV) into the milk were generated. The genes encoding a chimeric Mab with the variable modules of the murine TGEV-specific Mab 6A.C3 and the constant modules of a human IgG, isotype Mab were expressed under the control of regulatory sequences derived from the whey acidic protein, which is an abundant milk protein. The Mab 6A.C3 binds to a highly conserved epitope present in coronaviruses of several species, which does not allow the selection of neutralization escape mutants. Antibody expression titers of 104 were obtained in the milk of transgenic mice that reduced TGEV infectivity 104-fold. The antibody was synthesized at high levels throughout lactation. Integration of matrix attachment region sequences with the antibody genes led to a 20- to 10,000-fold increase in the antibody titer in 50% of the transgenic animals. Antibody expression levels were transgene copy number independent and related to the site of integration. The generation of transgenic animals producing virus neutralizing antibodies in milk could provide an approach to protection against neonatal infections of the enteric tract.","Antibody engineering; Applied immunology; Coronavirus; Mucosal immunity","complementary dna; dna; immunoglobulin g; monoclonal antibody; neutralizing antibody; animal cell; animal experiment; antibody titer; article; coronavirus; gastroenteritis; gene expression; genetic engineering; immunoglobulin gene; milk level; mouse; mucosal immunity; newborn infection; nonhuman; polymerase chain reaction; priority journal; transgenic mouse; virus neutralization; Animals; Antibodies, Monoclonal; Base Sequence; DNA Primers; Female; Genetic Engineering; Humans; Immunity, Maternally-Acquired; Immunization, Passive; Immunoglobulin G; Lactation; Mice; Mice, Transgenic; Milk; Murine hepatitis virus; Neutralization Tests; Recombinant Proteins; Animalia; Coronavirus; Mica; Murinae; Mus musculus; Transmissible gastroenteritis virus","Lamm, M.E., Nedrud, J.G., Kaetzel, C.S., Mazanec, M.B., IgA and mucosal defense (1995) APMIS, 103, pp. 241-246; Liew, F.Y., Russell, S.M., Appleyard, G., Brand, C.M., Beale, J., Cross-protection in mice infected with influenza A virus by the respiratory route is correlated with local IgA antibody rather than serum antibody or cytotoxic T cell reactivity (1984) Eur. J. Immunol., 14, pp. 350-356; Staats, H.F., Jackson, R.J., Marinaro, M., Takahashi, I., Kiyono, H., McGhee, J.R., Mucosal immunity to infection with implications for vaccine development (1994) Curr. Opin. Immunol., 6, pp. 572-583; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , Leman, A.D., Straw, B.E., Mengeling, W.L., D'Allaire, S., and Taylor, D.J. (eds.). Wolfe Publishing, Ames, IA; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , Siddell, S.G. (ed.). Plenum Press, New York; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG, and IgM(A) to protect neonatal pigs against the coronavirus transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288; Castilla, J., Sola, I., Enjuanes, L., Interference of coronavirus infection by expression of immunoglobulin G (IgG) or IgA virus-neutralizing antibodies (1997) J. Virol., 71, pp. 5251-5258; Hennighausen, L., Ruíz, L., Wall, R., Transgenic animals-production of foreign proteins in milk (1990) Curr. Opin. Biotechnol., 1, pp. 74-78; Simons, J.P., McClenaghan, M., Clark, A.J., Alteration of the quality of milk by expression of sheep β-lactoblobulin in transgenic mice (1987) Nature, 328, pp. 530-532; Sola, I., Castilla, J., Pintado, B., Sánchez-Morgado, J.M., Whitelaw, B., Clark, J., Enjuanes, L., Transgenic mice secreting coronavirus neutralizing antibodies into the milk (1997) J. Virol., , In press; Antón, I.M., Suñé, C., Meloen, R.H., Borrás-Cuesta, F., Enjuanes, L., A transmissible gastroenteritis coronavirus nucleoprotein epitope elicits T helper cells that collaborate in the in vitro antibody synthesis to the three major structural viral proteins (1995) Virology, 212, pp. 746-751; Torres, J.M., Sánchez, C.M., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñié, C., Bullido, M.J., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Bonifer, C., Vidal, M., Grosveld, F., Sippel, A.E., Tissue specific and protein position independent expression of the complete gene domain for chicken lysozyme in transgenic mice (1990) EMBO J., 9, pp. 2843-2848; Jenuwein, T., Forrester, W.C., Fernández-Herrero, L.A., Laible, G., Dull, M., Grosschedl, R., Extension of chromatin accessibility by nuclear matrix attachment regions (1997) Mature, 385, pp. 269-272; Kirillov, A., Kidtler, B., Mostoslavsky, R., Cedar, H., Wirtz, T., Bergman, Y., A role for nuclear NF-kB in B-cell-specific demethylation of the Ig k locus (1996) Nat. Genet., 13, pp. 435-441; Ball, R.K., Friis, R.R., Schoenenberger, C.A., Doppler, W., Groner, B., Prolactin regulation of β-casein gene expression and of a cytosolic 120-kd protein in a cloned mouse mammary epithelial cell line (1988) EMBO J., 7, pp. 2089-2095; Shamay, A., Solinas, S., Pursel, V.G., McKnight, R.A., Alexander, L., Beattie, C., Production of the mouse whey acidic protein in transgenic pigs during lactation (1991) J. Anim. Sci., 69, pp. 4552-4562; Hogan, B., Beddington, R., Costantini, F., Lacy, E., (1994) Manipulating the Mouse Embryo, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Pittius, C.W., Hennighausen, L., Lee, E., Westphal, H., Nicols, E., Vitale, J., Gordon, K., A milk protein gene promoter directs the expression of human tissue plasminogen activator cDNA to the mammary gland in transgenic mice (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 5874-5878; Wall, R.J., Pursel, V.G., Shamay, A., McKnight, R.A., Pittius, C.W., Hennighausen, L., High-level synthesis of a heterologous milk protein in the mammary glands of transgenic swine (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 1696-1700; Velander, W.H., Johnson, J.L., Page, R.L., Russell, G.G., Subramanian, A., Wilkins, T.D., High-level expression of a heterologous protein in the milk of transgenic swine using the cDNA encoding human protein C (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 12003-12007; Phi-Van, L., Von Kries, J.P., Odtertag, W., Stratling, W.H., The chicken lysozyme 5′ matrix attachment region increases transcription from a heterologous promoter in heterologous cells and dampens position effects on the expression of transfected genes (1990) Mol. Cell. Biol., 10, pp. 2302-2307; McKnight, R.A., Shamay, A., Sankaran, L., Wall, R.J., Hennighausen, L., Matrix-attachment regions can impart position-independent regulation of a tissue-specific gene in transgenic mice (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 6943-6947; McKnight, R.A., Spencer, M., Wall, R.J., Hennighausen, L., Severe position effects imposed on a 1 Kb mouse whey acidic protein gene promoter are overcome by heterologous matrix attachment regions (1996) Mol. Reprod. Dev., 44, pp. 179-184; Poljak, L., Seum, C., Mattioni, T., Laemmli, U.K., SARs stimulate but do not confer position independent gene expression (1994) Nucl. Acids. Res., 22, pp. 4386-4394; Storb, U., Transgenic mice with immunoglobulin genes (1987) Annu. Rev. Immunol., 5, pp. 151-174; Lo, D., Pursel, V.G., Linton, P.J., Sandgren, E., Behringer, R., Rexroad, C., Expression of mouse IgA by transgenic mice, pigs, and sheep (1991) Eur. J. Immunol., 21, pp. 1001-1006; Weidle, U.H., Lenz, H., Brem, G., Genes encoding a mouse monoclonal antibody are expressed in transgenic mice, rabbits and pigs (1991) Gene, 98, pp. 185-191; Kooyman, D.L., Pinkert, C.A., Transgenic mice expressing a chimeric anti-E. coli immunoglobulin α heavy chain gene (1994) Transgenic Res., 3, pp. 167-175; Yarus, S., Rosen, J.M., Cole, A.M., Diamond, G., Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 14118-14121; Reed, W.A., Elzer, P.H., Enright, F.M., Jaynes, J.M., Morrey, J.D., White, K.L., Interleukin 2 promoter/enhancer controlled expression of a synthetic cecropin-class lytic peptide in transgenic mice and subsequent resistance to Brucella abortus (1997) Transgenic Res., 6, pp. 337-347; Limonta, J., Pedraza, A., Rodríguez, A., Freyre, F.M., Barral, A.M., Castro, F.O., Production of active anti-CD6 mouse-human chimeric antibodies in the milk of transgenic mice (1995) Immunotechnology, 1, pp. 107-113; Liu, A.Y., Mack, P.W., Champion, C.I., Robinson, R.R., Expression of mouse: Human immunoglobulin heavy chain cDNA in lymphoid cells (1987) Gene, 54, pp. 33-40; (1987) Expression of Mouse-human Immunoglobulins, , Patent WO 87/02671; Potter, H., Weir, L., Leder, P., Enhancer-dependent expression of human k immunoglobulin genes introduced into mouse pre-B lymphocytes by electroporation (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 7161-7165; Phi-Van, L., Stratling, W.H., The matrix attachment regions of the chicken lysozyme gene co-map with the boundaries of the chromatin domain (1988) EMBO J., 7, pp. 655-664; Fink, P.S., Using sodium chloride step gradients to fractionate DNA fragments (1991) Bio/Techniques, 10, pp. 447-449; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Nagasawa, H., A device for milk collection from mice (1979) Lab. Anim. Sci., 29, pp. 633-635","Enjuanes, L.; Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Consejo Superior Invest. Cientificas, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,10870156,,NABIF,"9555725","English","Nat. Biotechnol.",Article,"Final",,Scopus,2-s2.0-0031981820
"Rao P.V., Gallagher T.M.","36868545200;7202310503;","Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections",1998,"Journal of Virology","72","4",,"3278","3288",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031949315&partnerID=40&md5=f570bf6166cf48c130d201fd74bb0330","Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States; Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","Rao, P.V., Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Gallagher, T.M., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States, Dept. of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States","Murine hepatitis virus (MHV) infections exhibit remarkable variability in cytopathology, ranging from acutely cytolytic to essentially asymptomatic levels. In this report, we assess the role of the MHV receptor (MHVR) in controlling this variable virus-induced cytopathology. We developed human (HeLa) cell lines in which the MHVR was produced in a regulated fashion by placing MHVR cDNA under the control of an inducible promoter. Depending on the extent of induction, MHVR levels ranged from less than ~1,500 molecules per cell (designated R(1o)) to ~300,000 molecules per cell (designated R(hi)). Throughout this range, the otherwise MHV-resistant HeLa cells were rendered susceptible to infection. However, infection in the R(1o) cells occurred without any overt evidence of cytopathology, while the corresponding R(hi) cells died within 14 h after infection. When the HeLa-MHVR cells were infected with vaccinia virus recombinants encoding MHV spike (S) proteins, the R(hi) cells succumbed within 12 h postinfection; R(1o) cells infected in parallel were intact, as judged by trypan blue exclusion. This acute cytopathology was not due solely to syncytium formation between the cells producing S and MHVR, because fusion-blocking antiviral antibodies did not prevent it. These findings raised the possibility of an intracellular interaction between S and MHVR in the acute cell death. Indeed, we identified intracellular complexes of S and MHVR via coimmunoprecipitation of endoglycosidase H-sensitive forms of the two proteins. We suggest that MHV infections can become acutely cytopathic once these intracellular complexes rise above a critical threshold level.",,"virus receptor; article; cell death; coronavirus; cytopathogenic effect; cytopathology; hela cell; human; human cell; murine hepatitis coronavirus; priority journal; promoter region; syncytium; virus cell interaction; virus infection; Animals; Cell Death; Cell Line; Cytopathogenic Effect, Viral; Giant Cells; Glycoproteins; Golgi Apparatus; Hela Cells; Humans; Membrane Glycoproteins; Murine hepatitis virus; Organelles; Rabbits; Receptors, Virus; Viral Envelope Proteins","Ahmed, R., Morrison, L.A., Knipe, D.M., Persistence of viruses (1996) Fields Virology, Vol. 1, 3rd Ed., 1, pp. 219-249. , B. N. Fields, D. M. Knipe, and P. M. 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Virol., 68, pp. 6523-6534; Knobler, R.L., Lampert, P.W., Oldstone, M.B.A., Virus persistence and recurring demyelination produced by a temperature-sensitive mutant of MHV-4 (1982) Nature, 298, pp. 279-280; Konopka, K., Pretzer, E., Duzgunes, N., Differential effects of a hydrophobic tripeptide on human immunodeficiency virus type 1 (HIV-1)-induced syncytium formation and viral infectivity (1995) Biochem. Biophys. Res. Commun., 208, pp. 75-81; Koolen, M.J.M., Love, S., Wouda, W., Calafat, J., Horzinek, M.C., Van Der Zeijst, B.A.M., Induction of demyelination by a temperature-sensitive mutant of the coronavirus MHV-A59 is associated with restriction of viral replication in the brain (1987) J. Gen. Virol., 68, pp. 703-714; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lavi, E., Suzumura, A., Hiragama, M., Highkin, M.K., Dambach, D.M., Silberberg, D.H., Weiss, S.R., Coronavirus mouse hepatitis virus (MHV)-A59 causes persistent, productive infection in primary glial cell cultures (1987) Microb. Pathol., 3, p. 79; Majno, G., Joris, I., Apoptosis, oncosis and necrosis, an overview of cell death (1995) Am. J. Pathol., 146, pp. 3-15; Nash, T.C., Buchmeier, M.J., Spike glycoprotein-mediated fusion in biliary glycoprotein-independent cell-associated spread of mouse hepatitis virus infection (1996) Virology, 223, pp. 68-78; Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) J. 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Virol., 64, pp. 3817-3823; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Gallagher, T.M.; Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 S. First Ave., Maywood, IL 60153, United States; email: tgallag@luc.edu",,,0022538X,,JOVIA,"9525655","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031949315
"Paltrinieri S., Cammarata Parodi M., Cammarata G., Mambretti M.","7003879241;6506781296;7003671847;36966026400;","Type IV Hypersensitivity in the Pathogenesis of FIPV-Induced Lesions",1998,"Journal of Veterinary Medicine, Series B","45","3",,"151","159",,14,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032041096&partnerID=40&md5=74ed28b4b66936c8e47e448cf5244ae1","Ist. di Patol. Generale Veterinaria, Via Celona 10, 20133 Milan, Italy; Ist. di Patol. Generale Veterinaria, Milan, Italy; Ist. Anat. Patologica Vet. Patol. A., Milan, Italy","Paltrinieri, S., Ist. di Patol. Generale Veterinaria, Via Celona 10, 20133 Milan, Italy, Ist. Anat. Patologica Vet. Patol. A., Milan, Italy; Cammarata Parodi, M., Ist. di Patol. Generale Veterinaria, Milan, Italy; Cammarata, G., Ist. di Patol. Generale Veterinaria, Milan, Italy; Mambretti, M., Ist. di Patol. Generale Veterinaria, Milan, Italy","In focal lesions of feline infectious peritonitis (FIP), the cells involved in the delayed-type hypersensitivity were identified in formalin-fixed paraffin-embedded and frozen samples taken from 35 affected cats. The clinical diagnosis of FIP was confirmed by necropsy, histology and direct immunofluorescence against the coronaviruses on cryostatic sections. The immune cells were detected immunohistochemically by the Avidin-Biotin-Complex (ABC) method using either polyclonal antibodies against lymphoid antigens (CD3) or monoclonal antibodies against lymphoid (PAN-T, CD4, CD8) and myeloid antigens (MAC387). Better identification of T cells and macrophages was found on formalin-fixed paraffin-embedded sections than on cryostatic ones, while T lymphocyte subpopularions could be differentiated only in cryostatic sections. Type IV hypersensitivity was detected in focal feline infectious peritonitis virus (FIPV)-induced lesions from progressive activation of T lymphocytes, mainly CD4+, and the presence of granulocytes and macrophages. The FIPV-induced lesions could be studied as examples of granulomas caused by unconventional antigens, such as viruses or immune complexes.",,"CD3 antigen; monoclonal antibody; animal; animal disease; article; cat; cat disease; CD4+ T lymphocyte; CD8+ T lymphocyte; Coronavirus; cryopreservation; delayed hypersensitivity; fluorescent antibody technique; immunohistochemistry; immunology; pathology; tissue fixation; Animals; Antibodies, Monoclonal; Antigens, CD3; Cats; CD4-Positive T-Lymphocytes; CD8-Positive T-Lymphocytes; Coronavirus, Feline; Cryopreservation; Feline Infectious Peritonitis; Fluorescent Antibody Technique, Direct; Hypersensitivity, Delayed; Immunohistochemistry; Tissue Fixation","Barlough, J.E., Stoddardd, C.A., La peritonite infettiva del felini (1990) Vet. Reports, 1, pp. 13-17; Cammarata Parodi, M., Cammarata, G., Paltrinieri, S., Lavazza, A., Ape, F., Using direct immunofluorescence to detect coronaviruses in peritoneal and pleural effusions (1993) J. Small An. Pract., 34, pp. 609-613; Fenner, F., Coronaviridae (1987) Veterinary Virology, 2nd Edn., pp. 505-508. , F. FENNER, P. A. BACHMANN, E. P. J. GIBBS, F. A. MURPHY, M. J. STODDERT, D. O. WHITE, eds Academic Press Inc., Orlando; Gerber, J.D., Ingersoll, J.D., Gast, A.M., Christianson, K.K., Selzer, N.L., Pfeiffer, N.E., Sharpee, R.L., Beckenhauer, W.H., Protection against feline infectious peritonitis by intranasal inoculation of a temperature-sensitive FIPV vaccine (1990) Vaccine, 8, pp. 536-542; Goebeler, M., Roth, J., Teigelkamp, S., Sorg, C., Monoclonal antibody MAC387 detects an epitope on the calcium-binding protein MRP14 (1994) J. 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Pathol., 49, pp. 1194-1199; Modlin, R.L., Hofman, F.M., Horwitz, D.A., Husmann, L.A., Gillis, S., Taylor, C.R., Rea, T.H., In situ identification of cells in human leprosy granulomas with mononuclear antibodies to interleukin-2 and its receptor (1984) J. Immunol., 132, pp. 3085-3090; Momotani, E., Kubo, M., Ishikawa, Y., Yoshino, T., Immunohistochemical localisation of immunoglobulins in bovine granulomatous lesions (1989) J. Comp. Path., 100, pp. 129-136; Olsen, C.W., Corpai, W.V., Jacobson, R.H., Simkins, R.A., Saif, L.J., Scott, F.W., Identification of antigenic sites mediating antibody-dependent enhancement of feline infectious peritonitis virus infectivity (1993) J. General Virol., 74, pp. 745-749; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Pastoret, P.P., Bourtonboy, S., Le point sur la péritonite infectieuse féline (1991) Ann. Med. Vet, 135, pp. 35-41; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-537; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-20; Pedersen, N.C., Black, J.W., Attempted immunization of cats against feline infectious peritonitis using a virulent live virus or sublethal amounts of virulent virus (1983) Am. J. Vet. Res., 44, pp. 229-234; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Roitt, L., Brostoff, J., Male, D., Hypersensitivity - Type IV (1996) Immunology, 4th Edn., pp. 251-2512. , I. ROITT, J. BROSTOFF, D. MALE, eds Mosby, London; Scanziani, E., Paltrinieri, S., Ponti, W., Abdirahaman, O.M., Identificazione in situ di cellule inflammatorie nel granuloma tubercolare del bovino (1990) Atti S.I.S. Vet., 44, pp. 889-891; Weiss, R.C., Cox, N.R., Delayed-type hypersensitivity skin response associated with feline infectious peritonitis in two cats (1988) Res. Vet. Sci., 44, pp. 396-398; Weiss, R.C., Dodds, W.J., Scott, F.W., Disseminated intravascular coagulation in experimentally induced feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 663-671; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Pathologic changes and immunofluorescence (1981) Am. J. Vet. Res, 42, pp. 2036-2047","Paltrinieri, S.; Ist. di Patol. Generale Veterinaria, Via Celona 10, 20133 Milan, Italy",,,09311793,,JVMBE,"9588109","English","J. Vet. Med. Ser. B",Article,"Final",,Scopus,2-s2.0-0032041096
"Ng L.F.P., Liu D.X.","7201477950;8972667300;","Identification of a 24-kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites",1998,"Virology","243","2",,"388","395",,29,"10.1006/viro.1998.9058","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032502749&doi=10.1006%2fviro.1998.9058&partnerID=40&md5=f4297777a664b1e2f18411e38266215a","Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore, 118240, Singapore","Ng, L.F.P., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore, 118240, Singapore; Liu, D.X., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore, 118240, Singapore","We report here the identification of a 24-kDa polypeptide in IBV- infected Vero cells by immunoprecipitation with a region-specific antiserum raised in rabbits against the IBV sequence encoded between nucleotides 10928 and 11493. Coexpression, deletion, and mutagenesis studies have demonstrated that this protein is encoded by ORF 1a from nucleotide 10915 to 11544 and is released from the la polyprotein by the 3C-like proteinase-mediated proteolysis. A previously predicted Q-S (Q3462S3463) dipeptide bond encoded by the IBV sequence from nucleotide 10912 to 10917 is identified as the N-terminal cleavage site, and a Q-N (Q3672N3673) dipeptide bond encoded by the IBV sequence between nucleotides 11542 and 11547 is identified as the C-terminal cleavage site of the 24-kDa polypeptide.",,"polypeptide; proteinase; virus protein; animal cell; article; bronchitis; Coronavirus; mutagenesis; nonhuman; nucleotide sequence; peptide analysis; polymerase chain reaction; priority journal; Vaccinia virus; Vero cell; virus infection; Animalia; Avian infectious bronchitis virus; Coronavirus; Oryctolagus cuniculus; RNA viruses; Vaccinia; Vaccinia virus","Alonso-Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., Replication and morphogenesis of avian coronavirus in Vero cells and their inhibition by monensin (1984) Virus Res., 1, pp. 153-167; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. 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Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4860; Grotzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., 71, pp. 5631-5634; Heusipp, G., Grotzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78, pp. 2789-2794; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87 kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Brown, T.D.K., Characterisation and mutational analysis of an ORF-1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Schaad, M.C., Jensen, P.E., Carrington, J.C., Formation of plant RNA virus replication complexes on membranes: Role of an endoplasmic reticulum-targeted viral protein (1997) EMBO J., 16, pp. 4049-4059; Van Kuppeveld, F.J.M., Hoenderop, J.G.J., Smeets, R.L.L., Willems, P.H.G.M., Dijkman, H.B.P.M., Galama, J.M.D., Melchers, W.J.G., Coxsachievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release (1997) EMBO J., 16, pp. 3519-3553; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Liu, D.X.; Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; email: liudx@ima.org.sg",,"Academic Press Inc.",00426822,,VIRLA,"9568037","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032502749
"Paton D.J., Christiansen K.H., Alenius S., Cranwell M.P., Pritchard G.C., Drew T.W.","7103157927;7103110363;7004457776;6602579906;7101687286;7006554568;","Prevalence of antibodies to bovine virus diarrhoea virus and other viruses in bulk tank milk in England and Wales",1998,"Veterinary Record","142","15",,"385","391",,108,"10.1136/vr.142.15.385","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032507341&doi=10.1136%2fvr.142.15.385&partnerID=40&md5=494d99e662299da2c4736f8faa5d299b","Veterinary Laboratories Agency, Central Veterinary Laboratory, New Haw, Addlestone, Surrey KT15 3NB, United Kingdom; National Veterinary Institute, S-750 07, Uppsala, Sweden; Veterinary Laboratories Agency, Veterinary Investigation Centre, Starcross, Exeter, Devon EX6 8PE, United Kingdom; Veterinary Laboratories Agency, Veterinary Investigation Centre, Rougham Hill, Bury St Edmunds, Suffolk IP33 2RX, United Kingdom","Paton, D.J., Veterinary Laboratories Agency, Central Veterinary Laboratory, New Haw, Addlestone, Surrey KT15 3NB, United Kingdom; Christiansen, K.H., Veterinary Laboratories Agency, Central Veterinary Laboratory, New Haw, Addlestone, Surrey KT15 3NB, United Kingdom; Alenius, S., National Veterinary Institute, S-750 07, Uppsala, Sweden; Cranwell, M.P., Veterinary Laboratories Agency, Veterinary Investigation Centre, Starcross, Exeter, Devon EX6 8PE, United Kingdom; Pritchard, G.C., Veterinary Laboratories Agency, Veterinary Investigation Centre, Rougham Hill, Bury St Edmunds, Suffolk IP33 2RX, United Kingdom; Drew, T.W., Veterinary Laboratories Agency, Central Veterinary Laboratory, New Haw, Addlestone, Surrey KT15 3NB, United Kingdom","Bulk tank milk samples from 1070 dairy herds in England and Wales were tested by ELISA for antibodies to bovine virus diarrhoea virus (BVDV). A subset of 341 herds was tested by ELISA for antibodies to bovine herpesvirus 1 (BHV-1), bovine respiratory syncytial virus (BRSV) and bovine coronavirus (BCV). None of the herds had less than 40 dairy cows and none had been vaccinated against BVDV. The prevalence of BVDV antibody-positive herds in the national population was estimated at 95 per cent and approximately 65 per cent of the herds had a high level of bulk tank antibody suggestive of recent infection with BVDV. Dairy herds in East Anglia and the south-east of England had a significantly lower risk of being BVDV antibody-positive than herds in the rest of England and Wales. However, these regional differences tended to diminish with increasing herd size. Around 69 per cent of the herds were BHV-1 antibody-positive and all the herds were antibody positive to BRSV and BCV. Comparison with earlier serologicai surveys revealed that there had been little change in the prevalence and distribution of BVDV antibody-positive herds in England and Wales over the last 20 years, but that there had been an increase in the prevalence of BHV-1 antibody-positive herds.",,"Bovinae; Bovine coronavirus; Bovine herpesvirus 1; Bovine respiratory syncytial virus; Bovine viral diarrhea virus 1; Coronavirus; Herpesviridae; herpesvirus 1; Respiratory syncytial virus; Syncytial virus; virus antibody; animal; article; Bovine diarrhea virus; cattle; cattle disease; Coronavirus; enzyme linked immunosorbent assay; food contamination; immunology; Infectious bovine rhinotracheitis virus; milk; prevalence; Respiratory syncytial pneumovirus; United Kingdom; virology; Animals; Antibodies, Viral; Bovine Virus Diarrhea-Mucosal Disease; Cattle; Coronavirus, Bovine; Diarrhea Viruses, Bovine Viral; England; Enzyme-Linked Immunosorbent Assay; Food Contamination; Herpesvirus 1, Bovine; Milk; Prevalence; Respiratory Syncytial Virus, Bovine; Wales","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., (1991) Acta Veterinaria Scandinavica, 32, p. 163; Alenius, S., Lindberg, A., Larsson, B., (1997) Proceedings of the 3rd ESVV Conference on Pestiviruses, , Lelystad, September 19-20, 1996; Bitsch, V., Ronsholt, L., (1995) Veterinary Clinics of North America, 11, p. 627. , November 1995. Eds J. C. Baker, H. Houe. Philadelphia, W. B. Saunders; Brownlie, J., Clarke, M.C., Hooper, L.B., Bell, G.D., (1995) Veterinary Record, 137, p. 58; Dean, A.G., Dean, J.A., Burton, A.H., Dicker, R.C., (1990) Epi Info, Version 5: A Word Processing, Database and Statistics Program for Epidemiology on Microcomputers, , Georgia, USD Incorporated; Duefell, S.J., Harkness, J.W., (1985) Veterinary Record, 117, p. 240; Edwards, S., (1988) Veterinary Record, 123, p. 614; Edwards, S., (1990) Review Scientifique et Technique de L'Office International Des Épizooties, 9, p. 115; Edwards, S., Drew, T.W., Bushnell, S.E., (1987) Veterinary Record, 120, p. 71; Elvander, M., (1996) Veterinary Record, 138, p. 101; Elvander, M., Edwards, S., Näslund, K., Linde, N., (1995) Journal of Veterinary Diagnostic Investigation, 7, p. 177; Espuna, E., Verdrell, J., Artigas, C., (1988) Medicina Veterinaria, 5, p. 499; Frankena, K., Franken, P., Vandehoek, J., Koskamp, G., Kramps, J.A., (1997) Veterinary Record, 140, p. 90; Harkness, J.W., Sands, J.J., Richards, M.S., (1978) Research in Veterinary Science, 24, p. 98; Hartman, A., Van Wuijckhuise, L., Frankena, K., Franken, P., Wever, P., Dewitt, J., Cramps, J.A., (1997) Veterinary Record, 140, p. 484; Hogg, A.A., (1992) Proceedings of the British Cattle Veterinary Association 1991-1992, p. 347; Houe, H., (1995) Veterinary Clinics of North America, November 1995, 11, p. 521. , Eds J. C. Baker, H. Houe. Philadelphia, W. B. Saunders; Houe, H., Meyling, A., (1991) Preventive Veterinary Medicine, 11, p. 9; Levy, P.S., Lemeshow, S., (1980) Sampling for Health Professionals, p. 37. , California, Lifetime Learning Publications; Lindberg, A., (1995) Proceedings of the Society for Veterinary Epidemiology and Preventive Medicine, p. 132. , Reading, March 29-31, 1995; Mccullough, S.J., Adair, B.M., Mckillop, E.R., (1987) Irish Veterinary Journal, 41, p. 342; (1996) Agricultural and Horticultural Census England and Wales, , MAFF, June 1995; Niskanen, R., Alenius, S., Larsson, B., Jacobsson, S.O., (1991) Archives of Virology Supplement, 3, p. 245; Niskanen, R., (1993) Veterinary Record, 133, p. 341; Pritchard, G.C., (1992) Proceedings of the Society for Veterinary Epidemiology and Preventive Medicine, p. 168. , Edinburgh, 1992; (1993) Egret Reference Manual Revision 4, , Seattle, SERC; Verhoeff, J., Van Nieuwstadt, A.P., (1984) Veterinary Record, 114, p. 288; Van Wuijkhuise, L., Bosch, J., Franken, P., Hage, J., Verhoeff, J., Zimmer, G., (1993) Proceedings of the Dutch Society for Veterinary Epidemiology and Economics, p. 7. , Boxtel; (1996) Veterinary Investigation Surveillance Report 1995 and 1988-95, p. 34; Waage, S., Krogsrud, J., Nyberg, O., (1994) Proceedings of the 18th World Buiatric Congress, p. 773. , Bolosne, Italy",,,"British Veterinary Association",00424900,,VETRA,"9586130","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0032507341
"Herrewegh A.A.P.M., Smeenk I., Horzinek M.C., Rottier P.J.M., De Groot R.J.","6602355430;6506930653;7102624836;7006145490;7103077066;","Feline coronavirus type II trains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus",1998,"Journal of Virology","72","5",,"4508","4514",,215,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031958109&partnerID=40&md5=9ba62678d50187fb8ba1b089460c2b1e","Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, POB 80.165, 3508 TD Utrecht, Netherlands","Herrewegh, A.A.P.M., Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Smeenk, I., Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Horzinek, M.C., Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; De Groot, R.J., Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands, Dept. of Infect. Dis. and Immunology, Faculty of Veterinary Medicine, Utrecht University, POB 80.165, 3508 TD Utrecht, Netherlands","Recent evidence suggests that the type II feline coronavirus (FCoV) strains 79-1146 and 79-1683 have arisen from a homologous RNA recombination event between FCoV type I and canine coronavirus (CCV). In both cases, the template switch apparently took place between the S and M genes, giving rise to recombinant viruses which encodes a CCV-like S protein and the M, N, 7a, and 7b proteins of FCoV type I (K. Motowaka, T. Hohdatsu, H. Hashimoto, and H. Koyama, Microbiol. Immunol. 40:425-433, 1996; H. Vennema, A. Poland, K. Floyd Hawkins, and N. C. Pedersen, Feline Pract. 23:40-44, 1995). In the present study, we have looked for additional FCoV-CCV recombination sites. Four regions in the pol gene were selected for comparative sequence analysis of the type II FCoV strains 79-1683 and 79-1146, the type I FCoV strains TN406 and UCD1, the CCV strain K378, and the TGEV strain Purdue. Our data show that the type II FCoVs have arisen from double recombination events: additional crossover sites were mapped in the ORF1ab frameshifting region of strain 79-1683 and in the 5' half of ORF1b of strain 79-1146.",,"animal cell; article; cat; coronavirus; crossing over; dog; frameshift mutation; nonhuman; priority journal; strain difference; virus recombination; virus typing; Animals; Base Sequence; Cats; Cell Line; Coronavirus; Coronavirus, Canine; DNA, Viral; Dogs; Molecular Sequence Data; Recombination, Genetic","Banner, L.R., Lai, M.M.C., Random nature of coronavirus RNA recombination in the absence of selection pressure (1991) Virology, 185, pp. 441-445; Baric, R.S., Fu, K.F., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map of murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab. 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Siddell (ed.), Plenum Press, New York, N.Y; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A.M., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organisation of the Nidovirales: Similarities and differences among arteri-, toro- And coronaviruses (1997) Semin. Virol., 8, pp. 33-48; Eleouet, J., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Hasony, H.J., Macnaughton, M.R., Antigenicity of mouse hepatitis virus strain 3 subcomponents in C57 strain mice (1981) Arch. Virol., 69, pp. 33-41; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Veldkamp, A., De Rooij, E., Vennema, H., De Groot, R.J., (1997) Nucleotide Sequence of the 3a, 3b, 3c, E, M and N Genes of FCoV Strain FECV 79-1683, , Database accession no. Y13921. EMBL, Heidelberg, Germany; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Higgins, D.G., Sharp, P.M., Fast and sensitive multiple sequence alignments on a micro computer (1989) Comput. Appl. Biosci., 5, pp. 151-153; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenie relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs): Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol., 28, pp. 13-24; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, S., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Koolen, M.J.M., Borst, M.A.J., Horzinek, M.C., Spaan, W.J.M., Immunogenic peptide comprising a mouse hepatitis virus A59 B-cell epitope and an influenza virus T-cell epitope protects against lethal infection (1990) J. Virol., 64, pp. 6270-6273; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kusters, J.G., Jager, E.J., Niesters, H.G.M., Zeist, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Semin. Virol., 7, pp. 381-388; Lai, M.M.C., Baric, R.C., Makino, S., Keck, J.G., Engbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Liao, C., Lai, M.M.C., RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments (1992) J. Virol., 66, pp. 6117-6124; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-739; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Canine coronavirus infection in cats; a possible role in feline infectious peritonitis (1990) Adv. Exp. Med. Biol., 276, pp. 475-479; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of monoclonal antibodies on lethal mouse hepatitis virus infection in mice (1986) J. 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Sci., 45, pp. 383-388; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Vennema, H., Personal communication; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44; Wang, L., Junker, D., Collision, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wesseling, J.G., Godeke, G., Schijns, V.E.C.J., Prevec, L., Graham, F.L., Horzinek, M.C., Rottier, P.J.M., Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection (1993) J. Gen. Virol., 74, pp. 2061-2069; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","De Groot, R.J.; Virology Unit, Infectious Diseases/Immunol. Dept., Faculty of Veterinary Medicine, POB 80.165, 3508 TD Utrecht, Netherlands; email: R.Groot@vetmic.dgk.ruu.nl",,,0022538X,,JOVIA,"9557750","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031958109
"Risco C., Muntión M., Enjuanes L., Carrascosa J.L.","56251715300;8114506300;7006565392;35481302900;","Two types of virus-related particles are found during transmissible gastroenteritis virus morphogenesis",1998,"Journal of Virology","72","5",,"4022","4031",,31,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031957565&partnerID=40&md5=8a896166e9801246e082777074a85f51","Dept. of Macromolecular Structure, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Dept. of Macromolecular Structure, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Risco, C., Dept. of Macromolecular Structure, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Muntión, M., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain; Carrascosa, J.L., Dept. of Macromolecular Structure, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, 28049 Madrid, Spain, Dept. of Macromolecular Structure, Ctro. Natl. de Biotecnologia (CSIC), Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The intracellular assembly of the transmissible gastroenteritis coronavirus (TGEV) was studied in infected swine testis (ST) cells at different postinfection times by using ultrathin sections of conventionally embedded infected cells, freeze-substitution, and methods for detecting viral proteins and RNA at the electron microscopy level. This ultrastructural analysis was focused on the identification of the different viral components that assemble in infected cells, in particular the spherical, potentially icosahedral internal core, a new structural element of the extracellular infectious coronavirus recently characterized by our group. Typical budding profiles and two types of virion-related particles were detected in TGEV-infected cells. While large virions with an electron- dense internal periphery and a clear central area are abundant at perinuclear regions, smaller viral particles, with the characteristic morphology of extracellular virions (exhibiting compact internal cores with polygonal contours) accumulate inside secretory vesicles that reach the plasma membrane. The two types of virions coexist in the Golgi complex of infected ST cells. In nocodazole-treated infected cells, the two types of virions coexist in altered Golgi stacks, while the large secretory vesicles filled with virions found in normal infections are not detected in this case. Treatment of infected cells with the Golgi complex-disrupting agent brefeldin A induced the accumulation of large virions in the cisternae that form by fusion of different membranous compartments. 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"Luo Z., Weiss S.R.","55460270800;57203567044;","Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein",1998,"Virology","244","2",,"483","494",,71,"10.1006/viro.1998.9121","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032503238&doi=10.1006%2fviro.1998.9121&partnerID=40&md5=db9f1515a323fa673a2f5b3476d2b0eb","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","Luo, Z., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","The spike (S) protein of coronavirus, mouse hepatitis virus (MHV), mediates attachment and fusion during viral entry and cell-to-cell fusion later in infection. By analogy with other viral proteins that induce cell fusion the MHV S protein would be expected to have a hydrophobic stretch of amino acids that serves as a fusion peptide. Sequence analysis suggests that the S protein falls within the group of fusion proteins having internal rather than N-terminal fusion peptides. Based on the features of known viral fusion peptides, we identified two regions (PEP1 and PEP2) of MHV-A59 S2 aS possible fusion peptides. Site-directed mutagenesis and an in vitro cell-to- cell fusion assay were used to evaluate the roles of PEP1 and PEP2, as well as a third previously identified putative fusion domain (PEP3) in membrane fusion. Substitution of bulky hydrophobic residues with charged residues within PEP1 affects the fusion activity of the S protein without affecting processing and surface expression. Similar substitutions within PEP2 result in a fusion-negative phenotype; however, these mutant S proteins also exhibit defects in protein processing and surface expression which likely explain the loss of the ability to induce fusion. Thus PEP1 remains a candidate fusion peptide, while PEP2 may play a significant role in the overall structure or oligomerization of the S protein. 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Physiol., 52, pp. 675-697; White, J.M., Membrane fusion (1992) Science, 258, pp. 917-924; Yu, Y.G., King, D.S., Shin, Y.K., Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes (1994) Science, 266, pp. 274-276","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"9601516","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032503238
"Sizun J., Arbour N., Talbot P.J.","35605340000;6602762564;7102670281;","Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture",1998,"Journal of Virological Methods","72","2",,"145","152",,25,"10.1016/S0166-0934(98)00013-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031749788&doi=10.1016%2fS0166-0934%2898%2900013-5&partnerID=40&md5=f147f8869c3e7703918dca14858a0b58","Laboratory of Neuroimmunovirology, Armand-Frappier Inst., Univ. Q., Laval, Que. H7V 1B7, Canada","Sizun, J., Laboratory of Neuroimmunovirology, Armand-Frappier Inst., Univ. Q., Laval, Que. H7V 1B7, Canada; Arbour, N., Laboratory of Neuroimmunovirology, Armand-Frappier Inst., Univ. Q., Laval, Que. H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Armand-Frappier Inst., Univ. Q., Laval, Que. H7V 1B7, Canada","Human coronaviruses, with two known serogroups named 229E and OC43, cause up to one third of common colds and may be associated with serious diseases such as nosocomial respiratory infections, enterocolitis, pericarditis and neurological disorders. Reliable methods of detection in clinical samples are needed for a better understanding of their role in pathology. As a first step in the design of such diagnostic procedures, the sensitivities and specificities of two viral diagnostic assays were compared in an experimental cell culture model: an indirect immuno-fluorescence assay using monoclonal antibodies and reverse transcriptase-polymerase chain reaction amplification of viral RNA from infected cells. Immunofluorescence detected human coronaviruses in cells infected at a MOI as low as 10-2 (log TCID50/ml = 4.25 for HCV-229E and 2.0 for HCV-OC43; log PFU/ml = 4.83 for HCV-229E and 1.84 for HCV-OC43) versus 10-3 (HCV-OC43) or 10-4 (HCV-229E) for reverse transcriptase-polymerase chain reaction amplification (log TCID50/ml = 1.75 for HCV-229E and 1.5 for HCV-OC43; log PFU/ml = 2.3 for HCV-229E and 1.34 for HCV-OC43). There were no false positive signals with other human respiratory pathogens: influenza virus, respiratory syncytial virus and adenovirus. Moreover, each assay was coronavirus serogroup-specific. These results demonstrate the potential usefulness of immunofluorescence with monoclonal antibodies and reverse transcriptase-polymerase chain reaction RNA amplification for the rapid detection of human coronaviruses in infected cell cultures. Both methods could be applied to clinical specimens for the diagnosis of human infections.","229E; Coronavirus; Diagnostic; Immunofluorescence; OC43; RT-PCR","article; cell culture; coronavirus; human; human cell; immunofluorescence; intermethod comparison; priority journal; reverse transcription polymerase chain reaction; serotype; virus characterization; Antibodies, Monoclonal; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Fluorescent Antibody Technique, Indirect; Humans; Polymerase Chain Reaction; Sensitivity and Specificity","Bonavia, A., Arbour, N., Wee Yong, V., Talbot, P.J., Infection of primary cultures of human neural cells by human coronaviruses 229E and OC43 (1997) J. Virol., 71, pp. 800-806; Chany, C., Moscovici, O., Lebon, P., Rousset, S., Association of Coronavirus with neonatal necrotizing enterocolitis (1982) Pediatrics, 69, pp. 209-214; Chomczynski, P., Sacchi, N., Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1989) Anal. Biochem., 162, pp. 156-159; Gill, E.P., Dominguez, E.A., Greenberg, S.B., Atmar, R.L., Hogue, B.G., Baxter, B.D., Couch, R.B., Development and application of an enzyme immunoassay for Coronavirus OC43 antibody in acute respiratory illness (1994) J. Clin. Microbiol., 32, pp. 2372-2376; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc. Soc. Exp. Biol., 121, pp. 190-193; Ieven, M., Goossens, H., Relevance of nucleic acid amplification techniques for diagnosis of respiratory tract infections in the clinical laboratory (1997) Clin. Microbiol. Rev., 10, pp. 242-256; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of the nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Kapikian, A.Z., James, H.D., Kelly, S.J., Dees, J.H., Turner, H.C., McIntosh, K., Kim, H.W., Chanock, R.M., Isolation from man of 'Avian infectious bronchitis virus-like' viruses (coronaviruses) similar to 229E virus, with some epidemiological observations (1969) J. Infect. Dis., 119, pp. 282-290; Kraaijeveld, C.A., Reed, S.E., McNaughton, M.R., Enzyme-linked immunosorbent assay for detection of antibody in volunteers experimentally infected with human coronavirus strain 229E (1980) J. Clin. 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New York: Plenum; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell. Probes, 8, pp. 357-364; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) Br. Med. J., 307, pp. 982-986; Payment, P., Trudel, M., Isolement et identification des virus (1989) Manuel de Techniques Virologiques, pp. 21-44. , Québec: Presses de Université du Québec; Riski, H., Hovi, T., Coronavirus infections in man associated with diseases other than the common cold (1980) J. Med. Virol., 6, pp. 259-265; Robbins, M.A., Witsenboer, H., Michelmore, R.W., Fortin, M.G., Genetic mapping of turnip mosaic virus resistance in Lactuca sativa (1994) Theor. Appl. Genet., 89, pp. 583-589; Schreiber, S.S., Kamahora, T., Lai, M.C., Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Sizun, J., Soupre, D., Legrand, M.C., Giroux, J.D., Rubio, S., Chastel, C., Alix, D., De Parscau, L., Neonatal nosocomial respiratory infection with coronavirus: A prospective study in a neonatal intensive care unit (1995) Acta Paediatr., 84, pp. 617-620; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Valenti, W.M., Clarke, T.A., Hall, C.B., Menegus, M.A., Shapiro, D.L., Concurrent outbreaks of rhinovirus and respiratory syncytial virus in an intensive care nursery: Epidemiology and associated risk factors (1982) J. Pediatr., 100, pp. 722-726; Wilson, C.W., Stevenson, D.K., Arvin, A.M., A concurrent epidemic of respiratory syncytial virus and parainfluenza virus type 3 in a newborn nursery (1989) Pediatr. Infect. Dis. J., 8, pp. 24-29","Talbot, P.J.; Laboratory of Neuroimmunovirology, Armand-Frappier Institute, University of Quebec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,,01660934,,JVMED,"9694322","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0031749788
"Eleouet J.-F., Chilmonczyk S., Besnardeau L., Laude H.","6602581440;6701397181;6602382869;7006652624;","Transmissible gastroenteritis coronavirus induces programmed cell death in infected cells through a caspase-dependent pathway",1998,"Journal of Virology","72","6",,"4918","4924",,74,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031954467&partnerID=40&md5=96a331bff85d7ffab2340553b7fea68e","U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; INRA, U. Virologie Immunol. Moleculaires, 78352 Jouy-en-Josas Cedex, France","Eleouet, J.-F., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France, INRA, U. Virologie Immunol. Moleculaires, 78352 Jouy-en-Josas Cedex, France; Chilmonczyk, S., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Besnardeau, L., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Laude, H., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France","In this report, we show that apoptosis (or programmed cell death) is induced in different cell lines infected with a coronavirus, the porcine transmissible gastroenteritis virus (TGEV). Kinetic analysis of internucleosomal DNA cleavage by agarose gel electrophoresis and flow cytometry or cytometric monitoring of the mitochondrial transmembrane potential showed that, for ST cells infected with TGEV, the first overt signs of apoptosis appeared from 10 to 12 h postinfection on. They preceded morphological changes characteristic of cells undergoing apoptosis, as observed by light and electron microscopy. The tripeptide pan-ICE (caspase) inhibitor N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone blocked TGEV- induced apoptosis with no effect on virus production. The thiol agent pyrrolidine dithiocarbamate inhibited apoptosis, suggesting that TGEV infection may lead to apoptosis via cellular oxidative stress. The effect of TGEV infection on activation of NF-κB, a transcription factor known to be activated by oxidative stress, was examined. NF-κB DNA binding was shown to be strongly and quickly induced by TGEV infection. However, transcription factor decoy experiments showed that NF-κB activation is not critical for TGEV-induced apoptosis.",,"caspase; cysteine proteinase; immunoglobulin enhancer binding protein; proteinase inhibitor; pyrrolidine dithiocarbamate; transcription factor; unclassified drug; animal cell; apoptosis; article; controlled study; coronavirus; dna cleavage; gastroenteritis; membrane potential; mitochondrial membrane; nonhuman; oxidative stress; priority journal; swine disease; virus gene; virus infection; Amino Acid Chloromethyl Ketones; Animals; Apoptosis; Cell Line; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Gastroenteritis, Transmissible, of Swine; Signal Transduction; Swine; Transmissible gastroenteritis virus","Baeuerle, P.A., Henkel, T., Function and activation of NF-kappa B in the immune system (1994) Annu. Rev. 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Virol., 67, pp. 119-130; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Lee, S.K., Youn, H.Y., Hasegawa, A., Nakayama, H., Goto, N., Apoptotic changes in the thymus of mice infected with mouse hepatitis virus, MHV-2 (1994) J. Vet. Med. Sci., 56, pp. 879-882; Levine, B., Huang, Q., Isaacs, J.T., Reed, J.C., Griffin, D.E., Hardwick, J.M., Conversion of lytic to persistent alphavirus infection by the bcl-2 cellular oncogene (1993) Nature, 361, pp. 739-742; Liao, C.L., Lin, Y.L., Wang, J.J., Huang, Y.L., Yen, C.T., Ma, S.H., Chen, L.K., Effect of enforced expression of human bcl-2 on Japanese encephalitis virus-induced apoptosis in cultured cells (1997) J. 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USA, 24, pp. 5202-5206; Vaux, D.L., Strasser, A., The molecular biology of apoptosis (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 2239-2244; Wyllie, A., Clues in the p53 murder mystery (1997) Nature, 389, pp. 237-238; Zhu, H., Fearnhead, H.O., Cohen, G.M., An ICE-like protease is a common mediator of apoptosis induced by diverse stimuli in human monocytic THP.1 cells (1995) FEBS Lett., 374, pp. 303-308","Eleouet, J.-F.; INRA, Unite Virologie/Immunologie Molec., 78352 Jouy-en-Josas Cedex, France; email: eleouet@biotec.jouy.inra.fr",,,0022538X,,JOVIA,"9573259","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031954467
"Lim K.P., Liu D.X.","7403175857;8972667300;","Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein",1998,"Virology","245","2",,"303","312",,37,"10.1006/viro.1998.9164","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032486388&doi=10.1006%2fviro.1998.9164&partnerID=40&md5=e4cee7f1309668f3b035ab4bc3f4c5b4","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore, 117604, Singapore","Lim, K.P., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore, 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore, 117604, Singapore","In a previous report, we showed that proteolytic processing of an 87- kDa mature viral protein from the coronavirus infectious bronchitis virus (IBV) 1a and 1a/1b polyproteins was mediated by two putative overlapping papain-like proteinase domains (PLPDs) encoded within the region from nucleotides 4243 to 5553 of ORF 1a (Liu et al., 1995). In this study, we demonstrate that only the first domain, PLPD-1, is responsible for this cleavage, as deletion of the second domain did not affect the formation of the 87-kDa protein. Site-directed mutagenesis studies further showed that a previously predicted nucleophilic cysteine residue (Cys1274) and a histidine residue (His1437) were essential for the proteinase activity, indicating that they may be important components of the catalytic center of the proteinase. Meanwhile, expression of a series of deletion mutants revealed that the 87-kDa protein was encoded by the 5'-most 2.6 kb of ORF 1a. Deletion and amino acid substitution mutation studies demonstrated that the Gly673-Gly674 dipeptide bond was most likely the cleavage site responsible for releasing the C-terminus of the 87-kDa protein from the 1a and 1a/1b polyproteins.",,"proteinase; virus enzyme; article; bronchitis; carboxy terminal sequence; Coronavirus; nonhuman; priority journal; protein determination; sequence analysis; site directed mutagenesis; virus characterization; virus detection; Avian infectious bronchitis virus; Coronavirus; RNA viruses","Baker, S.C., Yokomori, K., Dong, S.H., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. 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Biol., 276, pp. 275-281; Denison, M., Perlman, S., Identification of putative polymerase gene product in cells infected with murine coronavirus A59 (1987) Virology, 157, pp. 565-568; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotien of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Dong, S.H., Baker, S.C., Determination of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. 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Virol., 69, pp. 809-813; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lee, H-J., Shieh, C-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 190, pp. 567-582; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression and processing of an 87 kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Location of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol., 50, pp. 22-29; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Liu, D.X.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; email: liudx@ima.org.sg",,"Academic Press Inc.",00426822,,VIRLA,"9636369","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032486388
"Hohdatsu T., Izumiya Y., Yokoyama Y., Kida K., Koyama H.","57197786893;7004265074;57206435327;36965056800;7402164528;","Differences in virus receptor for type I and type II feline infectious peritonitis virus",1998,"Archives of Virology","143","5",,"839","850",,44,"10.1007/s007050050336","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031832221&doi=10.1007%2fs007050050336&partnerID=40&md5=cdca97ea6e2342ed04a51a93ce91dd8a","Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan; Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan","Hohdatsu, T., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan, Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034, Japan; Izumiya, Y., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan; Yokoyama, Y., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan; Kida, K., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan; Koyama, H., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori, Japan","Feline infectious peritonitis viruses (FIPVs) are classified into type I and type II serogroups. Here, we report that feline aminopeptidase N (APN), a cell-surface metalloprotease on the intestinal, lung and kidney epithelial cells, is a receptor for type II FIPV but not for type I FIPV. A monoclonal antibody (MAb) R-G-4, which blocks infection of Fells cams whole fetus (fcwf-4) cells by type II FIPV, was obtained by immunizing mice with fcwf-4 cells, which are highly susceptible to FIPV. This MAb also blocked infection of fcwf-4 cells by type II feline enteric coronavirus (FECV), canine coronavirus (CCV), and transmissible gastroenteritis virus (TGEV). On the other hand, it did not block infection by type I FIPVs. MAb R-G-4 recognized a polypeptide of relative molecular mass 120-130 kDa in feline intestinal brush-border membrane (BBM) proteins. The polypeptide possessed aminopeptidase activity, and the first 15 N-terminal amino acid sequence was identical to that of the feline APN. Feline intestinal BBM proteins and the polypeptide reacted with MAb R-G-4 (feline APN) inhibited the infectivity of type II FIPV, type II FECV, CCV and TGEV to fcwf-4 cells, but did not inhibit the infectivity of type I FIPVs.",,"amino acid sequence; brush border; cell surface; coronavirus; enzyme activity; epithelium cell; feline enteric coronavirus; infectivity; metalloproteinase; microsomal aminopeptidase; monoclonal antibody; mouse; n terminal; polypeptide; transmissible gastroenteritis virus; virus receptor; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antigens, CD13; Cats; Cells, Cultured; Coronavirus; Coronavirus, Canine; Coronavirus, Feline; Dogs; Feline panleukopenia virus; Humans; Intestines; Membrane Proteins; Mice; Microvilli; Molecular Sequence Data; Receptors, Virus; Swine; Transmissible gastroenteritis virus; Canine coronavirus; Coronavirus; Enteric coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; Transmissible gastroenteritis virus","Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab Anim Sci, 34, pp. 592-597; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Booth, A.G., Kenny, A.J., A rapid method for the preparation of microvilli from rabbit kidney (1974) Biochem J, 142, pp. 575-581; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J Virol, 66, pp. 6695-6705; Corapi, W.V., Darteil, R.J., Audonnet, J.C., Chappuis, G.E., Localization of antigenic site of the S glycoprotein of feline infectious peritonitis virus involved in neutralization and antibody-dependent enhancement (1995) J Virol, 69, pp. 2858-2862; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Siddell SG (ed) Plenum Press, New York; Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase N that is distinct from the enzymatic site (1994) J Virol, 68, pp. 5216-5224; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-419; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase N as a receptor for coronaviruses (1994) Adv Exp Med Biol, 342, pp. 293-298; Drexler, H.G., Sagawa, K., Menon, M., Minoada, J., Reactivity pattern of ""myeloid monoclonal antibodies"" with emphasis on MCS-2 (1986) Leukemia Res, 10, pp. 17-23; Hohdatsu, T., Yamada, H., Ishizuka, Y., Koyama, H., Enhancement and neutralization of feline infectious peritonitis virus infection in feline macrophages by neutralizing monoclonal antibodies recognizing different epitopes (1993) Microbiol Immunol, 37, pp. 499-504; Hohdatsu, T., Nakamura, M., Ishizuka, Y., Yamada, H., Koyama, H., A study on the mechanism of antibody-dependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies (1991) Arch Virol, 120, pp. 207-217; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine and canine coronaviruses (1991) Arch Virol, 117, pp. 85-95; Kenny, A.J., Maroux, S., Topology of microvillar membrane hydorolases of kidney and intestine (1982) Physiol Rev, 62, pp. 91-128; Köhler, G., Milstein, C., Continuous cultures of fused cells secreting antibody of predefined specificity (1975) Nature, 256, pp. 495-497; Lentz, T.L., The recognition event between virus and host cell receptor: A target for antiviral agents (1990) J Gen Virol, 71, pp. 751-766; Levis, R., Cardellichio, C.B., Scanga, C.A., Compton, S.R., Holmes, K.V., Multiple receptor-dependent steps determine the species specificity of HCV-229E infection (1995) Adv Exp Med Biol, 380, pp. 337-343; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp 150) is identical to aminopeptidase N (1989) J Clin Invest, 83, pp. 1299-1307; 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(1993) Blood, 82, pp. 1052-1070; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Siddell SG (ed) Plenum Press, New York; Stoddart, C.A., Barlough, J.E., Baldwin, C.A., Scott, F.W., Attempted immunisation of cats against feline infectious peritonitis using canine coronavirus (1988) Res Vet Sci, 45, pp. 383-388; Soderberg, C., Giugni, T.D., Zaia, J.A., Larsson, S., Wahlberg, J.M., Moller, E., CD 13 (Human Aminopeptidase N) mediates human cytomegalovirus infection (1993) J Virol, 67, pp. 6576-6585; Tresnan, D.B., Levis, R., Homles, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J Virol, 70, pp. 8669-8674; Woods, R.D., Cheville, N.F., Gallagher, J.E., Lesions in the small intestine of newborn pigs inoculated with porcine, feline, and canine coronaviruses (1981) Am J Vet Res, 42, pp. 1163-1169; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Hohdatsu, T.; Dept. of Veterinary Infect. Diseases, Sch. of Veterinary Med./Animal Sci., Kitasato University, Towada, Aomori 034, Japan",,,03048608,,ARVID,"9645192","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0031832221
"Cornelissen L.A.H.M., Van Woensel P.A.M., De Groot R.J., Horzinek M.C., Visser N., Egberink H.F.","57200893222;6602238435;7103077066;7102624836;7004184852;7004767057;","Cell culture-grown putative bovine respiratory torovirus identified as a coronavirus",1998,"Veterinary Record","142","25",,"683","686",,4,"10.1136/vr.142.25.683","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032550973&doi=10.1136%2fvr.142.25.683&partnerID=40&md5=d77b8901cd39e2d471805f8225254f37","Department of Large Animal Medicine, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Virology Unit, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Intervet International BV, 5830 AA Boxmeer, Netherlands","Cornelissen, L.A.H.M., Department of Large Animal Medicine, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Van Woensel, P.A.M., Intervet International BV, 5830 AA Boxmeer, Netherlands; De Groot, R.J., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands; Visser, N., Intervet International BV, 5830 AA Boxmeer, Netherlands; Egberink, H.F., Virology Unit, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands","A putative bovine respiratory torovirus (BRTV) was propagated in bovine fetal diploid lung and human colonic tumour cells, and fringed pleomorphic particles were detected in the culture supernatants by electron microscopy. Antisera directed against a bovine (Breda strain) and equine (Berne strain) torovirus failed to react with BRTV-infected cells in immunofluorescence assays and did not neutralise BRTV. No toroviral RNA was found in the supernatants of infected cells by means of a reverse transcriptase-polymerase chain reaction with torovirus-specific primers. On the other hand, bovine coronavirus-specific antisera and monoclonal antibodies did neutralise the cytopathic effects, and coronaviral antigen was detected in the cultures by immunofluorescence. Furthermore, bovine coronavirus RNA was detected in the supernatants of BRTV-infected cells after nucleic acid amplification. It is concluded that the cytopathic BRTV isolate is a coronavirus.",,"Bovinae; Bovine coronavirus; Coronavirus; Equidae; Torovirus; virus RNA; animal; article; cattle; cattle disease; classification; Coronavirus; culture technique; fluorescent antibody technique; human; in vitro study; isolation and purification; methodology; polymerase chain reaction; Torovirus; virology; Animals; Cattle; Cattle Diseases; Cell Culture Techniques; Coronavirus, Bovine; Fluorescent Antibody Technique, Direct; Humans; Polymerase Chain Reaction; RNA, Viral; Torovirus","Beards, G.M., Brown, D.W.G., Green, J., Flewett, T.H., (1986) Journal of Medical Virology, 20, p. 67; Beards, G.M., Green, J., Hall, C., Flewett, T.H., Lamouliatte, F., Du Pasquier, P., (1984) Lancet, 2, p. 1050; Brown, D.W.G., Beards, G.M., Flewett, T.H., (1987) Journal of Clinical Microbiology, 25, p. 637; Brown, D.W.G., Selvakumar, R., Daniel, D.J., Mathan, V.I., (1988) Archives of Virology, 98, p. 267; Cornelissen, L.A.H.M., Wierda, C.M.H., Van der Meer, F.J., Herrewegh, A.A.P.M., Horzinek, M.C., Egberink, H.F., De Groot, R.J., (1997) Journal of Virology, 71, p. 5277; Kaeffer, B., Van Kooten, P., Ederveen, J., Van Eden, W., Horzinek, M.C., (1989) American Journal of Veterinary Research, 50, p. 1131; Koopmans, M., Van den Boom, U., Woode, G.N., Horzinek, M.C., (1989) Veterinary Microbiology, 19, p. 233; Koopmans, M., Cremers, H., Woode, G.N., Horzinek, M.C., (1990) American Journal of Veterinary Research, 51, p. 1443; Koopmans, M., Ederveen, J., Woode, G.N., Horzinek, M.C., (1986) American Journal of Veterinary Research, 47, p. 1896; Koopmans, M., Herrewegh, A.A.P.M., Horzinek, M.C., (1991) Lancet, 337, p. 859; Koopmans, M., Horzinek, M.C., (1994) Advances in Virus Research, 43, p. 233; Koopmans, M., Van Wuijckhuise-Sjouke, L., Cremers, H., Horzinek, M.C., (1991) American Journal of Veterinary Research, 52, p. 1769; Kroneman, A., Cornelissen, L.A.H.M., De Groot, R.J., Horzinek, M.C., Egberink, H.F., (1998) Journal of Virology, 72, p. 3507; Mcnulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., (1984) Veterinary Microbiology, 9, p. 425; Muir, P., Harbour, D.A., Gruyffydd-Jones, T.J., Howard, T.J., Hopper, C.D., Gruyffydd-Jones, E.A.D., Broadhead, H.M., Jones, M.E., (1990) Veterinary Record, 127, p. 324; Pringle, C.R., (1992) American Society for Microbiology News, 58, p. 475; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., (1985) Archives of Virology, 85, p. 71; Rekik, M.R., Dea, S., (1994) Archives of Virology, 135, p. 319; Rottier, P.J.M., Spaan, W.J.M., Horzinek, M.C., Van der Zeist, B.A.M., (1981) Journal of Virology, 40, p. 350; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., (1986) American Journal of Veterinary Research, 47, p. 1426; Scott, A.C., Chaplin, M.J., Stack, M.J., Lund, L.J., (1987) Veterinary Record, 120, p. 583; Scott, F.M.M., Holliman, A., Jones, G.W., Gray, E.W., Fitton, J., (1996) Veterinary Record, 138, p. 284; Snijder, E.J., Den Boon, J.A., Spaan, W.J.M., Verjans, G.M.G.M., Horzinek, M.C., (1989) Journal of General Virology, 70, p. 3363; Snijder, E.J., Horzinek, M.C., (1993) Journal of General Virology, 74, p. 2305; St Cyr-Coats, K., Payne, H.R., Storz, J., (1988) Journal of Veterinary Medicine, 35, p. 752; Storz, J., Rott, R., Kaluza, G., (1981) Infection Find Immunity, 31, p. 1214; Tsunemitsu, H., Saif, L.J., (1995) Archives of Virology, 140, p. 1303; Vanopdenbosch, E., Wellemans, G., Charlier, G., Petroff, K., (1992) Vlaams Diergeneesktundig Tijdschrift, 61, p. 45; Vanopdenbosch, E., Wellemans, G., Oudewater, J., Petroff, K., (1992) Vlaams Diergeneeskundig Tijdschrift, 61, p. 187; Vanopdenbosch, E., Wellemans, G., Petroff, K., (1991) Veterinary Record, 129, p. 203; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (1997) Seminars in Virology, 8, p. 33; Weiss, M., Horzinek, M.C., (1986) Veterinary Microbiology, 11, p. 41; Weiss, M., Steck, F., Horzinek, M.C., (1983) Journal of General Virology, 64, p. 1849; Weiss, M., Steck, F., Kaderli, R., Horzinek, M.C., (1984) Veterinary Microbiology, 9, p. 523; Wellemans, G., Vanopdenbosch, E., De Kegel, D., (1979) Annales de Médicine Vétérinaire, 123, p. 185; Woode, G.N., Novel Diarrhoea Viruses (1987) CIBA Foundation Symposium, 128, p. 175. , Eds G. Bock, J. Whelan. Chichester, Wiley & Sons; Woode, G.N., Reed, D.E., Runnels, P.L., Herrig, M.A., Hill, H.T., (1982) Veterinary Microbiology, 7, p. 221; Woode, G.N., Saif, L.J., Quesada, M., Winand, N.J., Pohlenz, J.F., Kelso Gourley, N., (1985) American Journal of Veterinary Research, 46, p. 1003","Cornelissen, L.A.H.M.; Department of Large Animal Medicine, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, Netherlands",,"British Veterinary Association",00424900,,VETRA,"9670455","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0032550973
"Yamanaka M., Crisp T., Brown R., Dale B.","7201926826;7006308365;57213543415;16188679200;","Nucleotide sequence of the inter-structural gene region of feline infections peritonitis virus",1998,"Virus Genes","16","3",,"317","318",,2,"10.1023/A:1008099209942","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031868106&doi=10.1023%2fA%3a1008099209942&partnerID=40&md5=a90aac93d5e09058226c9246a4756185","Intl. Lab. Molec. Biol. Trop. D., Dept. Vet. Pathol., Microbiol. I., University of California, Davis, CA 95616, United States; Roche Molecular Systems, Inc., 1145 Atlantic Avenue, Alameda, CA 94501, United States; Scios, Inc., 2450 Bayshore Parkway, Mountain View, CA 94043, United States","Yamanaka, M., Intl. Lab. Molec. Biol. Trop. D., Dept. Vet. Pathol., Microbiol. I., University of California, Davis, CA 95616, United States; Crisp, T., Scios, Inc., 2450 Bayshore Parkway, Mountain View, CA 94043, United States; Brown, R., Scios, Inc., 2450 Bayshore Parkway, Mountain View, CA 94043, United States; Dale, B., Roche Molecular Systems, Inc., 1145 Atlantic Avenue, Alameda, CA 94501, United States","The sequence of the region located between the S and M glycoprotein genes of the 79-1146 strain of feline infectious peritonitis virus (FIPV) is presented. The inter-structural gene region encodes 3 open reading frames (ORFs), termed ORFs 3a, 3b and 4, with nucleotide sequences conforming to the minimum conserved transcription signal upstream of each. An additional ORE 3x, partially overlaps the 3' end of ORF 3a. The FIPV interstructural gene region is identical in length when compared to the Insavc-1 strain of canine coronavirus (CCV) but differs from various strains of transmissible gastroenteritis virus (TGEV) by the presence of deletions and insertions. The sizes of ORF 3a and 4 are conserved in FIPV, TGEV and CCV. However, as with CCV, the FIPV ORF 3b is truncated in comparison with TGEV.","Comparative analysis; Feline infectious peritonitis virus; Open reading frames 3a, 3b and 4","glycoprotein; article; coronavirus; gene sequence; hepatitis virus; nonhuman; nucleotide sequence; open reading frame; peritonitis; priority journal; structural gene; virus gene; Animals; Base Sequence; Cats; Coronavirus, Feline; DNA, Viral; Genes, Viral; Molecular Sequence Data; Open Reading Frames; Canine coronavirus; Coronavirus; Felidae; Feline infectious peritonitis virus; RNA viruses; Staphylococcus phage 3A; Transmissible gastroenteritis virus","De Groot, R.J., Horzinek, M.C., (1995) The Coronaviridae, pp. 293-315. , Siddell S. (ed.). Plenum Press, New York; Rasschaert, D., Gelfi, J., Laude, H., (1987) Biochimie, 69, pp. 591-600; Kapke, P.A., Tung, F.Y.T., Brian, D.A., (1988) Virus Genes, 2, pp. 293-294; Britton, P., Lopez Otin, C., Martin Alonso, J.M., Parra, F., (1989) Arch Virol, 105, pp. 165-178; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., (1989) Virus Res, 13, pp. 87-100; Horsburgh, B.C., Brierley, I., Brown, T.D.K., (1992) J Gen Virol, 73, pp. 2849-2862; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., (1995) Feline Practice, 23, pp. 40-44; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van De Zeijst, B.A.M., Spaan, W.J.M., (1987) J Gen Virol, 68, pp. 2639-2646; Spaan, W., Cavanagh, D., Horzinek, M.C., (1988) J Gen Virol, 69, pp. 2939-2952","Yamanaka, M.; Internatl Lab Mol Biol Tropical Dis, Dept Veter Pathol Microbiol Immunol, University of California, Davis, CA 95616, United States; email: mkyamanaka@ucdavis.edu",,,09208569,,VIGEE,"9654687","English","Virus Genes",Article,"Final",,Scopus,2-s2.0-0031868106
"Gunn-Moore D.A., Gruffydd-Jones T.J., Harbour D.A.","7004448390;7005620906;7005502394;","Detection of feline coronaviruses by culture and reverse transcriptase-polymerase chain reaction of blood samples from healthy cats and cats with clinical feline infectious peritonitis",1998,"Veterinary Microbiology","62","3",,"193","205",,63,"10.1016/S0378-1135(98)00210-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032424235&doi=10.1016%2fS0378-1135%2898%2900210-7&partnerID=40&md5=baf85e5b69af4046a7d7e2fb26e8ccd6","Dept. of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol BS40 5DU, United Kingdom","Gunn-Moore, D.A., Dept. of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol BS40 5DU, United Kingdom; Gruffydd-Jones, T.J., Dept. of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol BS40 5DU, United Kingdom; Harbour, D.A., Dept. of Clinical Veterinary Science, University of Bristol, Langford House, Langford, Bristol BS40 5DU, United Kingdom","A reverse transcriptase-polymerase chain reaction (RT-PCR) assay for the detection of the feline coronavirus (FCoV) genome and a co-cultivation method for the isolation of field strains of FCoV are described. Using the RT-PCR assay to assess blood samples from cats with feline infectious peritonitis (FIP) (n=47) and healthy cats from households with endemic FCoV (n=69) it was shown that approximately 80% of the cats were viraemic, irrespective of their health status. It was also shown that, over a 12-month period, a similar percentage of healthy cats remained viraemic, and that the presence of viraemia did not appear to predispose the cats to the development of FIP. The co-cultivation system proved to be a suitable method for the culture of field strains of FCoV from blood samples, so long as the cultures were maintained for at least 4 weeks. Using this system, followed by the RT-PCR, viraemia was detected as frequently as by RT-PCR on RNA extracted directly from peripheral blood mononuclear cells. Copyright (C) 1998 Elsevier Science B.V.","Cat; Cell culture; Co-cultivation; Feline coronavirus; Polymerase chain reaction","animal experiment; animal model; article; cat; cat disease; cell culture; coronavirus; female; male; nonhuman; reverse transcription polymerase chain reaction; virus culture; virus detection; virus isolation; Animals; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; Peritonitis; Reference Values; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Time Factors","Addie, D.D., Jarrett, J.O., A study of naturally occurring feline coronavirus infection in kittens (1992) Vet. Rec., 130, pp. 133-137; Addie, D.D., Toth, S., Herrewegh, A.A.P.M., Jarrett, J.O., Feline coronavirus in the intestinal contents of cats with feline infectious peritonitis (1996) Vet. Rec., 139, pp. 522-523; Barlough, J.E., Scott, F.W., Feline infectious peritonitis (1988) Manual of Small Animal Infectious Diseases, pp. 63-78. , Barlough, J.E. (Ed.), Churchill Livingston, New York; Cammarata Parodi, M., Cammarata, G., Paltrinieri, S., Lavazza, A., Ape, F., Using direct immunofluorescence to detect coronaviruses in peritoneal and pleural effusions (1993) J. Small Ani. Prac., 34, pp. 609-613; Chen, W., Baric, R.F., Function of a 5′ end genomic mutation that evolves during persistent mouse hepatitis infection in vitro (1995) J. Virol., 69 (12), pp. 7529-7540; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A., Spaan, W.J., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) Journal of General Virolology, 68, pp. 2639-2646; Egberink, H.F., Herrewegh, A.A.P.M., Schuurman, N.M.P., Van Der Linde-Sipman, Horzinek, M.C., De Groot, R.J., FIP, Easy to Diagnose? (1995) Vet. Quart., 17 (1), pp. S24-S25; Feh, D., Bolla, S., Herrewegh, A.A.P.M., Horzinek, M.C., Lutz, H., Nachweis feliner Coronaviren mittels RT-PCR: Grundlage zum Studium der Pathogenese der Felinen Infektiosen Peritonitis (FIP) (1996) Schweizer Archiv fur Tierheilkunde, 138, pp. 74-79. , Zurich; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Amer. Vet. Med. Associ., 210, pp. 1307-1312; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33 (3), pp. 684-689; Herrewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Hirsch, M.S., Immune activation of endogenous viruses (1976) Tumour Virus Infections and Immunity, pp. 175-186. , Crowell, R.L., Friedman, H., Prier, J.E. (Eds.). Baltimore, University Park Press; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Medi. Sci., 54, pp. 557-562; Hok, K., Demonstration of feline coronavirus (FCV) antigen in organs of cats suspected of feline infectious peritonitis (FIP) disease (1989) APMIS, 98, pp. 659-664; Hok, K., Demonstration of feline infectious peritonitis virus in conjunctival epithelial cells from cats (1989) APMIS, 87, pp. 820-824; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet. Microbiol., 42, pp. 65-77; Martinez, M.L., Weiss, R.C., Detection of feline infectious peritonitis virus in cell culture and peripheral blood mononuclear leukocytes of experimentally infected cats using a biotinylated cDNA probe (1993) Vet. Microbiol., 34, pp. 259-271; Pedersen, N.C., Coronavirus diseases (coronavirus enteritis, feline infectious peritonitis) (1987) Diseases of the Cat. Medicine and Surgery Volume 1, 1, pp. 193-214. , Holzworth, J. (Ed.), Saunders, W.B., Philadelphia; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Ameri. J. Vet. Res., 42, pp. 368-377; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Ad. in E. Med. Biol., 173, pp. 365-380; Richter, M., Schinkinger, M.F., Mostl, K., Nachweis von Infektionen mit felinen Coronaviren Typ II im Blut von Katzen mittels Reverser Transcritase Polymerase-Kettenreaktion (RT-PCR) (1996) Wiener Tierarztliche Monatsschrift, 83, pp. 263-268; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterisation of spike deletion variants during persistent infection (1997) J. Virol., 71 (4), pp. 2959-2969; Scott, F.W., Feline Infectious Peritonitis and other feline coronaviruses (1986) Current Veterinary Therapy IX, pp. 1059-1062. , Kirk, R.W., Saunders, W.B. (Eds), Philadelphia; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., Feline infectious peritonitis: A review of clinicopathological changes in 65 cases, and a critical assessment of their diagnostic value (1991) Vet. Rec., 129, pp. 209-212; Stock, N.D., Ferrer, J.F., Replicating C type virus in phytohemagglutinin treated buffy coat cultures of bovine origin (1972) Journal of the National Cancer Institute, 48, pp. 985-996; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Pearson, G.R., The sites of early viral replication in feline infectious peritonitis (1988) Vet. Microbiol., 18, pp. 259-271; Tammer, R., Evensen, O., Lutz, H., Reinacher, M., Immunohistological demonstration of feline infectious peritonitis virus antigen in paraffin-embedded tissues using feline ascites or murine monoclonal antibodies (1995) Vet. Immun. and Immunopathol., 49, pp. 177-182; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Nature and development of viraemia (1981) American Journal of Veterinary Research, 42, pp. 382-390","Gunn-Moore, D.A.; Department Clinical Veterinary Sci., University of Bristol, Langford House, Langford, Bristol BS40 5DU, United States; email: d.a.gunn-moore@bristol.ac.uk",,,03781135,,VMICD,"9791867","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0032424235
"Pewe L., Xue S., Perlman S.","6603143496;7202791284;7102708317;","Infection with cytotoxic T-lymphocyte escape mutants results in increased mortality and growth retardation in mice infected with a neurotropic coronavirus",1998,"Journal of Virology","72","7",,"5912","5918",,30,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031775861&partnerID=40&md5=280ed23e17daedd222dc509e38a5a5b9","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Dept. Interdisciplinay Prog. I., University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Pewe, L., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Xue, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Dept. Interdisciplinay Prog. I., University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","C57BL/6 mice infected with mouse hepatitis virus strain JHM (MHV-JHM) develop a chronic demyelinating encephalomyelitis several weeks after inoculation. Previously, we showed that mutations in the immunodominant CD8 T-cell epitope (S-510-518) could be detected in nearly all samples of RNA and virus isolated from these mice. These mutations abrogated recognition by T cells harvested from the central nervous systems of infected mice in direct ex vivo cytotoxicity assays. These results suggested that cytotoxic T- lymphocyte (CTL) escape mutants contributed to virus amplification and the development of clinical disease in mice infected with wild-type virus. In the present study, the importance of these mutations was further evaluated by infecting naive mice with MHV-JHM variants isolated from infected mice and in which epitope S-510-518 was mutated. Compared to mice infected with wild- type virus, variant virus-infected animals showed higher mortality and morbidity manifested by decreased weight gain and neurological signs. Although a delay in the kinetics of virus clearance has been demonstrated in previous studies of CTL escape mutants, this is the first illustration of significant changes in clinical disease resulting from infection with viruses able to evade the CD8 T-cell immune response.",,"cd8 antigen; animal model; article; coronavirus; cytotoxic t lymphocyte; deletion mutant; encephalomyelitis; gene mutation; growth retardation; hepatitis virus; molecular recognition; mortality; mouse; neurotropism; nonhuman; priority journal; Animals; Coronavirus Infections; Encephalomyelitis; Epitopes, T-Lymphocyte; Growth Disorders; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Mutation; T-Lymphocytes, Cytotoxic","Banner, L., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted CTL response (1996) J. Gen. Virol., 77, pp. 315-325; Bertoletti, A., Costanzo, A., Chisari, F.V., Levero, M., Artini, M., Sette, A., Penna, A., Ferrari, C., Cytotoxic T lymphocyte response to a wild type hepatitis B virus epitope in patients chronically infected by variant viruses carrying substitutions within the epitope (1994) J. Exp. Med., 180, pp. 933-943; Bertoletti, A., Sette, A., Chisari, F.V., Penna, A., Levrero, M., De Carli, M., Fiaccadori, F., Ferrari, C., Natural variants of cytotoxic epitopes are T-cell receptor antagonists for antiviral cytotoxic T cells (1994) Nature, 369, pp. 407-410; Borrow, P., Lewicki, H., Wei, X., Horwitz, M., Peffer, N., Meyers, H., Nelson, J.A., Shaw, G., Antiviral pressure exerted by HIV-1-specific cytotoxic T lymphocytes (CTLs) during primary infection demonstrated by rapid selection of CTL escape mutants (1997) Nat. 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Med., 304, pp. 1152-1155; Heemskerk, M., Schoemaker, H., Spaan, W., Boog, C., Predominance of MHC class II-restricted CD4+ cytotoxic T cells against mouse hepatitis virus A59 (1995) Immunology, 84, pp. 521-527; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Hudrisier, D., Mazarguil, H., Oldstone, M.B.A., Gairin, J.E., Relative implication of peptide residues in binding to major histocompatibility complex class I H-2Db: Application to the design of high-affinity, allele-specific peptides (1995) Mol. 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Pathog., 2, pp. 185-194; Pewe, L., Wu, G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Pewe, L., Xue, S., Perlman, S., Cytotoxic T-cell-resistant variants arise at early times after infection in C57BL/6 but not in SCID mice infected with a neurotropic coronavirus (1997) J. 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Neuroimmunol., 30, pp. 31-41; Weiner, A., Erickson, A., Kanospon, J., Crawford, K., Muchmore, E., Hughes, A., Houghton, M., Walker, C.M., Persistent hepatitis C virus infection in a chimpanzee is associated with emergence of a cytotoxic T lymphocyte escape variant (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 2755-2759; Williamson, J.S., Stohlman, S.A., Effective clearance of mouse hepatitis virus from the central nervous system requires both CD4+ and CD8+ T cells (1990) J. Virol., 64, pp. 4589-4592; Wolinsky, S.M., Korber, B., Neumann, A.U., Daniels, M., Kunstman, K., Whetsell, A., Furtado, M., Koup, R., Adaptive evolution of human immunodeficiency virus-type 1 during the natural course of infection (1996) Science, 272, pp. 537-542; Xue, S., Perlman, S., Antigen specificity of CD4 T cell response in the central nervous system of mice infected with mouse hepatitis virus (1997) Virology, 238, pp. 68-78","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"9621053","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031775861
"Peremyslov V.V., Hagiwara Y., Dolja V.V.","9042964600;16052931600;7005753067;","Genes required for replication of the 15.5-Kilobase RNA genome of a plant closterovirus",1998,"Journal of Virology","72","7",,"5870","5876",,76,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031777342&partnerID=40&md5=a9a337561b85e6bb477bd6de000fbbdf","Dept. of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331, United States; Ctr. for Gene Res. and Biotechnology, Oregon State University, Corvallis, OR 97331, United States; Dept. of Botany and Plant Pathology, Oregon State University, Cordley Hall 2082, Corvallis, OR 97331, United States","Peremyslov, V.V., Dept. of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331, United States; Hagiwara, Y., Dept. of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331, United States; Dolja, V.V., Dept. of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331, United States, Ctr. for Gene Res. and Biotechnology, Oregon State University, Corvallis, OR 97331, United States, Dept. of Botany and Plant Pathology, Oregon State University, Cordley Hall 2082, Corvallis, OR 97331, United States","A full-length cDNA clone of beet yellows closterovirus (BYV) was engineered and used to map functions involved in the replication of the viral RNA genome and subgenomic RNA formation. Among 10 open reading frames (ORFs) present in BYV, ORFs 1a and 1b suffice for RNA replication and transcription. The proteins encoded in these ORFs harbor putative methyltransferase, RNA helicase, and RNA polymerase domains common to Sindbis virus-like viruses and a large interdomain region that is unique to closteroviruses. The papain- like leader proteinase (L-Pro) encoded in the 5'-proximal region of ORF 1a was found to have a dual function in genome amplification. First, the autocatalytic cleavage between L-Pro and the remainder of the ORF 1a product was essential for replication of RNA. Second, an additional L-Pro function that was separable from proteolytic activity was required for efficient RNA accumulation. The deletion of a large, ~5.6-kb, 3'-terminal region coding for a 6-kDa hydrophobic protein, an HSP70 homolog, a 64-kDa protein, minor and major capsid proteins, a 20-kDa protein, and a 21-kDa protein (p21) resulted in replication-competent RNA. However, examination of mutants with replacements of start codons in each of these seven 3'-terminal ORFs revealed that p21 functions as an enhancer of genome amplification. The intriguing analogies between the genome organization and replicational requirements of plant closteroviruses and animal coronavirus-like viruses are discussed.",,"methyltransferase; rna helicase; rna polymerase; article; closterovirus; gene amplification; genetic engineering; molecular cloning; nonhuman; nucleotide sequence; plant; priority journal; protein domain; rna replication; rna transcription; sindbis virus; Closterovirus; Enhancer Elements (Genetics); Gene Amplification; Genes, Viral; Genome, Viral; Open Reading Frames; Protein Sorting Signals; RNA, Viral","Adkins, S., Siegel, R.W., Sun, J.H., Kao, C.C., Minimal templates directing accurate initiation of subgenomic RNA synthesis in vitro by the brome mosaic virus RNA-dependent RNA polymerase (1997) RNA, 3, pp. 634-647; Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V., Dolja, V.V., Putative 65kDa protein of beet yellows closterovirus is a homologue of HSP70 heat shock proteins (1991) J. Mol. Biol., 217, pp. 603-610; Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Lunina, N.A., Koonin, E.V., Dolja, V.V., Nucleotide sequence of the 3′-terminal half of beet yellows closterovirus RNA genome: Unique arrangement of eight virus genes (1991) J. Gen. Virol., 72, pp. 15-23; Agranovsky, A.A., Koonin, E.V., Boyko, V.P., Maiss, E., Frotschl, R., Lunina, N.A., Atabekov, J.G., Beet yellows closterovirus: Complete genome structure and identification of a leader papain-like thiol protease (1994) Virology, 198, pp. 311-324; Agranovsky, A.A., Lesemann, D.E., Maiss, E., Hull, R., Atabekov, J.G., ""Rattlesnake"" structure of a filamentous plant RNA virus built of two capsid proteins (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 2470-2473; Atreya, C.D., Pirone, T.P., Mutational analysis of the helper component-proteinase gene of a potyvirus: Effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 11919-11923; (1987) Bio-Rad Bulletin 1393, , Bio-Rad Laboratories, Richmond, Calif; Boyko, V.P., Karasev, A.V., Agranovsky, A.A., Koonin, E.V., Dolja, V.V., Capsid protein gene duplication in a filamentous RNA virus of plants (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 9156-9160; Carrington, J.C., Cary, S.M., Parks, T.D., Dougherty, W.G., A second proteinase encoded by a plant potyvirus genome (1989) EMBO J., 8, pp. 365-370; Collmer, C.W., Kaper, J.M., Double-stranded RNAs of cucumber mosaic virus and its satellite contain an unpaired terminal guanosine: Implications for replication (1985) Virology, 145, pp. 249-259; Craven, M.G., Pawlyk, D.M., Choi, G.H., Nuss, D.L., Papain-like protease p29 as a symptom determinant encoded by a hypovirulence-associated virus of the chestnut blight fungus (1993) J. 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Brinton (ed.), ASM Press, Washington, D.C; Dolja, V.V., McBride, H.J., Carrington, J.C., Tagging of plant potyvirus replication and movement by insertion of β-glucuronidase (GUS) into the viral polyprotein (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 10208-10212; Dolja, V.V., Herndon, K.L., Pirone, T.P., Carrington, J.C., Spontaneous mutagenesis of a plant potyvirus genome after insertion of a foreign gene (1993) J. Virol., 67, pp. 5968-5975; Dolja, V.V., Karasev, A.V., Koonin, E.V., Molecular biology and evolution of closteroviruses: Sophisticated build-up of large RNA genomes (1994) Annu. Rev. Phytopathol., 32, pp. 261-285; Dolja, V.V., Hong, J., Keller, K.E., Martin, R.R., Peremyslov, V.V., Suppression of potyvirus infection by coexpressed closterovirus protein (1997) Virology, 234, pp. 243-252; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; French, R., Ahlquist, P., Characterization and engineering of sequences controlling in vivo synthesis of brome mosaic virus subgenomic RNA (1988) J. Virol., 62, pp. 2411-2420; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.-C., Putative papain-related thiol proteases of positive-strand RNA viruses (1991) FEBS Lett., 288, pp. 201-205; He, X.-H., Rao, A.L.N., Creamer, R., Characterization of beet yellows closterovirus-specific RNAs in infected plants and protoplasts (1997) Phytopathology, 87, pp. 347-352; Herz, J.M., Huang, H.V., Evolution of the Sindhis virus subgenomic mRNA promoter in cultured cells (1995) J. Virol., 69, pp. 7768-7774; Hilf, M.E., Karasev, A.V., Pappu, H.R., Gumpf, D.J., Niblett, C.L., Garnsey, S.M., Characterization of citrus tristeza virus subgenomic RNAs in infected tissue (1995) Virology, 208, pp. 576-582; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68, pp. 2615-2623; Karasev, A.V., Agranovsky, A.A., Rogov, V.V., Miroshnichenko, N.A., Dolja, V.V., Atabekov, J.G., Virion RNA of beet yellows closterovirus: Cell-free translation and some properties (1989) J. Gen. Virol., 70, pp. 241-245; Karasev, A.V., Boyko, V.P., Gowda, S., Nikolaeva, O.V., Hilf, M.E., Koonin, E.V., Niblett, C.L., Dawson, W.O., Complete sequence of the citrus tristeza virus RNA genome (1995) Virology, 208, pp. 511-520; Karasev, A.V., Nikolaeva, O.V., Mushegian, A.R., Lee, R.F., Dawson, W.O., Organization of the 3′-terminal half of beet yellow stunt virus genome and implications for the evolution of closteroviruses (1996) Virology, 221, pp. 199-207; Karasev, A.V., Hilf, M.E., Garnsey, S.M., Dawson, W.O., Transcriptional strategy of closteroviruses: Mapping the 5′ termini of the citrus tristeza virus subgenomic RNAs (1997) J. 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Virol., 69, pp. 5376-5382; Pruss, G., Ge, X., Shi, X.M., Carrington, J.C., Vance, V.B., Plant viral synergism: The potyviral genome encodes a broad-range pathogenicity enhancer that transactivates replication of heterologous viruses (1997) Plant Cell, 9, pp. 859-868; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Valverde, R.A., Nameth, S.T., Jordan, R.L., Analysis of double-stranded RNA for plant virus diagnosis (1990) Plant Dis., 74, pp. 255-258; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Van Marle, G., Luytjes, W., Van Der Most, R., Van Der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic RNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Dolja, V.V.; Dept. of Botany and Plant Pathology, Oregon State University, Cordley Hall 2082, Corvallis, OR 97331, United States; email: doljav@bcc.orst.edu",,,0022538X,,JOVIA,"9621048","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031777342
"Liu D.X., Shen S., Xu H.Y., Wang S.F.","8972667300;7403431806;55703819800;7410341717;","Proteolytic mapping of the coronavirus infectious bronchitis virus lb polyprotein: Evidence for the presence of four cleavage sites of the 3C-like proteinase and identification of two novel cleavage products",1998,"Virology","246","2",,"288","297",,33,"10.1006/viro.1998.9199","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032486611&doi=10.1006%2fviro.1998.9199&partnerID=40&md5=e21fb0a7f207705e08d1c8969b7b5b89","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Shen, S., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Wang, S.F., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","We have previously reported that the 3C-like proteinase of the coronavirus infectious bronchitis virus (IBV) is responsible for processing of the 1a and 1a/1b polyproteins to three mature products of 24, 10, and 100 kDa (Liu et al., 1994, 1997; Ng and Liu, 1998). The C-terminal cleavage site of the 100-kDa protein was defined to be the Q(891(1b))-S(892(1b)) dipeptide bond encoded by nucleotides 15,129 to 15,134 (Liu and Brown, 1995). In this report, other cleavage sites of the 3C-like proteinase in the polyprotein encoded by the ORF 1b region were mapped by coexpression, deletion, and site- directed mutagenesis studies. Using two ORF 1b-specific antisera, V58 and V17, three more Q-S(G) dipeptide bonds, encoded by nucleotides 16,929 to 16,934, 18,492 to 18,497, and 19,506 to 19,511, respectively, were demonstrated to be the cleavage sites of the 3C-like proteinase. Cleavage at these four positions would result in the release of four mature products with molecular masses of approximately 68, 58, 39, and 35 kDa. Among them, the 39- and 35-kDa proteins were specifically identified in IBV-infected cells. Taken together with the 100-kDa protein previously identified, these results suggest that the ORF 1b region of IBV mRNA1 may be able to encode five mature products.",,"virus protein; article; Coronavirus; gene expression; nonhuman; priority journal; protein degradation; protein expression; protein structure; site directed mutagenesis; Avian infectious bronchitis virus; Coronavirus; RNA viruses","Alonso-Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., Replication and morphogenesis of avian coronavirus in Vero cells and their inhibition by monensin (1984) Virus Res., 1, pp. 153-167; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. 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Virol., 78, pp. 2789-2794; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Lee, H-J., Shieh, C-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lim, K.P., Liu, D.X., Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87 kDa protein (1998) Virology, 245, pp. 303-312; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3c protein with the virion envelope (1991) Virology, 185, pp. 911-917; Liu, D.X., Brown, T.D.K., Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87-kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10 kDa polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Ng, L.F.P., Liu, D.X., Identification of a 24 kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites (1998) Virology, 243, pp. 388-395; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Location of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol., 50, pp. 22-29; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Liu, D.X.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; email: liudx@ima.org.sg",,"Academic Press Inc.",00426822,,VIRLA,"9657947","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032486611
"Ryzhikov A.B., Goncharova E.P., Bulychev L.E., Sergeev A.N., Dmitriev I.P., Pliasunov I.V., Kotliarov L.A.","7004762920;7005926297;6603793324;7201446581;7005895851;7801463132;57105943600;","Studying the possibility of respiratory immunization against tick-borne encephalitis [Izuchenie vozmozhnosti respiratornoi immunizatsii protiv kleshchevogo éntsefalita.]",1998,"Vestnik Rossiiskoi akademii meditsinskikh nauk / Rossiiskaia akademiia meditsinskikh nauk",,"4",,"17","20",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031608876&partnerID=40&md5=7210992a89146a7b4c80310f9d5d2d0d",,"Ryzhikov, A.B.; Goncharova, E.P.; Bulychev, L.E.; Sergeev, A.N.; Dmitriev, I.P.; Pliasunov, I.V.; Kotliarov, L.A.","There are known 3 likely mechanisms of virus conveyance into the central nervous system (CNS). These include hematogenic penetration, spread along the peripheral nerves, and the olfactory pathway which begins from the infected olfactory neuroepithelial cells. The possibility of viral spread into CNS via the olfactory pathway was shown for the representatives of togaviruses, herpesviruses, coronaviruses, rhabdoviruses, and for some others. This study suggests that the olfactory pathway of viral conveyance into CNS may be blocked by specific mucosal antibodies in the nasal mucosa. The recombinant TK- variant of WR vaccinia strain with inserted genes coding structural and nonstructural proteins of TBE virus is accumulated in the branches of the respiratory tract only while the parenteral vaccinia strain is detected in the brain regions, spleen, respiratory tract, and in blood. The protective activity of recombinant strain and inactivated TBE vaccine after mice immunization by escarification or intranasally, or subcutaneously was comparatively studied. The findings indicate that intranasal immunization by recombinant strain is the most protective against intraperitoneal challenge by TBE virus. The mucosal and humoral immune response that was induced by intranasal immunization seems to provide the highest levels of protection, which was experimentally observed.",,"recombinant vaccine; virus vaccine; animal; article; Bagg albino mouse; brain; comparative study; disease model; Flavivirus; immunology; intranasal drug administration; isolation and purification; mouse; pathogenicity; tick borne encephalitis; vaccination; virology; Administration, Intranasal; Animals; Brain; Disease Models, Animal; Encephalitis, Tick-Borne; Flavivirus; Mice; Mice, Inbred BALB C; Vaccination; Vaccines, Synthetic; Viral Vaccines",,"Ryzhikov, A.B.",,,08696047,,,"9633235","Russian","Vestn. Akad. Med. Nauk SSSR",Article,"Final",,Scopus,2-s2.0-0031608876
"Lachance C., Arbour N., Cashman N.R., Talbot P.J.","57210675095;6602762564;16169124200;7102670281;","Involvement of aminopeptidase N (CD13) in infection of human neural cells by human coronavirus 229E",1998,"Journal of Virology","72","8",,"6511","6519",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031926503&partnerID=40&md5=0525e621d7fc69b4b95187b4e057d584","Laboratory of Neuroimmunovirology, Armand-Frappier Institute, University of Quebec, Laval, Que. H7V 1B7, Canada; Montreal Neurol. Inst. and Hospital, Montreal, Que. H3A 2B4, Canada; Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Lachance, C., Laboratory of Neuroimmunovirology, Armand-Frappier Institute, University of Quebec, Laval, Que. H7V 1B7, Canada; Arbour, N., Laboratory of Neuroimmunovirology, Armand-Frappier Institute, University of Quebec, Laval, Que. H7V 1B7, Canada; Cashman, N.R., Montreal Neurol. Inst. and Hospital, Montreal, Que. H3A 2B4, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Armand-Frappier Institute, University of Quebec, Laval, Que. H7V 1B7, Canada, Laboratoire de Neuroimmunovirologie, Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Attachment to a cell surface receptor Can be a major determinant of virus tropism. Previous studies have shown that human respiratory coronavirus HCV-229E uses human aminopeptidase N (hAPN [CD13]) as its cellular receptor for infection of lung fibroblasts. Although human coronaviruses are recognized respiratory pathogens, occasional reports have suggested their possible neurotropism. We have previously shown that human neural cells, including glial cells in primary cultures, are susceptible to human coronavirus infection in vitro (A. Bonavia, N. Arbour, V. W. Yong, and P. J. Talbot, J. Virol. 71:800-806, 1997). However, the only reported expression of hAPN in the nervous system is at the level of nerve synapses. Therefore, we asked whether hAPN is utilized as a cellular receptor for infection of these human neural cell lines. Using flow cytometry, we were able to show the expression of hAPN on the surfaces of various human neuronal and glial cell lines that are susceptible to HCV-229E infection. An hAPN-specific monoclonal antibody (WM15), but not control antibody, inhibited the attachment of radiolabeled HCV-229E to astrocytic, neuronal, and oligodendrocytic cell lines. A correlation between the apparent amount of cell surface hAPN and the level of virus attachment was observed. Furthermore, the presence of WM15 inhibited virus infection of these cell lines, as detected by indirect immunofluorescence. These results indicate that hAPN (CD13) is expressed on neuronal and glial cell lines in vitro and serves as the receptor for infection by HCV-229E. This further strengthens the neurotropic potential of this human respiratory virus.",,"microsomal aminopeptidase; article; coronavirus; flow cytometry; glia cell; human; human cell; immunofluorescence; nerve cell; priority journal; virus adsorption; virus cell interaction; Antigens, CD13; Cell Line; Coronavirus; Coronavirus 229E, Human; Humans; Neurons; Tumor Cells, Cultured","Arbour, N., Talbot, P.J., Persistent infection of neural cell lines by human coronaviruses (1998) Adv. Exp. Med. Biol., 440, pp. 575-581; Arbour, N., Talbot, P.J., (1998), Unpublished data; Ashmun, R.A., Look, A.T., Metalloprotease activity of CD13/aminopeptidase N on the surface of human myeloid cells (1990) Blood, 75, pp. 462-469; Barnes, K., Kenny, A.J., Turner, A.J., Localization of aminopeptidase N and dipeptidyl peptidase IV in pig striatum and in neuronal and glial cell cultures (1994) Eur. J. 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Lett., 195, pp. 105-108; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Jouvenne, P., Talbot, P.J., Neurotropic potential of coronaviruses (1992) Med. Sci., 8, pp. 119-125; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) J. Gen. Virol., 77, pp. 2515-2521; Kolb, A.F., Hegyi, A., Siddell, S.G., Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N (1997) J. Gen. Virol., 78, pp. 2795-2802; Kunz, J., Krause, D., Kremer, M., Dermietzel, R., The 140-kDa protein of blood-brain barrier-associated pericytes is identical to aminopeptidase N (1994) J. 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Virol., 70, pp. 8669-8674; Vallee, B.L., Auld, D.S., Zinc coordination, function, and structure of zinc enzymes and other proteins (1990) Biochemistry, 29, pp. 5647-5659; Watt, C.M., Willard, H.F., The human aminopeptidase N gene: Isolation, chromosome localization, and DNA polymorphism analysis (1990) Hum. Genet., 6, pp. 651-654; Weingartl, H.M., Derbyshire, J.B., Evidence for a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs (1994) J. Virol., 68, pp. 7253-7259; Weiss, S.R., Coronaviruses SD and SK share extensive nucleotide homology with murine coronavirus MHV-A59, more than that shared between human and murine coronaviruses (1983) Virology, 126, pp. 669-677; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Zar, J.H., Multiple comparisons (1984) Biostatistical Analysis, 2nd Ed., pp. 185-205. , B. Kurtz (ed.), Prentice-Hall, Inc. Englewood Cliffs, N.J","Talbot, P.J.; Laboratoire de neuroimmunovirologie, Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,,0022538X,,JOVIA,"9658094","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031926503
"De Haan C.A.M., Kuo L., Masters P.S., Vennema H., Rottier P.J.M.","7003682643;7101601942;7006234572;7003697291;7006145490;","Coronavirus particle assembly: Primary structure requirements of the membrane protein",1998,"Journal of Virology","72","8",,"6838","6850",,107,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031950008&partnerID=40&md5=4209bd3640df1bc1800e5537d59d73ab","Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","De Haan, C.A.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Kuo, L., Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Masters, P.S., Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Vennema, H., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","Coronavirus-like particles morphologically similar to normal virions are assembled when genes encoding the vital membrane proteins M and E are coexpressed in eukaryotic cells. Using this envelope assembly assay, we have studied the primary sequence requirements for particle formation of the mouse hepatitis virus (MHV) M protein, the major protein of the coronavirion membrane. Our results show that each of the different domains of the protein is important. Mutations (deletions, insertions, point mutations) in the luminal domain, the transmembrane domains, the amphiphilic domain, or the carboxy-terminal domain had effects on the assembly of M into enveloped particles. Strikingly, the extreme carboxy-terminal residue is crucial. Deletion of this single residue abolished particle assembly almost completely; most substitutions were strongly inhibitory. Site-directed mutations in the carboxy terminus of M were also incorporated into the MHV genome by targeted recombination. The results supported a critical role for this domain of M in vital assembly, although the M carboxy terminus was more tolerant of alteration in the complete virion than in virus-like particles, likely because of the stabilization of virions by additional intermolecular interactions. Interestingly, glycosylation of M appeared not essential for assembly. Mutations in the luminal domain that abolished the normal O glycosylation of the protein or created an N-glycosylated form had no effect. Mutant M proteins unable to form virus-like particles were found to inhibit the budding of assembly-competent M in a concentration-dependent manner. However, assembly-competent M was able to rescue assembly-incompetent M when the latter was present in low amounts. These observations support the existence of interactions between M molecules that are thought to be the driving force in coronavirus envelope assembly.",,"membrane protein; amino terminal sequence; animal cell; article; carboxy terminal sequence; cell strain bhk; concentration response; glycosylation; murine hepatitis coronavirus; mutation; nonhuman; polyacrylamide gel electrophoresis; polymerase chain reaction; priority journal; protein structure; site directed mutagenesis; virus assembly; virus genome; virus particle; Amino Acid Sequence; Animals; Cell Line; Cricetinae; Cytoplasm; Glycosylation; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Rabbits; Structure-Activity Relationship; Viral Matrix Proteins; Virion; Virus Assembly","Allison, S.L., Stadler, K., Mandl, C.W., Kunz, C., Heinz, F.X., Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form (1995) J. Virol., 69, pp. 5816-5820; Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Arpin, N., Talbot, P.J., Molecular characterization of the 229E strain of human coronavirus (1990) Adv. Exp. Med. Biol., 276, pp. 73-80; Barth, B.U., Suomalainen, M., Liljeström, P., Garoff, H., Alphavirus assembly and entry: Role of the cytoplasmic tail of the E1 spike subunit (1992) J. Virol., 66, pp. 7560-7564; Bilsel, P., Castrucci, M.R., Kawaoka, Y., Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions (1993) J. 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Virol., 67, pp. 213-221; Zhao, H., Lindqvist, B., Garoff, H., Von Bonsdorff, C.-H., Liljeström, P., A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding (1994) EMBO J., 13, pp. 4204-4211; Zoller, M.J., Smith, M., Oligonucleotide-directed mutagenesis using M13-derived vectors: An efficient and general procedure for the production of point mutations in any fragment of DNA (1982) Nucleic Acids Res., 10, pp. 6487-6500","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands; email: P.Rottier@vetmic.dgk.ruu.nl",,,0022538X,,JOVIA,"9658133","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031950008
"Smith D.R., Nielsen P.R., Gadfield K.L., Saif L.J.","7410366749;7402902693;6508283179;7102226747;","Further validation of antibody-capture and antigen-capture enzyme-linked immunosorbent assays for determining exposure of cattle to bovine coronavirus",1998,"American Journal of Veterinary Research","59","8",,"956","960",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032133406&partnerID=40&md5=29f9098abba0a0e901f0e89423af9064","Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Dept. of Vet. and Biomed. Sciences, University of Nebraska, PO Box 830905, Lincoln, NE 68583-0905, United States","Smith, D.R., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States, Dept. of Vet. and Biomed. Sciences, University of Nebraska, PO Box 830905, Lincoln, NE 68583-0905, United States; Nielsen, P.R., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Gadfield, K.L., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States","Objective - To further validate an antibody-capture ELISA for measuring bovine coronavirus (BCV) exposure (antibody seroresponse) in cattle and to explain the apparent loss of sensitivity of a BCV antigen-capture ELISA when testing feces from adult versus neonatal cattle. Animals - 98 adult cows from herds with and without winter dysentery; 10 gnotobiotic or colostrum-deprived calves. Procedures - Results of an antibody-capture ELISA for BCV and a plaque reduction virus neutralization assay performed on paired serum samples from 24 cattle were compared with each other and with results of immunoelectron microscopy (IEM) of feces for BCV. For samples from 98 cattle, results of antibody-capture ELISA were compared with results of IEM. Calves were inoculated with feces ELISA-positive or IEM-positive for BCV and monitored for BCV infection. An ELISA was developed to detect BCV antigen-antibody complexes in feces and results were compared with results of an antigen-capture ELISA and IEM. Results - Antibody-capture ELISA results correlated with neutralization assay results, but agreed more closely with results of IEM. Calves became infected with BCV following inoculation with either ELISA-positive or ELISA-negative but IEM-positive feces. Results of the antigen-antibody ELISA correlated with results of IEM and the antigen-capture ELISA. Clinical Implications - In adult cattle, testing of paired serum samples by use of an antibody-capture ELISA may be a better indicator of recent BCV exposure than results of virus neutralization tests. Antigen-antibody binding in feces may interfere with results of antigen-capture ELISA for BCV.",,"virus antibody; virus antigen; animal; animal disease; antigen antibody complex; article; blood; cattle; cattle disease; comparative study; Coronavirus; enzyme linked immunosorbent assay; immunology; methodology; reproducibility; serodiagnosis; virus infection; Animals; Antibodies, Viral; Antigen-Antibody Complex; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; Neutralization Tests; Reproducibility of Results","Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Epidemiology of winter dysentery in dairy cattle: Assessment of herd-level causative agents and risk factors (1998) Am J Vet Res, 59, pp. xxx-xxx; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Cow-level risk factors for the occurrence of winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. xxx-xxx; Saif, L.J., Bohl, E.H., Kohler, E.M., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1995) J Vet Diagn Invest, 8, pp. 99-105; Crouch, C.F., Bielefeldt Ohman, H., Watts, T.C., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J. Gen Virol, 66, pp. 1489-1500; Crouch, C.F., Acres, S.D., Prevalence of rotavirus and coronavirus antigens in the feces of normal cows (1984) Can J Comp Med, 48, pp. 340-342; Saif, L.J., Heckert, R.A., Miller, K.L., Cell culture propagation of bovine coronavirus (1988) J Tiss Cult Methods, 11, pp. 139-145; Martin, S.W., The evaluation of tests (1977) Can J Comp Med, 41, pp. 19-25; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am J Vet Res, 57, pp. 48-53; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Saif, L.J., Coronavirus immunogens (1993) Vet Microbiol, 37, pp. 285-297; Shott, S., Regression (1991) J Am Vet Med Assoc, 198, pp. 798-801; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311","Saif, L.J.; Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, 1680 Madison Ave, Wooster, OH 44691, United States",,,00029645,,AJVRA,"9706198","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0032133406
"Smith D.R., Fedorka-Cray P.J., Mohan R., Brock K.V., Wittum T.E., Morley P.S., Hoblet K.H., Saif L.J.","7410366749;7005225892;7201546879;7005813632;7004009529;35269363700;7004524021;7102226747;","Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle",1998,"American Journal of Veterinary Research","59","8",,"994","1001",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032134585&partnerID=40&md5=d6a4669fa72e70c66974b31ed941159e","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States; Animal Disease Diagnostic Laboratory, 8995 E Main St, Reynoldsburg, OH 43068, United States; Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Dept. of Vet. and Biomed. Sciences, University of Nebraska, Lincoln, NE 68583-0905, United States; Department of Pathobiology, College of Veterinary Medicine, Auburn University, AL 36849-5519, United States; USDA, Agricultural Research Service, Russell Research Center, Athens, GA 30604, United States","Smith, D.R., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Dept. of Vet. and Biomed. Sciences, University of Nebraska, Lincoln, NE 68583-0905, United States; Fedorka-Cray, P.J., USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States, USDA, Agricultural Research Service, Russell Research Center, Athens, GA 30604, United States; Mohan, R., Animal Disease Diagnostic Laboratory, 8995 E Main St, Reynoldsburg, OH 43068, United States; Brock, K.V., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Department of Pathobiology, College of Veterinary Medicine, Auburn University, AL 36849-5519, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Morley, P.S., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Hoblet, K.H., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States","Objective - To test the association between exposure to bovine coronavirus (BCV) and outbreaks of winter dysentery (WD) in dairy herds and to examine other risk factors for outbreaks of WD in dairy herds. Animals - 12 dairy herds in Ohio affected with WD (case herds). For each case herd, 2 unaffected herds from the same area were concurrently used as control herds. Procedure - A case-control study was conducted, using herds as the unit of investigation. Multivariate logistic regression modeling was used to identify risk factors for contracting disease. Results - 4 factors appeared to increase a herd's risk for WD: increase in herd prevalence of adult cows that had a fourfold or more increase in BCV serum IgG antibody titer; increase in herd prevalence of adult cows that had a fourfold or more increase in bovine viral diarrhea virus (BVDV) titer; housing cattle in tie-stall or stanchion barns rather than free-stall facilities; and use of equipment to handle manure and subsequently handle feed. The adjusted population-attributable risk for these variables was 71, 43, 53, and 31%, respectively, and 99% overall, indicating that these variables had considerable impact on WD outbreaks for the study population. Conclusions and Clinical Relevance - In dairies in Ohio, recent herd exposure to BCV appeared to increase the risk for WD outbreaks. Some WD outbreaks might have been associated with acute BVDV infection. Certain housing and management practices may have increased the risk of an outbreak of WD.",,"virus antigen; animal; animal disease; animal salmonellosis; article; case control study; cattle; cattle disease; Coronavirus; dysentery; epidemic; feces; female; isolation and purification; multivariate analysis; prevalence; regression analysis; risk assessment; risk factor; season; species difference; United States; virology; virus infection; Animals; Antigens, Viral; Case-Control Studies; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Disease Outbreaks; Dysentery; Feces; Female; Multivariate Analysis; Ohio; Prevalence; Regression Analysis; Risk Assessment; Risk Factors; Salmonella Infections, Animal; Seasons; Species Specificity","Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Vet, 68, pp. 423-441; Kahrs, R.F., Scott, F.W., Hillman, R.B., Epidemiologic observations on bovine winter dysentery (1973) Bovine Pract, 8, pp. 36-39; Rollinson, D.H.L., Infectious diarrhoea of dairy cows (1948) Vet Rec, 60, pp. 191-192; Roberts, S.J., Winter dysentery in dairy cattle (1957) Cornell Vet, 47, pp. 372-388; Jones, F.S., Infectious diarrhea (winter scours) of cattle (1933) Cornell Vet, 23, pp. 117-122; Van Kruiningen, H.J., Castellano, V.P., Koopmans, M., A serologic investigation for coronavirus and Breda virus antibody in winter dysentery of dairy cattle in the northeastern United States (1992) J Vet Diagn Invest, 4, pp. 450-452; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Horner, G.W., Hunter, R., Kirkbride, C.A., A coronavirus-like agent present in faeces of cows with diarrhoea (1975) NZ Vet J, 23, p. 98; Takahashi, E., Inaba, Y., Sato, K., Epizootic diarrhoea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Van Kruiningen, H.J., Khairallah, L.H., Sassevelle, V.G., Calfhood coronavirus enterocolitis: A clue to the etiology of winter dysentery (1987) Vet Pathol, 24, pp. 564-567; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet Rec, 123, pp. 300-301; Fleetwood, A.J., Edwards, S., Foxell, P.W., Winter dysentery in adult dairy cattle (1989) Vet Rec, 125, pp. 553-554; Durham, P.J.K., Hassard, L.E., Armstrong, K.R., Coronavirus associated diarrhea (winter dysentery) in adult cattle (1989) Can Vet J, 30, pp. 825-827; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Alenius, S., Niskanen, R., Juntti, N., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet Scand, 32, pp. 163-170; Carnero, R., Costes, C., Schelcher, F., Entente hemorragique d'hiver en France: Confirmation de son association avec un coronavirus par microscopie electronique et par culture sur cellules HRT 18 (1992) 25th Conf Am Assoc Bovine Pract, 3, pp. 141-142. , Proceedings; Van Kruiningen, H.J., Castellano, V.P., Torres, A., Serologic evidence of coronavirus infection in New York and New England dairy cattle with winter dysentery (1991) J Vet Diagn Invest, 3, pp. 293-296; MacPherson, L.W., Bovine virus enteritis (winter dysentery) (1957) Can J Comp Med, 57, pp. 184-192; Scott, F.W., Kahrs, R.F., Campbell, S.G., Etiologic studies on bovine winter dysentery (1973) Bovine Pract, 8, pp. 40-43; Van Kruiningen, H.J., Heistand, L., Hill, D.L., Winter dysentery in dairy cattle: Recent findings (1985) Compend Contin Educ Pract Vet, 7, pp. S591-S599; Traven, M., Silvan, A., Larsson, B., Experimental infection with bovine coronavirus (BCV) in lactating cows: Clinical disease, viral excretion, interferon-α, and antibody response (1995) Bovine Pract, 29, pp. 64-65; Koopmans, M., Van Wuijckhuise-Sjouke, L., Schukken, Y.H., Association of diarrhea in cattle with torovirus infections on farms (1991) Am J Vet Res, 52, pp. 1769-1773; Traven, M., Sundberg, J., Larsson, R., Winter dysentery diagnosed by farmers in dairy herds in central Sweden: Incidence, clinical signs and protective immunity (1993) Vet Rec, 133, pp. 315-318; White, M.E., Schukken, Y.H., Tanksley, B., Space-time clustering of, and risk factors for, farmer-diagnosed winter dysentery in dairy cattle (1989) Can Vet J, 30, pp. 948-951; Jactel, B., Espinasse, J., Viso, M., An epidemiological study of winter dysentery in fifteen herds in France (1990) Vet Res Commun, 14, pp. 367-379; Ashfar, A., Dulac, G.C., Boufard, A., Application of peroxidase labeled antibody for detection of porcine IgG antibodies to hog cholera and bovine viral diarrhea virus (1989) J Virolog Methods, 23, pp. 253-262; Radwan, G.S., Brock, K.V., Hogan, J.S., Development of a PCR amplification assay as a screening test using bulk milk samples for identifying dairy herds infected with bovine viral diarrhea virus (1995) Vet Microbiol, 44, pp. 77-92; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Evaluation of cow-level risk factors for the development of winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 986-993; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1995) J Vet Diagn Invest, 8, pp. 99-105; Bruzzi, P., Green, S.B., Byar, D.P., Estimating the population attributable risk for multiple risk factors using case-control data (1985) J Epidemiol, 122, pp. 904-914; Schlesselman, J.J., Stolley, P.D., Sources of bias (1982) Case-control Studies, pp. 124-143. , New York: Oxford University Press; Martin, S.W., Shoukri, M., Thorburn, M.A., Evaluating the health status of herds based on tests applied to individuals (1992) Prev Vet Med, 14, pp. 33-43; Breslow, N.E., Day, N.E., Halvorsen, K.T., Estimation of multiple relative risk functions in matched case-control studies (1978) Am J Epidemiol, 108, pp. 299-307; Cornfield, J., A method of estimating comparative rates from clinical data. Applications to cancer of the lung, breast, and cervix (1951) J Natl Cancer Inst, 11, pp. 1269-1275; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Kahrs, R.F., A serological comparison of winter dysentery with bovine virus diarrhea and infectious bovine rhinotracheitis. Incidence of winter dysentery in vaccinated animals (1965) Cornell Vet, 55, pp. 505-511; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Baker, J.C., Bovine viral diarrhea virus: A review (1987) J Am Vet Med Assoc, 190, pp. 1449-1458; Schlesselman, J.J., Sample size (1982) Case-control Studies, pp. 144-145. , New York: Oxford University Press; Rothman, K.J., Causes (1976) Am J Epidemiol, 104, pp. 587-592","Saif, L.J.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States",,,00029645,,AJVRA,"9706203","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0032134585
"Quintana C., Marco S., Bonnet N., Risco C., Gutiérrez M.L., Guerrero A., Carrascosa J.L.","56213836100;57205474551;55400268900;56251715300;57207159302;57206223818;35481302900;","Optimization of phosphorus localization by EFTEM of nucleic acid containing structures",1998,"Micron","29","4",,"297","307",,9,"10.1016/S0968-4328(98)00011-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032146839&doi=10.1016%2fS0968-4328%2898%2900011-0&partnerID=40&md5=eb4b237c9c0bd5cf5d37c97f1570fb23","Inst. de Microelectronica de Madrid, CNM-CSIC, Parque Tecnológico de Madrid, Isaac Newton 8, E-28760 Madrid, Spain; Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, E-28049 Madrid, Spain; INSERM Unit 314, Université de Reims (LERI), 21 rue Clément Ader, F-51685 Reims Cedex, France; Departamento de Electrónica, Facultad de Físicas, Universidad Complutense de Madrid, 28040 Madrid, Spain","Quintana, C., Inst. de Microelectronica de Madrid, CNM-CSIC, Parque Tecnológico de Madrid, Isaac Newton 8, E-28760 Madrid, Spain; Marco, S., Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, E-28049 Madrid, Spain; Bonnet, N., INSERM Unit 314, Université de Reims (LERI), 21 rue Clément Ader, F-51685 Reims Cedex, France; Risco, C., Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, E-28049 Madrid, Spain; Gutiérrez, M.L., Departamento de Electrónica, Facultad de Físicas, Universidad Complutense de Madrid, 28040 Madrid, Spain; Guerrero, A., Departamento de Electrónica, Facultad de Físicas, Universidad Complutense de Madrid, 28040 Madrid, Spain; Carrascosa, J.L., Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, E-28049 Madrid, Spain","Energy Filtered Transmission Electron Microscopy (EFTEM) has been used to study nucleic acids localization in unstained thin sections of virus-infected cells. For this purpose, phosphorus maps (P-maps) have been obtained by applying the N-windows Egerton model for background subtraction from data acquired by a non-dedicated TEM Jeol 1200EXII equipped with a post-column PEELS Gatan 666-9000 and a Gatan Image Filter (GIF-100). To prevent possible errors in the evaluation of elemental maps and thus incorrect nucleic acid localization, we have studied different regions of swine testis (ST) cells with similar local density containing either high concentration of nucleic acids (condensed chromatin and ribosomes) or a very low concentration (mitochondria). Special care was taken to optimize the sample preparation conditions to avoid as much as possible the traditional artifacts derived from this source. Selection of the best set of preedge images for background fitting was also considered in order to produce 'true P-maps'. A new software for interactive processing of images series has been applied to estimate this set. Multivariate Statistical Analysis was used as a filtering tool to separate the 'useful information' present in the inelastic image series (characteristic signal) from the 'non-useful information' (noise and acquisition artifacts). The reconstitution of the original image series preserving mainly the useful information allowed the computation of P-maps with improved signal-to-noise ratio (SNR). This methodology has been applied to study the RNA content of maturation intermediate coronavirus particles found inside infected cells.","Coronaviruses; EFTEM; Elemental P-maps; Image processing","nucleic acid; phosphorus; virus RNA; animal; computer program; conference paper; electron microscopy; image processing; male; methodology; multivariate analysis; swine; testis; Transmissible gastroenteritis virus; ultrastructure; virology; Animals; Image Processing, Computer-Assisted; Male; Microscopy, Electron; Multivariate Analysis; Nucleic Acids; Phosphorus; RNA, Viral; Software; Swine; Testis; Transmissible gastroenteritis virus; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Adamson-Sharpe, K.M., Ottensmeyer, F.P., Spatial resolution and detection sensitivity in microanalysis by electron energy loss selected imaging (1981) J. Microsc., 122, pp. 309-314; Abolhassani-Dadras, S., Vazquez-Nin, G.H., Echevarria, O.M., Boutinard Rouelle-Rossier, V., Fakan, S., ESI in situ analysis of extrachromosomal RNP granules (1994) J. Microsc., 174, pp. 23-238; Abolhassani-Dadras, S., Vazquez-Nin, G.H., Echevarria, O.M., Fakan, S., Image-EELS for in situ estimation of phosphorus content of RNP granules (1996) J. Microsc., 183, pp. 215-222; Bazett-Jones, D.P., Ottensmeyer, F.P., Phosphorus distribution in the nucleosome (1981) Science, 211, pp. 169-170; Bazett-Jones, D.P., Empirical basis for phosphorus mapping and structure determination of DNA: Protein complexes by electron spectroscopic imaging (1993) Microbeam Anal. J., 2, pp. 69-79; Beniac, D.R., Czarnota, G.J., Rutherford, B.L., Ottensmeyer, F.P., Harauz, G., Three-dimensional architecture of Thermomyces lanuginosus small subunit ribosomal RNA (1997) Micron, 28, pp. 13-20; Beniac, D.R., Czarnota, G.J., Rutherford, B.L., Ottensmeyer, F.P., Harauz, G., The in situ architecture of E. coli ribosomal RNA derived from electron spectroscopic imaging and three-dimensional reconstruction (1997) J. Microsc., 188, pp. 24-35; Bonnet, N., Colliex, C., Mory, C., Tence, M., Developments in processing image sequences for elemental mapping (1988) Scanning Microsc. Suppl., 2, pp. 351-364; Bonnet, N., Simova, E., Lebonvallet, S., Kaplan, X., New applications of multivariate statistical analysis in spectroscopy and microscopy (1992) Ultramicroscopy, 40, pp. 1-11; Bonnet, N., Trebbia, P., Multi-dimensional data analysis and processing in electron-induced microanalysis (1992) Scanning Microscopy Suppl., 6, pp. 163-177; Bonnet, N., Processing of images and image series: A tutorial review for chemical microanalysis (1995) Mikrochim. Acta, 120, pp. 195-210; Bonnet, N., Zahm, J.M., Analysis of image sequences in fluorescence videomicroscopy of stationary objects (1998) Cytometry, 31, pp. 217-228; Bretaudiere, J.P., Frank, J., Reconstitution of molecular images analyzed by correspondence analysis: A tool for structural interpretation (1986) J. Microsc., 144, pp. 1-14; Colliex, C., Tence, M., Lefévre, E., Mory, C., Gu, H., Bouchet, D., Jeanguillaume, C., Electron energy loss spectrometry mapping (1994) Mikrochim. Acta, 114-115, pp. 71-87; Egerton, R.F., Inelastic scattering of 80 keV electrons in amorphous carbon (1975) Phil. Mag., 31, pp. 199-215; Le Furgey, A., Davilla, S.D., Kopf, D.A., Sommer, J.R., Ingram, P., Real-time quantitative elemental analysis and mapping: Microchemical imaging in cell physiology (1992) J. of Microsc., 165, pp. 191-223; Grief, C., Nermut, M.V., Hockley, D.J., A morphological and immunolabeling study of freeze-substituted human and simian immunodeficiency viruses (1994) Micron, 25, pp. 119-128; Harauz, G., Ottensmeyer, F.P., Nucleosome reconstitution via Phosphorus mapping (1984) Science, 226, pp. 936-940; Harauz, G., Evans, D.H., Beniac, D.R., Arsenault, A.L., Rutherford, B., Ottensmeyer, F.P., Electron spectroscopic imaging of encapsidated DNA in vaccinia virus (1995) Can. J. Microbiol., 41, pp. 889-894; Hofer, F., Warbichler, P., Grogger, W., Imaging of nanometer-sized precipitates in solids by electron spectroscopic imaging (1995) Ultramicroscopy, 59, pp. 15-31; Heng, Y.-M., Simon, G.T., Boublik, M., Ottensmeyer, F.P., Experimental ionization cross-sections of phophorus and calcium by electron spectroscopic imaging (1990) J. Microsc., 160, pp. 161-171; Jeanguillaume, C., Colliex, C., Trebbia, P., About the use of electron energy loss spectroscopy for chemical mapping of thin foils with high spacial resolution (1978) Ultramicroscopy, 3, pp. 137-142; Korn, A.P., Spitnik-Elson, P., Elson, D., Ottensmeyer, F.P., Specific visualization of ribosomal RNA in the intact ribosome by electron spectroscopic imaging (1983) Eur. J. Cell Biol., 31, pp. 334-340; Krivanek, O.L., Alexander, J.G., Dellby, N., Meyer, C.E., Design and first applications of a post-column imaging filter (1992) Microsc. Microanal. Microsctruct., 3, pp. 187-199; Krivanek, O.L., Friedman, S.L., Gubbens, A.J., Kraus, B., An imaging filter for biological applications (1995) Ultramicroscopy, 59, pp. 267-282; Krivanek, O.L., Kundmann, M.K., Kimoto, K., Spatial resolution in EFTEM elemental maps (1995) J. Microsc., 180, pp. 277-287; Leapman, R.D., Scanning transmission electron microscope (STEM) elemental mapping by electron energy loss spectroscopy (1986) Annals New York Acad. Sci., 483, pp. 327-338; Leapman, R.D., Hunt, J.A., Comparison of detection limits for EELS and EDXS (1991) Microsc. Microanal. Microstruct., 2, pp. 231-244; Olins, A.L., Olins, D.E., Bazett-Jones, D.P., Osmium ammine-B and electron spectroscopic imaging of ribonucleoproteins: Correlation of stain and phosphorus (1996) Biol. Cell, 87, pp. 143-147; Ottensmeyer, F.P., Elemental mapping by energy filtration: Advantages, limitations, compromises (1986) Annals New York Acad. Sci., 483, pp. 339-353; Ottensmeyer, F.P., Andrew, J.W., High-resolution microanalysis of biological specimens by electron energy loss spectroscopy and by electron spectroscopic imaging (1980) J. Ultrastruct. Res., 72, pp. 336-348; Ottensmeyer, F.P., Frankland, B.W., Spectral processing for parallel recording of elemental maps (1988) Scanning Microsc. Suppl., 2, pp. 343-350; Ottensmeyer, F.P., Andrews, A.L., Arsenault, Y.M., Heng, G.T., Simon, G.C., Weatherly, G.C., Elemental imaging by Electron Energy Loss Microscopy (1988) Scanning, 10, pp. 227-238; Özel, M., Pauli, G., Gelderblom, H.R., Electron spectroscopic imaging (ESI) of viruses using thin-section and immunolabeling preparations (1990) Ultramicroscopy, 32, pp. 35-41; Quintana, C., X-ray microanalysis of cell nuclei (1991) J. Electron Microsc. Techn., 18, pp. 411-423; Quintana, C., Cryofixation, cryosubstitution, cryoembedding for ultrastructural, immunocytochemical and microanalytical studies (1994) Micron, 25, pp. 63-99; Quintana, C., Bonnet, N., Improvements in biological X-ray microanalysis: Cryoembedding for specimen preparation and multivariate statistical analysis for data interpretation (1994) Scanning Microsc. Suppl., 8, pp. 83-99; Quintana, C., Bonnet, N., Multivariate statistical analysis applied to X-ray spectra and X-ray mapping of liver cell nuclei (1994) Scanning Microsc., 8, pp. 563-586; Quintana, C., Marco, S., Carrascosa, J.L., Evaluation of the analytical and imaging performances of a non-dedicated TEM equipped with a parallel electron energy loss spectrometer (PEELS) and image filter (IF) (1997) J. Trace Microprobe Techn., 15, pp. 175-188; Rattner, J.B., Bazett-Jones, D.P., Kinetochore structure: Electron spectroscopic imaging of the kinetochore (1989) J. Cell Biol., 108, pp. 1209-1219; Reimer, L., Messemer, W.M.R., Contrast in the electron spectroscopic imaging mode of a TEM. II. Z-ratio, structure-sensitive and phase contrast (1990) J. Microsc., 159, pp. 143-160; Risco, C., Antón, I.M., Suñé, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxyterminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Risco, C., Muntión, M., Enjuanes, L., Carrascosa, J.L., Two types of viral-related particles are found during TGEV morphogenesis (1998) J. Virol., 12, pp. 4022-4031; Tenailleau, H., Martin, J.M., A new background subtraction for low-energy EELS core edges (1992) J. of Microsc., 166, pp. 297-306; Shuman, H., Chang, C.F., Buhle, J.R., Somlyo, A.P., Electron energy spectroscopy: Quantitation and imaging (1986) Annals New York Acad. Sci., 483, pp. 295-310; Trebbia, P., Bonnet, N., EELS elemental mapping with unconventional methods. I. Theoretical basis: Image analysis with multivariate statistics and entropy concepts (1990) Ultramicroscopy, 34, pp. 165-178; Trebbia, P., Mory, C., EELS elemental mapping with unconventional methods. II. Applications to biological specimens (1990) Ultramicroscopy, 34, pp. 179-203; Vazquez-Nin, G.H., Abolhassani-Dadras, S., Echevarria, O.M., Boutinard Rouelle-Rossier, V., Fakan, S., Phosphorus distribution in perichromatin granules and surrounding nucleoplasm as visualized by electron spectroscopic imaging (1996) Biol. Cell, 87, pp. 171-177","Quintana, C.; Inst. de Microelectronica de Madrid, CNM-CSIC, Parque tecnologico de Madrid, Isaac Newton 8, E-28760 Madrid, Spain",,,09684328,,MCONE,"9744088","English","Micron",Conference Paper,"Final",,Scopus,2-s2.0-0032146839
"Smith D.R., Fedorka-Cray P.J., Mohan R., Brock K.V., Wittum T.E., Morley P.S., Hoblet K.H., Saif L.J.","7410366749;7005225892;7201546879;7005813632;7004009529;35269363700;7004524021;7102226747;","Evaluation of cow-level risk factors for the development of winter dysentery in dairy cattle",1998,"American Journal of Veterinary Research","59","8",,"986","993",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032134485&partnerID=40&md5=2e8e97ee106ff0cd7517d75aac22e449","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States; Animal Disease Diagnostic Laboratory, 8995 E Main St, Reynoldsburg, OH 43068, United States; Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Dept. of Vet. and Biomed. Sciences, University of Nebraska, Lincoln, NE 68583-0905, United States; Department of Pathobiology, College of Veterinary Medicine, Auburn University, AL 36849-5519, United States; USDA, Agricultural Research Service, Russell Research Center, Athens, GA 30604, United States","Smith, D.R., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Dept. of Vet. and Biomed. Sciences, University of Nebraska, Lincoln, NE 68583-0905, United States; Fedorka-Cray, P.J., USDA, Agricultural Research Service, National Animal Disease Center, PO Box 70, Ames, IA 50010, United States, USDA, Agricultural Research Service, Russell Research Center, Athens, GA 30604, United States; Mohan, R., Animal Disease Diagnostic Laboratory, 8995 E Main St, Reynoldsburg, OH 43068, United States; Brock, K.V., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States, Department of Pathobiology, College of Veterinary Medicine, Auburn University, AL 36849-5519, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Morley, P.S., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Hoblet, K.H., Dept. of Vet. Preventive Medicine, College of Veterinary Medicine, Ohio State University, Columbus, OH 43210, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States","Objective - To identify exposures to etiologic agents and to identify characteristics that could explain risk of disease for adult cattle in herds affected by winter dysentery (WD). Animals - 229 lactating and nonlactating adult cattle (125 case and 104 control cattle) selected from 12 dairy herds. Procedure - A case-control study, using multivariate conditional logistic regression and controlling for herd effects, was used to develop a model for risk factors associated with disease for each cow. Results - Likelihood of developing disease increased as the ELISA value for bovine coronavirus (BCV) antigen detectable in feces increased (odds ratio [OR] = 2.94 for each 0.100 increase in BCV antigen ELISA value). Pregnant cattle were less likely to develop WD, compared with nonpregnant herdmates. Cows with high acute BCV antibody titers that seroresponded had greater odds of developing disease, compared with seroresponding cows with low acute titers. However, among those cows that did not serorespond, high acute antibody titers were associated with lower odds of developing the disease. Conclusion - In herds affected by WD, ill cows were more likely to shed detectable amounts of BCV antigen in their feces, and pregnancy appeared to protect cattle from the disease. The measured interaction between BCV seroresponse and acute BCV antibody titer may be evidence of an immunopathologic condition, but could also have been attributable to dynamics of the ELISA or study design. Clinical Relevance - Factors that explained a cow's risk for illness within WD-affected herds may have been surrogate measures for that cow's nonspecific and BCV-specific immune profile.",,"virus antibody; virus antigen; animal; animal disease; article; blood; breeding; cattle; cattle disease; Coronavirus; dysentery; enzyme linked immunosorbent assay; feces; female; isolation and purification; lactation; physiology; pregnancy; risk; risk factor; season; virology; virus infection; Animals; Antibodies, Viral; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Dysentery; Enzyme-Linked Immunosorbent Assay; Feces; Female; Lactation; Odds Ratio; Pregnancy; Pregnancy, Animal; Risk Factors; Seasons","Kahrs, R.F., Scott, F.W., Hillman, R.B., Epidemiologic observations on bovine winter dysentery (1973) Bovine Pract, 8, pp. 36-39; Van Kruiningen, H.J., Heistand, L., Hill, D.L., Winter dysentery in dairy cattle: Recent findings (1985) Compend Contin Educ Pract Vet, 7, pp. S591-S599; Horner, G.W., Hunter, R., Kirkbride, C.A., A coronavirus-like agent present in faeces of cows with diarrhoea (1975) NZ Vet J, 23, p. 98; Takahashi, E., Inaba, Y., Sato, K., Epizootic diarrhoea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Van Kruiningen, H.J., Khairallah, L.H., Sassevelle, V.G., Calfhood coronavirus enterocolitis: A clue to the etiology of winter dysentery (1987) Vet Pathol, 24, pp. 564-567; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet Rec, 123, pp. 300-301; Fleetwood, A.J., Edwards, S., Foxell, P.W., Winter dysentery in adult dairy cattle (1989) Vet Rec, 125, pp. 553-554; Durham, P.J.K., Hassard, L.E., Armstrong, K.R., Coronavirus associated diarrhea (winter dysentery) in adult cattle (1989) Can Vet J, 30, pp. 825-827; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Alenius, S., Niskanen, R., Juntti, N., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet Scand, 32, pp. 163-170; Van Kruiningen, H.J., Castellano, V.P., Torres, A., Serologic evidence of coronavirus infection in New York and New England dairy cattle with winter dysentery (1991) J Vet Diagn Invent, 3, pp. 293-296; Van Kruiningen, H.J., Castellano, V.P., Koopmans, M., A serologic investigation for coronavirus and Breda virus antibody in winter dysentery of dairy cattle in the northeastern United States (1992) J Vet Diagn Invest, 4, pp. 450-452; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 994-1001; Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Vet, 68, pp. 423-441; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1995) J Vet Diagn Invest, 8, pp. 99-105; Saif, L.J., Bohl, E.H., Kohler, E.M., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Shott, S., Nonparametric statistics (1991) J Am Vet Med Assoc, 198, pp. 1126-1128; Martin, S.W., The evaluation of tests (1977) Can J Comp Med, 41, pp. 19-25; Schlesselman, J.J., Stolley, P.D., Sources of bias (1982) Case-control Studies, pp. 124-143. , New York: Oxford University Press; Spangler, L., Using and interpreting diagnostic tests (1992) Bovine Pract, 24, pp. 22-28; Crouch, C.F., Bielefeldt-Ohman, H., Watts, T.C., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; MacPherson, L.W., Bovine virus enteritis (winter dysentery) (1957) Can J Comp Med, 57, pp. 184-192; Scott, F.W., Kahrs, R.F., Campbell, S.G., Etiologic studies on bovine winter dysentery (1973) Bovine Pract, 8, pp. 40-43; Kleinbaum, D.G., Analysis of matched data using logistic regression (1994) Logistic Regression: A Self Learning Text, pp. 227-251. , New York: Springer-Verlag Inc; Curtis, C.R., Mauritsen, R.H., Salman, M.D., The enigma of herd: A comparison of different models to account for group effects in multiple logistic regression analysis (1988) Acta Vet Scand, 84, pp. 462-465; Roberts, S.J., Winter dysentery in dairy cattle (1957) Cornell Vet, 47, pp. 372-388; Rollinson, D.H.L., Infectious diarrhoea of dairy cows (1948) Vet Rec, 60, pp. 191-192; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet Microbiol, 36, pp. 1-37; Olsen, C.W., Corapi, W.V., Jacobson, R.H., Identification of antigenic sited mediating antibody-dependent enhancement of feline infectious peritonitis virus infectivity (1993) J Gen Virol, 74, pp. 745-749; Vennema, H., DeGroot, R.J., Harbour, D.A., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409; Yolken, R.H., Enzyme immunoassays for the detection of infectious antigens in body fluids: Current limitations and future prospects (1982) Rev Infect Dis, 4, pp. 35-68; Voller, A., Bidwell, D.E., Bartlett, A., (1979) The Enzyme Linked Immunosorbent Assay (ELISA), , Alexandria, Va: Dynatech Laboratories Inc; Edwards, M.J., Sier, A.M., Bovine epizootic diarrhoea in Western Australia (1960) Aust Vet J, 36, pp. 402-404; Rich, K.C., Siegel, J.N., Jennings, C., CD4+ lymphocytes in perinatal human immunodeficiency virus (HIV) infection: Evience for pregnancy induced depression in uninfected and HIV-infected women (1995) J Infect Dis, 172, pp. 1221-1227; Bhat, N.M., Mithal, A., Bieber, M.M., Human CD5+ lymphocytes (B-1 cells) decrease in peripheral blood during pregnancy (1995) J Reprod Immunol, 28, pp. 53-60; Crouch, S.P., Crocker, I.P., Fletcher, J., The effect of pregnancy on polymorphonuclear leukocyte function (1995) J Immunol, 155, pp. 5436-5443; Barriga, C., Rodriquez, A.B., Ortega, E., Increased phagocytic activity of polymorphonuclear leukocytes during pregnancy (1994) Eur J Obstet Gynecol Reprod Biol, 57, pp. 43-46; Shmagel, K.V., Increase of non-specific resistance of the body in normal pregnancy (1994) Akush Ginekol, 6, pp. 18-21; D'Alfonso, A., Picariello, A., Maccarone, D., Modification of immunologic parameters in physiological pregnancy (1993) Minerva Ginecol, 45, pp. 145-148; Moncharmont, P., Bonnard, M., Bernaud, J., Study of the immune profile of pregnant women (1992) Journal de Gynecologie, Obstetrique et Biologie de la Reproduction, 21, pp. 214-218","Saif, L.J.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States",,,00029645,,AJVRA,"9706202","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0032134485
"De La Fuente R., Garcia A., Ruiz-Santa-Quiteria J.A., Luzón M., Cid D., García S., Orden J.A., Gómez-Bautista M.","6507240946;54406740900;6701468772;6602384929;6701327952;7201561300;6506947568;6701627325;","Proportional morbidity rates of enteropathogens among diarrheic dairy calves in central Spain",1998,"Preventive Veterinary Medicine","36","2",,"145","152",,49,"10.1016/S0167-5877(98)00077-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032493524&doi=10.1016%2fS0167-5877%2898%2900077-4&partnerID=40&md5=b7ae3a1e1830a8399f5222eef329f018","Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain","De La Fuente, R., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Garcia, A., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Ruiz-Santa-Quiteria, J.A., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Luzón, M., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Cid, D., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; García, S., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Orden, J.A., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; Gómez-Bautista, M., Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain","Faecal samples from 218 diarrheic dairy calves in 65 dairy herds, selected by convenience, were screened for the presence of rotavirus, coronavirus, Cryptosporidium spp., F5+ Escherichia coli and Salmonella spp. Animals surveyed were from 1 to 30 days old. Cryptosporidium and rotavirus were the most commonly detected agents (52.3% and 42.7% of the samples positive, respectively). F5+ E. coli was detected in the faeces of 11.9% of the calves and bovine coronavirus was detected in the faeces of 7.3% of the calves. Salmonella spp. was only found in the faeces of two calves (0.9%). Mixed infections with two or more agents occurred in 28% of the calves. Concurrent infection of rotavirus and Cryptosporidium was found in 21.6% of the calves. Two tests were used for the detection of rotavirus (a commercial ELISA and PAGE), F5+ E. coli (ELISA and bacterial culture) and Cryptosporidium (ELISA and microscopy). The validity of the commercial ELISA for the detection of rotavirus, F5+ E. coli and Cryptosporidium in faeces from diarrheic calves was evaluated using PAGE, bacterial culture and microscopy as gold standard, respectively. The ELISA showed a very low sensitivity (28.6%) for the detection of F5+ E. coli compared to bacterial culture. © 1998 Elsevier Science B.V.","Cattle-microbiological diseases; Coronavirus; Cryptosporidium spp.; Escherichia coli; Neonatal calf diarrhea; Rotavirus; Salmonella spp.","animal; animal disease; animal salmonellosis; article; cattle; cattle disease; cryptosporidiosis; Cryptosporidium; diarrhea; Enterobacter infection; enzyme linked immunosorbent assay; microbiology; parasitology; Spain; virology; virus infection; Animals; Cattle; Cattle Diseases; Cryptosporidiosis; Cryptosporidium; Diarrhea; Enzyme-Linked Immunosorbent Assay; Escherichia coli Infections; Rotavirus Infections; Salmonella Infections, Animal; Spain","Bellinzoni, R.C., Blackball, J., Terzolo, H.R., Moreira, A.R., Auza, N., Mattion, N., Micheo, G.L., Scodeller, E.A., Microbiology of diarrhoea in young beef and dairy calves in Argentina (1990) Rev. Argent. Microbiol., 22, pp. 130-137; Bulgin, M.S., Anderson, B.C., Ward, A.C.S., Evermann, J.F., Infectious agents associated with neonatal calf disease in southwestern Idaho and eastern Oregon (1982) J. Am. Vet. Med. Assoc., 180, pp. 1222-1226; Casemore, D.P., Armstrong, M., Sands, R.L., Laboratory diagnosis of cryptosporidiosis (1985) J. Clin. Pathol., 38, pp. 1337-1341; Contrepois, M., Martel, J.L., Bordas, C., Hayers, F., Millet, A., Ramisse, J., Sendral, R., Fréquence des pili FY et K99 parmi des souches de Escherichia coli isolées de veaux diarrhéiques en France (1985) Ann. Rech. Vét., 16, pp. 25-28; Heine, J., Eine einfache Nachweismethode für Krytosporidiosen im Kot Zentralbl (1982) Veterinaermed. Reihe B, 29, pp. 324-327; Herring, A.J., Inglis, N.F., Ojeh, C.K., Snodgrass, D.R., Menzies, J.D., Rapid diagnosis of rotavirus infection by direct detection of viral nucleic acid in silver-stained polyacrylamide gels (1982) J. Clin. Microbiol., 16, pp. 473-477; Martin, L.A., Follet, E.A.C., An assessment of the sensitivity of three methods for the detection of rotavirus (1987) J. Virol. Methods, 16, pp. 39-44; McDonough, S.P., Stull, C.L., Osburn, B.I., Enteric pathogens in intensively reared veal calves (1994) Am. J. Vet. Res., 55, pp. 1516-1520; Morin, M., Lariviee, S., Lallier, R., Begin, M.E., Ethier, R., Roy, R.S., Tremblay, A., Diarrhoea of newborn calves. II. Agents responsible for the disease on Quebec dairy farms (1980) Med. Vet. Quebec., 10, pp. 60-65; Morris, J.A., Thorns, C.J., Wells, G.A.H., Scott, A.C., Sojka, W.J., The production of F41 fimbriae by piglet strains of enterotoxigenic Escherichia coli that lack K88, K99 and 987P fimbriae (1983) J. Gen. Microbiol., 129, pp. 2753-2759; Radostits, O.M., Leslie, K.E., Fetrow, J., Health management of dairy calves (1994) Herd Health Food Animal Production Medicine. 2nd Edn., pp. 184-213. , Saunders, Philadelphia; Reynolds, D.J., Morgan, J.H., Chanter, N., Jones, P.W., Bridger, J.C., Debney, T.G., Bunch, K.J., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec., 119, pp. 34-39; Runnels, P.L., Moon, H.W., Matthews, P.J., Whipp, S.C., Woode, G.N., Effect of microbial and host variables on the interaction of rotavirus and Escherichia coli infections in gnotobiotic calves (1986) Am. J. Vet. Res., 47, pp. 1542-1550; Sherwood, D., Snodgrass, D.R., Lawson, G.H.K., Prevalence of enterotoxigenic Escherichia coli in calves in Scotland and northern England (1983) Vet. Rec., 113, pp. 208-212; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Adv. Vet. Sci. Comp. Med., 29, pp. 103-206; Waltner-Toews, D., Martin, S.W., Meek, A.H., An epidemiological study of selected calf pathogens on Holstein dairy farms in southwestern Ontario (1986) Can. J. Vet. Res., 50, pp. 307-313; Waltner-Toews, D., Martin, S.W., Meek, A.H., The effect of early calfhood status on survivorship and age at first calving (1986) Can. J. Vet. Res., 50, pp. 314-317; Warnick, L.D., Erb, H.N., White, M.E., Lack of association between calf morbidity and subsequent first lactation milk production in 25 New York holstein (1995) J. Dairy Sci., 78, pp. 2819-2830; Zrelli, M., Messadi, L., Ben Miled, L., Jemli, M.H., Haddad, N., Les agents infectieux associés aux diarrhées néonatales du veau en Tunisio (1990) Revue Méd. Vét., 141, pp. 861-872","De La Fuente, R.; Depto. Patología Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; email: rifuente@eucmax.sim.ucm.es",,"Elsevier",01675877,,PVMEE,"9762735","English","Prev. Vet. Med.",Article,"Final",,Scopus,2-s2.0-0032493524
"Pitkaranta A., Virolainen A., Jero J., Arruda E., Hayden F.G.","7003331729;6701758010;7004052788;7004935664;7103233446;","Detection of rhinovirus, respiratory syncytial virus, and coronavirus infections in acute otitis media by reverse transcriptase polymerase chain reaction",1998,"Pediatrics","102","2 I",,"291","295",,194,"10.1542/peds.102.2.291","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031904440&doi=10.1542%2fpeds.102.2.291&partnerID=40&md5=cebea8f8e5c68ad81152b071c74b2e91","University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Pitkaranta, A., University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States; Virolainen, A., University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States; Jero, J., University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States; Arruda, E., University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States; Hayden, F.G., University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States","Objective. To determine the frequencies of human rhinovirus (HRV), respiratory syncytial virus (RSV), and coronavirus (HCV) infection in children with acute otitis media (AOM). Methods. Middle ear fluids (MEF) collected by tympanocentesis and nasopharyngeal aspirates (NPA) at the time of the AOM diagnosis were examined by reverse transcriptase polymerase chain reaction for HRV, RSV, and HCV RNA. Patients. Ninety-two children aged 3 months to 7 years during a 1-year period. Results. Virus RNA was detected in a total of 69 children (75%) and in 44 MEF samples (48%) and 57 NPA samples (62%) at the time of AOM diagnosis. HRV RNA was detected in both MEF and NPA in 18 (20%), in MEF alone in 4 (4%), and in NPA alone in 10 (11%). RSV was detected in both MEF and NPA in 12 (13%), in MEF alone in 5 (5%), and in NPA alone in 9 (10%). HCV RNA was detected in both MEF and NPA in 5 (5%), in MEF alone in 2 (2%), and in NPA alone in 9 (10%). Dual viral infections were detected in 5% of children. HRV and RSV were detected simultaneously in 2 MEF samples and in 2 NPA samples; RSV and HCV were detected in 1 NPA sample. Bacterial pathogens were detected in 56 (62%) MEF from 91 children. Viral RNA was detected in 20 (57%) MEF of 35 bacteria-negative and in 25 (45%) of 56 bacteria-positive MEF samples. No important differences in the risk of treatment failure, relapse, or occurrence of late secretory otitis media were noted between children with virus-positive and virus-negative MEF aspirates. Conclusion. These findings highlight the importance of common respiratory viruses, particularly HRV and RSV, in predisposing to and causing AOM in young children.","Acute otitis media; Coronavirus; Respiratory syncytial virus; Rhinovirus; RT-PCR","article; bacterium culture; child; coronavirus; demography; diagnostic accuracy; diagnostic value; disease association; disease predisposition; human; infant; major clinical study; middle ear; myringotomy; otitis media; priority journal; respiratory syncytial pneumovirus; reverse transcription polymerase chain reaction; rhinovirus; treatment planning; virus infection; Acute Disease; Bacterial Infections; Child; Child, Preschool; Common Cold; Coronaviridae Infections; Coronavirus; Diagnosis, Differential; Ear, Middle; Female; Humans; Infant; Male; Nasopharynx; Otitis Media; Picornaviridae Infections; Polymerase Chain Reaction; Respiratory Syncytial Virus Infections; Respiratory Syncytial Virus, Human; Rhinovirus; RNA, Viral; Treatment Failure",,"Hayden, F.G.; University of Virginia, Health Sciences Center, Box 473, Charlottesville, VA 22908, United States",,,00314005,,PEDIA,"9685428","English","Pediatrics",Article,"Final",,Scopus,2-s2.0-0031904440
"Walker P.G., Constable P.D., Morin D.E., Drackley J.K., Foreman J.H., Thurmon J.C.","7403666712;7005433243;7101955868;7004504934;7102204728;7006949002;","A reliable, practical, and economical protocol for inducing diarrhea and severe dehydration in the neonatal calf",1998,"Canadian Journal of Veterinary Research","62","3",,"205","213",,36,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031828904&partnerID=40&md5=7368672cab5a8cc81f0ce8b77dee711a","College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States; Coll. Agric.. Consum./Environ. Sci., Department of Animal Sciences, University of Illinois, Urbana, IL 61802, United States","Walker, P.G., College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States; Constable, P.D., College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States; Morin, D.E., College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States; Drackley, J.K., Coll. Agric.. Consum./Environ. Sci., Department of Animal Sciences, University of Illinois, Urbana, IL 61802, United States; Foreman, J.H., College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States; Thurmon, J.C., College of Veterinary Medicine, Dept. of Vet. Clinical Medicine, University of Illinois, Urbana, IL 61802, United States","Fifteen healthy, colostrum-fed, male dairy calves, aged 2 to 7 d were used in a study to develop a diarrhea protocol for neonatal calves that is reliable, practical, and economical. After instrumentation and recording baseline data, diarrhea and dehydration were induced by administering milk replacer [16.5 mL/kg of body weight (BW), PO], sucrose (2 g/kg in a 20 % aqueous solution, PO), spironolactone and hydrochlorothiazide (1 mg/kg, PO) every 8 h, and furosemide (2 mg/kg, IM, q6h). Calves were administered sucrose and diuretic agents for 48 h to induce diarrhea and severe dehydration. Clinical changes after 48 h were severe watery diarrhea, severe depression, and marked dehydration (mean, 14 % BW loss). Cardiac output, stroke volume, mean central venous pressure, plasma volume, thiocyanate space, blood pH and bicarbonate concentration, base excess, serum chloride concentration, and fetlock temperature were decreased. Plasma lactate concentration, hematocrit, and serum potassium, creatinine, phosphorus, total protein and albumin concentrations were increased. This noninfectious calf diarrhea protocol has a 100 % response rate, while providing a consistent and predictable hypovolemic state with diarrhea that reflects most of the clinico-pathologic changes observed in osmotic/maldigestive diarrhea caused by infection with rotavirus, coronavirus or cryptosporidia. Limitations of the protocol, when compared to infectious diarrhea models, include failure to induce a severe metabolic acidosis, absence of hyponatremia, renal instead of enteric loss of chloride, renal as well as enteric loss of free water, absence of profound clinical depression and suspected differences in the morphologic and functional effect on intestinal epithelium. Despite these differences, the sucrose/diuretic protocol should be useful in the initial screening of new treatment modalities for calf diarrhea. To confirm their efficacy, the most effective treatment methods should then be examined in calves with naturally-acquired diarrhea.",,"albumin; bicarbonate; chloride; furosemide; hydrochlorothiazide; lactic acid; phosphorus; potassium; spironolactone; sucrose; thiocyanate; animal experiment; animal model; article; blood ph; body temperature; cattle disease; central venous pressure; colostrum; controlled study; dehydration; diarrhea; economic aspect; heart output; heart stroke volume; hematocrit; lactate blood level; male; nonhuman; plasma volume; reliability; Animals; Animals, Newborn; Blood Glucose; Blood Proteins; Body Temperature; Body Weight; Cattle; Colostrum; Dehydration; Diarrhea; Electrolytes; Feces; Furosemide; Hemodynamic Processes; Hydrochlorothiazide; Male; Spironolactone; Sucrose","(1996) Part II: Changes in the U.S. Dairy Industry: 1991-1996, pp. 17-21. , Fort Collins. Colorado: Veterinary Services. NAHMS. Animal and Plant Inspection Service. US Dept of Agriculture; (1994) Pan III- Beef Cow/calf Health & Health Management, p. 37. , Fort Collins. Colorado: Veterinary Services. NAHMS. Animal and Plant Inspection Service. US Dept of Agriculture; Logan, E.F., Penhale, W.J., Studies on the immunity of the calf to Colibacillosis. V. the experimental reproduction of enteric colibacillosis (1972) Vet Rec, 91, pp. 419-423; Bywater, R.J., Logan, E.F., The site and characteristics of interstitial water and electrolyte loss in Escherichia coli-Induced diarrhea in calves (1974) J Comp Path, 84, pp. 599-610; Bywater, R.J., Evaluation of an oral glucose-glycine-electrolyte formulation and amoxicilin for treatment of diarrhea in calves (1977) Am J Vet Res, 38, pp. 1983-1987; Logan, E.F., Pearson, G.R., Mcnulty, M.S., Studies on the immunity of the calf to colibacillosis. VII: The experimental reproduction of enteric colibacillosis in colostrum-fed calves (1977) Vet Rec, 101, pp. 443-446; Dupe, R.J., Goddard, M.E., Bywater, R.J., A comparison of two oral rehydration solutions in experimental models of dehydration and diarrhoea in calves (1989) Vet Rec, 125, pp. 620-624; Guard, C.L., Tennant, B.C., Rehydration of neonatal calves with experimental colibacillosis: Oral v. intravenous fluids (1986) 14h World Congr Dis Cattle, pp. 356-361. , August 26-29. 1986, Dublin. Ireland. Ballsbridge, Ireland: Univ. College; Heath, S.E., Naylor, J.M., Guedo, B.L., Petrie, L., Rousseaux, C.G., Radostits, O.M., The effects of feeding milk to diarrheic calves supplemented with oral electrolytes (1989) Can J Vet Res, 53, pp. 477-485; Tzipori, S., Smith, M., Halpin, C., Angus, K.W., Sherwood, D., Campbell, I., Experimental cryptosporidiosis in calves: Clinical manifestations and pathologic findings (1983) Vet Rec, 112, pp. 116-120; Harp, J.A., Woodmansee, D.B., Moon, H.W., Effects of colostral antibody on susceptibility of calves to Cryptosporidium parvum infection (1989) Am J Vet Res, 50, pp. 2117-2119; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Lewis, L.D., Phillips, R.W., Pathophysiologic changes due to coronavirus-induced diarrhea in the calf (1978) J Am Vet Med Assoc, 173, pp. 636-642; Phillips, R.W., Lewis, L.D., Viral induced changes in intestinal transport and resultant body fluid alterations in neonatal calves (1973) Ann Rech Vétér, 4, pp. 87-98; Booth, A.J., Naylor, J.M., Correction of metabolic acidosis in diarrheal calves by oral administration of electrolyte solutions with or without bicarbonate (1987) J Am Vet Med Assoc, 191, pp. 62-68; Naylor, J.M., Petrie, L., Rodriguez, M.I., Skilnick, P., A comparison of three oral electrolyte solutions in the treatment of diarrheic calves (1990) Can Vet J, 31, pp. 753-760; Velu, J.G., Kendall, K.A., Gardner, K.E., Utilization of various sugars by the young dairy calf (1960) J Dairy Sci, 43, pp. 546-552; Huber, J.T., Jacobson, N.L., Mcgilliard, A.D., Allen, R.S., Utilization of carbohydrates introduced directly into the omaso-abomasal area of the stomach of cattle of various ages (1961) J Dairy Sci, 44, pp. 321-330; Lewis, L.D., Phillips, R.W., Water and electrolyte losses in neonatal calves with acute diarrhea: A complete balance study (1972) Cornell Vet, pp. 596-607; Phillips, R.W., Lewis, L.D., Knox, K.L., Alterations in body water turnover and distribution in neonatal calves with acute diarrhea (1971) Ann NY Acad Sci, 176, pp. 231-243; 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Pt. II: The role of oxygen and potassium (1967) Br Vet J, 23, pp. 4-7; Dalton, R.G., Fisher, E.W., Mcintyre, W.I., Changes in blood chemistry, body weight and haematocrit of calves affected with neonatal diarrhea (1965) Br Vet J, 121, pp. 34-41; Phillips, R.W., Knox, K.L., Diarrheic acidosis in calves (1969) J Comp Lab Med, 3, pp. 1-3; Tennant, B., Harrold, D., Reinaguerra, M., Physiologic and metabolic factors in the pathogenesis of neonatal enteric infections of calves (1972) J Am Vet Med Assoc, 161, pp. 993-1007; Phillips, R.W., Case, G.L., Altered metabolism, acute shock, and therapeutic response in a calf with severe coronavirus-induced diarrhea (1980) Am J Vet Res, 41, pp. 1039-1044; Lewis, L.D., Phillips, R.W., Elliott, C.D., Changes in plasma glucose and lactate concentrations and enzyme activities in the neonatal calf with diarrhea (1975) Am J Vet Res, 36, pp. 413-416; Fayet, J.C., Plasma and fecal osmolality, water kinetics and body fluid compartments in neonatal calves with diarrhea (1971) Br Vet J, 127, pp. 37-43; Naylor, J.M., Severity and nature of acidosis in diarrheic calves over and under one week of age (1987) Can Vet J, 28, pp. 168-173; Rasková, H., Sechser, T., Vanecek, J., Polak, L., Treu, M., Muzik, J., Sklenar, V., Matejovska, V., Neonatal Escherichia coli infections in calves I. Appraisal of rehydration (1976) Zbl Vet Med, 23, pp. 131-142; Naylor, J.M., A retrospective study of the relationship between clinical signs and severity of acidosis in diarrheic calves (1989) Can Vet J, 30, pp. 577-580; Chaudry, I.H., Cellular mechanisms in shock and ischemia and their correction (1983) Am J Physiol, 14, pp. R117-R134; Jones, R., Phillips, R.W., Cleek, J.L., Hyperosmotic oral replacement fluids for diarrheic calves (1984) J Am Vet Med Assoc, 184, pp. 1501-1505; Dupe, R.J., Bywater, R.J., Goddard, M.E., A hypertonic infusion in the treatment of experimental shock in calves and clinical shock in dogs and cats (1993) Vet Rec, 133, pp. 585-590; Tennant, B., Reina-Guerra, H.M., Hypoglycemia in neonatal calves associated with acute diarrhea Cornell Vet, 1968, pp. 136-146; Fisher, E.W., Hydrogen ion and electrolyte disturbances in neonatal calf diarrhea (1971) Ann NY Acad Sci, 176, pp. 223-230","Walker, P.G.; College of Veterinary Medicine, Dept. of Veterinary Clinical Med., University of Illinois, Urbana, IL 61802, United States",,,08309000,,CJVRE,"9684050","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0031828904
"Maeda A., An S., Makino S.","7201779383;55107136200;7403067550;","Importance of coronavirus negative-strand genomic RNA synthesis prior to subgenomic RNA transcription",1998,"Virus Research","57","1",,"35","42",,3,"10.1016/S0168-1702(98)00090-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031759059&doi=10.1016%2fS0168-1702%2898%2900090-2&partnerID=40&md5=ae999b7ff02a1ab1adf07673f630221c","Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","Maeda, A., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; An, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","The (-)-strand viral RNAs that result from after infection of cells with coronaviruses, which possess RNA genomes of message polarity, are genomic-sized and subgenomic-sized. Each of the (-)-strand subgenomic RNAs corresponds in size to each of the subgenomic mRNA species that are made in infected cells. We tested whether (-)-strand subgenomic RNAs might initially be synthesized from the input single-stranded (+)-strand genomic RNA prior to the production of subgenomic mRNAs. We used a mouse hepatitis virus (MHV) defective interfering (DI) RNA, from which subgenomic RNA was produced in DI RNA-replicating cells, because this DI RNA had a functional MHV intergenic region inserted in its interior. MHV samples containing the DI particles were irradiated with UV-light and then superinfected into cells that had been infected with MHV 4 h prior to superinfection. Northern blot analysis of intracellular RNAs that were extracted 3 h after superinfection showed that genomic DI RNA and subgenomic DI RNA had similar UV-target sizes, indicating that (-)-strand genomic DI RNA synthesis from input genomic DI RNA probably occurred prior to the subgenomic-size DI RNA synthesis. We discuss why, in the course of coronavirus transcription, (-)-strand genomic-length coronavirus RNA synthesis might occur before subgenomic-sized RNAs of either polarity are made. Copyright (C) 1998 Elsevier Science B.V.","Coronavirus; Negative-strand RNA; RNA transcription","virus RNA; article; controlled study; coronavirus; hepatitis virus; messenger RNA synthesis; nonhuman; northern blotting; priority journal; ultraviolet radiation; Animals; Mice; Murine hepatitis virus; RNA, Viral; Transcription, Genetic; Coronavirus; Murine hepatitis virus; Murine hepatitis virus strain 4","Adams, R.H., Brown, D.T., BHK cells expressing sindbis virus-induced homologous interference allow the translation of nonstructural genes of the superinfecting virus (1985) J. Virol., 54, pp. 351-357; An, S., Maeda, A., Makino, S., Coronavirus transcription early in infection (1998) J. Virol., , in press; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Den Boon, J.A., Spaan, W.J.M., Snijder, E.J., Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies (1995) Virology, 213, pp. 364-372; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Ges. Virusforch., 44, pp. 298-302; Jacobs, L., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., The synthesis of the subgenomic mRNAs of mouse hepatitis virus is initiated independently: Evidence from UV transcription mapping (1981) J. Virol., 39, pp. 401-406; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effect of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Kim, Y.-N., Makino, S., Characterization of a murine coronavirus defective interfering RNa internal cis-acting replication signal (1995) J. Virol., 69, pp. 4963-4971; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: mRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol., 46, pp. 1027-1033; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Liao, C.-L., Lai, M.M.C., Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J. 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Virol., 70, pp. 7236-7240; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J. Virol., 64, pp. 6045-6053; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis virus, strain A59 (1989) Virology, 171, pp. 141-148; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. 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Virol., 42, pp. 755-759; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′-end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Yokomori, K., Banner, L.R., Lai, M.M.C., Coronavirus mRNA transcription: UV light transcription mapping studies suggest an early requirement for a genomic-length template (1992) J. Virol., 66, pp. 4671-4678","Makino, S.; Department of Microbiology, Institute Cellular/Molecular Biology, University of Texas, Austin, TX 78712-1095, United States; email: makino@mail.utexas.edu",,,01681702,,VIRED,"9833884","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0031759059
"Zelus B.D., Wessner D.R., Williams R.K., Pensiero M.N., Phibbs F.T., Desouza M., Dveksler G.S., Holmes K.V.","6602571243;6603847933;7409603207;6701528751;56321579000;7003446340;6603790777;7201657724;","Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities",1998,"Journal of Virology","72","9",,"7237","7244",,33,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031816799&partnerID=40&md5=70ccef57a198bc53fa61e03b25f629bf","Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States; Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Medical Virology Section, Laboratory of Clinical Investigation, NIAID, Bethesda, MD 20892, United States; Genetic Therapy Inc., Gaithersburg, MD 20878, United States; H. M. Jackson Foundation, AFRIMS, Bangkok, Thailand","Zelus, B.D., Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States; Wessner, D.R., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Williams, R.K., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Medical Virology Section, Laboratory of Clinical Investigation, NIAID, Bethesda, MD 20892, United States; Pensiero, M.N., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Genetic Therapy Inc., Gaithersburg, MD 20878, United States; Phibbs, F.T., Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States; Desouza, M., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, H. M. Jackson Foundation, AFRIMS, Bangkok, Thailand; Dveksler, G.S., Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States; Holmes, K.V., Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States, Department of Pathology, Uniformed Serv. Univ. Hlth. Sci., Bethesda, MD 20814, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Mouse hepatitis virus receptor (MHVR) is a murine biliary glycoprotein (Bgp1a). Purified, soluble MHVR expressed from a recombinant vaccinia virus neutralized the infectivity of the A59 strain of mouse hepatitis virus (MHV- A59) in a concentration-dependent manner. Several anchored murine Bgps in addition to MHVR can also function as MHV-A59 receptors when expressed at high levels in nonmurine cells. To investigate the interactions of these alternative MHVR glycoproteins with MHV, we expressed and purified to apparent homogeneity the extracellular domains of several murine Bgps as soluble, six-histidine-tagged glycoproteins, using a baculovirus expression system. These include MHVR isoforms containing four or two extracellular domains and the corresponding Bgp1b glycoproteins from MHV-resistant SJL/J mice, as well as Bgp2 and truncation mutants of MHVR and Bgp1b comprised of the first two immunoglobulin-like domains. The soluble four-domain MHVR glycoprotein (sMHVR[1-4]) had fourfold more MHV-A59 neutralizing activity than the corresponding soluble Bgp1b (sBgp1b) glycoprotein and at least 1,000-fold more neutralizing activity than sBgp2. Although virus binds to the N-terminal domain (domain 1), soluble truncation mutants of MHVR and Bgp1b containing only domains 1 and 2 bound virus poorly and had 10- and 300-fold less MHV-A59 neutralizing activity than the corresponding four-domain glycoproteins. In contrast, the soluble MHVR glycoprotein containing domains 1 and 4 (sMHVR[1,4]) had as much neutralizing activity as the four-domain glycoprotein, sMHVR[1-4]. Thus, the virus neutralizing activity of MHVR domain 1 appears to be enhanced by domain 4. The sBgp1b[1-4] glycoprotein had 500-fold less neutralizing activity for MHV-JHM than for MHV-A59. Thus, MHV strains with differences in S-glycoprotein sequence, tissue tropism, and virulence can differ in the ability to utilize the various murine Bgps as receptors.",,"glycoprotein; recombinant protein; virus receptor; article; baculovirus; coronavirus; hepatitis virus; nonhuman; priority journal; protein expression; protein purification; vaccinia virus; virus neutralization; virus recombinant; 3T3 Cells; Animals; Antigens, CD; Baculoviridae; Cell Adhesion Molecules; Cell Line; Cell Line, Transformed; Cercopithecus aethiops; Genetic Vectors; Glycoproteins; Histidine; Mice; Murine hepatitis virus; Neutralization Tests; Receptors, Virus; Recombinant Fusion Proteins; Solubility; Spodoptera; Vaccinia virus; Vero Cells","Asanka, M., Lai, M.M., Cell fusion studies identified multiple Cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Banfield, M.J., King, D.J., Mountain, A., Brady, R.L., VL:VH domain rotations in engineered antibodies: Crystal structures of the Fab agments from two murine antitumor antibodies and their engineered human constructs (1997) Proteins, 29, pp. 161-171; Barthold, S.W., Mouse hepatitis virus: Biology and epizootiology (1986) Viral and Mycoplasma Infections of Laboratory Rodents. 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Center, 4200 East 9th Ave., Denver, CO 80262, United States; email: kathryn.holmes@uchsc.edu",,,0022538X,,JOVIA,"9696818","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031816799
"Tresnan D.B., Holmes K.V.","6602328481;7201657724;","Feline aminopeptidase N is a receptor for all group I coronaviruses",1998,"Advances in Experimental Medicine and Biology","440",,,"69","75",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754016&partnerID=40&md5=a6e6c0ccb51591638da43e53effa6edd","Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States","Tresnan, D.B., Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States; Holmes, K.V., Department of Microbiology, University of Colorado, Health Sciences Center, Denver, CO 80262, United States","Human coronavirus HCV-229E and porcine transmissible gastroenteritis virus (TGEV), both members of coronavirus group I, use aminopeptidase N (APN) as their cellular receptors. These viruses show marked species specificity in receptor utilization as they can only use APN of their respective species to initiate virus infection. Feline and canine coronaviruses are also group I coronaviruses. To determine whether feline APN could serve as a receptor for feline coronaviruses (FCoVs), we cloned the cDNA encoding feline APN (fAPN) by PCR from feline cells and stably expressed it in FCoV-resistant mouse or hamster cells. These became susceptible to infection with either of several biotypes of FCoVs. The expression of recombinant fAPN also made hamster and mouse cells susceptible to infection with other group I coronaviruses, including several canine coronavirus strains, transmissible gastroenteritis virus (TGEV), and human coronavirus HCV-229E. Thus, fAPN served as a functional receptor for each of these coronaviruses in group I. As expected, fAPN could not serve as a receptor for mouse hepatitis virus (MHV), a group II coronavirus which uses murine biliary glycoproteins as receptors. Thus, fAPN acts as a common receptor for coronaviruses in group I, in marked contrast to human and porcine APN glycoproteins which serve as receptors only for human and porcine coronaviruses, respectively. These observations suggest that cats could serve as a 'mixing vessel' in which simultaneous infection with several group I coronaviruses could lead to recombination of vital genomes.",,"aminopeptidase; virus receptor; amino acid sequence; article; coronavirus; drug receptor binding; genetic recombination; nonhuman; nucleotide sequence; priority journal; receptor affinity; virus genome; virus transmission; virus virulence; 3T3 Cells; Animals; Antigens, CD13; Cats; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus, Canine; Coronavirus, Feline; Cricetinae; Dogs; Humans; Mice; Receptors, Virus; Swine; Canine coronavirus; Coronavirus; Cricetinae; Felidae; Felis catus; Hepatitis C virus; Hepatitis virus A; human coronavirus; Murinae; Murine hepatitis virus; Suidae; Transmissible gastroenteritis virus","Barlough, J.E., Stoddart, C.A., Feline coronaviral infections (1990) Infectious Diseases of the Dog and Cat, pp. 300-312. , (C. E. Greene, ed.), W. B. 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Virol., 71, pp. 734-737; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-419; Delmas, B., Gelfi, J., Kut, E., Sjöström, H., Norén, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase N that is distinct from the enzymatic site (1994) J. Virol., 68, pp. 5216-5224; Delmas, B., Gelfi, J., Sjöström, H., Norén, O., Laude, H., Further characterization of aminopeptidase N as a receptor for coronaviruses (1994) Adv. Exp. Med. 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Res., 41, pp. 868-876; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeiman, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 337-344; Reynolds, D.J., Garwes, D.J., Virus isolation and serum antibody responses after infection of cats with transmissible gastroenteritis virus (1979) Arch. Virol., 60, pp. 161-166; Scott, F.W., Feline infectious peritonitis and other feline coronaviruses (1986) Current Veterinary Therapy IX, pp. 1059-1062. , (R. W. Kirk, ed.), W. B. Saunders Co., Philadelphia; Scolt, F.W., Immunization against feline coronaviruses (1986) Adv. Exp. Med. Biol., 218, pp. 569-576; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N (fAPN) serves as a receptor for feline, canine, porcine and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Wege, H., Siddell, S., Ter Meulen, V., The Biology and Pathogenesis of Coronaviruses (1982) Curr. Topics Microbiol. Immunol., 99, pp. 165-200; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature (London), 357, pp. 420-422","Tresnan, D.B.; Department of Microbiology, Univ. of Colorado Health Sci. Ctr., Denver, CO 80262, United States",,,00652598,,AEMBA,"9782266","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754016
"Welter M.W.","7004347897;","Adaptation and serial passage of bovine coronavirus in an established diploid swine testicular cell line and subsequent development of a modified live vaccine",1998,"Advances in Experimental Medicine and Biology","440",,,"707","711",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754402&partnerID=40&md5=35953491304c9705d3e5cecc3ae4361f","Oragen L.C., Des Moines, IA 50322, United States","Welter, M.W., Oragen L.C., Des Moines, IA 50322, United States","A virulent bovine coronavirus isolate (newborn calf diarrheal) was adapted and serially passaged in an established diploid swine testicular cell line (ST cells). The same cells have been used to produce modified live porcine rotavirus and coronavirus vaccines that are federally licensed and sold worldwide. Growth of the bovine coronavirus resulted in cytopathic effect characterized by cellular stranding and subsequent cell lysis. Virus yields were relatively high in the ST cells and active replication was confirmed by immune electron microscopy and immunofluorescence. Adaptation of bovine coronavirus to a diploid swine cell line has not been previously reported. Different cell culture passage levels of bovine coronavirus were evaluated by oral inoculation of clean-catch, colostrum-deprived calves. A passage level of bovine coronavirus was identified that multiplied in the calf without the clinical signs of disease associated with virulent passages. The modified live bovine coronavirus vaccine remained safe and efficacious even after 5-backpassages in calves. Further efficacy studies have shown that the modified live bovine coronavirus vaccine significantly protected calves from highly virulent challenges with either winter dysentery or newborn calf diarrheal coronavirus isolates.",,"live vaccine; virus vaccine; animal cell; animal disease; animal experiment; animal model; article; cattle; controlled study; coronavirus; cytopathogenic effect; drug efficacy; drug safety; nonhuman; priority journal; swine; testis cell; virogenesis; Adaptation, Biological; Animals; Cattle; Cell Line; Coronavirus Infections; Coronavirus, Bovine; Dysentery; Male; Swine; Testis; Viral Vaccines; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; Porcine rotavirus; Rotavirus; Suidae; Sus scrofa","Babiuk, L.A., Sabara, M., Hudson, G.R., Rotavirus and coronavirus infections in animals (1985) Prog. Vet. Microbiol. Immunol., 1, pp. 80-120; Millane, G., Michaud, L., Dea, S., Biological and molecular differentiation between coronaviruses associated with neonatal calf diarrhoea and winter dysentery in adult cattle (1995) Adv. Exp. Med. Biol., 380, pp. 29-33; Saif, L.J., Theil, K.T., (1990) Viral Diarreheas of Man and Animals, , CRC Press, Boca Raton, Florida","Welter, M.W.; Oragen L.C., Des Moines, IA 50322, United States",,,00652598,,AEMBA,"9782348","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754402
"Tobler K., Ackermann M.","6701508835;7102624625;","Comparison of the di- and trinucleotide frequencies from the genomes of nine different coronaviruses",1998,"Advances in Experimental Medicine and Biology","440",,,"801","804",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751354&partnerID=40&md5=25154921c131039b34f9598f9d69f016","Institute of Virology, Vet.-med. Faculty, University of Zurich, Winterthurerstrasse 266a, 8057 Zurich, Switzerland; BCBMB, Northwestern University, 2153, North Campus Drive, Evanston, IL 60208-3500, United States","Tobler, K., Institute of Virology, Vet.-med. Faculty, University of Zurich, Winterthurerstrasse 266a, 8057 Zurich, Switzerland, BCBMB, Northwestern University, 2153, North Campus Drive, Evanston, IL 60208-3500, United States; Ackermann, M., Institute of Virology, Vet.-med. Faculty, University of Zurich, Winterthurerstrasse 266a, 8057 Zurich, Switzerland","As an alternative to protein alignments for the comparison of sequences, the reiterations of mono- di- and trinucleotide frequencies were used for the comparison of coronavirus sequences. The relative abundance of the di- and trinucleotide frequencies within the 3' part from nine coronavirus genomes were determined. The patterns of dinucleotide frequencies and the trinucleotide frequencies showed some common features for all coronaviruses but also differences between the groups formerly defined on the base of antigenic relatedness. The normalised dinucleotide frequencies were further used to calculate the distances between coronavirus sequences. Based on the dinucleotide frequency distances, coronaviruses can be divided into two groups which roughly reflect the taxonomic groups. In this kind of evaluation, however, IBV occupies a position different to the one that it would take based on most protein sequence comparisons. Based on similarities within coding sequences and antigenic properties IBV occupies a place outside of both groups. Based on the dinucleotide frequencies IBV gained a position in between of the TGEV-related and the MHV-clustered coronaviruses.",,"amino acid sequence; article; coronavirus; gene frequency; nonhuman; priority journal; taxonomy; virus genome; Animals; Coronavirus; Dinucleotide Repeats; Genome, Viral; Humans; Trinucleotide Repeats; Avian infectious bronchitis virus; Coronavirus; Murine hepatitis virus; Transmissible gastroenteritis virus","Burge, C., Campbell, A.M., Karlin, S., Over- and under-representation of short oligonucleotides in DNA sequences (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 1358-1362; Josse, J., Kaiser, A.D., Kornberg, A., (1961) J. Biol. Chem., 236, pp. 864-875; Karlin, S., Burge, C., Dinucleotide relative abundance extremes: A genomic signature (1995) Trends in Genetics, 11, pp. 283-290; Karlin, S., Ladunga, I., Blaisdell, B.E., Heterogeneity of genomes: Measures and values (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 12837-12841","Tobler, K.; BCBMB, Northwestern University, North Campus Drive, Evanston, IL 60208-3500, United States",,,00652598,,AEMBA,"9782361","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751354
"Kolb A.F., Hegyi A., Maile J., Heister A., Hagemann M., Siddell S.G.","7005622195;6603368848;8048534500;57213128696;20334339800;7005260816;","Molecular analysis of the coronavirus-receptor function of aminopeptidase N",1998,"Advances in Experimental Medicine and Biology","440",,,"61","67",,24,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031722290&partnerID=40&md5=e5a3c7f6c99a64a9dd746aadbd2dcfe5","Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany","Kolb, A.F., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Hegyi, A., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Maile, J., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Heister, A., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Hagemann, M., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacherstr. 7, D-97078 Würzburg, Germany","Aminopeptidase N (APN) is a major cell surface for coronaviruses of the serogroup I. By using chimeric APN proteins assembled from human, porcine and feline APN we have identified determinants which are critically involved in the coronavirus-APN interaction. Our results indicate that human coronavirus 229E (HCV 229E) is distinct from the other serogroup I coronaviruses in that determinants located within the N-terminal pans of the human and feline APN proteins mediate the infection of HCV 229E, whereas determinants located within the C-terminal parts of porcine, feline and canine APN mediate the infection of transmissible gastro-enteritis virus (TGEV), feline infectious peritonitis virus (FIPV) and canine coronavirus (CCV), respectively. A further analysis of the mapped amino acid segments by site directed mutagenesis revealed that a short stretch of 8 amino acids in the hAPN protein plays a decisive role in mediating HCV 229E reception.",,"aminopeptidase; virus receptor; amino terminal sequence; animal cell; article; coronavirus; gene mapping; nonhuman; priority journal; protein assembly; receptor affinity; seroconversion; site directed mutagenesis; virus cell interaction; virus characterization; Amino Acid Sequence; Animals; Antigens, CD13; Cats; Coronavirus; Coronavirus 229E, Human; Coronavirus, Canine; Coronavirus, Feline; Dogs; Humans; Molecular Sequence Data; Receptors, Virus; Swine; Transmissible gastroenteritis virus; Animalia; Canine coronavirus; Coronavirus; Felidae; Feline infectious peritonitis virus; Hepatitis C virus; human coronavirus; Human coronavirus 229E; Suidae","Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J. Virol., 71, pp. 734-737; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Adv. Exp. Med. Biol., 342, pp. 293-298; Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) J. Virol., 68, pp. 5216-5224; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) J. Gen. Virol., pp. 2515-2521; Rost, B., PHD: Predicting one dimensional protein structure by profile based neural networks (1996) Meth. Enzymol., 266, pp. 525-539; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , (S. G. Siddell), Plenum Press, New York; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Kolb, A.F.; Institute of Virology and Immunology, University of Wurzburg, Versbacherstr. 7, D-97078 Wurzburg, Germany",,,00652598,,AEMBA,"9782265","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031722290
"Nguyen V.-P., Hogue B.G.","57199220079;7003393593;","Coronavirus envelope glycoprotein assembly complexes",1998,"Advances in Experimental Medicine and Biology","440",,,"361","365",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751707&partnerID=40&md5=217972796b51bf9c15c5fa7654029fc0","Division of Molecular Virology; Department of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States","Nguyen, V.-P., Division of Molecular Virology; Hogue, B.G., Division of Molecular Virology, Department of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States","Protein:protein interactions, and their subcellular localization, play important roles in coronavirus assembly. In this study, we have identified similar envelope glycoprotein complexes that are present in mouse hepatitis coronavirus A59 (MHV-A59) and bovine coronavirus (BCV) infected cells. Complexes consisting of the spike (S) and membrane (M) proteins were identified in cells infected with MHV-A59 or BCV. Kinetic analyses demonstrated that S and M quickly associated after translation, and suggested that both initially interacted in a pre-Golgi site. In addition, the hemagglutinin esterase (HE) was identified as part of a complex with M and S in BCV infected cells. Taken together, our data indicate that similar glycoprotein complexes are present in cells infected with two different coronaviruses, and thus likely represent important prerequisite complexes involved in virus assembly.",,"envelope protein; esterase; hemagglutinin esterase; membrane protein; unclassified drug; virus glycoprotein; animal cell; article; cellular distribution; controlled study; coronavirus; golgi complex; human; human cell; mouse; murine hepatitis coronavirus; nonhuman; priority journal; protein protein interaction; virus assembly; virus transcription; Animals; Cattle; Cell Line; Coronavirus, Bovine; Hemagglutinins, Viral; Membrane Glycoproteins; Mice; Murine hepatitis virus; Viral Envelope Proteins; Viral Fusion Proteins; Viral Matrix Proteins; Viral Proteins; Animalia; Bovinae; Bovine coronavirus; Coronavirus; mouse hepatitis coronavirus; Murinae; Murine hepatitis virus","Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Sahara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J. Gen. Virol., 68, pp. 2863-2877; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Hogue, B.G., King, B., Brian, D.A., Antigenic relationship among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J. Virol., 51, pp. 384-388; Hogue, B.G., Kienzle, T.E., Brian, D.A., Synthesis and processing of the bovine enteric hemagglutinin protein (1989) J. Gen. Virol., 70, pp. 345-352; King, B., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Klumperman, J., Krijinse-Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virus budding (1994) J. Virol., 68, pp. 6523-6534; Krijinse-Locker, J., Griffiths, G., Horzinek, M.C., Rottier, R.J.M., O-glycosylation of the coronavirus M protein (1992) J. Biol. Chem., 267, pp. 14094-14101; Krijinse-Locker, J., Ericsson, M., Rottier, P.J.M., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J. Cell. Biol., 124, pp. 55-70; Krijinse-Locker, J., Opstelten, D.-J.E., Ericsson, M., Horzinek, M.C., Rottier, P.J.M., Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention (1995) J. Biol. Chem., 270, pp. 8815-8821; Opstelten, D.-J.E., Raasmsman, M.J.B., Wolfs, K., Horzinek, M.C., Rottier, R.J.M., Envelope glycoprotein interactions in coronavirus assembly (1995) J. Cell. Biol., 131, pp. 339-349; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in Sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell. Biol., 33, pp. 281-293","Nguyen, V.-P.; Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States",,,00652598,,AEMBA,"9782304","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751707
"Cologna R., Hogue B.G.","7801604385;7003393593;","Coronavirus nucleocapsid protein: RNA interactions",1998,"Advances in Experimental Medicine and Biology","440",,,"355","359",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754397&partnerID=40&md5=7831f10be6e32065162f27b4e9fbb043","Division of Molecular Virology; Baylor College of Medicine, Houston, TX, United States","Cologna, R., Division of Molecular Virology; Hogue, B.G., Division of Molecular Virology, Baylor College of Medicine, Houston, TX, United States","The coronavirus nucleocapsid protein (N) is involved in encapsidation and packaging of vital RNA. In this study we investigated the ability of the bovine coronavirus (BCV) N protein to interact with RNA. Histidine-tagged BCV N (his-N) protein was expressed in bacteria. A filter binding assay was established to quantitatively measure the binding efficiency of purified his- N to different RNAs. The results indicate that bacterially expressed N bound both BCV and mouse hepatitis coronavirus (MHV) RNAs. Binding to in vitro generated BCV and MHV RNA transcripts was significantly higher than binding to a non-coronavirus RNA. Similar binding efficiencies were measured for a BCV defective genome, pDrep, and a transcript that contained the MHV packaging signal. Interestingly, the entire MHV DI, pMIDI-C, was bound at a higher efficiency than the packaging signal alone. This is one of the first reports to show that N interacts with the MHV packaging signal.",,"capsid protein; messenger rna; phosphorus 32; virus rna; article; controlled study; coronavirus; murine hepatitis coronavirus; nonhuman; priority journal; protein purification; protein rna binding; virus nucleocapsid; Animals; Cattle; Coronavirus, Bovine; Mice; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; Recombinant Fusion Proteins; RNA, Viral; Virus Assembly; Bovinae; Bovine coronavirus; Coronavirus; Miridae; mouse hepatitis coronavirus; Murinae; Murine hepatitis virus","Baric, W.R., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. Virol., 62, pp. 4280-4287; Bos, E.C.W., Dobbe, J.C., Luytjes, W., Spaan, W.J.M., A subgenomic mRNA transcript of the coronavirus mouse hepatitis virus strain A59 defective interfering (DI) RNA is packaged when it contains the di packaging signal (1997) J. Virol., 71, pp. 5684-5687; Cavanagh, D., Revision of the taxonomy of the Coronavirus, Torovirus, and Arterivirus general (1994) Arch. Virol., 135, pp. 226-237; Chang, R.-Y., Brian, D.A., Cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus Di-1 and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5898-5905; Fosmire, J., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Makino, S., Yokomori, K., Lai, M.M.C., (1990) Analysis of Efficiently Packaged Defective Interfering RNAs of Murine Coronavirus: Localization of a Possible RNA-packaging Signal, 64, pp. 6045-6053; Siddell, S.G., The Coronaviridae. An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed), Plenum Press, New York; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interactions between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-1527","Cologna, R.; Division of Molecular Virology, Houston, TX, United States",,,00652598,,AEMBA,"9782303","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754397
"Perlman S.","7102708317;","Pathogenesis of coronavirus-induced infections: Review of pathological and immunological aspects",1998,"Advances in Experimental Medicine and Biology","440",,,"503","513",,55,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031750728&partnerID=40&md5=deea840036f6473eabd1da1b799a9115","Department of Pediatrics and Microbiology, Interdisciplinary Program in Immunology, University of Iowa, Iowa City, IA 52242, United States","Perlman, S., Department of Pediatrics and Microbiology, Interdisciplinary Program in Immunology, University of Iowa, Iowa City, IA 52242, United States","Coronaviruses and arteriviruses infect multiple species of mammals, including humans, causing diseases that range from encephalitis to enteritis. Several of these viruses infect domestic animals and cause significant morbidity and mortality, leading to major economic losses. In this category are included such pathogens as transmissible gastroenteritis virus, porcine respiratory and reproductive virus and infectious bronchitis virus. The feline coronaviruses (FECV) generally do not cause infections with high morbidity but in a small percentage of cases, the virus mutates to become more virulent. This virus, feline infectious peritonitis virus (FIPV), causes severe disease in young cats. This disease is in large part immunopathological and understanding it is a major goal of coronavirus research.",,"cytokine; animal experiment; animal model; article; cellular immunity; cytokine release; demyelinating disease; demyelination; humoral immunity; mouse; murine hepatitis coronavirus; nonhuman; paralysis; persistent virus infection; priority journal; rat; virus infection; Animals; Cats; Coronavirus Infections; Cytokines; Demyelinating Diseases; Mice; Murine hepatitis virus; Rats; Virus Latency; Animalia; Avian infectious bronchitis virus; Coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus; Mammalia; Murinae; Murine hepatitis virus; Suidae; Transmissible gastroenteritis virus","Barac-Latas, V., Suchanek, G., Breitschopf, H., Stuehler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in coronavirus-induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, 19, pp. 1-12; Barnett, E., Perlman, S., The olfactory nerve and not the trigeminal nerve is the major site of CNS entry for mouse hepatitis virus, strain JHM (1993) Virology, 194, pp. 185-191; Bergmann, C., McMillan, M., Stohlman, S.A., Characterization of the Ld-restricted cytotoxic T-lymphocyte epitope in the mouse hepatitis virus nucleocapsid protein (1993) J. Virol., 67, pp. 7041-7049; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted CTL response (1996) J. Gen. Virol., 77, pp. 315-325; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Castro, R.F., Perlman, S., CD8+ T cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J. Virol., 69, pp. 8127-8131; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin (1949) J. Exp. Med., 90, pp. 181-194; Chen, W., Baric, R., Molecular anatomy of MHV persistence: Coevolution of increased host resistance and virus virulence (1996) J. Virol., 70, pp. 3947-3960; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Dorries, R., Watanabe, R., Wege, H., Ter Meulen, V., Murine coronavirus-induced encephalomyelitides in rats: Analysis of immunoglobulins and virus-specific antibodies in serum and cerebrospinal fluid (1986) J. Neuroimmunol., 12, pp. 131-142; Fleming, J.O., Trousdale, M.D., Bradbury, J., Stohlman, S.A., Weiner, L.P., Experimental demyelination induced by coronavirus JHM (MHV-4): Molecular identification of a viral determinant of paralytic disease (1987) Microb. Pathog., 3, pp. 9-20; Flory, E., Stuhler, A., Barac-Latas, V., Lassmann, H., Wege, H., Coronavirus-induced encephalomyelitis: Balance between protection and immunopathology depends on the immunization schedule with spike protein S (1995) J. Gen. Virol, 76, pp. 873-879; Gombold, J., Sutherland, R., Lavi, E., Paterson, Y., Weiss, S.R., Mouse hepatitis virus A59-induced demyelination can occur in the absence of CD8+ T cells (1995) Microb. Pathog., 18, pp. 211-221; Haspel, M.V., Lampert, P.W., Oldstone, M.B.A., Temperature-sensitive mutants of mouse hepatitis virus produce a high incidence of demyelination (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 4033-4036; Heemskerk, M., Schoemaker, H., De Jong, I., Schijns, V., Spaan, W., Boog, C.J.P., Differential activation of mouse hepatitis virus-specific CD4+ cytotoxic T cells is defined by peptide length (1995) Immunology, 85, pp. 517-522; Heemskerk, M., Schoemaker, H., Spaan, W., Boog, C., Predominance of MHC class II-restricted CD4+ cytotoxic T cells against mouse hepatitis virus A59 (1995) Immunology, 84, pp. 521-527; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirology, 2, pp. 101-110; Jacobsen, G., Perlman, S., Localization of virus and antibody response in mice infected persistently with MHV-JHM (1990) Adv. Exp. Med. Biol., 276, pp. 573-578; Jordan, C., Friedrich, V., Godfraind, C., Caardellechio, C., Holmes, K., Dubois-Dalcq, M., Expression of viral and myelin gene transcripts in a murine CNS demyelinating disease caused by a coronavirus (1989) Glia, 2, pp. 318-329; Körner, H., Schliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S., Wege, H., Nucleocapsid or spike protein-specific CD4+ T lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CD8+ T cells (1991) J. Immunol., 147, pp. 2317-2323; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronvirus, strain JHM in the central nervous system of mice (1990) Sem. 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Neurol., 37, pp. 478-484; Stohlman, S.A., Bergmann, C.C., Van Der Veen, R.C., Hinton, D.R., Mouse hepatitis virus-specific cytotoxic T lymphocytes protect from lethal infection without eliminating virus from the central nervous system (1995) J. Virol., 69, pp. 684-694; Stohlman, S.A., Fleming, J.O., Brayton, P.R., Weiner, L.P., Lai, M.M.C., Murine coronaviruses: Isolation and characterization of two plaque morphology variants of the JHM neurotropic strain (1982) J. Gen. Virol., 63, pp. 265-275; Stohlman, S.A., Frelinger, J.A., Resistance to fatal central nervous system disease by mouse hepatitis virus, strain JHM (1978) Immunogenetics, 6, pp. 277-281; Stohlman, S.A., Hinton, D.R., Cua, D., Dimacali, E., Sensintaffar, J., Hofman, F.M., Tahara, S.M., Yao, Q., Tumor necrosis factor expression during mouse hepatitis virus-induced demyelinating encephalomyelitis (1995) J. 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Neuroimmunol., 32, pp. 1-9","Perlman, S.; Dept. of Pediatrics and Microbiology, Interdisciplinary Prog. in Immunol., University of Iowa, Iowa City, IA 52242, United States",,,00652598,,AEMBA,"9782322","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031750728
"Ziebuhr J., Heusipp G., Seybert A., Siddell S.G.","7003783935;6603559110;7004923617;7005260816;","Substrate specificity of the human coronavirus 229E 3C-like proteinase",1998,"Advances in Experimental Medicine and Biology","440",,,"115","120",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031720727&partnerID=40&md5=dfebe283da8a36435ce28cd072cee4f0","Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Ziebuhr, J., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Heusipp, G., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Seybert, A., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Coronavirus gene expression involves proteolytic processing of the gene 1-encoded polyproteins and a key enzyme in this process is the virus-encoded 3C-like proteinase. In this study, we describe the biosynthesis of the human coronavirus 229E 3C-like proteinase in Escherichia coli and the substrate specificity of the purified protein. Using immunofluorescence microscopy, we have also investigated the subcellular localization of the 3C-like proteinase and have found a punctate, perinuclear distribution of the proteinase in virus-infected cells.",,"proteinase; animal cell; article; cell compartmentalization; cellular distribution; coronavirus; enzyme specificity; gene expression; nonhuman; priority journal; protein degradation; protein processing; protein purification; virus expression; virus gene; virus genome; virus infection; Amino Acid Sequence; Cell Line; Coronavirus; Coronavirus 229E, Human; Cysteine Endopeptidases; Humans; Molecular Sequence Data; Substrate Specificity; Viral Proteins; Animalia; Coronavirus; Escherichia coli; human coronavirus; Human coronavirus 229E","Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Süss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Urology, 195, pp. 680-691; Heusipp, G., Grötzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41-kDa, polyprotein lab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., , in press; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kDa polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., , in press; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5773-5780; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Lu, Y., Denison, M.R., Determinants of mouse hepatitis virus 3C-like proteinase activity (1997) Virology, 230, pp. 335-342; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Urology, 222, pp. 375-382; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Seybert, A., Ziebuhr, J., Siddell, S.G., Expression and characterization of a recombinant murine coronavirus 3C-like proteinase (1997) J. Gen. Virol., 78, pp. 71-75; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Van Dinten, L.C., Wassenaar, A.L.M., Gorbalenya, A.E., Spaan, W.J.M., Snijder, E.J., Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) J. Virol., 70, pp. 6625-6633; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997","Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,,00652598,,AEMBA,"9782272","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031720727
"Hirano N., Ono K.","7101604276;7403889877;","A serological survey of human coronavirus in pigs of the Tohoku District of Japan",1998,"Advances in Experimental Medicine and Biology","440",,,"491","494",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783037&partnerID=40&md5=868ab59d5c788986e6143d1153a4a0a2","Department of Veterinary Microbiology, Iwate University, Morioka, Japan","Hirano, N., Department of Veterinary Microbiology, Iwate University, Morioka, Japan; Ono, K., Department of Veterinary Microbiology, Iwate University, Morioka, Japan","A total of 2496 swine sera from 60 farms in the Tohoku District of Japan was examined for hemagglutination inhibiting (HI) antibodies to human coronavirus (HCV), swine hemagglutinating encephalomyelitis virus (HEV) and bovine coronavirus (BCV). HI antibodies to HCV OC43 strain and HEV 67N strain were highly prevalent with positivity rates of 91.4 and 82.1%, respectively, while the BCV Kakegawa strain was 44.2% positive. Farm D in Miyagi Prefecture showed the highest antibody titers to HCV OC43 strain with geometric mean titers (GMT) of 1:200. These results suggest that pigs might be infected with HCV or an antigenetically related virus as well as HEV.",,"hemagglutination inhibiting antibody; animal tissue; antibody titer; antigenicity; article; controlled study; coronavirus; japan; mouse; nonhuman; priority journal; serology; swine; Animals; Antibodies, Viral; Cattle; Coronavirus; Coronavirus Infections; Coronavirus OC43, Human; Coronavirus, Bovine; Humans; Japan; Seroepidemiologic Studies; Swine; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Hepatitis C virus; human coronavirus; Porcine hemagglutinating encephalomyelitis virus; Sus scrofa","Hirai, K., Chang, C.N., Shimakura, S., A serological survey on hemagglutinating encephalomyelitis virus infection in pigs in Japan (1974) Jpn. J. Vet. Sci., 36, pp. 375-382; Hirahara, T., Yasuhara, H., Kodama, K., Nakai, M., Sasaki, N., Isolation of hemagglutinating encephalomyelitis virus from respiratory tract of pigs in Japan (1987) Jpn. J. Vet. Sci., 49, pp. 85-93; Hirano, N., Ono, K., Takasawa, H., Murakami, T., Haga, S.J., Replication and plaque formation of swine hemagglutinating encephalomyelitis virus (67N) in swine cell line, SK-K culture (1990) J. Virol. Meth., 27, pp. 91-100; Hirano, N., Sada, F., Tsuchiya, K., Ono, K., Murakami, T., Plaque assay of bovine coronavirus in BEK-1 cells (1985) Jpn. J. Vet. Sci., 47, pp. 679-681; Kaye, H.S., Yarbrough, W.R., Reed, C.J., Harrison, A.K.J., Antigenic relationship between human coronavirus strain OC 43 and hemagglutinating encephalomyelitis virus strain 67N of swine: Antibody responses in human and animal sera (1977) Inf. Dis., 135, pp. 201-209; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Chanock, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc. Natl. Acad. Sci. USA, 57, pp. 933-940; Mengeling, W.L., Boothe, A.D., Richte, A.E., Characteristics of a coronavirus (Strain 67N) of pigs (1972) Am. J. Vet. Res., 33, pp. 297-308","Hirano, N.; Dept. of Veterinary Microbiology, Iwate University, Morioka, Japan",,,00652598,,AEMBA,"9782320","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783037
"Thiel V., Herold J., Siddell S.G.","35238592100;7006838690;7005260816;","Long distance RT-PCRS of human coronavirus 229E RNA",1998,"Advances in Experimental Medicine and Biology","440",,,"269","273",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783036&partnerID=40&md5=057986e9a12fc4a6b7a19b5f9553154f","Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany","Thiel, V., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany; Herold, J., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany","The generation and cloning of cDNA fragments longer than 10 kb is often a difficult and time consuming task. In this study, we have analysed the conditions necessary to produce reverse transcripts longer than 10 kb that can be amplified by polymerase chain reaction. Thus, we isolated poly(A)-RNA from human coronavirus 229E infected MRC-5 cells and did reverse transcription using a sequence-specific primer. Subsequently, we amplified PCR products of varying length upstream of the primer position. Optimisation of the poly(A)-RNA preparation, the reverse transcription protocol and the polymerase chain reaction cycle conditions enabled us to successfully amplify regions of the human coronavirus 229E genome between 11.5 and 20.3 kb in length.",,"virus rna; article; coronavirus; molecular cloning; nonhuman; priority journal; reverse transcription polymerase chain reaction; rna sequence; sequence analysis; virus characterization; virus detection; Cell Line; Coronavirus; Coronavirus 229E, Human; DNA, Viral; Humans; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Coronavirus; human coronavirus; Human coronavirus 229E","Barnes, W.M., PCR amplification of up to 35-kb DNA with high fidelity and high yield from 1 bacteriophage templates (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 2216-2220; Cheng, S., Fockler, C., Barnes, W.M., Higuchi, R., Effective amplification of long targets from cloned inserts and human genomic DNA (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 5695-5699; Cheng, S., Higuchi, R., Stoneking, M., Complete mitochondrial genome amplification (1994) Nature Genet., 7, pp. 350-351; Chumakov, K.M., PCR Engeneering of Viral Quasispecies: A New Method to Preserve and Manipulate Genetic Diversity of RNA Virus Populations (1996) J. Virol., 70, pp. 7331-7334; Fakhfakh, H., Vilaine, F., Makni, M., Robaglia, C., Cell-free cloning and biolistic inoculation of an infectious cDNA of potato virus Y (1996) J. Gen. Virol., 77, pp. 519-523; Martinez, J.M., Breidenbach, H.H., Cawthon, R., Long RT-PCR of the Entire 8.5-kb NF1 Open Reading Frame and Mutation Detection on Agarose Gels (1996) Genome Res., 6, pp. 58-66; Tellier, R., Bukh, J., Emerson, S.U., Purcell, R.H., Amplification of the full-length hepatitis A virus genome by long reverse transcription-PCR and transcription of infectious RNA directly from the amplicon (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 4370-4373","Thiel, V.; Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany",,,00652598,,AEMBA,"9782292","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783036
"Sawicki S.G., Sawicki D.L.","7004118344;7003804556;","A new model for coronavirus transcription",1998,"Advances in Experimental Medicine and Biology","440",,,"215","219",,138,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783431&partnerID=40&md5=8096e21131eaf384b269c8c3c56a7195","Department of Microbiology and Immunology, Medical College of Ohio, Toledo, OH 43699, United States","Sawicki, S.G., Department of Microbiology and Immunology, Medical College of Ohio, Toledo, OH 43699, United States; Sawicki, D.L., Department of Microbiology and Immunology, Medical College of Ohio, Toledo, OH 43699, United States","Coronaviruses contain an unusually long (27-32,000 ribonucleotide) positive sense RNA genome that is polyadenylated at the 3' end and capped at the 5' end. In addition to the genome, infected cells contain subgenomic mRNAs that form a 3' co-terminal nested set with the genome. In addition to their common 3' ends, the genome and the subgenomic mRNAs contain an identical 5' leader sequence. The transcription mechanism that coronaviruses use to produce subgenomic mRNA is not known and has been the subject of speculation since sequencing of the subgenomic mRNAs showed they must arise by discontinuous transcription. The current model called leader-primed transcription has subgenomic mRNAs transcribed directly from genome-length negative strands. It was based on the failure to find in coronavirus infected cells subgenome-length negative strands or replication intermediates containing subgenome-length negative strands. Clearly, these structures exist in infected cells and are transcriptionally active. We proposed a new model for coronavirus transcription which we called 3' discontinuous extension of negative strands. This model predicts that subgenome-length negative strands would be derived directly by transcription using the genome RNA as a template. The subgenome-length templates would contain the common 5' leader sequence and serve as templates for the production of subgenomic mRNAs. Our findings include showing that: 1. Replication intermediates (RIs) containing subgenome-length RNA exist in infected cells and are separable from RIs with genome-length templates. The RFs with subgenome-length templates are not derived by RNase treatment of RIs with genome-length templates. 2. The subgenome-length negative strands are formed early in infection when RIs are accumulating and the rate of vital RNA synthesis is increasing exponentially. 3. Subgenome-length negative strands contain at their 3' ends a complementary copy of the 72 nucleotide leader RNA that is found in the genome only at their 5' end. 4. RIs with subgenomic templates serve immediately as templates for transcription of subgenomic mRNAs. Because subgenomic mRNAs are not replicated, i.e., copied into negative strands that in turn are used as templates for subgenomic mRNA synthesis, we propose that the subgenome- length negative strands must arise directly by transcription of the genome and acquire their common 3' anti-leader sequence after polymerase jumping from the intergenic regions to the leader sequence at the 5' end of the genome. This would make negative strand synthesis discontinuous and subgenomic mRNA synthesis continuous, which is the opposite of what was proposed in the leader primed model.",,"article; coronavirus; messenger rna synthesis; nonhuman; priority journal; rna sequence; sequence analysis; transcription regulation; virus transcription; Animals; Coronavirus; Models, Genetic; RNA, Viral; Transcription, Genetic; Coronavirus","Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, p. 633; Brian, D.A., Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Role of subgenomic minus-strand RNA in coronavirus replication (1994) Arch. Virol. (Suppl.), 9, pp. 173-180; Chang, R.Y., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. Virol., 70, pp. 2720-2729; Komissarova, N., Kashlev, M., Transcription arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′ end of the RNA intact and extruded (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 1755-1760; Lai, M.M.C., Patton, C.D., Stohlman, S.A., Replication of mouse hepatitis virus: Negative-stranded RNA and replicative form RNA are of genome length (1982) J. Virol., 44, pp. 487-492; Lai, M.M.C., Coronavirus-organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRN a synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis (1994) J. Virol., 68, pp. 328-337; Nudler, E., Mustaev, A., Lukhtanov, E., Goldfarb, A., The RNA-DNA hybrid maintains the register of transcription by preventing backtracking on RNA polymerase (1997) Cell, 89, pp. 33-41; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands (1995) Corona and Related Viruses, pp. 499-505. , (P.J. Talbot and G.A. Levy, eds) Plenum Press, New York; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Stillman, E.A., Whitt, M.A., Mutational analysis of the intergenic dinucleotide and the transcriptional start sequence of vesicular stomatitis virus (VSV) define sequences required for efficient termination and initiation of VSV transcripts (1997) J. Virol., 71, pp. 2127-2137; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.W., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666","Sawicki, S.G.; Dept. of Microbiology and Immunology, Medical College of Ohio, Toledo, OH 43699, United States",,,00652598,,AEMBA,"9782283","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783431
"Arbour N., Talbot P.J.","6602762564;7102670281;","Persistent infection of neural cell lines by human coronaviruses",1998,"Advances in Experimental Medicine and Biology","440",,,"575","581",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721669&partnerID=40&md5=0a8d8f6a57852bf48d5b5134f8995cb5","Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada","Arbour, N., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada","Human coronaviruses (HCV) have been associated mainly with infections of the respiratory tract. Accumulating evidence from in vitro and in vivo observations is consistent with the neurotropism of these viruses in humans. To verify the possibility of a persistent infection within the central nervous system (CNS), various human cell lines of neural origin were tested for their ability to maintain chronic infection by both known strains of HCV, OC43 and 229E. Production of infectious progeny virions was monitored by an immunoperoxydase assay on a susceptible cell line and viral RNA was observed after RT-PCR. Astrocytic cell lines U-373 MG and U-87 MG did not sustain a persistent HCV-229E infection, even though they were susceptible to an acute infection by this virus. On the other hand, these two cell lines could maintain a persistent infection by HCV- OC43 for as many as 25 cell passages (about 130 days of culture). Relatively stable titers of infectious viral particles, as well as apparently constant amounts of viral RNA were detected throughout the persistent infection of U-87 MG cells. However, persistent infection of U-373 MG cells was accompanied by the detection of infectious viral particles from passage 0 to passage 13 and then from passage 20 to the end of the experiment. This gap in the production of infectious virions was correlated by a drop in the apparent amount of viral RNA detected at passages 15 and 20. These results confirm the ability of HCV-OC43 to persistently infect cells of an astrocytic lineage and, together with our previous observations of HCV infection of primary cultures of human astrocytes and the detection of HCV RNA in human brains, are consistent with the possibility that this human coronavirus could persist in the human CNS by targeting astrocytes.",,"article; astrocyte; coronavirus; human; human cell; immunoperoxidase staining; nerve cell; neuropathology; persistent virus infection; priority journal; reverse transcription polymerase chain reaction; virion; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus OC43, Human; Humans; Neuroglia; Neurons; RNA, Viral; Virion; Virus Latency; Coronavirus; Hepatitis C virus; human coronavirus","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Arbour, N., Talbot, P.J., (1997), unpublished observations; Barnett, E.M., Perlman, S., The olfactory nerve and not the trigeminal nerve is the major site of CNS entry for mouse hepatitis virus, strain JHM (1993) Virology, 194, pp. 185-191; Bonavia, A., Arbour, N., Yong, V.W., Talbot, P.J., Infection of primary cultures of human neural cells by human coronaviruses 229E and OC43 (1997) J. Virol., 71, pp. 800-806; Cabirac, G.F., Soike, K.F., Zhang, J.Y., Hoel, K., Butunoi, C., Cai, G.Y., Johnson, S., Murray, R.S., Entry of coronavirus into primate CNS following peripheral infection (1994) Microb. Path., 16, pp. 349-357; Collins, A.R., Sorensen, O., Regulation of viral persistence in human glioblastoma and rhabdomyosarcoma cells infected with coronavirus OC43 (1986) Microb. Path., 1, pp. 573-582; Ercolani, L., Florence, B., Denaro, M., Alexander, M., Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene (1988) J. Biol. Chem., 263, pp. 15335-15341; Jouvenne, P., Mounir, S., Stewart, J.N., Richardson, C.D., Talbot, P.J., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res., 22, pp. 125-141; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann. Neurol., 31, pp. 525-533; Murray, R.S., Cai, G.Y., Soike, K.F., Cabirac, G.F., Further observations on coronavirus infection of primate CNS (1997) J. Neurovirol., 3, pp. 71-75; Myint, S.H., Human coronaviruses-a brief review (1994) Rev. Med. Virol., 4, pp. 35-46; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J. Med. Virol., 6, pp. 259-265; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterization of spike deletion variants during persistent infection (1997) J. Virol., 71, pp. 2959-2969; Salmi, A., Ziola, B., Hovi, T., Reunanen, M., Antibodies to coronaviruses OC43 and 229E in multiple sclerosis patients (1982) Neurology, 32, pp. 292-295; Schreiber, S.S., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Sizun, J., Soupre, D., Legrand, M.C., Giroux, J.D., Rubio, S., Cauvin, J.M., Chastel, C., De Parscau, L., Neonatal nosocomial respiratory infection with coronavirus: A prospective study in a neonatal intensive care unit (1995) Acta Paediatr., 84, pp. 617-620; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Sun, N., Perlman, S., Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes (1995) J. Virol., 69, pp. 633-641; Sun, N., Grzybicki, D., Castro, R.F., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Talbot, P.J., Ékandé, S., Cashman, N.R., Mounir, S., Stewart, J.N., Neurotropism of human coronavirus 229E (1994) Adv. Exp. Med. Biol., 342, pp. 339-346; Ter Meulen, V., Massa, P.T., Dörries, R., Coronaviruses (1989) Handbook of Clinical Neurology: Viral Disease, Revised Series, 12, pp. 439-451. , (P.J. Vinken, G.W. Bruyn, and H.L. Klawans, eds.), Elsevier, New-York","Arbour, N.; Laboratory o f Neuroimmunovirology, Institut Armand-Frappier, Universite du Quebec, Laval, Que. H7V 1B7, Canada",,,00652598,,AEMBA,"9782332","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721669
"Herold J., Thiel V., Siddell S.G.","7006838690;35238592100;7005260816;","Characterization of a papain-like cysteine-proteinase encoded by gene 1 of the human coronavirus HCV 229E",1998,"Advances in Experimental Medicine and Biology","440",,,"141","147",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753725&partnerID=40&md5=7382b038a22a646caaa16193bb3e55bf","Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Herold, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Thiel, V., Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany","Expression of the coronaviral gene 1 polyproteins, pp 1 a and pp1ab, involves a series of proteolytic events that are mediated by virus-encoded proteinases similar to cellular papain-like cysteine-proteinases and the 3C- like proteinases of picornaviruses. In this study, we have characterized, in vitro, the human coronavirus HCV 229E papain-like cysteine-proteinase PCP 1. We show that PCP 1 is able to mediate cleavage of an aminoterminal polypeptide, p9, from in vitro translation products representing the aminoproximal region of pp1a/pp1ab. Mutagenesis studies support the prediction of Cys 1054 and His 1278 as the catalytic amino acids of the HCV 229E PCP 1, since mutation of these residues abolishes the proteolytic activity of the enzyme.",,"cysteine proteinase; papain; amino terminal sequence; article; coronavirus; drug receptor binding; mutagenesis; nonhuman; priority journal; protein degradation; protein domain; virus characterization; virus expression; virus replication; virus transcription; Coronavirus; Coronavirus 229E, Human; Cysteine Endopeptidases; Humans; Papain; Viral Proteins; Coronavirus; Hepatitis C virus; human coronavirus","Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.N., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and strutural similarities with cellular enzymes (1993) Micribiol. Rev., 57, pp. 781-822; Gorbalenya, A.E., Snijder, E.J., Viral cysteine proteinases (1996) Perspectives in Drug Discovery and Design, 6, pp. 64-86; Herold, J., Siddell, S.G., An elaborated pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., (1995) Organization and Expression of RNA Polymerase Locus of the Human Coronavirus 229E, , Ph.D. Thesis., University of Würzburg, Germany; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275, pp. 68-89; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Heusipp, G., Grötzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41-kDa, polyprotein lab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., , in press; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Herold, J.; Institute of Virology and Immunology, University of Wurzburg, Versbacher Strasse 7, 97078 Wurzburg, Germany",,,00652598,,AEMBA,"9782276","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753725
"Schiller J.J., Baker S.C.","56354099200;7403307881;","Maturation of the polymerase polyprotein of the coronavirus MHV strain JHM involves a cascade of proteolytic processing events",1998,"Advances in Experimental Medicine and Biology","440",,,"135","139",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751350&partnerID=40&md5=be039b0ba6a65ad920e254b9ba79d8e3","Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Ave., Maywood, IL 60153, United States","Schiller, J.J., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Ave., Maywood, IL 60153, United States; Baker, S.C., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Ave., Maywood, IL 60153, United States","The RNA polymerase gene of the murine coronavirus mouse hepatitis virus (MHV) encodes a polyprotein of greater than 750 kDa. The amino-terminal cleavage product of the MHV polymerase polyprotein, p28, has been shown to be cleaved from the polyprotein by the virus-encoded protease PCP-1. We aim to identify the MHV-JHM proteolytic products downstream of p28 and to determine which viral proteinase domains are responsible for generating each of them. To this end, we have generated antisera directed at specific MHV-JHM ORF1a regions and have used these antisera to identify six viral proteins, representing a large portion of ORF1a, from MHV-JHM-infected cells. These proteins include p28, p72, p65, p250, p210, and p27.",,"dna directed dna polymerase alpha; animal cell; article; cell lysate; cell maturation; coronavirus; hepatitis virus; immunoprecipitation; nonhuman; open reading frame; priority journal; protein degradation; protein domain; protein localization; protein polymerization; protein processing; virus strain; Animals; Cell Line; DNA-Directed RNA Polymerases; Endopeptidases; Mice; Murine hepatitis virus; Protein Precursors; Protein Processing, Post-Translational; Proteins; Rabbits; Viral Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene a polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. Virol., 71, pp. 900-909; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Gao, H.-Q., Schiller, J.J., Baker, S.C., Identification of the polymerase polyprotein products p72 and p65 of the murine coronavirus MHV-JHM (1996) Virus Research, 45, pp. 101-109; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Guan, K., Dixon, J.E., Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure for fusion proteins with glutathione S-transferase (1991) Anal. Biochem., 192, pp. 262-267; Hughes, S.A., Bonilla, P., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 222, pp. 375-382; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Seybert, A., Ziebuhr, J., Siddell, S.G., Expression and characterization of a recombinant murine coronavirus 3C-like proteinase (1997) J. Gen. Virol., 78, pp. 71-75; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338","Schiller, J.J.; Dept. of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 South First Ave., Maywood, IL 60153, United States",,,00652598,,AEMBA,"9782275","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751350
"Wang Q., Haluskey J.A., Lavi E.","16044062200;6507007625;7006986911;","Coronavirus MHV-A59 causes upregulation of interferon-β RNA in primary glial cell cultures",1998,"Advances in Experimental Medicine and Biology","440",,,"451","454",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751708&partnerID=40&md5=791736d5fdf625b1785e3530f1ccb8f4","Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphiam, PA 19104, United States","Wang, Q., Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphiam, PA 19104, United States; Haluskey, J.A., Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphiam, PA 19104, United States; Lavi, E., Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphiam, PA 19104, United States","Infection of mice with coronavirus mouse hepatitis virus strain MHV-A59 causes focal acute encephalitis, hepatitis and chronic demyelinating disease. To investigate host interferon (IFN) response to viral infection within the brain, RNA was extracted from A59-or MHV-2- infected and mock-infected primary astrocyte cultures from newborn mice, RT-PCR amplified RNA with primers specific for the various IFNs, transferred to nylon membranes and hybridized with IFN specific digoxigenin-labeled probes. Infection of primary astrocyte cultures from newborn mice with either A59 or MHV-2 caused upregulation of IFN-β RNA, but not IFN-γ or IFN-α. Thus, brain astrocytes are capable of producing a local IFN-β response upon infection with MHV. The response of the other IFNs following MHV infection may be derived from inflammatory cells.",,"alpha interferon; beta actin; beta interferon; digoxigenin; gamma interferon; glial fibrillary acidic protein; rna; animal cell; article; astrocyte; controlled study; demyelination; glia cell; inflammatory cell; mouse; murine hepatitis coronavirus; newborn; nonhuman; priority journal; reverse transcription polymerase chain reaction; virus encephalitis; virus hepatitis; Animals; Astrocytes; Cells, Cultured; Female; Interferon Type II; Interferon-alpha; Interferon-beta; Mice; Mice, Inbred C57BL; Murine hepatitis virus; RNA; Up-Regulation; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., Persistence of MHV-A59 RNA in a slow virus demyelinating infection in mice as detected by in situ hybridization (1984) J. Virol., 51, pp. 563-566; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Suzumura, A., Hirayama, M., Highkin, M.K., Dambach, D.M., Silberberg, D.H., Weiss, S.R., Coronavirus MHV-A59 causes a persistent, productive infection in glial cells (1987) Microbial Pathogenesis, 3, pp. 79-86; Lavi, E., Suzumura, A., Lampson, L.A., Siegel, R.M., Murasko, D.M., Silberberg, D.H., Weiss, S.R., Expression of MHC class I genes in mouse hepatitis virus (MHV-A59) infection and in multiple sclerosis (1987) Adv. Exp. Med. Biol., 218, pp. 219-222; Lavi, E., Suzumura, A., Murray, E.M., Silberberg, D.H., Weiss, S.R., Induction of MHC class I antigens on glial cells is dependent on persistent mouse hepatitis virus infection (1989) J. Neuroimmunol., 22, pp. 107-111; Lavi, E., Wang, Q., The protective role of cytotoxic T cells and interferon against coronavirus invasion of the brain (1995) Adv. Exp. Med. Biol., 380, pp. 145-149; Lavi, E., Weiss, S.R., Coronaviruses (1989) Clinical and Molecular Aspects of Neurotropic Viral Infections, pp. 101-139. , (D. H. Gilden, and H. L. Lipton, Eds.), Kluwer, Academic Publishers, Boston; Lieberman, A.P., Pitha, P.M., Shin, H.S., Shin, M.L., Production of tumor necrosis factor and other cytokines by astrocytes stimulated with lipopolysaccharide or a neurotropic virus (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 6348-6352; McCarthy, K.D., De Vellis, J., Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue (1980) J. Cell Biol., 85, pp. 890-902; Suzumura, A., Lavi, E., Bhat, S., Murasko, D.M., Weiss, S.R., Silberberg, D.H., Induction of glial cell MHC antigen expression in neurotropic coronavirus infection: Characterization of the H-2 inducing soluble factor elaborated by infected brain cells (1988) J. Immunol., pp. 2068-2072; Suzumura, A., Lavi, E., Weiss, S.R., Silberberg, D.H., Coronavirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes (1986) Science, 232, pp. 991-993; Wang, F.I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41","Wang, Q.; Division of Neuropathology, Dept. of Pathology/Lab. Medicine, University of Pennsylvania, Philadelphiam, PA 19104, United States",,,00652598,,AEMBA,"9782314","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751708
"Yamada Y.K., Takimoto K., Yabe M., Taguchi F.","55471420900;7004647272;7005872003;7103209890;","Requirement of proteolytic cleavage of the murine coronavirus MHV-2 spike protein for fusion activity",1998,"Advances in Experimental Medicine and Biology","440",,,"89","93",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754017&partnerID=40&md5=7d118cac44b78ad6b1f631c3d3b2e7b2","National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama Tokyo 208, Japan; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira Tokyo 187, Japan","Yamada, Y.K., National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama Tokyo 208, Japan; Takimoto, K., National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama Tokyo 208, Japan; Yabe, M., National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama Tokyo 208, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira Tokyo 187, Japan","The spike (S) protein of a non-fusogenic murine coronavirus, MHV-2, was compared to that of a variant, MHV-2f, with fusion activity. Two amino acids differed between the S proteins of these viruses; one was located in the signal sequence (amino acid 12) and the other in the putative cleavage site (amino acid 757). To determine which one of these amino acid changes is important for the alteration of fusogenicity, chimeric S proteins between MHV-2 and -2f were constructed and expressed in DBT cells by a vaccinia virus expression system. The results revealed that one amino acid change (Ser to Arg) at position 757 is responsible for the acquisition of fusogenicity of the MHV-2f S protein. This change also altered the susceptibility to proteolytic cleavage of the MHV-2 S protein which was originally uncleavable. We concluded that the non-fusogenic activity of MHV-2 results from the lack of cleavage of its S protein.",,"amino acid sequence; animal cell; article; chimera; coronavirus; dna cleavage; mouse; nonhuman; nucleotide sequence; priority journal; protein degradation; protein expression; syncytium; virus expression; virus isolation; Animals; Cell Line; Endopeptidases; Membrane Fusion; Membrane Glycoproteins; Mice; Murine hepatitis virus; Viral Envelope Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Vaccinia; Vaccinia virus","Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutation analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M.C., RNA recombination of murine coronaviruses: Recombination between fusion-positive mouse hepatitis A59 and fusion-negative mouse hepatitis virus 2 (1988) J. Virol., 62, pp. 1989-1998; Stauber, R., Pfleiderera, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a Murine Coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219","Yamada, Y.K.; Natl. Institute of Infectious Dis., 4-7-1 Gakuen, Musashimurayama, Tokyo 208, Japan",,,00652598,,AEMBA,"9782269","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754017
"Saeki K., Ohtsuka N., Taguchi F.","36854828200;7005191275;7103209890;","Isolation and characterization of murine coronavirus mutants resistant to neutralization by soluble receptors",1998,"Advances in Experimental Medicine and Biology","440",,,"11","16",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721166&partnerID=40&md5=5fa57b47a1455fad7b40bc371a33da7e","Division of Animal Models for Human Diseases, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Saeki, K., Division of Animal Models for Human Diseases, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Ohtsuka, N., Division of Animal Models for Human Diseases, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan; Taguchi, F., Division of Animal Models for Human Diseases, National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan","Murine coronavirus mutants resistant to neutralization with soluble receptors were isolated to study the receptor-binding site on the S proteins since such mutants were expected to have mutations in an important site for receptor-binding. We have isolated five soluble receptor-resistant (srr) mutants which had mutations of a single amino acid at 3 different positions in S protein. Srr mutant 11 with an amino acid change at position 65 (Leu to His) in the S1 subunit showed an extremely reduced binding by virus overlay protein blot assay. However srr mutants with a mutation at 1114 (Leu to Phe) (srr mutants 3, 4 and 7) or 1163 (Cys to Phe) (srr mutant 18) in the S2 subunit had receptor-binding activity similar to that of wild type cl-2. These results suggest that an amino acid at position 62 located in a conserved region among MHV strains is in particular important for receptor binding. We also discuss why srr mutants with a mutation in S2 showed high resistance to neutralization by soluble receptor, irrespective of their binding to MHV receptors.",,"amino terminal sequence; animal cell; article; coronavirus; drug receptor binding; mouse; nonhuman; priority journal; protein domain; site directed mutagenesis; virus characterization; virus isolation; virus mutant; virus neutralization; virus virulence; Animals; Antigens, CD; Cell Adhesion Molecules; Genes, Viral; Glycoproteins; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutation; Receptors, Virus; Sequence Analysis, DNA; Solubility; Viral Envelope Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion (1982) Virology, 119, pp. 358-371; Colston, E., Racaniello, V.R., Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor (1994) EMBO J., 13, pp. 5855-5862; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van Der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike of coronaviruses (1988) J. Mol. Biol., 196, pp. 963-966; Flory, E., Pfleiderer, M., Stuhler, A., Wege, H., Induction of protective immunity against coronavirus-induced encephalomyelitis: Evidence for an important role of CD8+ T cells in vivo (1993) Eur. J. Immunol., 23, pp. 1757-1761; Fuerst, T.R., Earl, P.L., Moss, B., Use of hybrid vaccinia virus-T7 RNA polymerase system for the expression of target genes (1987) Mol. Cell. Biol., 7, pp. 2538-2544; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J. Virol., 71, pp. 3129-3137; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1-specific monoclonal antibody (1994) Virology, 2202, pp. 814-824; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Matsubara, Y., Watanabe, R., Taguchi, F., Neurovirulence of six different murine coronavirus JHMV variants for rats (1991) Virus Res., 20, pp. 45-58; Ohtsuka, N., Yamada, Y.K., Taguchi, F., Difference in virus-binding activity of two distinct receptor proteins for mouse hepatitis virus (1996) J. Gen. Virol., 77, pp. 1683-1692; Routledge, E., Stauber, R., Pfleiderer, M., Siddell, S.G., Analysis of murine coronavirus surface glycoprotein functions by using monoclonal antibodies (1991) J. Virol., 65, pp. 254-262; Stauber, R., Pfleiderer, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Sturman, L.S., Holmes, K.V., Proteolytic cleavage of peplomer glycoprotein E2 of MHV yields two 90 K subunits and activates cell fusion (1984) Adv. Exp. Med. Biol., 173, pp. 25-35; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536","Saeki, K.; Div. of Animal Models for Human Dis., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187, Japan",,,00652598,,AEMBA,"9782259","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721166
"De Haan C.A.M., Vennema H., Rottier P.J.M.","7003682643;7003697291;7006145490;","Coronavirus envelope assembly is sensitive to changes in the terminal regions of the viral M protein",1998,"Advances in Experimental Medicine and Biology","440",,,"367","375",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031754153&partnerID=40&md5=875864e31ebe4ad6cd0d04aa5b6585eb","Institute of Virology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","De Haan, C.A.M., Institute of Virology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Vennema, H., Institute of Virology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Department of Infectious Diseases and Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Recently we demonstrated that the co-expressed coronavirus membrane proteins have the capacity to assemble vital envelopes which are similar to normal virus particles in dimensions and appearance, and which can form independent of a nucleocapsid (Vennema et al., 1996). For the formation of these particles only the M and the E protein are required; the S protein is dispensable but is incorporated when present. As we illustrate here, this virus-like particle assembly system is an ideal tool to study the interactions between the essential assembly partners M and E in molecular detail. Taking a mutagenetic approach we demonstrate that envelope assembly is critically sensitive to changes in the primary structure of both terminal domains of the M protein. The effects were most dramatically observed after mutation of the carboxy-terminal domain where the deletion of just one single amino acid at the extreme terminus abolished particle formation almost completely. But also some subtle mutations in the amino-terminal domain were severely inhibitory to the assembly process. Interestingly, mutant M proteins that were themselves incompetent to support particle formation appeared to inhibit, in a concentration dependent manner, the assembly of particles by wild-type M and E protein.",,"membrane protein; virus protein; amino acid sequence; amino terminal sequence; article; carboxy terminal sequence; controlled study; coronavirus; nonhuman; priority journal; virus envelope; virus particle; Amino Acid Sequence; Binding Sites; Cell Line; Cytoplasm; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Viral Envelope Proteins; Viral Matrix Proteins; Virion; Virus Assembly; Coronavirus","Arpin, N., Talbot, P.J., Molecular characterization of the 229E strain of human coronavirus (1990) Adv. Exp. Med. Biol., 276, pp. 73-80; De Vries, A.A.F., Raamsman, M.J.B., Van Dijk, H.A., Horzinek, M.C., Rottier, P.J.M., The small envelope glycoprotein (Gs) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer (1995) J. Virol., 69, pp. 344-3448; Delchambre, M., Gheysen, D., Thines, D., Thiriart, C., Jacobs, E., Verdin, E., Horth, M., Bex, F., The Gag precursor of simian immunodeficiency virus assembles into virus-like particles (1989) EMBO J., 8, pp. 2653-2660; Ekström, M., Liljeström, P., Garoff, H., Membrane protein lateral interactions control Sernliki Forest virus budding (1994) EMBO J., 13, pp. 1058-1064; Gheysen, D., Jacobs, E., De Foresta, A., Thiriart, C., Francotte, M., Thines, D., De Wilde, M., Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected cells (1989) Cell, 59, pp. 103-112; Hobman, T.C., Lundstrom, M.L., Mauracher, C.A., Woodward, L., Gilliam, S., Farquhar, M.G., Assembly of rubella virus structural proteins into virus-like particles in transfected cells (1994) Virology, 115, pp. 574-585; Klumperman, J., Krijnse Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion buddin (1994) J. Virol., 68, pp. 6523-6534; Krijnse Locker, J., Opstelten, D.-J.E., Ericsson, M., Horzinek, M.C., Rottier, P.J.M., Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention (1995) J. Biol. Chem., 270, p. 88158821; Mead, D.A., Szczesna-Skorupa, E., Kemper, B., Single-stranded DNA 'blue' T7 promotor plasmids: A versatile tandem promotor system for cloning and protein engineering (1986) Prot. Engineering, 1, pp. 67-74; Mebatsion, T., König, M., Conzelman, K.-K., Budding of rabies virus particles in the absence of the spike glycoprotein (1996) Cell, 84, pp. 941-951; Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Rottier, P.J.M., Brandenburg, D., Armstrong, J., Van Der Zeijst, B.A.M., Warren, G., Assembly in vitro of a spanning membrane protein of the endoplasmatic reticulum: The E1 glycoprotein of coronavirus mouse hepatitis virus A59 (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 1421-1425; Rottier, P.J.M., Krijnse Locker, J., Horzinek, M.C., Spaan, W.J.M., Expression of MHV-A59 M glycoprotein: Effects of deletions on membrane integration and intracellular transport (1990) Adv. Exp. Med. Biol., 276, pp. 127-135; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S. G. Siddell (ed.), Plenum Press, New York; Schalich, J., Allison, S.L., Stiasny, K., Mandl, C.J., Kunz, C., Heinz, F.X., Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions (1996) J. Virol., 70, pp. 4549-4557; Simon, K., Lingappa, V.R., Ganem, D., Secreted hepatitis B surface antigen polypeptides are derived from a transmembrane precursor (1988) J. Cell Biol., 107, pp. 2163-2168; Suomalainen, M., Liljeström, P., Garoff, H., Spike protein-nucleocapsid interations drive the budding of alphaviruses (1992) J. Virol., 66, pp. 4737-4747; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of corona virus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028","De Haan, C.A.M.; Institute of Virology, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,00652598,,AEMBA,"9782305","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031754153
"Baudoux P., Besnardeau L., Carrat C., Rottier P., Charley B., Laude H.","57199559554;6602382869;6603249904;7006145490;7004130118;7006652624;","Interferon alpha inducing property of coronavirus particles and pseudoparticles",1998,"Advances in Experimental Medicine and Biology","440",,,"377","386",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721783&partnerID=40&md5=1434e12fe64b2f75be706c5d567009ef","Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France; Institute of Virology, Veterinary Faculty, Utrecht University, Netherlands","Baudoux, P., Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France; Besnardeau, L., Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France; Carrat, C., Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France; Rottier, P., Institute of Virology, Veterinary Faculty, Utrecht University, Netherlands; Charley, B., Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France; Laude, H., Unite de Virologie Immunologie Moléculaires, INRA, Jouy-en-Josas, France","Previous work in our laboratory have provided evidence that the membrane glycoprotein M of TGEV is centrally involved in efficient induction of alpha interferon (IFN-α) synthesis by non-immune peripheral blood mononuclear cells incubated with fixed, TGEV-infected cells or inactivated virions. Here we report recent completion of studies initiated to get a better understanding of the nature of the interferogenic determinant(s). Transfected cells expressing TGEV M together with the minor structural component E (formerly called sM) were found to trigger IFN-α synthesis. Co-expression of these two proteins was shown to be necessary and sufficient for assembly and release of pseudoparticles resembling TGEV virions. Purified pseudoparticles exhibited an interferogenic activity close to that of authentic virions. Chimeric recombinant particles expressing BCV M ectodomain also induced IFN. Examination of cell cultures infected by viruses representative of the three Nidovirales genera revealed that the capacity to act as an efficient IFN-α inducer is a common feature of viral particles of the coronavirus genus. Altogether these data bring new insights regarding the putative nature of the viral structure involved in IFN-α induction.",,"alpha interferon; chimeric protein; virus glycoprotein; animal cell; arterivirus; article; controlled study; coronavirus; enzyme linked immunosorbent assay; interferon production; mononuclear cell; nonhuman; priority journal; protein expression; swine; torovirus; virus particle; Animals; Cell Line; Cercopithecus aethiops; Coronavirus; Coronavirus, Bovine; Cricetinae; Gene Expression; Humans; Interferon-alpha; Recombinant Fusion Proteins; Transmissible gastroenteritis virus; Vero Cells; Viral Envelope Proteins; Viral Matrix Proteins; Virion; Virus Assembly; Virus Replication; Animalia; Arterivirus; Bovine coronavirus; Coronavirus; Nidovirales; Sus scrofa; Torovirus; Transmissible gastroenteritis virus","Baudoux, P., Charley, B., Laude, H., Recombinant expression of the TGEV membrane protein (1995) Adv. Exp. Med. Biol., 380, pp. 305-310. , ""Coronaand related viruses"" P. Talbot & G. Levy Eds; Charley, B., Laude, H., Induction of interferon alpha by transmissible gastroenteritis coronavirus : Role of transmembrane glycoprotein E1 (1988) J. Urol., 62, pp. 8-11; Fitzgerald-Bocarsly, P., Human Natural Interferon-a producing cells (1993) Pharmacol. Ther., 60, pp. 39-62; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; La Bonnardière, C., Laude, H., High interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infec. Immun., 32, pp. 28-31; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis coronavirus I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by coronavirus TGEV (1992) J. Virol., 66, pp. 743-749; Laude, H., Rasschaert, D., Huet, J.C., Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis Virus (1987) J. Gen. Virol., 68, pp. 1687-1693; Riffault, S., Carrat, C., Besnardeau, L., La Bonnardiere, C., Charley, B., In vivo induction of interferon-a in pig by non-infectious coronavirus: Tissue localization and in situ phenotypic characterization of interferon-a producing cells (1997) J. Gen. Virol., 78, pp. 2483-2487; Savoysky, E., Boireau, P., Finance, C., Laporte, J., Sequence and analysis of BECV F15 matrix protein (1990) Res. Virol., 141, pp. 411-425; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Vorhout, W.F., Horzinek, M.C., Opstelten, D.-J., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus -like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Woloszyn, N., Boireau, P., Laporte, J., Nucleotide sequence of the bovine enteric coronavirus F15 mRNA 5 and mRNA 6 unique regions (1990) Nucl. Ac. Res., 18, p. 1303","Baudoux, P.; Unite Virol. Immunol. Moleculaires, INRA, Jouy-en-Josas, France",,,00652598,,AEMBA,"9782306","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721783
"Wege H., Schluesener H., Meyermann R., Barac-Latas V., Suchanek G., Lassmann H.","7005516649;7006032773;55796798200;6506163291;6603076780;35420677900;","Coronavirus infection and demyelination: Development of inflammatory lesions in Lewis rats",1998,"Advances in Experimental Medicine and Biology","440",,,"437","444",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783814&partnerID=40&md5=42d2899dc229cd7fb0a944ed27b01a62","Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany; Institute of Brain Research, D-72076 Tübingen, Germany; Institute of Neurology, A-1090 Vienna, Austria","Wege, H., Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany; Schluesener, H., Institute of Brain Research, D-72076 Tübingen, Germany; Meyermann, R., Institute of Brain Research, D-72076 Tübingen, Germany; Barac-Latas, V., Institute of Neurology, A-1090 Vienna, Austria; Suchanek, G., Institute of Neurology, A-1090 Vienna, Austria; Lassmann, H., Institute of Neurology, A-1090 Vienna, Austria","Coronavirus infections of rodents can cause diseases of the central nervous system characterised by inflammatory demyelination. The lesions mimick in many aspects the pathology of multiple sclerosis in humans and of other neurological diseases. As an animal model for demyelination, we studied the MHV-JHM induced encephalomyelitis of Lewis rats. The pathomorphological analysis revealed patterns of lesions which developed in stages. Infected oligodendrocytes were first destroyed by necrosis. Later stages were characterized by demyelinated plaques. In the center of plaques, no virus antigen was found and oligodendrocytes were mainly destroyed by apoptosis. At the edge of plaques, virus antigen was expressed in parallel to infiltrations consisting of lymphocytes and macrophages. The prevailing mechanisms leading to demyelination may change individually and during defined stages of the disease. The transcriptional expression of chemoattractants and other mediators of inflammation was studied by semiquantitative RT-PCR. Virus induced inflammatory demyelination was accompanied by high expression of a relatively novel cytokine, the endothelial monocyte activating polypeptide II (EMAP II). By immunocytochemistry, EMAP II was detected in parenchymal microglia located both within the lesions and in unaffected areas. Furthermore, the level of transcriptional expression of the regulatory calcium binding S100 proteins MRP8, MRP14 and CP10 was associated with inflammatory demyelination and expression of IFN γ, IL-2, TNF α, and iNOS.",,"cytokine; endothelial monocyte activating polypeptide ii; gamma interferon; interleukin 2; nitric oxide synthase; protein s 100; tumor necrosis factor alpha; unclassified drug; virus antigen; animal experiment; animal model; animal tissue; apoptosis; article; controlled study; demyelination; encephalomyelitis; immunocytochemistry; immunomodulation; inflammatory disease; lymphocyte; macrophage; microglia; murine hepatitis coronavirus; nonhuman; oligodendroglia; priority journal; rat; Animals; Brain; Central Nervous System; Coronavirus Infections; Cytokines; Demyelinating Diseases; Gene Expression; Mice; Murine hepatitis virus; Neoplasm Proteins; Nitric Oxide Synthase; Rats; Rats, Inbred Lew; RNA-Binding Proteins; Spinal Cord; Transcription, Genetic; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Rodentia","Barac-Latas, V., Suchanek, G., Breitschopf, H., Stühler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in coronavirus induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, 19, pp. 1-12; Bhardwaj, R.S., Zotz, C., Zwadlo-Klarwasser, G., Roth, J., Goebeler, M., Mahnke, K., Falk, M., Sorg, C., The calcium-binding proteins MRP8 and MRP14 form a membrane-associated heterodimer in a subset of monocytes/macrophages present in acute but absent in chronic inflammatory lesions (1992) Eur. J. Immunol., 22, pp. 1891-1897; Breitschopf, H., Suchanek, G., Gould, R.M., Colman, D.R., Lassmann, H., In situ hybridization with digoxigenin-labeled probes: Sensitive and reliable dedection method applied to myelinating rat brain (1992) Acta Neuropathol., 84, pp. 581-587; Fazakerley, J.K., Buchmeier, M., Pathogenesis of virus-induced demyelination (1993) Adv. Virus Res., 42, pp. 249-324; Flory, E., Stühler, A., Barac-Latas, V., Lassmann, H., Wege, H., Coronavirus induced encephalomyelitis: Balance between protection and immune pathology depends on the immunization schedule with spike protein S (1995) J. Gen. Virol., 76, pp. 873-879; Gold, R., Schmied, M., Giegerich, G., Breitschopf, H., Hartung, H.P., Toyka, K.V., Lassmann, H., Differentiation between cellular apoptosis and necrosis by combined use of in situ tailing and nick translation techniques (1994) Lab Invest., 71, pp. 219-225; Imamichi, T., Uchida, I., Wahl, S.M., McCartney-Francis, N., Expression and cloning of migration inhibitory factor-related protein MRP 8 and MRP14 in arthritis-susceptible rats (1993) Biochem. Biophys. Res. Comm., 194, pp. 819-825; Kao, J., Houck, K., Fan, Y., Haehnel, I., Libutti, S.K., Kayton, M.L., Grikscheit, T., Stern, D.M., Characterization of a novel tumor-derived cytokine - Endothelial-monocyte activating polypeptide II (1994) J. Biol. Chem., 269, pp. 25106-25119; Körner, H., Schliephake, A., Winter, J., Zimprich, F., Lassmann, H., Sedgwick, J., Siddell, S.G., Wege, H., Nucleocapsid or spike protein-specific CD4+ T-lymphocytes protect against coronavirus-induced encephalomyelitis in the absence of CD8+ T-cells (1991) J. Immunol., 147, pp. 2317-2323; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Lackmann, M., Rajasekariah, P., Lismaa, S.E., Jones, G., Cornish, C.J., Hu, S.P., Simpson, R.J., Geczy, C.L., Identification of a chemotactic domain of the proinflammatory S 100 protein CP-10 (1993) J. Immunol., 150, pp. 2981-2991; Linington, C., Bradl, M., Lassmann, H., Brunner, C., Vass, K., Augmentation of demyelination in rat acute allergic encephalomyelitis by circulating mouse monoclonal antibodies against myelin/oligodendroglia glycoprotein (1988) Am. J. Pathol., 130, pp. 443-454; Ozawa, K., Suchanek, G., Breitschopf, H., Brueck, W., Budka, H., Jellinger, K., Lassmann, H., Patterns of oligodendroglia pathology in multiple sclerosis (1994) Brain, 117, pp. 1311-1322; Pearce, B.D., Hobbs, V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol., 68, pp. 5483-5495; Piddlesden, S., Lassmann, H., Zimprich, F., Morgan, B.P., Linington, C., The demyelinating potential of antibodies to myelin oligodendrocyte glycoprotein is related to their ability to fix complement (1993) Am. J. Pathol., 143, pp. 555-564; Stühler, A., Flory, E., Wege, H., Lassmann, H., Wege, H., No evidence for quasispecies populations during persistence of the coronavirus mouse hepatitiis virus JHM: Sequence conservationwithin the surface glycoprotein gene S in Lewis rats (1997) J. Gen. Virol., 78, pp. 747-756; Schluesener, H.J., Seid, K., Zhao, Y., Meyermann, R., Localization of endothelial-monocyte-activating polypeptide II (EMAP II), a novel proinflammatory cytokine, to lesions of experimental autoimmune encephalomyelitis, neuritis and uveitis (1997) Glia, , In press; Stohlmann, S.A., Bergmann, C.C., Van Der Veen, R.C., Hinton, D.R., Mouse hepatitis virus-specific cytotoxic T lymphocytes protect from lethal infection without eliminating virus from the central nervous system (1995) J. Virol., 69, pp. 684-694; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions by BMP stimulated lymphocytes from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Semin, in Immunopathol., 17, pp. 133-148; Wege, H., Watanabe, R., Ter Meulen, V., Relapsing subacute demyelinating encephalomyelitis in rats in the course of coronavirus JHM infection (1984) J. Neuroimmunol., 6, pp. 325-336; Zimprich, F., Winter, J., Wege, H., Lassmann, H., Coronavirus induced primary demyelination: Indications for the involvement of a humoral immune response (1991) Neuropathol. Appl. Neurobiol., 17, pp. 469-484","Wege, H.; Institute of Diagnostic Virology, Fed. Res. Ctr. for Virus Dis. Anim., Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany",,,00652598,,AEMBA,"9782312","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783814
"Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.","6603799081;6506004042;6701508835;7006444628;7102624625;","Further analysis of the genome of porcine epidemic diarrhoea virus",1998,"Advances in Experimental Medicine and Biology","440",,,"781","786",,30,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751710&partnerID=40&md5=90c0ed8efee4756dc6d5599b3274f988","Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Institute of Virology, Church Street, Glasgow G11 5JR, United Kingdom","Bridgen, A., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland, Institute of Virology, Church Street, Glasgow G11 5JR, United Kingdom; Kocherhans, R., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Tobler, K., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Carvajal, A., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Ackermann, M., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland","We report here the continued determination and analysis of the nucleotide sequence of both wild type (wt) and cell culture adapted (ca) porcine epidemic diarrhoea coronavirus (PEDV). These studies were undertaken with two objectives in mind: the identification of common and divergent features in the genomic sequences of wt and ca PEDV which can explain the differences in virulence of these isolates and the further exploration of the relationship of PEDV to other coronaviruses.",,"article; coronavirus; genetic analysis; molecular cloning; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; virogenesis; virus genome; Animals; Cell Culture Techniques; Cloning, Molecular; Coronavirus; Genome, Viral; Open Reading Frames; Polymerase Chain Reaction; Swine; Transcription, Genetic; Coronavirus; Porcine epidemic diarrhea virus; Suidae","Bernasconi, C., Guscetti, F., Utiger, A., Van Reeth, K., Ackermann, M., Pospischil, A., Experimental infection of gnotobiotic piglets with a cell culture adapted porcine epidemic virus: Clinical, histopathological and immunohistochemical findings (1995) Immunobiology of Viral Infections, pp. 542-546. , (M. Schwyzer, M. Ackermann, G. Bertoni, R. Kocherhans, K. McCullough, M. Engels, R. Wittek, and R. Zanoni, eds.), Fondation Marcel Merieux, Lyon, France; Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen. Virol., 74, pp. 1795-1804; Bridgen, A., Tobler, K., Ackermann, M., Identification of coronaviral conserved sequences and application to viral genome amplification (1994) Adv. Exp. Med. Biol., 342, pp. 81-82. , Coronaviruses: Molecular Biology and Virus-Host Interactions (H. Laude and J-F. Vautherot, eds.); Carvajal, A., Lanza, I., De Arriba, M.L., Rubio, P., Del Pozo, M., Ackermann, M., Carmenes, P., Preliminary characterisation of a Spanish isolate of porcine epidemic diarrhoea coronavirus (1995) IVth National Virology Congress, , Madrid, 21-23 September 1995; Duarte, M., Laude, H., Sequence of the spike protein of the porcine epidemic diarrhoea virus (1994) J. Gen. Virol., 75, pp. 1195-1200; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF (1994) Virology, 198, pp. 466-476; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Tobler, K., Ackermann, M., PEDV leader and junction sites (1995) Adv. Exp. Med. Biol., 380, pp. 541-542. , Corona- and Related Viruses (P.J. Talbot and G.A. Levy, eds.)","Bridgen, A.; Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057 Zurich, Switzerland",,,00652598,,AEMBA,"9782358","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751710
"Luo Z., Weiss S.R.","55460270800;57203567044;","Mutational analysis of fusion peptide-like regions in the mouse hepatitis virus strain A59 spike protein",1998,"Advances in Experimental Medicine and Biology","440",,,"17","23",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753580&partnerID=40&md5=d471fc4f68aa9701cc56b65eacc292a3","Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States","Luo, Z., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States","The coronavirus peplomer protein S is responsible for attachment and fusion during viral entry as well as for the induction of cell to cell fusion. While several regions within S have been shown to influence the ability to induce fusion, the region of the protein actually responsible for fusion, the fusion peptide, has not yet been identified. We identified two hydrophobic peptides (peptides 1 and 2) within MHV-A59 S2 as possible fusion domains. This was based on hydrophobicity, conservation among coronavirus S proteins and the prediction of a sided helix conformation. Using site directed mutagenesis and an in vitro cell to cell fusion assay we showed that substitution of hydrophobic amino acids with charged amino acids, within the predicted hydrophobic face of either of these two peptides eliminated fusion. Within peptide 1 substitution of the same hydrophobic amino acids with other hydrophobic amino acids or substitution of polar amino acids with charged or polar amino acids had little effect on fusion. Thus peptides 1 and 2 remain likely candidates for the MHV fusion peptide. A third previously identified peptide within S2 (Chambers et al., 1990) is unlikely as a fusion peptide as it is not well conserved among coronaviruses and substitution within the hydrophobic face with charged amino acids does not effect fusion.",,"peptide; alpha helix; animal cell; article; cell fusion; coronavirus; gene mutation; hepatitis virus; hydrophobicity; lipid bilayer; mouse; nonhuman; peptide synthesis; priority journal; protein domain; protein processing; site directed mutagenesis; Amino Acid Sequence; Animals; Membrane Fusion; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Peptides; Viral Envelope Proteins; Animalia; Coronavirus; Murine hepatitis virus","Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell to cell fusion (1996) Virology, 214, pp. 453-463; Chambers, P., Pringle, C.R., Easton, A.J., Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins (1990) J. Gen. Virol., 71, pp. 3075-3080; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization resistant variants of a neurotropic coronavirus are generated by deletions within the amino terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Gallaher, W.R., Segrest, J.P., Hunter, E., Are fusion peptides really ""sided"" insertional helices? (1992) Cell, 70, pp. 531-532; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virusA59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Landt, O., Grunert, H.P., Hahn, U., A general method for rapid site directed mutagenesis (1990) Gene, 96, pp. 125-128; Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virrus glycoproteins analyzeed by a novel recombinant vacciniavirus-based assay qunatitating cell fusion-dependent reporter gene activation (1994) J. Virol., 68, pp. 5411-5422; Pereira, F.B., Goni, F.M., Nieva, J.L., Liposome destabilisation induced by the HIV fusion peptide: Effect of single aminom acid changes (1995) FEBS Letters, 362, pp. 2243-2246; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; White, J., Membrane fusion (1992) Science, 258, pp. 917-924; White, J.M., Viral and cellular membrane fusion proteins (1990) Ann. Rv. Physiol., 52, pp. 675-697","Luo, Z.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States",,,00652598,,AEMBA,"9782260","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753580
"Stirrups K., Shaw K., Evans S., Dalton K., Cavanagh D., Britton P.","57210222541;7202206256;7402709581;7006042187;26642890500;57203302770;","Rescue of IBV D-RNA by heterologous helper virus strains",1998,"Advances in Experimental Medicine and Biology","440",,,"259","264",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031781369&partnerID=40&md5=80f0881b362ef5fcb31d64e70e3e38d5","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom","Stirrups, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Evans, S., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Dalton, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom","Coronavirus defective RNA (D-RNA) vectors could be developed to deliver selected genes for the production of recombinant coronavirus vaccines. An IBV D-RNA, CD-61, derived from a naturally occurring IBV Beaudette D-RNA, CD-91, is being developed as a D-RNA vector for IBV. In order to use CD-61 as a vector it will require rescue by heterologous strains in addition to Beaudette. Rescue will be determined by recognition of replication and packaging signals within the D-RNA by the helper virus. The 5' and 3' UTRs are believed to contain sequences involved in replication and transcription. The 5' and 3' UTRs of six strains of IBV have been sequenced and experiments performed using six strains of helper virus for rescue of CD-61 to determine whether rescue correlates with sequence conservation within the 5' and 3' UTRs. Results indicate that all strains of helper virus rescued the D-RNA to varying degrees. Sequence comparisons show a high degree of sequence identity in the UTRs, but enough strain differences exist to be used as markers. The 5' and 3' UTRs of the D-RNAs rescued by the heterologous strains were also sequenced and leader switching between the helper virus and the Beaudette leader on the D-RNAs was observed.",,"virus rna; article; gene targeting; helper virus; nonhuman; priority journal; rna replication; rna transcription; sequence analysis; strain difference; vaccine production; virus replication; 3' Untranslated Regions; 5' Untranslated Regions; Animals; Base Sequence; DNA, Viral; Helper Viruses; Infectious bronchitis virus; Molecular Sequence Data; RNA, Viral; Avian infectious bronchitis virus; Coronavirus","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Chang, R.-Y., Krishnan, R., Brian, D.A., The UCUAAAC Promoter motif is not required for high efficiency leader recombination in bovine coronavirus defective interfering RNA (1996) J. Virol., 70, pp. 2720-2729; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Ann. Rev. Microbiol., 44, pp. 303-333; Makino, S., Lai, M.M.C., High frequency leader switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of Avian coronavirus Infectious Bronchitis Virus (1994) Virology, 203, pp. 286-293; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Analysis of a hypervariable region in the 3′ non-coding region of the infectious bronchitis virus genome (1993) Virus Res., 28, pp. 19-27; Zhang, L., Homberger, F., Spaan, W., Luytjes, W., Recombinant genomic RNA of Coronavirus MHV-A59 after coreplication with a di RNA containing the MHV-RI spike gene (1997) Virology, 230, pp. 93-102; Zwaagstra, K.A., Van Der Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1991) J. Clin. Microbiol., 30, pp. 70-84","Stirrups, K.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom",,,00652598,,AEMBA,"9782290","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031781369
"Tahara S.M., Dietlin T.A., Nelson G.W., Stohlman S.A., Manno D.J.","7103354164;6602911334;7402779709;35502534500;7005705895;","Mouse hepatitis virus nucleocapsid protein as a translational effector of viral mRNAs",1998,"Advances in Experimental Medicine and Biology","440",,,"313","318",,33,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753101&partnerID=40&md5=0a911d6f748addb4d540c73104dcaf03","Department of Molecular Microbiology and Immunology; Department of Neurology, USC, School of Medicine, Los Angeles, CA 90033, United States","Tahara, S.M., Department of Neurology, USC, School of Medicine, Los Angeles, CA 90033, United States; Dietlin, T.A., Department of Molecular Microbiology and Immunology; Nelson, G.W., Department of Molecular Microbiology and Immunology; Stohlman, S.A., Department of Neurology, USC, School of Medicine, Los Angeles, CA 90033, United States; Manno, D.J., Department of Molecular Microbiology and Immunology","The mouse hepatitis virus (MHV) nucleocapsid protein stimulated translation of a chimeric reporter mRNA containing an intact MHV 5'- untranslated region and the chloramphenicol acetyltransferase (CAT) coding region. The nucleocapsid protein binds specifically the tandemly repeated - UCYAA- of the MHV leader. This RNA sequence is the same as the intergenic motif found in the genome RNA. Preferential translation of viral mRNA in MHV infected cells is stimulated in part by this interaction and represents a specific, positive translational control mechanism employed by coronaviruses.",,"messenger rna; virus rna; article; murine hepatitis coronavirus; nonhuman; priority journal; rna sequence; rna translation; sequence analysis; virus transcription; Animals; Cell Line; Gene Expression Regulation, Viral; Mice; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; Protein Biosynthesis; RNA, Messenger; RNA, Viral; Coronavirus; Felis catus; Murinae; Murine hepatitis virus; RNA viruses","Bradford, M., A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of dye binding (1976) Anal. Biochem., 72, pp. 248-254; Cullen, B., Malim, M.H., Secreted placental alkaline phosphatase as a eukaryotic reporter gene (1992) Meth. Enzymol., 216, pp. 362-368; Gorman, C.M., Moffat, L.F., Howard, B.H., Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells (1982) Molec. Cell. Biol., 2, pp. 1044-1051; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol., 67, pp. 923-932; Kyuwa, S., Cohen, M., Nelson, G., Tahara, S.M., Stohlman, S.A., Modulation of cellular macromolecular synthesis by coronavirus: Implication for pathogenesis (1994) J. Virol., 68, pp. 6815-6819; Lin, A.Y., Chang, S.C., Lee, A.S., A calcium ionophore-inducible cellular promoter is highly active and has enhancerlike properties (1986) Molec. Cell Biol., 6, pp. 1235-1243; Nelson, G.W., (1996), Ph.D. Dissertation. (University of Southern California, Los Angeles, CA); Nelson, G.W., Stohlman, S.A., Localization of the RNA-binding domain of mouse hepatitis virus nucleocapsid protein (1993) J. Gen. Virol., 74, pp. 1975-1979; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schneider, R., Shenk, T., Impact of virus infection on host cell protein synthesis (1987) Annu. Rev. Biochem., 56, pp. 317-332; Siddell, S., Wege, H., Barthel, A., Ter Meulen, V., Intracellular protein synthesis and the in vitro translation of coronavirus JHM mRNA (1981) Adv. Exptl. Biol. Med., 142, pp. 193-207; Southern, P.J., Berg, P., Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter (1982) J. Mol. Appl. Gen., 1, pp. 327-341; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Van Marie, G., Luytjes, W., Van Der Most, R.G., Van Der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Zhang, X., Liao, C.-L., Lai, M.M.-C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Tahara, S.M.; Department of Neurology, USC School of Medicine, Los Angeles, CA 90033, United States",,,00652598,,AEMBA,"9782298","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753101
"Thiel V., Siddell S.G., Herold J.","35238592100;7005260816;7006838690;","Replication and transcription of HCV 229E replicons",1998,"Advances in Experimental Medicine and Biology","440",,,"109","113",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753581&partnerID=40&md5=46807b65f772e6eb2954733505491ef3","Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany","Thiel, V., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany; Herold, J., Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany","Replicons based upon the human coronavirus 229E (HCV 229E) genome were transfected into HCV 229E infected cells. We demonstrate that a synthetic RNA comprised of 646 nucleotides from the 5' end and 1465 nucleotides from the 3' end of the HCV 229E genome is replication competent. We conclude that the cis-acting elements necessary for replication are located in these 5' and 3' genomic regions. Furthermore, we inserted the intergenic region of the HCV 229E nucleocapsid protein gene into this basic construct and were able to demonstrate the transcription of 'subgenomic' RNAs.",,"article; coronavirus; dna template; nonhuman; priority journal; promoter region; replicon; rna sequence; virus cell interaction; virus genome; virus nucleocapsid; virus replication; virus transcription; Coronavirus; Coronavirus 229E, Human; Humans; Replicon; RNA, Viral; Transcription, Genetic; Coronavirus; Hepatitis C virus; human coronavirus; Human coronavirus 229E","Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Meinkoth, J., Wahl, G., Hybridization of nucleic acids immobilized on solid supports (1984) Anal.Biochem., 138, pp. 267-284; Van Der Most, R.G., Bredenbeck, P.J., Spaan, W.J.M., A domain at the 3' end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226","Thiel, V.; Institute of Virology and Immunology, University of Wuerzburg, Versbacherstr. 7, 97078 Wuerzburg, Germany",,,00652598,,AEMBA,"9782271","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753581
"Kim K.H., Narayanan K., Makino S.","7409323179;7101933409;7403067550;","Characterization of coronavirus DI RNA packaging",1998,"Advances in Experimental Medicine and Biology","440",,,"347","353",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031784046&partnerID=40&md5=a527ced5c424be948c597ecbb92a6ffb","Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States","Kim, K.H., Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States; Narayanan, K., Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States; Makino, S., Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States","Studies of defective interfering (DI) RNAs of mouse hepatitis virus (MHV), suggest that a 69 nt-long packaging signal, which is located about 20 kb from the 5'-end of the 31 kb-long MHV genomic RNA, is necessary and sufficient for MHV genomic RNA packaging into MHV particles. We demonstrated that use of a low pH culture medium combined with subsequent ultrafiltration increased MHV infectivity about 60 times over MHV preparations grown in neutral medium. Using this virus concentration procedure, we successfully prepared DI particle-rich MHV preparations. Characterization of virus samples released from the cells infected with DI particle-rich MHV revealed that infectious MHV genomic RNA was not required for packaging of DI RNAs. These data suggested that interaction of the DI packaging signal with an unidentified region(s) of helper virus genomic RNA is unlikely, and therefore unlikely to facilitate the packaging of MHV DI RNA into the MHV virion. Rather, both DI RNA and MHV genomic RNA probably use the packaging signal for RNA packaging.",,"virus envelope protein; virus rna; animal cell; article; controlled study; culture medium; genetic transfection; mouse; murine hepatitis coronavirus; nonhuman; ph; priority journal; rna transcription; ultrafiltration; virus infectivity; Animals; Cell Line; Defective Viruses; Hydrogen-Ion Concentration; Mice; Murine hepatitis virus; RNA, Viral; Virus Assembly; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Alexander, D.J., Collins, M.S., Effect of pH on the growth and cytopathogenicity of avian infectious bronchitis virus in chicken kidney cells (1975) Arch. Virol., 49, pp. 339-348; Bos, E.C.W., Luytjes, W., Van Der Muelen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Feigner, P.L., Gadek, T.R., Holm, M., Roman, R., Chan, H.W., Wenz, M., Northrop, J.P., Danielson, M., Lipofection: A high efficient, lipid- Mediated DNA-transfection procedure (1987) Proc. Natl. Acad. Sci. USA, 84, pp. 7413-7417; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J.Virol., 66, pp. 3522-3530; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte. Virusforch., 44, pp. 298-302; Kim, K.H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J.Virol., 71, pp. 3922-3931; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J.Virol., 26, pp. 236-242; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Urology, 180, pp. 567-582; Macnaughton, M.R., Davies, H.A., Nermut, M.V., Ribonucleoprotein-like structures from coronavirus particles (1978) J.Gen.Virol., 39, pp. 545-549; Makino, S., unpublished data; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J.Virol., 63, pp. 5285-5292; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Urology, 139, pp. 138-151; Makino, S., Shieh, C.-K., Keck, J.G., Lai, M.M.C., Defective-interfering particles of murine coronavirus: Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA- packaging signal (1990) J. Virol., 64, pp. 6045-6053; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J.Virol., 65, pp. 6031-6041; McMaster, G.K., Carmichael, G.G., Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 4835-4838; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis virus, strain A59 (1989) Virology, 171, pp. 141-148; Pocock, D.H., Garwes, D.J., The influence of pH on the growth and stability of transmissible gastroenteritis virus in vitro (1975) Arch. Virol., 49, pp. 239-247; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J.Virol., 71, pp. 824-1527","Kim, K.H.; Department of Microbiology, Inst. of Cellular/Molecular Biology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"9782302","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031784046
"Lim K.P., Liu D.X.","7403175857;8972667300;","Characterisation of a papain-like proteinase domain encoded by ORF1a of the coronavirus IBV and determination of the C-terminal cleavage site of an 87 kDa protein",1998,"Advances in Experimental Medicine and Biology","440",,,"173","184",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753726&partnerID=40&md5=79c8a82cc88b6b9343592389e2eae35d","Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","Lim, K.P., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Liu, D.X., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","Our previous studies have shown that two overlapping papain-like proteinase domains (PLPDs) encoded by the IBV sequence from nucleotides 4155 to 5550 is responsible for cleavage of the ORF 1a polyprotein to an 87 kDa protein. In this study, we demonstrate that only the more 5' one of the two domains, PLPD-1 encoded between nucleotides 4155 and 5031, is required for processing to the 87 kDa protein. Site-directed mutagenesis studies have shown that the Cys1274 and His1435 residues are essential for the PLPD-1 activity, suggesting that they may be the components of the catalytic centre of this proteinase. Coexpression and immunoprecipitation studies have further revealed that PLPD can interact with the 87 kDa protein. Meanwhile, data obtained from the construction and expression of a series of deletion mutants have indicated that the 87 kDa protein is encoded by the 5'- most 2600 bp part of ORF1a. Further deletion and mutagenesis studies are underway to determine precisely the C-terminal cleavage site of the 87 kDa protein.",,"papain; proteinase; amino acid sequence; article; carboxy terminal sequence; coronavirus; enzyme assay; nonhuman; nucleotide sequence; open reading frame; priority journal; protein degradation; sequence analysis; site directed mutagenesis; Animals; Binding Sites; Catalysis; Infectious bronchitis virus; Mutagenesis, Site-Directed; Papain; Protein Precursors; Viral Proteins; Avian infectious bronchitis virus; Coronavirus","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesises bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.Y., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Research, 17, pp. 4847-4860; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Laemmli, U.K., Cleavage of structural proteins during the assembly of the bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brierley, I., Tibbies, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus IBVis processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbies, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression and processing of an 87 kDa polypeptide encoded by ORF1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus IBV1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol, 208, pp. 48-57","Lim, K.P.; Institute of Molecular Agrobiology, 59A Fleming, 1 Science Park Drive, Singapore 118240, Singapore",,,00652598,,AEMBA,"9782279","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753726
"Liu D.X., Shen S., Xu H.Y., Brown T.D.K.","8972667300;7403431806;55703819800;56248391000;","Proteolytic processing of the polyprotein encoded by ORF1b of the coronavirus infectious bronchitis virus (IBV)",1998,"Advances in Experimental Medicine and Biology","440",,,"149","159",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721915&partnerID=40&md5=6ee7391165e125bc71e4a85e7dac6fc1","Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","Liu, D.X., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore, Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Shen, S., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","We present here evidence demonstrating that four previously predicted Q- S(G) cleavage sites, encoded by the IBV sequences from nucleotide 15129 to 15134, 16929 to 16934, 18492 to 18497, and 19506 to 19511, respectively, can be recognised and transcleaved by the 3C-like proteinase. Five mature products with sizes of approximately 100 kDa, 65 kDa, 63 kDa, 42 kDa and 35 kDa are released from the ORF1b polyprotein by the 3C-like proteinase- mediated cleavage at these positions. Meanwhile, expression of plasmids containing only the ORF1b region showed no autocleavage of the polyprotein encoded, suggesting that the 3C-like proteinase may be the sole proteinase involved in processing of the 1b polyprotein. These data may therefore represent a complete processing map of the polyprotein encoded by ORF1b of mRNA1.",,"amino acid sequence; animal cell; article; avian infectious bronchitis virus; coronavirus; dna cleavage; gene mutation; molecular recognition; nonhuman; polymerase chain reaction; priority journal; protein degradation; protein domain; protein processing; site directed mutagenesis; Antibodies; Binding Sites; Cysteine Endopeptidases; Endopeptidases; Eukaryotic Cells; Gene Expression; Infectious bronchitis virus; Metals; Protein Processing, Post-Translational; Proteins; RNA Helicases; Viral Proteins; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus","Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.Y., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nuc. Ac. Res., 17, pp. 4847-4860; Laemmli, U.K., Cleavage of structural proteins during the assembly of the bacteriophage T4 (1970) Nature (London), 227, pp. 680-1385; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Brown, T.D.K., Characterization and mutational analysis of an ORF-1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbies, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87-kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identificaiton of a 10 kDa polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820","Liu, D.X.; Institute of Molecular Agrobiology, 59A Fleming, 1 Science Park Drive, Singapore 118240, Singapore",,,00652598,,AEMBA,"9782277","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721915
"Banerjee S., Makino S.","55851941934;7403067550;","Studies of murine coronavirus DI RNA replication from negative-strand transcripts",1998,"Advances in Experimental Medicine and Biology","440",,,"241","246",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721428&partnerID=40&md5=134cb95d1d8ef4b66df30694d882407f","Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States","Banerjee, S., Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States; Makino, S., Department of Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States","The positive-strand transcripts as well as negative-strand transcripts of mouse hepatitis virus (MHV) defective interfering (DI) RNA, when introduced into MHV-infected cells, resulted in DI RNA replication and accumulation. The leader sequence of the majority of DI RNAs that accumulated from the expression of negative-strand DI RNA transcripts with no extra non- MHV nucleotides at the 3' end switched to that of helper virus, whereas this leader sequence switching did not occur in most of the positive-strand DI RNAs that accumulated from the expressed negative-strand DI RNA transcripts with extra non-MHV nucleotides at the 3' end. These data demonstrated that the extra 4 nucleotides at the 3'-end of negative-strand DI RNA transcripts affected leader sequence switching on DI RNA, and indicated that the leader switching probably occurred during positive-strand DI RNA synthesis.",,"virus rna; article; murine hepatitis coronavirus; nonhuman; priority journal; rna replication; rna sequence; rna transcription; sequence analysis; transcription regulation; virus replication; virus transcription; Animals; Cell Line; Defective Viruses; Mice; Murine hepatitis virus; RNA, Spliced Leader; RNA, Viral; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Chang, R.-Y., Krishnan, R., Brian, D., The UCUAAAC promoter motif is not required for high frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. Virol., 70, pp. 2720-2729; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombination vaccinia virus that synthesizes bacteriophage T7 polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Jeong, Y.S., Makino, S., Mechanism of coronavirus transcription:duration of primary transcription initiation activity and effect of subgenomic RNA transcription on RNA replication (1992) J. Virol., 66, pp. 3339-3346; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol.., 26, pp. 236-242; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNA of mouse hepatitis virus, a cytoplasmic virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Vlrol., 39, pp. 823-1334; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Leibowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Makino, S., Lai, M.M.C., High frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139, pp. 138-151; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand mRNA synthesis and effect of cyclohexamide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNA contain antileaders (1991) J. Virol., 65, pp. 320-325; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non- Contiguous sequences (1983) EMBO J., 2, pp. 1939-1944; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827","Banerjee, S.; Department of Microbiology, Inst. of Cellular/Molecular Biology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"9782287","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721428
"Woods R.D., Wesley R.D.","7401706916;7103154080;","Transmissible gastroenteritis coronavirus carrier sow",1998,"Advances in Experimental Medicine and Biology","440",,,"641","647",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031720836&partnerID=40&md5=6d19cb78e02b9a436fcdec0fe44bcb8f","Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States","Woods, R.D., Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States; Wesley, R.D., Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States","A sow infected with virulent transmissible gastroenteritis virus (TGEV) shed virulent virus in her feces for 18 months. The virus was isolated from rectal swabs beginning 2 days postexposure (PE) and continued at irregular intervals. Virus shedding was detected on 24 separate occasions. The titer of the virus shed ranged from &lt;1 x 102 pfu/ml to 7.2 x 103 pfu/ml, while the duration of the shedding ranged from I to 5 consecutive days. Inoculation of 3-day-old piglets with TGEV isolated from the sow proved the virus was virulent throughout the study. Virulent TGEV was isolated from the spleen, mesenteric lymph nodes, and the liver of the sow 544 days PE. This study demonstrates an apparently healthy sow can be a reservoir and shed virulent TGEV for an extended period of time.",,"animal experiment; animal model; animal tissue; article; coronavirus; nonhuman; priority journal; swine disease; virus carrier; virus shedding; virus titration; virus virulence; Animals; Female; Gastroenteritis, Transmissible, of Swine; Swine; Transmissible gastroenteritis virus; Animalia; Coronavirus; Sus scrofa; Transmissible gastroenteritis virus","Cook, D., Hill, H., Taylor, J., Oral transmission of transmissible gastroenteritis virus by muscle and lymph node from slaughtered pigs (1991) Aust. Vet. J., 68, pp. 68-70; Frederick, G.T., Bohl, E.H., Local and systemic cell-mediated immunity against transmissible gastroenteritis, an intestinal viral infection of swine (1976) J. Immunol., 116, pp. 1000-1004; Gough, P.M., Jorgenson, R.D., Identification of porcine transmissible gastroenteritis virus in house flies (Musca domestica Linneaus) (1983) Am. J. Vet. Res., 44, pp. 2078-2082; Haelterman, E.O., Epidemiological studies of transmissible gastroenteritis of swine (1962) Proceeding,. U.S. Livest. Sanit. Assoc., 1962, pp. 305-315; Harris, D.L., Bevier, G.W., Wiseman, B.S., Eradication of transmissible gastroenteritis virus without depopulation (1987) Proc. 18th Am. Assoc. Swine Pract., 18, pp. 557-561; Kemeny, L.J., Isolation of transmissible gastroenteritis virus from pharyngeal swabs obtained from sows at slaughter (1978) Am. J. Vet. Res., 39, pp. 703-705; Kemeny, L.J., Wiltsey, V.L., Riley, J.L., Upper respiratory infection of lactating sows with transmissible gastroenteritis virus following contact exposure to infected piglets (1975) Cornell Vet., 65, pp. 352-362; Laude, H., Charley, B., Bonnardiere, C., Interactions of porcine enteric coronavirus TGEV with macrophages and lymphocytes (1984) Adv. Exp. Med. Biol., 173, pp. 385-386; Lee, K., Moro, M., Baker, J., Transmissible gastroenteritis in pigs (1954) Am. J. Vet. Res., 15, pp. 364-372; Maes, R.K., Haelterman, E.O., A sero-epizootiological study of five viruses in a swine-evaluation station (1979) Am. J. Vet. Res., 40, pp. 1642-1645; Morin, M., Solorzano, R.F., Morehouse, L.G., Olson, L.D., The postulated role of feeder swine in the perpetuation of the transmissible gastroenteritis virus (1978) Can. J. Comp. Med., 42, pp. 379-384; Mousing, J., Vagsholm, I., Carpenter, T.E., Mousing, J., Gardner, I.A., Hird, D.W., Financial impact of transmissible gastroenteritis in pigs (1988) J. Am. Vet. Med. Assoc., 192, pp. 756-759; Pensaert, M.B., Cox, E., Porcine respiratory coronavirus related to transmissible gastroenteritis virus (1989) Agri-Pract., 10, pp. 17-21; Pensaert, M.B., Haelterman, E.O., Burnstein, T., Transmissible gastroenteritis of swine; virus-intestinal cell interactions. I. Immunofluorescence, histopathology and virus production in the small intestine through the course of infection (1970) Arch. Gesamte Virusforsch, 31, pp. 321-334; Pilchard, E.I., Experimental transmission of transmissible gastroenteritis by starlings (1965) Am. J. Vet. Res., 26, pp. 1177-1179; Pritchard, G.C., Transmissible gastroenteritis in endemically infected breeding herds of pigs in East Anglia, 1981-1985 (1985) Vet. Rec., 120, pp. 226-230; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Edition, pp. 362-386. , A.D., Leman, B.E. Straw, W.L. Mengeling, S. D'Allaire, and D.J. Taylor, eds., Iowa State University Press, Ames, Iowa; Underdahl, N.R., Mebus, C.A., Torres-Medina, A., Recovery of transmissible gastroenteritis virus from chronically infected experimental pigs (1975) Am. J. Vet. Res., 36, pp. 1473-1476; Wiseman, B.S., Harris, D.L., Curran, B.J., Elimination of transmissible gastroenteritis virus from a herd affected with the enzootic form of the disease (1988) Proc 19th Am Assoc Swine Pract, 19, pp. 145-149; Woods, R.D., Small plaque variant transmissible gastroenteritis virus (1978) J. Am. Vet. Med. Assoc., 173, pp. 643-647; Woods, R.D., Wesley, R.D., Kapke, P.A., Neutralization of porcine transmissible gastroenteritis virus by complement-dependent monoclonal antibodies (1988) Am. J. Vet. Res., 49, pp. 300-304","Woods, R.D.; Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States",,,00652598,,AEMBA,"9782340","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031720836
"Izeta A., Sanchez C.M., Smerdou C., Mendez A., Alonso S., Balasch M., Plana-Durán J., Enjuanes L.","6602523425;57193985365;6602856664;36823007700;57210695335;6602693824;6604038063;7006565392;","The spike protein of transmissible gastroenteritis coronavirus controls the tropism of pseudorecombinant virions engineered using synthetic minigenomes",1998,"Advances in Experimental Medicine and Biology","440",,,"207","214",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031720730&partnerID=40&md5=5424b2dba211b5cceff138353743fb32","Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Fort Dodge Veterinaria, Vall de Bianya 17813 Girona, Spain","Izeta, A., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Sanchez, C.M., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Smerdou, C., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Mendez, A., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Alonso, S., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain; Balasch, M., Fort Dodge Veterinaria, Vall de Bianya 17813 Girona, Spain; Plana-Durán, J., Fort Dodge Veterinaria, Vall de Bianya 17813 Girona, Spain; Enjuanes, L., Department of Molecular and Cell Biology, Centra Nacional de Biotecnologia, Campus Universidad Autonoma, Canto Blanco 28049 Madrid, Spain","The minimum sequence required for the replication and packaging of transmissible gastroenteritis virus (TGEV)-derived minigenomes has been determined. To this end, cDNAs encoding defective RNAs have been cloned and used to express heterologous spike proteins, to determine the influence of the peplomer protein in the control of TGEV tropism. A TGEV defective interfering RNA of 9.7 kb (DI-C) was isolated, and a cDNA complementary to DI-C RNA was cloned under the control of T7 promoter. In vitro transcribed DI-C RNA was replicated in trans upon transfection of helper virus-infected cells. A collection of DI-C deletion mutants (TGEV minigenomes) was generated and tested for their ability to be replicated and packaged. The size of the smallest minigenome replicated in trans was 3.3 kb. The rescue system was used to express the spike protein of an enteric TGEV isolate (C11) using as helper virus a TGEV strain (C8) that replicates very little in the gut. A mixture of two pseudorecombinant viruses containing either the helper virus genome or the minigenome was obtained. These pseudorecombinants display in the surface the S proteins from the enteric and the attenuated virus, and showed 104-fold increase in their gut replication levels as compared to the helper isolate (C8). In addition, the pseudorecombinant virus increased its enteric pathogenicity as compared to the C8 isolate.",,"virus rna; article; deletion mutant; gastroenteritis; genetic engineering; nonhuman; priority journal; promoter region; protein determination; rna transcription; virus genome; virus infectivity; virus replication; virus transmission; Animals; Base Sequence; Cell Line; Defective Viruses; Gene Expression; Genome, Viral; Molecular Sequence Data; RNA, Viral; Swine; Transmissible gastroenteritis virus; Viral Proteins; Virion; Virus Assembly; Virus Replication; Coronavirus; RNA viruses; Transmissible gastroenteritis virus","Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilo-bases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , (S. G. Siddell, Ed.), Plenum Press, New York; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Vir. Res., 48, pp. 1-100; Liao, C.-L., Lai, M.M.C., Requirement of 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J. Virol., 68 (8), pp. 4727-4737; Liao, C.-L., Zhang, X., Lai, M.M.C., Coronavirus defective-interfering RNA as an expression vector: The generation of a pseudorecombinant mouse hepatitis virus expressing hemagglutinin-esterase (1995) Virology, 208, pp. 319-327; Lin, Y.J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lunney, J.K., Pescovitz, M.D., Sachs, D.H., The swine major histocompatibility complex: Its structure and function (1986) Swine in Biomedical Research, pp. 1821-1836. , (M. E. Tumbleson, Ed.), Plenum Press, New York; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci., 30, pp. 190-198; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Pattnaik, A.K., Ball, L.A., LeGrone, A.W., Wertz, G.W., Infectious defective interfering particles of VSV from transcripts of a cDNA clone (1992) Cell, 69, pp. 1011-1020; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Sachs, D., Leight, G., Cone, J., Schwarz, S., Stuart, L., Rosemberg, S., Transplantation in miniature swine. I. Fixation of the major histocompatibility complex (1976) Transplantation, 22, pp. 559-567; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, New York; Sanchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sanchez, C.M., Gebauer, F., Suñé, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sanchez, C.M., Ballesteros, M.L., Enjuanes, L., (1997) Tropism, Virulence and Primary Genome Structure in a Cluster of Transmissible Gastroenteritis Coronavirus Derived from the Purdue Isolate, , Submitted for publication; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M.C., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338","Izeta, A.; Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, CSIC Campus Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"9782282","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031720730
"Dalton K., Penzes Z., Wroe C., Stirrups K., Evans S., Shaw K., Brown T.D.K., Britton P., Cavanagh D.","7006042187;55761804900;7004689887;57210222541;7402709581;7202206256;56248391000;57203302770;26642890500;","Sequence elements involved in the rescue of IBV defective RNA CD-91",1998,"Advances in Experimental Medicine and Biology","440",,,"253","257",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031722291&partnerID=40&md5=78f8be04661e7fd67bce2dbd751ecaea","IAH, Compton RG20 7NN, United Kingdom; Division of Virology, Department of Pathology, University of Cambridge, United Kingdom","Dalton, K., IAH, Compton RG20 7NN, United Kingdom; Penzes, Z., IAH, Compton RG20 7NN, United Kingdom; Wroe, C., Division of Virology, Department of Pathology, University of Cambridge, United Kingdom; Stirrups, K., IAH, Compton RG20 7NN, United Kingdom; Evans, S., IAH, Compton RG20 7NN, United Kingdom; Shaw, K., IAH, Compton RG20 7NN, United Kingdom; Brown, T.D.K., Division of Virology, Department of Pathology, University of Cambridge, United Kingdom; Britton, P., IAH, Compton RG20 7NN, United Kingdom; Cavanagh, D., IAH, Compton RG20 7NN, United Kingdom","Deletion mutagenesis has been used to identify essential regions for rescue of coronavirus defective RNAs (D-RNAs). Using this technique on a cloned IBV D-RNA CD-91, we have identified a region potentially important in its rescue. Comparing the sequence of D-RNAs rescued with those not rescued we have deduced that a 72 base region corresponding to base number 13824 to 13896 in the viral genome is required for rescue. This may be an IBV D-RNA packaging signal or a cis-acting element involved in replication. Further experiments and modification of our techniques will be required to differentiate between the two processes.",,"virus rna; article; conformational transition; coronavirus; gene deletion; molecular cloning; nonhuman; priority journal; rna replication; rna sequence; signal transduction; site directed mutagenesis; virus genome; Animals; Base Sequence; Defective Viruses; Infectious bronchitis virus; RNA, Viral; Avian infectious bronchitis virus; Coronavirus","Chang, R.Y., Brian, D.A., cis Requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; De Groot, R.J., Van Der Most, R.G., S, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J. Virol., 66, pp. 5895-5905; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Kim, Y., Lai, M.M.C., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Kim, Y.N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.N., Makino, S., Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal (1995) J. Virol., 69, pp. 4963-4971; Lin, Y.J., Lai, M.M., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.J., Liao, C.L., Lai, M.M., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Woo, K., M., J., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-1527","Dalton, K.; IAH, Compton RG20 7NN, United Kingdom",,,00652598,,AEMBA,"9782289","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031722291
"Rowe C.L., Baker S.C., Nathan M.J., Sgro J.-Y., Palmenberg A.C., Fleming J.O.","7103076229;7403307881;7102650902;7004544310;7003937294;7401457370;","Quasispecies development by high frequency RNA recombination during MHV persistence",1998,"Advances in Experimental Medicine and Biology","440",,,"759","765",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721559&partnerID=40&md5=a6e453089e7663c7fce9e86d177365dc","Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Departments of Neurology and Medical Microbiology, University of Wisconsin, William S. Middleton Veterans Hospital, Madison, WI, United States; Institute for Molecular Virology, University of Wisconsin, Madison, WI, United States; Department of Animal Health and Biomedical Science, University of Wisconsin, Madison, WI, United States","Rowe, C.L., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Baker, S.C., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL 60153, United States; Nathan, M.J., Departments of Neurology and Medical Microbiology, University of Wisconsin, William S. Middleton Veterans Hospital, Madison, WI, United States; Sgro, J.-Y., Institute for Molecular Virology, University of Wisconsin, Madison, WI, United States; Palmenberg, A.C., Institute for Molecular Virology, University of Wisconsin, Madison, WI, United States, Department of Animal Health and Biomedical Science, University of Wisconsin, Madison, WI, United States; Fleming, J.O., Departments of Neurology and Medical Microbiology, University of Wisconsin, William S. Middleton Veterans Hospital, Madison, WI, United States","Recent studies suggest that infectious viruses and particularly persisting viral RNAs often exist as diverse populations or 'quasispecies'. We have developed an approach to characterize populations of the murine coronavirus mouse hepatitis virus (MHV) generated during persistent infection which has allowed us to begin to address the role of the viral quasispecies in MHV pathogenesis. We analyzed the population of persisting vital RNAs using reverse-transcription polymerase chain reaction amplification (RT-PCR) of the S1 'hypervariable' region of the spike gene followed by differential colony hybridization to identify spike deletion variants (SDVs) from acute and persistently infected mice. Sequence analysis revealed that mice with the most severe chronic paralysis harbored the most complex quasispecies. Mapping of the SDVs to the predicted RNA secondary structure of the spike RNA revealed that an isolated stem loop structure is frequently deleted. Overall, these results are consistent with high frequency recombination at sites of RNA secondary structure contributing to expansion of the viral quasispecies and persisting vital pathogenesis.",,"virus rna; animal model; article; mouse; murine hepatitis coronavirus; nonhuman; persistent virus infection; priority journal; reverse transcription polymerase chain reaction; rna structure; rna virus infection; species; virus morphology; virus pathogenesis; virus recombination; Animals; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Recombination, Genetic; RNA, Viral; Viral Envelope Proteins; Virus Latency; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Baczko, K., Lampe, J., Liebert, U.G., Brinckmann, U., Ter Meulen, V., Pardowitz, I., Budka, H., Rima, B.K., Clonal expansion of hypermutated measles virus in a SSPE brain (1993) Virology, 197, pp. 188-195; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response (1996) J. Gen. Virol., 77, pp. 315-325; Cascone, P.J., Haydar, T.F., Simon, A.E., Sequences and structures required for recombination between virus-associated RNAs (1993) Science, 260, pp. 801-805; Castro, R.F., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicitiy (1995) J. Virol., 69, pp. 8127-8131; Lai, M.M., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 556, pp. 61-79; Martell, M., Esteban, J.I., Quer, J., Genesca, J., Weiner, A., Esteban, R., Guardia, J., Gomez, J., Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution (1992) J. Virol., 66, pp. 2547-2556; Novella, I.S., Domingo, E., Holland, J.J., Rapid viral quasispecies evolution - Implications for vaccine and drug strategies (1995) Molecular Medicine Today, 1, pp. 248-253; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of Mouse Hepatitis Virus: Detection and Characterization of Spike Deletion Variants during Persistent Infection (1997) J. Virol., 71, pp. 2959-2969; Rowe, C.L., Fleming, J.O., Sgro, J.-Y., Palmenberg, A.C., Baker, S.C., Generation of coronavirus spike deletion variants (SDVs) by high frequency recombination at regions of predicted RNA secondary structure (1997) J. Virol., , in press; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072. , published erratum appears in J Gen Virol 1992 Oct; 73(Pt10):2767; Wang, F.I., Fleming, J.O., Lai, M.M., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; White, K.A., Morris, T.J., RNA determinants of junction site selection in RNA virus recombinants and defective interfering RNAs (1995) RNA, 1, pp. 1029-1040","Rowe, C.L.; Dept. of Microbiology and Immunology, Molecular Biology Program, Loyola University of Chicago, Maywood, IL 60153, United States",,,00652598,,AEMBA,"9782355","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721559
"Schickli J.H., Wentworth D.E., Zelus B.D., Holmes K.V., Sawicki S.G.","6603027057;57203154014;6602571243;7201657724;7004118344;","Selection in persistently infected murine cells of an MHV-A59 variant with extended host range",1998,"Advances in Experimental Medicine and Biology","440",,,"735","741",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783551&partnerID=40&md5=2bae376a05f7a22cbe7f86c108a37bfc","Department of Microbiology, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Department of Microbiology, Medical College of Ohio, Toledo, OH 43699, United States","Schickli, J.H., Department of Microbiology, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Wentworth, D.E., Department of Microbiology, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Zelus, B.D., Department of Microbiology, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Holmes, K.V., Department of Microbiology, University of Colorado Health Sciences Center, Denver, CO 80262, United States; Sawicki, S.G., Department of Microbiology, Medical College of Ohio, Toledo, OH 43699, United States","Murine coronavirus MHV-A59 normally infects only murine cells in vitro and causes transmissible infection only in mice. In the 17 Cl 1 line of murine cells, the receptor for MHV-A59 is MHVR, a biliary glycoprotein in the carcinoembryonic antigen (CEA) family of glycoproteins. We found that virus released from the 600th passage of 17 Cl 1 cells persistently infected with MHV-A59 (MHV/pi600) replicated in hamster (BHK-21) cells. The virus was passaged and plaque-purified in BHK-21 cells, yielding the MHV/BHK strain. Because murine cells persistently infected with MHV-A59 express a markedly reduced level of MHVR (Sawicki, et al., 1995), we tested whether virus with altered receptor interactions was selected in the persistently infected culture. Infection of 17 Cl 1 cells by MHV-A59 can be blocked by treating the cells with anti-MHVR MAb-CC1, while infection by MHV/BHK was only partially blocked by MAb-CC1. MHV/BHK virus was also more resistant than wild-type MHV- A59 to neutralization by purified, recombinant, soluble MHVR glycoprotein (sMHVR). Cells in the persistently infected culture may also express reduced levels of and have altered interactions with some of the Bgp-related glycoproteins that can serve as alternative receptors for MHV-A59. Unlike the parental MHV-A59 which only infects murine cells, MHV/BHK virus was able to infect cell lines derived from mice, hamsters, rats, cats, cows, monkeys and humans. However, MHV/BHK was not able to infect all mammalian species, because a pig (ST) cell line and a dog cell line (MDCK I) were not susceptible to infection. MHV/pi600 and MHV/BHK replicated in murine cells more slowly than MHV-A59 and formed smaller plaques. Thus, in the persistently infected murine cells which expressed a markedly reduced level of MHVR, virus variants were selected that have altered interactions with MHVR and an extended host range. In vivo, in mice infected with coronavirus, virus variants with altered receptor recognition and extended host range might be selected in tissues that have low levels of receptors. Depending upon the tissue in which such a virus variant was selected, it might be shed from the infected animal or eaten by a predator, thus presenting a possible means for initiating the transition of a variant virus into a new host as a model for an emerging virus disease.",,"animal cell; animal model; article; cat; cow; dog; hamster; host; human; human cell; mouse; murine hepatitis coronavirus; nonhuman; priority journal; rat; rna virus infection; swine; virus expression; virus neutralization; virus plaque; virus replication; Animals; Cats; Cell Line; Cricetinae; Dogs; Mice; Murine hepatitis virus; Rats; Selection (Genetics); Variation (Genetics); Virus Latency; Animalia; Canis familiaris; Coronavirus; Cricetinae; Felis catus; Mammalia; Murinae; Murine hepatitis virus; RNA viruses; Sus scrofa","Cabirac, G.F., Soike, K.F., Zhang, J.Y., Hoel, K., Butunoi, C., Cai, G.Y., Johnson, S., Murray, R.S., Entry of coronavirus into primate CNS following peripheral infection (1994) Microb. Pathog., 16, pp. 349-357; Chen, D.S., Asanaka, M., Chen, F.S., Shively, J.E., Lai, M.M.C., Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors (1997) J. Virol., 71, pp. 1688-1691; Chen, D.S., Asanaka, M., Yokomori, K., Wang, F.I., Hwang, S.B., Li, H.P., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 12095-12099; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Coutelier, J.-P., Godfraind, C., Dveksler, G.S., Wysocka, M., Cardellichio, C.B., Noel, H., Holmes, K.V., B lymphocyte and macrophage expression of carcinoembryonic antigen-related adhesion molecules that serve as receptors for murine coronavirus (1994) Eur. J. Immunol., 24, pp. 1383-1390; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Gagneten, S., Gout, O., Dubois-Dalcq, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutation in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus (1995) Lab. Invest., 73, pp. 615-627; Murray, R.S., Cai, G.Y., Hoel, K., Zhang, J.Y., Soike, K.F., Cabirac, G.F., Coronavirus infects and causes demyelination in primate central nervous system (1992) Virology, 188, pp. 274-284; Nash, T.C., Buchmeier, M.J., Entry of mouse hepatitis virus into cells by endosomal and nonendosomal pathways (1997) Virology, , in press; Nedellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; Sawicki, S.G., Lu, J.H., Holmes, K.V., Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from the epigenetic expression of the MHV receptor (1995) J. Virol., 69, pp. 5535-5543; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Schickli, J.H., Zelus, B.D., Wentworth, D.E., Sawicki, S.G., Holmes, K.V., (1997) Murine Coronavirus MHV-A59 from Persistently Infected Murine Cells Exhibits An Extended Host Range, , submitted; Sugiyama, K., Ishikawa, R., Fukuhara, N., Structural polypeptides of the murine coronavirus DVIM (1986) Arch. Virol., 89, pp. 245-254; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J. Virol., 62, pp. 4686-4690; Wagaman, P.C., Spence, H.A., O'Callaghan, R.J., Detection of influenza C virus by using an in situ esterase assay (1989) J. Clin. Microbiol., 27, pp. 832-836; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Yokomori, K., Banner, L.R., Lai, M.M., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657","Schickli, J.H.; Department of Microbiology, Univ. of Colorado Health Sci. Ctr., Denver, CO 80262, United States",,,00652598,,AEMBA,"9782352","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783551
"Lavi E., Haluskey J.A., Masters P.S.","7006986911;6507007625;7006234572;","The pathogenesis of mhv nucleocapsid gene chimeric viruses",1998,"Advances in Experimental Medicine and Biology","440",,,"537","541",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031784047&partnerID=40&md5=6819b3d1f5621d8e494b5ba031d58bd1","Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States","Lavi, E., Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Haluskey, J.A., Division of Neuropathology, Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Masters, P.S., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States","A set of viruses in which various segments of the nucleocapsid (N) gene of MHV have been substituted with the corresponding segments of bovine coronavirus (BCV) by targeted recombination were analyzed for their biologic properties. Histology for organ pathology and plaque assay for viral titer analysis following intracerebral (IC) inoculation were studied. One chimeric virus (Alb85), in which only a small segment of the N gene was replaced, exhibited a phenotype similar to wild type MHV-A59. However, three of the chimeric viruses (Alb106, Alb112 and Alb100) produced acute encephalitis and demyelination but without hepatitis following IC inoculation. Intravenous (IV) and intrahepatic (IH) inoculations were able to restore the ability of these viruses to produce hepatitis. The common denominator of the three chimeric viruses with a different phenotype is a region between aa 306 and aa 386 in which 17 amino acids (aa) differences exist between the two strains. Thus this region may contain determinants which enable the virus to exit the brain and reach the blood stream.",,"virus nucleoprotein; animal experiment; animal model; animal tissue; article; chimera; controlled study; demyelination; encephalitis; genetic recombination; male; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virus hepatitis; virus nucleocapsid; virus pathogenesis; virus replication; Animals; Coronavirus Infections; Demyelinating Diseases; Injections, Intravenous; L Cells (Cell Line); Male; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; Reassortant Viruses; Virulence; Virus Replication; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Murinae; Murine hepatitis virus","Bergmann, C.C., Stohlman, S.A., Specificity of the H-2 L(d)-restricted cytotoxic T-lymphocyte response to the mouse hepatitis virus nucleocapsid protein (1996) J. Virol., 70, pp. 3252-3257; Gombold, J.L., Sutherland, R.M., Lavi, E., Paterson, Y., Weiss, S.R., Mouse hepatitis virus A59-induced demyelination can occur in the absence of CD8+ T cells (1995) Microb. Pathogen., 18, pp. 211-221; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Lavi, E., Fishman, S.P., Highkin, M.K., Weiss, S.R., Limbic encephalitis following inhalation of murine coronavirus MHV-A59 (1988) Lab. Invest., 58, pp. 31-36; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., Detection of MHV-A59 RNA by in situ hybridization (1984) Molecular Biology and Pathogenesis of Coronaviruses, 173, pp. 247-258. , P. M. Rottier, B. M. A. van der Zeijst, W. J. M. Spaan, and M. C. Horzinek, Eds., Plenum Press, New York; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., The organ tropism of mouse hepatitis virus A59 is dependent on dose and route of inoculation (1986) Lab. Anim. Sci., 36, pp. 130-135; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab. Invest., 62, pp. 570-578; Lavi, E., Weiss, S.R., Coronaviruses (1989) Clinical and Molecular Aspects of Neurotropic Viral Infections, pp. 101-139. , D. H. Gilden, and H. L. Lipton, Eds., Kluwer, Academic Publishers, Boston; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484","Lavi, E.; Division of Neuropathology, Dept. of Pathology and Lab. Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States",,,00652598,,AEMBA,"9782326","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031784047
"Buddaert W., Van Reeth K., Pensaert M.","8980049000;57191565576;55905425400;","In vivo and in vitro interferon (IFN) studies with the porcine reproductive and respiratory syndrome virus (PRRSV)",1998,"Advances in Experimental Medicine and Biology","440",,,"461","467",,125,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031751351&partnerID=40&md5=ed6f91900fa36280003cc0fba02a1fdf","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium","Buddaert, W., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Van Reeth, K., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium","Some of the interactions between the porcine reproductive and respiratory syndrome virus (PRRSV) and the porcine interferon-α (IFN-α) system were studied. In a first experiment, it was shown that pretreatment of primary porcine alveolar macrophages (AMs) with recombinant porcine (rPo) IFN-α 1 resulted in significant reductions of PRRSV yield and numbers of antigen expressing cells. In a second experiment, sensitivity of PRRSV to IFN-α was confirmed in vivo. In pigs inoculated with porcine respiratory coronavirus (PRCV) - a potent inducer of endogenous IFN-α in the lungs of pigs - followed 2 days later by PRRSV - lung PRRSV titers were 1.7 to 2.9 log10 TCID50 reduced compared to those in singly PRRSV inoculated pigs. It was concluded therefore that PRRSV has a fairly good sensitivity to the antiviral effects of IFN-α. A third experiment documented that in vivo PRRSV infection generally does not affect PRCV-induced IFN-α production in the lungs of pigs. In addition, it was shown that the IFN-inducing capacity of PRRSV is at least 159 times lower than that of PRCV. This finding suggests that cells other than AMs may be responsible for IFN production in the lungs of pigs.",,"alpha interferon; animal experiment; animal model; animal tissue; antigen expression; antiviral activity; article; controlled study; coronavirus; interferon production; lung alveolus macrophage; nonhuman; priority journal; swine; virus infection; virus replication; Animals; Cells, Cultured; Interferon Type I, Recombinant; Interferon-alpha; Lung; Macrophages, Alveolar; Porcine Reproductive and Respiratory Syndrome; Porcine respiratory and reproductive syndrome virus; Swine; Animalia; Coronavirus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Suidae; Sus scrofa","Albina, E., Carrat, C., Charley, B., Interferon alpha response to porcine reproductive and respiratory syndrome virus (PRRSV) (1997) J. Gen. Virol., , submitted; Artursson, K., Wallgren, P., Aim, G., Appearance of interferon-α in serum and signs of reduced immune function in pigs after transport and installation in a fattening farm (1989) Vet. Immunol. Immunopathol., 23, pp. 345-353; Babiuk, L.A., Bielefeldt Ohmann, H., Gifford, G., Czarniecki, C.W., Scialli, V.T., Hamilton, E.B., (1985) J. Gen. Virol., 66, pp. 2383-2394; Charley, B., Lavenant, L., Characterization of blood mononuclear cells producing IFN-α following induction by coronavirus-infected cells (transmissible porcine gastroenteritis virus) (1990) Res. Immunol., 141, p. 141; Duan, X., Nauwynck, H.J., Pensaert, M.B., Virus quantification and identification of cellular targets in the lungs and lymphoid tissues of pigs at different time intervals after inoculation with porcine reproductive and respiratory syndrome virus (PRRSV) (1997) Vet. Microbiol., 56, pp. 9-19; Esparza, I., Gonzalez, J.C., Vinuela, E., Effect of interferon-α, interferon-̃ and tumour necrosis factor-α on African swine fever virus replication in porcine monocytes and macrophages (1988) J. Gen. Virol., 69, pp. 2973-2980; Holland, S.P., Fulton, R.W., Short, E.C., Wyckoff, J.H., Fox, J.C., In vitro and in vivo 2′, 5′-oligoadenylate synthetase activity induced by recombinant DNA-derived bovine interferon αl1 in bovine alveolar macrophages and blood mononuclear cells (1991) Am. J. Vet. Res., 52, pp. 1779-1783; Iglesias, G., Pijoan, C., Molitor, T., Effects of pseudorabies virus infection upon cytotoxicity and antiviral activities of porcine alveolar macrophages (1992) Comp. Immunol. Microbiol. Infect. Dis., 15, pp. 249-259; Lefèvre, F., L'Haridon, R., Borras-Cuesta, F., La Bonnardière, C., Production, purification and biological properties of an Escherichia coli-derived recombinant porcine alpha interferon (1990) J. Gen. Virol., 71, pp. 1057-1063; Powell, P.P., Dixon, L.K., Parkhouse, R.M., An IkappaB homolog encoded by African swine fever virus provides a novel mechnanism for downregulation of proinflammatory cytokine responses in host macrophages (1996) J. Virol., 70, pp. 8527-8533; Saksela, E., Virtanen, I., Hovi, T., Secher, D.S., Cantell, K., Monocyte is the main producer of human alpha interferons following Sendai virus induction (1984) Prog. Med. Virol., 30, p. 78; Van Reeth, K., Pensaert, M.B., Porcine respiratory coronavirus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) Am. J. Vet. Res., 55, pp. 1275-1281; Van Reeth, K., Pensaert, M., Production of interferon-α, tumor necrosis factor-α and interleukin-1 in the lungs of pigs infected with the porcine respiratory coronavirus (1995) Proc. 3rd Congress Europ. Soc. Vet. Virol., pp. 197-201. , Interlaken, Switzerland; Van Reeth, K., Pensaert, M., A clinical and virological study in pigs infected with Aujeszky's disease virus shortly after infection with porcine respiratory coronavirus (1996) Proc. 14th Congress Int. Pig Vet. Soc., p. 137. , Bologna, Italy; Wensvoort, G., Terpstra, C., Pol, J.M.A., Ter Laak, E.A., Bloemraad, M., De Kluyver, E.P., Kragten, C., Braanskamp, J., Mystery swine disease in the Netherlands: The isolation of the Lelystad virus (1991) Vet. Q., 13, pp. 121-130","Buddaert, W.; Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburylaan 133, B-9820 Merelbeke, Belgium",,,00652598,,AEMBA,"9782316","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031751351
"Evans S.A., Stirrups K., Dalton K., Shaw K., Cavanagh D., Britton P.","7402709581;57210222541;7006042187;7202206256;26642890500;57203302770;","Utilising a defective IBV RNA for heterologous gene expression with potential prophylactic application",1998,"Advances in Experimental Medicine and Biology","440",,,"687","692",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783038&partnerID=40&md5=13dc54130c93727203ed7b1a914e2410","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom","Evans, S.A., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom; Stirrups, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom; Dalton, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, RG20 7NN, United Kingdom","Based on the natural ability of coronaviruses to undergo homologous RNA recombination, we are working to produce infectious bronchitis virus (IBV) recombinants using RNA generated from recombinant fowlpox viruses (FPV). The aim is to replace the spike (S) gene of an existing IBV vaccine strain with the S gene of a heterologous strain. CD-61 is an IBV defective RNA (D-RNA) derived from a naturally occurring IBV D-RNA (CD-91). CD-61 D-RNA is being investigated as an RNA vector for the expression of heterologous genes. T7- derived RNA transcripts of CD-61 can be replicated and passaged in the presence of helper virus, following electroporation into IBV-infected cells. CD-61 cDNA was modified by the addition of the hepatitis delta virus ribozyme plus T7 terminator downstream of the 3' UTR. This allowed the synthesis of discreet RNA transcripts. The complete cassette was cloned into an FPV transfer vector (pEFL10) for generating recombinant fowlpox viruses. FPV/CD- 61 recombinants will be assessed for D-RNA production in IBV-infected cells. The luciferase reporter gene sequence has been inserted into the modified CD- 61, under the control of the IBV transcription associated sequence (TAS) from gene 5. Luciferase has been successfully expressed from CD-61 in helper virus-infected cells.",,"virus rna; article; avian infectious bronchitis virus; gene expression; gene insertion; gene sequence; molecular cloning; nonhuman; priority journal; rna replication; rna transcription; virus expression; virus replication; Animals; Cells, Cultured; Chickens; Defective Viruses; Fowlpox virus; Gene Expression; Genetic Vectors; Infectious bronchitis virus; RNA, Viral; Aves; Avian infectious bronchitis virus; delta virus; Fowlpox virus; Hepatitis delta virus","Britton, P., Green, P., Kottier, S., Mawditt, K.L., Pénzes, Z., Cavanagh, D., Skinner, M.A., Expression of bacteriophage T7 RNA polymerase in avian and mammalian cells by a recombinant fowlpox virus (1996) J. Gen. Virol., 77, pp. 963-967; Cavanagh, D., Coronavirus IBV: Structural characterisation of the spike protein (1983) J. Gen. Virol., 64, pp. 2577-2583; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Pénzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterisation of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Pénzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70 (12), pp. 8660-8668","Evans, S.A.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom",,,00652598,,AEMBA,"9782345","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783038
"Schmitz A., Tobler K., Suter M., Ackermann M.","57212747606;6701508835;7101609550;7102624625;","Prokaryotic expression of porcine epidemic diarrhoea virus ORF3",1998,"Advances in Experimental Medicine and Biology","440",,,"775","780",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031784048&partnerID=40&md5=ef5a33b7a748b567fc6941828521f620","Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland","Schmitz, A., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Tobler, K., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Suter, M., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland; Ackermann, M., Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057, Switzerland","Wild type (wt) and cell culture adapted (ca) strains of the coronavirus PEDV differ in their ability to cause diarrhea in neonate piglets: the wt strains are virulent; the ca strains are attenuated. Comparison of the available nucleotide sequences obtained from the different viral isolates revealed almost complete sequence identity with the exception of variations and truncations in open reading frame 3 (ORF3) observed exclusively in ca- PEDV isolates. In order to study the biological function(s) of the putative ORF3 product, the molecule was expressed as a heterodimeric fusion protein in E. coli. ORF3 was fused in frame to the alkaline phosphatase gene. Simultaneously, the construct was designed to form specific heterodimers by inclusion of the well known leucine zipper motiv of Jun and Fos. The heterodimerization partner contained the E. coli heat-labile enterotoxin subunit B (LTB) to allow specific binding to the eukaryotic cell receptor GM1. Our results indicate that heterodimeric fusion protein containing a truncated form of ORF3 was produced in high amounts, carried the expected ORF3 epitope, showed phosphatase activity, and was able to bind to the GM1 receptor. In contrast, a fusion protein containing the entire sequence of the ORF3 product was produced in minute amounts, indicating that it may have biological activity in prokaryotes, which led to the reduction of the amounts of proteins expressed.",,"article; coronavirus; enzyme activity; escherichia coli; nonhuman; nucleotide sequence; open reading frame; priority journal; protein expression; virus expression; Animals; Bacterial Toxins; Binding Sites; Coronavirus; Enterotoxins; Escherichia coli; Escherichia coli Proteins; Gene Expression; Genetic Vectors; Open Reading Frames; Prokaryotic Cells; Recombinant Fusion Proteins; Swine; Viral Proteins; Coronavirus; Escherichia coli; Eukaryota; Porcine epidemic diarrhea virus; Prokaryota; Suidae","Aitken, R., Brock, J., Sinclair, M.C., Receptor-binding subunits from cholera toxin and heat-labile enterotoxin as immunological carriers (1994) Zbl. Bakt. Suppl., 24, pp. 467-473. , Bacterial protein toxins, (Freer et al., eds), Gustav Fischer, Stuttgart; Crameri, R., Suter, M., Display of biologically active proteins on the surface of filamentous phages: A cDNA cloning system for selection of functional gene products linked to the genetic information responsible for their production (1993) Gene, 137, pp. 69-75; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF (1994) Virology, 198, pp. 466-476; Holmgren, J., Lonnroth, I., Svenerholm, L., Tissue receptor for cholera exotoxin: Postulated struture from studies with GM1 ganglioside and related glycolipids (1973) Infect. Immun., 8, pp. 208-214; Tobler, K., Ackermann, M., PEDV leader and junction sites (1995) Adv. Exp. Med. Biol., 380, pp. 541-542. , Corona- and Related Viruses (P.J. Talbot and G.A. Levy, eds.); Utiger, A., Tobler, K., Bridgen, A., Suter, M., Singh, M., Ackermann, M., Identification of proteins specified by porcine epidemic diarrhoea virus (1995) Adv. Exp. Med. Biol., 380, pp. 287-290. , Corona- and Related Viruses (P.J. Talbot and G.A. Levy, eds.)","Schmitz, A.; Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH 8057 Zurich, Switzerland",,,00652598,,AEMBA,"9782357","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031784048
"Fischer F., Stegen C.F., Koetzner C.A., Masters P.S.","7202883540;6602557632;6602982748;7006234572;","Construction of a mouse hepatitis virus recombinant expressing a foreign gene",1998,"Advances in Experimental Medicine and Biology","440",,,"291","295",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721071&partnerID=40&md5=dda3e39847d28aadaad140a384155b6f","David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States","Fischer, F., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States; Stegen, C.F., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States; Koetzner, C.A., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States; Masters, P.S., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States","The genome of the coronavirus mouse hepatitis virus (MHV) contains genes which have been shown to be nonessential for viral replication and which could, in principle, be used as sites for the introduction of foreign sequences. We have inserted heterologous genetic material into gene 4 of MHV in order (i) to test the applicability of targeted RNA recombination for site-directed mutagenesis of the MHV genome upstream of the N gene; (ii) to develop further genetic tools for mutagenesis of structural genes other than N; and (iii) to examine the feasibility of using MHV as an expression vector. A DI-like donor RNA vector containing the MHV S gene and all genes distal to S was constructed. Initially, a derivative of this was used to insert a 19- nucleotide tag into the start of ORF 4a of MHV-A59 using the N gene deletion mutant Alb4 as the recipient virus. Subsequently, the entire gene for the green fluorescent protein (GFP) was inserted in place of gene 4. This heterologous gene was shown to be expressed by recombinant viruses but not at levels sufficient to allow detection of fluorescence of vital plaques. Northern blot analysis of transcripts of GFP recombinants showed the expected displacement of the mobility, relative to those of wild-type, of all subgenomic mRNAs larger than mRNA5. An unexpected result of the Northern analysis was the observation that GFP recombinants also produced an RNA species the same size as that of wild-type mRNA4. RT-PCR analysis of the 5' end of this species revealed that it was actually a collection of mRNAs originating from a cluster of 10 different sites, none of which possessed a canonical intergenic sequence. The finding of these aberrant mRNAs, all of nearly the same size as wild-type mRNA4, suggests that long range structure of the MHV genome can sometimes be the sole determinant of the site of initiation of transcription.",,"virus rna; article; nonhuman; northern blotting; nucleotide sequence; priority journal; site directed mutagenesis; transcription initiation; virus expression; virus recombination; virus replication; Animals; Gene Expression; Genes, Reporter; Genetic Vectors; Green Fluorescent Proteins; L Cells (Cell Line); Luminescent Proteins; Mice; Murine hepatitis virus; Recombinant Proteins; Coronavirus; Murine hepatitis virus; Murine hepatitis virus (strain S)","Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W., Prasher, D.C., Green fluorescent protein as a marker for gene expression (1994) Science, 263, pp. 802-805; Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revenants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns 4 gene of mouse hepatitis virus (MHV), strain A59 contains two ORFs and thus differs from ns 4 of the JHM and S strains (1993) Arch. Virol., 129, pp. 301-309; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Zhang, X., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633","Fischer, F.; David Axelrod Institute, Wadsworth Center for Lab./Research, New York State Department of Health, Albany, NY 12201-2002, United States",,,00652598,,AEMBA,"9782295","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721071
"Hensley L.E., Baric R.S.","55303564700;7004350435;","Human biliary glycoproteins function as receptors for interspecies transfer of mouse hepatitis virus",1998,"Advances in Experimental Medicine and Biology","440",,,"43","52",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753382&partnerID=40&md5=2cb24ed9f955c0cd13d349a19a971676","Department of Epidemiology; Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, United States","Hensley, L.E., Department of Epidemiology; Baric, R.S., Department of Epidemiology, Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, United States","A variant Mouse Hepatitis virus (MHV), designated MHV-H2, was isolated by serial passage in mixed cultures of permissive DBT cells and nonpermissive Syrian Hamster Kidney (BHK) cells. MHV-H2 replicated efficiently in hamster, mouse, primate kidney (Vero, Cos 1, Cos 7), and human adenocarcinoma (HRT) cell lines but failed to replicate in porcine testicular (ST), feline kidney (CRFK), and canine kidney (MDCK) cells. To understand the molecular basis for coronavirus cross-species transfer into human cell lines, the replication of MHV-H2 was studied in hepatocellular carcinoma (HepG2) cells which expressed high levels of the human homologue of the normal murine receptor, biliary glycoprotein (Bgp). MHV-H2 replicated efficiently in human HepG2 cells, at low levels in breast carcinoma (MCF7) cells, and poorly, if at all, in human colon adenocarcinoma (LS 174T) cell lines which expressed high levels of carcinoembryonic antigen (CEA). These data suggested that MHV-H2 may utilize the human Bgp homologue as a receptor for entry into HepG2 cells. To further study MHV-H2 receptor utilization in human cell lines, blockade experiments were performed with a panel of different monoclonal or polyclonal antiserum directed against the human CEA genes. Pretreatment of HepG2 cells with a polyclonal antiserum directed against all CEA family members, or with a monoclonal antibody, Kat4c (cd66abde), directed against Bgp1, CGM6, CGM1a, NCA and CEA, significantly reduced virus replication and the capacity of MHV- H2 to infect HepG2 cells. Using another panel of monoclonals with more restricted cross reactivities among the human CEA's, Col-4 and Col-14, but not B6.2, B1.13, Col-1, Col-6 and Col-12 blocked MHV-H2 infection in HepG2 cells. These antibodies did not block sindbis virus (SB) replication in HepG2 cells, or block SB, MHV-A59 or MHV-H2 replication in DBT cells. Monoclonal antibodies Col-4, Col-14, and Kat4c (cd66abde) all reacted strongly with human Bgp and CEA, but displayed variable binding patterns with other CEA genes. Following expression of human Bgp in normally nonpermissive porcine testicular (ST) and feline kidney (CRFK) cells, the cells became susceptible to MHV-H2 infection. These data suggested that phylogenetic homologues of virus receptors represent natural conduits for virus xenotropism and cross- species transfer.",,"glycoprotein; animal cell; article; coronavirus; drug receptor binding; mouse; nonhuman; phylogeny; priority journal; receptor affinity; virus cell interaction; virus expression; virus isolation; virus replication; virus transmission; Animals; Antibodies; Antigens, CD; Carcinoembryonic Antigen; Cats; Cell Adhesion Molecules; Cell Line; Cercopithecus aethiops; CHO Cells; Cricetinae; Dogs; Glycoproteins; Humans; Mice; Murine hepatitis virus; Receptors, Virus; Species Specificity; Swine; Tumor Cells, Cultured; Vero Cells; Animalia; Coronavirus; Cricetinae; Felidae; Mesocricetus auratus; Murinae; Murine hepatitis virus; Primates; Sindbis virus; Suidae","Baric, R.S., Yount, B., Hensley, L., Peel, S., Chen, W., Episodic Evolution and interspecies Transfer of a Murine Coronavirus (1997) J. Virol., 71, pp. 1946-1955; Barnett, Drake, Pickle, I.I., Human Biliary Glycoporein Gene: Characterization of a family of novel Alternatively Spliced RNAs and their Expressed proteins (1993) Molec. Cell Biol., 13, pp. 1273-1282; Bozzola, R., (1992) Electron Microscopsy, , Jones and Bartlett Publishers, Boston; Chen, C.S., Asanaka, M., Yokomori, K., Wang, F.-I., Hwang, S.B., Li, H.-P., Lai, M.M.C., Pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. USA, 71, pp. 1688-1691; Chen, D.S., Asanaka, M., Chen, F.S., Shively, J.E., Lai, M.M.C., Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors (1997) J. Virol, 71, pp. 1688-1691; Chen, W., Baric, R.S., Molecular anatomy of mouse hepatitis virus persistence: Coevolution of increased host cell resistance and virus virulence (1996) J. Virol., 70, pp. 3947-3960; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Hauck, Nédellec, Turbide, Stanners, Barnett, Transcriptional Control of the human biliary glycoprotein gene, a CEA gene family member down-regulated in colorectal carcinomas (1994) Euro. J. Biochem., 223, pp. 529-541; Haywood, A.M., Virus receptors: Binding, adhesion strengthening, and changes in viral structure (1994) J. Virol., 68, pp. 1-5; Hinoda, Y., Neumaier, M., Hefta, S.A., Drzeniek, Z., Wagner, C., Shively, L., Hefta, L.J., Paxton, R.J., Molecular cloning of a cDNA coding biliary glycoprotein I: Primary structure of a glycoprotein immunologically crossreactive with carcinoembryonic antigen (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 6959-6963; Hirano, N., Murakami, T., Fugiwara, K., Matsumoto, M., Utility of the cell line DBT for propagation and assay of mouse hepatitis virus (1978) Jph. J. Exp. Med., 48, pp. 71-75; Holmes, K.V., (1994) Cellular Receptors for Animal Viruses, pp. 1-14. , E. Wimmer eds., Coldspring Harbor Laboratory Press; Kilbourne, E.D., New viruses and new disease: Mutation, evolution and ecology (1991) Curr. Opin. Immunol., 3, pp. 518-524; Michler, Xenotransplantation: Risks, clinical potentail and future prospects (1996) Emerging Infect. Dis., 2, pp. 64-70; Morrison, M.E., Racaniello, V.R., Molecular cloning and expression of a murine homolog of a the human poliovirus receptor gene (1992) J. Virol., 66, pp. 2807-2813; Morrison, M.E., He, Y.-H., Wien, M.W., Hogle, J.M., Racaniello, V.R., Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication (1994) J. Virol, 68, pp. 2578-2588; Morse, S.S., Schluederberg, A., Emerging viruses: The evolution of viruses and viral diseases (1990) J. Infect. Dis., 162, pp. 1-15; Morse, S.S., (1994) The Evolutionary Biology of Viruses, , New York, Raven Press; Murphy, F.A., New emerging and reemerging infectious diseases (1994) Adv. Vir. Res., 43, pp. 1-52; Murray, Cai, G., Hoel, K., Zhang, J.-Y., Soike, K.F., Cabirac, G.F., Coronavirus Infects and Causes Demylination in Primate Central Nervous System (1992) Virology, 188, pp. 274-278; Rudert, F., Saunders, A., Rebstock, S., Thompson, J.A., Zimmermann, W., Characterization of murine carcinoembryonic antigen gene family members (1992) Mammalian Genome, 3, pp. 262-273; Schochetman, G., Stevens, R.H., Simpson, W., Presence of infectious polyadenylated RNA in the coronavirus avian infectious bronchitis virus (1977) Virology, 77, pp. 772-778; Signoret, N., Poignard, P., Blanc, D., Sattentau, Q.J., Human and simian immunodeficiency viruses: Virus-receptor interactions (1993) Trends Microbiol., 1, pp. 328-333; Tom, B.H., Rutzkey, L.P., Jakstys, M., Human colon adenocarcinoma cells I. Establishment and description of a new line (1976) In Vitro, 12, p. 180; Williams, R.K., Jiang, G.-S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6149-6199; Wimmer, B., An Introduction (1994) Cellular Receptors for Animal Viruses, pp. 1-14. , E. Wimmer eds., Coldspring Harbor Laboratory Press","Hensley, L.E.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599, United States",,,00652598,,AEMBA,"9782263","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753382
"Gómez N., Carrillo C., Salinas J., Parra F., Borca M.V., Escribano J.M.","57212697516;7006713396;7102468348;7005551438;7004561390;55402647000;","Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants",1998,"Virology","249","2",,"352","358",,95,"10.1006/viro.1998.9315","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032581989&doi=10.1006%2fviro.1998.9315&partnerID=40&md5=4c89d8ae80c57a36ca94159dccf1e3c6","Ctro. de Invest. en Sanid. Anim. C., Valdeolmos, 28130, Madrid, Spain; Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Depto. de Biotecnologia y Mejora G., INIA, 28040, Madrid, Spain; Inst. Univ. de Biotecnologia de A., Facultad de Medicina, Universidad de Oviedo, 33006, Oviedo, Spain","Gómez, N., Ctro. de Invest. en Sanid. Anim. C., Valdeolmos, 28130, Madrid, Spain; Carrillo, C., Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Salinas, J., Depto. de Biotecnologia y Mejora G., INIA, 28040, Madrid, Spain; Parra, F., Inst. Univ. de Biotecnologia de A., Facultad de Medicina, Universidad de Oviedo, 33006, Oviedo, Spain; Borca, M.V., Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Escribano, J.M., Ctro. de Invest. en Sanid. Anim. C., Valdeolmos, 28130, Madrid, Spain","The use of transgenic plants as vaccine production systems was described recently. We report on the immunological response elicited by two recombinant versions of the glycoprotein S from the swine-transmissible gastroenteritis coronavirus (TGEV) expressed in transgenic plants. Arabidoposis plants were genetically transformed with cDNAs constructs encoding either the N-terminal domain (amine acid residues 1-750) or the full-length glycoprotein S of TGEV, responsible for the neutralizing antibody induction against the virus, under the control of the cauliflower mosaic virus 35S (CaMV 35S) promoter. Genomic DNA and mRNA analyses of leaf extracts from transformed plants demonstrated the incorporation of the foreign cDNA into the arabidopsis genome, as well as their transcription. Expression of recombinant polypeptides were observed in most transgenic plants by ELISA using specific antibodies. Mice immunized with leaf extracts from transgenic plants developed antibodies that reacted specifically with TGEV in ELISA, immunoprecipitated the virus-induced protein, and neutralized the virus infectivity. From these results, we conclude that transgenic plants expressing glycoprotein S polypeptides may possibly be used as a source of recombinant antigen for vaccine production.",,"virus glycoprotein; Arabidopsis; article; Coronavirus; gene expression regulation; nonhuman; priority journal; protein expression; transgene; vaccine production","Arakawa, T., Chong, D.K.X., Langridge, W.H.R., Efficacy of a food plant-based oral cholera toxin B subunit vaccine (1998) BioTechniques, 16, pp. 292-297; Baulcombe, D.C., Saunders, G.R., Bevan, M.W., Mayo, M.A., Harrison, B.D., Expression of biologically active viral satellite RNA from nuclear genome of transformed plants (1986) Nature, 321, pp. 446-449; Bechtold, N., Ellis, J., Pelletier, G., AgrobacteriumArabidopsis thaliana (1993) C. R. Acad. Sci. Paris Sci. Vie, 316, pp. 1194-1199; Bullido, R., Alonso, F., Gómez De Moral, M., Ezquerra, A., Alvarez, B., Ortuño, E., Dominguez, J., Monoclonal antibody 2F4/11 recognizes the α chain of the porcine β2 (1996) J. Immunol. Methods, 195, pp. 125-134; Carrillo, C., Wigdorovitz, A., Oliveros, J.C., Zamorano, P.I., Sadir, A.M., Gómez, N., Salinas, J., Borca, M.V., Protective immune response to foot-and-mouth disease virus with VP1 expressed in transgenic plants (1998) J. Virol., 72, pp. 1688-1690; Correa, I., Jiménez, G., Suñé, C., Bullido, M.J., Enjuanes, L., Antigenic structure of E2-glycoprotein of transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-94; De Diego, M., Laviada, M.D., Enjuanes, L., Escribano, J.M., Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 6502-6508; De Diego, M., Rodríguez, F., Alcaraz, C., Gómez, N., Alonso, C., Escribano, J.M., Characterization of the IgA and subclass IgG responses to neutralizing epitopes after infection of pregnant sows with the transmissible gastroenteritis virus or the antigenically related porcine respiratory coronavirus (1994) J. Gen. Virol., 75, pp. 2585-2593; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S (1990) J. Gen. Virol., 71, pp. 1313-1323; Faye, L., Fitchette-Laine, A.C., Gomord, V., Chekkati, A., Delaunay, A.M., Driouich, A., Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins (1993) Soc. Exp. Biol. Semin. Ser., 53, pp. 213-242; Garwes, D.J., Lucas, M.H., Higgins, D.A., Pike, B.V., Cartwright, S.F., Antigenicity of structural components from porcine transmissible gastroenteritis virus (1978) Vet. Microbiol., 3, pp. 179-190; Gebauer, F., Posthumus, W.P.A., Correa, I., Suñé, C., Smerdou, C., Sánchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virology, 183, pp. 225-238; Haq, T.A., Mason, H.S., Clements, J.D., Arntzen, C.J., Oral immunization with a recombinant bacterial antigen produced in transgenic plants (1995) Science, 268, pp. 714-716; Haughn, G., Somerville, C., Sulfonylurea-resistant mutants ofArabidopsis thaliana (1986) Mol. Gen. Genet., 204, pp. 430-434; Hu, S., Bruszewski, J., Smallig, R., Browne, J.K., Studies of TGEV spike protein GP195 expressed inE coli (1987) Immunobiology of Proteins and Peptides. II. Viral and Bacterial Antigens, , New York: Plenum Press. p. 63; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Mason, H.S., Lam, D.M.-K., Arntzen, C.J., Expression of hepatitis B surface antigen in transgenic plants (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 11745-11749; Mason, H.S., Ball, J.M., Shi, J.-J., Jiang, X., Estes, M.K., Arntzen, C.J., Expression of Norwalk virus capsid protein in transgenic tobacco and potato and its oral immunogenicity in mice (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 5335-5340; McGarvey, P.B., Hammond, J., Dienelt, M.M., Hooper, D.C., Fu, Z.F., Dietzschold, B., Koprowski, H., Michaels, F.H., Expression of the rabies virus glycoprotein in transgenic tomatoes (1995) BioTechnology, 13, pp. 1484-1487; Saif, L.J., Bohl, E.H., Passive immunity in transmissible gastroenteritis of swine: Immunoglobulin classes of milk antibodies after oral-intranasal inoculation of sows with a live low cell culture-passaged virus (1979) Am. J. Vet. Res., 40, pp. 115-117; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Smerdou, C., Urniza, A., Curtis R. III, Enjuanes, L., Characterization of transmissible gastroenteritis coronavirus S protein expression products in avirulent S. typhimurium (1996) Vet. Microbiol., 48, pp. 87-100; Tacket, C.O., Mason, H.S., Losonsky, G., Clements, J.D., Levine, M.M., Arntzen, C.J., Immunogenicity in humans of a recombinant bacterial antigen delivered in a transgenic potato (1998) Nat. Med., 4, pp. 607-609; Thanavala, Y., Yang, Y.-F., Lyons, P., Mason, H.S., Arntzen, C., Immunogenicity of transgenic plant-derived hepatitis B surface antigen (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 3358-3361; Torres, J.M., Alonso, C., Ortega, A., Mittal, S., Graham, F., Enjuanes, L., Tropism of human adenovirus type 5-based vectors in swine and their ability to protect against transmissible gastroenteritis coronavirus (1996) J. Virol., 70, pp. 3770-3780; Torres, J.M., Sánchez, C., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protectionin vivo (1988) Vet. Microbiol., 18, pp. 197-203","Escribano, J.M.; CISA-INIA, Valdeolmos, 28130 Madrid, Spain; email: escriban@inia.es",,"Academic Press Inc.",00426822,,VIRLA,"9791026","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032581989
"Clark K.J., Sarr A.B., Grant P.G., Phillips T.D., Woode G.N.","16681335500;7003769325;57197566552;7401766659;7005628239;","In vitro studies on the use of clay, clay minerals and charcoal to adsorb bovine rotavirus and bovine coronavirus",1998,"Veterinary Microbiology","63","2-4",,"137","146",,30,"10.1016/S0378-1135(98)00241-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031786695&doi=10.1016%2fS0378-1135%2898%2900241-7&partnerID=40&md5=e4110b9a81c5ed33f8fdfd5d1a5b5676","Dept. Vet. Pathobiology Pub. Hlth., Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States; Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States","Clark, K.J., Dept. Vet. Pathobiology Pub. Hlth., Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States; Sarr, A.B., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States; Grant, P.G., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States; Phillips, T.D., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States; Woode, G.N., Dept. Vet. Pathobiology Pub. Hlth., Coll. of Vet. Med., Texas AM Univ., College Station, TX 77845, United States","Rotaviruses are the leading cause and coronaviruses are the major contributors of acute gastroenteritis in the young of various mammalian and avian species. Despite numerous trials and decades of research, vaccines have limited efficacy particularly for calves. As an alternative method of controlling infection, we have investigated broad spectrum antiviral agents that are not discriminatory among various viruses. This report involves testing a variety of adsorbent agents including charcoal, clay, and clay minerals to adsorb rotavirus and coronavirus in vitro. Results revealed that all the adsorbent agents had good to excellent capability of adsorbing rotavirus and excellent capability of adsorbing coronavirus. Percent adsorptions ranged from 78.74% to 99.89% for rotavirus and 99.99% for coronavirus; while sand (negative control) was <0.01%. A high affinity binding was present as determined by a low percent desorption (0.06-3.09%). However, the adsorbent bound virus complex retained, and may have actually enhanced, infectivity. Copyright (C) 1998 Elsevier Science B.V.","Charcoal; Clay; Coronavirus; Rotavirus; Viral adsorbers","antivirus agent; charcoal; animal cell; article; binding affinity; clay; controlled study; coronavirus; fowl; gastroenteritis; in vitro study; infection control; mammal; nonhuman; rotavirus; sand; virus adsorption; virus infectivity; Adsorption; Aluminum Silicates; Animals; Cattle; Cattle Diseases; Charcoal; Coronavirus Infections; Coronavirus, Bovine; Minerals; Rotavirus; Rotavirus Infections","Abehsera, M., Clay cures for modern ailments (1979) The Healing Clay Vol. 2, 2, pp. 83-109. , In: Anonymous (Ed.), Swan House Brooklyn, NY; Bern, C., Glass, R.I., Impact of Diarrheal Diseases Worldwide (1994) Viral Infections of the Gastrointestinal Tract, 2, pp. 1-26. , In: Kapikian, A.Z. (Ed.) Marcel Dekker, New York; Black, R.E., Merson, M.H., Taylor, P.R., Yolken, R.H., Sack, D.A., Glucose vs. sucrose in oral rehydration solutions for infants and young children with rotavirus-associated diarrhea (1981) Pediatrics, 67, pp. 79-83; Bridger, J.C., Woode, G.N., Characterization of two particle types of calf rotavirus (1976) J. Gen. Virol., 31, pp. 245-250; Bywater, R.J., Diarrhoea treatments: Fluid replacement and alternatives (1983) Ann. Rech. Vet., 14, pp. 556-560; Bywater, R.J., Woode, G.N., Oral fluid replacement by a glucose glycine electrolyte formulation in E. coli and rotavirus diarrhoea in pigs (1980) Vet. Rec., 106, pp. 75-78; De Leeuw, P.W., Ellens, D.J., Talmon, F.P., Zimmer, G.N., Kommerij, R., Rotavirus infections in calves: Efficacy of oral vaccination in endemically infected herds (1980) Res. Vet. Sci., 29, pp. 142-147; Dwyer, R.M., Powell, D.G., Roberts, W., Donahue, M., Lyons, E.T., Osborne, M., Woode, G., A study of the etiology and control of infectious diarrhea among foals in central Kentucky (1991) Proc. 36th Annual Meeting. AAEP, pp. 337-355; Fernelius, A.L., Ritchie, A.E., Classick, L.G., Norman, J.O., Mebus, C.A., Cell culture adaptation and propagation of a reovirus-like agent of calf diarrhea from a field outbreak in Nebraska (1972) Arch. Virusforsch., 37, pp. 114-130; Hardy, M.E., Woode, G.N., Xu, Z., Gorziglia, M., Comparative amino acid sequence analysis of VP4 for VP7 serotype 6 bovine rotavirus strains NCDV, B641, and UK (1991) J. Virol., 65, pp. 5535-5538; House, J.A., Economic impact of rotavirus and other neonatal disease agents of animals (1978) J. Am. Vet. Med. Assoc., 173, pp. 573-576; Kelly, S., Sanderson, W.W., Reidl, C., Removal of enteroviruses from sewage by activated sludge (1961) J. Water Pollut. Control Fed., 33, pp. 1056-1062; Lipson, S.M., Stotzky, G., Adsorption of reovirus to clay minerals: Effects of cation-exchange capacity, cation saturation, and surface area (1983) Appl. Environ. Microbiol., 46, pp. 673-682; Lipson, S.M., Stotzky, G., Effect of proteins on reovirus adsorption to clay minerals (1984) Appl. Environ. Microbiol., 48, pp. 525-530; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attentuation, and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Myers, L.L., Snodgrass, D.R., Colostral and milk antibody titers in cows vaccinated with a modified live-rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Assoc., 181, pp. 486-488; Parwani, A.V., Hussein, H.A., Rosen, B.I., Lucchelli, A., Navarro, L., Saif, L.J., Characterization of field strains of group A bovine rotaviruses by using polymerase chain reaction-generated G and P type-specific cDNA probes (1993) J. Clin. Microbiol., 31, pp. 2010-2015; Phillips, T.D., Kubena, L.F., Harvey, R.B., Taylor, D.R., Heidelbaugh, N.D., Hydrated sodium calcium aluminosilicate: A high affinity sorbent for aflatoxin (1988) Poult. Sci., 67, pp. 243-247; Phillips, T.D., Sarr, A.B., Grant, P.G., Selective chemisorption and detoxification of aflotoxins by phyllosilicate clay (1995) Natural Toxins, 3, pp. 204-213; Preston, D.R., Farrah, S.R., Activation thermodynamics of virus adsorption to solids (1988) Appl. Environ. Microbiol., 54, pp. 2650-2654; Ramu, J., Clark, K., Woode, G.N., Sarr, A.B., Phillips, T.D., Adsorption of cholera and heat-labile Escherichia coli enterotoxins by various adsorbents: An in vitro study (1997) J. Food Protection, 60, pp. 1-5; Reed, I.J., Muench, H., A simple method in estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Schaub, S.A., Sagik, B.P., Association of enteroviruses with natural and artificially introduced colloidal solids in water and infectivity of solids-associated virions (1975) Appl. Microbiol., 30, pp. 212-222; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am. J. Vet. Res., 37, pp. 1031-1041; Snodgrass, D.R., Nagy, L.K., Sherwood, D., Campbell, I., Passive immunity in calf diarrhea: Vaccination with K99 antigen of enterotoxigenic Escherichia coli and rotavirus (1982) Infect. Immun., 37, pp. 586-591; Storz, J., Herrler, G., Snodgrass, D.R., Hussain, K.A., Zhang, X.M., Clark, M.A., Rott, R., Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine coronavirus (1991) J. Gen. Virol., 72, pp. 2817-2820; Taylor, D.H., Moore, R.S., Sturman, L.S., Influence of pH and electrolyte composition on adsorption of poliovirus by soils and minerals (1981) Appl. Environ. Microbiol., 42, pp. 976-984; Tzipori, S., The aetiology and diagnosis of calf diarrhoea (1981) Vet. Rec., 108, pp. 510-515; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Adv. Vet. Sci. Comp. Med., 29, pp. 103-206; Waltner-Toews, D., Martin, S.W., Meek, A.H., McMillan, I., Crouch, C.F., A field trial to evaluate the efficacy of a combined rotavirus-coronavirus/Escherichia coli vaccine in dairy cattle (1985) Can. J. Comp. Med., 49, pp. 1-9; Ward, R.L., McNeal, M.C., Sander, D.S., Greenberg, H.B., Bernstein, D.I., Immunodominance of the VP4 neutralization protein of rotavirus in protective natural infections of young children (1993) J. Virol., 67, pp. 464-468; Woode, G.N., Kelso, N.E., Simpson, T.F., Gaul, S.K., Evans, L.E., Babiuk, L., Antigenic relationships among some bovine rotaviruses: Serum neutralization and cross-protection in gnotobiotic calves (1983) J. Clin. Microbiol., 18, pp. 358-364; Woode, G.N., Zheng, S.L., Rosen, B.I., Knight, N., Gourley, N.E., Ramig, R.F., Protection between different serotypes of bovine rotavirus in gnotobiotic calves: Specificity of serum antibody and coproantibody responses (1987) J. Clin. Microbiol., 25, pp. 1052-1058; Woode, G.N., Crouch, C.F., Naturally occurring and experimentally induced rotaviral infections of domestic and laboratory animals (1978) J. Am. Vet. Med. Assoc., 173, pp. 522-526; Xu, Z., Hardy, M.E., Woode, G.N., Ramig, R.F., Immunodominant neutralizing antigens depend on the virus strain during a primary immune response in calves to bovine rotaviruses (1993) Vet. Microbiol., 35, pp. 33-43; Xu, Z., Woode, G.N., Studies on the role of VP4 of G serotype 10 rotavirus (B223) in the induction of the heterologous immune response in calves (1993) Virology, 196, pp. 294-297; Yuan, L., Kang, S.Y., Ward, L.A., To, T.L., Saif, L.J., Antibody-secreting cell responses and protective immunity assessed in gnotobiotic pigs inoculated orally or intramuscularly with inactivated human rotavirus (1998) J. Virol., 72, pp. 330-338; Zheng, S.L., Woode, G.N., Melendy, D.R., Ramig, R.F., Comparative studies of the antigenic polypeptide species VP4, VP6, and VP7 of three strains of bovine rotavirus (1989) J. Clin. Microbiol., 27, pp. 1939-1945","Woode, G.N.; Dept. Veterinary Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77845, United States; email: mzemanek@cvm.tamu.edu",,,03781135,,VMICD,"9850994","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0031786695
"Fischer F., Stegen C.F., Masters P.S., Samsonoff W.A.","7202883540;6602557632;7006234572;6603736426;","Analysis of constructed E gene mutants of mouse hepatitis: Virus confirms a pivotal role for E protein in coronavirus assembly",1998,"Journal of Virology","72","10",,"7885","7894",,116,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031689187&partnerID=40&md5=d04afb2b8253af69a81c2b729472106b","Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States; Department of Biological Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States; Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; LaboRétro, INSERM U412, ENS, 46 allee d'Italie, 69364 Lyon Cedex 07, France; Physiologisch-Chemisches Institut, Universitaet Tuebingen, Germany","Fischer, F., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States, LaboRétro, INSERM U412, ENS, 46 allee d'Italie, 69364 Lyon Cedex 07, France; Stegen, C.F., Department of Biological Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States, Physiologisch-Chemisches Institut, Universitaet Tuebingen, Germany; Masters, P.S., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; Samsonoff, W.A., Department of Biomedical Sciences, State Univ. of New York at Albany, Albany, NY 12201, United States, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States","Expression studies have shown that the coronavirus small envelope protein E and the much more abundant membrane glycoprotein M are both necessary and sufficient for the assembly of virus-like particles in cells. As a step toward understanding the function of the mouse hepatitis virus (MHV) E protein, we carried out clustered charged-to-alanine mutagenesis on the E gene and incorporated the resulting mutations into the MHV genome by targeted recombination. Of the four possible clustered charged-to-alanine E gene mutants, one was apparently lethal and one had a wild-type phenotype. The two other mutants were partially temperature sensitive, forming small plaques at the nonpermissive temperature. Revertant analyses of these two mutants demonstrated that the created mutations were responsible for the temperature-sensitive phenotype of each and provided support for possible interactions among E protein monomers. Both temperature-sensitive mutants were also found to be markedly thermolabile when grown at the permissive temperature; suggesting that there was a flaw in their assembly. Most significantly, when virions of one of the mutants were examined by electron microscopy, they were found to have strikingly aberrant morphology in comparison to the wild type: most mutant virions had pinched and elongated shapes that were rarely seen among wild-type virions. These results demonstrate an important, probably essential, role for the E protein in coronavirus morphogenesis.",,"virus protein; animal cell; article; controlled study; coronavirus; electron microscopy; gene structure; hepatitis virus; mouse; mutagenesis; nonhuman; priority journal; protein expression; temperature sensitive mutant; virus assembly; virus morphogenesis; virus mutant; Amino Acid Sequence; Animals; Base Sequence; Cell Line; DNA, Viral; Mice; Microscopy, Electron; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis; Mutation; Phenotype; Sequence Homology, Amino Acid; Virus Assembly","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Bass, S.H., Mulkerrin, M.G., Wells, J.A., A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor (1991) Proc. 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Virol., 66, pp. 1841-1848; Leibowitz, J.L., Perlman, S., Weinstock, G., DeVries, J.R., Budzilowicz, C., Weissemann, J.M., Weiss, S.R., Detection of a murine coronavirus nonstructural protein encoded in a downstream open reading frame (1988) Virology, 164, pp. 156-164; Liljeström, P., Lusa, S., Huylebroeck, D., Garoff, H., In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: The small 6,000-molecular-weight membrane protein modulates virus release (1991) J. Virol., 65, pp. 4107-4113; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3c protein with the virion envelope (1991) Virology, 185, pp. 911-917; Loewy, A., Smyth, J., Von Bonsdorff, C.-H., Liljeström, P., Schlesinger, M.J., The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process (1995) J. Virol., 69, pp. 469-475; Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Parker, M.M., Masters, P.S., Unpublished data; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Reijo, R.A., Cooper, E.M., Beagle, G.J., Huffaker, T.C., Systematic mutational analysis of the yeast beta-tubulin gene (1994) Mol. Biol. Cell, 5, pp. 29-43; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schwarz, B., Routledge, E., Siddell, S.G., Murine nonstructural protein ns2 is not essential for virus replication in transformed cells (1990) J. Virol., 64, pp. 4784-4791; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene of bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Skinner, M.A., Ebner, D., Siddell, S.G., Coronavirus MHV-JHM mRNA 5 has a sequence arrangement which potentially allows translation of a second, downstream open reading frame (1985) J. Gen. Virol., 66, pp. 581-592; Skinner, M.A., Siddell, S.G., Coding sequence of coronavirus MHV-JHM mRNA4 (1985) J. Gen. Virol., 66, pp. 593-596; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns 4 gene of mouse hepatitis virus (MHV), strain A59 contains two ORFs and thus differs from ns 4 of the JHM and S strains (1993) Arch. Virol., 129, pp. 301-309; Wertman, K.F., Drubin, D.G., Botstein, D., Systematic mutational analysis of the yeast ACT1 gene (1992) Genetics, 132, pp. 337-350; Xiang, W., Cuconati, A., Paul, A.V., Cao, X., Wimmer, E., Molecular dissection of the multifunctional poliovirus RNA-binding protein 3AB (1995) RNA, 1, pp. 892-904; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Samsonoff, W.A.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"9733825","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031689187
"Clark K.J., Grant P.G., Sarr A.B., Belakere J.R., Swaggerty C.L., Phillips T.D., Woode G.N.","16681335500;57197566552;7003769325;6504111020;35585950200;7401766659;7005628239;","An in vitro study of theaflavins extracted from black tea to neutralize bovine rotavirus and bovine coronavirus infections",1998,"Veterinary Microbiology","63","2-4",,"147","157",,38,"10.1016/S0378-1135(98)00242-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031787413&doi=10.1016%2fS0378-1135%2898%2900242-9&partnerID=40&md5=2930f15363a46f856845f9f9f0cc3664","Dept. of Veterinary Pathobiology, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States","Clark, K.J., Dept. of Veterinary Pathobiology, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Grant, P.G., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Sarr, A.B., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Belakere, J.R., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Swaggerty, C.L., Dept. of Veterinary Pathobiology, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Phillips, T.D., Dept. of Vet. Anat. and Pub. Health, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States; Woode, G.N., Dept. of Veterinary Pathobiology, Coll. of Vet. Med., Texas AM Univ., College Station, TX 77843-4467, United States","Crude theaflavin was extracted from black tea and then fractionated by HPLC into five components (initial peaks (IP), TF1, TF(2A), TF(2B), and TF3). The crude extract and the various fractions of theaflavin were collected and tested, individually and in combination, for antirotaviral activity. The mean effective concentration (EC50) was calculated and compared. Activity varied from the most active being the uncharacterized theaflavin-like initial peaks (IP) with an EC50 of 0.125μg/ml to the least active being theaflavin-3 monogallate (TF(2A)) with an EC50 of 251.39μg/ml. The combination of TF1+TF(2A)+TF(2B)+TF3 was more active than the sum of the activities of these four fractions individually, indicating synergism among the peaks. Only the crude extract was assayed for activity against coronavirus; the EC50 was 34.7μg/ml. Copyright (C) 1998 Elsevier Science B.V.","Coronavirus; Neutralization; Rotavirus; Tea; Theaflavin; Theaflavin gallate","antivirus agent; quercetin; theaflavin; unclassified drug; animal cell; antiviral activity; article; cattle; controlled study; Coronavirus; dose response; high performance liquid chromatography; nonhuman; Rotavirus; tea; virus infection; virus neutralization; Animals; Antiviral Agents; Biflavonoids; Catechin; Cattle; Cattle Diseases; Cell Line; Chelating Agents; Chromatography, High Pressure Liquid; Coronavirus Infections; Coronavirus, Bovine; Gallic Acid; Models, Molecular; Molecular Conformation; Rotavirus; Rotavirus Infections; Tea","(1993) ChemPlus: Extension for HyperChem, pp. 95-127. , Anonymous Hypercube Ont., Canada; (1994) HyperChem: Computational Chemistry, pp. 1-285. , Anonymous, Hypercube, Ont., Canada; Clark, K.J., Sarr, A.B., Grant, P.G., Phillips, T.D., Woode, G.N., In vitro studies on the use of clay, clay minerals, and charcoal to adsorb bovine rotavirus and bovine coronavirus (1998) Vet. Microbiol., 63, pp. 137-146; De Leeuw, P.W., Ellens, D.J., Talmon, F.P., Zimmer, G.N., Kommerij, R., Rotavirus infections in calves: Efficacy of oral vaccination in endemically infected herds (1980) Res. Vet. Sci., 29, pp. 142-147; Fernelius, A.L., Ritchie, A.E., Classick, L.G., Norman, J.O., Mebus, C.A., Cell culture adaptation and propagation of a reovirus-like agent of calf diarrhea from a field outbreak in Nebraska (1972) Arch. Virusforsch., 37, pp. 114-130; Green, R.H., Inhibition of multiplication of influenza virus by extracts of tea (1949) Proc. Soc. Exp. Biol. Med., 71, pp. 84-85; Hara, Y., Matsuzaki, T., Suzuki, T., Angiotensin I converting enzyme inhibiting activity of tea component (1987) Nippon Nokeikagaku Kaishi, 61, pp. 803-808; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attentuation, and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Mukoyama, A., Ushijima, H., Nishimura, S., Koike, H., Toda, M., Hara, Y., Shimamura, T., Inhibition of rotavirus and enterovirus infections by tea extracts (1991) Jpn. J. Med. Sci. Biol., 44, pp. 181-186; Myers, L.L., Snodgrass, D.R., Colostral and milk antibody titers in cows vaccinated with a modified live rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Assoc., 181, pp. 486-488; Nakayama, M., Toda, M., Okubo, S., Shimamura, T., Inhibition of influenza virus infection by tea (1990) Lett. Appl. Microbiol., 11, pp. 38-40; Nakayama, M., Suzuki, K., Toda, M., Okubo, S., Hara, Y., Shimamura, T., Inhibition of the infectivity of influenza virus by tea polyphenols (1993) Antiviral. Res., 21, pp. 289-299; Reed, I.J., Muench, H., A simple method in estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Roberts, E.A.H., Myers, M., The phenolic substances of manufactured tea. VI. The preparation of theaflavin and of theaflavin gallate (1959) J. Sci. Food Agric., pp. 176-179; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am. J. Vet. Res., 37, pp. 1031-1041; Snodgrass, D.R., Nagy, L.K., Sherwood, D., Campbell, I., Passive immunity in calf diarrhea: Vaccination with K99 antigen of enterotoxigenic Escherichia coli and rotavirus (1982) Infect. Immun., 37, pp. 586-591; Storz, J., Herrler, G., Snodgrass, D.R., Hussain, K.A., Zhang, X.M., Clark, M.A., Rott, R., Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine coronavirus (1991) J. Gen. Virol., 72, pp. 2817-2820; Takino, Y., Ferretti, A., Flanagan, V., Gianturco, M., Vogel, M., The structure of theaflavin, a polyphenol of black tea (1965) Tetrahedron Lett., 45, pp. 4019-4025; Waltner-Toews, D., Martin, S.W., Meek, A.H., McMillan, I., Crouch C.F. A field trial to evaluate the efficacy of a combined rotavirus-coronavirus/Escherichia coli vaccine in dairy cattle (1985) Can. J. Comp. Med., 49, pp. 1-9; Woode, G.N., Zheng, S.L., Rosen, B.I., Knight, N., Gourley, N.E., Ramig, R.F., Protection between different serotypes of bovine rotavirus in gnotobiotic calves: Specificity of serum antibody and coproantibody responses (1987) J. Clin. Microbiol., 25, pp. 1052-1058; Zheng, S.L., Woode, G.N., Melendy, D.R., Ramig, R.F., Comparative studies of the antigenic polypeptide species VP4, VP6, and VP7 of three strains of bovine rotavirus (1989) J. Clin. Microbiol., 27, pp. 1939-1945","Woode, G.N.; Department Veterinary Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843-4467, United States; email: mezemanek@cvm.tamu.edu",,,03781135,,VMICD,"9850995","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0031787413
"Repass J.F., Makino S.","57186535600;7403067550;","Importance of the positive-strand RNA secondary structure of a murine coronavirus defective interfering RNA internal replication signal in positive-strand RNA synthesis",1998,"Journal of Virology","72","10",,"7926","7933",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031694636&partnerID=40&md5=ccc5a2617f8e3112a83a4bf01fc0ee56","Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States; Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States","Repass, J.F., Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States; Makino, S., Department of Microbiology, University of Texas at Austin, Austin, TX 78712, United States, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States","The RNA elements that are required for replication of defective interfering (DI) RNA of the JHM strain of mouse hepatitis virus (MHV) consist of three discontinuous genomic regions: about 0.46 to 0.47 kb from both terminal sequences and an internal 58-nucleotide (nt)-long sequence (58-nt region) present at about 0.9 kb from the 5' end of the DI genome. The internal region is important for positive-strand DI RNA synthesis (Y. N. Kim and S. Makino, J. Virol. 69:4963-4971, 1995). We further characterized the 58-nt region in the present study and obtained the following results. (i) The positive-strand RNA structure in solution was comparable with that predicted by computer modeling. (ii) Positive-strand RNA secondary structure, but not negative-strand RNA structure, was important for the biological function of the region. (iii) The biological function had a sequence-specific requirement. We discuss possible mechanisms by which the internal cis-acting signal drives MHV positive-strand DI RNA synthesis.",,"oligonucleotide; ribonuclease; virus rna; article; base pairing; coronavirus; nonhuman; priority journal; rna analysis; rna replication; rna structure; rna synthesis; sequence analysis; signal transduction; virus genome; Animals; Base Sequence; Cell Line; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RNA, Viral; Solutions","Barrera, I., Schuppli, U., Sogo, J.M., Weber, H., Different mechanisms of recognition of bacteriophage Qβ plus and minus strand RNAs by Qβ replicase (1993) J. Mol. Biol., 232, pp. 512-521; Baudin, F., Bach, C., Cusack, S., Ruigrok, R.W.H., Structure of influenza virus RNP. 1. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent (1994) EMBO J., 13, pp. 3158-3165; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; De Groot, R.J., Van Der Most, R.G., Spaan, W.J.M., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frame shift mutations (1992) J. Virol., 66, pp. 5898-5905; Furuya, T., Lai, M.M.C., Three different cellular proteins bind to complementary sites on the 5′-end-positive and 3′-end-negative strands of mouse hepatitis virus RNA (1993) J. Virol., 67, pp. 7215-7222; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Jacobson, S.J., Konings, D.A., Sarnow, P., Biochemical and genetic evidence for a pseudoknot structure at the 3′ terminus of the poliovirus RNA genome and its role in viral RNA amplification (1993) J. Virol., 67, pp. 2961-2971; Joo, M., Banerjee, S., Makino, S., Replication of murine coronavirus defective interfering RNA from negative-strand transcripts (1996) J. Virol., 70, pp. 5769-5776; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenie consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.-N., Makino, S., Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal (1995) J. Virol., 69, pp. 4963-4971; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: mRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Lee, H.J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Li, H.P., Zhang, X., Duncan, R., Comai, L., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9544-9549; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNa reveals the requirement of an internal and discontinuous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Luytjes, W., Gerritsma, H., Spaan, W.J.M., Replication of synthetic defective interfering RNAs derived from coronavirus mouse hepatitis virus-A59 (1996) Virology, 216, pp. 174-183; Makino, S., Fujioka, N., Fujiwara, K., Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus (1985) J. Virol., 54, pp. 329-336; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNa synthesis: A regulated, expressed subgenomic defective interfering RNa results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Meyer, F., Weber, H., Weissman, C., Interactions of Qβ replicase with Qβ RNA (1981) J. Mol. Biol., 153, pp. 631-660; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis virus, strain A59 (1989) Virology, 171, pp. 141-148; Schuppli, D., Barrera, I., Weber, H., Identification of replication elements on bacteriophage Qβ minus strand RNA that are essential for template activity with Qβ replicase (1994) J. Mol. Biol., 243, pp. 811-815; Stern, S., Moazed, D., Noller, H.F., Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension (1988) Methods Enzymol., 164, pp. 481-489; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Winship, P.R., An improved method for directly sequencing PCR material using dimethyl sulfoxide (1989) Nucleic Acids Res., 17, p. 1266; Yu, W., Leibowitz, J., A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology, 214, pp. 128-138; Yu, W., Leibowitz, J., Specific binding of host cellular proteins to multiple sites within the 3′ end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Zuker, M., Steigler, P., Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information (1981) Nucleic Acids Res., 9, pp. 133-148","Makino, S.; Department of Microbiology, University of Texas, Austin, TX 78712, United States; email: makino@mail.utexas.edu",,,0022538X,,JOVIA,"9733830","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031694636
"Smith A., Thomas M., Kent J., Nicholson K.","35429650000;11339148200;57197399234;7103216939;","Effects of the common cold on mood and performance",1998,"Psychoneuroendocrinology","23","7",,"733","739",,35,"10.1016/S0306-4530(98)00042-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032416934&doi=10.1016%2fS0306-4530%2898%2900042-0&partnerID=40&md5=854ecba813dfc2831bd42019c8738334","Health Psychology Research Unit, Dept. of Experimental Psychology, University of Bristol, Bristol BS8 1TN, United Kingdom; Department of Microbiology, University of Leicester, Leicester, United Kingdom; Health Psychology Research Unit, Department of Psychology, 8 Woodland Road, Bristol BS8 1TN, United Kingdom","Smith, A., Health Psychology Research Unit, Dept. of Experimental Psychology, University of Bristol, Bristol BS8 1TN, United Kingdom, Health Psychology Research Unit, Department of Psychology, 8 Woodland Road, Bristol BS8 1TN, United Kingdom; Thomas, M., Health Psychology Research Unit, Dept. of Experimental Psychology, University of Bristol, Bristol BS8 1TN, United Kingdom; Kent, J., Department of Microbiology, University of Leicester, Leicester, United Kingdom; Nicholson, K., Department of Microbiology, University of Leicester, Leicester, United Kingdom","Previous research has shown that both experimentally-induced and naturally occurring upper respiratory tract illnesses (URTIs) influence mood and mental functioning. None of the previous studies of naturally occurring colds has conducted appropriate virological assays to determine the nature of the infecting agent. This is an essential methodological step in studies of malaise associated with URTIs. The aim of this research was to investigate the effects of naturally occurring colds on mood and objective measures of performance. This was done by first conducting a cross-sectional comparison of 37 healthy people and 158 volunteers with colds and then a longitudinal study in which 100 volunteers developed colds and 87 remained healthy. Virological techniques were used to identify infecting agents and comparisons made across the different groups. The results showed that having a cold was associated with reduced alertness and slowed reaction times. These effects were observed both for colds where the infecting virus was identified and those where it was not. Similar effects were obtained for both rhinovirus and coronavirus colds. One may conclude that upper respiratory tract illnesses lead to a reduction in subjective alertness and impaired psychomotor functioning. This was true for both illnesses where the infecting agent was identified and for those clinical illnesses where no virus was detected. It is now important to identify the mechanisms linking infection and illness with the behavioural changes. Similarly, the impact of these effects on real- life activities such as driving needs examining. Finally, methods of treatment need to be developed which not only treat the local symptoms of the illnesses but remove the negative mood and the performance impairments.","Alertness; Common cold; Coronavirus; Reaction time; Rhinovirus","adult; alertness; article; common cold; controlled study; coronavirus; female; human; major clinical study; malaise; male; mental health; mood; priority journal; psychomotor disorder; reaction time; rhinovirus; upper respiratory tract infection; Adolescent; Adult; Affect; Arousal; Attention; Common Cold; Cross-Sectional Studies; Female; Humans; Longitudinal Studies; Male; Psychomotor Performance; Reaction Time; Serial Learning; Students","Grant, J., Postinfluenzal judgement deflection among scientific personnel (1972) Asian Journal of Medicine, 8, pp. 535-539; Hall, S., Smith, A.P., Investigation of the effects and after-effects of naturally occurring upper respiratory tract illnesses on mood and performance (1996) Physiology and Behavior, 59, pp. 569-577; Kraaijeveld, C.A., Reed, S.E., Macnaughton, M.R., Enzyme-linked immunosorbent assay for detection of antibody in volunteers experimentally infected with coronavirus 229E group viruses (1980) Journal of Clinical Microbiology, 12, pp. 493-497; Nicholson, K.G., Baker, D.J., Farquhar, A., Hurd, D., Kent, J., Smith, S.H., Acute upper respiratory tract viral illness and influenza immunization in homes for the elderly (1990) Epidemiology and Infection, 105, pp. 609-618; Smith, A.P., Respiratory viruses and performance (1990) Philosophical Transactions of the Royal Society of London, 327 B, pp. 519-528; Smith, A.P., Thomas, M., Brockman, P., Noise, respiratory virus infections and performance (1993) Actes Inrets, 34, pp. 311-314; Smith, A.P., Thomas, M., Brockman, P., Kent, J., Nicholson, K.G., Effect of influenza B virus infection on human performance (1993) British Medical Journal, 306, pp. 760-761; Smith, A.P., Thomas, M., Perry, K., Whitney, H., Caffeine and the common cold (1997) Journal of Psychopharmacology, 11, pp. 319-324; Smith, A.P., Tyrrell, D.A.J., Al-Nakib, W., Coyle, K.B., Donovan, C.B., Higgins, P.G., Willman, J.S., Effects of experimentally induced respiratory virus infections and illness on psychomotor performance (1987) Neuropsychobiology, 18, pp. 144-148; Smith, A.P., Tyrrell, D.A.J., Al-Nakib, W., Coyle, K.B., Donovan, C.B., Higgins, P.G., Willman, J.S., The effects of experimentally induced respiratory virus infections on performance (1988) Psychological Medicine, 18, pp. 65-71; Smith, A.P., Tyrrell, D.A.J., Al-Nakib, W., Barrow, G.I., Higgins, P.G., Leekam, S., Trickett, S., Effects and after effects of the common cold and influenza on human performance (1989) Neuropsychobiology, 21, pp. 90-93; Smith, A.P., Tyrrell, D.A.J., Barrow, G.I., Higgins, P.G., Willman, J.S., Bull, S., Coyle, K.B., Trickett, S., Mood and experimentally-induced respiratory virus infections and illnesses (1992) Psychology and Health, 6, pp. 205-212; Smith, A.P., Tyrrell, D.A.J., Coyle, K., Willman, J.S., Selective effects of minor illnesses on human performance (1987) British Journal of Psychology, 78, pp. 183-188; Smith, A.P., Whitney, H., Thomas, M., Brockman, P., Perry, K., A comparison of the acute effects of a low dose of alcohol on mood and performance of healthy volunteers and subjects with upper respiratory tract illnesses (1995) Journal of Psychopharmacology, 9, pp. 267-272; Tye, J., The invisible factor-an inquiry into the relationship between influenza and accidents (1960) London: British Safety Council Report","Smith, A.; Health Psychology Research Unit, Department of Psychology, 8 Woodland Road, Bristol BS8 1TN, United Kingdom; email: Andy.P.Smith@bris.ac.uk",,,03064530,,PSYCD,"9854744","English","Psychoneuroendocrinology",Article,"Final",,Scopus,2-s2.0-0032416934
"Chouljenko V.N., Kousoulas K.G., Lin X., Storz J.","6603655227;7003476092;36768282000;7006694594;","Nucleotide and predicted amino acid sequences of all genes encoded by the 3' genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses",1998,"Virus Genes","17","1",,"33","42",,40,"10.1023/A:1008048916808","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031786419&doi=10.1023%2fA%3a1008048916808&partnerID=40&md5=8a3afc6abe3db752c53c511294b7a3b5","Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Chouljenko, V.N., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Kousoulas, K.G., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Lin, X., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Storz, J., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","The 3'-ends of the genomes (9538 bp) of two wild-type respiratory bovine coronavirus (RBCV) isolates LSU and OK were obtained by cDNA sequencing. In addition, the 3'-end of the genome (9545) of the wild-type enteric bovine coronavirus (EBCV) strain LY-138 was assembled from available sequences and by cDNA sequencing of unknown genomic regions. Comparative analyses of RBCV and EBCV nucleotide and deduced amino acid sequences revealed that RBCV-specific nucleotide and amino acid differences were disproportionally concentrated within the S gene and the genomic region between the S and E genes. Comparisons among virulent and avirulent BCV strains revealed that virulence-specific nucleotide and amino acid changes were located within the S and E genes, and the 32 kDa open reading frame.","cDNA; Coronavirus; Non-structural; Respiratory; S; Structural","complementary dna; nucleotide; amino acid sequence; amino terminal sequence; article; coronavirus; dna sequence; gene locus; human; human cell; intestine infection; nonhuman; nucleotide sequence; open reading frame; priority journal; respiratory tract infection; viral genetics; virus infection; virus virulence; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus, Bovine; Digestive System; DNA, Viral; Genes, Viral; Humans; Membrane Glycoproteins; Molecular Sequence Data; Open Reading Frames; Phylogeny; Respiratory System; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Tumor Cells, Cultured; Viral Envelope Proteins; Viral Proteins; Viral Structural Proteins; Virulence","Spaan, W., Cavanagh, D., Horzinek, M.C., (1988) J Gen Virol, 69, pp. 2939-2952; Wege, H., Siddell, S., Ter Meulen, V., (1982) Curr Top Microb & Immunol, 99, pp. 165-200; Storz, J., Stine, L., Liem, A., Anderson, G.A., (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Lai, M.M.C., (1990) Annu Rev Microbiol, 44, pp. 303-333; Lai, M.M., Cavanagh, D., (1997) Adv Virus Res, 48, pp. 1-100; Cox, G.J., Parker, M.D., Babiuk, L.A., (1989) Nuc Acids Res, 17, p. 5847; Cox, G.J., Parker, M.D., Babiuk, L.A., (1991) Virology, 185, pp. 509-512; Hofmann, M.A., Chang, R.Y., Ku, S., Brian, D.A., (1993) Virology, 196, pp. 163-171; Schultze, B., Herrler, G., (1992) J Gen Virol, 73, pp. 901-906; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., (1991) J Virol, 65, pp. 6232-6237; Rasschaert, D., Duarte, M., Laude, H., (1990) J Gen Virol, 71, pp. 2599-2607; Krempl, C., Schultze, B., Laude, H., Herrler, G., (1997) J Virol, 71, pp. 3285-3287; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., (1997) Virology, 227, pp. 378-388; Storz, J., Zhang, X.M., Rott, R., (1992) Arch Virol, 125, pp. 193-204; Zhang, X.M., Kousoulas, K.G., Storz, J., (1991) Virology, 185, pp. 847-852; Zhang, X.M., Kousoulas, K.G., Storz, J., (1991) Virology, 183, pp. 397-404; Sanger, F., Nicklen, S., Coulson, A.R., (1977) Proc Nattl Acad Sci USA, 74, pp. 5463-5467; Jimenez, C., Herbst, W., Biermann, U., Muller, J.M., Schliesser, T., (1989) Zentralblatt fur Veterinarmedizin. Reihe B, 36, pp. 635-638; Zhang, X.M., Kousoulas, K.G., Storz, J., (1992) Virology, 186, pp. 318-323; Zhang, X., Herbst, W., Kousoulas, K.G., Storz, J., (1994) Arch Virol, 134, pp. 421-426; Mounir, S., Talbot, P.J., (1993) J Gen Virol, 74, pp. 1981-1987; Vieler, E., Schlapp, T., Herbst, W., (1996) J Gen Virol, 77, pp. 1443-1447; Laude, H., (1995) Corona and Related Viruses: Functional Domains in the Spike Protein of Transmissible Gastroenteritis Virus, pp. 299-394. , Talbot P.J. and Levy G.A. (eds). Plenum Press, New York; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., (1991) Virology, 180, pp. 221-228; Cavanagh, D., (1995) The Coronaviridae: The Coronavirus Surface Glycoprotein, pp. 73-113. , Siddell S.G. (ed.). Plenum Press, New York and London; Yoo, D.W., Parker, M.D., Babiuk, L.A., (1991) Virology, 180, pp. 395-399; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., (1991) J Virol, 65, pp. 1916-1928; Chang, R.Y., Krishnan, R., Brian, D.A., (1996) J Virol, 70, pp. 2720-2729; Labonte, P., Mounir, S., Talbot, P.J., (1995) J Gen Virol, 76, pp. 431-435; Mounir, S., Labonte, P., Talbot, P.J., (1993) Adv Exp Med & Biol, 342, pp. 61-67; Brown, T.D.K., Brierly, I., (1995) The Coronaviridae: The Coronavirus Non-Structural Proteins, pp. 191-217. , Siddell S. (ed.) Plenum Press, New York and London; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., (1992) Virology, 188, pp. 666-675; Corpel, F., (1988) Nucl Acids Res, 16, pp. 10881-10890","Kousoulas, K.G.; Dept Veterin Microbiology Parasitol, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",,,09208569,,VIGEE,"9778786","English","Virus Genes",Article,"Final",Open Access,Scopus,2-s2.0-0031786419
"Belyavsky M., Belyavskaya E., Levy G.A., Leibowitz J.L.","6505627947;57189013946;35391580500;7006843902;","Coronavirus MHV-3-induced apoptosis in macrophages",1998,"Virology","250","1",,"41","49",,30,"10.1006/viro.1998.9356","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032505544&doi=10.1006%2fviro.1998.9356&partnerID=40&md5=61a7fec3f1276822a415a93e70527bf1","Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Coll. of Med., 208 Reynolds Building, College Station, TX 77843-1114, United States; Multi Organ Transplant Program, Toronto Hospital, University of Toronto, 621 University Ave. NU-10-151, Toronto, Ont. M5G 2C4, Canada","Belyavsky, M., Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Coll. of Med., 208 Reynolds Building, College Station, TX 77843-1114, United States; Belyavskaya, E., Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Coll. of Med., 208 Reynolds Building, College Station, TX 77843-1114, United States; Levy, G.A., Multi Organ Transplant Program, Toronto Hospital, University of Toronto, 621 University Ave. NU-10-151, Toronto, Ont. M5G 2C4, Canada; Leibowitz, J.L., Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Coll. of Med., 208 Reynolds Building, College Station, TX 77843-1114, United States","Infection with mouse hepatitis virus strain 3 (MHV-3) results in lethal fulminant hepatic necrosis in fully susceptible BALB/c mice compared to the minimal disease observed in resistant strain A/J mice. Macrophages play a central role in the pathogenesis of MHV-3-induced hepatitis. In the present study we have shown that MHV-3 infection of macrophages induces these cells to undergo apoptosis. Three methods to detect apoptosis were applied: flow cytometry analysis of nuclear DNA content, fluorescence microscopic visualization of apoptotic cells labeled by the TUNEL assay, and gel electrophoresis to detect DNA laddering. Apoptosis in A/J and BALB/c macrophages was first detected at 8 h postinfection (p.i.) and reached a maximum by 12 h p.i. The degree of MHV-3-induced apoptosis was much greater in A/J-derived macrophages than in BALB/c-derived cells. Apoptosis was inversely correlated with the development of typical MHV cytopathology, namely syncytia formation. Infected macrophages from A/J mice did not form synctia in contrast to the extensive synctia formation observed in BALB/c- derived macrophages. In MHV-3-infected BALB/c macrophage cultures, apoptotic cells were not incorporated into syncytia. Apoptosis was also inversely correlated with the expression of MHV-3-induced fgl2 prothrombinase in macrophages. These results add the murine coronavirus MHV-3 to the list of RNA-containing viruses capable of inducing apoptosis.",,"blood clotting factor 10a; animal cell; apoptosis; article; controlled study; Coronavirus; cytopathology; flow cytometry; macrophage; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; virus pathogenesis; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Antoni, B., Sabbatini, P., Rabson, A., White, E., Inhibition of apoptosis in human immunodeficiency virus-infected cells enhances virus production and facilitates persistent infection (1995) J. Virol., 69, pp. 2384-2392; Bang, F.B., Warwick, A., Mouse macrophages as host cells for the mouse hepatitis virus and the genetic basis of their susceptibility (1960) Proc. Natl. Acad. Sci. 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Virol., 71, pp. 1992-2003; Kulomaa, P., Paavonen, J., Lehtinen, M., Herpes simplex virus induces unscheduled DNA synthesis in virus-infected cervical cancer cell lines (1992) Res. Virol., 143, pp. 351-359; Lee, E., Hu, N., Yuan, S., Cox, L., Bradley, A., Herrup, K., Dual roles of the retinoblastoma protein in cell cycle regulation and neuron differentiation (1994) Genes Dev., 8, pp. 2008-2021; Leibowitz, J.L., Devries, J.R., Rodriguez, M., Increased hepatotropism of mutants of MHV, strain JHM, selected with monoclonal antibodies (1987) Adv. Exp. Med. Biol., 218, pp. 321-331; Levine, B., Goldman, J., Jiang, H., Griffin, D., Hardwick, J., Bcl-2 protects mice against fatal alphavirus encephalitis (1996) Proc. Natl. Acad. Sci. 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Med., 176, pp. 689-697; Lin, K.I., Lee, S., Narayanan, R., Baraban, J., Hardwick, J., Ratan, R., Thiol agents and Bcl-2 identify an alphavirus-induced apoptotic pathway that requires activation of the transcription factor NF-kappaB (1995) J. Cell Biol., 131, pp. 1149-1161; MacNaughton, M., Patterson, S., Mouse hepatitis virus strain 3 infection of C57, A/Sn and A/J strain mice and their macrophages (1980) Arch. Virol., 66, pp. 71-75; MacPhee, P., Dindzans, V., Fung, L., Levy, G., Acute and chronic changes in the microcirculation of the liver in inbred strain of mice following infection with mouse hepatitis virus type 3 (1985) Hepatology, 5, pp. 649-660; Nurse, P., Ordering S phase and M phase in the cell cycle (1994) Cell, 79, pp. 547-550; Parr, R.L., Fung, L.S., Reneker, S.J., Myers-Mason, N., Leibowitz, J.L., Levy, G.A., The association of mouse fibrinogen-like protein (musfiblp) with murine hepatitis virus induced prothrombinase activity (1995) J. Virol., 69, pp. 5033-5038; Pekosz, A., Phillips, J., Pleasure, D., Merry, D., Gonzalez-Scarano, F., Induction of apoptosis by La Crosse virus infection and role of neuronal differentiation and human bcl-2 expression in its prevention (1996) J. Virol., 70, pp. 5329-5335; Piazza, M., (1969) Experimental Viral Hepatitis, , Springfield: CA Thomas; Pope, M., Rotstein, O., Cole, E., Sinclair, S., Parr, R., Cruz, B., Gorczynski, R., Levy, G., Pattern of disease after murine hepatitis virus strain 3 infection correlates with macrophage activation and not viral replication (1995) J. Virol., 69, pp. 5252-5260; Prikhod'Ko, E., Miller, L., Induction of apoptosis by baculovirus transactivator IE1 (1996) J. Virol., 70, pp. 7116-7124; Rao, L., Debbas, M., Sabbatini, P., Hockenbery, D., White, E., The adenovirus E1A proteins induce apoptosis, which is inhibited by the E1B 19-kDa and Bcl-2 proteins (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 7742-7746; Ray, C., Black, R., Kronheim, S., Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme (1992) Cell, 69, pp. 597-604; Schang, L., Hossain, A., Jones, C., The latency-related gene of bovine herpesvirus 1 encodes a product which inhibits cell cycle progression (1996) J. Virol., 70, pp. 3807-3814; Schutte, B., Reynders, M., Van Assche, C.L.M., Hupperets, P.S.G.J., Bosman, F.T., Blijham, G.H., An improved method for the immunocytochemical detection of bromodeoxyuridine labeled nuclei using flow cytometry (1987) Cytometry, 8, pp. 372-376; Shen, Y., Shenk, T., Viruses and apoptosis (1995) Curr. Opin. Genet. Dev., 1995, pp. 105-111; Sherr, C., Mammalian G1 cyclins (1993) Cell, 73, pp. 1059-1065; Suarez, P., Diaz-Guerra, M., Prieto, C., Esteban, M., Castro, J., Nieto, A., Ortin, J., Open reading frame 5 of porcine reproductive and respiratory syndrome virus as a cause of virus-induced apoptosis (1996) J. Virol., 70, pp. 2876-2882; Takizawa, T., Matsukawa, S., Higuchi, Y., Nakamura, S., Nakanishi, Y., Fukuda, R., Induction of programmed cells death (apoptosis) by influenza virus infection in tissue culture cells (1993) J. Gen. Virol., 74, pp. 2347-2355; Teodoro, J., Branton, P., Regulation of apoptosis by viral gene products (1997) J. Virol., 71, pp. 1739-1746; Tolskaya, E., Romanova, L., Kolesnikova, M., Ivannikova, T., Smirnova, E., Agol, V., Apoptosis-inducing and apoptosis preventing function of poliovirus (1995) J. Virol., 69, pp. 1181-1189; Tolskaya, E., Romanova, L., Kolesnikova, M., Ivannikova, T., Smirnova, E., Raikhlin, N., Agol, V., Apoptosis-inducing and apoptosis-preventing functions of poliovirus (1995) J. Virol., 69, pp. 1181-1189; Tyler, K.L., Squier, M., Rodgers, S., Schneider, B., Oberhaus, S., Grdina, T., Cohen, J., Dermody, T., Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein sigma 1 (1995) J. Virol., 69, pp. 6972-6979; Ubol, S., Park, S., Budihardjo, I., Desnoyers, S., Montrose, M., Poirier, G., Kaufmann, S., Griffin, D., Temporal changes in chromatin, intracellular calcium, and poly(ADP-Ribose) polymerase during sindbis virus-induced apoptosis in neuroblastoma cells (1996) J. Virol., 70, pp. 2215-2220; Virelizier, J.-L., Allison, A.C., Correlation of persistent mouse hepatitis virus (MHV-3) infection with its effect on mouse macrophage cultures (1976) Arch. Virol., 50, pp. 279-285; Wyllie, A.H., Kerr, J.F.R., Currie, A.R., Cell death: The significance of apoptosis (1980) Int. Rev. Cytol., 68, pp. 251-306; Wilhelmsen, K.C., Leibowitz, J.L., Bond, C.W., Robb, J.A., The replication of murine coronaviruses in enucleate cells (1981) Virology, 110, pp. 225-230; Yuan, J., Molecular control of life and death (1995) Curr. Opin. Cell Biol., 7, pp. 211-214","Leibowitz, J.L.; Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Coll. of Med., 208 Reynolds Medical Building, College Station, TX 77843-1114, United States; email: jleibowitz@tamu.edu",,"Academic Press Inc.",00426822,,VIRLA,"9770418","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0032505544
"Kipar A., Bellmann S., Kremendahl J., Köhler K., Reinacher M.","7004576445;6603322735;6507138764;9747682900;7003284148;","Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis",1998,"Veterinary Immunology and Immunopathology","65","2-4",,"243","257",,86,"10.1016/S0165-2427(98)00158-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032561431&doi=10.1016%2fS0165-2427%2898%2900158-5&partnerID=40&md5=bdd2abfd8898e9f8ba882b282a5996b8","Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany","Kipar, A., Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany; Bellmann, S., Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany; Kremendahl, J., Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany; Köhler, K., Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany; Reinacher, M., Inst. für Vet.-Pathologie, Univ. Leipzig, Margarete Blank S., 04103 Leipzig, Germany","Twenty-three cats with spontaneous feline infectious peritonitis (FIP) were examined by light microscopy including immunohistology and histochemistry in order to determine the cellular composition and the expression of viral antigen in lesions in FIP. Furthermore, the presence of plasma-cells producing coronavirus-specific antibodies was evaluated in situ. Macrophages and neutrophils were demonstrated by an antibody against calprotectin (leukocyte protein L1, myeloid/ histiocyte antigen), neutrophils were recognized due to their chloroacetate esterase activity, and Band T- lymphocytes were identified by antibodies against the CD3 antigen and the CD45R antigen, respectively. Expression of viral antigen was immunohistologically demonstrated by a monoclonal antibody (mAb) against coronavirus while coronavirus-specific antibodies in situ were identified by the application of feline coronavirus prior to the coronavirus antibody. Lesions were classified as diffuse alterations at serosal surfaces, granulomas with areas of necrosis, granulomas without extended necrosis, focal and perivascular lymphoplasmocytic infiltrates, and granulomatousnecrotizing vasculitis. Diffuse alterations on serosal surfaces were represented either by activated mesothelial cells with single coronavirus antigen-bearing macrophages or by layers of precipitated exudate containing single to numerous granulomas with areas of necrosis. In liver and spleen, the exudate was often underlaid by a small band of subcapsular B- cells with an occasional plasma-cell producing coronavirus-specific antibodies. In other locations, a variably broad band of B-cells and plasma- cells, often infiltrating between underlying muscle fibers, separated the exudate from the unaltered tissue. Some of these plasma-cells were positive for coronavirus-specific antibodies. In granulomas with areas of necrosis, the central necrosis was surrounded by macrophages usually expressing considerable amounts of viral antigen. Few B-cells and plasma-cells were found in the periphery. In granulomas without extended necrosis, the number of macrophages were lower. Only few macrophages expressing low amounts of viral antigen were present. B-cells and plasma-cells formed a broad rim. Few plasma-cells stained positive for coronavirus-specific antibodies. In both types of granulomas, few neutrophils were found between macrophages. Few T- cells were seen scattered throughout the lesions. Focal and perivascular lymphoplasmocytic infiltrates were mainly seen in omentum and leptomeninx. B- cells were the predominant cells; some plasma-cells were positive for coronavirus-specific antibodies. Viral antigen was not readily detected in these alterations. Granulomatous-necrotizing vasculitis was occasionally found in kidneys and leptomeninx. It was dominated by macrophages which often stained strongly positive for coronavirus antigen. Different types of alteration were often seen in the same animal and even the same tissue. There was no obvious correlation between the cat's age, gross pathological changes, and the histological types of alteration. Single plasma-cells positive for coronavirus-specific antibodies were found around blood vessels distant from inflammatory alterations, within the lung parenchyma, as infiltrating cells in the mucosa of the small intestine, and in spleen and mesenteric lymph node. Results show that alterations in FIP are heterogeneous concerning cellular composition and expression of viral antigen. The dominance of B- cells in part of the lesions together with the presence of plasma-cells positive for coronavirus-specific antibodies indicate that these cells may play a role in the maintenance of inflammatory processes in FIP.","B-cells; Coronavirus antigen; Coronavirus-specific antibodies; Feline infectious peritonitis; Immunohistology; Plasma-cells","chloroacetic acid; esterase; monoclonal antibody; virus antibody; virus antigen; animal cell; animal experiment; animal model; animal tissue; antibody production; b lymphocyte; cat disease; cell composition; conference paper; controlled study; coronavirus; granuloma; liver; macrophage; necrotizing arteritis; neutrophil; nonhuman; plasma cell; spleen; t lymphocyte; Animals; Antibodies, Viral; Antibody Formation; Antigens, Viral; B-Lymphocytes; Cats; Feline Infectious Peritonitis; Female; Immunity, Cellular; Immunodeficiency Virus, Feline; Immunoenzyme Techniques; Leukocytes; Macrophages; Male; Neutrophils; T-Lymphocytes","Beebe, A.M., Dua, N., Faith, T.G., Moore, P.F., Pedersen, N.C., Dandekar, S., Primary stage of feline immunodeficiency virus infection: Viral dissemination and cellular targets (1994) J. Virol., 68, pp. 3080-3091; Cotter, S.M., Hardy W.D., Jr., Essex, M., Association of feline leukemia virus with lymphosarcoma and other disorders in the cat (1975) J. Am. Vet. Med. Assoc., 166, pp. 449-454; Dale, I., Fagerhol, M.K., Naesgard, I., Purification and partial characterization of highly immunogenic human leukocyte protein, the L1 antigen (1983) Eur. J. Biochem., 134, pp. 1-6; Domingo, M., Reinacher, M., Burkhardt, E., Weiss, E., Monoclonal antibodies directed towards the two major cell populations in the Bursa of Fabricius of the chicken (1986) Vet. Immunol. Immunopathol., 11, pp. 305-317; Evermann, J.F., McKeirnan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Vet. Microbiol., 28, pp. 243-255; Flavell, D.J., Jones, D.B., Wright, D.H., Identification of tissue histiocytes on paraffin sections by a new monoclonal antibody (1987) J. Histochem. Cytochem., 35, pp. 1217-1226; Goitsuka, R., Hirota, Y., Hasegawa, A., Tomoda, I., Release of interleukin-1 from peritoneal exudate cells of cats with feline infectious peritonitis (1987) J. Vet. Med. Sci., 49, pp. 811-818; Goitsuka, R., Onda, C., Hirota, Y., Hasegawa, A., Tomoda, I., Feline interleukin-1 production induced by feline infectious peritonitis virus (1988) Jpn. J. Vet. Sci., 50, pp. 209-214; Goitsuka, R., Ohashi, T., Ono, K., Yasukawa, K., Koishibara, Y., Fukui, H., Ohsugi, Y., Hasegawa, A., IL-6 activity in feline infectious peritonitis (1990) J. Immunol., 144, pp. 2599-2603; Haagmans, B.T., Egberink, H.F., Horzinek, M.C., Apoptosis and T-cell depletion during feline infectious peritonitis (1996) J. Virol., 70, pp. 8977-8983; Hasegawa, T., Hasegawa, A., Interleukin-1 alpha mRNA-expressing cells on the local inflammatory response in feline infectious peritonitis (1991) J. Vet. Med. Sci., 53, pp. 995-999; Hayashi, T., Goto, N., Takahashi, R., Fujiwara, K., Systemic vascular lesions in feline infectious peritonitis (1977) Jpn. J. Vet. Sci., 39, pp. 365-377; Hayashi, T., Goto, N., Takahashi, R., Fujiwara, K., Detection of coronavirus-like particles in a spontaneous case of feline infectious peritonitis (1978) Jpn. J. Vet. Sci., 40, pp. 207-212; Hayashi, T., Utsumi, F., Takahashi, R., Fujiwara, K., Pathology of non-effusive type feline infectious peritonitis and experimental transmission (1980) Jpn. J. Vet. Sci., 42, pp. 197-210; Hsu, S.M., Raine, L., Fanger, H., Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques (1981) J. Histochem. Cytochem., 29, pp. 577-580; Jacobse-Geels, H.E.L., Horzinek, M.C., Expression of feline infectious peritonitis coronavirus antigens on the surface of macrophage-like cells (1983) J. Gen. Virol., 64, pp. 1859-1866; Kishimoto, T., The biology of interleukin-6 (1989) Blood, 74, pp. 1-10; Kovacevic, S., Kipar, A., Kremendahl, J., Teebken-Schuler, D., Grant, C.K., Reinacher, M., Immunohistochemical diagnosis of feline leukemia virus infection in formalin-fixed tissue (1997) Eur. J. Vet. Pathol., 3, pp. 13-19; Montali, R.J., Strandberg, J.D., Extraperitoneal lesions in feline infectious peritonitis (1972) Vet. Path., 9, pp. 109-121; Monteith, C.E., Chelack, B., Davis, W., Haines, D.M., Identification of monoclonal antibodies for immunohistochemical staining of feline B-lymphocytes in frozen and formalin-fixed paraffin-embedded tissues (1996) Can. J. Vet. Res., 60, pp. 193-198; Osbaldiston, G.W., Sullivan, R.J., Fox, A., Cytochemical demonstration of esterases in peripheral blood leukocytes (1978) Am. J. Vet. Res., 39, pp. 683-685; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Reinacher, M., Diseases associated with spontaneous feline leukemia virus (FeLV) infection in cats (1989) Vet. Immunol. Immunopathol., 21, pp. 85-89; Schaefer, H.E., Histology and histochemistry in paraffin sections (1983) Verh. Dtsch. Ges. Path., 67, pp. 6-7; Sternberger, L.A., Hardy P.H., Jr., Cuculis, C.C., Meyer, H.G., The unlabeled antibody-enzyme method for immunohistochemistry. Preparation and properties of soluble antigen-antibody-complex (Horseradish peroxidase-antihorseradish peroxidase) and its use in identification of spirochetes (1971) J. Histochem. Cytochem., 18, pp. 315-333; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Pearson, G.R., The sites of early viral replication in feline infectious peritonitis (1988) Vet. Microbiol., 18, pp. 259-271; Tammer, R., Evensen, O., Lutz, H., Reinacher, M., Immunohistological demonstration of feline infectious peritonitis virus antigen in paraffin-embedded tissues using feline ascites or murine monoclonal antibodies (1995) Vet. Immunol. Immunopathol., 49, pp. 177-182; Ward, J.M., Gribble, D.H., Dungworth, D.L., Feline infectious peritonitis: Experimental evidence for its multiphasic nature (1974) Am. J. Vet. Res., 35, pp. 1271-1275; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Nature and development of viremia (1981) Am. J. Vet. Res., 42, pp. 382-390; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Pathologic changes and immunofluorescence (1981) Am. J. Vet. Res., 42, pp. 2036-2048; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: Comparisons with dengue hemorrhagic fever (1981) Comp. Immun. Microbiol. Infect. Dis., 4, pp. 175-189; Weiss, R.C., Feline infectious peritonitis and other coronaviruses (1994) The Cat: Diseases and Clinical Management, 2nd Edn., 1, pp. 453-455. , In: Sherding, R.G. (Ed.), Churchill Livingstone, New York; Wolfe, L.G., Griesemer, R.A., Feline infectious peritonitis (1966) Path. Vet., 3, pp. 255-270; Zook, B.C., King, N.W., Robison, R.L., McCombs, H.L., Ultrastructural evidence for the viral etiology of feline infectious peritonitis (1968) Path. Vet., 5, pp. 91-95","Kipar, A.; Institut fur Veterinar-Pathologie, Universitat Leipzig, Margarete Blank Strasse 4, 04103 Leipzig, Germany; email: kipar@rz.uni-leipzig.de",,,01652427,,VIIMD,"9839877","English","Vet. Immunol. Immunopathol.",Conference Paper,"Final",Open Access,Scopus,2-s2.0-0032561431
"Hofmann-Lehmann R., Berger M., Sigrist B., Schawalder P., Lutz H.","7003867023;7404267807;6602227168;7004155368;57202819852;","Feline immunodeficiency virus (FIV) infection leads to increased incidence of feline odontoclastic resorptive lesions (FORL)",1998,"Veterinary Immunology and Immunopathology","65","2-4",,"299","308",,25,"10.1016/S0165-2427(98)00163-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032561145&doi=10.1016%2fS0165-2427%2898%2900163-9&partnerID=40&md5=07c88b7269f7bfa15a0332b9bccd7cc2","Clinical Laboratory, Dept. Int. Vet. Med., Fac. Vet. M., CH-8057, Zurich, Switzerland; Department of Surgery, Orthopedics Stomatology Clin. S., Bern, Switzerland","Hofmann-Lehmann, R., Clinical Laboratory, Dept. Int. Vet. Med., Fac. Vet. M., CH-8057, Zurich, Switzerland; Berger, M., Department of Surgery, Orthopedics Stomatology Clin. S., Bern, Switzerland; Sigrist, B., Clinical Laboratory, Dept. Int. Vet. Med., Fac. Vet. M., CH-8057, Zurich, Switzerland; Schawalder, P., Department of Surgery, Orthopedics Stomatology Clin. S., Bern, Switzerland; Lutz, H., Clinical Laboratory, Dept. Int. Vet. Med., Fac. Vet. M., CH-8057, Zurich, Switzerland","Feline odontoclastic resorptive lesions (FORL), previously known as 'neck lesions,' are commonly known in domestic, but also in non-domestic cats. They are characterized by odontoclastic resorptive processes, which take place at the dental root and at the periodontium. Chronic inflammation of gingiva and periodontium is believed to be an important etiological factor in the development of FORL. In this context, various feline viruses have been discussed to play a relevant role in the pathogenesis of these lesions. The aim of this project was to determine in a blinded study the incidence of FORL in 10 cats which were infected for several years with feline immunodeficiency virus (FIV), but were otherwise free of feline viral infections (feline leukemia virus, feline calicivirus, feline herpesvirus, feline parvovirus, feline coronavirus, feline syncytium-forming virus). Nine age-matched controls were kept under identical conditions, but free of FIV. Subgingival resorptive lesions were found in six of 10 FIV-positive cats, but in three of nine controls only. FIV-positive cats had significantly more often gingivae with an increased tendency for bleeding upon probing than FIV-negative cats (p=0.0055), and they had slightly more often hyperplastic gingivae (p=0.0867). in conclusion, signs characteristic of FORL such as subgingival lesions, granulomatous or hyperplastic gingivae with a tendency for bleeding, were found significantly more often in FIV-positive cats than in the controls (p=0.0198). Therefore, it was concluded that FIV infection is an important factor for the occurrence of FORL, possibly through immune suppression or changes of the (sub)gingival micro-environment. However, non-infected control cats also showed some evidence of FORL in the absence of all tested viral infections. Therefore, factors other than viral infections must also play a role in the development of FORL in cats.","Cats; Feline immunodeficiency virus (FIV); Feline odontoclastic resorptive lesions (FORL); Feline viruses; Neck lesions","animal experiment; animal model; cat; conference paper; controlled study; feline immunodeficiency virus; gingiva bleeding; gingiva hyperplasia; gingivitis; incidence; nonhuman; periodontal disease; virus infection; Animals; Antibodies, Viral; Cat Diseases; Cats; CD4-CD8 Ratio; CD4-Positive T-Lymphocytes; CD8-Positive T-Lymphocytes; Enzyme-Linked Immunosorbent Assay; Feline Acquired Immunodeficiency Syndrome; Immunodeficiency Virus, Feline; Incidence; Risk Factors; Root Resorption; Specific Pathogen-Free Organisms; Stomatognathic Diseases","Barlough, J.E., Ackley, C.D., George, J.W., Levy, N., Acevedo, R., Moore, P.F., Rideout, B.A., Pedersen, N.C., Acquired immune dysfunction in cats with experimentally induced feline immunodeficiency virus infection: Comparison of short-term and long-term infections (1991) J. Acquir. Immune. Defic. Syndr., 4, pp. 219-227; Berger, M., Schawalder, P., Stich, H., Lussi, A., Neck Lesion bei Grosskatzen; Untersuchungen beim Leoparden (Panthera pardus) (1995) Kleintierpraxis, 40, pp. 537-549; Berger, M., Schawalder, P., Stich, H., Lussi, A., Feline dental resorptive lesions in captive and wild leopards and lions (1996) J. Vet. Dent., 13, pp. 13-21; Berger, M., Schawalder, P., Stich, H., Lussi, A., Differentialdiagnose von resorptiven Zahnerkrankungen (FORL) und Karies (1996) Schweiz. Arch. Tierheilkd., 138, pp. 546-551; Calzolari, M., Young, E., Cox, D., Davis, D., Lutz, H., Serological diagnosis of feline immundeficiency virus infection using recombinant transmembrane glycoprotein (1995) Vet. Immunol. Immunopathol., 46, pp. 83-92; Coles, S., The prevalence of buccal cervical root resorptions in Australian cats (1990) J. Vet. Dent., 7, pp. 14-16; Diehl, K., Rosychuk, R.A.W., Feline gingivitis-stomatitis-pharyngitis (1993) Vet. Clin. North Am. Small Anim. Pract., 23, pp. 139-153; Harvey, C.E., Feline dental resorptive lesions (1993) Semin. Vet. Med. Surg. (Small. Anim), 8, pp. 187-196; Harvey, C.E., Feline oral pathology, diagnosis and management (1995) Manual of Small Animal Dentistry, pp. 129-138. , BSAVA; Harvey, C.E., Flax, B.M., Feline oral-dental radiographic examination and interpretation (1992) Vet. Clin. North Am. Small Anim. Pract., 22, pp. 1279-1295; Hofmann-Lehmann, R., Fehr, D., Grob, M., Elgizoli, M., Packer, C., Martenson, J.S., O'Brien, S.J., Lutz, H., Prevalence of antibodies to feline parvovirus, calicivirus, herpesvirus, coronavirus and immunodeficiency virus and of feline leukemia virus antigen and the interrelationship of these viral infections in free-ranging lions in East Africa (1996) Clin. Diagn. Lab. Immunol., 3, pp. 554-562; Hofmann-Lehmann, R., Holznagel, E., Ossent, P., Lutz, H., Parameters of disease progression in long-term experimental feline retrovirus (feline immunodeficiency virus and feline leukemia virus) infections: Hematology, clinical chemistry and lymphocyte subsets (1997) Clin. Diagn. Lab. Immunol., 4, pp. 33-42; Ishida, T., Tomoda, I., Clinical staging of feline immunodeficiency virus infection (1990) Jpn. J. Vet. Sci., 52, pp. 645-648; Knowles, J.O., Gaskell, R.M., Gaskell, C.J., Harvey, C.E., Lutz, H., Prevalence of feline calicivirus, feline leukaemia virus and antibodies to FIV in cats with chronic stomatitis (1989) Vet. Rec., 124, pp. 336-338; Kölbl, S., Lutz, H., Die Infektion mit felinem Spumavirus (FeSFV): Häufigkeit bei Katzen in Oesterreich und Beziehung zur Infektion mit dem felinen Immunschwächevirus (FIV) (1992) Kleintierpraxis, 37, pp. 307-318; Lehmann, R., Franchini, M., Aubert, A., Wolfensberger, C., Cronier, J., Lutz, H., Vaccination of cats experimentally infected with feline immunodeficiency virus, using a recombinant feline leukemia virus vaccine (1991) J. Am. Vet. Med. Assoc., 199, pp. 1446-1452; Lutz, H., Pedersen, N.C., Durbin, R., Theilen, G.H., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) J. Immunol. Methods, 56, pp. 209-220; Lutz, H., Arnold, P., Hubscher, U., Egberink, H., Pedersen, N., Horzinek, M.C., Specificity assessment of feline T-lymphotropic lentivirus serology (1988) Zentralbl. Veterinarmed. B, 35, pp. 773-778; Lyon, K.F., Subgingival odontoclastic resorptive lesions: Classification, treatment, and results in 58 cats (1992) Vet. Clin. North Am. Small Anim. Pract., 22, pp. 1415-1432; Morikawa, S., Lutz, H., Aubert, A., Bishop, D.H., Identification of conserved and variable regions in the envelope glycoprotein sequences of two feline immunodeficiency viruses isolated in Zurich (1991) Switzerland. Virus Res., 21, pp. 53-63; Okuda, A., Harvey, C.E., Etiopathogenesis of feline dental resorptive lesions (1992) Vet. Clin. North Am. Small Anim. Pract., 22, pp. 1385-1404; Okuda, A., Harvey, C.E., Immunohistochemical distributions of interleukins as possible stimulators of odontoclastic resorption activity in feline dental resorptive lesions (1992) Proc. Vet. Dent. Forum, 6, pp. 41-43; Osterhaus, A.D., Horzinek, M.C., Reynolds, D.J., Seroepidemiology of feline infectious peritonitis virus infections using transmissible gastroenteritis virus as antigen (1977) Zentralbl. Veterinarmed. B, 24, pp. 835-841; Pedersen, N.C., Inflammatory oral cavity diseases of the cat (1992) Vet. Clin. North Am. Small Anim. Pract., 22, pp. 1323-1345; Pedersen, N.C., Barlough, J.E., Clinical overview of feline immunodeficiency virus (1991) J. Am. Vet. Med. Assoc., 199, pp. 1298-1305; Pedersen, N.C., Ho, E.W., Brown, M.L., Yamamoto, J.K., Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome (1987) Science, 235, pp. 790-793; Schneck, G.W., Osborn, J.W., Neck lesions in the teeth of cats (1976) Vet. Rec., 99, p. 100; Shelton, G.H., Linenberger, M.L., Persik, M.T., Abkowitz, J.L., Prospective hematologic and clinicopathological study of asymptomatic cats with naturally acquired feline immunodeficiency virus infection (1995) J. Vet. Intern. Med., 9, pp. 133-140; Sparger, E.E., Luciw, P.A., Elder, J.H., Yamamoto, J.K., Lowenstine, L.J., Pedersen, N.C., Feline immunodeficiency virus is a lentivirus associated with an AIDS-like disease in cats (1989) AIDS, 3, pp. 43-49; Tenorio, A.P., Franti, C.E., Madewell, B.R., Pedersen, N.C., Chronic oral infections of cats and their relationship to persistent oral carriage of feline calici-, immunodeficiency, or leukemia viruses (1991) Vet. Immunol. Immunopathol., 29, pp. 1-14; Torten, M., Franchini, M., Barlough, J.E., George, J.W., Mozes, E., Lutz, H., Pedersen, N.C., Progressive immune dysfunction in cats experimentally infected with feline immunodeficiency virus (1991) J. Virol., 65, pp. 2225-2230; Van Wessum, R., Harvey, C.E., Hennet, P., Feline dental resorptive lesions. Prevalence patterns (1992) Vet. Clin. North Am. Small Anim. Pract., 22, pp. 1405-1416; Von Schlup, D., Epidemiologische und morphologische Untersuchungen am Katzengebiss I. Mitteilung: Epidemiologische Untersuchungen (1982) Kleintierpraxis, 27, pp. 87-94; Von Schlup, D., Stich, H., Epidemiologische und morphologische Untersuchungen am Katzengebiss. II Mitteilung: Morphologische Untersuchungen der neck lesions (1982) Kleintierpraxis, 27, pp. 179-188; Williams, C.A., Aller, M.S., Gingivitis/stomatitis in cats (1992) Vet. Clin. North Am Small Anim. Pract., 22, pp. 1361-1383; Yamamoto, J.K., Hansen, H., Ho, E.W., Morishita, T.Y., Okuda, T., Sawa, T.R., Nakamura, R.M., Pedersen, N.C., Epidemiologic and clinical aspects of feline immunodeficiency virus isolation in cats from the continental United States and Canada and possible mode of transmission (1989) J. Am. Vet. Med. Assoc., 194, pp. 213-220; Zetner, K., Neck Lesions bei der Katze: Diagnostisch-aetiologische Untersuchungen über Zusammenhänge zwischen Röntgenbefund und Fütterung (1990) Waltham Report, 30, pp. 15-23; Zetner, K., The influence of dry food and the development of feline neck lesions (1992) J. Vet. Dent., 9, pp. 4-6","Lutz, H.; Dept. Internal Veterinary Medicine, Faculty of Veterinary Medicine, University of Zurich, Wintherthurerstrasse, 260, CH-8057 Zurich, Switzerland; email: hanslutz@vetktinik.unizh.ch",,,01652427,,VIIMD,"9839881","English","Vet. Immunol. Immunopathol.",Conference Paper,"Final",,Scopus,2-s2.0-0032561145
"Baudoux P., Carrat C., Besnardeau L., Charley B., Laude H.","57199559554;6603249904;6602382869;55246691600;7006652624;","Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes",1998,"Journal of Virology","72","11",,"8636","8643",,117,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031713686&partnerID=40&md5=0d04b20361877c9ea60d346cebf6a27a","U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France","Baudoux, P., U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France; Carrat, C., U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France; Besnardeau, L., U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France; Charley, B., U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France; Laude, H., U. Virologie Immunol. Moleculaires, INRA, 78350 Jouy-en-Josas, France","Transmissible gastroenteritis virus (TGEV), an enteric coronavirus of swine, is a potent inducer of alpha interferon (IFN-α) both in vivo and in vitro. Incubation of peripheral blood mononuclear cells with noninfectious vital material such as inactivated virions or fixed, infected cells leads to early and strong IFN-α synthesis. Previous studies have shown that antibodies against the virus membrane glycoprotein M blocked the IFN induction and that two viruses with a mutated protein exhibited a decreased interferogenic activity, thus arguing for a direct involvement of M protein in this phenomenon. In this study, the IFN-α-inducing activity of recombinant M protein expressed in the absence or presence of other TGEV structural proteins was examined. Fixed cells coexpressing M together with at least the minor structural protein E were found to induce IFN-α almost as efficiently as TGEV-infected cells. Pseudoparticles resembling authentic virions were released in the culture medium of cells coexpressing M and E proteins. The interferogenic activity of purified pseudoparticles was shown to be comparable to that of TGEV virions, thus establishing that neither ribonucleoprotein nor spikes are required for IFN induction. The replacement of the externally exposed, N-terminal domain of M with that of bovine coronavirus (BCV) led to the production of chimeric particles with no major change in interferogenicity, although the structures of the TGEV and BCV ectodomains markedly differ. Moreover, BCV pseudoparticles also exhibited interferogenic activity. Together these observations suggest that the ability of coronavirus particles to induce IFN-α is more likely to involve a specific, multimeric structure than a definite sequence motif.",,"alpha interferon; e protein; m protein; mutant protein; recombinant protein; ribonucleoprotein; unclassified drug; virus protein; animal cell; article; coronavirus; human; human cell; interferon induction; mononuclear cell; nonhuman; priority journal; protein domain; protein expression; swine; swine disease; virus gene; virus particle; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus, Bovine; DNA Primers; Humans; Interferon-alpha; Leukocytes; Microscopy, Electron; Molecular Sequence Data; Mutation; Recombinant Fusion Proteins; Swine; Transmissible gastroenteritis virus; Viral Matrix Proteins; Viral Proteins","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential non-structural proteins of 4.9, 4.8, 12.7 and 9.5 kDa encoded between the spike and membrane protein genes of bovine coronavirus (1990) Virology, 177, pp. 488-495; Ankel, H., Capobianchi, M.R., Castiletti, C., Dianzani, F., Interferon induction by HIV glycoprotein 120: Role of the V3 loop (1994) Virology, 205, pp. 34-43; Baudoux, P., (1996), Ph. 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Virol., 62, pp. 8-11; Charley, B., Lavenant, L., Delmas, B., Glycosylation is required for coronavirus TGEV to induce an efficient production of IFNα by blood mononuclear cells (1991) Scand. J. Immunol., 33, pp. 435-440; De Arce, H.D., Artursson, K., L'Haridon, R., Perers, A., La Bonnardière, C., Aim, G.V., A sensitive immunoassay for porcine interferon-α (1992) Vet. Immunol. Immunopathol., 30, pp. 319-327; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., Laude, H., Aminopeptidase is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature (London), 357, pp. 417-1120; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. 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Immunol., 44, pp. 164-172; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Vorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Vennema, H., Rottier, P.J.M., Unpublished data; Woloszyn, N., Boireau, P., Laporte, J., Nucleotide sequence of the bovine enteric coronavirus F15 mRNA 5 and mRNA 6 unique regions (1990) Nucleic Acids Res., 18, p. 1303; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zinkernagel, R.M., Immunology taught by viruses (1996) Science, 271, pp. 173-178","Laude, H.; Unite Virologic Immunol. Molecul., INRA, 78350 Jouy-en-Josas, France; email: laude@biotec.jouy.inra.fr",,,0022538X,,JOVIA,"9765403","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031713686
"An S., Maeda A., Makino S.","55107136200;7201779383;7403067550;","Coronavirus transcription early in infection",1998,"Journal of Virology","72","11",,"8517","8524",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031660971&partnerID=40&md5=2ad6b6eddeeb48a5f56036b96322f52d","Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States","An, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Maeda, A., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States","We studied the accumulation kinetics of murine coronavirus mouse hepatitis virus (MHV) RNAs early in infection by using cloned MHV defective interfering (DI) RNA that contained an intergenic sequence from which subgenomic DI RNA is synthesized in MHV-infected cells. Genomic DI RNA and subgenomic DI RNA accumulated at a constant ratio from 3 to 11 h postinfection (p.i.) in the cells infected with MHV-containing DI particles. Earlier, at 1 h p.i., this ratio was not constant; only genomic DI RNA accumulated, indicating that MHV RNA replication, but not MHV RNA transcription, was active during the first hour of MHV infection. Negative- strand genomic DI RNA and negative-strand subgenomic DI RNA were first detectable at 1 and 3 h p.i., respectively, and the amounts of both RNAs increased gradually until 6 h p.i. These data showed that at 2 h p.i., subgenomic DI RNA was undergoing synthesis in the cells in which negative- strand subgenomic DI RNA was undetectable. These data, therefore, signify that negative-strand genomic DI RNA, but not negative-strand subgenomic DI RNA, was an active template for subgenomic DI RNA synthesis early in infection.",,"article; coronavirus; genetic transcription; murine hepatitis coronavirus; nonhuman; priority journal; rna replication; rna synthesis; rna transcription; virus infection; virus particle; Animals; Base Sequence; Cell Line; Coronavirus Infections; Defective Viruses; DNA, Viral; Genome, Viral; Kinetics; Mice; Molecular Sequence Data; Murine hepatitis virus; Oligodeoxyribonucleotides; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; RNA, Viral; Transcription, Genetic","An, S., Makino, S., Characterization of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency (1998) Virology, 243, pp. 198-207; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. 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Virol., 46, pp. 1027-1033; Leibowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114, pp. 39-51; Lin, Y.-J., Liao, C.-L., Lai, M.M.C., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implication for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Lu, X.T., Sims, A.C., Denison, M.R., Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro (1998) J. 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Virol., 69, pp. 4331-4338; Zinn, K., Dimaio, D., Maniatis, T., Identification of two distinct regulatory regions adjacent to the human beta-interferon gene (1983) Cell, 34, pp. 865-879","Makino, S.; Department of Microbiology, University of Texas at Austin, Austin, TX 78712-1095, United States; email: makino@mail.utexas.edu",,,0022538X,,JOVIA,"9765389","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031660971
"Kyuwa S., Tagawa Y.-I., Shibata S., Doi K., Machii K., Iwakura Y.","7006444820;35394959400;7402120346;57202414936;7005995877;7102119714;","Murine coronavirus-induced subacute fatal peritonitis in C57BL/6 mice deficient in gamma interferon",1998,"Journal of Virology","72","11",,"9286","9290",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031661793&partnerID=40&md5=78c7a1d6ba34e1c86988b27f7592782c","Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan; Laboratory Animal Research Center, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan; Laboratory of Veterinary Pathology, Faculty of Agriculture, University of Tokyo, Tokyo 113, Japan; Dept. of Veterinary Public Health, Institute of Public Health, Tokyo 108, Japan; Ctr. for Anim. Rsrc. and Development, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan","Kyuwa, S., Department of Animal Pathology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan, Ctr. for Anim. Rsrc. and Development, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan; Tagawa, Y.-I., Laboratory Animal Research Center, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan; Shibata, S., Laboratory of Veterinary Pathology, Faculty of Agriculture, University of Tokyo, Tokyo 113, Japan; Doi, K., Laboratory of Veterinary Pathology, Faculty of Agriculture, University of Tokyo, Tokyo 113, Japan; Machii, K., Dept. of Veterinary Public Health, Institute of Public Health, Tokyo 108, Japan; Iwakura, Y., Laboratory Animal Research Center, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan","Gamma interferon-deficient (IFN-γ-/-) mice with a C57BL/6 background were infected intraperitoneally with mouse hepatitis virus strain JHM (JHMV). In contrast to IFN-γ-+/- and IFN-γ+/+ mice, JHMV persisted in IFN-γ-/- mice and induced death during the subacute phase of the infection. Unexpectedly, infected IFN-γ-/- mice showed severe peritonitis accompanying the accumulation of a viscous fluid in the abdominal and thoracic cavities in the subacute phase. Destructive changes of hepatocytes were not observed. Administration of recombinant IFN-γ protracted the survival time of IFN-γ- /- mice after JHMV infection. These results demonstrate that IFN-γ plays a critical role in viral clearance in JHMV infection. They also show that a resultant persistent JHMV infection induces another form of disease in IFN- γ-/- mice, which bears a resemblance to feline infectious peritonitis in cats.",,"alanine aminotransferase; gamma interferon; recombinant gamma interferon; animal experiment; animal model; animal tissue; article; ascites fluid; cat disease; controlled study; death; disease simulation; fatality; female; intraperitoneal drug administration; mouse; murine hepatitis coronavirus; nonhuman; peritonitis; persistent virus infection; priority journal; survival time; thorax; Alanine Transaminase; Animals; Cats; Coronavirus Infections; Feline Infectious Peritonitis; Female; Immunity, Cellular; Interferon Type II; Interferon-gamma, Recombinant; Liver; Mice; Mice, Inbred C57BL; Mice, Knockout; Murine hepatitis virus; Peritonitis; T-Lymphocytes","Baumgarth, N., Kelso, A., In vivo blockade of gamma interferon affects the influenza virus-induced humoral and the local cellular immune response in lung tissue (1996) J. 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Virol., 68, pp. 7540-7545; Smith, A.L., Barthold, S.W., De Souza, M.S., Bottomly, K., The role of gamma interferon in infection of susceptible mice with murine coronavirus, MHV-JHM (1991) Arch. Virol., 121, pp. 89-100; Smyth, M.J., Trapani, J.A., The relative role of lymphocyte granule exocytosis versus death receptor-mediated cytotoxicity in viral pathophysiology (1998) J. Virol., 72, pp. 1-9; Stohlman, S.A., Frelinger, J.A., Resistance to fatal nervous system disease by mouse hepatitis virus, strain JHM. 1. Genetic analysis (1978) Immunogenetics, 6, pp. 277-281; Tagawa, Y., Sekikawa, K., Iwakura, Y., Suppression of concanavalin A-induced hepatitis in IFN-γ-/- mice, but not in TNF-α-/- mice (1997) J. Immunol., 159, pp. 1418-1428; Williamson, J.S.P., Stohlman, S.A., Effective clearance of mouse hepatitis virus from the central nervous system requires both CD4+ and CD8+ T cells (1990) J. Virol., 64, pp. 4589-4592; Yanagisawa, T., Nakanaga, K., Kyuwa, S., Fujiwara, K., Ascitic disease in nude mice infected with mouse hepatitis virus (1985) Jpn. J. Vet. Sci., 47, pp. 171-174; Yanagisawa, T., Nakanaga, K., Kyuwa, S., Fujiwara, K., Ascitic disease in ICR-nude mice due to mouse hepatitis virus (1986) Jpn. J. Vet. Sci., 48, pp. 7-14; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M.C., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338","Kyuwa, S.; Ctr. for Animal Resources and Devt., Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan; email: kyuwa@gpo.kumamoto-u.ac.jp",,,0022538X,,JOVIA,"9765476","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031661793
"Busato A., Lentze T., Hofer D., Burnens A., Hentrich B., Gaillard C.","7006678871;6508240532;57197588318;7006802781;6603659340;8236359900;","A Case Control Study of Potential Enteric Pathogens for Calves Raised in Cow-calf Herds",1998,"Journal of Veterinary Medicine, Series B","45","9",,"519","528",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032196654&partnerID=40&md5=aab4a2de3b0efac459761d2392b85b6d","Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland; Institute of Veterinary Bacteriology, Faculty of Veterinary Medicine, University of Berne, Längass-Strasse 122, CH-3012 Berne, Switzerland; Institute of Veterinary Parasitology, Faculty of Veterinary Medicine, University of Berne, Längass-Strasse 122, CH-3012 Berne, Switzerland; Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland","Busato, A., Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland; Lentze, T., Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland; Hofer, D., Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland; Burnens, A., Institute of Veterinary Bacteriology, Faculty of Veterinary Medicine, University of Berne, Längass-Strasse 122, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland; Hentrich, B., Institute of Veterinary Parasitology, Faculty of Veterinary Medicine, University of Berne, Längass-Strasse 122, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland; Gaillard, C., Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland, Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Berne, Switzerland","A matched case control study was performed to describe the epidemiological features of potential enteric pathogens for calves reared in 53 cow-calf herds located in western Switzerland. A total of 106 diarrhoeic calves and 126 healthy control calves were collected, all calves were less than 4 months old. Faecal samples were analysed for presence of infectious agents related to calf diarrhoea including enterotoxigenic E. coli, Verotoxin producing E. coli (VTEC), Campylobacter sp., Yersima sp., Salmonella sp., rotavirus, coronavirus., helminths and coccidian protozoa. Multivariate logistic models were used to analyse the relationship between presence of infection and onset of diarrhoea. The study provided evidence of significant associations between diarrhoea and infection with rotavirus, Campylobacter coli and the presence of Verotoxin in faecal samples. With the exception of Cryptosporidium parvum intestinal parasites including Strongylidae and Eimeria sp. were found to be less prevalent in cases than in controls. Control calves were significantly more frequently infected with Strongyloides papillosus than case animals.",,"animal; animal disease; animal parasitosis; article; bacterial infection; case control study; cattle; cattle disease; diarrhea; enteropathy; female; microbiology; multivariate analysis; parasitology; Switzerland; virus infection; Animals; Bacterial Infections; Case-Control Studies; Cattle; Cattle Diseases; Diarrhea; Female; Intestinal Diseases; Multivariate Analysis; Parasitic Diseases, Animal; Switzerland; Virus Diseases","Archambault, D., Morin, G., Blazhary, Y., Roy, R.S., Study of virus excretion in faeces of diarrhoeic and asymptomatic calves infected with rotavirus (1990) J. Vet. Med. B, 37, pp. 73-76; Behymer, D.E., Riemann, H.P., Utterback, W., D-Elmi, C., Franti, C.E., Mass screening of cattle sera against 14 infectious agents, using an ELISA system for monitoring health in livestock (1991) Amer. J. Vet. Res., 52, pp. 1699-1705; Blanco, M., Blanco, J., Blanco, J.E., Ramos, J., Enterotoxigenic, verotoxigenic and necrotoxigenic Escherichia coli isolated from cattle in Spain (1993) Am. J. Vet. Res., 54, pp. 1446-1450; Blanco, M., Blanco, J.E., Blanco, J., Gonzales, E.A., Alonso, M.P., Maas, H., Jansen, W.H., Prevalence and characteristics of human and bovine verotoxgenic Escbericbia coli strains isolated in Galicia (north-western Spain) (1996) Eur. J. Epidemiol., 12, pp. 13-19; Boss, P., Monckton, P.P., Nicolet, J., Burnens, A.P., Nachweis von Toxigenen verschiedener E. coli Pathotypen beim Schwein mit nichtradioaktiv markierten Sonden (1992) Schweiz. Arch. Tierheilkd., 134, pp. 31-37; Breslow, N.E., Day, N.E., (1987) Statistical Methods in Cancer Research, Vol. II - The Design and Analysis of Cohort Studies, 2. , IARC scientific publications no. 82; Bruzzi, P., Gren, S.B., Byar, D.P., Brinton, A., Schairer, C., Estimating the population attributable fractions for multiple risk factors using case-control data (1985) Am. J. Epidemiol., 122, pp. 904-913; Burnens, A.P., Frey, A., Lior, H., Nicolet, J., Prevalence and clinical significance of verocytotoxin-producing Escherichia coli (VTEC) isolated from cattle in herds with and without calf diarrhoea (1995) J. Vet. Med. B, 42, pp. 311-318; Burnens, A.P., Stanley, J., Schaad, U.B., Nicolet, J., Novel Campylobacter-like organism resembling Helicobacter fennelliae isolated from a boy with gastroenteritis and from dogs (1993) J. Clin. Microbiol., 31, pp. 1916-1917; Dowel, D., Untersuchungen bei Wiederkäuern zum Vorkommen von Eiern gastro-intestinaler Nematoden im Kot in Relation zur Wurmbhrde (1990) Mitt. Osterr. Ges. Tropenmed. Parasitol., 12, pp. 69-90; Eckert, J., Kutzer, E., Rommel, M., Bürger, H.-J., Körting, W., (1992) Veterinärmedizinische Parasitologie. 4. Auflage, , Verlag Paul Parey Berlin und Hamburg; Eller, G., (1991) Eimeria-Infektionen bei Kälbern: Vorkommen und Verlauf Bei Unterschiedlichen Haltungsformen, , Vet. med. Diss., Giessen; Fleiss, J.L., (1986) The Design and Analysis of Clinical Experiments, , John Wiley and Sons, New York; Ganaba, R., Belanger, D., Dea, S., Bigras-Poulin, M., A seroepidemiological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from northwestern Quebec (1995) Can. J. Vet. Res., 59, pp. 26-33; Garcia, M.M., Lior, H., Stewart, R.B., Ruckerbauer, G.M., Trudel, J.R.R., Skljarevski, A., Isolation, characterisation and serotyping of Campylobacter jejuni and Campylobacter coli from slaughter cattle (1985) Appl. Environ. Microbiol., 49, pp. 667-672; Griffin, P.M., Tauxe, R.V., The epidemiology of infections caused by Escbericbia coli O157: H7, other enterohemorhagic E. coli, and the associated hemolytic uremic syndrome (1991) Epidemiol. Rev., 13, pp. 60-98; Harp, J.A., Woodmanse, D.B., Moon, H.W., Resistance of calves to Cryptosporidium parvum: Effects of age and previous exposure (1990) Infect. Immun., 58, pp. 2237-2240; Henriksen, S.A., Pohlenz, J.F., Staining of cryptosporidia by a modified Ziehl-Neelsen technique (1981) Acta. Vet. Scand., 22, pp. 594-596; Hosmer, D.W., Lemeshow, S.L., (1989) Applied Logistic Regression, , John Wiley and Sons, New York; Janke, B.H., Francis, D.H., Collins, J.E., Libal, M.C., Zeman, D.H., Johnson, D.D., Neiger, R.D., Attaching and effacing Escherichia coli infection as a cause of diarrhea in young calves (1990) J. Am. Vet. Med. Assoc., 196, pp. 897-901; Kaufmann, J., (1996) Parasitic Infections in Domestic Animals; a Diagnostic Manual, , Birkhäuser Verlag, Basel; Kehl, K.S., Havens, P., Behnke, C.E., Acheson, D.W.K., Evaluation of the Premier EHEC assay for detection of Shiga toxin-producing Escherichia coli (1997) J. Clin. Microbiol., 35, pp. 2051-2054; Levine, M.M., Escbericbia coli that cause diarrhea: Enterotoxigenic, enteropathogenic, enteroinvasive, enterohemorrhagic, and enteroadherent (1987) J. Infect. Dis., 155, pp. 377-389; Moore, D.A., Zeman, D.H., Cryptosporidiosis in neonatal calves: 277 cases (1986-87) (1991) J. Am. Vet. Med. Assoc., 198, pp. 1969-1972; Radostits, O.M., Blood, D.C., Gray, C.C., (1994) Veterinary Medicine, a Textbook of the Diseases of Cattle, Sheep, Pigs, Goats and Horses, 8th Edn., , Baillière Tindall; Rebhuhn, W.H., Guard, C., Richards, C.M., (1995) Diseases of Dairy Cattle, , Williams and Wilkins, Baltimore; Rosef, O., Gondrosen, B., Kapperud, G., Underal, B., Isolation and characterization of Campylobacter jejuni and Campylobacter coli from domestic and wild mammals in Norway (1983) Appl. Env. Microbiol., 46, pp. 855-859; Schoonderwoerd, M., Clarke, R.C., Van Dreumel, A.A., Rawluk, S.A., Colitis in calves: Natural and experimental infection with a verotoxin-producing strain of Escbericbia coli O111: NM (1988) Can. J. Vet. Res., 52, pp. 484-487; Tauxe, R.V., Hargrett-Bean, N., Patton, C.M., Wachsmuth, I.K., Campylobacter isolates in the United States, 1982-86 (1988) MMWR CDC Surveillance Summaries, 37, pp. 1-13; Tokhi, A.M., Peiris, J.S.M., Scotland, S.M., Willshaw, G.A., Smith, H.R., Cheasty, T., A longitudinal study of vero cytotoxin producing Escbericbia coli in cattle calves in Sri Lanka (1993) Epidemiol. Infect., 110, pp. 197-208; Torres-Medina, A., Schlafer, D.H., Mebus, C.A., Rotaviral and coronaviral diarrhea (1985) Vet. Clin. N Amer-Food Anim. Pr., 1 (3); Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Adv. Vet. Sc. Comp. Med., 29, pp. 104-175; Tzipori, S., Smith, M., Halpin, C., Angus, K.W., Sherwood, D., Campell, I., Experimental cryptosporidiosis in calves: Clinical manifstations and pathological findings (1983) Vet. Rec., 112, pp. 116-120; Warner, D.P., Bryner, J.H., Campylobacter jejuni and Campylobacter coli inoculation of neonatal calves (1983) Am. J. Vet. Res., 45, pp. 1822-1824; Webster, K.A., Giles, M., Green, J.A., Dawson, C., Catchpole, J., Diagnosis in a veterinary laboratory comparison of techniques for the routine detection of Cryptosporidium parvum (1997) VIIth International Coccidiosis Conference, 1, p. 5. , September 1997, Oxford, UK; Willshaw, G.A., Smith, H.R., Roberts, D., Thirlwell, J., Cheasty, T., Rowe, B., Examination of raw beef products for the presence of Verocytotoxin producing Escbericbia coli, particularly those of serogroup O157 (1993) J. Appl. Bacteriol., 75, pp. 420-426; Wray, C., Mclaren, I., Pearson, G.R., Occurrence of attaching and effacing lesions in the small intestine of calves experimentally infected with bovine isolates of verocytoxic E. coli (1989) Vet. Rec., 125, pp. 365-368","Busato, A.; Institute of Animal Breeding, Faculty of Veterinary Medicine, University of Berne, Bremgartenstrasse 109a, CH-3012 Berne, Switzerland",,,09311793,,JVMBE,"9852767","English","J. Vet. Med. Ser. B",Article,"Final",,Scopus,2-s2.0-0032196654
"De Haan C.A.M., Roestenberg P., De Wit M., De Vries A.A.F., Nilsson T., Vennema H., Rottier P.J.M.","7003682643;22941948200;7102191667;7202909794;35594417400;7003697291;7006145490;","Structural requirements for O-glycosylation of the mouse hepatitis virus membrane protein",1998,"Journal of Biological Chemistry","273","45",,"29905","29914",,37,"10.1074/jbc.273.45.29905","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032491611&doi=10.1074%2fjbc.273.45.29905&partnerID=40&md5=b5b2a6001da7c34a6fd291e84e78216f","Cell Biology Programme, EMBL, 69012 Heidelberg, Germany; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P. O. Box 80.165, 3508 TD Utrecht, Netherlands","De Haan, C.A.M.; Roestenberg, P.; De Wit, M.; De Vries, A.A.F.; Nilsson, T., Cell Biology Programme, EMBL, 69012 Heidelberg, Germany; Vennema, H.; Rottier, P.J.M., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P. O. Box 80.165, 3508 TD Utrecht, Netherlands","The mouse hepatitis virus (MHV) membrane (M) protein contains only O- linked oligosaccharides. We have used this protein as a model to study the structural requirements for O-glycosylation. We show that MHV M is modified by the addition of a single oligosaccharide side chain at the cluster of 4 hydroxylamino acids present at its extreme amino terminus and identified Thr at position 5 as the functional acceptor site. The hydroxylamino acid cluster, which is quite conserved among O-glycosylated coronavirus M proteins, is not in itself sufficient for O-glycosylation. Downstream amino acids are required to introduce a functional O-glycosylation site into a foreign protein. In a mutagenic analysis O-glycosylation was found to be sensitive to some particular changes but no unique sequence motif for O- glycosylation could be identified. Expression of mutant M proteins in cells revealed that substitution of any 1 residue was tolerated, conceivably due to the occurrence of multiple UDP-N-acetylgalactosamine:polypeptide N- acetylgalactosaminyltransferases (GalNAc transferases). Indeed, MHV M served as a substrate for GalNac-T1, -T2, and -T3, as was demonstrated using an in situ glycosylation assay based on the co-expression of endoplasmic reticulum- retained forms of the GalNAc transferases with endoplasmic reticulum-resident MHV M mutants. The GalNAc transferases were found to have largely overlapping, but distinct substrate specificities. The requirement for a threonine as acceptor rather than a serine residue and the requirement for a proline residue three positions downstream of the acceptor site were found to be distinctive features.",,"hydroxyamino acid; membrane protein; oligosaccharide; virus envelope protein; animal cell; animal experiment; animal model; article; coronavirus; dna flanking region; endoplasmic reticulum; enzyme activity; enzyme specificity; gene expression; glycosylation; hepatitis virus; mouse; nonhuman; priority journal; protein binding; protein structure; Acetylgalactosamine; Amino Acid Sequence; Amino Acid Substitution; Animals; Base Sequence; Cell Line; Cricetinae; DNA Primers; Fluorescent Antibody Technique, Indirect; Glycosylation; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Site-Directed; Viral Matrix Proteins","Serafini-Cessi, F., Dall'Olio, F., Malagolini, N., Campadelli-Fiume, G., (1989) Biochem. 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Chem., 267, pp. 25010-25018; Yoshida, A., Suzuki, M., Ikenga, H., Takeuchi, M., (1997) J. Biol. Chem., 272, pp. 16884-16888; Wang, Y., Agarwal, N., Eckhardt, A.E., Stevens, R.D., Hill, R.L., (1993) J. Biol. Chem., 268, pp. 22979-22983; Stern, D.F., Sefton, B.M., (1982) J. Virol., 44, pp. 804-812; Niemann, H., Boschek, B., Evans, D., Rosing, M., Tamura, T., Klenk, H.D., (1982) EMBO J., 1, pp. 1499-1504; Armstrong, J., Niemann, H., Smeekens, S., Rottier, P.J.M., Warren, G., (1984) Nature, 308, pp. 751-752; Pfleiderer, M., Skinner, M.A., Siddell, S.G., (1986) J. Infect. Dis., 154, pp. 443-447; Sugiyama, K., Ishikawa, R., Fukuhara, N., (1986) Arch. Virol., 87, pp. 331-337; Homberger, F.R., (1994) Virus Res., 31, pp. 49-56; Mounir, S., Talbot, P.J., (1992) J. Gen. Virol., 73, pp. 2731-2736; Deregt, D., Sahara, M., Babiuk, L.A., (1987) J. Gen. Virol., 68, pp. 2863-2877","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands; email: P.Rottier@vetmic.dgk.ruu.nl",,,00219258,,JBCHA,"9792708","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0032491611
"Vabret A., Brouard J., Petitjean J., Eugene-Ruellan G., Freymuth F.","7003959575;7005417717;7006379234;6506460268;7103410207;","Human coronavirus infections [Infections a coronavirus humains]",1998,"Presse Medicale","27","35",,"1813","1817",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032517587&partnerID=40&md5=78d66951c5369158cf11ad870e48b634","Lab. de Virologie Hum. et Molec., CHU de Caen; Service de Pédiatrie A, CHU de Caen; Lab. de Virologie Hum. et Molec., CHU de Caen, avenue Georges Clémenceau, F 14033 Caen Cedex, France","Vabret, A., Lab. de Virologie Hum. et Molec., CHU de Caen; Brouard, J., Service de Pédiatrie A, CHU de Caen; Petitjean, J., Lab. de Virologie Hum. et Molec., CHU de Caen; Eugene-Ruellan, G., Lab. de Virologie Hum. et Molec., CHU de Caen; Freymuth, F., Lab. de Virologie Hum. et Molec., CHU de Caen, Lab. de Virologie Hum. et Molec., CHU de Caen, avenue Georges Clémenceau, F 14033 Caen Cedex, France","Poorly-known virus: Coronaviruses, so named because of their sun-ray- like aspect, were discovered in the sixties. The biology of these RNA viruses is complex and poorly understood. Known pathogens: Coronaviruses are known pathogens in veterinary medicine, causing disease states in several domestic species. In human medicine, they can cause benign respiratory infections, but few laboratories include coronaviruses in their routine diagnostic tests. Suspected pathogens: There is some data in the literature suggesting coronaviruses might be implicated in more severe diseases including multiple sclerosis, necrotizing enterocolitis, and lower respiratory tract infections, particularly in infants. Improving diagnostic methods: Due to the lack of reliable and sensitive diagnostic techniques, it is impossible to date to correctly assess the medical impact of these ubiquitous and endemic viruses. Molecular biology techniques enabling detection of human coronavirus infections should be applied to verifying the suspected implication of these viruses in diverse disease states.",,"coronavirus; france; human; infection risk; nonhuman; respiratory tract infection; review; virus detection; virus infection; animal; cat; cattle; chicken; child; comparative study; Coronavirus; dog; enzyme linked immunosorbent assay; fluorescence; genetics; immunology; isolation and purification; mouse; preschool child; respiratory tract infection; swine; turkey (bird); virology; virus gene; virus infection; virus antibody; virus antigen; virus RNA; Animals; Antibodies, Viral; Antigens, Viral; Cats; Cattle; Chickens; Child; Child, Preschool; Coronavirus; Coronavirus Infections; Dogs; Enzyme-Linked Immunosorbent Assay; Fluorescence; Genes, Viral; Humans; Mice; Respiratory Tract Infections; RNA, Viral; Swine; Turkeys","Myint, S.H., Human Coronaviruses : A Brief Review (1994) Medical Virology, 4, pp. 35-46; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc Soc Exp Biol Med, 121, pp. 190-193; Mc Intosh, K., Dees, J., Becker, W.B., Kapikian, A.Z., Chanock, R.M., Recovery in tracheal organ culture of novel viruses from patients with respiratory disease (1967) Proc Natl Acad Sci USA, 57, pp. 933-940; Burks, J.S., Devald, B.L., Jankovski, L.S., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Murray, R.S., Mac Millan, B., Burks, J.S., Detection of coronavirus genome in the CNS of MS patients and control patients (1987) Neurology, 37 (1 SUPPL.), p. 109; Cristallo, A., Gambaro, F., Biamonti, G., Ferrante, P., Battaglia, M., Cereda, P.M., Human coronavirus polyadenylated RNA sequences in cerebrospinal fluid from multiple sclerosis patients (1997) Microbiologica, 20, pp. 105-114; Mc Intosh, K., Coronaviruses (1990) Fields Virology, pp. 857-864. , Fields BN, Knipe DM eds. Raven Press, Ltd., New York Second Edition; Siddell, S.G., The Coronaviridae: An Introduction (1995) The Coronaviridae, pp. 1-10. , Siddell SG ed. Plenum Press, New York; Macnaughton, M.R., Davies, H.A., Human Enteric Coronavirus Brief Review (1981) Arch Virol, 70, pp. 301-313; Brian, D.A., Brenda, G.H., Kienzle, T.E., The Coronavirus Hemagglutinin Esterase Glycoprotein (1995) The Coronaviridae, pp. 165-179. , Siddell SG ed. Plenum Press, New York; Lai, M.M., Liao, C.L., Lin, Y.J., Zhang, X., Coronavirus: How a large RNA viral genome is replicated and transcribed (1994) Infect Agents Dis, 3, pp. 98-105; Van Der Most, R.G., Spaan, W.J.M., Coronavirus Replication, Transcription, and RNA Recombinaison (1995) The Coronaviridae, pp. 11-31. , Siddell SG ed. Plenum Press, New York; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombinaison in Coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis Coronavirus spike protein result in the loss of‡ enteric tropism (1997) Virology, 227, pp. 378-388; Yeager, C.L., Ashmun, R.A., William, R.K., Human amino-peptidase N is a receptor for human Coronavirus 229E (1992) Nature, 357, pp. 420-422; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine Coronavirus recognise sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529; Collins, A.R., Human Coronavirus OC43 interacts with major histocompatibility complex class I molecules at the cell surface to establish infection (1994) Immunol Invest, 23, pp. 313-321; Afzelius, B.A., Ultrastructure of human nasal epithelium during an episode of coronavirus infection (1994) Virchows-Arch, 424, pp. 295-300; Lina, B., Valette, M., Foray, S., Surveillance of Community-Acquired Viral Infections Due to Respiratory Viruses in Rhone-Alpes (France) during Winter 1994 to 1995 (1996) J Clin Microbiol, 34, pp. 3007-3011; Trigg, C.J., Nicholson, K.G., Wang, J.H., Bronchial inflammation ant the common cold : A comparison of atpic and non-atopic individuals (1996) Clin Exp Allergy, 26, pp. 665-676; McIntosh, K., Chao, R.K., Krauses, H.E., Coronavirus Infection in Acute Lower Respiratory Tract Diseases of Infants (1974) J Infect Dis, 130, pp. 502-507; Mc Intosh, K., McQuillin, J., Reed, S.E., Gardner, P.S., Diagnosis of human coronavirus infection by immunofluorescence: Method and application to respiratory disease in hospitalized children (1978) J Med Virol, 2, pp. 341-346; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other the the common cold (1980) J Med Virol, 6, pp. 259-265; Falsey, A.R., McCann, R.M., Hall, W.J., Acute respiratory tract infection in daycare centers for olders persons (1995) J Am Geriatr Soc, 1, pp. 30-36; Freymuth, F., Quibriac, M., Petitjean, J., Daon, F., Amiel, M.L., Les virus responsables d'infections repsiratoires en pédiatrie. Bilan de 3480 aspirations nasales réalisées chez l'enfant en une période de six ans (1987) Ann Pediatr, 34, pp. 493-501; Monto, A.S., Lim, S.K., The Tecumseh study of respiratory illness VI. Frequency of and relationship between out-beaks of coronavirus infection (1974) J Infect Dis, 129, pp. 271-274; Gerna, G., Achill, G., Cattaneo, E., Cereda, P.M., Determination of coronavirus 229E antibody by an immune-adherence hemagglutination method (1978) J Med Virol, 2, pp. 215-223; Sizun, J., Soupre, D., Legrand, M.C., Rôle pathogène des coronavirus en réanimation pédiatrique : Analyse rétrospective de 19 prélèvements positifs en immunofluorescence indirecte (1994) Arch Pédiatr, 1, pp. 477-480; Freymuth, F., Vabret, A., Eugène, G., Petitjean, J., Mammes, O., Gennetay, E., Diagnostic moléculaire des infections respiratoires communes (1997) Biologie Prospective, , CR du 9e Colloque International de Pont-à-Mousson. Galteau MM, Delwaide P eds. J. Libbey Eurotext, Londres-Paris; Myint, S., Siddell, S., Tyrrell, D., Detection of human coronavirus 229E in nasal washings using RNA:RNA hybridization (1989) J Med Virol, 29, pp. 70-73; Stewart, J.N., Mounir, S., Talbot, J.P., Detection of coronaviruses by the polymerase chain raction (1995) Diagnosis of Human Viruses by Polymerase Chain Reaction Technology, pp. 316-327. , Becker Y, Daraï G eds. Springer-Verlag, New-York; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364","Freymuth, F.; Lab. Virologie Humaine/Moleculaire, CHU de Caen, avenue Georges Clemenceau, F 14033 Caen Cedex, France",,,07554982,,PRMEE,"9850702","French","Presse Med.",Review,"Final",,Scopus,2-s2.0-0032517587
"Hays J.P., Myint S.H.","7102191402;35479862600;","PCR sequencing of the spike genes of geographically and chronologically distinct human coronaviruses 229E",1998,"Journal of Virological Methods","75","2",,"179","193",,9,"10.1016/S0166-0934(98)00116-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031752934&doi=10.1016%2fS0166-0934%2898%2900116-5&partnerID=40&md5=22fa0f37b79e6281df0680b1555064c4","Dept. of Microbiology and Immunology, University of Leicester, LE1 9HN, Leicester, United Kingdom","Hays, J.P., Dept. of Microbiology and Immunology, University of Leicester, LE1 9HN, Leicester, United Kingdom; Myint, S.H., Dept. of Microbiology and Immunology, University of Leicester, LE1 9HN, Leicester, United Kingdom","A reverse transcription nested PCR (RT-PCR) sequencing methodology was developed and used to generate sequence data from the spike genes of three geographically and chronologically distinct human coronaviruses 229E. These three coronaviruses were isolated originally from the USA in the 1960s (human coronavirus 229E strain ATCC VR-74), the UK in the 1990s (human coronavirus 229E LRI 281) and Ghana (human coronavirus 229E A162). Upon translation and alignment with the published spike protein sequence of human coronavirus 229E 'LP' (isolated in the UK in the 1970s), it was found that variation within the translated protein sequences was rather limited. In particular, minimal variation was observed between the translated spike protein sequence of human coronaviruses 229E LP and ATCC VR-74 (1/1012 amino acid differences), whilst most variation was observed between the translated spike protein sequence of human coronaviruses 229E LP and A162 (47/1012 amino acid changes). Further, the translated spike protein sequence of human coronavirus 229E A162 showed three clusters of amino acid changes, situated within the 5' half of the translated spike protein sequence. Copyright (C) 1998 Elsevier Science B.V.","Human coronaviruses 229E; PCR; Spike genes","virus protein; amino acid sequence; amino acid substitution; article; coronavirus; human; nonhuman; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; virus gene; Adult; Amino Acid Sequence; Child; Coronavirus; Coronavirus 229E, Human; Genes, Viral; Ghana; Great Britain; Humans; Membrane Glycoproteins; Molecular Sequence Data; Polymerase Chain Reaction; Sequence Homology, Amino Acid; Time Factors; United States; Variation (Genetics); Viral Envelope Proteins","Banner, L.R., Keck, J.G., Lai, M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Banner, L.R., Lai, M.M., Random nature of coronavirus recombination in the absence of selection pressure (1990) Virology, 185, p. 441; Callow, K.A., Effect of specific humoral immunity and some non-specific factors on resistance of volunteers to respiratory coronavirus infection (1985) J. Hyg., 95, p. 173; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, , S.G. Siddell. London: Plenum Press; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidium thiocyanate phenol chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, p. 358; De Groot, R.J., Van Leen, R.W., Dalderup, M.J.M., Vennema, H., Horzinek, M.C., Spaan, W.J., Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralising antibodies in mice (1989) Virology, 171, p. 493; (1995) DNA Sequencing: Chemistry Guide, , Part Number 903563, Perkin Elmer, Warrington, Cheshire, UK; Don, R.H., Cox, P.T., Wainwright, B.J., Baker, K., Mattick, J.S., Touchdown PCR to circumvent spurious priming during gene amplification (1991) Nucl. Acids. Res., 19, p. 4008; Gwaltney, J.M., Epidemiology of the common cold (1980) Ann. N.Y. Acad. Sci., 353, pp. 54-690; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc. Soc. Exp. Biol., 121, pp. 190-193; Horsburgh, B.C., Brown, T.D., Cloning, sequencing and expression of the S protein from two geographically distinct strains of canine coronavirus (1995) Virus Res., 39, pp. 63-74; Hruskova, J., Heinz, F., Svandova, E., Pennigerova, S., Antibodies to human coronaviruses 229E and OC43 in the population of C.R (1990) Acta. Virologica., 34, pp. 346-352; Jimenez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gatroenteritis virus neutralization (1986) J. Virol., 60, p. 131; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of the role of viral infections in exacerbations of asthma in 9-11 year old children (1995) Br. Med. J., 310, pp. 1225-1229; Kusters, J.G., Jager, E.J., Neisters, H.G., Van Der Zeijst, B.A., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, p. 605; Lai, M.M.C., Coronavirus-organization, replication and expression of genome (1990) Ann. Rev. Microbiol., 44, p. 303; Lai, M.M., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, p. 449; La Monica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localisation of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virology, 182, p. 838; MacNaughton, M.R., Occurrence and frequency of coronavirus infections in humans as determined by enzyme linked immunosorbant assay (1982) Infect. Immunol., 38, p. 419; Matsumoto, I., Kawana, R., Virological surveillance of acute respiratory tract illnesses of children in Morioka, Japan. III. Human respiratory coronavirus (1992) J. Jpn. Assoc. Infect. Dis., 66, pp. 319-326; McIntosh, K., Kapikian, A.Z., Turner, H.C., Hartley, J.W., Parrott, R.H., Chanock, R.M., Seroepidemologic studies of coronavirus infection in adults and children (1970) Am J. Epidemiol., 91, p. 585; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, M.A., Copronavirus infections in lower respiratory tract disease of infants (1974) J. Infect. Dis., 130, p. 502; Monto, A.S., Lim, S.K., The Tecumseh study of respiratory illness. VI. Frequency and relationship between outbreaks of coronavirus infection (1974) J. Infect. Dis., 129, pp. 271-276; Myint, S.H., Human coronavirus infections (1995) Book in the Series, the Viruses, , In: Siddell, S.G. (Eds.), The Coronaviridae. Plenum Press, London. Fraenkel-Conrat, H., Wagner, R.R. (series Eds.), Plenum Press, New York; Naeve, C.W., Buck, G.A., Nieces, R.L., Pon, R.T., Robertson, M., Accuracy of automated DNA sequencing-a multilaboratory comparison of sequencing results (1995) Biotechniques, 19, pp. 48-453; Parker, L.T., Deng, Q., Zakeri, H., Carlson, C., Nickeroson, D.A., Kwok, D.Y., Peak height variations in automated sequencing of PCR products using Taq dye-terminator chemistry (1995) Biotechniques, 19, pp. 116-121; Payne, C.M., Ray, C.G., Borduin, V., Minnich, L.L., Lebowitz, M.D., An eight year study of the viral agents of acute gastroenteritis in humans: Ultrastructural observations and seasonal distribution with a major emphasis on coronavirus-like particles (1986) Diagn. Microbiol. Infect., 5, pp. 39-54; Philpotts, R., Clones of MRC-c cells may be superior to the parent line for the culture of 229E-like strains of human respiratory coronavirus (1983) J. Virol. Methods, 6, pp. 267-269; Raabe, T., Schelle, P.B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) J. Gen. Virol., 71, pp. 1065-1073; Roux, K.H., Using mis-matched primer pairs in touchdown PCR (1994) Biotechniques, 16, p. 812; Siddell, S.G., The Coronaviridae: An Introduction in the Coronaviridae (1995) Book in the Series, the Viruses, , Plenum Press, London. Fraenkel-Conrat, H., Wagner, R.R. (series Eds.), Plenum Press, New York; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brain of a multiple sclerosis patients (1992) Virology, 191, p. 502; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common cold virus in organ culture (1965) Br. Med. J., 1, p. 1467; Wesseling, J.G., Vennema, H., Godeke, G-J., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Myint, S.H.; Dept. of Microbiology/Immunology, University of Leicester, Leicester LE1 9HN, United Kingdom; email: dsm@le.ac.uk",,,01660934,,JVMED,"9870593","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0031752934
"Morita E., Ebina H., Muto A., Himeno H., Hatakeyama K., Sugiyama K.","7102013872;16836146700;57190154609;7005113644;7202837552;57210523397;","Primary structures of hemagglutinin-esterase and spike glycoproteins of murine coronavirus DVIM",1998,"Virus Genes","17","2",,"123","128",,3,"10.1023/A:1008060522426","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031740052&doi=10.1023%2fA%3a1008060522426&partnerID=40&md5=a101124e68fbd064300cdc4999b80632","Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan","Morita, E., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan; Ebina, H., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan; Muto, A., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan; Himeno, H., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan; Hatakeyama, K., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan; Sugiyama, K., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan","Diarrhea virus of infant mice (DVIM) is a member of murine hepatitis viruses (MHVs). The nucleotide sequences of the genes encoding the hemagglutinin-esterase (HE) and the spike (S) glycoproteins from DVIM were determined and compared with those of other MHVs. The deduced amino acid sequence of the HE protein was most similar to that of MHV-S strain (94% identity), and the S protein sequence was most similar to that of MHV-Y strain (90% identity). The DVIM HE protein has a unique N-linked glycosylation site in addition to other glycosylation sites common to many MHV strains. Unlike in some typical MHV strain, such as MHV-A59 and MHV-JHM, the vast majority of the S glycoprotein molecules in DVIM exist an uncleaved form probably due to several amino acid substitutions around the cleavage site.","Cleavage of surface glycoprotein; DVIM; Hemagglutinin-esterase glycoprotein; MHV; N-linked glycosylation site; Spike glycoprotein","esterase; hemagglutinin; virus enzyme; virus glycoprotein; amino acid sequence; article; coronavirus; enzyme structure; glycosylation; nonhuman; nucleotide sequence; priority journal; sequence homology; Amino Acid Sequence; Animals; Diarrhea; Glycoproteins; Glycosylation; Hemagglutinins, Viral; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Sequence Alignment; Viral Envelope Proteins; Viral Fusion Proteins; Viral Proteins; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus (strain S); RNA viruses","Homberger, F.R., (1997) Laboratory Animals, 31, pp. 97-115; Spaan, W., Cavanagh, D., Horzinek, M.C., (1988) J Gen Virol, 69, pp. 2939-2952; Lai, M.M.C., (1990) Annu Rev Microbiol, 44, pp. 303-333; Sugiyama, K., Amano, Y., (1980) Arch Virol, 66, pp. 95-105; Sugiyama, K., Amano, Y., (1981) Arch Virol, 67, pp. 241-251; Homberger, F.R., (1994) Virus Res, 31, pp. 49-56; Homberger, F.R., (1995) Arch Virol, 140, pp. 571-579; Homberger, F.R., Zhang, L., (1997) Laboratory Animal Science, 47, pp. 86-90; Sugiyama, K., Ishikawa, R., Fukuhara, N., (1986) Arch Virol, 89, pp. 245-254; Cavanagh, D., (1995) The Coronaviridae, pp. 73-113. , Siddell S.G. (ed). Plenum press, New York; Talbot, P.J., (1989) Intervirology, 30, pp. 117-120; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., (1988) J Virol, 62, pp. 4686-4690; Brian, D.A., Hogue, B.G., Kienzle, T.E., (1995) The Coronaviridae, pp. 165-179. , Siddell S.G. Plenum press, New York; Luytjes, W., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., (1987) Virology, 161, pp. 479-487; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., (1997) Virology, 227, pp. 215-219; Kunita, S., Zhang, L., Homberger, F.R., Compton, S.R., (1995) Virus Res, 35, pp. 277-289; Gagneten, S., Goutg, O., Dubois-Dalco, M., Rottier, P., Rossen, J., Holmes, K.V., (1995) J Virol, 69, pp. 889-895; Williams, R.K., Jiang, G.S., Snyder, S.W., Frana, M.F., Holmes, K.V., (1990) J Virol, 64, pp. 3817-3823; James, L.G., Susan, T.H., Susan, R.W., (1993) J Virol, 67, pp. 4504-4512; Taguchi, F., (1993) J Virol, 67, pp. 1195-1202","Sugiyama, K.; Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan",,,09208569,,VIGEE,"9857985","English","Virus Genes",Article,"Final",Open Access,Scopus,2-s2.0-0031740052
"István K., András B.-P., Sándor K., Katalin M., János T., Klingeborn B.S., Sándor B.","6603849862;6602706957;6603764465;6602448973;6603437628;35611673800;56248472000;","Prevalence of coronavirus infections in urban cats. Preliminary publication [Városi macskák coronavírus-fertozöttsége: Elozetes közlemény]",1998,"Magyar Allatorvosok Lapja","120","11",,"655","658",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3743076418&partnerID=40&md5=2639a29e5759072e05d55c4283820b0b","Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; National Veterinary Institute, P.O. Box 7073, S-750 07 Uppsala, Sweden","István, K., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; András, B.-P., National Veterinary Institute, P.O. Box 7073, S-750 07 Uppsala, Sweden; Sándor, K., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; Katalin, M., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; János, T., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; Klingeborn, B.S., National Veterinary Institute, P.O. Box 7073, S-750 07 Uppsala, Sweden; Sándor, B., National Veterinary Institute, P.O. Box 7073, S-750 07 Uppsala, Sweden","Caused by a coronavirus, feline infectious peritonitis (FIP) is one of the major viral diseases of Felids. Presumably, there is a strong relationship between the agent of FIP (FIPV) and the enterai coronavirus (FECV) that is generally asymptomatically carried: recent findings indicate that FIPV develop from FECV variants through recombination. Hence the ""harmless"" FECV-carrier status of clinically healthy animals constitutes real risk factor of developing lethal FIP later on. The key role of cats in the evolution of coronaviruses with structurally related antigens is becoming more and more evident: it is known that feline cells are permissive to all type I coronaviruses and it has also been shown that the development of some FIPV follows from the recombination of feline and canine coronaviruses, presumably in feline hosts. The authors examined 102 domestic cats and 11 Persian cats of a breeding colony to determine the proportion of asymptomatic coronavirus carriers in the clinically healthy cat population. Rectal swab samples were collected and prepared to yield viral nucleic acid for polimerase chain reaction (PCR) involving one of the most conservative segments of the FIPV genome. Thirty-one of the 102 domestic cats were PCR positive, i.e. carriers of a feline coronavirus. The proportion of positives was 35.5% among mixed breed cats, 30.1 % among pure-bred animals and 43.5% among Persian cats. Seven out of the eleven adults (63.6%) of the Persian breeding colony were also PCR positive. Sequencing of the PCR products and their comparison with various FIPV genome segments indicated that most of the cats were infected with FECV. However, some cats were shown to be asymptomatic carriers of FIPV, and in one cat the PCR product showed greatest homology with canine coronavirus. As these results were only one ""snapshot"" in virus evolution, the authors are planning further and more detailed examinations on the positive animals along with their clinical monitoring to contribute to a better understanding of the biology and evolution of feline coronaviruses that will, hopefully, and ultimately, lead to the manufacture of effective tools for their prevention.",,,"Baric, R.S., Fu, K.F., Establishing a genetic recombination map of murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Boom, R., Sol, C.J.A., Rapid and simple method for purification of nucleic acid (1990) J. Clin. Microbiol., 28, pp. 495-503; Cheung, R.C., Matsui, S., Greenberg, H., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) J. Clin. Microbiol., 32, pp. 2593-2597; De Groot, R.J., Ter Haar, R.J., Intracellular RNAs of the feline infectious peritonitis virus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , SIDDELL, S. G. (ed.): Plenum Press. New York; De Vries, A.A.F., Horzinek, M.C., The genome organization of the Nidovirales: Similarities and differences between Arteri-, Toro-, and Coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Domingo, E., Díez, J., New observations on antigenic diversification of RNA viruses. Antigenic variation is not dependent on immune selection (1993) J. Gen. Virol., 74, pp. 2039-2045; Evermann, J.F., Mckeirnan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Vet.Microbiol., 28, pp. 243-255; Foley, J.F., Poland, A., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) J. Am. Vet. Med. Ass., 210, pp. 1313-1318; Foley, J.F., Poland, A., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Am. Vet. Med. Ass., 210, pp. 1307-1312; Gamble, D.A., Lobbiani, A., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35, pp. 673-675; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) J. Am. Vet. Med. Ass., 209, pp. 1117-1120; Herrewegh, A.A.P.M., De Grout, R., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A.P.M., Mähler, M., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Vennema, H., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 662-1631; Herrewegh, A.A.P.M., Smeenk, I., Feline coronavirus type II strains 79-1638 and 79-1146 originate from a duble recombination between feline coronavirus type I and canine coronavirus (1998) J. Gen. Virol., 79, pp. 4508-4514; Higgins, D.G., Bleasby, A.J., Fuchs, R., Clustal, V., Improved software for multiple sequence alignment (1992) Comput. Appl. Biosci., 8, pp. 189-191; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Antigenic analysis of feline coronaviruses with monoclonal antibodies (Mabs): Preparation of Mabs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol., 25, pp. 13-24; Hohdatsu, T., Okada, S., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Holdnd, J.J., De La Torre, J.C., Steinhauer, D.A., RNA virus populations as quasispecies (1992) Curr.Topics Microbiol.Immunol., 176, pp. 1-20; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Keck, J.G., Matsushima, G.K., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kurosaki, M., Enomoto, N., Evolution and selection of hepatitis C virus variants in patients with chronic hepatitis C (1994) Virology, 205, pp. 161-169; Kusters, J.G., Jager, E.J., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M.C., Baric, R.C., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Lai, M.M.C., Genetic recombination in RNA viruses (1992) Curr. Topics Microbiol. and Immunol., 176, pp. 21-32; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Seminars Virol., 7, pp. 381-388; Lázaro, C., Estivill, X., Mutation analysis of genetic diseases by asymmetric-PCR SSCP and ethidium bromide staining: Application to neurofibromatosis and cystic fibrosis (1992) Mol. Cell. Probes, 6, pp. 357-359; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet. Microbiol., 42, pp. 65-77; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , SIDDELL, S. G. (ed.): Plenum Press. New-York; Makino, S., Keck, J.G., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-739; Martell, M., Esteban, J.I., Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution (1992) J. Virol., 66, pp. 3225-3229; Motokava, K., Hohdatsu, T., Comparison of the aminoacid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-37; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Poland, A.M., Vennema, H., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34, pp. 3180-3184; Saitou, N., Nei, M., The neighbor-joining method: A new method for reconscructing phylogenetic trees (1987) Mol. Biol. Evol., 4, pp. 406-425; Tresnan, D.B., Levis, R., Holmes, K., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Vennema, H., De Groot, R., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J. Virol., 64, pp. 1407-1409; Vennema, H., Rossen, W.A., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140","István, K.; Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Article,"Final",,Scopus,2-s2.0-3743076418
"Gonon V.","6505953263;","Les coronavirus félins",1998,"Virologie","2","3",,"205","213",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2742530337&partnerID=40&md5=b279cc65fde529ed486ffa3f124c414e","URA INRA de Genet. Molec. et C., Ecl. Natl. Veterinaire d'Alfort, 7, avenue du General-de Gaulle, 94704 Maisons-Alfort, France","Gonon, V., URA INRA de Genet. Molec. et C., Ecl. Natl. Veterinaire d'Alfort, 7, avenue du General-de Gaulle, 94704 Maisons-Alfort, France","The feline coronaviruses, members of the family Coronaviridae are enveloped viruses which contain single-strand positive sense RNA. They replicate by a mechanism which results in a high frequency of recombination. Therefore, feline coronaviruses are pathogens of cats exhibiting a spectrum of virulence dependant on the strain. Some strains produce an asymptomatique infection, but others induce an immune-mediated and fatal systemic disease called feline infectious peritonitis (FIP). This paper briefly review the current knowledge about the molecular organization, the replication, the natural immunity and the transmission of feline coronaviruses. The knowledge of the pathogenesis of FIP is still incomplete but can explain the problem encountered to succeed in vaccinating cats against feline infectious peritonitis.","ADE; Cats; Coronaviruses; FIP; Molecular biology",,"Laude, H., Porcine respiratory coronavirus : Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Evermann, Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis Vet Microbiol, 28, pp. 243-255; Wege, H., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Olsen, C., A review of feline infectious peritonitis virus : Molecular biology, immunopathogenesis, clinical aspects and vaccination (1993) Vet Microbiol, 36, pp. 1-37; Hoskins, J.D., Coronavirus infection in cats (1993) Vet Clinics of North America : Small Animal Pract, 23, pp. 1-15; Holmes, K.V., Cornaviridae and their replication (1990) Virology, Second Edition, , edited by BN Fields. DM Knipe. et al. Raven Press. Ltd. New York; Scott, F., Transmission and epidemiology (1991) Proceedings of the Symposium, , jan. 11, Orlando, Florida; Lai, M.M.C., Coronaviruses : Organization, replication and expression of genome (1990) Annu Rev Microbiol, 44, pp. 303-330; Herrewegh, A.P., Detection of feline coronavirus RNA in feces, tissues and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Pedersen, N.C., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am J Vet Res, 45, pp. 2580-2585; Pedersen, N.C., Infection studies in kittens, using feline infectious peritonitis virus propagated in cell culture (1981) Am J Vet Res, 42, pp. 363-367; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus : FIPV-UCD2, FIPV-UCD3 and FIPV-UCD4 (1985) Compendium on Continuing Education for the Practicing Veterinarian, 7, pp. 1001-1011; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Coronaviruses, 218, pp. 529-550; Ingersoll, J., Wylie, D., Identification of viral antigens that induce antibody responses on exposure to Coronaviruses (1988) Am J Vet Res, 49, pp. 1467-1471; Ingersoll, J., Wylie, D., Comparison of serologic assays for measurement of antibody response to coronavirus in cats (1988) Am J Vet Res, 49, pp. 1472-1479; Reed, Cloning and sequence analysis of the spike gene from several feline coronaviruses (1993) Adv Exp Med Biol, 342, pp. 17-21; Fiscus, S.A., Terramoto, Y.A., Functional differences in the peplomer glycoproteins of feline coronavirus isolates (1987) J Virol, 61, pp. 2655-2657; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species - Specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Spaan, Coronaviruses : Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Weiss, R.C., Scott, F., Pathogenesis of feline infectious peritonitis : Nature and development of viremia (1981) Am J Vet Res, 42, pp. 382-390; Pedersen, N.C., Black, J.W., Attempted immunization of cats against feline infectious peritonitis, using avirulent live virus or sublethal amounts of virulent virus (1983) Am J Vet Res, 44, pp. 229-234; Corapi, Monoclonal antibody analysis of maturation and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J Virol, 66, pp. 6695-6705; Olsen, C., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J Virol, 66, pp. 956-965; Hohdatsu, T., A study on mechanism of antibody-dependent enhancement of FIPV infection in feline macrophages by monoclonal antibodies (1991) Arch Virol, 120, pp. 207-217; Porterfield, J.S., Antibody-dependent enhancement of viral infectivity (1986) AdvVirus Res, 31, pp. 335-355; Vennema, H., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409; Corapi, Localisation of antigemc sites of the S glycoprotein of feline infectious peritonitis virus involved in neutralisation and anti-body-dependent enhancement (1995) J Virol, 69, pp. 2858-2862; Barlough, J.E., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis Virus (1985) Can J Comp Med, 49, pp. 303-307; Evermann, J.F., Clinical update : Feline infectious peritonitis (1995) JAVMA., 206, pp. 1130-1134; Addie, D.D., Jarrett, O., A study of naturally occuring feline coronavirus infections in kittens (1992) Vet Rec, 130, pp. 133-137; Scott, F., Immunization against feline Coronaviruses (1987) Adv. in Expert Mental Medicine and Biology, 218, pp. 569-576. , Ed. Michael MC Lai and Stephen A Stohlman; Hayashi, T., Role of circulating antibodies in feline infectious peritonitis after oral infection (1983) Jpn J Vet Sci, 45, pp. 487-494; Pedersen, N.C., Boyle, J.E., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am J Vet Res, 41, pp. 868-876; Weiss, R.C., Scott, F., Pathogenesis of feline infectious peritonitis : Pathologic changes and immunofluorescence (1981) Am J Vet Res, 42, pp. 2036-2038; Kai, K., Humoral immune responses of cats to feline infectious peritonitis virus infection (1992) J Vet Med Sci, 54, pp. 501-507; Pedersen, N.C., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Am J Vet Res, 42, pp. 368-377; August, J.R., Feline infectious peritonitis, an immune-mediated coronaviral vasculitis (1984) Vet Clinics of North America : Small Animal Pract, 14, pp. 971-983; Weiss, R.C., Cox, N.R., Delayed-type hypersensitivity skin response associated with feline infectious peritonitis in two cats (1988) Res Vet Sci, 44, pp. 396-398; Hayashi, T., Role of thymus-dependent lymphocytes and antibodies in feline infectious peritonitis after oral infection (1983) Jpn J Vet Sci, 45, pp. 759-766; Weiss, R.C., Cox, N.R., Evaluation of immunity to feline infectious peritonitis in cats with cutaneous viral induced delayed hypersensitivity (1989) Vet Immunol and Immunopathol, 21, pp. 293-309; Addie, D.D., Jarrett, O., Risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) Am J Vet Res, 56, pp. 429-434; Woods, R.D., Pedersen, N.C., Cross protection studies between feline infectious peritonitis and porcine transmissible gastroenteritis (1976) Vet Microbiol, 4, pp. 11-16; Christianson, K.K., Characterization of a temperature sensitive feline infectious peritonitis coronavirus (1989) Arch Virol, 109, pp. 185-196; Postorino-Reeves, Longterm follow-up study of cats vaccinated with a temperature-sensitive feline infectious peritonitis vaccine (1992) Cornell Vet, 82, pp. 117-123; Scott, Evaluation of the safety and efficacy of Primucell-FIP vaccine (1992) Feline Health Topics, 7, pp. 6-8; Vennema, H., Primary structure of the membrane and nucleocapsid protein genes of FIPV and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virol, 181, pp. 327-335; Gonin, P., Evaluation of a replication-defective adenovirus expressing the feline infectious peritonitis membrane protein as a vaccine in cats (1996) Vaccine Research, 4, pp. 217-227; Stoddart, C.A., Attempted immunization of cats against feline infectious peritonitis using canine coronavirus (1988) Res Vet Sci, 45, pp. 383-388; Gerber, J.D., New perspectives on prevention of FIP (1991) Proceedings of the Symposium, , jan II, Orlando, Florida; Chalmers, W.S.K., Enhancement of FIP in cats immunised with vaccine virus recombinants expressing CCV and TGEVV spike glycoprotein (1994) Coronaviruses, , edited by H Laude and JF Vautherot. Plenum Press, New York; Escobar, J.C., Immunization of cats against FIP with anti-idiotypic antibodies (1992) Viral Immunol, 5, pp. 71-78","Gonon, V.; URA INRA de Genet. Molec. et C., Ecl. Natl. Veterinaire d'Alfort, 7, avenue du General-de Gaulle, 94704 Maisons-Alfort, France",,,12678694,,VIROF,,"French","Virologie",Article,"Final",,Scopus,2-s2.0-2742530337
"Laude H., Rasschaert D., Delmas B., Eleouët J.-F.","7006652624;7004067163;7003294168;6602581440;","Le coronavirus respiratoire porcin PRCV : Un virus émergent pas comme les autres",1998,"Virologie","2","4",,"305","316",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2442688627&partnerID=40&md5=270b50d638df9eb85b49f431cf9b20bd","U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France","Laude, H., U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France; Rasschaert, D., U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France; Delmas, B., U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France; Eleouët, J.-F., U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France","Since 1984, a previously unrecognized respiratory coronavirus. causing a mostly unapparent infection, has rapidly and massively spread within the swine population in Europe. A few years later, viruses with similar caracteristics have been identified in the USA. The agent, designated PRCV, appears to be derived from the porcine enteropathogenic virus TGEV. The aim of this review is to analyze the data regarding this new agent and the infection it induces, mainly from a molecular point of view. Indeed, such investigations have greatly contributed to elucidate the nature of the events involved in the emergence of PRCV. All the PRCV genotypes known to date are characterized by the presence of multiple deletions, one of each targets the gene encoding the spike protein. The study of this virus has undeniably brought new insights about the bases determining the tropism - either intestinal or respiratory - of this group of coronaviruses. some of which infect humans.","Coronavirus; Emerging virus; Enterotropism; Pneumotropism; Porcine respiratory coronavirus; PRCV; TGEV","Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Savey, M., Laude, H., Les diarrhées néo-natales d'origine virale chez le porc (1) (1979) Le Point Vétérinaire, 9, pp. 47-54; Laude, H., Savey, M., Les diarrhées néo-natales d'origine virale chez le pore (2) (1980) Le Point Vétérinaire, 10, pp. 83-89; Pensaert, M., Cox, E., Van Deun, K., Callebaut, P., A seroepizootiological study of the porcine respiratory coronavirus m the Belgian swine population (1993) Vet Quart, 15, pp. 16-20; Jestin, A., Leforban, Y., Vannier, P., Madec, F., Gourreau, J., Un nouveau coronavirus porcin. 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Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res Vet Sci, 48, pp. 165-169; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with pneumotropic porcine coronavirus (1989) Res Vet, 47, pp. 23-29; Cox, E., Pensaert, M., Callebaut, P., Van Deun, K., Intestinal replication of a porcine respiratory coronavirus antigenically closely related to transmissible gastroenteritis virus (1990) Vet Microbiol, 23, pp. 237-243; Duret, C., Brun, A., Guilmoto, H., Dauvergne, M., Isolement, identification et pouvoir pathogène chez le porc d'un coronavirus apparenté au virus de la gastro-enténte transmissible (1988) Recl Med Vet, 164, pp. 221-226; Onno, M., Jestin, A., Cariolet, R., Vannier, P., Rapid diagnosis of TGEV-like coronavirus in fattened pigs by indirect fluorescence labelling in nasal cells (1989) J Vet Med, B 36, pp. 629-634; Vannier, P., Disorders, induced by the experimental infection of pigs with the porcine respiratory coronavirus (1990) J Vet Med, B 37, pp. 117-180; 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New York : Plenum Press; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J Virol, 64, pp. 5367-5375; Delmas, B., Laude, H., Carbohydrate-induced conformational changes strongly modulate the antigenicity of coronavirus TGEV glycoproteins S and M (1991) Virus Res, 20, pp. 107-120; Vennema, H., Godeke, G.J., Rossen, J.W.A., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral protein genes EMBO J 1996 ; 15, pp. 2020-2028; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S J Gen Virol 1990 ; 71, pp. 1313-1323; Laude, H., Gelfi, J., Rasschaert, D., Delmas, B., Caractérisation antigénique du coronavirus respiratoire porcin à l'aide d'anticorps monoclonaux dirigés contre le virus de la gastro-entérite transmissible (1988) J Rech Porcine Fr, 20, pp. 89-94; Callebaut, P., Correa, I., Pensaert, M., Jimenez, G., Enjuanes, L., Antigenic differentiation between transmissible gastroenteritis virus of swine and a related porcine respiratory coronavirus (1988) J Gen Virol, 69, pp. 1725-1730; Callebaut, P., Pensaert, M., Hooyberghs, J., A competitive inhibition Elisa for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19; Page, K.W., Mawditt, K.L., Britton, P., Sequence comparison of the 5′ end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J Gen Virol, 72, pp. 579-587; Sanchez, C.M., Gebauer, F., Suné, C., Mendez, J., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Underdahl, N.R., Mebus, C.A., Torres-Medina A. Recovery of transmissible gastroenteritis virus from chronically infected experimental pigs (1975) Am J Vet Res, 36, pp. 1473-1476; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J Virol, 64, pp. 4761-4766; Britton, P., Kottier, S., Chen, C.M., Pocock, D.H., Salmon, H., Aynaud, J.M., The use of PCR genome mapping for the characterization of TGEV strains (1992) Coronaviruses : Molecular Biology and Virus-host Interactions, pp. 29-34. , Laude H and Vautherot JF, eds. New York : Plenum Press; Jacobs, L., De Groot, R., Van der Zeysl, B.A.M., Horzinek, M.C., Spaan, W., The nucleotide sequence of porcine transmissible gastroenteritis virus (TGEV) : Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res, 8, pp. 363-371; Duarte, M., Laude, H., Sequence of the spike protein of the porcine epidemic diarrhea virus (1994) J Gen Virol, 75, pp. 1195-1200; Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J Gen Virol, 76, pp. 2235-2241; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Yeager, C.L., Ashmun, R.A., Williams, R.K., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, H., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J Virol, 68, pp. 8008-8016; Delmas, B., Gelfi, J., Kut, E., Sjöström, H., Norén, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) J Virol, 68, pp. 5216-5224; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) J Gen Virol, 77, pp. 2515-2521; Delmas, B., Gelfi, J., Sjöström, H., Noren, O., Laude, H., Further characterization of amino-peptidase N as a receptor for coronaviruses (1992) Coronaviruses : Molecular Biology and Virus-host Interactions, pp. 293-298. , Laude H and Vautherot JF, eds. New York : Plenum Press; Laude, H., Gelfi, J., Aynaud, J.M., In vitro properties of low- and high-passaged strains of transmissible gastroenteritis coronavirus of swine (1981) Am J Vet Res, 42, pp. 447-449; Hansen, G.H., Delmas, B., Besriardeau, L., The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment (1998) J Virol, 72, pp. 527-534; Schultze, B., Krempl, C., Ballesteros, M.L., Transmissible gastroenteritis coronavirus. but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) J Virol, 70, pp. 5634-5637; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S proteins connect the sialic acid inding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J Virol, 71, pp. 3285-3287; Van Nieuwstadt, A.P., Zetstra, T., Boonstra, J., Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet Rec, 125, pp. 58-60; De Diego, M., Lavrada, M.D., Enjuanes, L., Escribano, J.M., Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J Virol, 66, pp. 6502-6508; Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-272; Paton, D.J., Brown, I.H., Sows infected in pregnancy with porcine respiratory coronavirus show no evidence of protecting their suckling piglets against transmissible gastroenteritis (1990) Vet Res Comm., 14, pp. 329-337; Bernard, S., Bottreau, E., Aynaud, J.M., Have, P., Szymansky, L., Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis (1989) Vet Microbiol, 21, pp. 1-8; Vaucher, Y.E., Ray, C.G., Minnich, L.L., Payne, C.M., Beck, D., Lowe, P., Pleomorphic. envelopped, virus-like particles associated with gastrointestinal illness in neonates (1982) J Infect Dis, 145, pp. 27-30; Chany, E., Moscovici, O., Lebon, P., Roussel, S., Association of coronavirus infection with neonatal necrotizing enterocolitis (1982) Pediatrics, pp. 209-214; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981","U. de Virologie Immunol. M., INRA, 78350 Jouy-en-Josas, France",,,12678694,,VIROF,,"French","Virologie",Article,"Final",,Scopus,2-s2.0-2442688627
"Leparc-Goffart I., Hingley S.T., Chua M.M., Phillips J., Lavi E., Weiss S.R.","57213052499;6701491322;7006092803;7404582468;7006986911;57203567044;","Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism",1998,"Journal of Virology","72","12",,"9628","9636",,60,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031771849&partnerID=40&md5=94daade37bb36c2a9fbb1864b2f09277","Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Department of Microbiology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States; Department of Pathology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Dept. of Microbiology, University of Pennsylvania, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States","Leparc-Goffart, I., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States, Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Hingley, S.T., Department of Microbiology, Philadelphia Coll. Osteopathic Med., Philadelphia, PA 19131, United States; Chua, M.M., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Phillips, J., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Lavi, E., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States, Department of Pathology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States, Dept. of Microbiology, University of Pennsylvania, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Previous studies of a group of mutants of the murine coronavirus mouse hepatitis virus (MHV)-A59, isolated from persistently infected glial cells, have shown a strong correlation between a Q159L amino acid substitution in the S1 subunit of the spike gene and a loss in the ability to induce hepatitis and demyelination. To determine if Q159L alone is sufficient to cause these altered pathogenic properties, targeted RNA recombination was used to introduce a Q159L amino acid substitution into the spike gene of MHV- A59. Recombination was carried out between the genome of a temperature- sensitive mutant of MHV-A59 (Alb4) and RNA transcribed from a plasmid (pFV1) containing the spike gene as well as downstream regions, through the 3' end, of the MHV-A59 genome. We have selected and characterized two recombinant viruses containing Q159L. These recombinant viruses (159R36 and 159R40) replicate in the brains of C57BL/6 mice and induce encephalitis to a similar extent as wild-type MHV-A59. However, they exhibit a markedly reduced ability to replicate in the liver or produce hepatitis compared to wild-type MHV- A59. These viruses also exhibit reduced virulence and reduced demyelination. A recombinant virus containing the wild-type MHV-A59 spike gene, wtR10, behaved essentially like wild-type MHV-A59. This is the first report of the isolation of recombinant viruses containing a site-directed mutation, encoding an amino acid substitution, within the spike gene of any coronavirus. This technology will allow us to begin to map the molecular determinants of pathogenesis within the spike glycoprotein.",,"amino acid; recombinant rna; virus rna; amino acid substitution; animal experiment; animal model; animal tissue; article; controlled study; demyelination; encephalitis; genetic recombination; mouse; murine hepatitis coronavirus; nonhuman; priority journal; temperature sensitive mutant; virus gene; virus hepatitis; virus recombinant; virus replication; Amino Acid Substitution; Animals; Base Sequence; Brain; Cell Line; Coronavirus Infections; Demyelinating Diseases; DNA Primers; Genes, Viral; Hepatitis, Viral, Animal; Liver; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Recombination, Genetic; Viral Envelope Proteins; Virulence; Virus Replication","Chambers, P., Pringle, C.R., Easton, A.J., Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins (1990) J. Gen. Virol., 71, pp. 3075-3080; DeGroot, R.J., Luytjes, W., Horzinek, M.C., Van Der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike proteins of coronaviruses (1987) J. Mol. Biol., 196, pp. 963-966; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Frana, M.F., Behnke, J.N., Sturman, S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Godfraind, C., Langreth, S., Cardellichio, C., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus (1995) Lab. Investig., 73, pp. 615-627; Gombold, J.L., Hingely, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gombold, J.L., Sutherland, R., Lavi, E., Paterson, Y., Weiss, S.R., Mouse hepatitis virus-induced demyelination can occur in the absence of CD8+ T cells (1995) Microb. Pathog., 18, pp. 211-221; Higuchi, R., (1990) PCR Protocols: A Guide to Methods and Applications, pp. 177-183. , Academic Press, San Diego, Calif; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Joseph, J., Kim, R., Siebert, K., Lublin, F.D., Offenbach, C., Knobler, R.L., Organ specific endothelial cell heterogeneity influences differential replication and cytopathogenicity of MHV-3 and MHV-4 (1995) Corona- and Related Viruses, pp. 43-50. , P. J. Talbot and G. A. Levy (ed.), Plenum Press, New York, N.Y; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the murine coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5404-5410; Lavi, E., Fishman, P.S., Highkin, M.K., Weiss, S.R., Limbic encephalitis after inhalation of a murine coronavirus (1988) Lab. Investig., 58, pp. 31-36; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M.C., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab. Investig., 62, pp. 570-578; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein (1997) Virology, 239, pp. 1-10; Luytjes, W., Sturman, L., Bredenbeek, P.J., Charite, J., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Martin, J.P., Chen, W., Koehren, F., Pereira, C.A., The virulence of mouse hepatitis virus 3, as evidenced by permissivity of cultured hepatic cells toward escape mutants (1994) Res. Virol., 145, pp. 297-302; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoproteins of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Peng, D., Koetzner, C.A., McMahon, T., Zhao, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Ramig, R.F., Isolation and genetic characterization of temperature sensitive mutants of simian rotavirus SA11 (1982) Virology, 120, pp. 93-135; Reed, L.J., Muench, H., A simple method of estimating fifty per cent points (1938) Am. J. Hyg., 27, pp. 493-497; Suzuki, H., Taguchi, F., Analysis of the receptor-binding site of murine coronavirus spike protein (1996) J. Virol., 70, pp. 2632-2635; Taguchi, F., Kawamura, S., Fujiwara, K., Replication of mouse hepatitis viruses with high and low virulence in cultured hepatocytes (1983) Infect. Immun., 39, pp. 955-959; Zhang, L., Homberger, F., Spaan, W., Luytjes, W., Recombinant genomic RNA of coronavirus MHV-A59 after co-replication with a di RNA containing the MHV-RI spike gene (1997) Virology, 230, pp. 93-102","Weiss, S.R.; Dept. of Microbiology, University of Pennsylvania, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"9811696","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0031771849
"Collins A.R.","24439435400;","Human macrophages are susceptible to coronavirus OC43",1998,"Advances in Experimental Medicine and Biology","440",,,"635","639",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783817&partnerID=40&md5=d952e333c32c145b55c72c575b360156","Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY 14214, United States","Collins, A.R., Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY 14214, United States","Adherent adult and cord blood macrophages were infected with human coronavirus OC43 at a multiplicity of 1-1.5 and washed twice to remove unbound virus. Virus progeny was detected in the supernatant on day 1 and peaked at 2-3 days at an average titer of 5±3.9 × 106 pfu/ml from seven samples. Viral RNA was detected by nested set RT-PCR in infected macrophages incubated for 48 hr. Intracellular viral nucleocapsid was detected in 15% of the cells and surface staining for viral spike antigen was observed using monoclonal antibodies. Amplification of infectious virus and detection viral RNA and antigen synthesis in macrophages in vitro indicates susceptibility to OC43 virus.",,"virus antigen; virus rna; article; coronavirus; human; human cell; infection sensitivity; macrophage; priority journal; reverse transcription polymerase chain reaction; umbilical cord blood; virus nucleocapsid; Adult; Coronavirus; Coronavirus OC43, Human; Humans; Macrophages; Coronavirus; human coronavirus","Becker, S., Koren, H.S., Henke, D.C., Interleukin-8 expression in normal nasal epithlelium and its modualtion by infection with respiratory syncytial virus and cytokines tumor necrosis factor, interleukin-I and interleukin-6 (1993) Amer. J. Resp. Cell. Mol. Biol., 8, pp. 20-27; Bonavia, A., Arbour, N., Yong, V.W., Talbot, P.J., Infection of primary cultures ofhuman neural cells by human coronavirus 229E and OC43 (1997) J. Virol., 71, pp. 800-806; Collins, A.R., Sorenson, O., Regulation of viral persistence in human glioblastoma and rhabdosarcoma cells infected with coronavirus OC43 (1986) Microb. Path., 1, pp. 573-582; Collins, A.R., Interferon gamma potentiates human coronavirus infection of neuronal cells by modulation of HLA class I (1995) Immunol. Invest., 24, pp. 977-986; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Mc Intosh, K., Coronaviruses (1996) Fundamental Virology, pp. 1093-1103. , B.N. Fields, D.M. Knipe, R.M. Chanok, M. S. Hirsch, J.L. Melnick, T.P. Monath, B. Roizman, eds., Raven, Philadelphia; Midulla, F., Huang, Y.T., Gilbert, I.A., Respiratory syncytial virus infection of human cord and adult blood monocytes and alveolar macrophages (1989) Amer Rev. Res. Dis., 140, pp. 771-777; Myint, S., Johnson, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronavirus 229E and OC43 (1994) Molec. Cell. Probes, 8, pp. 357-361; Talbot, P.J., Cote, G., Arbour, N., Human coronavirus OC43 and 229E persistence in neural cell cultures and human brains (1997) Adv. Exp. Med. Biol., , In press; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common cold virus in organ culture (1965) Br. Med. J., 1, pp. 1467-1470","Collins, A.R.; Department of Microbiology, School of Medicine and Biomedical Sciences, State University of New York at Buffalo, Buffalo, NY 14214, United States",,,00652598,,AEMBA,"9782339","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783817
"Liu D.X., Xu H.Y., Lim K.P.","8972667300;55703819800;7403175857;","Regulation of mRNA 1 expression by the 5′-untranslated region (5′-UTR) of the coronavirus Infectious Bronchitis Virus (IBV)",1998,"Advances in Experimental Medicine and Biology","440",,,"303","311",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031753727&partnerID=40&md5=a4310e910da391a98b2a55a7e775e262","Institute of Molecular Agrobiology, National University of Singapore, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, National University of Singapore, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Lim, K.P., Institute of Molecular Agrobiology, National University of Singapore, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","In this report, we show that expression of the coronavirus IBV mRNA1 is regulated by its 5′-UTR. Evidence presented domonstrates that the IBV sequence from nucleotide 1 to 1904 directs very inefficient synthesis of a product of approximately 43 kDa. Deletion of either the first 362 bp or the whole part of the 5′-UTR, however, dramatically increased the expression of the 43 kDa protein species. The mechanisms involved were investigated by two different approaches. Firstly, translation of the same construct in the presence of [3H]-leucine ruled out the possibility that initiation of small reading frames from non-AUG codons located in the 5′-UTR may compete with the authentic AUG initiation codon, and therefore inhibit the expression of ORF 1a. Secondly, expression and deletion analyses of a dicistronic construct showed that translation of the 43 kDa protein was initiated by ribosome internal entry mechanism. These studies suggest that a 'weak' ribosome internal entry signal is located in the 5′-UTR and is involved in the regulation of mRNA1 expression.",,"article; coronavirus; gene expression regulation; messenger rna synthesis; nonhuman; priority journal; protein expression; strain difference; transcription initiation; virus expression; 5' Untranslated Regions; Animals; Codon, Initiator; Gene Expression Regulation, Viral; Infectious bronchitis virus; Protein Biosynthesis; Reading Frames; RNA Caps; RNA, Messenger; RNA, Viral; Viral Proteins; Avian infectious bronchitis virus; Coronavirus","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO. J., 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Contreras, R., Cheroutre, H., Degrave, W., Fiers, W., Simple efficient in vitro synthesis of capped RNA useful for direct expression of cloned DNA (1982) Nucleic Acids Res., 10, pp. 6353-6362; Gorbalenya, A.E., Koonin, E.Y., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Research, 17, pp. 4847-4860; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Liu, D.X., Inglis, S.C., Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus (1992) J. Virol., 66, pp. 6142-6154; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression and processing of an 87 kDa polypeptide encoded by ORFIa of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5 (1994) J. Gen. Virol., 75, pp. 3041-3046","Liu, D.X.; Institute of Molecular Agrobiology, National University of Singapore, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore",,,00652598,,AEMBA,"9782297","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031753727
"Wege H., Stühler A., Lassmann H., Wege H.","7005516649;6602388166;35420677900;7005516646;","Coronavirus infection and demyelination: Sequence conservation of the S-gene during persistent infection of Lewis-rats",1998,"Advances in Experimental Medicine and Biology","440",,,"767","773",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783438&partnerID=40&md5=b876800b5de457444aefd3f7f99e6fc5","Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany; Ludwig Institute for Cancer Research, London W2 1PG, United Kingdom; Institute of Neurology, A-1090 Vienna, Austria","Wege, H., Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany; Stühler, A., Ludwig Institute for Cancer Research, London W2 1PG, United Kingdom; Lassmann, H., Institute of Neurology, A-1090 Vienna, Austria; Wege, H., Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany","Coronaviruses display a large phenotypic variability, which may be an important factor for diversification and selection. Previous studies have demonstrated that the S-protein is an essential determinant of virulence and pathogenicity. Therefore we studied the S-gene as an indicator molecule for selection processes employing two different MHV-JHM variants. First, Lewis-rats were infected with MHV-JHM-Pi, a variant that causes demyelinating disease after several weeks p. i. It was not possible to isolate infectious MHV-JHM-Pi from such rats, although viral proteins were expressed. The S-gene was rescued directly from brain tissue employing RT-PCR technology. The amplicons were sequenced in bulk or at the level of single clones. We detected no evidence for an increase of S-gene mutants during the length of time. Only few mutations were found at the clonal level. The changes were distributed throughout the analysed S-gene fragments without a predilection in their location. The frequency of mutation remained low within a range of 0.03 to 0.5 mutations per thousand nucleotides. As a second approach, we sequenced the S-genes of viruses isolated from brain tissue infected with MHV-JHM-ts43. Infection of adult Lewis rats with that mutant resulted several weeks to months p.i. in demyelinating encephalomyelitis. The S-gene of this virus contains an insertion of 423 bp in the S1 region, which is identical to a polymorphic region described for MHV-4. In contrast to JHM-Pi, infectious MHV-JHM-ts43 was readily to isolate from brain tissue. The S-gene sequences of virus isolated 45-106 days p.i. from diseased rats were identical with that of the input virus. These results show, that during a persistent infection of Lewis-rats the S-gene was highly conserved.",,"animal model; animal tissue; article; demyelinating disease; gene insertion; gene sequence; murine hepatitis coronavirus; nonhuman; persistent virus infection; priority journal; rat; reverse transcription polymerase chain reaction; rna virus infection; virus gene; virus mutation; virus pathogenesis; virus virulence; Animals; Cell Line; Coronavirus Infections; Demyelinating Diseases; Membrane Glycoproteins; Mice; Murine hepatitis virus; Rats; Rats, Inbred Lew; Variation (Genetics); Viral Envelope Proteins; Virulence; Virus Latency; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus strain 4; RNA viruses","Adami, C., Pooly, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virologi, 209, pp. 337-346; Banner, L.R., Keck, G.K., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virol., 175, pp. 548-555; Barac-Latas, V., Suchanek, G., Breitschopf, H., Stühler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in coronavirus induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, 19, pp. 1-12; Baric, R., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. Virol., 71, pp. 1946-1955; Baybutt, H.N., Wege, H., Carter, M.J., Ter Meulen, V., Adaptation of coronavirus JHM to persistent infection of murine Sac(-) cells (1984) J. Gen. Virol., 65, pp. 915-924; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alterations of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the aminoterminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Holland, J.J., Genetic diversity of RNA viruses (1992) Curr. Top. Microbiol. Immunol., 176. , Springer-Verlag, Berlin-Heidelberg-New York; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Kottier, S., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virologi, 213, pp. 569-580; Lamonica, N., Banner, L.R., Morris, V.L., Lai, M.M.C., Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM (1991) Virol., 182, pp. 883-888; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virologi, 173, pp. 664-673; Pewe, L., Wu, F.G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Rowe, C.L., Fleming, J.O., Nathan, M.J., Sgro, J.-Y., Palmenberg, A., Baker, S.C., Generation of coronavirus spike deletion variants by high-frequency recombination at regions of predicted RNA secondary structure (1997) J. Virol., 71, pp. 6183-6190; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterization of spike deletion variants during persistent infection (1997) J. Virol., 71, pp. 2959-2969; Schmidt, I., Skinner, M.A., Siddell, S.G., Nucleotide sequence of the gene encoding the surface projection glycoprotein of the coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Smith, D.B., McAllister, J., Casino, C., Simmonds, P., Virus ""quasispecies"": Making a mountain out of a molehill? (1997) J. Gen. Virol., 78, pp. 1511-1519; Stühler, A., Flory, E., Wege, H., Lassmann, H., Wege, H., No evidence for quasispecies populations during persistence of the coronavirus mouse hepatitis virus JHM: Sequence conservation within the surface glycoprotein gene S in Lewis rats (1997) J. Gen. Virol., 78, pp. 747-756; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Semin. Immunopathol., 17, pp. 133-148; Wege, H., Watanabe, R., Ter Meulen, V., Relapsing subacute demyelinating encephalomyelitis in rats in the course of coronavirus JHM infection (1984) J. Neuroimmunol., 6, pp. 325-336; Wege, H., Koga, M., Watanabe, R., Nagashima, K., Ter Meulen, V., Neurovirulence of murine coronavirus JHM temperature sensitive mutants in rats (1983) Infect. Immun., 39, pp. 1316-1324; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98","Wege, H.; Institute of Diagnostic Virology, Federal Research Centre for Virus Diseases of Animals, Friedrich-Loeffler-Institutes, D-17498 Isle of Riems, Germany",,,00652598,,AEMBA,"9782356","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783438
"Ng L.F.P., Liu D.X.","7201477950;8972667300;","Further characterisation of the coronavirus IBV ORF 1a products encoded by the 3C-like proteinase domain and the flanking regions",1998,"Advances in Experimental Medicine and Biology","440",,,"161","171",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031720729&partnerID=40&md5=9cd34986da8b4d2a4a164f75bc8b3aee","Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","Ng, L.F.P., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore; Liu, D.X., Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore","Coronavirus IBV encodes a piconarvirus 3C-like proteinase. In a previous report, this proteinase was shown to undergo rapid degradation in vitro in reticulocyte lysate due to a posttranslational event involving ubiquitination of the protein. Several lines of evidence presented here indicate that the proteinase itself is stable. Translation of the IBV sequence from nucleotide 8864 to 9787 resulted in the synthesis of a 33 kDa protein, representing the full-length 3C-like proteinase. Pulse-chase and time-course experiments showed that this protein was stable in reticulocyte lysate for up to 2 hours. However, a 45 kDa protein encoded by the IBV sequence from nucleotide 8693 to 9911 underwent rapid degradation in reticulocyte lysate, but was stable in wheat germ extract, suggesting that an ATP-dependent protein degradation pathway may be involved in the turnover of the 45 kDa protein. To identify the IBV sequence responsible for the instability of this 45 kDa protein species, the region from nucleotide 8693 to 9787 was translated both in vitro and in vivo , leading to the synthesis of a stable 43 kDa protein. These results suggest that a destabilising signal may be located in the IBV sequences between the nucleotides 9787 and 9911. Meanwhile, protein aggregation was observed when the product encoded by the IBV sequence from nucleotide 9911 to 10510 was boiled for 5 minutes before being analysed in SDS-PAGE; when the same product was treated at 37°C for 15 minutes, however, protein aggregation was not detected. Deletion studies indicate that the presence of a hydrophobic domain downstream of the 3C-like proteinase-encoding region may be the cause for the aggregation of the product encoded by this region of ORF 1a.",,"proteinase; animal cell; article; cell lysate; coronavirus; dna flanking region; nonhuman; priority journal; protein degradation; protein domain; reticulocyte; virus characterization; virus detection; virus replication; Animals; Cercopithecus aethiops; Cysteine Endopeptidases; Gene Expression; Infectious bronchitis virus; Rabbits; Vero Cells; Viral Proteins; Animalia; Avian infectious bronchitis virus; Coronavirus; Triticum aestivum","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Brierley, I., Boursnell, M.E.G., Binns, M.M., Billimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO. J., 6, pp. 3779-3785; Contreras, R., Cheroutre, H., Degrave, W., Fiers, W., Simple efficient in vitro synthesis of capped RNA useful for direct expression of cloned DNA (1982) Nucleic Acids Res., 10, pp. 6353-6362; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8127; Gorbalenya, A.E., Koonin, E.Y., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4860; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100 kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87 kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Brown, T.D.K., Characterisation and mutational analysis of an ORF- 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10 kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 48-57; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., A region of the infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate (1995) J. Gen. Virol., 76, pp. 3059-3070","Ng, L.F.P.; Institute of Molecular Agrobiology, 59A The Fleming, 1 Science Park Drive, Singapore 118240, Singapore",,,00652598,,AEMBA,"9782278","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031720729
"Martin S.W., Nagy É., Shewen P.E., Harland R.J.","7404840647;57203079361;7004642090;7103070905;","The Association of Titers to Bovine Coronavirus with Treatment for Bovine Respiratory Disease and Weight Gain in Feedlot Calves",1998,"Canadian Journal of Veterinary Research","62","4",,"257","261",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032177488&partnerID=40&md5=02dfabf5c03616a1e6b01c4f6586adc4","Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Vet. Infectious Disease Organization, Saskatoon, Sask., Canada","Martin, S.W., Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Nagy, É., Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Shewen, P.E., Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Harland, R.J., Vet. Infectious Disease Organization, Saskatoon, Sask., Canada","The association between bovine respiratory disease (BRD) and antibody titers to bovine coronavirus (BCV) was studied in 604 calves (19 different groups in 4 different feedlots from 2 provinces). Almost all calves had antibody titers on arrival in the Alberta feedlot and 82% of the calves had an antibody titer on arrival at the Ontario feedlots; titers in calves in Alberta were almost twice as high as those in calves in Ontario. The incidence of infection, in the first mo after arrival as judged by seroconversion, ranged from 61% to 100%; titer increases were much greater in calves in Ontario feedlots. Titer variables were not significantly related to BRD, except on a withingroup basis (group was a confounding variable for BCV-BRD associations). Given control of group effects, calves with an antibody titer on arrival appeared to be protected against BRD for the first 28 d in the feedlot, and the association was reasonably linear over the range of titers. Each titer unit on arrival decreased the risk of BRD by about 0.8X (odds ratio). Titer change was not strongly related to the risk of BRD and the relationship was not linear over the range of titer changes. Titer change was strongly and negatively correlated with titer on arrival, and titer change was not significantly related to BRD in the presence of arrival titers. Arrival titer retained its relationship with BRD in the presence of titer data for other putative pathogens. Each higher unit of titer to BCV on arrival increased the 28-day weight gain (controlling for group, initial weight and the occurrence of BRD) by slightly more than 1 kg. Titer change was associated with decreased weight gain, when initial titer was not in the model. The lack of a linear or multivariable association between BCV titer change and BRD, and weight gain, may indicate that BCV is not a major pathogen; or, its lack of significance may merely be due to its strong correlation with arrival titer. Given the associations found in this study, particularly the interprovincial differences in arrival titers, more and different approaches to studying the possible effects of BCV on BRD are in order.",,"virus antibody; animal; animal disease; article; cattle; cattle disease; Coronavirus; immunology; isolation and purification; pathogenicity; regression analysis; respiratory tract infection; risk factor; virology; virus infection; weight gain; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Regression Analysis; Respiratory Tract Infections; Risk Factors; Weight Gain","Carman, P.S., Hazlett, M.J., Bovine coronavirus infection in Ontario 1990-1991 (1992) Can Vet J, 33, pp. 812-814; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208 (9), pp. 1452-1455; Martin, S.W., Harland, R.J., Bateman, K.G., Nagy, É., The Association of Titers to Haemophilus somnus, and Other Putative Pathogens, with the Occurrence of Bovine Respiratory Disease and Weight Gain in Feedlot Calves (1998) Can J Vet Res, 62, pp. 262-267; Allen, J.W., Viel, L., Batemen, K.G., Nagy, É., Rosendal, S., Shewen, P.E., Serological titers to bovine herpesvirus 1, bovine viral diarrhea virus, parainfluenza 3 virus, bovine respiratory syncytial virus and Pasteurella haemolytica in feedlot calves with respiratory disease: Associations with bacteriological and pulmonary cvtological variables (1992) Can J Vet Res, 56, pp. 281-1188; Harland, R.J., Potter, A.A., Van-Den Hurk-Vandrunen-Littel, S., Van Donkersgoed, J., Parker, M.D., Zamb, T.J., Janzen, E.D., The effect of subunit or modified live bovine herpesvirus-1 vaccines on the efficacy of a recombinant Pasteurella haemolytica vaccine for the prevention of respiratory disease in feedlot calves (1992) Can Vet J, 33, pp. 734-741; Shewen, P.E., Wilkie, B.N., Vaccination of calves with leukotoxic culture supernatant from Pasteurella haemolytica (1988) Can J Vet Res, 52, pp. 30-36; Walter, S.D., Feinstein, A.R., Wells, C.K., Coding ordinal independent variables in multiple regression analyses (1987) Am J Epidemiol, 125 (2), pp. 319-323; Ganaba, R., Belanger, D., Dea, S., Bigras-Poulin, M., A seroepidemiological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from northwestern Quebec (1995) Can J Vet Res, 59, pp. 26-33; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet Microbiol, 22 (2-3), pp. 187-201; Meckert, R.A., Saif, L.J., Myers, G.W., Agnes, A.G., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am J Vet Res, 52 (6), pp. 845-851; Heckert, R.A., Saif, L.J., Mengel, J.P., Myers, G.W., Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces, and mucosal secretions from experimentally challengeexposed colostrum-deprived calves (1991) Am J Vet Res, 52 (5), pp. 692-6999","Martin, S.W.; Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada",,,08309000,,CJVRE,"9798090","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0032177488
"Morović M., Barac-Latas V.","6603937208;6506163291;","Postinfectious and postvaccination encephalomyelitis [Postinfekcijski i postimuniza cijski encefalomijelitis]",1998,"Paediatria Croatica, Supplement","42","1",,"101","105",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-34247526831&partnerID=40&md5=d9b36654b55b5fa65f2e7410cc628c64","Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Zavod za Fiziologiju I Imunologiju, Croatia; Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Cambierieva 17, 51000 Rijeka, Croatia","Morović, M., Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Zavod za Fiziologiju I Imunologiju, Croatia, Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Cambierieva 17, 51000 Rijeka, Croatia; Barac-Latas, V., Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Zavod za Fiziologiju I Imunologiju, Croatia","Epidemiological and clinicopathological characteristics of postinfectious and postvaccination encephalomyelitis are briefly outlined. Also the main similarities between this serious neurological syndrome in humans and those found in our model of experimental allergic encephalomyelitis induced by the murine coronavirus MHV-JHM are presented. For both of the diseases immune-mediated demyelination is the most probable pathogenetic mechanism.","Encephalomyelitis; MHV-JHM coronavirus; Postinfectious; Postvaccination","virus vaccine; allergic encephalomyelitis; conference paper; Coronavirus; human; nonhuman; pathogenesis; postvaccinal encephalitis; prevalence","Johnson, R.T., Acute encephalitis (1996) Clin Infect Dis, 23, pp. 219-226; Khan, S., Yaqub, B.A., Poser, C.M., al Deeb, S.M., Bohlega, S., Multiphasic disseminated encephalomyelitis presenting as alternating hemiplegia (1995) J Neurol Neurosurg Psychiatry, 58, pp. 467-470; Mancini, J., Chabrol, B., Moulene, E., Pinsard, N., Relapsing acute encephalopathy: A complication of diphteria-tetanus-poliomyelitis immunization in a young boy (1996) Eur J Pediatr, 155, pp. 136-138; Jubelt, B., Miller, J.R., Viral infections (1995) Merritt's textbook of Neurology, pp. 142-179. , Rowland LP, ur, 9.izd. Baltimore:Williams and Wilkins; Yamamoto, K., Takayanagi, M., Yoshikara, Y., Acute disseminated encephalomyelitis associated with Mycoplasma pneumoniae infection (1996) Arch Paediatr Jpn, 38, pp. 46-51; Pellegrini, M., O'Brien, T.J., Hoy, J., Sedal, L., Mycoplasma pneumoniae infection associated with an acute brain stem syndrome (1996) Acta Neurol Scand, 93, pp. 203-206; Kanzaki, A., Yabuki, S., Acute disseminated encephalomyelitis (ADEM) associated with cytomegalovirus infection - a case report (1994) Rinsho Shinkeigaku, 34, pp. 511-513; Evans, G., Vaccine liability and safety: A progress report (1996) Pediatr Infect Dis J, 15, pp. 477-478; Neff, J.M., Variola (Smallpox) and monkeypox viruses (1995) Principles and Practice of Infectious Diseases, pp. 1328-1329. , Mandell GL, Bennett JE, Dolin R, ur, 4, izd. New York: Churchill Livingstone; Hamachudha, T., Rabies (1989) Mc Kendall RR, izd. Handbook of Clinical Neurology, 12 (56), pp. 383-404. , Amsterdam: Elsevier Science Publishers BV; Crowley, S., Al'Jawad, S.T., Kovar, I.Z., Mumps, measles, and rubella vaccination and encephalitis (1989) Brit Med J, 299, p. 660; Nalin, D.R., Mumps, measles, and rubella vaccination and encephalitis (1989) Brit Med J, 299, p. 1219; Ohtaki, E., Murakami, Y., Komori, H., Yamashita, Y., Matsuishi, T., Acute disseminated encephalomyelitis after Japanese B encephalitis vaccination (1992) Pediatr Neurol, 8, pp. 137-139; Jennings, A.D., Gibson, C.A., Miller, B.R., Analysis of a yellow fever virus isolated from a fatal case of vaccine-associated human encephalitis (1994) J Infect Dis, 169, pp. 512-518; Abdennebi, A., Dumas, J.L., Salama, J., Benromdhane, H., Belin, C., Goldlust, D., Postvaccination myelitis. Aspects and course followed by MRI (1996) J Radiol, 77, pp. 363-366; Sunaga, Y., Hikima, A., Ostuka, T., Morikawa, A., Acute cereblar ataxia with normal MRI lesions after varicella vaccination (1995) Pediatr Neurol, 13, pp. 340-342; Cowan, L.D., Griffin, M.R., Howson, C.P., Acute encephalopathy and chronic neurologic damage after pertussis vaccine (1993) Vaccine, 11, pp. 1371-1379; Cherry, J.D., Historical review of pertussis and the classical vaccine (1996) J Infect Dis, 174 (SUPPL. 3), pp. S259-S263; Murphy, J., Austin, J., Spontaneous infection or vaccination as a cause of acute disseminated encephalomyelitis (1985) Neuroepidemiology, 4, pp. 138-145; Ter Meulen, V., Massa, P.T., Dorries, R., Corona viruses (1989) Handbook of Clinical Neruology, 12 (56), pp. 439-451. , Mc Kendall RR, ur, Amsterdam: Elsevier Science Publishers BV; Hauser, S.L., Goodkin, D.E., Multiple sclerosis and other demyelinating diseases. U: Fauci AS, Braunwald E, Isselbacher KJ i sur, ur (1998) Harrison's Principles of Internal Medicine, pp. 2409-2419. , 14. izd. New York: Mc Graw-Hill; Barac-Latas, V., (1995) Morfološka i imunološka istraživanja u koronavirus induciranom demijelinizirajućem encefalomijelitisu, , Doktorska disertacija, Rijeka; Barac-Latas, V., Suchanek, G., Breitschope, H., Stuehler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in corona-induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, 19, pp. 1-12; Whitley, R.J., Cobbs, C.G., Alford Jr, C.A., Diseases that mimic herpes simplex encephalitis: Diagnosis, presentation and outcome (1989) JAMA, 262, pp. 234-239; Johnson, R.T., The pathogenesis of acute viral encephalitis and postinfectious encephalomyelitis (1987) J Infect Dis, 155, pp. 359-364; Weller, R.O., Engrelhardt, B., Phillips, M.J., Lymphocyte targeting of the central nervous system: A review of afferent and efferent CNS-immune pathways (1996) Brain Pathol, 6, pp. 275-288; Berger, T., Weerth, S., Kojima, K., Linington, C., Wekerle, H., Lassmann, H., Experimental autoimmune encephalomyelitis: The antigen specifity of T lymphocytes determines the topography of lesions in the central and peripheral nervous system (1997) Lab Invest, 76, pp. 355-364; Hartung, H.P., Riechmann, P., Pathogenesis of immune mediated demyelination in the CNS (1997) J Neural Transm Suppl, 50, pp. 173-181; Woody, R.C., Steele, R.W., Charlton, R.K., Smith, V., Histocompatibility determinants in childhood postinectious encephalomyelitis (1989) J Child Neurol, 4, pp. 204-207; Tselis, A.C., Lisak, R.P., Acute disseminated encephalomyelitis and isolated central nervous system demielinative syndromes (1995) Curr Opin Neurol, 8, pp. 227-229; Orrell, R.W., Grand rounds-Hammersmith Hospitals. Distinguishing acute disseminated encephalomyelitis from multiple sclerosis (1996) Brit Med J, 313, pp. 802-804; Kesselring, J., Miller, D.H., Robb, S.A., Acute disseminated encephalomyelitis: MRI findings and the distinction from multiple sclerosis (1990) Brain, 113, pp. 291-302; Tenorio, G., Whitaker, J.N., Steroid-dependent postvaricella encephalomyelitis (1991) J Child Neurol, 6, pp. 45-48; Sticker, R.B., Miller, R.G., Kiprov, D.D., Role of plasmapheresis in acute disseminated (postinfectious) encephalomyelitis (1992) J Clin Apheresis, 7, pp. 173-179; Kanter, D.S., Horensky, D., Sperling, R.A., Kaplan, J.D., Malachowski, M.E., Churchill Jr., W.H., Plasmapheresis in fulminant acute disseminated encephalomyelitis (1995) Neurology, 45, pp. 824-827","Morović, M.; Klinički Bolnički Centar Rijeka, Klinika za Infektivne Bolesti, Cambierieva 17, 51000 Rijeka, Croatia",,,1330724X,,,,"Croatian","Paediatr. Croat.",Conference Paper,"Final",,Scopus,2-s2.0-34247526831
"Hsue B., Masters P.S.","7801347035;7006234572;","An essential secondary structure in the 3′ untranslated region of the Mouse Hepatitis Virus genome",1998,"Advances in Experimental Medicine and Biology","440",,,"297","302",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031721308&partnerID=40&md5=a16bdecffa1cf217e20afd2d9f6c646d","David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States","Hsue, B., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States; Masters, P.S., David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States","The 3′ untranslated regions (3′ UTRs) of coronaviruses contain the signals necessary for negative strand RNA synthesis and may also harbor elements essential for positive strand replication and subgenomic RNA transcription. The 3′ UTRs of mouse hepatitis virus (MHV) and bovine coronavirus (BCV) are more than 30% divergent. In an effort to learn what parts of these regions might be functionally interchangeable, we attempted to replace the 3′ UTR of MHV with its BCV counterpart by targeted RNA recombination. Initially, we tried to substitute the 3′ 267 nucleotides (nt) of the 301 nt MHV 3′ UTR with the corresponding region of the BCV 3′ UTR. This exchange did not yield viable recombinant viruses, and the donor DI RNA was shown to be unable to replicate with MHV as a helper virus. Subsequent analysis revealed that the entire BCV 3′ UTR could be inserted into the MHV genome in place of the entire MHV 3′ UTR. It resulted that the failure of the initial attempted substitution was due to the inadvertent disruption of an essential conserved bulged stem-loop secondary structure in the MHV and BCV 3′ UTRs immediately downstream of the N gene stop codon.",,"virus rna; article; gene sequence; murine hepatitis coronavirus; nonhuman; priority journal; rna transcription; sequence analysis; stop codon; structure analysis; virus genome; virus recombination; virus replication; 3' Untranslated Regions; Animals; Cattle; Genome, Viral; L Cells (Cell Line); Mice; Murine hepatitis virus; Nucleic Acid Conformation; RNA, Viral; Bovinae; Bovine coronavirus; Coronavirus; Murinae; Murine hepatitis virus","Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; Hsue, B., Masters, P.S., A bulged stem-loop structure in the 3′ untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J. Virol.; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Urology, 197, pp. 53-63; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Lin, Y.-J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.-J., Liao, C.-L., Lai, M.M.C., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68, pp. 8131-8140; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Peng, D., Koetzner, C.A., Masters, P.S., Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination (1995) J. Virol., 69, pp. 3449-3457; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Stemmer, W.P.C., Rapid evolution of a protein in vitro by DNA shuffling (1994) Nature, 370, pp. 389-391; Stemmer, W.P.C., DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 10747-10751; Van Der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propogation of defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751","Hsue, B.; David Axelrod Institute, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201-2002, United States",,,00652598,,AEMBA,"9782296","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031721308
"Schelcher F., Bichet H., Valarcher J.-F., Foucras G., Bouisset S.","7006601789;6602968267;6603528818;6701596308;57214029091;","Vaccination against diarrhoeic gastroenteritis in the new-born calf : What to expect ? [Les vaccinations contre les gastroentérites diarrhéiques du veau nouveau-né : Que peut-on en attendre ?]",1998,"Point Veterinaire","29","189",,"35","42",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032367997&partnerID=40&md5=159f5820fae1b40e1c185d1074158cc8","Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France; Réseau Vega, rue Las Escoumes, 09000 Foix, France","Schelcher, F., Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France; Bichet, H., Réseau Vega, rue Las Escoumes, 09000 Foix, France; Valarcher, J.-F., Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France; Foucras, G., Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France; Bouisset, S., Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France","Coronavirus, rotavirus, BVD virus, E. coli and salmonella' and often their association represent the main agents of diarrhoeic gastroenteritis of the new-born calf, and are part of a vaccination programme in bovine herds. The antigenic diversity, as well as some physiological features of the new-born calf's immunity, raises problems in the elaboration of a vaccine. The vaccines car be administered to the calf or it's mother (passive transfer of immunity to the calf) (1 photo, 7 tables, 5 boxes, 62 references).","Calf; Diarrhoea; Gastro-enterology; Vaccine",,"Archambaul, T.D., Immune response of pregnant neifers and cows to bovine rotavirus inoculation and passive protection to rotavirus infection in newbom calves fed colostral antibodies or colostral lymphocytes (1988) Am. J. Vet. Res., 49, pp. 1084-1091; Besser, T.E., Gay, C.C., The importance of colostrum to the health of the neonatal calf (1994) Vet. Clin. North Am. Food Anim. Pract., 10, pp. 107-117; Besser, T.E., Gay, G.C., Mac Guire, T.C., Evermann, J.F., Passive immunity to bovine rotavirus infection associated with transfer of serum antibody into the intestinal lumen (1988) J. Virol., 62, pp. 2238-2242; Bridger, J.C., Non-group a Rotaviruses in Viral Infections of the Gastrointestinal Tract, pp. 369-408. , Ed. A.Z. KAPIKIAN 1994;2d ed., M. Dekker, New-York, USA; Bridger, C., A definition of bovine rotavirus virulence (1994) J. Gen. Virol., 75, pp. 2807-2812; Bridger, J.C., Hall, G.A., Parsons, K.R., A study of the basis of virulence variation of bovine rotaviruses (1992) Vet. Microb., 33, pp. 169-174; Castrucci, G., Ferrari, M., Angelillo, V., Field evaluation of the efficacy of Romovac 50 a new inactivated adjuvanted bovine rotavirus vaccine (1993) Comp. Immun. Microbiol. Infect. Dis., 3, pp. 235-239; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 149, pp. 51-70; Cornaglia, E.M., Fernandez, F.M., Gottschalk, M., Reduction in morbidity due to diarrhea in nursing beef calves by use of an inactivated oil-adjuvanted rotavirus-Escherichia coli vaccine in the dam (1992) Vet. Microbiol., 30, pp. 191-202; De Leeuw, P.W., Tiessink, J.W.A., Laboratory experiments on oral vaccination of calves against rotavirus or coronavirus induced diarrhoea (1985) Zbl. Vet. Med. B, 32, pp. 55-64; De Leeuw, P.W., Ellens, D.J., Talmon, F.P., Rotavirus infections in calves : Efficacy of oral vaccination in endemically infected herds (1980) Res. Vet. Sci., 29, pp. 142-149; Duchet-Suchaux, M., Protective antigens against enterotoxigenic Escherichia coli O101 : K99;F41 in the infant mouse diarrhea model (1988) Inf. Imm., 56, pp. 1364-1370; Duhamel, G.E., Bernoco, D., Davis, W.C., Esburn, B.I., Distribution of T and B lymphocytes in ammary dry secretions, colostrum and blood of adult dairy cattle (1987) Vet. Immun. Immunopathol., 14, pp. 101-122; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Saif, L., J Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am. J. Vet. Res., 57 (1), pp. 48-53; Grotelueschen, D.M., Duhamel, G.E., Lu, W., Possible vaccination failure in beef cow herds caused by infection with rotavirus distinct from the vaccine virus : Clinical observations Proc. 17th Buiatric Congress, 1, pp. 190-196. , St-Paul, USA; Gueguen, C., Maga, A., Mc Crae, M.A., Bataillon, G., Caprine and bovine B rotaviruses in western France : Group identification by Northern hybridization (1996) Vet. Res., 27, pp. 171-176; Hall, G.A., Bridger, J.C., Parsons, K.R., Cook, R., Variation in Rotavirus Virulence : A comparison of pathogenesis in calves between two rotaviruses of different virulence (1993) Vet. Pathol., 30, pp. 223-233; Harp, A., Goff, J.P., Protection of calves with a vaccine against cryptosporidium parvum (1995) J. Parasitol., 81 (1), pp. 54-57; Heath, S.E., Neonatal diarrhea in calves : Investigation of herd management practices (1992) Compendium Food Animal, 14 (3), pp. 385-393; Heckert, R.A., Saif, L.J., Mengel, J.P., Myers, G.W., Mucosal and systemic antibody responses to bovine coronavirus structural proteins in experimentally challenge-exposed calves fed low or high amounts of colostral antibodies (1991) Am. J. Vet. Res., 52 (5), pp. 700-708; Heckert, R.A., Saif, L.J., Mengel, P., Myers, G.W., Mucosal and systemic isotype-specific antibody responses to bovine coronavirus structural proteins in naturally infected dairy calves (1991) Am. J. Vet. Res., 52 (6), pp. 852-857; Holland, R.E., Some infectious causes of diarrhea in young farm animals (1990) Clin. Microb. Rev., 3, pp. 345-375; Isaacson, R.E., Vaccines against Escherichia coli diseases in Escherichia coli (1994) Domestic Animals and Humans, pp. 629-648. , Ed. C.L. GYLES, CAB International Wallingford, G.B; Kirkpatrick, C.E., Giardiasis in large animals (1989) Compendium Food Animal, 11, pp. 80-84; La Bonnardiere, C., Cohen, J., Contrepois, M., Interferon activity in rotavirus infected newborn calves (1981) Ann. Rech. Vet., 12, pp. 85-91; La Bonnardiere, C., De Vaureix, C., In vivo interference between heterologous rotavirus (1980) Viral Enteritis in Humans and Animals, pp. 95-98. , BRICOUT F, SCHERRER R. INSERM, Paris; Lu, W., Duhamel, G.E., Benfield, D.A., Grotelueschen, D.M., Serological and genotypic characterization of group A rotavirus reassortants from diarrheic calves born to dams vaccinated against rotavirus (1994) Vet. Microbiol., 42, pp. 159-170; Lucchelli, A., Lance, S.E., Bartlett, P.B., Miller, G.Y., Saif, L.J., Prevalence of bovine group A rotavirus shedding among dairy calves (1992) Ohio. Am. J. Vet. Res., 53, pp. 169-174; Mc Guirk, S.M., Neonatal calf management : A guide to disease investigation (1997) The Bovine Practitioner, 31, pp. 83-86; Mebus, C.A., White, R.G., Bass, E.P., Twiehaus, M.J., Immunity to neonatal calf diarrhea virus (1973) J. Am. Vet. Med. Assoc., 163, pp. 880-883; Milon, A., Mécanismes moléculaires de pathogénicité des Escherichia coli inducteurs de diarrhées chez l'home et l'animal (1993) Rev. Med. Vet., 144, pp. 857-878; Myers, L.L., Snodgrass, D.R., Colostral and milk antibody titers in cows vaccinated with a modified live-rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Ass., 181, pp. 486-488; Newby, T.J., Bourne, F.J., The nature of the local immune system of the bovine small intestine (1976) Immunology, 31, pp. 475-480; Newby, T.J., Bourne, F.J., The nature of the local immune system of the bovine mammary gland (1977) J. Immunol., 118, pp. 461-465; Paul, P.S., Lyoo, Y.S., Immunogens of rotaviruses (1993) Vet. Microbiol., 37, pp. 299-317; Parwani, A.V., Hussein, A.H., Rosen, B.I., Characterization of field strains of group. A bovine rotaviruses by using polymerase chain reaction-generated Grand P type-specificic C-DNA prbes (1993) J. Clin. Microbiol., 31, pp. 2010-2015; Pohl, P., Les souches pathogènes d'Escherichia coli : Histoire et classification (1993) Ann. Med. Vet., 137, pp. 325-333; Riedel-Caspari, G., The influence of colostral leukocytes on the course of an experimental E. coli infection and serum antibodies lin neonatal calves (1993) Vet. Immunol. Immunopathol., 35, pp. 275-288; Runnels, P.L., Moseley, S.L., Moon, H.W., F41 pili as protective antigens of enterotoxinogenic Escherichia coli that produce F41;K99 and both pilus antigens (1987) Inf Imm., 55, pp. 555-558; Saif, L.J., Coronavirus immunogens (1993) Vet. Microbiol., 37, pp. 285-297; Saif, L.J., Rosen, I.B., Parwani, A.V., Animal rotaviruses (1994) Viral Infections of the Gastrointestinal Tract, pp. 279-368. , 2d ed., Ed. A.Z. KAPIKIAN, M. Dekker, New-York, USA; Saif, L.J., Smith, K.L., Enteric viral infections of calves and passive immunity (1985) J. Dairy Sci., 68, pp. 206-228; Saif, L.J., Smith, K.L., Landmeier, B.J., Immune response of pregnant cows to bovine rotavirus immunization (1984) Am. J. Vet. Res., 45, pp. 49-58; Saif, L.J., Redman, D.R., Smith, K.L., Theil, K.W., Passive immunity to bovine rotavirus in newborn calves fed colostrum supplements from immunized or non immunized cows (1983) Inf. Immun., 41, pp. 1118-1131; Schelcher, F., De Rycke, J., Martel, J.L., Diarrhées colibacillaires néonatales du veau. Le Point (1993) Vétérinaire, 25, pp. 611-623; Snodgrass, D.R., Evaluation of a combined rotavirus and enterotoxigenic Escherichia coli vaccine in cattle (1986) Vet. Rec., 119, pp. 39-43; Snodgrass, D.R., Browning, G., Enteric vaccines for farm animals and horses (1993) Vaccines for Veterinary Applications, pp. 59-81. , Ed. A.R. PETERS, Butterworth Hememann, Oxford, U.K; Snodgrass, D.R., Fahey, K.J., Wells, P.W., Passive immunity in calf rotavirus infections : Maternal vaccination increases and prolong immunoglobulin G1 antibody secretion in milk (1980) Inf. Imm., 28, pp. 344-349; Snodgrass, D.R., Htzgerald, T.A., Campbell, I., Homotypic and heterotypic serological responses to rotavirus neutralization epitopes in immunologically naïve and experienced animals (1991) J. Clin. Microbiol., 29, pp. 2668-2672; Snodgrass, D.R., Hoshino, Y., Fitzgerald, T.A., Identification of four VP4 serological types P. serotypes of bovine rotavirus using viral reassortants (1992) J. Gen. Virol., 73, pp. 2319-2325; Snodgrass, D.R., Fitzgerald, T.A., Campbell, I., Rotavirus serotypes 6 and 10 Predominate in cattle (1990) J. Clin. Microbiol., 28 (3), pp. 504-507; Snodgrass, D.R., Fitzgerald, T.A., Campbell, I., Homotypic and heterotypic serological responses to rotavirus neutralization epitopes in immunologically naive and experienced animals (1991) J. Clin. Microbiol., 29 (11), pp. 2668-2672; Snodgrass, D.R., Ojeh, C.K., Campbell, I., Herring, A.J., Bovine rotavirus serotypes and their significance for immunization (1984) J. Clin. Microbiol., 20, pp. 342-346; Soulebot, J.P., Dauvergne, M., Brun, A., Rotavirus : Vaccination chez les bovins (1983) Rec. Méd. Vét., 159, pp. 335-344; Tizard, I., (1992) Veterinary Immunology. An Introduction, 498p. , 4th Ed., Saunders, Philadelphia, USA; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol, 140, pp. 1303-1311; Tsunemitsu, H., Shimizu, M., Hirai, T., Protection against bovine rotaviruses in newborn calves by continuous feeding of immune colostrum (1989) Jpn J. Vet. Sci., 51, pp. 300-308; Vallet, A., Les diarrhées des veaux liées à la conduite de l'alimentation et à la qualité de l'aliment (1994) Proc. Congrès FRCTV Bourgogne, pp. 21-24. , Beaune; Van Zaane, D., Ijzerman, J., De Leeuw, P.W., Intestinal antibody response after vaccination and infection with rotavirus of calves fed colostrum with or without rotavirus antibody (1986) Vet. Immunol. Immunopathol., 11, pp. 45-63; Vermunt, J.J., Rearing and management of diarrhoea in calves to weaning (1994) Aust. Vet J., 71 (2), pp. 33-41; Waltner-Toews, D., Martin, S.W., Meek, A.H., A field trial to evaluate the efficacy of a combined Rotavirus-Coronavirus/Escherichia coli Vaccine in dairy cattle (1985) Can. J. Comp. Med., 49, pp. 1-9; Woode, G.N., Kelso, N.E., Simpson, T.F., Antigenic relationships among some bovine rotaviruses : Serum neutralization and cross-protection in gnotobiotic calves (1983) J. Clin. Microb., 18, pp. 358-364","Schelcher, F.; Pathologie du Bétail, ENVT, 31076 Toulouse Cedex, France",,,03354997,,,,"French","Point Vet.",Article,"Final",,Scopus,2-s2.0-0032367997
"Sirinarumitr T., Kluge J.P., Paul P.S.","6602842923;7005760957;7202714004;","Transmissible gastroenteritis virus induced apoptosis in swine testes cell cultures",1998,"Archives of Virology","143","12",,"2471","2485",,21,"10.1007/s007050050477","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032446932&doi=10.1007%2fs007050050477&partnerID=40&md5=2a9ecdc3fc6c4d37695397180b5712d2","Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA, United States; Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA, United States; Dept. Microbiol., Immunol., Prev. M., College of Veterinary Medicine, Iowa State University, Ames, IA, United States; Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","Sirinarumitr, T., Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA, United States, Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA, United States; Kluge, J.P., Department of Veterinary Pathology, College of Veterinary Medicine, Iowa State University, Ames, IA, United States; Paul, P.S., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, Ames, IA, United States, Dept. Microbiol., Immunol., Prev. M., College of Veterinary Medicine, Iowa State University, Ames, IA, United States, Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","Transmissible gastroenteritis virus (TGEV) is a coronavirus which causes severe gastroenteritis and atrophy of intestinal villous epithelial cells in piglets. However, the mechanism of cell death caused by TGEV is not known. In this study, we report that TGEV induces cell death by apoptosis. TGEV-induced apoptosis was demonstrated by agarose gel electrophoresis, electron microscopy, and terminal deoxytransferase digoxigenin-dUTP nick end labeling (TUNEL). Double labeling experiment confirmed the result from electron microscopy and showed that most of the apoptotic cells were bystander cells as they were negative for TGEV nucleic acids. Results of this study indicate that TGEV induces apoptosis in vitro and that most of the cells undergoing apoptosis are bystander cells, thus amplifying the cytopathic effect of TGEV.",,"agar gel electrophoresis; apoptosis; atrophy; culture technique; electron microscopy; intestine epithelium cell; swine; transmissible gastroenteritis virus; virus detection; virus infection; Animals; Apoptosis; Cells, Cultured; Cytopathogenic Effect, Viral; DNA Fragmentation; In Situ Hybridization; In Situ Nick-End Labeling; Male; Microscopy, Electron; Swine; Testis; Transmissible gastroenteritis virus","Adler, B., Adler, H., Pfister, H., Jungi, T.W., Peterhans, E., Macrophages infected with cytopathic bovine viral diarrhea virus release a factor(s) capable of priming uninfected macrophages for activation-induced apoptosis (1997) J Virol, 71 (3), pp. 255-3258; Bostworth, B.T., Maclachlan, N.J., Johnston, M.I., Induction of the 2-5A system by interferon and transmissible gastroenteritis virus (1989) J Interferon Res, 9, pp. 731-739; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res, 18, pp. 71-80; Dejucq, N., Dugust, I., Ruffault, A., Van Der Meide, P., Jégou, B., Interferon-α and -γ expression in the rat testis (1995) Endocrinology, 136, pp. 4925-4931; Dong, C., Wilson, J.E., Winters, G.L., McManus, B.M., Human transplant coronary artery disease: Pathological evidence for fas-mediated apoptotic cytotoxicity in allograft arteriopathy (1996) Lab Invest, 74, pp. 921-931; Doyle, L.P., Hutchings, L.M., A transmissible gastroenteritis virus in pigs (1946) J Am Vet Med Assoc, 108, pp. 257-259; Gavrieli, Y., Sheman, Y., Ben-Sasson, S.A., Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation (1992) J Cell Biol, 119, pp. 493-501; Godfraind, C., Holmes, K.V., Coutelier, J.-P., Thymus involution induced by mouse hepatitis virus A59 in BALB/c mice (1995) J Virol, 69, pp. 6541-6547; Griebel, P.J., Ohmann, H.B., Lawman, M.J.P., Babiuk, L.A., The interaction between bovine herpesvirus type 1 and activated bovine T lymphocytes (1990) J Gen Virol, 71, pp. 369-377; Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Apoptosis and T-cell depletion during feline infectious peritonitis (1996) J Virol, 70, pp. 8977-8983; Hayat, M.A., (1989) Principles and Techniques of Electron Microscopy, 3rd Ed., , CRC Press, Boca Raton; Hinshaw, V.S., Olsen, C.W., Dybdahl-Sissoko, N., Evans, D., Apoptosis: A mechanism of cell killing by influenza A and B viruses (1994) J Virol, 68, pp. 3667-3673; Itoh, N., Yonehara, S., Ishii, A., Yonehara, M., Mizushima, S., Sameshima, M., Hase, A., Nagata, S., The polypeptide encoded by the cDNA for human cell surface antigen fas can mediate apoptosis (1991) Cell, 66, pp. 233-243; Kerr, J.F.R., Winterford, C.M., Harmon, B.V., Morphological criteria for identifying apoptosis (1994) Cell Biology a Laboratory Handbook, 1, pp. 319-329. , Celis JE (ed) Academic Press, New York; Kizaki, H., Nakadda, S., Ohnishi, Y., Axuma, Y., Mizuno, Y., Tadakuma, T., Tumour necrosis factor-α enhances cAMP-induced programmed cell death in mouse thymocytes (1993) Cytokine, 5, pp. 342-347; La-Bonnardiere, C., Laude, H., Interferon induction in rotavirus and coronavirus infections: A review of recent results (1983) Ann Rech Vet, 14, pp. 507-511; La-Bonnardiere, C., Laude, H., High interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infect Immun, 32, pp. 28-31; Lam, K.M., Vasconcelos, A.C., Newcastle disease virus-induced apoptosis in chicken peripheral blood lymphocytes (1994) Microb Pathog, 44, pp. 45-56; Laude, H., Charley, B., Gelfi, J., Replication of transmissible gastroenteritis corona-virus (TGEV) in swine alveolar macrophages (1984) J Gen Virol, 65, pp. 327-332; Laude, H., La-Bonnardiere, C., Cytocidal effect of interferons on porcine renal cells (1984) J Interferon Res, 4, pp. 101-110; Lebel, M., Bertrand, R., Mes-Mason, A., Decreased fas antigen receptor expression in testicular cell lines derived from polyoma virus large T-antigen transgenic mice (1996) Oncogene, 12, pp. 1127-1135; Loewen, K.G., Derbyshire, J.B., The effect of interferon induction in parturient sows and newborn piglets on resistance to transmissible gastroenteritis (1988) Can J Vet Res, 52, pp. 149-153; Lu, J.J., Chen, J., Hsu, T., Yu, W.C.Y., Su, I., Yan, C., Induction of apoptosis in epithelial cells by Epstein-Barr virus latent membrane protein 1 (1996) J Gen Virol, 77, pp. 1883-1892; May, W.S., Control of apoptosis by cytokines (1997) Apoptosis, 41, pp. 219-246. , Kaufmann SH (ed) Academic Press, San Diego London Boston New York Sydney Tokyo Toronto Advances in Pharmacology; McClurkin, A.W., Norman, O.J., Studies on transmissible gastroenteritis of swine II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can J Comp Med Vet Sci, 30, pp. 190-198; Meyard, L., Otto, S.A., Jonker, R.R., Mijnster, M.J., Keet, R.M., Miedema, F., Programmed cell death of T cells in HIV-1 infection (1992) Science, 257, pp. 217-219; Noteborn, M.H.M., Todd, D., Verschueren, C.A.J., De Gauw, H.W.F.M., Curran, W.L., Veldkamp, S., Douglas, A.J., Koch, G., A single chicken anemia virus protein induces apoptosis (1994) J Virol, 68, pp. 346-351; Oyaizu, N., McClosky, T.W., Than, S., Hu, R., Kalyanaraman, V., Pahwa, S., Cross-linking of CD4 molecules upregulates fas antigen expression in lymphocytes by inducing interferon-γ and tumor necrosis factor-α secretion (1994) Blood, 84, pp. 2622-2631; Ramiro-Iba Ñez, F., Ortega, A., Brun, A., Escribano, J.M., Alonso, C., Apoptosis: A mechanism of cell killing and lymphoid organ impairment during acute African swine fever virus infection (1996) J Gen Virol, 77, pp. 2209-2219; Rao, L., Debbas, M., Sabbatini, P., Hockenberry, D., Korsmeyer, S., White, E., The adenovirus E1A protein induce apoptosis, which is inhibited by the E1B19-kDa and Bcl-2 proteins (1992) Proc Natl Acad Sci USA, 89, pp. 7742-7746; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., pp. 362-386. , Leman AD, Strauss BE, Mengeling WL, D'Allaire S, Taylor DJ (eds) Iowa State University Press, Iowa; Schultz-Cherry, S., Hinshaw, V.S., Influenza virus neuraminidase activates latent transforming growth factor beta (1996) J Virol, 70, pp. 8624-8629; Seglen, P.O., Isolation of hepatocytes (1994) Cell Biology, pp. 96-108. , Celis JE (ed) Academic Press, San Diego London Boston New York Sydney Tokyo Toronto; Sirinarumitr, T., Paul, P.S., Halbur, P.G., Kluge, J.P., Rapid in situ hybridization technique for the detection of ribonucleic acids in tissues using radiolabelled and flourescein-labelled riboprobes (1997) Mol Cell Probes, 11, pp. 273-280; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in formalin-fixed paraffin-embedded tissues (1996) J Virol Methods, 56, pp. 149-160; Suarez, P., Díaz-Guerra, M., Prieto, C., Esteban, M., Castro, J.M., Open reading frame 5 of porcine reproductive and respiratory syndrome virus as a cause of virus-infected apoptosis (1996) J Virol, 70, pp. 2876-2882; Suda, T., Takahashi, T., Golstein, P., Nagata, S., Molecular cloning and expression of the fas ligand, a novel member of the tumor necrosis factor family (1993) Cell, 75, pp. 1169-1178; Takizawa, T., Fukuda, R., Miyawaki, T., Ohashi, K., Nakanishi, Y., Activation of the apoptotic fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon (1995) Virology, 209, pp. 288-296; Tanuma, S., Shiokawa, D., An endonuclease responsible for apoptosis (1996) Progress in Molecular and Subcellular Biology 1, 16, pp. 1-12. , Kuchino Y, Müller WEG (eds) Springer, Berlin Heidelberg New York, Tokyo; Thompson, C.B., Apoptosis in the pathogenesis and treatment of disease (1995) Science, 267, pp. 1456-1461; Tolskaya, E.A., Romanova, L.I., Kolesnicova, M.S., Ivannikova, T.A., Smirnova, E.A., Raikhlin, N.T., Agol, V.I., Apoptosis-inducing and apoptosis-preventing functions of polio-virus (1995) J Virol, 69, pp. 1181-1189; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Vaughn, E.M., Halbur, P.G., Paul, P.S., Use of nonradioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates (1996) J Vet Diagn Invest, 8, pp. 241-244; Weingartl, H., Derbyshire, J.B., Antiviral activity against transmissible gastroenteritis virus, and cytotoxicity, of natural porcine interferons alpha and beta (1991) Can J Vet Res, 55, pp. 143-149; Weller, M., Constam, D.B., Malipiero, U., Fontana, A., Transforming growth factor beta 2 induces apoptosis of murine T cell clones without down-regulating bcl-2 mRNA expression (1994) Eur J Immunol, 24, pp. 1293-1300; Zhang, G., Aldridge, S., Clarke, M.C., McCauley, J.W., Cell death induced by cytopathic bovine viral diarrhea virus is mediated by apoptosis (1996) J Gen Virol, 77, pp. 1677-1681; Zheng, L., Fisher, G., Miller, R., Peschon, J., Lynch, D., Lenardo, M., Induction of apoptosis in mature T cells by tumor necrosis factor (1995) Nature, 377, pp. 348-351","Paul, P.S.; Veterinary Med. Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States",,,03048608,,ARVID,"9930203","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0032446932
"Bajolet O., Chippaux-Hyppolite C.","57190427268;7003435497;","Rotaviruses and other diarrheal viruses [Les rotavirus et autres virus de diarrhées]",1998,"Bulletin de la Societe de Pathologie Exotique","91","5",,"432","437",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032242094&partnerID=40&md5=bf9525fd4f0fa25d2d1d42cfa34e966a","Fac. de Médecine de Reims, rue Cognacq-Jay, 51100 Reim, France","Bajolet, O., Fac. de Médecine de Reims, rue Cognacq-Jay, 51100 Reim, France; Chippaux-Hyppolite, C., Fac. de Médecine de Reims, rue Cognacq-Jay, 51100 Reim, France","Rotaviruses represent 80% of recognized viral etiologies and 140 million cases of diarrhea per year. They strike young children with similar frequency throughout the world, but the mortality rate is high in developing countries only, with some 870.000 deaths per year (WHO, 1997). Rotaviruses belong to the family of Reoviridae; they are segmented bicatenary RNA viruses, which explains their genetic variability, the presence of mixed infections, the establishment for some time already of a molecular epidemiology by electrophoretypes. The viruses are ""naked"" and thus resistant to the outside environment; their massive elimination, 108 to 1010viral particles per gram of faeces, begins with the first day of diarrhea. They are found in used water and can also be concentrated by shellfish; the environment thus constitutes a notable reservoir for the virus. Oral-faecal transmission is facilitated by deficient sanitary conditions. The 11 fragments of the genome each codify for 1 viral protein; 2 surface proteins, VP4 and VP7, bring about the formation of neutralizing antibodies, which are important for the protection and determination of different serotypes. A non structural protein-NSP4-would seem to intervene in the cytopathogenic effect and may act as a veritable viral enterotoxine. Numerous animal species are infected by rotaviruses which are district from the human ones. The pathology as it affects animals is of economic importance and of interest as an experimental and vaccinal model. Between human and animal rotaviruses there can be genetic rematchings and the VP6 protein is an antigen common to the group. The description of the other viruses responsible for diarrhea has benefited from widespread use of electronic microscopes from the very first years of study of rotaviruses. These other viruses belong to 6 different types: adenovirus, calicivirus, astrovirus, Norwalk agent and related viruses, coronavirus, enterovirus. They therefore have a structural and antigenic polymorphism but, except for the coronavirus, they are all ""naked"" virions with resistance in outside environments and means of transmission analogous to the rotaviruses. Clinical signs of viral gastroenterites, the age of the patient and epidemiological circumstances help in making an etiological diagnosis; the biological diagnosis has been simplified for the rotaviruses and the adenoviruses. Epidemics related to food, or of hydric and nosocomial origin, especially those due to the Norwalk agent, are under-declared and more frequent than those of bacterial origin. The prevention of dangers related to faeces, the improvement of sanitary conditions, health education, and better nutrition contribute to rotavirus prevention, but rotavirus diarrheas, the incidence of which is similar in developed and developing countries, would be more efficiently controlled through vaccination.","Biological diagnosis; Diarrhea; Norwalk agent; Rotavirus","capsid protein; DNA directed RNA polymerase; virus antibody; virus antigen; virus hemagglutinin; virus protein; VP4 protein, Rotavirus; VP6 protein, Rotavirus; animal; article; child; classification; developing country; diarrhea; disease carrier; epidemiology; feces; food control; gastroenteritis; genetics; human; immunology; microbiology; Norwalk gastroenteritis virus; physiology; Rotavirus; sanitation; serotyping; statistics; virion; virology; virus capsid; virus infection; virus shedding; water pollution; Animals; Antibodies, Viral; Antigens, Viral; Caliciviridae Infections; Capsid; Capsid Proteins; Child; Developing Countries; Diarrhea; Disease Reservoirs; DNA-Directed RNA Polymerases; Epidemiology, Molecular; Feces; Food Microbiology; Gastroenteritis; Hemagglutinins, Viral; Humans; Norwalk virus; Rotavirus; Rotavirus Infections; Sanitation; Serotyping; Viral Nonstructural Proteins; Virion; Virus Diseases; Virus Shedding; Water Microbiology; Water Pollution","Bern, C., Unicomb, L., Gentsch, J.R., Banul, N., Yunus, M., Rotavirus diarrhea in Bangladeshi children: Correlation of disease severity with serotypes (1992) J Clin Microbiol, 30, pp. 3234-3238; Bishop, R.F., Development of candidate rotavirus vaccines (1993) Vaccine, 11, pp. 247-254; Bishop, R.F., Davidson, G.P., Holmes, I.H., Ruck, B.J., Virus particles in epithelial cells of duodenal mucosa from children with acute nonbacterial gastroenteritis (1973) Lancet, 2, pp. 1281-1283; Buesa, J., Evaluation of reverse transcription and polymerase chain reaction (RT/PCR) for the detection of rotaviruses: Applications of the assay (1996) Res Virol, 147, pp. 353-361; Chippaux-Hyppolite, C., Loukou Yao, G., Chippaux, A., Les infections à rotavirus et leur prévention vaccinale chez l'enfant (1991) Bull Soc Path Ex, 84, pp. 918-925; Cohen, J., Structure et réplication des rotavirus (1997) Comptes Rendus de la Réunion sur les Rotavirus en Médecine Humaine et Vétérinaire, 10 Octobre 1996, pp. 15-22. , Editions Fondation Marcel Mérieux, Lyon; Coulson, B.S., Grimwood, K., Lund, J.S., Mermelstein, N., Comparison of rotavirus inununoglobulin a coproconversion with other indices of rotavirus infection in a longitudinal study in childhood (1990) J Clin Microbiol, 28, pp. 1367-1374; Crainic, R., Nicolas, J.C., (1993) Virologie Médicale, pp. 289-298. , Editions Médicales Internationales, Cachan; De Leon, R., Matsui, S.M., Baric, Hermann, J.E., Blacklow, N.R., Detection of Norwalk virus in stool specimens by reverse transcriptase-polymerase chain reaction and non radioactive oligoprobes (1992) J Clin Microbiol, 30, pp. 3151-3157; Dolin, R., Treanor, J.J., Madore, H.P., Novel agents of viral enteritis in humans (1987) J Infect Dis, 155, pp. 365-376; Dubois, E., Le Guyader, F., Kopecka, H., Miossec, L., Pommepuy, M., Contamination de l'environnement littoral par les rotavirus du groupe A (1997) Comptes Rendus de la Réunion sur les Rotavirus en Médecine Humaine et Vétérinaire, 10 Octobre 1996, pp. 43-54. , Editions Marcel Mérieux, Lyon; Gendrel, D., Diarrhées infectieuses dans les pays en développement (1997) Méd Mal Infect, 27, pp. 517-519; Gentsch, J.R., Woods, P.A., Ramachandran, M., Review of G and P typing results from global collection of rotavirus strains: Implications or vaccine development (1996) J Infect Dis, 174, pp. S30-S36; Gerna, G., Forster, J., Parea, M., Sarasini, A., Di Matteo, A., Nosocomial outbreak of neonatal gastroenteritis caused by a new serotype 4, subtype 4B human rotavirus (1990) J Med Virol, 31, pp. 175-182; Glass, R.I., Ki-Gore, P.E., Holman, R.C., The epidemiology of rotavirus diarrhea in the United States: Surveillance and estimates of disease burden (1996) J Infect Dis, 174, pp. S5-S11; Gordon, S.M., Oshiro, L.S., Jarvis, W.R., Donenfeld, D., Ho, M.S., Foodborne snow mountain agent gastroenteritis with secondary porson-to-person spread in a retirement community (1990) Am J Epidemiol, 131, pp. 702-710; Hedberg, C.W., Osterholm, M.T., Outbreaks of food-Borne and waterborn viral gastroenteritis (1993) Clin Microbiol Rev, 6, pp. 199-210; Kirkwood, C.D., Palombo, E.A., Genetic characterization of the rotavirus nonstructural protein, NSP4 (1997) Virology, 236, pp. 258-265; Kohn, M.A., Marlet, T.A., Amdo, T., Curtis, M., Wilson, S.A., An outbreak of Norwalk virus gastroenteritis associated with eating row oysters. Implications for maintening safe oyster beds (1995) JAMA, 273, pp. 466-471; Kukkula, M., Arstila, P., Klossner, M.L., Maunula, L., Bonsdorff, C.H.V., Jaatinen, P., Waterborne outbreak of viral gastroenteritis (1997) Scand J Infect Dis, 29, pp. 415-418; Navetat, H., Vaccination et gastroenterites à rotavirus du veau (1997) Comptes Rendus de la Réunion sur les Rotavirus en Médecine Humaine et Vétérinaire, 10 Octobre 1996, pp. 57-61. , Editions Marcel Mérieux, Lyon; Nicand, E., Buisson, Y., Stratégie diagnostique des gastro-entérites virales (1997) Le Péril Fécal, p. 44. , Société de pathologie exotique (hors série); Nicolas, J.C., Pothier, P., Cohen, J., Survey of human rotavirus propagation as studied by electrophoresis of genomic RNA (1984) J Infect Dis, 149, pp. 688-693; Orenstein, W.A., Hadler, S., Kuritsky, J.N., Bernier, R.H., Rotavirus vaccines - From licensure to disease reduction (1996) J Infect Dis, 174 (1 SUPPL.), pp. S118-S124; Smit, T.K., Steele, A.D., Peenze, I., Jiang, X.I., Estes, M.K., Study of Norwalk virus and Mexico virus infections at Ga-Rankuwa hospital, Ga-Rankuwa (1997) J Clin Microbiol, 35, pp. 2381-2385; Traore, O., Belliot, G., Ramanatsoa, C., Pozzetto, B., Laveran, H., Detection des astrovirus par RT-PCR dans des selles d'enfants d arrhéiques en milieu hospitalier (1997) Le Péril Fécal, p. 45. , Société de pathologie exotique (hors série)","Bajolet, O.; Fac. de Médecine de Reims, rue Cognacq-Jay, 51100 Reim, France",,,00379085,,,"10078381","French","Bull. Soc. Pathol. Exot.",Article,"Final",,Scopus,2-s2.0-0032242094
"Lamontagne L., Massicotte E., Page C.","7005766206;36973328000;7202916107;","Intrahepatic αβ-TcRintermediate LFA-1high T cells are stimulated during mouse hepatitis viral infection",1998,"Advances in Experimental Medicine and Biology","440",,,"479","483",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031783281&partnerID=40&md5=881782376899d76e7b78a041c3686d2a","Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Que. H3C 3P8, Canada","Lamontagne, L., Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Que. H3C 3P8, Canada; Massicotte, E., Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Que. H3C 3P8, Canada; Page, C., Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Que. H3C 3P8, Canada","Mouse hepatitis virus type 3 (MHV3), a coronavirus, is an excellent animal model for the study of thymic and extrathymic T cell subpopulation disorders induced during the viral hepatitis. To understand local hepatic immune responses, the phenotypes of resident hepatic lymphocytes were determined and compared that of splenic and thymic T cell subpopulations during the acute viral hepatitis induced by MHV3 in susceptible C57BL/6 mice. Single positive (SP) CD4+ or CD8+ cells strongly increased in the liver. A specific cell population, the double positive (CD4+C8+) cells, normally present in liver and thymic cell preparations, decreased in C57BL/6 mice following the viral infection. αβ-TcRintermediateT cells shifted toward αβ-TcRhigh T cells in the liver and thymus of infected mice, but not in their spleen. The specific αβ-TcRint or high lymphocytes occurring in the liver of MHV3-infected mice expressed higher levels of leukocyte function antigen-1 (LFA-1) and Pgp-1 (CD44) activation markers, suggesting that they were either activated or antigen-experienced during the viral infection. No significant changes in T cell subpopulations were detected in the spleen. These observations suggest that MHV3. infection could induce an early in situ stimulation of resident hepatic T cells, despite a peripheral immunodeficiency in the thymus and spleen.",,"hermes antigen; lymphocyte function associated antigen 1; animal cell; animal experiment; animal model; animal tissue; article; controlled study; female; immune response; liver; mouse; murine hepatitis coronavirus; nonhuman; priority journal; spleen; t lymphocyte; t lymphocyte subpopulation; thymus; virus hepatitis; Animals; CD4-Positive T-Lymphocytes; CD8-Positive T-Lymphocytes; Coronavirus Infections; Female; Lymphocyte Function-Associated Antigen-1; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Receptors, Antigen, T-Cell, alpha-beta; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Staphylococcus phage 3A","Abo, T., Ohteki, T., Seki, S., Koyamada, N., Yoshikai, Y., Masuda, T., Rikiish, H., Kumagai, K., The appearance of T cells bearing self-reactive T cell receptor in the liver of mice injected with bacteria (1991) J. Exp. Med., 174, pp. 417-423; Lamontagne, L., Descoteaux, J.P., Jolicoeur, P., T and B lymphotropisms of mouse hepatitis virus 3 correlate with viral pathogenicity (1989) J. Immunol., 142, pp. 4458-4467; Le Prévost, C., Levy-Leblond, B., Virelizier, J.L., Dupuy, J.M., Immunopathology of mouse hepatitis virus type 3 infection. I. Role of humoral and cell-mediated immunity in resistance mechanism (1975) J. Immunol., 114, pp. 221-225; Levy, G.A., Abecassis, M., Activation of the immune coagulation system by murine hepatitis virus strain 3 (1989) Rev. Infect. Dis., 11, pp. 712-727; Matsumoto, Y., Emoto, M., Usami, J., Maeda, K., Yoshikai, Y., A protective role of extrathymic ab TcR cells in the liver in primary murine salmonellosis (1994) Immunology, 81, pp. 8-10; Ohteki, T., Okuyama, R., Seki, S., Abo, T., Sugiura, K., Kusumi, A., Ohmori, T., Kumagai, K., Age-dependent increase in extrathymic T cells in the liver and their appearance in the periphery of older mice (1992) J. Immunol., 149, pp. 1562-1567; Pereira, C.A., Steffan, A.M., Kirn, A., Interaction between mouse hepatitis virus and primary cultures of Kupffer and endothelial liver cells from resistant and susceptible inbred mouse strains (1984) J. Gen. Virol., 65, pp. 35-41; Pham, B.N., Martinot-Peignoux, M., Mosnier, J.F., Njapoum, C., Marcellin, P., Bougy, F., Degott, C., Degos, F., CD4+/CD8+ ratio of liver-derived lymphocytes is related to viraemia and not to hepatitis C virus genotypes in chronic hepatitis C (1995) Clin. Exp. Immunol., 102, pp. 320-356; Shimizu, Y., Newman, W., Tanaka, Y., Shaw, S., Lymphocyte interactions with endothelial cells (1992) Immunol. Today, 13, pp. 106-108; Volpes, R., Van Den Oord, J.J., Desmet, V.J., Immunohistochemical study of adhesion molecules in liver inflammation (1990) Hepatology, 12, pp. 59-68; Watanabe, H., Ohtsuka, K., Kimura, M., Ikarashi, Y., Ohmori, K., Kusumi, A., Ohteki, T., Abo, T., Details of an isolation method for hepatic lymphocytes in mice (1992) J. Immunol. Meth., 146, pp. 145-154","Lamontagne, L.; Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Que. H3C 3P8, Canada",,,00652598,,AEMBA,"9782318","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0031783281
"Potter C.W.","7202295912;","Chapter 25 Respiratory tract viruses",1998,"Principles of Medical Biology","9","C",,"415","437",,,"10.1016/S1569-2582(97)80009-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-77957067267&doi=10.1016%2fS1569-2582%2897%2980009-8&partnerID=40&md5=cdc91d9b2cf25e6b157b25a245fefa7f",,"Potter, C.W.","Respiratory tract infections are among the commonest of illnesses, and most individuals will experience two to five infections during each year of their lives. The illnesses vary from relatively mild common colds caused by rhinoviruses and coronaviruses, to severe bronchiolitis and pneumonia caused by adenoviruses and influenza viruses and respiratory syncytial virus (RSV) in infants: the former is associated with little morbidity and no mortality, while influenza is responsible annually for between 1 and 25 thousand deaths per 50 million population. Over 140 viruses cause respiratory tract infections, with the added complications of influenza viruses where new antigenic variants are recognized almost annually; and immunity to infection by one virus strain offers little or no protection to infection by others. Knowledge of the mechanisms of spread of respiratory viruses is largely understood and has helped in infection control; however, the clinical signs and symptoms of infection tend not to be diagnostic of the causative agent; and although vaccines have been developed for the more serious infections such as influenza and some adenovirus infection, none are available for other important infections. Treatment is largely symptomatic, but the compounds ribovirin for RSV infection and amantadine for influenza virus infection have been shown to be effective. Much remains to be discovered before more effective measures can be implemented to limit the enormous costs incurred by these infections. The number of viruses involved is large, and the spectrum of illness complex: in the present chapter, the viruses are described, together with the features of the epidemiology, pathogenesis, clinical disease, and treatment. © 1997 Elsevier B.V. All rights reserved.",,,"Al-Nakib, W., Tyrrell, D.A.J., Common cold viruses-Rhinoviruses (1988) Laboratory Diagnosis of Infectious Diseases: Principles and Practices, pp. 723-742. , Ballows A., Hausler W.J., and Lennette E.H. (Eds), Springer-Verlag, New York; Brandt, C.D., Kim, K.W., Vargasko, A.J., Infections in 18,000 infants and children in a controlled study of respiratory tract disease. I. Adenovirus pathogenicity in relation to serological type and illness syndrome (1969) Amer. J. Epidemiol., 90, pp. 484-500; Chapman, R.S., Henderson, F.W., Clyde Jr., W.A., Collier, A.M., Denny, F.W., The epidemiology of tracheobronchitis in pediatric practice (1981) Amer. J. Epidemiol., 144, pp. 786-797; Carey, L., Rubin, R.J., Hattwick, M.A.W., Noble, G.R., Cassidy, E., A nationwide outbreak of Reye's syndrome (1976) Amer. J. Med., 61, pp. 615-625; Dolin, R., Reichman, R.C., Madore, P., Maynard, R.N., Linton, P.N., Webber-Jones, J., A controlled trial of amantadine and rimantadine in the prophylaxis of influenza A infection (1976) N. Engl. J. Med., 307, pp. 580-584; Glezen, W.P., Denny, F.W., Epidemiology of acute lower respiratory disease in children (1973) N. Eng. J. Med., 288, pp. 498-505; Gwaltney, J.M., Rhinoviruses (1982) Viral Infections of Humans: Epidemiology and Control, pp. 491-517. , Evans A.S. (Ed), Plenum, New York; Hall, C.B., McBride, J.T., Walsh, E.E., Aerosalised ribavirin treatment of infants with respiratory syncytial virus infection (1983) N. Eng. J. Med., 308, pp. 1443-1447; Hall, C.B., Powell, K.P., MacDonald, N.E., Gala, C.L., Menegus, M.E., Suffin, S.C., Cohen, M.J., Respiratory syncytial viral infection in children with compromised immune function (1986) N. Eng. J. Med., 815, pp. 77-80; Hamparian, V.V., Colonno, R.J., Cooney, M.K., Dick, E.C., Gwaltney, J.M., Hughes, J.A., Jordan, W.S., Tyrrell, D.A.J., A collaborative report: Rhinoviruses-extension of the numbering system from 89-100 (1987) Virology, 159, pp. 191-192; Hendley, J.O., Rhinovirus colds: immunology and pathogenesis (1983) Europ. J. Resp. Dis., 64 (SUPPL), pp. 340-345; Isaacs, D., Flowers, D., Clarke, J.R., Valman, A.B., MacNaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch. Dis. Child., 58, pp. 500-503; Lenair, G.M., Bornkamm, G.W., Burkitt's lymphoma, a human cancer model for the study of the multistep development of cancer: Proposal for a new scenario (1987) Advances in Viral Oncology, 7, pp. 173-206. , Klein G. (Ed), Lippincott-Raven, Philadelphia, PA; Parrott, R.H., Vargosko, A.J., Kim, H.W., Bell, J.A., Chanock, R.M., Myxoviruses. III. Parainfluenza (1962) Amer. J. Publ. Hlth., 52, pp. 907-917; Potter, C.W., Inactivated influenza virus vaccine (1982) Basic and Applied Influenza Research, pp. 119-158. , Beare A.S. (Ed), CRC Press, Boca Raton, Florida; Ray, C.G., Minnich, L., Efficiency of immunofluorescence for rapid diagnosis of common respiratory viruses (1987) J. Clin. Microbiol., 25, pp. 355-357; Robinson, J., Stevens, K.C., Production of autoantibodies to cellular antigens by human B cells transformed by Epstein-Barr virus (1984) Clin. Immunol. Immunopathol., 33, pp. 339-350; Schieble, J.H., Kapikian, A.Z., Coronaviruses (1979) Diagnostic Procedures for Viral, Rickettsial and Chlamydial Infections, pp. 709-723. , Lennette E.H., and Schmidt N.J. (Eds), Am. Pbl. Health. Ass, Washington, DC; Tarafuji, E.T., Gaydes, J.C., Allen, R.G., Tipf, H., Simultaneous administration of live, enteric-coated adenovirus 4, 7 and 21 vaccines: Safety and immunogenicity (1979) J. Inf. Dis., 140, pp. 48-53; Wadell, G., Molecular epidemiology of human adenoviruses (1984) Curr. Topics Microbiol. Immunol., 110, pp. 191-220; Welliver, R.C., Kaul, T.N., Sun, M., Ogra, P.L., Defective regulation of immune responses in respiratory syncytial virus infection (1984) J. Immunol., 133, pp. 1925-1930; Fox, J.P., Cooney, M.K., Hall, C.E., Rhinoviruses in Seattle families 1975-1979 (1985) Amer. J. Epidem., 122, pp. 830-846; Stott, E.J., Killington, R.A., Rhinoviruses (1972) Ann. Rev. Microbiol., 26, pp. 503-524; Monto, A.S., Lim, S.K., The Tecumseh study of respiratory disease VI. Frequency of the relationship between outbreaks of coronavirus infection (1974) J. Infect. Dis., 129, pp. 271-276; Schmitz, H., Wigand, R., Heinrich, W., World-wide epidemiology of human adenovirus infections (1983) Amer. J. Epidemiol., 117, pp. 455-466; (1989) Infectious Mononucleosis, , Schlosser D. (Ed), Springer-Verlag, New York; (1992) Seminars in Respiratory Infections, ""Influenza"", 7. , Sarosi G.A., and Ruben F.L. (Eds); Welliver, R.C., Wong, D.T., Sun, M., McCarthy, N., Parainfluenza virus bronchiolitis: epidemiology and pathology (1986) Amer. J. Dis. Child., 140, pp. 34-40; Brandt, C.D., Kim, H.W., Arribio, J.O., Epidemiology of respiratory syncytial virus infection in Washington D.C. III Composite analyses of eleven consecutive yearly epidemics (1973) Am. J. Epidemiol., 98, pp. 355-364; Stott, E.S., Taylor, G., Respiratory syncytial virus: Brief review (1985) Arch. Virol., 84, pp. 1-52",,,,15692582,,,,"English","Princ. Med. Biol.",Article,"Final",,Scopus,2-s2.0-77957067267
"Garoff H., Hewson R., Opstelten D.-J.E.","7004925644;36776805700;7003742658;","Virus maturation by budding",1998,"Microbiology and Molecular Biology Reviews","62","4",,"1171","1190",,268,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031770392&partnerID=40&md5=8ee687c2d9ac6989371e67825e0a306b","Department of Biosciences at Novum, S-141 57 Huddinge, Sweden; Department of Biosciences at Novum, Karolinska Institutet, S-141 57 Huddinge, Sweden; Ctr. of Appl. Microbiol. and Res., Viral Pathogens Unit, Porton Down, Salisbury, United Kingdom","Garoff, H., Department of Biosciences at Novum, S-141 57 Huddinge, Sweden, Department of Biosciences at Novum, Karolinska Institutet, S-141 57 Huddinge, Sweden; Hewson, R., Department of Biosciences at Novum, S-141 57 Huddinge, Sweden, Ctr. of Appl. Microbiol. and Res., Viral Pathogens Unit, Porton Down, Salisbury, United Kingdom; Opstelten, D.-J.E., Department of Biosciences at Novum, S-141 57 Huddinge, Sweden","Enveloped viruses mature by budding at cellular membranes. It has been generally thought that this process is driven by interactions between the viral transmembrane proteins and the internal virion components (core, capsid, or nucleocapsid). This model was particularly applicable to alphaviruses, which require both spike proteins and a nucleocapsid for budding. However, genetic studies have clearly shown that the retrovirus core protein, i.e., the Gag protein, is able to form enveloped particles by itself. Also, budding of negative-strand RNA viruses (rhabdoviruses, orthomyxoviruses, and paramyxoviruses) seems to be accomplished mainly by internal components, most probably the matrix protein, since the spike proteins are not absolutely required for budding of these viruses either. In contrast, budding of coronavirus particles can occur in the absence of the nucleocapsid and appears to require two membrane proteins only. Biochemical and structural data suggest that the proteins, which play a key role in budding, drive this process by forming a three-dimensional (cage-like) protein lattice at the surface of or within the membrane. Similarly, recent electron microscopic studies revealed that the alphavirus spike proteins are also engaged in extensive lateral interactions, forming a dense protein shell at the outer surface of the viral envelope. On the basis of these data, we propose that the budding of enveloped viruses in general is governed by lateral interactions between peripheral or integral membrane proteins. This new concept also provides answers to the question of how viral and cellular membrane proteins are sorted during budding. In addition, it has implications for the mechanism by which the virion is uncoated during virus entry.",,"capsid protein; gag protein; membrane protein; virus envelope protein; virus protein; vitronectin; article; cell maturation; coronavirus; molecular interaction; nonhuman; orthomyxovirus; paramyxovirus; protein interaction; protein targeting; retrovirus; three dimensional imaging; virogenesis; virus envelope; virus morphology; Gene Expression Regulation, Viral; Gene Products, gag; RNA Viruses; Viral Envelope Proteins; Virion; Alphavirus; Coronavirus; DNA viruses; Miridae; Orthomyxoviridae; Paramyxoviridae; RNA viruses; unidentified retrovirus","Acheson, N.H., Tamm, I., Replication of Semliki Forest virus: An electron microscopic study (1967) Virology, 32, pp. 128-143; Aronoff, R., Hajjar, A.M., Linial, M.L., Avian retroviral RNA encapsidation: Reexamination of functional 5′ RNA sequences and the role of nucleocapsid cys-his motifs (1993) J. 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Virol., 66, pp. 4966-4971; Yu, X., Yuan, X., McLane, M.F., Lee, T.-H., Essex, M., Mutations in the cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein impair the incorporation of env proteins into mature virions (1993) J. Virol., 67, pp. 213-221; Zavada, J., The pseudotypic paradox (1982) J. Gen. Virol., 63, pp. 15-24; Zhang, J., Lamb, R.A., Characterization of the membrane association of the influenza virus matrix protein in living cells (1996) Virology, 225, pp. 255-266; Zhao, H., Lindqvist, B., Garoff, H., Von Bonsdorff, C.-H., Liljeström, P., A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding (1994) EMBO J., 13, pp. 4204-4211; Zhao, H., Garoff, H., The M1 and NP proteins of influenza A virus form homo- But not heterooligomeric complexes when coexpressed in BHK-21 cells (1998) J. Gen. Virol., 79, pp. 2435-2446; Zhirnov, O.P., Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent (1992) Virology, 186, pp. 324-330; Zhou, W., Parent, L.J., Wills, J.W., Resh, M.D., Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 gag protein which interacts with acidic phospholipids (1994) J. Virol., 68, pp. 2556-2569; Zhou, W., Resh, M.D., Differential membrane binding of the human immunodeficiency virus type 1 matrix protein (1996) J. Virol., 70, pp. 8540-8548; Ziemiecki, A., Garoff, H., Subunit composition of the membrane glycoprotein complex of Semliki Forest virus (1978) J. Mol. Biol., 122, pp. 259-269; Ziemiecki, A., Garoff, H., Simons, K., Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell (1980) J. Gen. Virol., 50, pp. 111-123; Zingler, K., Littman, D.R., Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases env incorporation into particles and fusogenicity and infectivity (1993) J. Virol., 67, pp. 2824-2831","Garoff, H.; Department of Biosciences at Novum, Karolinska Institutet, S-141 57 Huddinge, Sweden; email: henrik.garoff@cbt.ki.se",,,10922172,,MMBRF,"9841669","English","Microbiol. Mol. Biol. Rev.",Article,"Final",,Scopus,2-s2.0-0031770392
"Atmar R.L., Guy E., Guntupalli K.K., Zimmerman J.L., Bandi V.D., Baxter B.D., Greenberg S.B.","7005296248;7006541788;35546311800;7401859884;9840181600;7102396651;7402294401;","Respiratory tract viral infections in inner-city asthmatic adults",1998,"Archives of Internal Medicine","158","22",,"2453","2459",,163,"10.1001/archinte.158.22.2453","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032556660&doi=10.1001%2farchinte.158.22.2453&partnerID=40&md5=1fc85b39caf56aa9f2daf95dfd1f0b93","Department of Medicine, Baylor College of Medicine, Houston, TX, United States; Dept. of Microbiol. and Immunology, Baylor College of Medicine, Houston, TX, United States; Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Atmar, R.L., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Dept. of Microbiol. and Immunology, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Guy, E., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Guntupalli, K.K., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Zimmerman, J.L., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Bandi, V.D., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States; Baxter, B.D., Dept. of Microbiol. and Immunology, Baylor College of Medicine, Houston, TX, United States; Greenberg, S.B., Department of Medicine, Baylor College of Medicine, Houston, TX, United States, Dept. of Microbiol. and Immunology, Baylor College of Medicine, Houston, TX, United States, Medicine Service, Ben Taub General Hospital, Houston, TX, United States, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Background: Respiratory tract viral infections (RTVIs) have been identified frequently in association with asthma exacerbations in children, but few studies have shown similar rates of viral infections in adults with asthma. Further studies using newer diagnostic techniques to evaluate the frequency of RTVIs in adults with acute exacerbations of asthma need to be performed. Methods: Twenty-nine asthmatic adults were recruited from the pulmonary clinic of an urban county hospital and were followed up in a longitudinal cohort study for signs and symptoms of asthma and RTVI. One hundred twenty-two asthmatic adults presenting to the emergency department (ED) of the same hospital with acute symptoms of asthma underwent evaluation for RTVI in a cross-sectional prevalence study. In both studies, respiratory secretions and paired serum samples were collected from subjects with acute wheezing episodes and evaluated using virus culture, serologic testing, and reverse transcription-polymerase chain reaction (RT-PCR). Results: In the longitudinal cohort study, 138 respiratory illnesses, of which 87 were asthma exacerbations, were evaluated; 41% of all illnesses and 44% of asthma exacerbations were associated with an RTVI. In the ED study, 148 asthma exacerbations were evaluated; 55% were associated with an RTVI. An RTVI was identified in 21 (50%) of 42 of the subjects hospitalized in the ED study. Picornaviruses (rhinoviruses), coronaviruses, and influenza viruses were the most commonly identified causes of RTVI. Forty-six (60%) of the 77 picornavirus infections and 22 (71%) of the 31 coronavirus infections were identified only using RT-PCR. Conclusions: Asthmatic exacerbations in adults are frequently associated with an RTVI. Identification of such infections often requires newer diagnostic methods, such as virus-specific RT-PCR. The high frequency of RTVIs identified in association with asthmatic exacerbations in adults from the inner city suggests that strategies for the prevention of RTVI should be targeted toward this population.",,"adolescent; adult; aged; article; asthma; Coronavirus; disease association; female; human; Influenza virus; major clinical study; male; Picornavirus; priority journal; respiratory tract infection; reverse transcription polymerase chain reaction; Rhinovirus; serodiagnosis; urban population; virus culture; virus infection","Adams, P.F., Marano, M.A., Current estimates from the National Health Interview Survey, 1994 (1995) Vital Health Stat 10, 193, p. 94; Weiss, K.B., Wagener, D.K., Changing patterns of asthma mortality: Identifying target populations at high risk (1990) JAMA, 264, pp. 1683-1687; Asthma mortality and hospitalization among children and young adults: United States, 1980-1993 (1996) MMWR Morb Mortal Wkly Rep, 45, pp. 350-353; Weiss, K.B., Gergen, P.J., Crain, E.F., Inner-city asthma: The epidemiology of an emerging US public health concern (1992) Chest, 101 (6 SUPPL.), pp. 362S-367S; 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Huhti, E., Mokka, T., Nikoskelainen, J., Halonen, P., Association of viral and mycoplasma infections with exacerbations of asthma (1974) Ann Allergy, 33, pp. 145-149; Minor, T.E., Dick, E.C., Baker, J.W., Ouellette, J.J., Cohen, M., Reed, C.E., Rhinovirus and influenza type A infections as precipitants of asthma (1976) Am Rev Respir Dis, 113, pp. 149-153; Clarke, C.W., Relationship of bacterial and viral infection to exacerbations of asthma (1979) Thorax, 34, pp. 344-347; Hudgel, D.W., Langston, L., Selner, J.C., McIntosh, K., Viral and bacterial infections in adults with chronic asthma (1979) Am Rev Respir Dis, 120, pp. 393-397; Beasley, R., Coleman, E., Hermon, Y., Holst, T.V., O'Donnell, T.V., Tobias, M., Viral respiratory tract infection and exacerbations of asthma in adult patients (1988) Thorax, 43, pp. 679-683; Bardin, P.G., Johnston, S.L., Pattemore, P.K., Viruses as precipitants of asthma symptoms, II: Physiology and mechanisms (1992) Clin Exp Allergy, 2, pp. 809-822; Corne, J.M., Holgate, S.T., Mechanisms of virus induced exacerbations of asthma (1997) Thorax, 52, pp. 380-389; Empey, D.W., Laitinen, L.A., Jacobs, L., Gold, W.M., Nadel, J.A., Mechanisms of bronchial hyperreactivity in normal subjects after respiratory tract infection (1976) Am Rev Respir Dis, 113, pp. 131-139; Lemanske Jr., R.F., Dick, E.C., Swenson, C.A., Vrtis, R.F., Busse, W.W., Rhinovirus upper respiratory infection increases airway hyperreactivity and late asthmatic reactions (1989) J Clin Invest, 83, pp. 1-10; Calhoun, W.J., Swenson, C.A., Dick, E.C., Schwartz, L.B., Lemanske Jr., R.F., Busse, W.W., Experimental rhinovirus 16 infection potentiates histamine release after antigen bronchoprovocation in allergic subjects (1991) Am Rev Respir Dis, 144, pp. 1267-1273; Grunberg, K., Timmers, M.C., Smits, H.H., Effect of experimental rhinovirus 16 colds on airway hyperresponsiveness to histamine and interleukin-8 in nasal lavage in asthmatic subjects in vivo (1997) Clin Exp Allergy, 27, pp. 36-45; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Am J Respir Crit Care Med, 151, pp. 879-886; Naclerio, R.M., Proud, D., Lichtenstein, L.M., Kinins are generated during experimental rhinoviral colds (1987) J Infect Dis, 157, pp. 133-142; Einarsson, O., Geba, G.P., Zhu, Z., Landry, M., Elias, J.A., Interleukin-11: Stimulation in vivo and in vitro by respiratory viruses and induction of airways hyperresponsiveness (1996) J Clin Invest, 97, pp. 915-924; Jenkins, C.R., Breslin, A.B.X., Upper respiratory tract symptoms in experimental rhinovirus infection (1984) Am Rev Respir Dis, 130, pp. 879-883; Halperin, S.A., Eggleston, P.A., Beasley, P., Exacerbations of asthma in adults during experimental rhinovirus infection (1985) Am Rev Respir Dis, 132, pp. 976-980; Gottlieb, D.J., Beiser, A.S., O'Connor, G.T., Poverty, race, and medication use are correlates of asthma hospitalization rates: A small area analysis in Boston (1995) Chest, 108, pp. 28-35; Call, R.S., Smith, T.F., Morris, E., Chapman, M.D., Platts-Mills, T.A., Risk factors for asthma in inner city children (1992) J Pediatr, 121, pp. 862-866; Rosenstreich, D.L., Eggleston, P., Kattan, M., The role of cockroach allergy and exposure to cockroach allergen in causing morbidity among inner-city children with asthma (1997) N Engl J Med, 336, pp. 1356-1363; Malveaux, F.J., Houlihan, D., Diamond, E.L., Characteristics of asthma mortality and morbidity in African-Americans (1993) J Asthma, 30, pp. 431-437; Murray, M.D., Stang, P., Tierney, W.M., Health care use by inner-city patients with asthma (1997) J Clin Epidemiol, 50, pp. 167-174; Evans III, R., Mullally, D.I., Wilson, R.W., National trends in the morbidity and morality of asthma in the US: Prevalence, hospitalization and death from asthma over two decades: 1965-1984 (1987) Chest, 91 (6 SUPPL.), pp. 65S-74S; Jamason, P.F., Kalkstein, L.S., Gergen, P.J., A synoptic evaluation of asthma hospital admissions in New York City (1997) Am J Respir Crit Care Med, 156, pp. 1781-1788; Matus, I., Bush, D., Asthma attack frequency in a pediatric population (1979) Psychosom Med, 41, pp. 629-636; Strunk, R.C., Mrazek, D.A., Fuhrmann, G.S., LaBrecque, J.F., Physiologic and psychological characteristics associated with deaths due to asthma in childhood: A case-controlled study (1985) JAMA, 254, pp. 1193-1198; Weiss, S.T., Tager, I.B., Speizer, F.E., Rosner, B., Persistent wheeze: Its relation to respiratory illness, cigarette smoking, and level of pulmonary function in a population sample of children (1980) Am Rev Respir Dis, 122, pp. 697-707; Murray, A.B., Morrison, B.J., Effect of passive smoking on asthmatic children who have and who have not had atopic dermatitis (1992) Chest, 101, pp. 16-18; Platts-Mills, T.A.E., Carter, M.C., Asthma and indoor allergens (1997) N Engl J Med, 336, pp. 1382-1384; Hahn, D.L., Dodge, R.W., Golubjatnikov, R., Association of Chlamydia pneumoniae (strain TWAR) infection with wheezing, asthmatic bronchitis, and adult-onset asthma (1991) JAMA, 266, pp. 225-230","Greenberg, S.B.; Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; email: stepheng@bcm.tmc.edu",,"American Medical Association",00039926,,AIMDA,"9855383","English","Arch. Intern. Med.",Article,"Final",,Scopus,2-s2.0-0032556660
"Kasai H., Morita E., Hatakeyama K., Sugiyama K.","36152810000;7102013872;7202837552;57210523397;","Characterization of haemagglutinin-esterase protein (HE) of murine corona virus DVIM by monoclonal antibodies",1998,"Archives of Virology","143","10",,"1941","1948",,1,"10.1007/s007050050431","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031731930&doi=10.1007%2fs007050050431&partnerID=40&md5=33ed223be64122c8a6294935000c6d3f","Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan; Dept. of Microbiology and Immunology, Medical School, Tohoku University, Sendai, Japan; Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan","Kasai, H., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Dept. of Microbiology and Immunology, Medical School, Tohoku University, Sendai, Japan; Morita, E., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Dept. of Microbiology and Immunology, Medical School, Tohoku University, Sendai, Japan; Hatakeyama, K., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan; Sugiyama, K., Department of Biology, Faculty of Science, Hirosaki University, Hirosaki, Japan, Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan","We analyzed the characteristics of seven monoclonal antibodies (mAbs) raised against purified HE (hemagglutinin-esterase) glycoprotein of the murine coronavirus DVIM (diarrhea virus of infant mice). Immunocrossreaction of these mAbs with JHM and/or MHV-S suggest that antigenic epitopes of HE of DVIM are similar to those of JHM and/or MHV-S. Four mAbs (1b4, 3a28, 4c19, 10b7), designated as group A mAbs, strongly inhibited both HA and AE activities. On the other hand, three mAbs (5a3, 6a6, 13a4), referred to as group B, had a comparatively weak HA inhibition activity. These results indicate that the antigenic epitopes of this glycoprotein can be classified into at least two groups and that the functional sites of HA and AE activities are similar but not identical. Neutralizing activity was shown in group A mAbs exclusively, suggesting that the ratio of HA and/or AE activities may play important roles in the cell fusion activity of DVIM-infected cells.",,"cell fusion; enzyme activity; enzyme analysis; enzyme inhibition; hemagglutinin esterase; monoclonal antibody; murine coronavirus; virus antigen; virus infection; virus protein; Animals; Antibodies, Monoclonal; Coronavirus; Hemagglutinins, Viral; Mice; Viral Fusion Proteins; Viral Proteins; Corona virus; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus (strain S)","Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J Virol, 61, pp. 185-189; Gagneten, S., Goutg, O., Dubois-Dalco, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that express the hemagglutininesterase glycoprotein (1995) J Virol, 69, pp. 889-895; Holmes, K., Coronaviridae and replication (1990) Virology, 2nd Ed., pp. 842-856. , Fields BN, Knipe DM (eds) Raven Press, New York; Siddel, S., Wege, H., Ter Meulen, V., The structure and replication of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 131-163; Sturman, L.S., Holmes, K.V., The molecular biology of coronavirus (1983) Adv Virus Res, 28, pp. 35-112; Sugiyama, K., Amano, Y., Hemagglutination and structural polypeptides of a new coronavirus associated with diarrhea in infant mice (1980) Arch Virol, 66, pp. 95-105; Sugiyama, K., Ishikawa, R., Fukuhara, N., Structural polypeptides of the murine coronavirus DVIM (1986) Arch Virol, 89, pp. 245-254; Sugiyama, K., Kasai, M., Kato, S., Kasai, H., Hatakeyama, K., Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (1998) Arch Virol, 143, pp. 1523-1534; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus a receplor-destroying enzyme with acetylesterase activity (1988) J Virol, 62, pp. 4686-4690","Sugiyama, K.; Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036, Japan",,,03048608,,ARVID,"9856082","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0031731930
"Schoenthaler S.L., Kapil S.","57103411500;7003293348;","Development and applications of a bovine coronavirus antigen detection enzyme-linked immunosorbent assay",1999,"Clinical and Diagnostic Laboratory Immunology","6","1",,"130","132",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032902656&partnerID=40&md5=b4b336c5de7f938e52e4044c8f7bef5c","Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-5606, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; University of Kansas Medical Center, Kansas City, KS 66103, United States","Schoenthaler, S.L., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-5606, United States, University of Kansas Medical Center, Kansas City, KS 66103, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-5606, United States, Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","We developed a monoclonal antibody-based, antigen capture sandwich enzyme-linked immunosorbent assay (ELISA) for bovine coronavirus. We compared the ELISA with electron microscopy and the hemagglutination test and found a close correlation between them. The sensitivity of the ELISA was 104 bovine coronavirus particles per ml of 10% fetal suspension. Compared with electron microscopy, bovine coronavirus ELISA had 96% specificity.",,"animal cell; animal tissue; antigen detection; article; cattle; coronavirus; diagnostic accuracy; diagnostic value; electron microscopy; enzyme linked immunosorbent assay; hemagglutination; intermethod comparison; nonhuman; priority journal; virus isolation; Animals; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; Evaluation Studies; Feces; Hemagglutination Tests; Microscopy, Electron; Sensitivity and Specificity","Craig, R.A., Kapil, S., (1994) Detection of Novel Enteric Viruses in Wisconsin Livestock, , American Association of Veterinary Laboratory Diagnosticians, Grand Rapids, Mich; Crouch, C.F., Bielefeldt Ohmann, H., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J. Gen. Virol., 66, pp. 1489-1500; Crouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture enzyme-linked immunosorbent assay for detection of bovine enteric coronavirus (1984) J. Clin. Microbiol., 19, pp. 388-393; Czerny, C.-P., Eichhorn, W., Characterization of monoclonal and polyclonal antibodies to bovine enteric coronavirus: Establishment of an efficient ELISA for antigen detection in feces (1989) Vet. Microbiol., 20, pp. 111-122; Goding, J., Purification, fragmentation and isotopic labelling of monoclonal antibodies (1986) Monoclonal Antibodies: Principles and Practice, pp. 104-141. , J. W. Goding (ed.), Academic Press, San Diego, Calif; Heckert, R.A., Saif, L.J., Myers, G.W., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immunofluorescence of nasal epithelial cells (1989) Vet. Microbiol., 19, pp. 217-231; Kapil, S., Basaraba, R.J., Infectious bovine rhinotracheitis, parainfluenza-3 and bovine respiratory coronavirus (1997) Vet. Clin. N. Am. Food Anim. Pract., 13, pp. 455-469; Reynolds, D.J., Chasey, D., Scott, A.C., Bridger, J.C., Evaluation of ELISA and electron microscopy for the detection of coronavirus and rotavirus in bovine faeces (1984) Vet. Rec., 114, pp. 397-401; Saif, L.A., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet., 80, pp. 303-311; Sato, M., Akashi, H., Detection of bovine coronavirus by enzyme-linked immunosorbent assay using monoclonal antibodies (1993) J. Vet. Med. Sci., 55, pp. 771-774; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J. Vet. Diagn. Investig., 8, pp. 99-105; Thorns, C.J., Bell, M.M., Chasey, D., Chesham, J., Roeder, P.L., Development of monoclonal antibody ELISA for simultaneous detection of bovine coronavirus, rotavirus serogroup A, and Escherichia coli K99 antigen in feces of calves (1992) Am. J. Vet. Res., 53, pp. 36-43; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Minocha, H.C., Kapil, S., Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalin-fixed intestins (1997) J. Clin. Microbiol., 35, pp. 2964-2965","Kapil, S.; Dept. Diagnostic Medicine-Pathobiol., College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,1071412X,,CDIME,"9874676","English","Clin. Diagn. Lab. Immunol.",Article,"Final",,Scopus,2-s2.0-0032902656
"Folz R.J., Elkordy M.A.","7003831884;14524779100;","Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer",1999,"Chest","115","3",,"901","905",,44,"10.1378/chest.115.3.901","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032995664&doi=10.1378%2fchest.115.3.901&partnerID=40&md5=c03b9a1e8428a488fd5006b66c03090e",,"Folz, R.J.; Elkordy, M.A.","Infectious bronchitis virus, otherwise known as coronavirus, can cause mild upper respiratory tract illnesses in children and adults. Rarely has coronavirus been linked, either by serology or nasal wash, to pneumonia. We report a ease of a young woman who, following treatment for stage IIIA breast cancer using a high-dose chemotherapy regimen followed by autologous bone marrow and stem cell transplantation, developed respiratory failure and was found to have coronavirus pneumonia as diagnosed by electron microscopy from BAL fluid. We propose that coronavirus should be considered in the differential diagnosis of acute respiratory failure in cancer patients who have undergone high-dose chemotherapy and autologous hematopoietic support.","Bone marrow transplantation; Breast cancer; Coronavirus pneumonia; High- dose chemotherapy; Idiopathic pneumonia syndrome","antineoplastic agent; clarithromycin; cotrimoxazole; cyclophosphamide; doxorubicin; erythromycin; fluorouracil; imipenem; methylprednisolone; prednisone; acute respiratory failure; adult; article; autologous bone marrow transplantation; breast cancer; cancer chemotherapy; case report; Coronavirus; differential diagnosis; disease course; electron microscopy; female; human; interstitial pneumonia; lung lavage; priority journal; stem cell transplantation; thorax radiography; virus pneumonia","Weiner, R.S., Boymer, M.M., Gale, R.P., Interstitial pneumonitis after bone marrow transplantation (1986) Ann Intern Med, 104, pp. 168-175; Wingard, J.R., Mellits, E.D., Sostrin, M.B., Interstitial pneumonitis after allogeneic bone marrow transplantation (1988) Medicine, 67, pp. 175-186; Jones, R.B., Matthes, S., Shpall, E.J., Acute lung injury following treatment with high-dose cyclophosphamide, cisplatin, and carmustine: Pharmacodynamic evaluation of carmustine (1993) J Natl Cancer Inst, 85, pp. 640-647; Clark, J.G., Hansen, J.A., Hertz, M.I., Idiopathic pneumonia syndrome after bone marrow transplantation (1993) Am Rev Respir Dis, 147, pp. 1601-1606; Cherniack, R.M., Abrams, J., Kalica, A.R., Pulmonary disease associated with breast cancer therapy (1994) Am J Respir Crit Care Med, 150, pp. 1169-1173; Wilczynski, S.W., Erasmus, J.J., Petros, W.P., Delayed pulmonary toxicity syndrome following high-dose chemotherapy and bone marrow transplantation for breast cancer (1998) Am J Respir Crit Care Med, 157, pp. 565-573; Wilczynski, S.W., Petros, W.P., Hussein, A.M., Increased incidence of pulmonary toxicity in breast cancer patients undergoing high dose chemotherapy (1996) Am J Respir Crit Care Med, 153, pp. A273; Patz E.F., Jr., Peters, W.P., Goodman, P.C., Pulmonary drug toxicity following high-dose chemotherapy with autologous bone marrow transplantation: CT findings in 20 cases (1994) J Thorac Imaging, 9, pp. 129-134; Aronin, P.A., Mahaley M.S., Jr., Rudnick, S.A., Prediction of BCNU pulmonary toxicity in patients with malignant gliomas (1980) N Engl J Med, 303, pp. 183-188; Rabinowitz, J., Petros, W.P., Stuart, A.R., Characterization of endogenous cytokine concentrations after high-dose chemotherapy with autologous bone marrow support (1993) Blood, 81, pp. 2452-2459; Murase, T., Anscher, M.S., Petros, W.P., Changes in plasma transforming growth factor beta in response to high-dose chemotherapy for stage II breast cancer: Possible implications for the prevention of hepatic veno-occlusive disease and pulmonary drug toxicity (1994) Bone Marrow Transplant, 15, pp. 173-178; Englund, J.A., Sullivan, C.J., Jordan, M.C., Respiratory syncytial virus infection in immunocompromised adults (1988) Ann Int Med, 109, pp. 203-208; Fouillard, L., Mouthon, L., Laporte, J.P., Sever respiratory syncytial virus pneumonia after autologous bone marrow transplantation: A report of three cases and review (1992) Bone Marrow Transplant, 9, pp. 97-100; Smith, A.C., Boyd, M.R., Preferential effects of 1,3-bis(2-chloroethyl)-1-nitrosurea (BCNU) on pulmonary glutathione reductase and glutathione/glutathione disulfide ratios: Possible implications for lung toxicity (1984) J Pharmacol Exp Ther, 229, pp. 658-663; Kaye, H.S., Marsh, H.B., Dowdle, W.R., Seroepidemiologic survey of coronavirus (strain OC43) related infections in a children's population (1971) Am J Epidemiol, 94, pp. 43-49; Hendley, J.O., Fishburne, H.B., Gwaltney, J.M., Coronavirus infections in working adults: Eight year study with 229E and OC43 (1972) Am Rev Respir Dis, 105, pp. 805-811; Hamre, D., Beem, M., Virologic studies of acute respiratory disease in young adults: V. Coronavirus 229E infections during 6 years of surveillance (1972) Am J Epidemiol, 96, pp. 94-106; McIntosh, K., Chao, R.K., Krause, H.E., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Wenzel, R.P., Hendley, J.O., Davies, J.A., Coronavirus infections in military recruits (1974) Am Rev Respir Dis, 109, pp. 621-624; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J Med Virol, 6, pp. 259-265; Todd, N.W., Peters, W.P., Ost, A.H., Pulmonary drug toxicity in patients with primary breast cancer treated with high-dose combination chemotherapy and autologous bone marrow transplantation (1993) Am Rev Respir Dis, 147, pp. 1264-1270; Fulkerson, W.J., McLendon, R.E., Prosnitz, L.R., Adult respiratory distress syndrome after limited thoracic radiotherapy (1986) Cancer, 57, pp. 1941-1946; Bhatt, P.N., Jacoby, R., Jonas, A.M., Respiratory infection in mice with sialodacryoadenitis virus, a coronavirus of rats (1977) Infect Immun, 18, pp. 823-827; Jabrane, A., Girard, C., Elazhary, Y., Pathogenicity of porcine respiratory coronavirus isolated in Quebec (1994) Can Vet J, 35, pp. 86-92; Bradburne, A.F., Bynoe, M.L., Tyrrell, D.A.J., Effects of a 'new' human respiratory virus in volunteers (1967) BMJ, 3, pp. 767-769; Reed, S.E., The behavior of recent isolates of human respiratory coronavirus in vitro and in volunteers: Evidence of heterogeneity among 229E-related strains (1984) J Med Virol, 13, pp. 179-192; Bende, M., Barrow, I., Heptonstall, J., Changes in human nasal mucosa during experimental coronavirus common colds (1989) Acta Otolaryngol (Stockh), 107, pp. 262-269; Higgins, P.G., Phillpotts, R.J., Scott, G.M., Intranasal interferon as protection against experimental respiratory coronavirus infection in volunteers (1983) Antimicrob Agents Chemother, 24, pp. 713-715; Turner, R.B., Felton, A., Kosak, K., Prevention of experimental coronavirus colds with intranasal α-2b interferon (1986) J Infect Dis, 154, pp. 443-447; Barrow, G.I., Higgins, P.G., Al-Nakib, W., The effect of intranasal nedocromil sodium on viral upper respiratory tract infections in human volunteers (1990) Clin Exp Allergy, 20, pp. 45-51; Single-breath carbon monoxide diffusing capacity (transfer factor) (1995) Am J Respir Crit Care Med, 152, pp. 2185-2198","Folz, R.J.; Duke University Medical Center, Div. of Pulmonary/Critical Care Med., Box 2620, Durham, NC 27710, United States; email: folz0001@mc.duke.edu",,"American College of Chest Physicians",00123692,,CHETB,"10084516","English","Chest",Article,"Final",Open Access,Scopus,2-s2.0-0032995664
"Uzelac-Keserović B., Spasić P., Bojanić N., Dimitrijević J., Lako B., Lepsanović Z., Kuljić-Kapulica N., Vasić D., Apostolov K.","6508258267;7003693254;7006036067;7005994770;57213761645;6602680262;6603748034;18937799700;57213866586;","Isolation of a coronavirus from kidney biopsies of endemic Balkan nephropathy patients",1999,"Nephron","81","2",,"141","145",,20,"10.1159/000045269","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032999834&doi=10.1159%2f000045269&partnerID=40&md5=6e0fc53835f3b26a9c19b83cfa9c4651","Institute of Virology 'Torlak', Belgrade, Serbia; Medical Military Academy, Belgrade, Serbia; Department of Urology, Doboj District Hospital, Doboj, Serbia; Virology Department, Royal Postgraduate Medical School, London, Serbia; 9 Forest Ridge, Beckenham. Kent BR3 3NH, Serbia","Uzelac-Keserović, B., Institute of Virology 'Torlak', Belgrade, Serbia; Spasić, P., Medical Military Academy, Belgrade, Serbia; Bojanić, N., Medical Military Academy, Belgrade, Serbia; Dimitrijević, J., Medical Military Academy, Belgrade, Serbia; Lako, B., Medical Military Academy, Belgrade, Serbia; Lepsanović, Z., Medical Military Academy, Belgrade, Serbia; Kuljić-Kapulica, N., Medical Military Academy, Belgrade, Serbia; Vasić, D., Department of Urology, Doboj District Hospital, Doboj, Serbia; Apostolov, K., Virology Department, Royal Postgraduate Medical School, London, Serbia, 9 Forest Ridge, Beckenham. Kent BR3 3NH, Serbia","Endemic Balkan nephropathy (EBN) is a kidney disease of unknown etiology limited to Bulgaria, Rumania and former Yugoslavia. Primary kidney tissue cultures were established as explants from tissue obtained at operations from 5 EBN patients with urinary tract tumors. Four out of the five biopsy specimens on extended culture incubation at 33°C yielded a coronavirus virus (EBNV) which was cytopathogenic for human fibroblast and Vero cells. In cells inoculated with EBNV, cytoplasmic immunofluorescence was found using antisera for human coronaviruses OC43 and 229E as well as the porcine transmissible gastroenteric virus and avian (chicken) bronchitis virus. In neutralization tests, EBNV failed to react with antisera to these viruses. Using hyperimmune serum raised with EBNV, positive cytoplasmic immunofluorescence was seen with cells infected with OC43, 229E, TGV and significantly with the kidney tissue of the biopsy specimens from the EBN patients. A screen for neutralizing antibody using the EBN virus revealed that 87.2% of EBN patients on dialysis were positive, also 74% of people from an endemic area were also positive, while only 13.5% from outside were positive. It is suggested that a coronavirus is involved in the etiology of the disease and that humans are an incidental host of a coronavirus zoonosis.","Endemic balkan nephropathy; Isolation of coronavirus","hyperimmune globulin; neutralizing antibody; article; Bulgaria; clinical article; controlled study; Coronavirus; cytopathogenic effect; cytoplasm; dialysis; fibroblast; human; human tissue; immunofluorescence; interstitial nephritis; kidney biopsy; priority journal; Romania; temperature; tissue culture; urinary tract tumor; Vero cell; virus isolation; Yugoslavia","Radovanović, Z., Epidemiology of endemic nephropathy (1985) Proc 3rd Symp Endemic Nephropathy, pp. 3-27. , Belgrade, Serbian Academy of Science Press; Danilović, V., Djurisić, M., Mokranjac, M., Stoimirović, B., Zivoinović, B., Stojković, P., Néphrites chronique provoquées par l'intoxication au plomb par voie digestive (farine) (1957) Presse Méd, 65, pp. 2039-2040; Krogh, P., Hald, B., Plestina, R., Ceović, Balkan (endemic) nephropathy and food-borne ochratoxin A: Preliminary results of a survey of foodstuffs (1997) Acta Pathol Microb Scand B, 85, pp. 238-240; Castegnaro, M., Chernozemsky, J., Endemic nephropathy and urinary tract tumours in the Balkans (1987) Cancer Res, 47, pp. 3608-3609; Polenaković, M.H., Stefanović, V., Balkan nephropathy (1992) Oxford Textbook of Clinical Nephrology, , Cameron S (ed). Oxford, Oxford Medical Publications; Apostolov, K., Spasić, P., Bojanić, N., Evidence of a viral aetiology in endemic (Balkan) nephropathy (1975) Lancet, 2, pp. 1271-1273; Apostolov, K., Spasić, P., Bojanić, N., Comparative ultrastructural studies on endemic (Balkan) nephropathy and chicken embryo nephritis caused by infectious bronchitis virus. I. Endemic (Balkan) nephropathy (1977) Acta Med Yug, 31, pp. 188-203; Apostolov, K., Spasić, P., Alexander, D., Comparative ultrastructural studies on endemic (Balkan) nephropathy and chicken embryo nephritis caused by infectious bronchitis virus. II. Chick embryo nephritis (1977) Acta Med Yug, 31, pp. 505-516; Schmidt, J.N., Cell culture techniques for diagnostic virology (1979) Diagnostic Procedures for Viral, Rickettsial and Chlamydial Infections, p. 65. , Lenette E, Schmidt N (eds), ed 5. Washington, American Public Health Association Press; Gardner, P.S., McQuillin, J., Rapid virus diagnosis (1980) Application of Immunofluorescence, p. 56. , London, Butterworths; Almeida, J.D., Tyrrell, D.A.J., The morphology of three previously uncharacterized human respiratory viruses that grow in organ culture (1967) J Gen Virol, 1, pp. 175-178; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fields' Virology, p. 1075. , Fields BN, Knipe DM. Howley PM et al (eds), ed 3. New York, Raven Press; McIntosh, K., Coronaviruses (1996) Fields' Virology, p. 1095. , Fields BN, Knipe DM, Howley PM et al (eds), ed 3. New York, Raven Press; Burks, S.J., DeVald, B.L., Jankovsky, D.L., Gerdes, C.J., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Murray, R.S., Cai, G.Y., Hoel, K., Johnson, S., Cabirac, G.F., Coronaviruses and multiple sclerosis (1993) Adv Exp Med Biol, 342, pp. 353-357; Kaye, H., Yarbrough, W., Reed, C., Harrison, K.A., Antigenic relationship between human coronaviruses strain OC43 and hemagglutinating encephalomyelitis virus strain 67N of swine. Antibody response in human and animal sera (1977) J Infect Dis, 135, pp. 201-209; Hall P.W. III, Damin, G.J., Balkan nephropathy (1978) Nephron, 22, pp. 281-300; Petković, S., The renal pelvic and ureteral tumors in regions of endemic nephropathy (1985) Proc 3rd Symp Endemic Nephropathy, pp. 279-289. , Belgrade, Serbian Academy of Science Press; Marković, B., Endemic nephritis and urinary tract cancer in Yugoslavia, Bulgaria and Rumania (1972) J Urol, 107, pp. 212-219; Hrisoho, D., Zafirovska, S., Bogdanovska, S., Medar, T., Distribution and frequency of endemic nephropathy in the province of Kosovo (1985) Proc 3rd Symp Endemic Nephropathy, pp. 61-66. , Belgrade, Serbian Academy of Science Press; Birtasević, B.B., Vuković, D., Drndarević, Z., Seguljev, M., Obradovic, D., Pokorni, V., Stanković, A., Foci of endemic nephropathy in the province of Vojvodina (1985) Proc 3rd Symp Endemic Nephropathy, pp. 53-59. , Belgrade, Serbian Academy of Science Press","Apostolov, K.9 Forest Ridge, Beckenham BR3 3NH, Serbia; email: apokoce@mcmail.com",,"S. Karger AG",00282766,,NPRNA,"9933748","English","Nephron",Article,"Final",,Scopus,2-s2.0-0032999834
"Luby J.A.P., Clinton R.E., Kurtz S.T.","35925941000;6701664612;57197299693;","Adaptation of human enteric coronavirus to growth in cell lines",1999,"Journal of Clinical Virology","12","1",,"43","51",,10,"10.1016/S0928-0197(98)00067-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033013846&doi=10.1016%2fS0928-0197%2898%2900067-1&partnerID=40&md5=20af20243b02d00f513315906f112580","UT Southwestern Medical Center, Div. Infect. Dis., 5323 Harry H., Dallas, TX 75235-9113, United States; 6102 Parliament, Austin, TX 78724, United States; 4129 Rowan Drive, Fort Worth, TX 76116, United States","Luby, J.A.P., UT Southwestern Medical Center, Div. Infect. Dis., 5323 Harry H., Dallas, TX 75235-9113, United States; Clinton, R.E., 6102 Parliament, Austin, TX 78724, United States; Kurtz, S.T., 4129 Rowan Drive, Fort Worth, TX 76116, United States","Background: The existence of human enteric coronavirus (HEC) has been debated since its first description in stool by electron microscopy (EM) in 1975. Needed to resolve the issue is its cultivation in readily available cell lines. Objectives: To grow HEC in cell lines. To describe its characteristics and to differentiate it from other human and animal coronaviruses. Study design: Originally grown in human fetal intestinal organ culture, HEC was passed in J774 cells (a mouse macrophage cell line) and C6/36 cells (a mosquito cell line). Its cytopathic effect (CPE) and pattern of immunofluorescence were described. Its appearance was ascertained by negative staining and transmission EM. Its structural proteins were delineated by polyacrylamide gel electrophoresis (PAGE) and Western blotting (WB). The antigenic character of the virus was determined by immunofluorescence and WB. Agglutination with mouse erythrocytes was performed. Results: In J774 cells, HEC induced the formation of giant cells and small syncytia. Immunofluorescence in both J774 and C6/36 cells was limited to the cytoplasm. Studies with transmission EM revealed the virus to have the typical appearance of other coronaviruses, to be 80-120 nm in diameter, and to bud into cysternae of the endoplasmic reticulum. By PAGE and WB, its major protein has an average molecular weight (MW) of 41 kilodaltons (kDa). Two other proteins had MWs of 190 and 24 kDa. By immunofluorescence and WB, HEC is antigenically distinct from human coronaviruses OC43 and 229E and mouse hepatitis virus (A59 strain). Preparations of HEC did not agglutinate mouse erythrocytes. Conclusion: We conclude that HEC is a human coronavirus that is antigenically unrelated to OC43 and 229E viruses. Growth of HEC in readily available cell lines should aid in elucidating its role as a pathogen in human diarrheal illnesses.","Adaptation; C6/36 cells; Growth in cell lines; Human enteric coronavirus; J774 cells","virus antigen; virus protein; animal cell; article; cell line; coronavirus; cytopathogenic effect; endoplasmic reticulum; enteric virus; giant cell; immunoblotting; immunofluorescence test; macrophage; mosquito; mouse; murine hepatitis coronavirus; nonhuman; polyacrylamide gel electrophoresis; priority journal; transmission electron microscopy; virogenesis; virus characterization; virus pathogenesis; Adaptation, Biological; Animals; Cell Line; Coronavirus; Coronavirus 229E, Human; Humans; Mice","Beards, G.M., Green, J., Hall, C., Flewett, T.H., Lamouliatte, F., Du Pasquier, P., An enveloped virus in stools of children and adults with gastroenteritis that resembles the Breda virus of calves (1984) Lancet, 1 (8385), pp. 1050-1052; Bencosme, S.A., Tsutsumi, V., A fast method for processing biologic material for electron microscopy (1970) Lab Invest, 23, pp. 447-450; Caul, E.O., Clarke, S.K.R., Coronavirus propagated from patient with non-bacterial gastroenteritis (1975) Lancet, 2, pp. 953-954; Caul, E.O., Paver, W.K., Clarke, S.K.R., Coronavirus particles in faeces from patients with gastroenteritis (1975) Lancet, 1, p. 1192; Chaney, C., Moscovici, O., Lebon, P., Rousset, S., Association of coronavirus infection with neonatal necrotizing enterocolitis (1982) Pediatrics, 69, pp. 209-214; Gerna, G., Cereda, P.M., Revello, M.G., Cattaneo, E., Battaglia, M., Gerna, M.T., Antigenic and biological relationships between human coronavirus OC43 and neonatal calf diarrhoea coronavirus (1981) J Gen Virol (Lond), 54, pp. 91-102; Gerna, G., Passarani, N., Cereda, P.M., Battaglia, M., Antigenic relatedness of human enteric coronavirus strains to human coronavirus OC43: A preliminary report (1984) J Infect Dis, 150, pp. 618-619; Gerna, G., Passarani, N., Battaglia, M., Rondanelli, E.G., Human enteric coronaviruses: Antigenic relatedness to human coronavirus OC43 and possible etiologic role in viral gastroenteritis (1985) J Infect Dis, 151, pp. 796-803; Grohmann, G.S., Glass, R.I., Pereira, H.G., Monroe, S.S., Hightower, R.W., Bryan, R.T., Enteric viruses and diarrhea in HIV-infected patients (1993) New Engl J Med, 329 (1), pp. 14-20. , for the Enteric Opportunistic Infections Working Group; Kern, P., Muller, G., Schmitz, H., Racz, P., Meigel, W., Riethmuller, G., Dietrich, M., Detection of coronavirus-like particles in homosexual men with acquired immunodeficiency and related lymphadenopathy syndrome (1985) Klin Wochenschrift, 63, pp. 68-72; Koopmans, M., Horzinek, M.C., Toroviruses of animals and humans: A review (1994) Adv Virus Res, 43, pp. 233-273; MacNaughton, M.R., Davies, H.A., Human enteric coronaviruses (1981) Arch Virol, 70, pp. 301-313; Mathan, M., Mathan, V.I., Swaminathan, S.P., Yesudoss, S., Baker, S.J., Pleomorphic virus-like particles in human faeces (1975) Lancet, 1, pp. 1068-1069; Mortensen, M.L., Ray, C.G., Payne, C.M., Friedman, A.D., Minnich, L.L., Rousseau, C., Coronaviruslike particles in human gastrointestinal disease (1985) Am J Dis Child, 139, pp. 928-934; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Rettig, P.J., Altshuler, G.P., Fatal gastroenteritis associated with coronaviruslike particles (1985) Am J Dis Child, 139, pp. 245-248; Rousset, S., Moscovici, O., Lebon, P., Barbet, J.P., Helardot, P., MacE, B., Bargy, F., Chaney, C., Intestinal lesions containing coronavirus-like particles in neonatal necrotizing enterocolitis: An ultrastructural analysis (1984) Pediatrics, 73, pp. 218-224; Schnagl, R.D., Holmes, I.J., MacKay-Scollay, E.M., Coronavirus-like particles in Aboriginals and non-Aboriginals in Western Australia (1978) Med J Aust, 1, pp. 307-309; Schnagl, R.D., Morey, F., Holmes, I.H., Rotavirus, coronavirus-like particles, bacteria and parasites in Central Australia (1979) Med J Aust, 2, pp. 115-118; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol, 169, pp. 169-178; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31 (3), pp. 1214-1222; Vaucher, Y.E., Ray, C.G., Minnich, L.L., Payne, C.M., Beck, D., Lowe, P., Pleomorphic, enveloped, virus-like particles associated with gastrointestinal illness in neonates (1982) J Infect Dis, 145, pp. 27-36; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 44, pp. 152-161","Luby, J.P.; UT Southwestern Medical Center, Division of Infectious Diseases, 5323 Harry Hines Blvd, Dallas, TX 75235-9113, United States",,,13866532,,JCVIF,"10073413","English","J. Clin. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033013846
"Gut M., Leutenegger C.M., Huder J.B., Pedersen N.C., Lutz H.","57213387515;7006706489;6701574143;7202299909;57202819852;","One-tube fluorogenic reverse transcription-polymerase chain reaction for the quantitation of feline coronaviruses",1999,"Journal of Virological Methods","77","1",,"37","46",,126,"10.1016/S0166-0934(98)00129-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032906092&doi=10.1016%2fS0166-0934%2898%2900129-3&partnerID=40&md5=f330f6b4f2723c72151dc02a5150fc6b","Clinical Laboratory, Dept. Int. Vet. Med., Univ. Z., Zurich, Switzerland; Swiss Natl. Center for Retroviruses, University of Zurich, Zurich, Switzerland; Center for Companion Animal Health, Sch. Vet. Med., Univ. of California, Davis, CA, United States","Gut, M., Clinical Laboratory, Dept. Int. Vet. Med., Univ. Z., Zurich, Switzerland; Leutenegger, C.M., Clinical Laboratory, Dept. Int. Vet. Med., Univ. Z., Zurich, Switzerland; Huder, J.B., Swiss Natl. Center for Retroviruses, University of Zurich, Zurich, Switzerland; Pedersen, N.C., Center for Companion Animal Health, Sch. Vet. Med., Univ. of California, Davis, CA, United States; Lutz, H., Clinical Laboratory, Dept. Int. Vet. Med., Univ. Z., Zurich, Switzerland","A one-tube reverse transcription-polymerase chain reaction (RT-PCR) for absolute feline coronavirus (FCoV) quantitation was developed. The assay is based on the 5' nuclease activity of the Thermus flavus (Tfl) polymerase and a fluorogenic probe which generates fluorescence when it is cleaved. The fluorogenic probe, also called TaqMan(TM) probe (Perkin Elmer, Foster City, USA), is an oligonucleotide designed to bind between the two PCR primers to the target cDNA and is labeled with a reporter and a quencher dye. In the intact probe, the quencher dye suppresses the fluorescence of the reporter dye by Forster-type energy transfer. During the polymerase extension steps the Tfl exonuclease activity cleaves the hybridised probe resulting in the generation of fluorescent emission of the reporter dye. The threshold cycle (C(T) value) indicates the increase of reporter fluorescence and is directly related to the initial amount of target cDNA or RNA, respectively. Fluorescence is monitored in real time after each cycle by a Perkin-Elmer ABI Prism® 7700 Sequence Detector. After completion of amplification, the C(T) values of the samples are calculated back to a standard curve, generated by amplification of diluted standard molecules. The one-tube RT-PCR described below allows precise quantitation, is highly sensitive, rapid (no separate reverse transcription step and no post-amplification steps), easy to handle, allows for a high sample throughput, shows a very good reproducibility, and can be executed with a low risk of contamination. The design of the primers-probe combination enables the detection of all known FCoV strains and is also useful for the detection of canine coronavirus, transmissible gastroenteritis virus and porcine respiratory coronavirus. Copyright (C) 1999 Elsevier Science B.V.","FCoV; Fluorogenic 5' nuclease assay; One-tube RT-PCR; Quantitation; TaqMan(TM); Viral RNA","exonuclease; RNA directed DNA polymerase; virus RNA; article; coronavirus; fluorescence; nonhuman; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; sequence analysis; virus detection; Animals; Base Sequence; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; DNA Primers; DNA Probes; DNA, Complementary; Dogs; Exodeoxyribonucleases; Fluorescent Dyes; Humans; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sensitivity and Specificity; Taq Polymerase; Canine coronavirus; Coronavirus; Felidae; Feline coronavirus; Porcine respiratory coronavirus; Suidae; Thermus thermophilus; Transmissible gastroenteritis virus","Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130 (7), pp. 133-137; Birnboim, H.C., Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA (1979) Nucleic Acids Res., 7 (6), pp. 1513-1523; Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen. Virol., 74 (PT 9), pp. 1795-1804; Dretzer, G., Bellard, M., Sassone-Corsi, P., Chambon, P., A reliable method for the recovery of DNA fragments from agarose and acrylamide gels (1981) Anal. Biochem., 112 (2), pp. 295-298; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A.P.M., Horziner, M.C., Lutz, H., Placebo-controlled evaluation of a modified life virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions (1997) Vaccine, 15 (10), pp. 1101-1109; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and faecal shedding from cats in multiple-cat environments (1997) J. Am. Vet. Med. Assoc., 210 (9), pp. 1307-1312; Förster, V.T., Zwischenmolekulare Energiewanderung und Fluoreszenz (1948) Ann. Phy., 2, pp. 55-57; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35 (3), pp. 673-675; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in faeces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33 (3), pp. 684-689; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (unpublished data); Kinoshita, T., Imamura, J., Nagai, H., Shimotohno, K., Quantification of gene expression over a wide range by the polymerase chain reaction (1992) Anal. Biochem., 206 (2), pp. 231-235; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet. Microbiol., 42 (1), pp. 65-77; Livak, K., Marmaro, J., Flood, S., Elmer, P., Guidelines for designing TaqMan™ fluorogenic probes for 5′ nuclease assays (1995) Perkin Elmer Applied Biosystems Research News, , December; Nagano, M., Kelly, P.A., Tissue distribution and regulation of rat prolactin receptor gene expression; Quantitative analysis by polymerase chain reaction (1994) J. Biol. Chem., 269 (18), pp. 13337-13345; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-22; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens, using feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42 (3), pp. 363-367; Singh, M., Tobler, K., Ackermann, M., A Novel Internal ORF Product Expressed from a Polycistronic Mrna of Porcine Epidemic Diarrhoea Virus Does Not Contribute to Viral Virulence, , (submitted for publication); Vennema, H., Poland, A., Hawkins, K.F., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Prac., 23 (3), pp. 40-44; Wang, A.M., Doyle, M.V., Mark, D.F., Quantitation of mRNA by the polymerase chain reaction (published erratum appears in Proc. Natl. Acad. Sci. USA, 1990 April 87 (7), 2865) (1989) Proc. Natl. Acad. Sci. USA, 86 (24), pp. 9717-9721","Gut, M.; Clinical Laboratory, Department Internal Veterinary Med., University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland; email: mgut@vetklinik.unizh.ch",,,01660934,,JVMED,"10029323","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0032906092
"Ziebuhr J., Siddell S.G.","7003783935;7005260816;","Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab",1999,"Journal of Virology","73","1",,"177","185",,51,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032888958&partnerID=40&md5=e97ee2f9fd1c225e66a991fb24f020fd","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Institute of Virology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","Ziebuhr, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Replicase gene expression by the human coronavirus 229E involves the synthesis of two large polyproteins, pp1a and pp1ab. Experimental evidence suggests that these precursor molecules are subject to extensive proteolytic processing. In this study, we show that a chymotrypsin-like enzyme, the virus-encoded 3C-like proteinase (3CL(pro)), cleaves within a common region of pp1a and pp1ab (amino acids 3490 to 4068) at four sites. trans-cleavage assays revealed that polypeptides of 5, 23, 12, and 16 kDa are processed from pp1a/pp1ab by proteolysis of the peptide bonds Q3546/S3547, Q3629/S3630, Q3824/N3825, and Q3933/A3934. Relative rate constants for the 3CL(pro)- mediated cleavages Q2965/A2966, Q3267/S3268, Q3824/N3825, and Q3933/A3934 were derived by competition experiments using synthetic peptides and recombinant 3CL(pro). The results indicate that coronavirus cleavage sites differ significantly with regard to their susceptibilities to proteolysis by 3CL(pro). Finally, immunoprecipitation with specific rabbit antisera was used to detect the pp1a/pp1ab processing end products in virus-infected cells, and immunofluorescence data that suggest an association of these polypeptides with intracellular membranes were obtained.",,"polypeptide; proteinase; rabbit antiserum; recombinant protein; RNA directed RNA polymerase; synthetic peptide; virus protein; article; chemical bond; controlled study; Coronavirus; human; human cell; immunofluorescence; immunoprecipitation; intracellular membrane; priority journal; protein degradation; protein processing","Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. Virol., 71, pp. 900-909; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; Eleouet, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Faaberg, K.S., Plagemann, P.G.W., Membrane association of the C-terminal half of the open reading frame la protein of lactate dehydrogenase-elevating virus (1996) Arch. Virol., 141, pp. 1337-1348; Falsey, A.R., McCann, R.M., Hall, W.J., Criddle, M.M., Formica, M.A., Wycoff, D., Kolassa, J.E., The ""common cold"" in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J. Am. Geriatr. Soc., 45, pp. 706-711; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Grötzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Herald, J., Gorbalenya, A.E., Thiel, V., Schelle, B., Siddell, S.G., Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate (1998) J. Virol., 72, pp. 910-918; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Siddell, S.G., An 'elaborated' pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res., 21, pp. 5838-5842; Herold, J., Siddell, S.G., Ziebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275, pp. 68-89; Heusipp, G., Grötzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 kDa, polyprotein lab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78, pp. 2789-2794","Ziebuhr, J.; Institute of Virology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; email: ziebuhr@vim.um-wuerzburg.de",,"American Society for Microbiology",0022538X,,JOVIA,"9847320","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032888958
"Gonon V., Duquesne V., Klonjkowski B., Monteil M., Aubert A., Eloit M.","6505953263;6602303047;6603155515;7006194853;24368235900;7004293800;","Clearance of infection in cats naturally infected with feline coronaviruses is associated with an anti-S glycoprotein antibody response",1999,"Journal of General Virology","80","9",,"2315","2317",,10,"10.1099/0022-1317-80-9-2315","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032840268&doi=10.1099%2f0022-1317-80-9-2315&partnerID=40&md5=be49e195c960a2be77be6d3b9a1b9a7a","URA INRA de Genet. Molec. et Cell., Génétique Virale, Ecl. Natl. Veterinaire d'Alfort, 94704 Maisons Alfort, France; Virbac, BP 27, 06516 Carros, France","Gonon, V., URA INRA de Genet. Molec. et Cell., Génétique Virale, Ecl. Natl. Veterinaire d'Alfort, 94704 Maisons Alfort, France; Duquesne, V., Virbac, BP 27, 06516 Carros, France; Klonjkowski, B., Virbac, BP 27, 06516 Carros, France; Monteil, M., URA INRA de Genet. Molec. et Cell., Génétique Virale, Ecl. Natl. Veterinaire d'Alfort, 94704 Maisons Alfort, France; Aubert, A., Virbac, BP 27, 06516 Carros, France; Eloit, M., URA INRA de Genet. Molec. et Cell., Génétique Virale, Ecl. Natl. Veterinaire d'Alfort, 94704 Maisons Alfort, France","We have investigated by Western blotting the antibody responses against the three major structural proteins in cats naturally infected with feline coronaviruses that cleared virus infection (group I), established chronic asymptomatic infection (group II) or were sick (group III). The cats of group I developed an anti-S glycoprotein response that was, relative to the anti-M glycoprotein response, at least 30-fold higher than that of chronically infected cats from groups II and III. These results suggest that the anti-S glycoprotein response against antigenic domains revealed by Western blot is associated with clearance of the virus after natural infection, and is not a risk factor for the establishment of a chronic infection.",,"antibody; glycoprotein; structural protein; antibody response; article; cat; chronic disease; controlled study; Coronavirus; nonhuman; priority journal; risk factor; virus infection; Western blotting; Animalia; Coronavirus; Felidae; Felis catus; RNA viruses","Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., Risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) American Journal of Veterinary Research, 56, pp. 429-434; Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: Evidence for markedly different peplomer glycoproteins (1987) Journal of Virology, 61, pp. 2607-2613; Gonin, P., Oualikene, W., Fournier, A., Soulier, M., Audonnet, J.C., Riviere, M., Eloit, M., Evaluation of a replication defective adenovirus expressing the feline infectious peritonitis membrane protein as a vaccine in cats (1995) Vaccine Research, 4, pp. 217-227; Herrewegh, A.A., De Groot, R., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in faeces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) Journal of Clinical Microbiology, 33, pp. 684-689; Herrewegh, A.A., Vennema, H., Horzinek, M.C., Rottier, P.J., De Groot, R., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hohdatsu, T., Nakamura, M., Ishizuka, Y., Yamada, H., Koyama, H., A study on the mechanism of antibody-dependent enhancement of feline infectious peritonitis virus infection in feline macrophages by monoclonal antibodies (1991) Archives of Virology, 120, pp. 207-217; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Archives of Virology, 117, pp. 85-95; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Archives of Virology, 140, pp. 469-480; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiology and Immunology, 40, pp. 425-433; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Veterinary Microbiology, 36, pp. 1-37; Vennema, H., De Groot, R., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) Journal of Virology, 64, pp. 1407-1409; Vennema, H., De Groot, R., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335","Eloit, M.; URA INRA Genetique Mol. Cellulaire, Genetique Virale, Ecole Nationale Veterinaire d'Alfort, 94704 Maisons Alfort, France; email: eloit@vet-alfort.fr",,"Society for General Microbiology",00221317,,JGVIA,"10501482","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0032840268
"Sestak K., Zhou Z., Shoup D.I., Saif L.J.","6701814572;56141188300;7003909464;7102226747;","Evaluation of the baculovirus-expressed S glycoprotein of transmissible gastroenteritis virus (TGEV) as antigen in a competition ELISA to differentiate porcine respiratory coronavirus from TGEV antibodies in pigs",1999,"Journal of Veterinary Diagnostic Investigation","11","3",,"205","214",,13,"10.1177/104063879901100301","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033128745&doi=10.1177%2f104063879901100301&partnerID=40&md5=5cd2f39c09c285056fffcd88acdca35e","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","Sestak, K., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Zhou, Z., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Shoup, D.I., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","The spike (S) glycoprotein of the Miller strain of transmissible gastroenteritis virus (TGEV) was recently cloned and expressed in baculovirus. The recombinant S protein was used as the coating antigen in a competition (blocking) enzyme-linked immunosorbent assay (ELISA) in combination with monoclonal antibodies to the S protein epitope A (conserved on TGEV and porcine respiratory coronavirus [PRCV]) or epitope D (present on TGEV only) to differentiate PRCV- from TGEV-induced antibodies. One set (set A) of 125 serum samples were collected at different times after inoculation of caesarean-derived, colostrum-deprived (n = 52) and conventional young pigs (n = 73) with 1 of the 2 porcine coronaviruses or uninoculated negative controls (TGEV/PRCV/negative = 75/30/20). A second set (set B) of 63 serum samples originated from adult sows inoculated with PRCV and the recombinant TGEV S protein or with mock-protein control and then exposed to virulent TGEV after challenge of their litters. Sera from set A were used to assess the accuracy indicators (sensitivity, specificity, accuracy) of the fixed-cell blocking ELISA, which uses swine testicular cells infected with the M6 strain of TGEV as the antigen source (ELISA 1) and the newly developed ELISA based on the recombinant S protein as antigen (ELISA 2). The sera from set B (adults) were tested for comparison. The plaque reduction virus neutralization test was used as a confirmatory test for the presence of antibodies to TGEV/PRCV in the test sera. The accuracy indicators for both ELISAs suggest that differential diagnosis can be of practical use at least 3 weeks after inoculation by testing the dual (acute/convalescent) samples from each individual in conjunction with another confirmatory (virus neutralization) antibody assay to provide valid and complete differentiation information. Moreover, whereas ELISA 1 had 10-20% false positive results to epitope D for PRCV-infected pigs (set A samples), no false-positive results to epitope D occurred using ELISA 2, indicating its greater specificity. The progression of seroresponses to the TGEV S protein epitopes A or D, as measured by the 2 ELISAs, was similar for both sets (A and B) of samples. Differentiation between TGEV and PRCV antibodies (based on seroresponses to epitope D) was consistently measured after the third week of inoculation.",,"diagnostic agent; monoclonal antibody; protein S; virus antigen; animal; animal disease; article; Baculovirus; biosynthesis; cell culture; Coronavirus; cytology; differential diagnosis; enzyme linked immunosorbent assay; female; immunology; male; respiratory tract infection; sensitivity and specificity; serodiagnosis; swine; swine disease; testis; Transmissible gastroenteritis virus; vaccination; virology; Animals; Antibodies, Monoclonal; Antigens, Viral; Baculoviridae; Cells, Cultured; Coronavirus; Diagnosis, Differential; Enzyme-Linked Immunosorbent Assay; Female; Gastroenteritis, Transmissible, of Swine; Male; Neutralization Tests; Protein S; Respiratory Tract Infections; Sensitivity and Specificity; Swine; Swine Diseases; Testis; Transmissible gastroenteritis virus; Vaccination","Bohl, E.H., Gupta, R.K.P., Olquin, M.V.F., Saif, L.J., Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect Immun, 6, pp. 289-301; Brown, I.H., Paton, D.J., Serological studies of transmissible gastroenteritis in Great Britain, using a competitive ELISA (1991) Vet Rec, 128, pp. 500-503; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19; Correa, I., Jimenez, G., Sune, C., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res, 10, pp. 77-93; Cubero, M.J., Leon, L., Contreras, A., Sero-epidemiological survey of porcine respiratory coronavirus (PRCV) infection in breeding herds in southeastern Spain (1992) Zentralbl Vet Med B, 39, pp. 290-298; De Diego, M., Laviada, M.D., Enjuanes, L., Epitope specificity of protective lactogenic immunity against swine transmissible gastroenteritis virus (1992) J Virol, 66, pp. 6502-6508; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. II. Domains in the peplomer glycoprotein (1986) J Gen Virol, 67, pp. 1405-1418; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, , ed. Siddell SG, Plenum, New York, NY; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus AR310 (1993) J Vet Diagn Invest, 5, pp. 184-188; Have, P., Infection with a new porcine respiratory coronavirus in Denmark: Serologic differentiation from transmissible gastroenteritis virus using monoclonal antibodies (1990) Adv Exp Med Biol, 276, pp. 435-439; Jackwood, D.J., Bae, I., Jackwood, R.J., Saif, L.J., Transmissible gastroenteritis virus and porcine respiratory coronavirus: Molecular characterization of the S gene using cDNA probes and nucleotide sequence analysis (1993) Adv Exp Med Biol, 342, pp. 43-48; Lai, C.H., Welter, M.W., Welter, L.M., The use of arms PCR and RFLP analysis in identifying genetic profiles of virulent, attenuated or vaccine strains of TGEV and PRCV (1995) Adv Exp Med Biol, 380, pp. 243-245; Lanza, I., Shoup, D.I., Saif, L.J., Lactogenic immunity and milk antibody isotypes to transmissible gastroenteritis virus in sows exposed to porcine respiratory coronavirus during pregnancy (1995) Am J Vet Res, 56, pp. 739-748; Laude, H., Godet, H., Bernard, S., Functional domains in the spike protein of transmissible gastroenteritis virus (1995) Adv Exp Med Biol, 380, pp. 299-304; Laude, H., Van-Reeth, K., Pensaert, M.B., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Paton, D.J., Brown, I.H., Vaz, E.K., An ELISA for the detection of serum antibodies to both transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) Br Vet J, 147, pp. 370-372; Pensaert, M.B., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Saif, L.J., Mucosal immunity: An overview and studies of enteric and respiratory coronavirus infections in a swine model of enteric disease (1996) Vet Immunol Immunopathol, 54, pp. 163-169; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, pp. 362-386. , ed. Leman AD, Straw B, Clock RD, et al., 7th ed., Iowa State University Press, Ames, IA; Shoup, D.I., Jackwood, D.J., Saif, L.J., Active and passive immune responses to transmissible gastroenteritis virus (TGEV) in swine inoculated with recombinant baculovirus-expressed TGEV spike glycoprotein vaccines (1997) Am J Vet Res, 58, pp. 242-250; Siddell, S.G., Wege, H., Ter Meulen, V., The structure and replication of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 131-163; Simkins, R.A., Saif, L.J., Weilnau, P.A., Epitope mapping and the detection of transmissible gastroenteritis viral proteins in cell culture using biotinylated monoclonal antibodies in a fixed-cell ELISA (1989) Arch Virol, 107, pp. 179-190; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am J Vet Res, 53, pp. 1253-1258; Simkins, R.A., Weilnau, P.A., VanCott, J., Competition ELISA, using monoclonal antibodies to the TGEV S protein, for serologic differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am J Vet Res, 54, pp. 254-259; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in formalin-fixed paraffin-embedded tissues (1996) J Virol Methods, 56, pp. 149-160; Stott, D.I., Immunoblotting and dot blotting (1989) J Immunol Methods, 119, pp. 153-187; Tuboly, T., Nagy, E., Dennis, J.R., Immunogenicity of the S protein transmissible gastroenteritis virus expressed in baculovirus (1994) Arch Virol, 137, pp. 55-67; VanCott, J.L., Brim, T.A., Lunney, J.K., Saif, D.J., Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J Immunol, 152, pp. 3980-3990; Van Nieuwstadt, A.P., Boonstra, J., Comparison of the antibody response to transmissible gastroenteritis virus and porcine respiratory coronavirus using monoclonal antibodies to antigenic sites A and X of the S glycoprotein (1992) Am J Vet Res, 53, pp. 184-190; Van Reeth, K., Pensaert, M.B., Porcine respiratory coronavirus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) Am J Vet Res, 55, pp. 1275-1281; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using cDNA probe (1991) J Vet Diagn Invest, 3, pp. 29-32; Wesley, R.D., Woods, R.D., McKean, J.D., Prevalence of coronavirus antibodies in Iowa swine (1997) Can J Vet Res, 61, pp. 305-308","Sestak, K.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"10353350","English","J. Vet. Diagn. Invest.",Review,"Final",Open Access,Scopus,2-s2.0-0033128745
"Tsunemitsu H., Smith D.R., Saif L.J.","7004628959;7410366749;7102226747;","Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coronavirus in feces by RT-PCR",1999,"Archives of Virology","144","1",,"167","175",,59,"10.1007/s007050050493","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032898695&doi=10.1007%2fs007050050493&partnerID=40&md5=101c01f77eb92eafca570ce2d2a8d6aa","Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States; Hokkaido Research Station, National Institute of Animal Health, Sapporo, Hokkaido, Japan; Dept. of Vet./Biomedical Sciences, University of Nebraska, Lincoln, NE 68583, United States; Food Animal Health Research Program, Ohio Agric. Res./Development Center, 1680 Madison Avenue, Wooster, OH 44691, United States","Tsunemitsu, H., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Hokkaido Research Station, National Institute of Animal Health, Sapporo, Hokkaido, Japan; Smith, D.R., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Dept. of Vet./Biomedical Sciences, University of Nebraska, Lincoln, NE 68583, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Food Animal Health Research Program, Ohio Agric. Res./Development Center, 1680 Madison Avenue, Wooster, OH 44691, United States","A reverse transcriptase PCR (RT-PCR) targeting a 407 bp fragment of the nucleocapsid gene of bovine coronavirus (BCV) was developed for detection of BCV RNA in feces of experimentally inoculated cattle. The sensitivity and specificity of the RT-PCR were confirmed using tissue culture-adapted BCV strains and feces of 2 calves inoculated with BCV. Ten nonpregant, BCV seropositive, adult dairy cows were inoculated with winter dysentery (WD) (n = 8) or calf diarrhea (CD) (n = 2) strains of BCV intranasally and orally (n = 2) or through a surgically-placed duodenal catheter (n = 8) with and without dexamethasone treatment or feeding ice water. The 6 cows inoculated with BCV intranasally and through a duodenal catheter (2 of 2 cows given CD BCV and 4 of 6 cows given WD BCV) developed mild diarrhea, and BCV was detected in diarrheal feces by RT-PCR, ELISA or immune electron microscopy. These results suggest that CD and WD strains of BCV can cause diarrhea in adult cows in conjunction with host or environmental factors and that RT-PCR might be useful to diagnose BCV infections in calves and adult cows.",,"Coronavirus; dexamethasone; enzyme linked immunosorbent assay; immunoelectron microscopy; inoculation; reverse transcription polymerase chain reaction; viral genetics; virus detection; virus gene; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus","Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Bulgin, M.S., Ward, A.S., Barrett, D.P., Lane, V.M., Detection of rotavirus and coronavirus shedding in two beef cow herds in Idaho (1989) Can Vet J, 30, pp. 235-239; Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Vet, 68, pp. 423-441; Chinsangaram, J., Akita, G.Y., Osburn, B., Detection of bovine group B rotaviruses in feces by pollymerase chain reaction (1994) J Vet Diagn Invest, 6, pp. 302-307; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Collins, J.K., Riegel, C.A., Olson, J.D., Fountain, A., Shedding of enteric coronavirus in adult cattle (1987) Am J Vet Res, 48, pp. 361-365; Crouch, C.F., Ohmann, H.B., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Cruciere, C., Laporte, J., Sequence and analysis of bovine enteric coronavirus (F15) genome. 1. Sequence of the gene coding for the nucleocapsid protein; analysis of the predicted protein (1988) Am Inst Pasteur Virol, 139, pp. 123-138; Dea, S., Michaud, L., Rekik, R., Antigenic and genomic variations among cytopathic and non-cytopathic strains of bovine enteric coronavirus (1995) Adv Exp Med Biol, 380, pp. 99-101; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Saif, L.J., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am J Vet Res, 57, pp. 48-53; Feng, N., Burns, J.W., Bracy, L., Greenberg, H.B., Comparison of mucosal and systemic humoral immune responses and subsequent protection in mice orally inoculated with a homologous or a heterologous rotavirus (1994) J Virol, 68, pp. 7766-17733; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Millane, G., Michaud, L., Dea, S., Biological and molecular differentiation between coronaviruses associated with neonatal calf diarrhoea and winter dysentery in adult cattle (1995) Adv Exp Med Biol, 380, pp. 29-33; Moe, C.L., Gentsch, J., Ando, T., Grohmann, G., Monroe, S.S., Jiang, X., Wang, J., Glass, R.I., Application of PCR to detect Norwalk virus in fecal specimens from outbreaks of gastroenteritis (1994) J Clin Microbiol, 32, pp. 642-648; Myint, S., Johnston, S., Sanderson, G., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Oldham, G., Bridger, J.C., The effect of dexamethasone-induced immunosuppression on the development of faecal antibody and recovery from and resistance to rotavirus infection (1992) Vet Immunol Immunopathol, 32, pp. 77-92; Rogan, D., Dea, S., Percy, D., Culbert, R., Ability of winter dysentery isolates of bovine coronaviruses to induce bloody diarrhea in newborn calves (1996) Conference of Research Workers in Animal Diseases, , Chicago IL, Abstract 107; Roy, M.J., Walsh, T.J., Histopathologic and immunohistochemical change in gut-associated lymphoid tissues after treatment of rabbits with dexamethasone (1992) Lab Invest, 64, pp. 437-443; Saif, A review of evidence implicating bovine coronavirus in the etiology of winter dysentery cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res 1977, 38, pp. 13-20; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Brock, K.V., Wittum, T.E., Morley, P.S., Hoblet, K.H., Saif, L.J., Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 994-1001; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Brock, K.V., Wittum, T.E., Morley, P.S., Hoblet, K.H., Saif, L.J., Evaluation of cow-level risk factors for the development of winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 986-993; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Reed Saif, L.J., Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J Clin Microbiol, 33, pp. 3264-3269; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Tsunemitsu, H., Yonemichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; VanKruiningen, R.J., Hill, S.L., Tilton, R.C., Ryan, R.W., Winter dysentery in dairy cattle: Recent findings (1995) Comp Cont Ed, 7, pp. S591-S599; White, M.E., Schukken, Y.H., Tanksley, B., Space-time clustering of, and risk factors for, farmer-diagnosed winter dysentery in dairy cattle (1989) Can Vet J, 30, pp. 948-951; Wilde, J., Eiden, J., Yolken, R., Removal of inhibitory substances from human fecal specimens for detection of group A rotaviruses by reverse transcriptase and polymerase chain reactions (1990) J Clin Microbiol, 28, pp. 1300-1307; Xu, L., Harbour, D., McCrae, M.A., The application of polymerase chain reaction to the detection of rotavirus in faeces (1990) J Virol Methods, 27, pp. 29-38","Saif, L.J.; Food Animal Health Research Program, Ohio Agricultural Res./Dev. Center, 1680 Madison Avenue, Wooster, OH 44691, United States",,"Springer Wien",03048608,,ARVID,"10076517","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0032898695
"Alexander L.K., Keene B.W., Yount B.L., Geratz J.D., Small J.D., Baric R.S.","36812461600;7006043632;6603564156;7004535575;7202783844;7004350435;","ECG changes after rabbit coronavirus infection",1999,"Journal of Electrocardiology","32","1",,"21","32",,4,"10.1016/S0022-0736(99)90018-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033042914&doi=10.1016%2fS0022-0736%2899%2990018-3&partnerID=40&md5=9aed9a55dc284e408c8e002b89522468","Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; Department of Pathology, School of Medicine, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; College of Veterinary Medicine, North Carolina State University, Raleigh, NC, United States; Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States","Alexander, L.K., Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; Keene, B.W., College of Veterinary Medicine, North Carolina State University, Raleigh, NC, United States; Yount, B.L., Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; Geratz, J.D., Department of Pathology, School of Medicine, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; Small, J.D., Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States; Baric, R.S., Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC, United States, Department of Epidemiology, School of Public Health, Univ. of N. Carolina at Chapel Hill, Chapel Hill, NC 27599-7400, United States","This study examines the electrocardiographic (ECG) changes following rabbit coronavirus (RbCV) infection. We have shown that infection with RbCV results in the development of myocarditis and congestive heart failure and that some survivors of RbCV infection go on to develop dilated cardiomyopathy in the chronic phase. Serial ECGs were recorded on 31 RbCV-infected rabbits. Measurements of heart rate; P-R interval; QRS duration; QTc interval; and P- , QRS-, and T-wave voltages were taken. The recordings were also examined for disturbances of conduction, rhythm, and repolarization. The acute and subacute phases were characterized by sinus tachycardia with depressed R- and T-wave voltages as well as disturbances of conduction, rhythm, and repolarization. In most animals in the chronic phase, the sinus rate returned to near-baseline values with resolution of the QRS voltage changes. The ECG changes observed during RbCV infection are similar to the spectrum of interval/segment abnormalities, rhythm disturbances, conduction defects, and myocardial pathology seen in human myocarditis, heart failure, and dilated cardiomyopathy. Because animals often died suddenly in the absence of severe clinical signs of congestive heart failure during the acute phase, RbCV infection may increase ventricular vulnerability, resulting in sudden cardiac death. RbCV infection may provide a rare opportunity to study sudden cardiac death in an animal model in which the ventricle is capable of supporting ventricular fibrillation, and invasive techniques monitoring cardiac function can be performed.","Coronavirus; ECG; Heart failure; Myocarditis","animal experiment; animal model; animal tissue; article; controlled study; Coronavirus; electrocardiogram; heart dilatation; histopathology; myocarditis; nonhuman; priority journal; QT interval; rabbit","Woodruff, J.F., Viral myocarditis (1980) Am J Pathol, 101, p. 427; Abelmann, W.H., Viral myocarditis and its sequelae (1973) Ann Rev Med, 24, p. 145; Abelmann, W.H., Virus and the heart (1971) Circulation, 44, p. 950; See, D.M., Tilles, J.G., Viral myocarditis (1991) Rev Infect Dis, 13, p. 951; Leslie, K., Blay, R., Haisch, C., Lodge, A., Weller, A., Huber, S., Clinical and experimental aspects of viral myocarditis (1989) Clin Microbiol Rev, 2, p. 191; Tracy, S., Wiegand, V., McManus, B., Molecular approaches to enteroviral diagnosis in idiopathic cardiomyopathy and myocarditis (1990) J Am Coll Cardiol, 15, p. 1688; Tracy, S., Chapman, N., McManus, B., Pallansch, M., Beck, M., Carstens, J., A molecular and serologic evaluation of enteroviral involvement in human myocarditis (1990) J Mol Cell Cardiol, 22, p. 403; Jin, O., Sole, M., Butany, J., Detection of enterovirus RNA in myocardial biopsies from patients with myocarditis and cardiomyopathy using gene amplification by polymerase chain reaction (1990) Circulation, 82, p. 8; Klingel, K., Hohenadl, C., Canu, A., Ongoing enterovirus-induced myocarditis is associated with persistent heart muscle infection: Quantitative analysis of virus replication, tissue damage and inflammation (1992) Proc Natl Acad Sci USA, 89, p. 314; Petitjean, J., Kopecka, H., Freymuth, F., Detection of enteroviruses in endomyocardial biopsy by molecular approach (1992) J Med Virol, 37, p. 76; Small, J.D., Aurelian, L., Squire, R.A., Rabbit cardiomyopathy. Associated with a virus antigenically related to human coronavirus strain 229E (1979) Am J Pathol, 95, p. 709; Edwards, S., Small, J.D., Geratz, J.D., Alexander, L.K., Baric, R.S., An experimental model for myocarditis and congestive heart failure after rabbit coronavirus infection (1992) J Infect Dis, 165, p. 134; Alexander, L.K., Small, J.D., Edwards, S., Baric, R.S., An experimental model for dilated cardiomyopathy after rabbit coronavirus infection (1992) J Infect Dis, 166, p. 978; Hoshino, T., Matsumori, A., Kawai, C., Imai, J., Electrocardiographic abnormalities in syrian golden hamsters with coxsackievirus B1 myocarditis (1982) Jpn Circ J, 46, p. 1305; Kishimoto, C., Matsumori, A., Ohmae, M., Tomioka, N., Kawai, C., Electrocardiographic findings in experimental myocarditis in DBA/2 mice: Complete atrioventricular block in the acute stage, low voltage of the QRS complex in the subacute stage and arrhythmias in the chronic stage (1984) J Am Coll Cardiol, 3, p. 1461; Morita, H., Kitaura, Y., Deguchi, H., Kotaka, M., Kawamura, K., Experimental coxsackie B3 virus myocarditis in golden hamsters. II. Evaluation of left ventricular function in intact in situ heart 14 months after inoculation (1984) Jpn Circ J, 48, p. 1097; Gwathmey, J.K., Nakao, S., Come, P.C., An experimental model of acute and subacute viral myocarditis in the pig (1992) J Am Coll Cardiol, 19, p. 864; Monath, T.P., Kemp, G.E., Cropp, C.B., Chandler, F.W., Necrotizing myocarditis in mice infected with western equine encephalitis virus: Clinical, electrocardiographic, and histopathologic correlations (1978) J Infect Dis, 138, p. 59; Kotaka, M., Kitaura, Y., Deguchi, H., Kawamura, K., Experimental influenza A virus myocarditis in mice. Light and electron microscopic, virologic, and hemodynamic study (1990) Am J Pathol, 136, p. 409; Olsen, G.R., Miller, L.D., Studies on the pathogenesis of heart lesions in dogs infected with pseudorabies virus (1986) Can J Vet Res, 50, p. 245; James, T.N., Anatomy of the cardiac conduction system in the rabbit (1967) Circ Res, 20, p. 638; Lange, K., Weiner, D., Gold, M.M.A., Studies on the mechanism of cardiac injury in experimental hypothermia (1949) Ann Intern Med, 31, p. 989; Van De Water, A., Verheyen, J., Xhonneux, R., Reneman, R.S., An improved method to correct the QT interval of the electrocardiogram for changes in heart rate (1989) J Pharmacol Meth, 22, p. 207; Fredericia, L.S., Die Systolendauer in EKG bei normalen Menschen u. bei Herzkranken (1920) Act Medica Scand, 53, p. 469; Hayes, E., Pugsley, M.K., Penz, W.P., Adaikan, G., Walker, M.J.A., Relationship between QaT and RR intervals in rats, guinea pigs, rabbits, and primates (1994) J Pharmacol Toxicol Meth, 32, p. 201; Wilkinson, L., (1990) SYSTAT: The System for Statistics, , SYSTAT, Inc., Evanston, IL; Saitanov, A.O., The electrocardiogram of healthy rabbits in standard and chest leads and methods of recording it (1960) Byulleten Eksperimentalnoi Biologii i Meditsiny, 49, p. 102; Nelson, C.V., Waggoner, W.C., Gastonguay, P.R., High-fidelity electrocardiograms of normal rabbits (1964) Am J Physiol, 207, p. 1107; Heger, J.W., Roth, R.F., Niemann, J.M., Criley, J.M., (1993) Cardiology, , Williams & Wilkins, Baltimore, MD; Brooks, H.L., (1987) Electrocardiography: 100 Diagnostic Criteria, , Year Book Medical Publishers, Chicago, IL; Scheidt, S., Basic electrocardiography: Leads, axes, arrhythmias (1983) Clin Symp, 35, p. 1; Regoezi, E., Über die Frequenzabhängigkeit der Austreibungszeit und der QT-Dauer beim Kaninchen (1961) Zeitschrift für Die Gesamte Experimentelle Medizin, 135, p. 30; Hodges, M., Salerno, D., Erlien, D., Bazett's QT correction reviewed: Evidence that a linear QT correction for heart rate is better (1983) J Am Coll Cardiol, 1, p. 694; Levine, H.D., Virus myocarditis: A critique of the literature from clinical, electrocardiographic, and pathologic standpoints (1979) Am J Med Sci, 277, p. 132; Talman, W.T., Cardiovascular regulation and lesions of the central nervous system (1985) Ann Neurol, 18, p. 1; James, T.N., Froggatt, P., Atkinson, W.J., Observations on the pathophysiology of the long QT syndromes with special reference to the neuropathology of the heart (1978) Circulation, 57, p. 1221; Baroldi, G., Pathology and mechanisms of sudden death (1986) The Heart, p. 529. , Hurst JW (ed): McGraw-Hill, New York; Bos, I., Johannisson, R., Djonlagic, H., Morphologic alterations in the long Q-T syndrome. Light and electron microscopic observations in the conduction system and in sympathic trunks (1985) Pathol Res Pract, 180, p. 691; Obeyesekere, I., Hermon, Y., Arbovirus heart disease: Myocarditis and cardiomyopathy following dengue and chikungunya fever - A follow-up study (1973) Am Heart J, 85, p. 186; Smith, W.G., Coxsackie B myopericarditis in adults (1970) Am Heart J, 80, p. 34; James, T.N., Intracardiac ganglionitis and sudden death. Herpes of the heart? (1979) Trans Am Clin Climatol Assoc, 91, p. 177; Tsiplenkova, V.G., Pavlovich, B.R., Balogh, I., Somogyi, E., Vikhert, A.M., Electron microscopic demonstration of viruses and bacteria in cardiac myocytes from victims of sudden cardiac death (1986) Acta Morphol Hung, 34, p. 209; Morales, A.R., Adelman, S., Fine, G., Varcella myocarditis. A case of sudden death (1971) Arch Pathol, 91, p. 29; James, T.N., Imamura, K., Virus-like particles associated with intracardiac ganglionitis in 2 cases of sudden unexpected death (1981) Jpn Heart J, 22, p. 447; Sevy, S., Kelly, J., Ernst, H., Fatal paroxysmal tachycardia associated with focal myocarditis of the Purkinje system in a 14-month-old girl (1968) J Pediatr, 72, p. 796; Sareli, P., Schamroth, M.B., Passias, J., Schamroth, L., Torsade de pointes due to coxsackie B3 myocarditis (1987) Clin Cardiol, 10, p. 361; Obeyesekere, I., Hermon, Y., Myocarditis and cardiomyopathy after arbovirus infections (dengue and chikungunya fever) (1972) Br Heart J, 34, p. 821; Levander-Lingren, M., Studies in myocarditis. I. Etiology and primary course (1964) Cardiologia, 45, p. 362; Hamby, R.I., Raia, F., Electrocardiographic aspects of primary myocardial disease in 60 patients (1968) Am Heart, 176, p. 316; Wilensky, R.L., Yudelman, P., Cohen, A.I., Serial electrocardiographic changes in idiopathic dilated cardiomyopathy confirmed at necropsy (1988) Am J Cardiol, 62, p. 276; Kitaura, Y., Morita, H., Secondary myocardial disease. Virus myocarditis and cardiomyopathy (1979) Jpn Circ J, 43, p. 1017","Baric, R.S.; Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7400, United States",,"Churchill Livingstone Inc.",00220736,,JECAB,"10037086","English","J. Electrocardiol.",Article,"Final",Open Access,Scopus,2-s2.0-0033042914
"Da Silva M.R., O'Reilly K.L., Lin X., Stine L., Storz J.","8372081000;7103313844;36768282000;6701699357;7006694594;","Sensitivity comparison for detection of respiratory bovine coronaviruses in nasal samples from feedlot cattle by ELISA and isolation with the G clone of HRT-18 cells",1999,"Journal of Veterinary Diagnostic Investigation","11","1",,"15","19",,10,"10.1177/104063879901100102","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032622547&doi=10.1177%2f104063879901100102&partnerID=40&md5=2eb57de73cf5481a4d1c34dae6d1d5b8","Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Diagnostic and Research Department, Natl. Veterinary Research Institute, PO Box 1922, Maputo, Mozambique; Immtech Biologies, Bucyrus, KS 66103, United States","Da Silva, M.R., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States, Diagnostic and Research Department, Natl. Veterinary Research Institute, PO Box 1922, Maputo, Mozambique; O'Reilly, K.L., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Lin, X., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Stine, L., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States, Immtech Biologies, Bucyrus, KS 66103, United States; Storz, J., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","A monoclonal antibody-based capture enzyme-linked immunosorbent assay (ELISA) was developed to detect respiratory bovine coronavirus (RBCV) antigens in nasal swabs collected from cattle showing signs of respiratory tract disease following shipping. These samples had been previously tested for RBCV by inoculation of G clone cultures of human rectal tumor cells (HRT-18G) and for bovine herpes virus 1, para-influenza virus 3, bovine adenovirus, bovine respiratory syncytial virus, and bovine viral diarrhea virus on other specifically permissive cell cultures. RBCV has not previously been recognized as an important etiological factor in the bovine respiratory disease complex of feedlot cattle. Thirty of 100 samples tested positive for RBCV antigen by capture ELISA in contrast to 38 of 100 samples that yielded RBCV isolates in G clone cells. Samples yielding other bovine respiratory viruses in the absence of RBCV were negative in the capture ELISA, which was based on the use of a single monoclonal antibody that recognizes one RBCV epitope on the S glycoprotein with the broadest reactivity with different strains of RBCV tested. Some RBCV strains may not be detected by this ELISA, which may account for the higher percentage of RBCV-infected cattle detected by RBCV isolation. However, the ELISA was simple to perform, sensitive, and specific and was more rapid than virus isolation. This assay will be useful for processing large numbers of field samples in future epidemiologic and diagnostic studies of RBCV infections of cattle.",,"animal; animal disease; article; cattle; cattle disease; cell clone; cell culture; comparative study; Coronavirus; enzyme linked immunosorbent assay; human; isolation and purification; laboratory diagnosis; methodology; nose mucosa; rectum tumor; reproducibility; respiratory tract infection; sensitivity and specificity; virology; virus infection; Animals; Cattle; Cattle Diseases; Clone Cells; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; Humans; Nasal Mucosa; Rectal Neoplasms; Reproducibility of Results; Respiratory Tract Infections; Sensitivity and Specificity; Specimen Handling; Tumor Cells, Cultured","Bryson, D.G., McFerran, J.B., Ball, H.J., Neill, S.D., Observations on outbreaks of respiratory disease in housed calves. Epidemiological, clinical and microbiological findings (1978) Vet Rec, 103, pp. 485-489; Carman, P.S., Hazlett, M.J., Bovine coronavirus infection in Ontario, 1990-1991 (1992) Can Vet J, 33, pp. 812-814; Herbst, V.W., Klatt, E., Schliesser, T., Serologisch-diagnostische Untersuchungen zum Vorkommen von Coronavirusinfektionen bei Atemwegserkrankungen des Rindes (1989) Berl Münch Tierärztl Wochenschr, 102, pp. 129-131; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Laporte, J., Bobulesco, P., Rossi, F., Une ligne particulierement sensible a la replication du coronavirus enteritique bovin: Les cellules HRT-18G (1980) CR Acad Sci Ser III Sci Vie, 290 D, pp. 623-626; Lin, X.Q., O'Reilly, K.L., Storz, J., Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny (1997) Am J Vet Res, 58, pp. 1120-1124; Martin, S.W., Analysis and causal interpretation of biologic data. A seroepidemiologic study of respiratory disease (1985) Vet Med, 57, pp. 46-54. , Fourth International Symposium on Veterinary Epidemiology and Economics; St Cyr-Coats, K., Storz, J., Bovine coronavirus-induced cytopatic expression and plaque formation: Host cell and virus strain determine trypsin dependence (1988) J Vet Med Ser B, 35, pp. 48-56; Storz, J., Rott, R., Uber die Verbreitung der Coronavirus-infektion bei Rindern in ausgewählten Gebieten Deutschlands: Antikörpernachweis durch Mikroimmundiffusion und Neutralisation (1980) Dtsch Tierärztl Wochenschr, 87, pp. 252-254; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol, 169, pp. 169-178; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swabs samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1454; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Thompkins, W.A., Watrach, A.M., Schmale, J.D., Cultural and antigenic properties of newly established cell strains from adenocarcinomas of human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 101-106; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 134, pp. 421-426","Da Silva, M.R.; Diagnostic and Research Department, Natl. Veterinary Research Institute, PO Box 1922, Maputo, Mozambique",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"9925206","English","J. Vet. Diagn. Invest.",Review,"Final",Open Access,Scopus,2-s2.0-0032622547
"Denison M.R., Spaan W.J.M., Van Der Meer Y., Gibson C.A., Sims A.C., Prentice E., Lu X.T.","7101971810;7007172944;7005678965;57196806022;7102763252;7003706540;56137171400;","The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis",1999,"Journal of Virology","73","8",,"6862","6871",,72,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032787420&partnerID=40&md5=e6250c8d2d1fcd000695a35f91ac3b55","Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States; Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States","Denison, M.R., Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States, Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States; Spaan, W.J.M., Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Van Der Meer, Y., Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Gibson, C.A., Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States; Sims, A.C., Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States; Prentice, E., Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States; Lu, X.T., Dept. of Microbiology and Immunology, Elizabeth B. Lamb Ctr. for P., Vanderbilt University, Nashville, TN, United States","The coronavirus mouse hepatitis virus (MHV) translates its replicase gene (gene 1) into two co-amino-terminal polyproteins, polyprotein 1a and polyprotein lab. The gene 1 polyproteins are processed by viral proteinases to yield at least 15 mature products, including a putative RNA helicase from polyprotein lab that is presumed to be involved in viral RNA synthesis. Antibodies directed against polypeptides encoded by open reading frame lb were used to characterize the expression and processing of the MHV helicase and to define the relationship of helicase to the viral nucleocapsid protein (N) and to sites of viral RNA synthesis in MHV-infected cells. The antihelicase antibodies detected a 67-kDa protein in MHV-infected cells that was translated and processed throughout the virus life cycle. Processing of the 67-kDa helicase from polyprotein lab was abolished by E64d, a known inhibitor of the MHV 3C-like proteinase. When infected cells were probed for helicase by immunofluorescence laser confocal microscopy, the protein was detected in patterns that varied from punctate perinuclear complexes to large structures that occupied much of the cell cytoplasm. Dual-labeling studies of infected cells for helicase and bromo-UTP-labeled RNA demonstrated that the vast majority of helicase-containing complexes were active in viral RNA synthesis. Dual-labeling studies for helicase and the MHV N protein showed that the two proteins almost completely colocalized, indicating that N was associated with the helicase-containing complexes. This study demonstrates that the putative RNA helicase is closely associated with MHV RNA synthesis and suggests that complexes containing helicase, N, and new viral RNA are the viral replication complexes.",,"antibody; helicase; nucleocapsid protein; polypeptide; protein; RNA directed RNA polymerase; virus RNA; animal cell; article; complex formation; confocal laser microscopy; controlled study; gene; immunofluorescence; immunoprecipitation; mouse; Murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; protein localization; RNA synthesis; virus replication","Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. Virol., 62, pp. 4280-4287; Barton, D.J., Sawicki, S.G., Sawicki, D.L., Solubilization and imiriunoprecipitation of alphavirus replication complexes (1991) J. Virol., 65, pp. 1496-1506; Bi, W., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., Intracellular localization of polypeptides encoded in mouse hepatitis virus open reading frame IA (1995) Adv. Exp. Med. Biol., 380, pp. 251-258; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Breedenbeek, P.J., Pachuk, C.J., Noten, A.F.H., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J.M., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Brierley, I., Boursnell, M.E.G., Binns, M.M., Billimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. Virol., 60, pp. 12-18; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the nidovirales: Similarities and differences between arteri-, toro, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Doedens, J., Maynell, L.A., Klymkowsky, M.W., Kirkegaard, K., Secretory pathway function, but not cytoskeletal integrity, is required in poliovirus infection (1994) Arch. Virol. Suppl., 9, pp. 159-172; Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes (1988) J. Cell Biol., 107, pp. 2075-2086; Gorbalenya, A., Koonin, E., Comparative analysis of amino-acid sequences of key enzymes of replication and expression of positive-strand RNA viruses: Validity of approach and functional and evolutionary implications (1993) Sov. Sci. Rev. Sect. D, 11, pp. 1-81; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative atnino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Lai, M.M.-C., Putative papainrelated thiol proteases of positive-strand RNA viruses (1991) FEBS Lett., 288, pp. 201-205; Gorbalenya, A.E., Koonin, E.V., Viral proteins containing the purine NTP-binding sequence pattern (1989) Nucleic Acids Res., 17, pp. 8413-8440; Grotzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222, pp. 227-235; Gran, J.B., Brinton, M.A., Separation of functional West Nile virus replication complexes from intracellular membrane fragments (1988) J. Gen. Virol., 69, pp. 3121-3127; Haukenes, G., Szilvay, A.-M., Brokstad, K.A., Kanestrom, A., Kalland, K.-H., Labeling of RNA transcripts in eukaryotic cells in culture with BrUTP using a liposome transfection reagent (DOTAP) (1997) BioTechniques, 22, pp. 308-312; Heusipp, G., Grotzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 KDa, polyprotein lab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78, pp. 2789-2794; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., 71, pp. 5631-5634; Hirano, N., Kujiwara, K., Matumoto, M., Mouse hepatitis virus (MHV-2); plaque assay and propagation in mouse cell line DBT cells (1976) Jpn. J. Microbiol., 20, pp. 219-225; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X.T., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cystcine proteinase inhibitor e64d (1995) Virology, 208, pp. 1-8; Koonin, E.V., Gorbalenya, A.E., Chumakov, K.M., Tentative identification of RNA-dependent RNA polymerases of ds RNA viruses and their relationship to positive strand RNA viral polymerases (1989) FEBS Lett., 252, pp. 42-46; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lavi, E., Wang, Q., Weiss, S.R., Gonatas, N.K., Syncytia formation induced by coronavirus infection is associated with fragmentation and rearrangement of the Golgi apparatus (1996) Virology, 221, pp. 325-334; Lee, H.J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., LaMonica, N., Tuler, J., Bagdzhadhzyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Liu, D.X., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Lu, X.T., Lu, Y.Q., Denison, M.R., Intracellular and in vitro translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 222, pp. 375-382; Lu, X.T., Sims, A.C., Denison, M.R., Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infecled cells and in vitro (1998) J. Virol., 72, pp. 2265-2271; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Lu, Y.Q., Denison, M.R., Determinants of mouse hepatitis virus 3C-like proteinase activity (1997) Virology, 230, pp. 335-342; Maynell, L.A., Kirkegaard, K., Klymkowsky, M.W., Inhibition of poliovirus RNA synthesis by brefeldin A (1992) J. Virol., 66, pp. 1985-1994; McBride, A.E., Schlegel, A., Kirkegaard, K., Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 2296-2301; Pachuk, C.J., Breedenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Pedersen, K.W., Van Der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) J. Virol., 73, pp. 2016-2026; Perlman, S., Reese, D., Bolger, E., Chang, L.J., Stoltzfus, C.M., MHV nucleocapsid synthesis in the presence of cycloheximide and accumu-lation of negative strand MHV RNA (1987) Virus Res., 6, pp. 261-272; Pinon, J., Mayreddy, R., Turner, J., Khan, F., Bonilla, P., Weiss, S., Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes (1997) Virology, 230, pp. 309-322; Rasband, W., (1999) NIH Image 1.62b. [Online.], , http://rsb.info.nih.gov/nih-image/; Restrepo-Hartwig, M.A., Ahlquist, P., Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis (1996) J. Virol., 70, pp. 8908-8916; Saborio, J.L., Pong, S.-S., Koch, G., Selective and reversible inhibition of initiation of protein synthesis in mammalian cells (1974) J. Mol. Biol., 85, pp. 195-211; Sawicki, D.L., Sawicki, S.G., Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Schlegel, A., Giddings, T.J., Ladinsky, M.S., Kirkegaard, K., Cellular origin and ultrastructure of membranes induced during poliovirus infection (1996) J. Virol., 70, pp. 6576-6588; Sethna, P.B., Brian, D.A., Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes (1997) J. Virol., 71, pp. 7744-7749; Snijder, E.J., Meulenberg, M., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Stohlman, S.A., Baric, R.S., Nelson, G.N., See, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Van Der Meer, Y., Van Tol, H., Krijnse Locker, J., Snijder, E.J., ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex (1998) J. Virol., 72, pp. 6689-6698; Van Dinten, L.C., Wassenaar, A.L., Gorbalenya, A.E., Spaan, W.J., Snijder, E.J., Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) J. Virol., 70, pp. 6625-6633","Denison, M.R.; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States; email: mark.denison@mcmail.vanderbilt.edu",,"American Society for Microbiology",0022538X,,JOVIA,"10400784","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032787420
"Schwender S., Hein A., Imrich H., Czub S., Dorries R.","7003953447;8047618900;6602841707;57212690106;7003359298;","Modulation of acute coronavirus-induced encephalomyelitis in γ-irradiated rats by transfer of naive lymphocyte subsets before infection",1999,"Journal of NeuroVirology","5","3",,"249","257",,5,"10.3109/13550289909015811","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032776573&doi=10.3109%2f13550289909015811&partnerID=40&md5=7da56a36edf2f41f31ae193bb0f0edab",,"Schwender, S.; Hein, A.; Imrich, H.; Czub, S.; Dorries, R.","Clinical course, recovery of infectious virus from brain tissue and histopathology of the central nervous system were examined in γ-irradiated Lewis rats reconstituted by naive lymphocytes before infection with coronavirus MHV-4 (strain JHM). Up to 9 days past infection, no differences were seen between immunologically competent and immuno-deficient animals in terms of onset and progression of neurological disease. However, in the latter animals neurological symptoms were dominated by signs of encephalitis instead of paralytic disease as usually seen in immunocompetent animals. Nevertheless, despite high titers of infectious virus in the CNS of immunodeficient animals only mild histopathological changes were noticeable. In contrast, infectious virus in the CNS of immunologically competent animals was below the detection limit of the assay. Paralytic disease and tissue destruction were T lymphocyte mediated because γ-irradiated rats that were reconstituted by CD4+ or CD8+ T lymphocyte enriched cells in the absence of B lymphocytes revealed an earlier onset of clinical symptoms and a more rapid deterioration of their clinical state compared to fully competent animals. Whereas in CD4+ T cell reconsituted animals infectious virus was moderately reduced and tissue destruction as well as inflammatory changes in the CNS were focal, in CD8+ T cell reconstituted animals vacuolizing white matter inflammation was diffuse without reduction of infectious virus in brain tissue. From the presented data we conclude that in the acute stage of JHMV-induced encephalomyelitis of Lewis rats: (i) tissue destruction and paralytic clinical symptomatology are mainly T cell-mediated; (ii) CD4+ T lymphocytes can directly contribute to reduction of viral load in the brain and (iii) only coordinated action of both, the T and the B cell compartment enables animals to survive the infection and recover from disease.","Central nervous system; Coronavirus; Encephalomyelitis; Lymphocyte subsets","CD4 antigen; CD8 antigen; animal cell; animal experiment; animal model; article; B lymphocyte; bioassay; brain tissue; cell vacuole; central nervous system infection; controlled study; Coronavirus; deterioration; disease course; encephalomyelitis; gamma irradiation; histopathology; immune deficiency; immunocompetent cell; inflammation; lymphocyte subpopulation; lymphocyte transfer; neurologic disease; nonhuman; paralysis; priority journal; rat; T lymphocyte; tissue degeneration; virus infection; virus infectivity; virus titration; white matter",,,,"Nature Publishing Group",13550284,,JNVIF,"10414515","English","J. Neurovirol.",Article,"Final",,Scopus,2-s2.0-0032776573
"Lavi E., Schwartz T., Jin Y.-P., Fu L.","7006986911;8781994100;26642975800;7401812822;","Nidovirus infections: Experimental model systems of human neurologic diseases",1999,"Journal of Neuropathology and Experimental Neurology","58","12",,"1197","1206",,11,"10.1097/00005072-199912000-00001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032786127&doi=10.1097%2f00005072-199912000-00001&partnerID=40&md5=3618eb440d5d7913cb0a4ae9865e6855","Division of Neuropathology, Laboratory Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., 613 Stellar-Chance Lab. Building, Philadelphia, PA 19104-6100, United States","Lavi, E., Division of Neuropathology, Laboratory Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States, Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., 613 Stellar-Chance Lab. Building, Philadelphia, PA 19104-6100, United States; Schwartz, T., Division of Neuropathology, Laboratory Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Jin, Y.-P., Division of Neuropathology, Laboratory Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Fu, L., Division of Neuropathology, Laboratory Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States","The presence of terminally differentiated slow- and non-dividing cells in the central nervous system (CNS) provides a safe harbor for viral persistence and latency and constitutes a unique immunologic environment for viral infections. Studies of experimental model systems of vital infections of the CNS provide insight into mechanisms of viral persistence and immune- mediated pathology. Nidoviruses are comprised of 2 families of viruses, coronaviruses and arteriviruses, and are common pathogens of humans and a variety of animal species. Both families of viruses contain neurotropic strains that produce experimental neurologic diseases in rodents. These include acute meningitis and encephalitis; acute poliomyelitis; and chronic inflammatory, immune-mediated, demyelination. Coronavirus-induced demyelinating disease mimics many of the pathologic features of Multiple Sclerosis (MS).","Arterivirus; Coronavirus; Demyelination; Encephalitis; Meningitis; Nidovirales; Tor ovirus","Arterivirus; central nervous system infection; Coronavirus; demyelination; disease simulation; human; immune mediated injury; multiple sclerosis; neurotropism; nonhuman; persistent virus infection; poliomyelitis; priority journal; review; virus encephalitis; virus infection; virus latency; virus meningitis","Fabry, Z., Raine, C.S., Hart, M.N., Nervous tissue as an immune compartment: The dialect of the immune response in the CNS (1994) Immunol Today, 15, pp. 218-224; Allen, I., Brankin, B., Pathogenesis of multiple sclerosis - The immune diathesis and the role of viruses (1993) J Neuropath Exp Neurol, 52, pp. 95-105; Dal Canto, M.C., Rabinowitz, S.G., Experimental models of virus-induced demyelination of the central nervous system (1982) Ann Neurol, 11, pp. 109-127; McIntosh, K., Coronaviruses: A comparative review (1974) Curr Top Microbiol Immunol, 63, pp. 80-129; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Adv Virol Immunol, 99, pp. 165-200; Barthold, S.W., Research complications and state of knowledge of rodent coronaviruses (1986) Complications of Viral and Mycoplasmal Infections in Rodents to Toxicological Research and Testing, pp. 53-89. , Hamm TA, ed. Washington, D.C.: Hemisphere Publishing Corp; Lavi, E., Weiss, S.R., Coronaviruses (1989) Clinical and Molecular Aspects of Neurotropic Viral Infections, pp. 101-139. , Gilden DH, Lipton HL, ed. 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Rossow, K.D., Porcine reproductive and respiratory syndrome (1998) Vet Pathol, 35, pp. 1-20; Johnson, B., Baldwin, C., Timoney, P., Ely, R., Arteritis in equine fetuses aborted due to equine viral arteritis (1991) Vet Pathol, 28, pp. 248-250; Balasuriya, U.B.R., Snijder, E.J., Van Dinten, L.C., Equine arteritis virus derived from an infectious cDNA clone is attenuated and genetically stable in infected stallions (1999) Virology, 260, pp. 201-208","Lavi, E.; Division of Neuropathology, Univ. of Pennsylvania Sch. of Med., 613 Stellar-Chance Lab. Building, Philadelphia, PA 19104-6100, United States",,"American Association of Neuropathologists Inc.",00223069,,JNENA,"10604745","English","J. Neuropathol. Exp. Neurol.",Review,"Final",Open Access,Scopus,2-s2.0-0032786127
"Ieki R.","6701370178;","Coronavirus",1999,"Nippon rinsho. Japanese journal of clinical medicine","57 Suppl",,,"298","300",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033217087&partnerID=40&md5=a4d1264ce1cdedea5283deac6f60beba","Department of Respiratory Medicine, Tokyo Metropolitan Komagome Hospital., Japan","Ieki, R., Department of Respiratory Medicine, Tokyo Metropolitan Komagome Hospital., Japan",[No abstract available],,"Coronavirus; human; isolation and purification; review; virology; virus infection; Coronavirus; Coronavirus Infections; Humans",,"Ieki, R.",,,00471852,,,"10635839","Japanese","Nippon Rinsho",Review,"Final",,Scopus,2-s2.0-0033217087
"Lavi E., Sarma J.D., Weiss S.R.","7006986911;55662977700;57203567044;","Cellular reservoirs for coronavirus infection of the brain in β2-microglobulin knockout mice",1999,"Pathobiology","67","2",,"75","83",,13,"10.1159/000028054","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032969810&doi=10.1159%2f000028054&partnerID=40&md5=69b410b1818d496bf856bccf6c5cc639","Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Division of Neuropathology, Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Division of Neuropathology, Dept. of Pathol. and Lab. Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6085, United States","Lavi, E., Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States, Division of Neuropathology, Dept. of Pathol. and Lab. Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6085, United States; Sarma, J.D., Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Weiss, S.R., Division of Neuropathology, Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States","Mouse hepatitis virus (MHV) A59 infection which causes acute encephalitis, hepatitis, and chronic demyelination, is one of the experimental models for multiple sclerosis. Previous studies showed that lethal infection of β2-microglobulin 'knockout' (β2M(-/-)) mice required 500-fold less virus and viral clearance was delayed as compared to infection of immunocompetent C57BI/6 (B6) mice. To investigate the mechanism of the increased susceptibility of β2M(-/-) mice to MHV-A59, we studied organ pathology and the distribution of viral antigen and RNA during acute and chronic infection. A59-infected β2M(-/-) mice were more susceptible to acute encephalitis and hepatitis, but did not have increased susceptibility to demyelination. Viral antigen and RNA distribution in the brain was increased in microglia, lymphocytes, and small vessel endothelial cells while the distribution in neurons and glia was similar in β2M(-/-) mice and B6 mice. Acute hepatitis and thymus cortical hypoplasia in β2M(-/-) mice were delayed in onset but pathologic changes in these organs were similar to those in B6 mice. The low rate of demyelination in β2M(-/-) mice was consistent with the low dose of the virus given. A less neurotropic virus MHV-2, caused increased parenchymal inflammation in β2M(-/-) mice, but without demyelination. Thus, CD8+ cells were important for viral clearance from endothelial cells, microglia and inflammatory cells, but not from neuronal and glial cells. In addition, CD8+ cells played a role in preventing the spread of encephalitis.","Coronaviruses; Immunohistochemistry; In situ hybridization; Nidoviruses; Pathogenesis","beta 2 microglobulin; CD8 antigen; virus antigen; virus RNA; animal experiment; animal model; animal tissue; article; brain infection; controlled study; demyelination; glia; hepatitis; hypoplasia; lymphocyte; microglia; mouse; Murine hepatitis coronavirus; nerve cell; newborn; nonhuman; priority journal; vascular endothelium; virus infection","McIntosh, K., Coronaviruses: A comparative review (1974) Curr Top Microbiol Immunol, 63, pp. 80-129; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Adv Virol Immunol, 99, pp. 165-200; Lavi, E., Weiss, S.R., Coronaviruses (1989) Clinical and Molecular Aspects of Neurotropic Viral Infections. Dev Med Virol., pp. 101-139. , Gilden DH, Lipton HL (eds): Boston, Kluwer; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch Neurol, 28, pp. 298-303; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Knobler, R.L., Haspel, M.V., Oldstone, M.B.A., Mouse hepatitis virus type 4 (JHM strain)-induced fatal central nervous system disease. 1. Genetic control and the murine neurone as the susceptible site for disease (1981) J Exp Med, 153, pp. 832-843; Sorensen, O., Durge, R., Percy, D., Dales, S., In vivo and in vitro models of demyelinating disease: Endogenous factors influencing demyelinating disease caused by mouse hepatitis virus in rats and mice (1982) Infect Immun, 37, pp. 1248-1260; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Barthold, S.W., Smith, A.L., Mouse hepatitis virus S in weanling Swiss mice following intranasal inoculation (1983) Lab Anim Sci, 33, pp. 355-360; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Perlman, S., Jacobsen, G., Olson, A.L., Afifi, A., Identification of the spinal cord as a major site of persistence during chronic infection with a murine coronavirus (1990) Virology, 175, pp. 418-426; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J Neurovirol, 2, pp. 361-376; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol, 5, pp. 9-14; Wang, F.I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J Neuroimmunol, 30, pp. 31-41; Suzumura, A., Lavi, E., Weiss, S.R., Silberberg, D.H., Coronavirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes (1986) Science, 232, pp. 991-993; Suzumura, A., Lavi, E., Bhat, S., Murasko, D.M., Weiss, S.R., Silberberg, D.H., Induction of glial cell MHC antigen expression in neurotropic coronavirus infection: Characterization of the H-2 inducing soluble factor elaborated by infected brain cells (1988) J Immunol, 140, pp. 2068-2072; Lavi, E., Suzumura, A., Lampson, L.A., Expression of MHC class I genes in mouse hepatitis virus (MHV-A59) infection and in multiple sclerosis (1987) Adv Exp Med Biol, 218, pp. 219-222; Lavi, E., Suzumura, A., Murray, E.M., Silberberg, D.H., Weiss, S.R., Induction of MHC class I antigens on glial cells is dependent on persistent mouse hepatitis virus infection (1989) J Neuroimmunol, 22, pp. 107-111; Gombold, J.L., Weiss, S.R., Mouse hepatitis virus A59 increases steady-state levels of MHC mRNAs in primary glial cell cultures and in the murine central nervous system (1992) Microb Pathog, 13, pp. 493-505; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J Neurovirol, 2, pp. 101-110; Fleming, J.O., Wang, F.I., Trousdale, M.D., Hinton, D.R., Stohlman, S.A., Interaction of immune and central nervous systems: Contribution of antiviral Thy-1+ cells to demyelination induced by coronarvirus JHM (1993) Reg Immunol, 5, pp. 37-43; Sussman, M.A., Shubin, R.A., Kyuwa, S., Stohlman, S.A., Cell-mediated clearance of mouse hepatitis virus strain JHM from the central nervous system (1989) J Virol, 63, pp. 3051-3056; Lin, M.T., Stohlman, S.A., Hinton, D.R., Mouse hepatitis virus is cleared from the central nervous systems of mice lacking perforin-mediated cytolysis (1997) J Virol, 71, pp. 383-391; Gombold, J.L., Sutherland, R.M., Lavi, E., Paterson, Y., Weiss, S.R., Mouse hepatitis virus A59-induced demyelination can occur in the absence of CD8+ T cells (1995) Microb Pathog, 18, pp. 211-221; Sutherland, R.M., Chua, M.-M., Lavi, E., Weiss, S.R., Paterson, Y., CD4+ and CD8+ T cells are not major effectors of mouse hepatitis virus A59-induced demyelinating disease (1997) J Neurovirol, 3, pp. 225-228; Koller, B.H., Marrack, P., Kappler, J.W., Smithies, O., Normal development of mice deficient in β2M, MHC class I proteins, and CD8+ T cells (1990) Science, 248, pp. 1227-1230; Keck, J.G., Matsushira, G.K., Makino, S., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J Virol, 62, pp. 1810-1813; Lavi, E., Fishman, S.P., Highkin, M.K., Weiss, S.R., Limbic encephalitis following inhalation of murine coronavirus MHV-A59 (1988) Lab Invest, 58, pp. 31-36; Lavi, E., Strizki, J.M., Ulrich, A.M., CXCR-4 (Fusin), a co-receptor for the type 1 human immunodeficiency virus (HIV-1), is expressed in the human brain in a variety of cell types including microglia and neurons (1997) Am J Pathol, 151, pp. 1035-1042; Lee, V.-Y., Page, C.D., Wu, H.L., Schlaepfer, W.W., Monoclonal antibodies to gel excised glial filament protein and their reactivities with other intermediate filament proteins (1984) J Neurochem, 42, p. 25; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab Invest, 62, pp. 570-578; Leparc-Goffart, I., Hingley, S.T., Chua, M.-M., Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis phenotypes of murine coronavirus MHV-A59 are associated with a Q159L amino acid substitution in the receptor binding domain of the spike protein (1997) Virology, 239, pp. 1-10; Roullet, E., Assuerus, V., Gozlan, J., Cytomegalovirus multifocal neuropathy in AIDS: Analysis of 15 consecutive cases (1994) Neurology, 44, pp. 2174-2182; Bender, B.S., Croghan, T., Zhang, L., Small, P.A.J., Transgenic mice lacking class I major histocompatibility complex-restricted T cells have delayed viral clearance and increased mortality after influenza virus challenge (1992) J Exp Med, 175, pp. 1143-1145; Doherty, P.C., Hou, S., Southern, P.J., Lymphocytic choriomeningitis virus induces a chronic wasting disease in mice lacking class I major histocompatibility complex glycoproteins (1993) J Neuroimmunol, 46, pp. 11-17; Muller, D., Koller, B.H., Whitton, J.L., LaPan, K.E., Brigman, K.K., Frelinger, J.A., LCMV-specific, class II-restricted cytotoxic T cells in beta-2-microglobulin-deficient mice (1992) Science, 255, pp. 1576-1578; Spriggs, M.K., Koller, B.H., Sato, T., Beta-2-microglobulin-, CD8+ T-cell-deficient mice survive inoculation with high doses of vaccinia virus and exhibit altered IgG responses (1992) Proc Natl Acad Sci USA, 89, pp. 6070-6074; Polic, B., Jonjic, S., Pavic, I., Crukovic, I., Zorica, I., Hengel, H., Lucin, P., Koszinoski, U.H., Lack of MHC class I complex expression has no effect on spread and control of cytomegalovirus infection in vivo (1996) J Gen Virol, 77, pp. 217-225; Lee, S.K., Youn, H.Y., Hasegawa, A., Nakayama, H., Goto, N., Apoptotic changes in the thymus of mice infected with mouse hepatitis virus, MHV-2 (1994) J Vet Med Sci, 56, pp. 879-882; Rodriguez, M., Dunkel, A.J., Thiemann, R.L., Leibowitz, J., Zijlstra, M., Jaenisch, R., Abrogation of resistance to Theiler's virus-induced demyelination in H-2b mice deficient in beta-2-microglobulin (1993) J Immunol, 151, pp. 266-276; Pullen, L.C., Miller, S.D., Dal Canto, M.C., Kim, B.S., Class I-deficient resistant mice intracerebrally inoculated with Theiler's virus show an increased T cell response to viral antigens and susceptibility to demyelination (1993) Eur J Immunol, 23, pp. 2287-2293; Fiette, L., Aubert, C., Brahic, M., Rossi, C.P., Theiler's virus infection of beta-2-microglobulin-deficient mice (1993) J Virol, 67, pp. 589-592; Miller, D.J., Rivera-Quinones, C., Njenga, M.K., Leibowitz, J., Rodriguez, M., Spontaneous CNS remyelination in beta-2-microglobulin-deficient mice following virus-induced demyelination (1995) J Neurosci, 15, pp. 8345-8352","Lavi, E.; Division of Neuropathology, Dept. Pathology Laboratory Medicine, University Pennsylvania Sch Medicine, Philadelphia, PA 19104-6085, United States; email: lavi@mail.med.upenn.edu",,"S. Karger AG",10152008,,PATHE,"10023135","English","Pathobiology",Article,"Final",,Scopus,2-s2.0-0032969810
"Uzelac-Keserovic, Apostolov K.","7409926355;57213866586;","Erratum: Isolation of a coronavirus from kidney biopsies of endemic Balkan nephropathy patients (Nephron (1999) 81 (141-145))",1999,"Nephron","82","4",,"371","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032818840&partnerID=40&md5=3507b34e818ff9690ad50c44303caefa",,"Uzelac-Keserovic; Apostolov, K.",[No abstract available],,"erratum; error; priority journal",,,,,00282766,,NPRNA,,"English","Nephron",Erratum,"Final",,Scopus,2-s2.0-0032818840
"Scott F.W.","35611898900;","Evaluation of risks and benefits associated with vaccination against coronavirus infections in cats",1999,"Advances in Veterinary Medicine","41","C",,"347","358",,3,"10.1016/S0065-3519(99)80026-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032608458&doi=10.1016%2fS0065-3519%2899%2980026-3&partnerID=40&md5=87a7261d0c2305ecb23c95105f1ba9f4","Cornell Feline Health Center College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Scott, F.W., Cornell Feline Health Center College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States",[No abstract available],,"virus vaccine; animal; animal disease; cat; cat disease; immunology; review; risk assessment; vaccination; virus infection; Animals; Cat Diseases; Cats; Coronavirus Infections; Risk Assessment; Vaccination; Viral Vaccines","Addie, D.D., Jarrett, O., Control of feline coronavirus infections in breeding catteries by serotesting, isolation, and early weaning (1995) Feline Pract., 23 (3), pp. 92-95; Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., The risk of typical and antibody enhanced feline infectious peritonitis among cats from feline coronavirus endemic households (1995) Feline Pract., 23 (3), pp. 24-26; Bonaduce, A., Infektiöse Pleuritis der Katzen (1942) Nuova Vet., 21, p. 32; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J.D., Characterization of a temperature sensitive feline infectious peritonitis coronavirus (1989) Arch. Virol., 109, pp. 185-196; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J. Virol., 66, pp. 6695-6705; de Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Chapter 14. Siddell S.G. (Ed), Plenum, New York; Elston, T., Rodan, I., Flemming, D., Ford, R.B., Hustead, D.R., Richards, J.R., Rosen, D.K., Scott, F.W., 1998 Report of the American Association of Feline Practitioners and Academy of Feline Medicine Advisory Panel on feline vaccines (1998) J. Am. Vet. Med. Assoc., 212, pp. 227-241; Fanton, R.W., Field safety studies of an intranasal FIPV vaccine (1991) New Perspectives on Prevention of Feline Infectious Peritonitis, pp. 47-50. , Pollock R.V.H. (Ed), SmithKline Beecham Animal Health, Lincoln, NB; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A.P.M., Horzinek, M.C., Lutz, H., Evaluation of the safety and efficacy of a modified live FIPV vaccine under field conditions (1995) Feline Pract., 23 (3), pp. 83-88; Feldmann, B.M., Jortner, B.S., Clinico-pathologic conference (1964) J. Am. Vet. Med. Assoc., 144, pp. 1409-1420; Fiscus, S.A., Teramoto, Y.A., Functional differences between the peplomers of two antigenically distinct feline infectious peritonitis virus isolates (1986) J. Cell. Biochem., 10 D, p. 293. , (abstr.); Fiscus, S.A., Teramoto, Y.A., Antigenic comparison of feline coronavirus isolates: evidence for markedly different peplomer glycoproteins (1987) J. Virol., 61, pp. 2607-2613; Gerber, J.D., Overview of the development of a modified live temperature-sensitive FIP virus vaccine (1995) Feline Pract., 23 (3), pp. 62-66; Gerber, J.D., Ingersoll, J.D., Gast, A.M., Christianson, K.K., Selzer, N.L., Landon, R.M., Pfeiffer, N.E., Beckenhauer, W.H., Protection against feline infectious peritonitis by intranasal inoculation of a temperature-sensitive FIPV vaccine (1990) Vaccine, 8, pp. 536-542; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Holmes, K., Coronavirus replication (1985) Virology, pp. 1331-1343. , Fields B.N., et al. (Ed), Raven Press, New York; Holmes, K.V., Compton, S.R., Coronavirus receptors (1995) The Coronaviridae, pp. 55-71. , Chapter 4. Siddell S.G. (Ed), Plenum, New York; Holzworth, J., Some important disorders of cats (1963) Cornell Vet., 53, pp. 157-160; Hoskins, J.D., Taylor, H.W., Lomax, T.L., Independent evaluation of a modified live feline infectious peritonitis virus vaccine under expermental conditions (Louisiana experience) (1995) Feline Pract., 23 (3), pp. 72-73; Hoskins, J.D., Henk, W.G., Storz, J., Kearney, M.T., The potential use of a modified live FIPV vaccine to prevent experimental FECV infection (1995) Feline Pract., 23 (3), pp. 89-90; Jacobse-Geels, H.E., Daha, M.R., Horzinek, M.C., Isolation and characterization of feline C3 and evidence for the immune complex pathogenesis of feline infectious peritonitis (1980) J. Immunol., 125 (4), pp. 1606-1610; Jakob, H., Therapeutische, kasuistische und statistische Mitteilungen aus der Klinik für kleine Haustiere an der Reichstierarzneischule in Utrecht (Holland). Jahrgang 1912/13 (1914) Z. Tiermed., 18, p. 193; Joshua, J.O., Vomiting in the cat (1960) Mod. Vet. Pract., 41 (22), pp. 36-42; Kass, P.H., Dent, T.H., The epidemiology of feline infectioius peritonitis in catteries (1995) Feline Pract., 23 (3), pp. 27-32; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; McArdle, F., Tennant, B., Kelly, D.F., Gaskell, C.J., Gaskell, R.M., Independent evaluation of a modified live FIPV vaccine under experimental conditions (University of Liverpool experience) (1995) Feline Pract., 23 (3), pp. 67-71; Montali, R.J., Strandberg, J.D., Extraperitoneal lesions in feline infectious peritonitis (1972) Vet. Pathol., 9, pp. 109-121; Ngichabe, C.K., Recombinant raccoon poxvirus-vectored feline vaccines (1992) Ph.D. Thesis, , Cornell University, Ithaca, NY; Olsen, C.W., A review of feline infectious peritonitis virus: molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-37; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Olsen, C.W., Corapi, W.V., Jacobson, R.H., Simkins, R.A., Saif, L.J., Scott, F.W., Identification of antigenic sites mediating antibody-dependent enhancement of feline infectious peritonitis virus infectivity (1993) J. Gen. Virol., 74, pp. 745-749; Pedersen, N.C., Morphologic and physical characteristics of feline infectious peritonitis and its growth in autochthonous peritoneal cell cultures (1976) Am. J. Vet. Res., 37, pp. 567-572; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections. Part 2: Feline infectious peritonitis (1983) Feline Pract., 13 (5), pp. 5-20; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; (1995) Feline Pract., 23, pp. 2-111. , Pedersen N.C. (Ed). University of California, Davis 3; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23 (3), pp. 7-20; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Reeves, N.P., Vaccination against naturally occurring FIP in a single large cat shelter (1995) Feline Pract., 23 (3), pp. 81-82; Scott, F.W., Feline infectious peritonitis: Transmission and epidemiology (1991) New Perspectives on Prevention of Feline Infectious Peritonitis, pp. 8-13. , Pollock R.V.H. (Ed), SmithKline Beecham Animal Health, Lincoln, NB; Scott, F.W., Corapi, W.V., Olsen, C.W., Evaluation of the safety and efficacy of Primucell-FIP vaccine (1992) Feline Health Top, 7 (3), pp. 6-8; Scott, F.W., Corapi, W.V., Olsen, C.W., Independent evaluation of a modified live FIPV vaccine under experimental conditions (Cornell experience) (1995) Feline Pract, 23 (3), pp. 74-76; Scott, F.W., Olsen, C.W., Corapi, W.V., Antibody-dependent enhancement of feline infectious peritonitis virus infection (1995) Feline Pract, 23 (3), pp. 77-80; Smith, H.A., Jones, T.C., (1961) Veterinary Pathology. 2nd ed., , Lea & Febiger, Philadelphia; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stoddart, C.A., Scott, F.W., Correlation between replication of feline coronaviruses in feline macrophages in vitro and the pathogenesis of feline infectious peritonitis (1986) J. Cell. Biochem., 10 D, p. 299. , (abstr.); Stoddart, C.A., Scott, F.W., Isolation and identification of feline peritoneal macrophages for in vitro studies of coronavirus-macrophage interactions (1988) J. Leukocyte Biol., 44, pp. 319-328; Stoddart, C.A., Barlough, J.E., Scott, F.W., Experimental studies of a coronavirus and coronavirus-like agent in a barrier-maintained feline breeding colony (1984) Arch. Virol., 79, pp. 85-94; Vennema, H., de Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J. Virol., 64, pp. 1407-1409; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: comparisons with dengue hemorrhagic fever (1981) Comp. Immunol. Microbiol. Infect. Dis., 4, pp. 175-189; Wolf, J., The impact of feline infectious peritonitis on catteries (1995) Feline Pract., 23 (3), pp. 21-23; Wolfe, L.G., Griesemer, R.A., Feline infectious peritonitis (1966) Vet. Pathol., 3, pp. 255-270; Woods, R.D., Pedersen, N.C., Cross-protection studies between feline infectious peritonitis and porcine transmissible gastroenteritis viruses (1979) Vet. Microbiol., 4, pp. 11-16","Scott, F.W.; Cornell Feline Health Center College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States",,"Academic Press Inc.",1093975X,,,"9890027","English","Adv. Vet. Med.",Book Chapter,"Final",Open Access,Scopus,2-s2.0-0032608458
"Pratelli A., Tempesta M., Roperto F.P., Sagazio P., Carmichael L., Buonavoglia C.","7004884960;7005599031;55143006800;6602970263;7101757988;7005623145;","Fatal coronavirus infection in puppies following canine parvovirus 2b infection",1999,"Journal of Veterinary Diagnostic Investigation","11","6",,"550","553",,50,"10.1177/104063879901100615","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0004618303&doi=10.1177%2f104063879901100615&partnerID=40&md5=0d7468c6b23af1cddd4c17df0dc3b264","Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy; Department of Veterinary Pathology, University of Naples, Naples, Italy; Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Pratelli, A., Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy; Tempesta, M., Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy; Roperto, F.P., Department of Veterinary Pathology, University of Naples, Naples, Italy; Sagazio, P., Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy; Carmichael, L., Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Buonavoglia, C., Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy",[No abstract available],,"animal; animal disease; article; case report; Coronavirus; dog; dog disease; enteritis; fatality; gastrointestinal hemorrhage; isolation and purification; newborn; Parvovirus; pathogenicity; pathology; virology; virus infection; Animals; Animals, Newborn; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Enteritis; Fatal Outcome; Gastrointestinal Hemorrhage; Parvoviridae Infections; Parvovirus, Canine","Appel, M.J., Canine coronavirus (1987) Virus Infections of Carnivores, pp. 115-122. , ed. Appel MJG, Elsevier, Amsterdam, The Netherlands; Appel, M.J., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet Med, 83, pp. 360-366; Binn, L.N., Lazar, E.C., Keenan, K.P., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc US Anim Health Assoc, 78, pp. 359-366; Carmichael, L.E., Binn, L.N., New enteric viruses in dog (1981) Adv Vet Sci Comp Med, 25, pp. 1-37; Carmichael, L.E., Joubert, J.C., Pollock, R.V.H., Hemagglutination by canine parvovirus: Serologic studies and diagnostic applications (1980) Am J Vet Res, 41, pp. 784-792; Carmichael, L.E., Schlafer, D.H., Hashimoto, A., Minute virus of canines (MVC, canine parvovirus type-1): Pathogenicity for pups and seroprevalence estimate (1994) J Vet Diagn Invest, 6, pp. 165-174; Evermann, J.F., Foreyt, W., Maag-Miller, L., Acute hemorrhagic enteritis associated with canine coronavirus and parvovirus infections in a captive coyote population (1980) J Am Vet Med Assoc, 177, pp. 784-786; Greene, C.E., Canine coronaviral enteritis (1990) Infectious Diseases of the Dog and Cat, pp. 281-283. , ed. Greene CE, WB Saunders, Philadelphia, PA; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical, and immunofluorescent techniques (1976) Am J Vet Res, 37, pp. 247-256; Martin, H.D., Zeidner, N.S., Concomitant cryptosporidia, coronavirus and parvovirus infection in a raccoon (Procyon lotor) (1992) J Wildl Dis, 28, pp. 113-115; Meunier, P.C., Cooper, B.J., Appel, M.J., Slauson, D.O., Pathogenesis of canine parvovirus enteritis: Sequential virus distribution and passive immunization (1985) Vet Pathol, 22, pp. 617-624; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet Microbiol, 36, pp. 1-37; Takeuchi, A., Binn, L.N., Jervis, H.R., Keenan, K.P., Electron microscopic study of experimental enteric infection in neonatal dogs with a canine coronavirus (1976) Lab Invest, 34, pp. 539-549; Yasoshima, A., Fujinami, F., Doi, K., Case report on mixed infection of canine parvovirus and canine coronavirus. Electron microscopy and recovery of canine coronavirus (1983) Jpn J Vet Sci, 45, pp. 217-225","Pratelli, A.; Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada Prov. per Casamassina km 3, 70010 Valenzano (Bari), Italy",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12968743","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0004618303
"Kiss I., Ros C., Kecskeméti S., Tanyi J., Klingeborn S.B., Belák S.","6603849862;7003764949;6603764465;6603437628;6506561031;56053373800;","Observations on the quasispecies composition of three animal pathogenic RNA viruses",1999,"Acta Veterinaria Hungarica","47","4",,"471","480",,11,"10.1556/AVet.47.1999.4.7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033256213&doi=10.1556%2fAVet.47.1999.4.7&partnerID=40&md5=f77d2f166cb7bdd49d9c99b166ca7123","Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","Kiss, I., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Ros, C., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Kecskeméti, S., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Tanyi, J., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Klingeborn, S.B., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Belák, S., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","The quasispecies nature of three animal pathogenic RNA viruses of field origin was examined by testing variants of classical swine fever virus (CSFV) originating from geographically different areas, feline coronavirus (FCoV) detected from the same animal by successive sampling, and rabbit haemorrhagic disease virus (RHDV) originating from successive outbreaks in the same geographic area. Clinical samples were investigated using reverse transcriptase polymerase chain reaction (RT-PCR) and ensuing single strand conformational polymorphism (SSCP) assay. By the combination of these methods even subtle differences could be detected among the amplified fragments of the same virus species of different origin. FCoV proved to comprise the most and CSFV the less heterogeneous virus quasispecies. The results show that the combination of RT-PCR and SSCP provides novel and highly sensitive means for the characterisation of RNA viruses, with special regard to genome composition, evolution, features of pathogenicity and molecular epizootiology.","CSFV; FCoV; Quasispecies; RHDV; RT-PCR; SSCP","Animalia; Classical swine fever virus; Coronavirus; Felidae; Feline coronavirus; Oryctolagus cuniculus; Rabbit hemorrhagic disease virus; RNA viruses; Sus scrofa; primer DNA; virus DNA; virus RNA; animal; animal disease; article; Calicivirus; cat; chemistry; classification; Coronavirus; genetics; isolation and purification; Pestivirus; rabbit; reverse transcription polymerase chain reaction; RNA virus; single strand conformation polymorphism; swine; swine disease; virology; virus infection; Animals; Caliciviridae Infections; Cats; Classical Swine Fever; Classical swine fever virus; Coronaviridae Infections; Coronavirus; DNA Primers; DNA, Viral; Hemorrhagic Disease Virus, Rabbit; Polymorphism, Single-Stranded Conformational; Rabbits; Reverse Transcriptase Polymerase Chain Reaction; RNA Viruses; RNA, Viral; Swine","Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-van Dillen, P.M.E., Van Der Nooredaa, J., Rapid and simple method for purification of nucleic acid (1990) J. Clin. Microbiol., 28, pp. 495-503; Cheung, R.C., Matsui, S., Greenberg, H., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) J. Clin. Microbiol., 32, pp. 2593-2597; Domingo, E., Diez, J., Martinez, M.A., Hernandez, J., Holguin, A., Borrego, B., Mateu, M.G., New observations on antigenic diversification of RNA viruses. Antigenic variation is not dependent on immune selection (1993) J. Gen. Virol., 74, pp. 2039-2045; Eggers, H.J., Tamm, I., Coxsackie A9 virus: Mutation from drug dependence to drug resistance (1965) Science, 148, pp. 97-98; Granoff, A., Induction of Newcastle disease virus mutants with nitrous acid (1961) Virology, 13, pp. 402-408; Gunn-Moore, D.A., Gunn-Moore, F.J., Harbour, D.A., Gruffydd-Jones, T.J., Detection of FCoV quasispecies using denaturing gradient gel electrophoresis (1998) First International Meeting on Virology of Carnivores, , Utrecht, The Netherlands, 13-15 May; Hayashi, K., PCR-SSCP: A simple and sensitive method for detection of mutations in the genomic DNA (1991) PCR Methods and Applications, 1, pp. 34-38; Holland, J.J., De La Torre, J.C., Steinhauer, D.A., RNA virus populations as quasispecies (1992) Curr. Topics Microbiol. Immunol., 176, pp. 1-20; Katz, J.B., Ridpath, J., Bolin, S.R., Presumptive diagnostic differentiation of hog cholera virus from bovine viral diarrhea and border disease viruses by using a cDNa nested-amplification approach (1993) J. Clin. Microbiol., 31, pp. 565-568; Kiss, I., Kecskernéti, S., Bajmócy, E., Tanyi, J., PCR as a diagnostic tool for the diagnosis and epizootiological investigation of swine fever (1999) Magyar Állatorvosok Lapja, 121, pp. 22-28; Kiss, I., Kecskeméti, S., Tanyi, J., Klingeborn, S.B., Belák, S., (1999) Preliminary Studies on Feline Coronavirus Distribution in Naturally and Experimentally Infected Cats, , submitted for publication; Kurosaki, M., Enomoto, N., Marumo, F., Sato, C., Evolution and selection of hepatitis C virus variants in patients with chronic hepatitis C (1994) Virology, 205, pp. 161-169; Lázaro, C., Estivill, X., Mutation analysis of genetic diseases by asymmetric-PCR SSCP and ethidium bromide staining: Application to neurofibromatosis and cystic fibrosis (1992) Mol. Cell. Probes, 6, pp. 357-359; Martell, M., Esteban, J.I., Quer, J., Genescá, J., Wainer, A., Esteban, R., Guardia, J., Gómez, J., Hepatitis C virus (HCV) circulates as a population of different but closely related genomes: Quasispecies nature of HCV genome distribution (1992) J. Virol., 66, pp. 3225-3229; Meyers, G., Wirblich, C., Thiel, H.-J., Rabbit hemorrhagic disease virus - Molecular cloning and nucleotide sequencing of a calicivirus genome (1991) Virology, 184, pp. 664-667; Radford, A.D., Turner, P.C., Bennett, M., McArdle, F., Dawson, S., Glenn, M.A., Williams, R.A., Gaskell, R.M., Quasispecies evolution of a hypervariable region of the feline calicivirus gene in cell culture and in persistently infected cats (1998) J. Gen. Virol., 79, pp. 1-10; Ros Bascuňana, C., Nowotny, N., Belák, S., Detection and differentiation of rabbit hemorrhagic disease and European brown hare syndrome viruses by amplification of VP60 genomic sequences from fresh and fixed tissue samples (1997) J. Clin. Microbiol., 35, pp. 2492-2495; Smith, D.B., McAllister, J., Csino, C., Simmonds, P., Virus 'quasispecies': Making a mountain out of a molehill? (1997) J. Gen. Virol., 78, pp. 1511-1519; Stadejek, T., Vilček, S., Lowings, J.P., Ballagi-Pordány, A., Paton, D.J., Belák, S., Genetic heterogeneity of classical swine fever virus in Central Europe (1997) Virus Res., 52, pp. 195-204; Studdert, M.J., Rabbit haemorrhagic disease virus: A calicivirus with differences (1994) Austr. Vet. J., 71, pp. 264-266; Van Rijn, P.A., Van Gennip, H.G., Leendertse, C.H., Bruschke, C.J., Paton, D.J., Moormann, R.J., Van Oirschot, J.T., Subdivision of the pestivirus genus based on envelope glycoprotein E2 (1997) Virology, 237, pp. 337-348; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vilček, S., Paton, D.J., Application of genetic methods to study the relationship between classical swine fever outbreaks (1998) Res. Vet. Sci., 65, pp. 89-90","Kiss, I.; Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; email: istvan_kiss@ccmail.oai.hu",,"Akademiai Kiado Rt.",02366290,,,"10641337","English","Acta Vet. Hung.",Article,"Final",,Scopus,2-s2.0-0033256213
"Walsh E.E., Falsey A.R., Hennessey P.A.","7202168527;7003365074;8380865100;","Respiratory syncytial and other virus infections in persons with chronic cardiopulmonary disease",1999,"American Journal of Respiratory and Critical Care Medicine","160","3",,"791","795",,129,"10.1164/ajrccm.160.3.9901004","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032827121&doi=10.1164%2fajrccm.160.3.9901004&partnerID=40&md5=f70f0bd56a5887c801b3d2555fb11f33","Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., Rochester, NY, United States; Rochester General Hospital, 1435 Portland Ave., Rochester, NY 14621, United States","Walsh, E.E., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., Rochester, NY, United States, Rochester General Hospital, 1435 Portland Ave., Rochester, NY 14621, United States; Falsey, A.R., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., Rochester, NY, United States; Hennessey, P.A., Department of Medicine, Rochester General Hospital, Univ. Rochester Sch. Med. and Dent., Rochester, NY, United States","Respiratory syncytial virus (RSV) has been increasingly recognized as an important cause of serious respiratory illness in some adult populations, including those with underlying cardiopulmonary diseases. However, the precise incidence and the clinical impact of RSV in this group are unknown. Therefore, the incidence and clinical impact of RSV infection in persons with chronic obstructive pulmonary disease (COPD) and congestive heart failure (CHF) who reside in the community were prospectively evaluated over two consecutive winters in 134 persons. Eight RSV (incidence of 4.3 per 100 subject-winters), 13 influenza A (incidence of 7.0 per 100 subject-winters), seven rhinovirus, nine coronavirus, and two parainfluenza virus infections were identified. The clinical illnesses associated with RSV and influenza A virus were similar, causing both upper and lower respiratory signs and symptoms. The clinical impact was significant as three of eight RSV-infected subjects were hospitalized compared with six of 13 influenza A-infected persons and zero of seven rhinovirus-infected persons.",,"adult; aged; article; chronic obstructive lung disease; clinical feature; congestive heart failure; Coronavirus; female; human; incidence; Influenza virus A; major clinical study; male; Parainfluenza virus; priority journal; Respiratory syncytial pneumovirus; Rhinovirus; RNA virus infection; winter","Parrott, R.H., Kim, H.W., Arrobio, J.O., Hodes, D.S., Murphy, B.R., Brandt, C.D., Camargo, E., Chanock, R.M., Epidemiology of respiratory syncytial virus infection in Washington, D.C (1973) Am. J. Epidemiol., 98, pp. 289-300; Falsey, A.R., Cunningham, C.K., Barker, W.H., Kouides, R.W., Yuen, J.B., Menegus, M., Weiner, L.B., Betts, R.F., Respiratory syncytial virus and influenza A infections in the hospitalized elderly (1995) J. Infect. Dis., 172, pp. 389-394; Agius, G., Dindinaud, G., Biggar, R.J., Peyre, R., Vaillant, V., Ranger, S., Poupet, J.Y., Castets, M., An epidemic of respiratory syncytial virus in elderly people: Clinical and scrological findings (1990) J. Med. Virol., 30, pp. 117-127; Dowell, S.F., Anderson, L.J., Gary, H.E.J., Erdman, D.D., Plouffe, J.F., File, T.M.J., Marston, B.J., Respiratory syncytial virus is an important cause of community-acquired lower respiratory infection among hospitalized adults (1996) J. Infect. Dis., 174, pp. 456-462; Falsey, A.R., McCann, R.M., Hall, W.J., Tanner, M.A., Griddle, M.M., Formica, M.A., Irvine, C.S., Treanor, J.J., Acute respiratory tract infection in daycare centers for older persons (1995) J. Am. Geriatr, Sor., 43, pp. 30-36; Gump, D., Phillips, C., Forsyth, B., Role of infection in chronic bronchitis (1976) Am. Rev. Respir. Dis., 113, pp. 465-474; Carilli, A., Gohd, R., Gordon, W., A virologic study of chronic bronchitis (1964) N. Engl. J. Med., 170, pp. 123-127; Smith, C.B., Golden, C.A., Kanner, R.E., Renzetti, A.D., Association of viral and Mycoplasma pneumoniae infections with acute respiratory illness in patients with chronic obstructive pulmonary diseases (1980) Am. Rev. Respir. Dis., 121, pp. 225-232; Fagon, J., Chastre, J., Severe exacerbations of COPD patients: The role of pulmonary infections (1996) Sem. Respir. Infect., 11, pp. 109-118; Wiselka, M.J., Kent, J., Cookson, J.B., Nicholson, K.G., Impact of respiratory infection in patients with chronic chest disease (1993) Epidemiol. Infect., 111, pp. 337-346; Buscho, R.O., Saxtan, D., Shultz, P.S., Finch, E., Mufson, M.A., Infections with viruses and Mycoplasma pneumoniae during exacerbations of chronic bronchitis (1978) J. Infect. Dis., 137, pp. 377-383; Sommerville, R.G., Respiratory syncytial virus in acute exacerbations of chronic bronchitis (1963) Lancet, pp. 1247-1248; Lambert, H.P., Stern, H., Infective factors in exacerbations of bronchitis and asthma (1972) B.M.J., 3, pp. 323-327; Lamy, M.E., Pouthier-Simon, F., Debacker-Willame, E., Respiratory viral infections in hospital patients with chronic bronchitis (1973) Chest, 63, pp. 336-341; Katz, S., Ford, A.B., Moskowitz, R.W., Jackson, B.A., Jaffe, M.W., Studies of illness in the aged: The index of ADL, a standardized measure of biological and psychological function (1963) J. A. M. A., 185, pp. 914-919; Lawton, P.M., The function assessment of elderly people (1971) J. Am. Geriatr. Soc., 19, pp. 465-481; Hospitalizations for the leading causes of death among the elderly-United States, 1987 (1990) M.M.W.R., 39, pp. 777-779; Nicholson, K.G., Impact of influenza and respiratory syncytial virus on mortality in England and Wales from January 1975 to December 1990 (1996) Epidemiol. Infect., 116, pp. 51-63; Fleming, D.M., Cross, K.W., Respiratory syncytial virus or influenza? (1993) Lancet, 342, pp. 1507-1510; Nicholson, K.G., Kent, J., Hammersley, V., Esperanza, C., Acute viral infections of upper respiratory tract in elderly people living in the community, comparative, prospective, population based study of disease burden (1997) B.M.J., 315, pp. 1060-1064; Falsey, A.R., Treanor, J.J., Betts, R.F., Walsh, E.E., Viral respiratory infections in the institutionalized elderly: Clinical and epidemiologic findings (1992) J. Am. Geriatr. Soc., 40, pp. 115-119; Chin, M.H., Goldman, M., Factors contributing to the hospitalisation of patients with congestive heart failure (1997) Am. J. Pub. Health, 87, pp. 643-648; Falsey, A.R., Walsh, E.E., Safety and immunogenicity of a respiratory syncytial virus subunit vaccine (PFP-2) in the institutionalized elderly (1997) Vaccine, 15, pp. 1130-1132; Karron, R.A., Wright, P.F., Crowe J.E., Jr., Clements, M.L., Thompson, J., Makhene, M., Evaluation of two live, cold-passaged, temperature-sensitive respiratory syncytial virus vaccines in chimpanzees and in human adults, infants, and children (1997) J. Infect. Dis., 176, pp. 1428-1436; Falsey, A.R., Walsh, E.E., Relationship of serum antibody to risk of respiratory syncytial virus infection in elderly adults (1998) J. Infect. Dis., 177, pp. 463-466","Walsh, E.E.; Rochester General Hospital, 1435 Portland Ave., Rochester, NY 14621, United States",,"American Lung Association",1073449X,,AJCME,"10471598","English","Am. J. Respir. Crit. Care Med.",Article,"Final",,Scopus,2-s2.0-0032827121
"Daniels M.J., Golder M.C., Jarrett O., MacDonald D.W.","7201966532;7003406615;7006845693;7401463172;","Feline viruses in wildcats from Scotland",1999,"Journal of Wildlife Diseases","35","1",,"121","124",,57,"10.7589/0090-3558-35.1.121","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032616319&doi=10.7589%2f0090-3558-35.1.121&partnerID=40&md5=7d2a4ce2a98bbd15ec833c017a0a3245","Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Department of Veterinary Pathology, University of Glasgow, Bearsden, Glasgow G61 1QH, United Kingdom","Daniels, M.J., Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom; Golder, M.C., Department of Veterinary Pathology, University of Glasgow, Bearsden, Glasgow G61 1QH, United Kingdom; Jarrett, O., Department of Veterinary Pathology, University of Glasgow, Bearsden, Glasgow G61 1QH, United Kingdom; MacDonald, D.W., Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom","Few data are available on the prevalence of feline viruses in European wildcats (Felis silvestris). Previous surveys have indicated that wildcats may be infected with the common viruses of domestic cats, apart from feline immunodeficiency virus (FIV). In the present study, 50 wildcats trapped throughout Scotland (UK) between August 1992 and January 1997 were tested for evidence of viral infection. All were negative for FIV by several serological or virological methods. By contrast, 10% of the cats were positive for feline leukemia virus (FeLV) antigen and infectious virus was isolated from 13% of a smaller subset. Of the wildcats tested for respiratory viruses, 25% yielded feline calicivirus (FCV) and although no feline herpesvirus was isolated, 16% of the samples had neutralizing antibodies to this virus. Antibodies to feline coronavirus (FCoV) were found in 6% of samples. Feline foamy virus (FFV) was an incidental finding in 33% of samples tested. This study confirms that wildcats in Scotland are commonly infected with the major viruses of the domestic cat, except for FIV.","Feline calicivirus; Feline corona virus; Feline foamy virus; Feline herpesvirus; Feline immunodeficiency virus; Feline leukemia virus; Felis silvestris; Survey; Wildcats","Caliciviridae; Corona virus; Coronavirus; Felidae; Feline calicivirus; Feline coronavirus; Feline foamy virus; Feline herpesvirus 1; Feline immunodeficiency virus; Feline leukemia virus; Felis catus; Felis silvestris; Herpes; Herpesviridae; Human spumaretrovirus; Spumavirus; animal; animal disease; article; Calicivirus; Carnivora; Coronavirus; Feline immunodeficiency virus; Feline leukemia virus; female; Herpes virus; Herpes virus infection; immunology; isolation and purification; male; prevalence; Retrovirus infection; Spuma virus; United Kingdom; virus infection; wild animal; Animals; Animals, Wild; Caliciviridae Infections; Calicivirus, Feline; Carnivora; Coronavirus; Coronavirus Infections; Female; Herpesviridae; Herpesviridae Infections; Immunodeficiency Virus, Feline; Leukemia Virus, Feline; Male; Prevalence; Retroviridae Infections; Scotland; Spumavirus; Virus Diseases","Addie, D.D., Jahrett, O., A study of naturally occuring feline coronavirus infections in kittens (1992) Veterinary Record, 130, pp. 133-137; Artois, M., Redmond, M., Viral diseases as a threat to free-living wild cats (Felis silvestris) in continental Europe (1994) Veterinary Record, 134, pp. 651-652; Brown, E.W., Yuhki, N., Packer, C., O'Brien, S.J., A lion lentivirus related to feline immunodeficiency virus: Epidemiologic and phylogenetic aspects (1994) Journal of Virology, 68, pp. 5953-5968; Callanan, J.J., Feline immunodeficiency virus infection: A clinical and pathological perspective (1995) Feline Immunology and Immunodeficiency, pp. 111-129. , B. J. Willet, and O. Jarrett (eds.). Oxford University Press, Oxford, UK; Carpenter, M.A., Brown, E.W., Culver, M., Johnson, W.E., Pecon, J., Genetic and phylogenetic divergence of feline immunodeficiency virus in the Puma (Puma concolor) (1996) Journal of Virology, 70, pp. 6682-6693; Daniels, M.J., (1997) The Biology and Conservation of the Wildcat in Scotland, , Ph.D. Dissertation, Oxford University, Oxford, UK, 207 pp; Daniels, M.J., Balharry, D., Hirst, D., Kitchener, A.C., Aspinall, R.J., Morphological and pelage characteristics of wild living cats in Scotland: Implications for defining the 'wildcat' (1998) Journal of Zoology, 244, pp. 231-247. , London; Evermann, J.F., Foreyt, W.J., Hall, B., McKeirnan, A.J., Occurrence of Puma lentivirus infection in cougars from Washington (1997) Journal of Wildlife Diseases, 33, pp. 316-320; Gaskell, R.M., Bennett, M., Other feline virus infections (1994) Feline Medicine and Therapeutics, 2nd Edition, pp. 535-543. , E. A. Chandler, C. J. Gaskell, and R. M. Gaskell (eds.). Blackwell Scientific Publications, Oxford, UK; Dawson, S., Viral induced upper respiratory tract disease (1994) Feline Medicine and Therapuetics, 2nd Edition, pp. 453-472. , E. A. Chandler, C. J. Gaskell, and R. M. Gaskell (eds.). Blackwell Scientific Publications, Oxford, UK; Horimoto, T., Limcumpao, J.A., Tohya, Y., Takahashi, E., Mikami, E., Enhancement of neutralizing activity of antifeline herpesvirus type 1 sera by complement supplementation (1989) Japanese Journal of Veterinary Science, 51, pp. 1025-1027; Hosie, M.J., Jarrett, O., Serological responses of cats to feline immunodeficiency virus (1990) AIDS, 4, pp. 215-220; Robertson, C., Jarrett, O., Prevalence of feline leukemia virus and antibodies to feline immunodeficiency virus in cats in the United Kingdom (1989) Veterinary Record, 128, pp. 293-297; Jarrett, O., Feline leukemia virus (1994) Feline Medicine and Therapuetics, 2nd Edition, pp. 473-487. , E. A. Chandler, C. J. Gaskell, and R. M. Gaskell (eds.). Blackwell Scientific Publications, Oxford, UK; Laird, H.M., Hay, D., Determinants of the host range ot feline leukaemia viruses (1973) Journal of General Virology, 20, pp. 169-175; Hay, D., Laird, H.M., Infection by feline syncytium-forming virus in Britain (1974) Veterinary Record, 69, p. 201; Ganiere, J.P., Comparative efficacy studies with a recombinant feline leukemia virus (1996) Veterinary Record, 138, pp. 7-11. , J. P; McOrist, S., Boid, R., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Some viral and protozool diseases in the European Wildcat (Felis silvestris) (1991) Journal of Wildlife Disease, 27, pp. 693-696; Ormerod, E., Jarrett, O., A classification of feline calicivirus isolates based on plaque morphology (1978) Journal of General Virology, 39, pp. 537-540; Paul-Murphy, J., Work, T., Hunter, D., McFie, E., Fjeline, D., Serological survey and senim biochemical reference ranges of the free ranging mountain lion (Felis concolor) in California (1994) Journal of Wildlife Diseases, 30, pp. 205-215; Roelke, M.E., Forrester, D.J., Jacobson, E.R., Kollias, G.V., Scott, F.W., Barr, M.C., Evermann, J.F., Pirtle, E.C., Seroprevelance of infectious disease agents in free-ranging Florida panthers (Felis concolor corgi) (1993) Journal of Wildlife Diseases, 29, pp. 36-49; Stoddart, M.E., Bennett, M., Feline coronavirus infection (1994) Feline Medicine and Therapuetics, 2nd Edition, pp. 506-514. , E. A. Chandler, C. J. Gaskell, and R. M. Gaskell (eds.). Blackwell Scientific Publications, Oxford, UK; Vandewoude, S., O'Brien, S.J., Hoover, E.A., Infectivity of lion and puma lentiviruses for domestic cats (1997) Journal of General Virology, 78, pp. 795-800; Yamaguchi, N., MacDonald, D.W., Passanisi, W.C., Harbour, D.A., Hopper, C.D., Parasite prevalence in free-ranging farm cats, Felis silvestris catus (1996) Epidemiology and Infection, 116, pp. 217-223","Daniels, M.J.; Wildlife Conservation Research Unit, Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, United Kingdom",,"Wildlife Disease Association, Inc.",00903558,,,"10073361","English","J. Wildl. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0032616319
"Tegtmeier C., Uttenthal Aa., Friis N.F., Jensen N.E., Jensen H.E.","6604083756;6701449735;7005851313;7201410580;35595226100;","Pathological and microbiological studies on pneumonic lungs from Danish Calves",1999,"Journal of Veterinary Medicine, Series B","46","10",,"693","700",,52,"10.1046/j.1439-0450.1999.00301.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033256816&doi=10.1046%2fj.1439-0450.1999.00301.x&partnerID=40&md5=e5dd6b7357d039209b1e0d5b64ed5b33","Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Roy. Vet. and Agric. University, Bülowsvej 13, DK-1870 Frederiksberg C, Denmark","Tegtmeier, C., Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Uttenthal, Aa., Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Friis, N.F., Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Jensen, N.E., Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark; Jensen, H.E., Roy. Vet. and Agric. University, Bülowsvej 13, DK-1870 Frederiksberg C, Denmark","During 1 year, the association between microbiological and pathological findings in 72 lungs from calves submitted to the Danish Veterinary Laboratory for diagnostic purposes was studied. All cases were evaluated pathologically and bacteriologically, whereas only 68 cases were examined for the presence of bovine respiratory syncytial virus (BRSV), parainfluenza-3 virus (PI-3 virus) and bovine coronavirus, 62 cases for bovine viral diarrhoea virus (BVD), 45 cases for bovine adenovirus and 51 cases for mycoplasmas. Based on histopathological examination, the cases were diagnosed as fibrinous and/or necrotizing bronchopneumonia, suppurative bronchopneumonia, embolic pneumonia and others. The diagnoses were based on the dominating and most severe lesions in each lung. Haemophilus somnus, Pasteurella multocida, Actinomyces pyogenes, P. haemolytica and BRSV were the most commonly found bacterial and viral lung pathogens, respectively. Pasteurella spp. and H. somnus were often associated with the more severe fibrinonecrotizing type of bronchopneumonia, whereas BRSV was primarily detected in cases of suppurative bronchopneumonia. Mycoplasma boris was isolated from one case only, whereas M. dispar, M. bovirbinis and Ureaplasma diversum were present, often concomitantly, in the majority of cases. Aspergillus fumigatus was isolated from one case. © 1999 Blackwell Wissenschafts-Verlag, Berlin.",,"animal; animal disease; article; bacterium; cattle; cattle disease; classification; Denmark; fungus; lung; microbiology; Mycoplasma; pathology; pneumonia; virology; virus; Animals; Bacteria; Cattle; Cattle Diseases; Denmark; Fungi; Lung; Mycoplasma; Pneumonia; Viruses","Adegboye, D.S., Halbur, P.G., Cavanaugh, D.L., Werdin, R.E., Chase, C.C.L., Miskimins, D.W., Rosenbusch, R.P., Immunohistochemical and pathological study of Mycoplasma bovis-associated lung abscesses in calves (1995) J. Vet. Diagn. Invest., 7, pp. 335-337; Almeida, R.A., Rosenbusch, R.F., Impaired tracheobronchial clearance of bacteria in calves infected with Mycoplasma dispar (1994) J. Vet. Med. B., 41, pp. 473-482; Andrews, J.J., Anderson, T.D., Slife, L.N., Stevenson, G.W., Microscopic lesions associated with the isolation of Haemophilus somnus from pneumonic bovine lungs (1985) Vet. Pathol., 22, pp. 131-136; Barrow, G.I., Feltham, R.K.A., (1993) Cowan and Steel's Manual for the Identification of Medical Bacteria, 3rd Edn., , Cambridge University Press, Cambridge; Binder, A., Amtsberg, G., Dose, S., Fischer, W., Scholz, M., Kirchhoff, H., Untersuchung von Rindern mit respiratorischen Erkrankungen auf Mykoplasmen und bakterielle Bronchopneumonieerreger (1990) J. Vet. Med. B., 37, pp. 430-435; Bitsch, V., Friis, N.F., Krogh, H.V., A microbiological study of pneumonic calf lungs (1976) Acta. Vet. Scand., 17, pp. 32-42; Blom, J.Y., (1981) Enzootic Pneumonia in Calves, , PhD Thesis, The Royal Veterinary and Agricultural University, Denmark; Bryson, D.G., Ball, H.J., McAliskey, M., McConnell, W., McCullough, S.J., Pathological, immunocytochemical and microbiological findings in calf pneumonias associated with Haemophilus somnus infection (1990) J. Comp. Path., 103, pp. 433-445; Casals, J.B., Pringler, N., (1993) The Zym-kits and Identification Tablets for Bacteria and Yeast, , Rosco Diagnostica, Taastrup; Clyde, W.A., Growth inhibition tests (1983) Methods in Mycoplasmology, pp. 405-410. , Razin, S. and J. G. Tully (eds), Academic Press, New York; Donkersgoed, J.V., Ribble, C.S., Boyer, L.G., Townsend, H.G.G., Epidemiological study of enzootic pneumonia in dairy calves in Saskatchewan (1993) Can. J. Vet. Res., 57, pp. 247-254; Dungworth, D.L., The respiratory system (1993) Pathology of Domestic Animals, 4th Edn., , Jubb, K. V. F., P. C. Kennedy, and N. Palmer (eds), Academic Press, San Diego; Friis, N.F., Ahrens, P., Larsen, H., Mycoplasma hyosynoviae isolation from the upper respiratory tract and tonsils of pigs (1991) Acta. Vet. Scand., 32, pp. 425-429; Friis, N.F., Krogh, H.V., Isolation of mycoplasmas from Danish cattle (1983) Nord Vet-Med., 35, pp. 74-81; Gourlay, R.N., Thomas, L.H., Wyld, S.G., Increased severity of calf pneumonia associated with the appearance of Mycoplasma bovis in a rearing herd (1989) Vet. Rec., 124, pp. 420-422; Ishino, S., Oka, M., Terui, S., Ikeda, S., Pathological and microbiological studies on calf pneumonia occurring in mass rearing facilities (1979) Nat. Inst. Anim. Hlth Qu., 19, pp. 91-103; Knudtson, W.U., Reed, D.E., Daniels, G., Identification of mycoplasmatales in pneumonic calf lungs (1986) Vet. Microbiol., 11, pp. 79-91; Kobisch, M., Friis, N.F., Swine mycoplasmoses (1996) Rev. Sci. Technical Off. Int. Epiz., 15 (4), pp. 1569-1605; Krogh, H.V., Pedersen, K.B., Friis, N.F., Pneumonia in calves associated with Haemophilus somnus (1986) Proceedings of the 14th International Congress on Diseases of Cattle, pp. 585-589. , Dublin, Irish Cattle Veterinary Association, Dublin; Laak, E.A.T., Noordergraaf, J.H., Dieltjes, R.P.J.W., Prevalence of mycoplasmas in the respiratory tracts of pneumonic calves (1992) J. Vet. Med. B., 39, pp. 553-562; Larone, D.H., (1995) Medically Important Fungi, a Guide to Identification, 3rd Edn., , ASM Press, Washington; Madsen, E.B., (1984) Morbidity of Calves in Specialized Fattening Calf Production, , PhD Thesis, The Royal Veterinary and Agricultural University, Copenhagen; Meyling, A., ELISA for detection of Bovine coronavirus in faeces and intestinal contents (1982) Curr. Top. Vet. Med. Anim. Sci., 22, pp. 161-169; Meyling, A., Detection of BVD virus in viremic cattle by an indirect immunoperoxidase technique (1984) Curr. Top. Vet. Med. Anim. Sci., 29, pp. 37-46; Orr, J.P., Haemophilus somnus infection: A retrospective analysis of cattle necropsied at the Western College of Veterinary Medicine from 1970 to 1990 (1992) Can. Vet. J., 33, pp. 719-722; Popoff, Y., Le Minor, L., (1992) Antigenic Formulas of the Salmonella Serovars, , Institut Pasteur, Paris; Razin, S., Urea hydrolysis (1983) Methods in Mycoplasmology, pp. 351-353. , Razin, S., and J. G. Tully (eds), Academic Press, New York; Schiefer, B., Ward, G.E., Moffatt, R.E., Correlation of microbiological and histological findings in bovine fibrinous pneumonia (1978) Vet. Pathol., 15, pp. 313-321; Settnes, O.P., Henriksen, S.A., Pneumocystis carinii in large domestic animals in Denmark. A preliminary report (1989) Acta. Vet. Scand., 30, pp. 437-440; Tegtmeier, C., Jensen, N.E., Jensen, H.E., (1995) Development of a Peroxidase-antiperoxidase (PAP) Technique for the Identification of Haemophilus Somnus in Pneumonic Calf Lungs in Denmark, 103, pp. 540-547. , APMIS; Uttenthal, A., Jensen, N.P.B., Blom, J.Y., Viral aetiology of enzootic pneumonia in Danish dairy herds: Diagnostic tools and epidemiology (1996) Vet. Rec., 139, pp. 114-117; Watts, J.L., Yancey, R.J., Sarah, J.R., Salmon, S.A., Case, C.A., A 4-year survey of antimicrobial susceptibility trends for isolates from cattle with bovine respiratory disease in North America (1994) J. Clin. Microbiol., 32, pp. 725-731","Tegtmeier, C.; Danish Veterinary Laboratory, Bülowsvej 27, DK-1790 Copenhagen V, Denmark",,"Blackwell Verlag GmbH Berlin",09311793,,JVMBE,"10676147","English","J. Vet. Med. Ser. B",Article,"Final",,Scopus,2-s2.0-0033256816
"France M.P., Smith A.L., Stevenson R., Barthold S.W.","7006625408;57203012240;57216088690;7103367422;","Granulomatous peritonitis and pleuritis in interferon-γ gene knockout mice naturally infected with mouse hepatitis virus",1999,"Australian Veterinary Journal","77","9",,"600","604",,19,"10.1111/j.1751-0813.1999.tb13199.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033195539&doi=10.1111%2fj.1751-0813.1999.tb13199.x&partnerID=40&md5=c4ae754989c3f2a3cccabe61f0fe3c74","Department of Pathology, Loyola University, Chicago, IL 60153, United States; Murine Virus Monitoring Service, 101 Blacks Plains Road, Adelaide, SA 5086, Australia; Center for Comparative Medicine, University of California, Davis, CA 95616, United States","France, M.P.; Smith, A.L., Department of Pathology, Loyola University, Chicago, IL 60153, United States; Stevenson, R., Murine Virus Monitoring Service, 101 Blacks Plains Road, Adelaide, SA 5086, Australia; Barthold, S.W., Center for Comparative Medicine, University of California, Davis, CA 95616, United States","Objective To investigate a disease outbreak in a colony of laboratory mice with targeted disruption of the gene for interferon-γ Format A case report based on necropsy, histopathology, serology and immunohistochemistry. Results Affected mice exhibited depression and variable ascites. Necropsy revealed a granulomatous peritonitis and pleuritis with extensive adhesions although parenchymal lesions were minimal. Serum samples had high concentrations of antibody to mouse hepatitis virus and immunohistochemical examination revealed the presence of mouse hepatitis virus antigen in granuloma macrophages. Sero-logical testing for other infectious agents and bacterial culture were negative and wild type mice kept in the same facility remained healthy. Despite the association between the disease and mouse hepatitis virus infection, the precise role played by mouse hepatitis virus was not determined. While the disease is superficially similar to feline infectious peritonitis (another coronavirus-induced serositis), differences exist between the histopathological findings in these two conditions. Conclusion This unusual disease process illustrates how new diagnostic challenges can arise in novel mouse genotypes created through molecular genetics. Furthermore, the association between the disease and mouse hepatitis virus illustrates the importance of maintaining laboratory animals under specific-pathogen free conditions.","Gene knockout; Granuloma; Interferon-γ; Macrophage; Mouse; Mouse hepatitis virus; Peritonitis; Pleuritis","Animalia; Bacteria (microorganisms); Coronavirus; Felidae; Murine hepatitis virus; gamma interferon; virus antibody; virus antigen; animal; animal disease; article; ascites fluid; blood; C57BL mouse; chemistry; colon; cytology; epidemic; experimental animal; female; fluorescence microscopy; genetics; germfree animal; granuloma; immunohistochemistry; male; mouse; mouse mutant; Murine hepatitis coronavirus; pathogenicity; pathology; peritonitis; pleurisy; rodent disease; virology; virulence; virus infection; Animals; Animals, Laboratory; Antibodies, Viral; Antigens, Viral; Ascitic Fluid; Colon; Coronavirus Infections; Disease Outbreaks; Female; Granuloma; Immunohistochemistry; Interferon Type II; Male; Mice; Mice, Inbred C57BL; Mice, Knockout; Microscopy, Fluorescence; Murine hepatitis virus; Peritonitis; Pleurisy; Rodent Diseases; Specific Pathogen-Free Organisms; Virulence","Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab Anim Sci, 43, pp. 15-28; Homberger, F.R., Enterotropic mouse hepatitis virus (1996) Lab Animals, 31, pp. 97-115; Jacoby, R.O., Lindsey, J.R., Health care for research animals is essential and affordable (1997) FASEB J, 11, pp. 609-614; Kraft, V., Meyer, B., Seromonitoring in small laboratory animal colonies. A five year survey: 1984-1988 (1990) Z Versuchstierkd, 33, pp. 29-35; Stevenson, R., Annual health report - Serology of Australian rodent colonies (1996) Australian and New Zealand Society for Laboratory Animal Science Annual Conference Proceedings, p. 71. , Perth; Mouse hepatitis virus (1991) Infectious Diseases of Mice and Rats., , National Academy Press, Washington DC; De Souza, M.S., Smith, A.L., Bottomly, K., Infection of BALB/cByJ mice with the JHM strain of mouse hepatitis virus alters in vitro splenic T cell proliferation and cytokine production (1991) Lab Anim Sci, 41, pp. 99-105; Boorman, G.A., Luster, M.I., Campbell, M.L., Peritoneal macrophage alterations caused by naturally occurring mouse hepatitis virus (1982) Am J Pathol, 106, pp. 110-117; Cray, C., Mateo, M.O., Altman, N.H., Vitro and long-term in vivo immune dysfunction after infection of BALB/c mice with mouse hepatitis virus strain A59 (1993) Lab Anim Sci, 43, pp. 169-174; Liang, S., Lian, W., Leu, F., Epizootic of low-virulence hepatotropic murine hepatitis virus in a nude mice breeding colony in Taiwan (1995) Lab Anim Sci, 45, pp. 519-522; Durbin, J.E., Hackenmiller, R., Simon, M.C., Levy, D.E., Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease (1996) Cell, 84, pp. 443-450; Matthaei, K.I., Berry, J.R., France, M.P., Use of polymerase chain reaction to diagnose a natural outbreak of mouse hepatitis virus infection in nude mice (1998) Lab Anim Sci, 48, pp. 137-144; Flanagan, S.P., 'Nude', a new hairless gene with pleiotropic effects in the mouse (1966) Genet Res Camb, 8, pp. 295-309; Durum, S.K., Muegge, K., Preface (1998) Cytokine Knockouts, pp. vii-xvi. , Durum SK, Muegge K, editors. Humana Press, Totowa, New Jersey; Dalton, D.K., Pitts-Meek, S., Keshav, S., Multiple defects of immune cell function in mice with disrupted interferon-γ genes (1993) Science, 259, pp. 1739-1742; Brownstein, D.G., Barthold, S.W., Mouse hepatitis virus immunofluorescence in formalin - Or Bouin's-fixed tissues using trypsin digestion (1982) Lab Anim Sci, 32, pp. 37-39; Kusnitz, A.L., Bray, M.V., Smith, A.L., Staining method for detecting concurrent viral infections in animals with Pneumocystis carinii (1994) J Histotechnol, 17, pp. 349-351; Gledhill, A.W., Dick, G.W.A., Niven, J.S.F., Mouse hepatitis virus and its pathogenic action (1955) J Path Bact, 69, pp. 299-309; Ward, J.M., Collins, M.J., Parker, J.C., Naturally occurring mouse hepatitis virus infection in the nude mouse (1977) Lab Anim Sci, 27, pp. 372-376; Yanagisawa, T., Nakanaga, K., Kyuwa, S., Fujiwara, K., Ascitic disease in ICR-nude mice due to mouse hepatitis virus (1986) Jpn J Vet Sci, 48, pp. 7-14; Boivin, G.P., Fnl, S., Idiopathic granulomas in IFN-γ-/-, IL-10-/- double knockout mice (1998) Lab Anim Sci, 48, p. 419; Kyuwa, S., Tagawa, Y., Shibata, S., Doi, K., Murine coronavirus-induced subacute fatal peritonitis in C57BL/6 mice deficient in gamma interferon (1998) J Virol, 72, pp. 9286-9290; Schijns, V.E.C.J., Wierda, C.M.H., Van Hoeij, M., Horzinek, M.C., Exacerbated viral hepatitis in IFN-γ receptor deficient mice is not suppressed by IL-12 (1996) J Immunol, 157, pp. 815-821; Lane, T.E., Paoletti, A.D., Buchmeier, M.J., Disassociation between the in vitro and in vivo effects of nitric oxide on a neurotropic murine coronavirus (1997) J Virol, 71, pp. 2202-2210; Schijns, V.E.C.J., Haagmans, B.L., Wierda, C.M.H., Mice lacking IL-12 develop polarized Th1 cells during viral infection (1998) J Immunol, 160, pp. 3958-3964; Smith, A.L., Barthold, S.W., De Souza, M.S., Bottomly, K., The role of gamma interferon in infection of susceptible mice with murine coronavirus, MHV-JHM (1991) Arch Virol, 121, pp. 89-100; Ma, L., Modolell, M., Eichmann, K., Pereira, C.A., Vivo depletion of interferon-gamma leads to susceptibility of A/J mice to mouse hepatitis virus 3 infection (1992) Immunobiology, 185, pp. 475-482; Melnicoff, M.J., Horna, P.K., Breslin, E.W., Morahan, P.S., Maintenance of peritoneal macrophages in the steady state (1988) J Leukocyte Biol, 44, pp. 367-375; Bellingan, G.J., Caldwell, H., Howie, S.E.M., Dransfield, I., Haslett, C., Vivo fate of the inflammatory macrophage during the resolution of inflammation. Inflammatory macrophages do not die locally, but emigrate to the drain ng lymph nodes (1996) J Immunol, 157, pp. 2577-2585; Billiau, A., Interferon-γ: Biology and role in pathogenesis (1996) Adv Immunol, 62, pp. 61-130; Dempsey, W.L., Smith, A.L., Morahan, P.S., Effect of inapparent murine hepatitis virus infections on macrophages and host resistance (1986) J Leukocyte Biol, 39, pp. 559-565; Puddu, P., Fantuzzi, L., Borghi, P., IL-12 induces IFN-γ expression and secretion in mouse peritoneal macrophages (1997) J Immunol, 159, pp. 3490-3497; Ishida, H., Hastings, R., Kearney, J., Howard, M., Continuous anti-interleukin 10 antibody administration depletes mice of Ly-1 B cells but not conventional B cells (1992) J Exp Med, 175, pp. 1213-1220; Hoskins, J.D., Coronavirus infection in cats (1993) Vet Clin North Am Small Animal Pract, 23, pp. 1-16",,,"Australian Veterinary Association",00050423,,,"10561796","English","Austr. Vet. J.",Article,"Final",,Scopus,2-s2.0-0033195539
"Leutenegger C.M., Hofmann-Lehmann R., Riols C., Liberek M., Worel G., Lups P., Fehr D., Hartmann M., Weilenmann P., Lutz H.","7006706489;7003867023;6507990585;6506444196;6507237248;6602710661;7004257478;7201667570;6507175508;35480426400;","Viral infections in free-living populations of the European wildcat",1999,"Journal of Wildlife Diseases","35","4",,"678","686",,54,"10.7589/0090-3558-35.4.678","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033203611&doi=10.7589%2f0090-3558-35.4.678&partnerID=40&md5=55caad8744027563b130f1f57117bff5","Maison Forestière de Geleneau, Trois-Fontaines l'Abbaye, France; Wildcat Release Program, Bund für Naturschutz, Bavaria, Wiesenfelden, Germany; Naturhistorisches Museum, Bern, Switzerland; Zoological Garden, Zurich, Switzerland; Dept. of Medicine and Epidemiology, University of California, Davis, CA 95616, United States","Leutenegger, C.M., Dept. of Medicine and Epidemiology, University of California, Davis, CA 95616, United States; Hofmann-Lehmann, R.; Riols, C., Maison Forestière de Geleneau, Trois-Fontaines l'Abbaye, France; Liberek, M.; Worel, G., Wildcat Release Program, Bund für Naturschutz, Bavaria, Wiesenfelden, Germany; Lups, P., Naturhistorisches Museum, Bern, Switzerland; Fehr, D.; Hartmann, M.; Weilenmann, P., Zoological Garden, Zurich, Switzerland; Lutz, H.","While the importance of viral infections is well studied in domestic cats, only limited information is available on their occurence and prevalence in the European wildcat (Felis silvestris silvestris). The aim of this study was to determine the prevalence of antibodies to feline coronavirus (FCoV), calicivirus (FCV), herpesvirus (FHV), parvovirus (FPV), immunodeficiency virus (FIV), leukemia virus (FeLV), and FeLV antigenemia in 51 European wildcat sera. Samples were collected between 1996 and 1997 from wildcat populations in France, Switzerland, and Germany. Antibodies to FCoV were detected in two cats (4%) and FCoV RNA was detected in feces of one of these two cats. Antibodies to FCV, FHV and FPV were found at relatively low frequencies of 16%, 4%, and 2%, respectively. Antibodies to FIV were not detected. Although antigen and antibodies to FeLV were detected in 49%, and 75%, respectively, no evidence of FeLV-associated pathology was found. From the low prevalence of FCoV, FCV, FHV and FPV infections and from the fact that the European wildcats live solitarily, it was concluded that these viral infections do not spread readily within a population. Therefore, it may be assumed that release into the wild of European wildcats bred in captivity would not bring about a high risk of introducing of these viral infections to the free-ranging wildcats. As an exception, wildcats should be tested for absence of FIV infection before release if they were at risk to acquire this infection from domestic cats.","European wildcat; Feline calicivirus; Feline coronavirus; Feline herpesvirus; Feline immunodeficiency virus; Feline infectious peritonitis; Feline leukemia virus; Feline parvovirus; Felis silvestris silvestris; Serosurvey","Caliciviridae; Coronavirus; Felidae; Feline calicivirus; Feline coronavirus; Feline herpesvirus 1; Feline immunodeficiency virus; Feline leukemia virus; Feline parvovirus; Felis catus; Felis silvestris; Herpes; Herpesviridae; Parvovirus; virus antibody; animal; animal disease; article; blood; Carnivora; cat; cat disease; DNA virus; enzyme linked immunosorbent assay; epidemiology; fluorescent antibody technique; France; Germany; Herpes virus infection; immunology; pathogenicity; prevalence; reverse transcription polymerase chain reaction; RNA virus; RNA virus infection; Switzerland; virus infection; wild animal; Animals; Animals, Wild; Antibodies, Viral; Caliciviridae Infections; Carnivora; Cats; Coronavirus Infections; DNA Virus Infections; DNA Viruses; Enzyme-Linked Immunosorbent Assay; Feline Acquired Immunodeficiency Syndrome; Feline Panleukopenia; Fluorescent Antibody Technique, Indirect; France; Germany; Herpesviridae Infections; Prevalence; Reverse Transcriptase Polymerase Chain Reaction; RNA Virus Infections; RNA Viruses; Seroepidemiologic Studies; Switzerland","Addie, D.D., Jarrett, O., A study of naturally occuring feline coronavirus infections in kittens (1992) Veterinary Record, 130, pp. 133-137; Artois, M., Remond, M., Viral diseases as a threat to free-living wildcats (Felis silvestris) in continental Europe (1994) Veterinary Record, 134, pp. 651-652; Barr, M., Zou, L., Holzschu, D.L., Phillips, L., Scott, F.W., Casey, J.W., Avert, R.J., Isolation of a highly cytopathic lentivirus from a nondomestic cat (1995) Journal of Virology, 69, pp. 7371-7374; Bazin, R., Boucher, G., Monier, G., Chevrieh, M.C., Verrette, S., Broly, H., Lemieux, R., Use of hu-IgG-SCID mice to evaluate the in vivo stability of human monoclonal IgG antibodies (1994) Journal of Immunological Methods, 172, pp. 209-217; Boid, R., McOrist, S., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Isolation of FeLV from a wild felid (Felis silvestris) (1991) Veterinary Record, 128, p. 256; Brown, E.W., Yuhki, N., Packer, C., O'Brien, S.J., A lion lentivirus related to feline immunodeficiency virus: Epidemiologic and phylogenetic aspects (1994) Journal of Virology, 68, pp. 5953-5968; Büttner, K.B., 10 jahre wiedereinbürgerung der europäischen wildkatze felis silvestris silvestris schreber 1777 in Bayern (1984-1993) (1994) Waldhygiene, 20, pp. 137-145; Calzolari, M., Young, E., Cox, D., Dams, D., Lutz, H., Serological diagnosis of feline immunodeficiency virus infection using recombinant transmembrane glycoprotein (1995) Veterinary Immunology and Immunopathology, 46, pp. 83-92; Carpenter, M.A., O'Brien, S.J., Co-adaptation and immunodeficiency virus: Lessons from the felidae (1995) Current Opinion in Genetics & Development, 5, pp. 739-745; Citino, S.B., Transient FeLV viremia in a clouded leopard (1986) Journal of Zoo and Animal Medicine, 15, p. 5; Colby, E.D., Low, R.J., Feline infectious peritonitis (1970) Veterinary Medicine, Small Animal Clinician, 65, pp. 783-786; Daniels, M.J., Golder, M.C., Jahrett, O., MacDonald, D.W., Feline viruses in wildcats from Scotland (1999) Journal of Wildlife Diseases, 35, pp. 121-124; Evermann, J.F., Burns, G., Roelke, M.E., McKeirnan, A.J., Greenlee, A., Ward, A.C., Pfeifer, M.L., Diagnostic features of an epizootic of feline infections peritonitis in captive cheetahs (1983) American Association of Veterinary Laboratory Diagnosis, 26, pp. 365-382; Fehr, D., Bolla, S., Herrewegh, A.A., Horzinek, M.C., Lutz, H., Detection of feline coronavirus using RT-PCR: Basis for the study of the pathogenesis of feline infectious peritonitis (FIP) (1996) Schweizer Archiv für Tierheilkunde, 138, pp. 74-79; Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A., Horzinek, M.C., Lutz, H., Placebo-controlled evaluation of a modified life virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions (1997) Vaccine, 15, pp. 1101-1109; Goldsmith, E.I., The convention on international trade in endangered species of wild fauna and flora (1978) Journal of Medical Primatology, 7, pp. 122-124; Hofmann-Lehmann, R., Fehr, D., Grob, M., Elgizoli, M., Packer, C., Martenson, J.S., O'Brien, S.J., Lutz, H., Prevalence of antibodies to feline parvovirus, calicivirus, herpesvirus, coronavirus, and immunodeficiency virus and of feline leukemia virus antigen and the interrelationship of these viral infections in free-ranging lions in east Africa (1996) Clinical and Diagnostic Laboratory Immunology, 3, pp. 554-562; Herrewegh, A.A., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) Journal of Clinical Microbiology, 33, pp. 684-689; Jarrett, W.F.H., Crawford, E.M., Martin, W.B., A virus-like particle associated with leukemia (lymphosarcoma) (1964) Nature, 202, pp. 567-569; Jessup, D.A., Pettan, K.C., Lowenstine, L.J., Pedersen, N.C., Feline leukemia virus infection and renal spirochetosis in free-ranging cougar (Felis concolor) (1993) Journal of Zoo and Wildlife Medicine, 24, pp. 73-79; Lutz, H., Pedersen, N.C., Higgins, J., Hübscher, U., Troy, T.A., Theilen, G.H., Humoral immune reactivity to feline leukemia virus and associated antigens in cats naturally infected with feline leukemia virus (1980) Cancer Research, 40, pp. 3642-3651; Pedersen, N.C., Durbin, R., Theilen, G.H., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) Journal of Immunological Methods, 56, pp. 209-220; Hauser, B., Horzinek, M.C., Feline infectious peritonitis (1985) Tijdschrift Voor Diergeneeskunde, 110, pp. 939-946; Arnold, P., Hübscher, U., Egberink, H., Pedersen, N., Horzinek, M.C., Specificity assessment of feline T-lymphotropic lentivirus serology (1988) Zentralblatt für Veterinärmedizin - Reihe B, 35, pp. 773-778; Isenbugel, E., Lehmann, R., Sabapara, R.H., Wolfensberger, C., Retrovirus infections in non-domestic felids: Serological studies and attempts to isolate a lentivirus (1992) Veterinary Immunology and Immunopathology, 35, pp. 215-224; Hofmann-Lehmann, R., Fehr, D., Leutenegger, C., Hartmann, M., Ossent, P., Grob, M., Elgizoli, M., Weilemmann, P., Liberation into the wild of wild felines -danger of the release of virus infections (1996) Schweizer Archiv für Tierheilkunde, 138, pp. 579-585; McOrist, S., Diseases of the European wildcat (Felis silvestris Schreber, 1777) in Great Britain (1992) Revue Scientifique et Technique, 11, pp. 1143-1149; Boid, R., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Some viral and protozool diseases in the European wildcat (Felis silvestris) (1991) Journal of Wildlife Diseases, 27, pp. 693-696; Meric, S.M., Suspected feline leukemia virus infection and pancytopenia in a western cougar (1984) Journal of the American Veterinary Medical Association, 185, pp. 1390-1391; Olmsted, R.A., Langley, R., Roelke, M.E., Goeken, R.M., Adger-Johnson, D., Goff, J.P., Albert, J.P., O'Brien, S.J., Worldwide prevalence of lentivirus infection in wild feline species: Epidemiologic and phylogenetic aspects (1992) Journal of Virology, 66, pp. 6008-6018; Osterhaus, A.D., Horzinek, M.C., Reynolds, D.J., Seroepidemiology of feline infectious peritonitis virus infections using transmissible gastroenteritis virus as antigen (1977) Zentralblatt für Veterinärmedizin - Reihe B, 24, pp. 835-841; Parent, G.H., La migration récente, a carastère invasionell, du chat sauvage, Felis silvestris lorraine belge (1975) Mammalia, 39, pp. 251-288; Paul-Murphy, J., Work, T., Hunter, D., McFie, E., Fjelline, D., Serologic survey and serum biochemical reference ranges of the free-ranging mountain lion (Felis concolor) in California (1994) Journal of Wildlife Diseases, 30, pp. 205-215; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) American Journal of Veterinary Research, 37, pp. 1449-1453; Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Advances in Experimental Medicine & Biology, 218, pp. 529-550; Piechocki, R., Ausbreitung, verluste, gewichte und masse der wildkatze, Felis silvestris schreber 1777, in der DDR (1986) Hercynia N.F., 23, pp. 125-147; Quensberry, K.E., Infectious diseases of nondomestic cats (1984) Veterinary Clinics of North America - Small Animal Practice, 14, pp. 1089-1106; Rasheed, S., Gardner, M.B., Isolation of feline leukemia virus from a leopard cat cell line and search for retrovirus in wild felidae (1981) Journal of the National Cancer Institute, 67, pp. 929-933; Schauenbehg, P., La stature du chat forestier Felis silvestris Schreber, et la variabilité morphologique de l'espèce (1977) Revue Suisse de Zoologie, 84, pp. 323-337; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., Coronavirus serology in healthy pedigree cats (1992) Veterinary Record, 131, pp. 35-36; Spencer, J.A., Survey of antibodies fo feline viruses in free-ranging lions (1991) South-African Journal of Wildlife Research, 21, pp. 59-61; Van Rensburg, I.B., Silkstone, M.A., Concomitant feline infectious peritonitis and toxoplasmosis in a cheetah (Acinonyx jubatus) (1984) Journal of South African Veterinary Association, 55, pp. 205-207; Watt, N.J., Macintyre, N.J., McOrist, S., An extended outbreak of infectious peritonitis in a closed colony of European wildcats (Felts silvestris) (1993) Journal of Comparative Pathology, 108, pp. 73-79","Leutenegger, C.M.; Dept. of Medicine and Epidemiology, University of California, Davis, CA 95616, United States; email: cmleutenegger@ucdavis.edu",,"Wildlife Disease Association, Inc.",00903558,,,"10574526","English","J. Wildl. Dis.",Article,"Final",,Scopus,2-s2.0-0033203611
"Langella P., Le Loir Y.","7003598187;6701812079;","Heterologous protein secretion in Lactococcus lactis: A novel antigen delivery system",1999,"Brazilian Journal of Medical and Biological Research","32","2",,"191","198",,38,"10.1590/S0100-879X1999000200007","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033071721&doi=10.1590%2fS0100-879X1999000200007&partnerID=40&md5=eaa37986f2a560ce1882d86b7f864d75","Lab. de Genet. Appliquée, U. Rech. Laitieres de Genet. Appl., Inst. Natl. de la Rech. Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France","Langella, P., Lab. de Genet. Appliquée, U. Rech. Laitieres de Genet. Appl., Inst. Natl. de la Rech. Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France; Le Loir, Y.","Lactic acid bacteria (LAB) are Gram-positive bacteria and are generally regarded as safe (GRAS) organisms. Therefore, LAB could be used for heterologous protein secretion and they are good potential candidates as antigen delivery vehicles. To develop such live vaccines, a better control of protein secretion is required. We developed an efficient secretion system in the model LAB, Lactococcus lactis. Staphylococcal nuclease (Nuc) was used as the reporter protein. We first observed that the quantity of secreted Nuc correlated with the copy number of the cloning vector. The nuc gene was cloned on a high-copy number cloning vector and no perturbation of the metabolism of the secreting strain was observed. Replacement of nuc native promoter by a strong lactococcal one led to a significant increase of nuc expression. Secretion efficiency (SE) of Nuc in L. lactis was low, i.e., only 60% of the synthesized Nuc was secreted. Insertion of a synthetic propeptide between the signal peptide and the mature moiety of Nuc increased the SE of Nuc. On the basis of these results, we developed a secretion system and we applied it to the construction of an L. lactis strain which secretes a bovine coronavirus (BCV) epitope-protein fusion (BCV-Nuc). BCV-Nuc was recognized by both anti-BCV and anti-Nuc antibodies. Secretion of this antigenic fusion is the first step towards the development of a novel antigen delivery system based on LAB-secreting strains.","Bovine coronavirus; Epitope; Lactococcus lactis; Propeptide; Protein secretion; Staphylococcal nuclease","Bovinae; Bovine coronavirus; Coronavirus; Lactococcus lactis; Posibacteria; antigen; bacterial protein; epitope; micrococcal nuclease; Coronavirus; Lactococcus lactis; metabolism; review; secretion; Antigens; Bacterial Proteins; Coronavirus, Bovine; Epitopes; Lactococcus lactis; Micrococcal Nuclease","De Vos, W.M., Simons, G.F.M., Gene cloning and expression in Lactococci (1994) Genetics and Biotechnology of Lactic Acid Bacteria, pp. 52-105. , Gasson MJ & de Vos WM (Editors), Chapman and Hall, London; Le Loir, Y., Gruss, A., Ehrlich, S.D., Langella, P., A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis (1998) Journal of Bacteriology, 180, pp. 1895-1903; Piard, J.C., Hautefort, I., Fischetti, V.A., Ehrlich, S.D., Fons, M., Gruss, A., Cell-wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria (1997) Journal of Bacteriology, 179, pp. 3068-3072; Poquet, I., Ehrlich, S.D., Gruss, A., An export-specific reporter designed for gram-positive bacteria: Application to Lactococcus lactis (1997) Journal of Bacteriology, 180, pp. 1904-1912; Van Asseldonk, M., Rutten, G., Oteman, M., Siezen, R.J., De Vos, W.M., Simons, G., Cloning, expression in Escherichia coli and characterization of usp45, a gene encoding a highly secreted protein from Lactococcus lactis MG1363 (1990) Gene, 95, pp. 155-160; Shortle, D., A genetic system analysis of staphylococcal nuclease (1983) Gene, 22, pp. 181-189; Lachica, R.V.F., Genigeorgis, C., Hoeprich, P.D., Metachromatic agar-diffusion methods for detecting staphylococcal nuclease activity (1971) Applied Microbiology, 21, pp. 585-587; Liebl, W., Sinskey, A.J., Schleifer, K.H., Expression, secretion, and processing of staphylococcal nuclease by Corynebacterium glutamicum (1992) Journal of Bacteriology, 174, pp. 1854-1861; Piard, J.C., Jimenez-Diaz, R., Ehrlich, S.D., Fischetti, V.A., Gruss, A., The M6 protein of Streptococcus pyogenes and its potential as a tool to anchor biologically active molecules at the surface of lactic acid bacteria (1997) Streptococci and the Host, pp. 545-550. , Horaud T (Editor), Plenum Press, New York; Makrides, S.C., Strategies for achieving high-level expression of genes in Escherichia coli (1996) Microbiological Reviews, 60, pp. 512-538; Simon, D., Chopin, A., Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis (1988) Biochimie, 70, pp. 559-567; Le Loir, Y., Gruss, A., Ehrlich, S.D., Langella, P., Direct screening of recombinants in Gram-positive bacteria using the secreted staphylococcal nuclease as a reporter (1994) Journal of Bacteriology, 176, pp. 5135-5139; Miller, J.R., Kovacevic, S., Veal, L.E., Secretion and processing of staphylococcal nuclease by Bacillus subtilis (1987) Journal of Bacteriology, 169, pp. 3508-3514; Davis, A., Moore, I.B., Parker, D.S., Taniuchi, H., Nuclease B: A possible precursor of nuclease A, an extracellular nuclease of Staphylococcus aureus (1977) Journal of Biological Chemistry, 252, pp. 6544-6553; Van Der Vossen, J.M.B.M., Van Der Lelie, D., Venema, G., Isolation and characterization of Streptococcus cremoris Wg-2 specific promoters (1987) Applied and Environmental Microbiology, 53, pp. 2452-2457; Simonen, M., Palva, I., Protein secretion in Bacillus species (1993) Microbiological Reviews, 57, pp. 109-137; Suciu, D., Inouye, M., The 19-residue propeptide of staphylococcal nuclease has a profound secretion-enhancing ability in Escherichia coli (1996) Molecular Microbiology, 21, pp. 181-195; Von Heijne, G., Net N-C charge imbalance may be important for signal sequence function in bacteria (1986) Journal of Molecular Biology, 192, pp. 287-290; Li, P.J., Beckwith, J., Inouye, H., Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli (1988) Proceedings of the National Academy of Sciences, USA, 85, pp. 7685-7689; Von Heijne, G., The signal peptide (1990) Journal of Membrane Biology, 115, pp. 195-201; Vautherot, J.F., Laporte, J., Boireau, P., Bovine coronavirus spike glycoprotein: Localization of an immunodominant region at the amino-terminal end of S2 (1992) Journal of General Virology, 73, pp. 3289-3294; Robinson, K., Chamberlain, L.M., Schofield, K.M., Wells, J.M., Le Page, R.W., Oral vaccination of mice against tetanus using recombinant Lactococcus lactis (1997) Nature Biotechnology, 15, pp. 653-657; Corthier, G., Delorme, C., Ehrlich, S.D., Renault, P., Use of luciferase genes as biosensors to study bacterial physiology in the digestive tract (1998) Applied and Environmental Microbiology, 64, pp. 2721-2725; Oliveira, S.C., Splitter, G.A., Immunization of mice with recombinant L7/L12 ribosomal protein confers protection against Brucella abortus infection (1996) Vaccine, 14, pp. 959-962","Langella, P.; Lab. de Genet. Appliquée, U. Rech. Laitieres de Genet. Appl., Inst. Natl. de la Rech. Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France; email: langella@biotec.jouy.inra.fr",,"Associacao Brasileira de Divulgacao Cientifica",0100879X,,RBPMB,"10347754","English","Braz. J. Med. Biol. Res.",Article,"Final",Open Access,Scopus,2-s2.0-0033071721
"Van Reeth K., Labarque G., Nauwynck H., Pensaert M.","57191565576;6602594644;7007141390;55905425400;","Differential production of proinflammatory cytokines in the pig lung during different respiratory virus infections: Correlations with pathogenicity",1999,"Research in Veterinary Science","67","1",,"47","52",,187,"10.1053/rvsc.1998.0277","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033175579&doi=10.1053%2frvsc.1998.0277&partnerID=40&md5=cb0b40505748437989ec7faa77df080c","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium","Van Reeth, K., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium; Labarque, G., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium; Nauwynck, H., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium","The acute stages of infection with swine influenza virus (SIV), porcine respiratory coronavirus (PRCV) and porcine reproductive-respiratory syndrome virus (PRRSV) were shown to differ in terms of clinical and lung inflammatory effects and proinflammatory cytokine profiles in bronchoalveolar lavage (BAL) fluids. Caesarian-derived colostrum-deprived pigs were inoculated intratracheally with one of the three viruses. SIV infection was followed within 1 day post inoculation (d PI) by characteristic respiratory and general signs, and excessive lung epithelial desquamation and neutrophil infiltration (38 to 56 per cent of BAL cells at 1 d PI vs 0 to 1 percent in controls). High concentrations of bioactive interferon-α (IFN-α), tumour necrosis factor-α (TNF-α) and interleukin-1 (IL-1) coincided with peak symptoms and neutrophil infiltration. PRCV infection was asymptomatic and produced a mild bronchointerstitial pneumonitis and neutrophil infiltration (13 to 22 percent of BAL cells at 4 d PI). IFN-α titres parallelled those found during SIV infection, TNF-α was negligible and IL-1 undetectable. PRRSV infection induced anorexia and lethargy between 3 and 5 d PI. There was marked infiltration with mononuclear cells in alveolar septa and BAL fluids between 7 and 10 d PI, while neutrophils remained at less than 11 per cent of BAL cells at any time. IL-1 was produced from three throughout 10 d PI, while IFN-α production was minimal and TNF-α undetectable. These data strongly suggest that proinflammatory cytokines can be important mediators of viral respiratory disease.",,"Coronavirus; Influenza virus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Simian immunodeficiency virus; Suidae; Sus scrofa; Swine influenza virus; cytokine; animal; animal disease; Arterivirus; article; biosynthesis; Coronavirus; Influenza virus A; lung; lung lavage; metabolism; Orthomyxovirus infection; pathogenicity; physiology; swine; swine disease; virology; virus infection; virus replication; Animals; Bronchoalveolar Lavage Fluid; Coronavirus; Coronavirus Infections; Cytokines; Influenza A virus; Lung; Orthomyxoviridae Infections; Porcine Reproductive and Respiratory Syndrome; Porcine respiratory and reproductive syndrome virus; Swine; Swine Diseases; Virus Replication","Albina, E., Carrat, C., Charley, B., Interferon-alpha response to swine arterivirus (PoAV), the porcine reproductive and respiratory syndrome virus (1998) Journal of Interferon and Cytokine Research, 18, pp. 485-490; Asai, T., Okado, M., Ono, M., Irisawa, T., Mori, Y., Yokimizo, Y., Sato, S., Increased levels of tumor necrosis factor and interleukin 1 in bronchoalveolar lavage fluids from pigs infected with Mycoplasma hyopneumoniae (1993) Veterinary Immunology and Immunopathology, 38, pp. 253-260; Baarsch, M.J., Scamurra, R.W., Burger, K., Foss, D.L., Maheswaran, S.K., Murtaugh, M.P., Inflammatory cytokine expression in swine experimentally infected with Actinobacillus pleuropneumoniae (1995) Infection and Immunity, 63, pp. 3587-3594; Bertoni, G., Kuhnert, P., Peterhans, E., Pauli, U., Improved bioassay for the detection of porcine tumor necrosis factor using a homologous cell line: PK (15) (1993) Journal of Immunological Methods, 160, pp. 267-271; Bielefeldt-Ohmann, H., Role of cytokines in the pathogenesis and treatment of respiratory disease (1995) Cytokines in Animal Health and Disease, pp. 291-332. , Myers MJ, Murtaugh MP eds. Marcel Dekker Inc., New York; Brown, I.H., Done, S.H., Spencer, Y.I., Cooley, W.A., Harris, P.A., Alexander, D.J., Pathogenicity of a swine influenza H1N1 virus antigenically distinguishable from classical and European strains (1993) The Veterinary Record, 132, pp. 598-602; Collins, J.E., Benfield, D.A., Christianson, W.T., Harris, L., Hennings, J.C., Shaw, D.P., Goyal, S.M., Chladek, D., Isolation of swine infertility and respiratory syndrome virus (isolate ATCC VR-2332) in north America and experimental reproduction of the disease in gnotobiotic pigs (1992) Journal of Veterinary Diagnostic Investigations, 4, pp. 117-126; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Research in Veterinary Science, 48, pp. 165-169; Duan, X., Nauwynck, H.J., Pensaert, M.B., Virus quantification and identification of cellular targets in the lungs and lymphoid tissues of pigs at different time intervals after inoculation with porcine reproductive and respiratory syndrome virus (PRRSV) (1997) Veterinary Microbiology, 56, pp. 9-19; Haesebrouck, F., Pensaert, M.B., Effect of intratracheal challenge of fattening pigs previously immunized with an inactivated influenza H1N1 vaccine (1986) Veterinary Microbiology, 11, pp. 239-249; Hayden, F.G., Fritz, R.S., Lobo, M.C., Alvord, W.G., Strober, W., Straus, S.E., Local and systemic cytokine responses during experimental human influenza A virus infection (1998) Journal of Clinical Investigations, 101, pp. 643-649; Hill, A.G., Siegel, J., Rounds, J., Wilmore, D.W., Metabolic responses to interleukin-1: Centrally and peripherally mediated (1997) Annals of Surgery, 225, pp. 246-251; Hopkins, S.J., Humphreys, M., Simple, sensitive and specific bioassay of interleukin-1 (1989) Journal of Immunological Methods, 120, pp. 271-276; Hopkins, S.J., Humphreys, M., Bioassay of interleukin-1 in serum and plasma following removal of inhibitory activity with polyethylene glycol (1990) Journal of Immunological Methods, 133, pp. 127-131; Hosang, K., Knoke, I., Klaudiny, J., Wempe, F., Wuttke, W., Scheit, K.H., Porcine luteal cells express monocyte chemoattractant protein-1 (MCP-1): Analysis by polymerase chain reaction and cDNA cloning (1994) Biochemical and Biophysical Research Communications, 199, pp. 962-968; Hosang, K., Knoke, I., Klaudiny, J., Wempe, F., Wuttke, W., Scheit, K.H., Porcine luteal cells express monocyte chemoattractant protein-2 (MCP-2): Analysis by cDNA cloning and Nothern analysis (1994) Biochemical and Biophysical Research Communications, 205, pp. 148-153; La Bonnardiere, C., Laude, H., High interferon titer in newborn pig intestine during experimentally induced viral enteritis (1981) Infection and Immunity, 32, pp. 28-31; Murtaugh, M.P., Baarsch, M.J., Zhou, Y., Scamurra, R.W., Lin, G., Inflammatory cytokines in animal health and disease (1996) Veterinary Immunology and Immunopathology, 54, pp. 45-55; Nain, M., Hinder, F., Gong, J.-H., Schmidt, A., Bender, A., Sprenger, H., Gemsa, D., Tumor necrosis factor-α production of influenza A virus-infected macrophages and potentiating effect of lipopolysaccharides (1990) Journal of Immunology, 145, pp. 1921-1928; Nielsen, J., Botner, A., Hematological and immunological parameters of 4 1/2-month old pigs infected with PRRS (1997) Veterinary Microbiology, 55, pp. 289-294; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with pneumotropic porcine coronavirus (1989) Research in Veterinary Science, 47, pp. 23-29; Pahl, H.L., Baeuerle, P.A., Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B (1995) Journal of Virology, 69, pp. 1480-1484; Paton, D.J., Brown, I.H., Scott, A.C., Done, S.H., Edwards, S., Isolation of a Lelystad virus-like agent from British pigs and scanning electron microscopy of infected macrophages (1992) Veterinary Microbiology, 33, pp. 195-201; Shibata, I., Mori, M., Uruno, K., Samegai, Y., Okado, M., In vivo replication of porcine reproductive and respiratory syndrome virus in swine alveolar macrophages and change in the cell population in bronchoalveolar lavage fluid after infection (1997) Journal of Veterinary Medical Science, 59, pp. 539-543; Tizard, I.R., Interferons (1995) Cytokines in Animal Health and Disease, pp. 1-59. , Myers MJ, Murtaugh MP eds; Vacheron, F., Rudent, A., Perin, S., Labarre, C., Quero, A.M., Guenounou, M., Production of interleukin-1 and tumour necrosis factor activities in bronchoalveolar washings following infection of mice by influenza virus (1990) Journal of General Virology, 71, pp. 477-479; Van Reeth, K., Nauwynck, H., Pensaert, M., Bronchoalveolar interferon-α, tumor necrosis factor-α, interleukin-1 and inflammation during acute influenza in pigs: A possible model for man? (1998) Journal of Infectious Diseases, 177, pp. 1076-1079; Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) American Journal of Veterinary Research, 55, pp. 1275-1281; Van Reeth, K., Pensaert, M., Production of interferon-α, tumor necrosis factor-α and interleukin-1 in the lungs of pigs infected with the porcine respiratory coronavirus (1995) Proc. 3 Rd Congress Europ. Soc. Vet. Virol., pp. 197-201. , Inlerlaken, Switzerland; Wyde, P.R., Wilson, M.R., Cate, T.R., Interferon production by leukocytes infiltrating the lungs of mice during primary influenza virus infection (1982) Infection and Immunity, 11, pp. 239-249; Zhou, Y., Barghusen, S., Choi, C., Rossow, K., Collins, J., Laber, J., Molitor, T., Murtaugh, M., Effect of SIRS virus infection in leukocyte populations in the peripheral blood and on cytokine expression in alveolar macrophages of growing pigs (1992) American Association of Swine Practioners Newsletter, 4, p. 28. , (Int. PRRS Symp. Ed.); Zoja, C., Wang, J.M., Bettoni, S., Sironi, M., Renzi, D., Chiaffarino, F., Abboud, H.E., Remuzzi, G., Interleukin-1 beta and tumor necrosis factor-alpha induce gene expression and production of leucocyte chemotactic factors, colony-stimulating factors, and interleukin-6 in human mesengial cells (1991) American Journal of Pathology, 138, pp. 991-1003","Van Reeth, K.; Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Gent, Salisburglaan, B-9820 Merelbeke, Belgium",,"Elsevier",00345288,,RVTSA,"10425240","English","Res. Vet. Sci.",Article,"Final",,Scopus,2-s2.0-0033175579
"Wang X., Khan M.I.","57192623988;7410319767;","A multiplex PCR for Massachusetts and Arkansas serotypes of infectious bronchitis virus",1999,"Molecular and Cellular Probes","13","1",,"1","7",,10,"10.1006/mcpr.1998.0204","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033083454&doi=10.1006%2fmcpr.1998.0204&partnerID=40&md5=e920d83c225c72382b4daaf1da37b282","Department of Pathobiology, University of Connecticut, U-89, 61 North Eagleville Road, Storrs, CT 06269-3089, United States","Wang, X., Department of Pathobiology, University of Connecticut, U-89, 61 North Eagleville Road, Storrs, CT 06269-3089, United States; Khan, M.I., Department of Pathobiology, University of Connecticut, U-89, 61 North Eagleville Road, Storrs, CT 06269-3089, United States","Infectious bronchitis virus (IBV), the prototype of the coronavirus family, is an enveloped, single-stranded RNA virus with a genome size of approximately 27.6 kilobase. Infectious bronchitis virus causes an acute, highly contagious respiratory and urogenital disease of chickens which results in significant economic losses in commercial broilers, layers and breeders. A rapid, highly sensitive and specific method is needed in the differential diagnosis of infections of different serotypes. A multiplex polymerase chain reaction (PCR) method was developed and optimized to simultaneously detect Massachusetts (Mass) and Arkansas (Ark) serotypes of IBV. One common primer and two serotype specific primers were chosen from the S1 gene sequences of IBV and used in one PCR reaction. Under optimized PCR conditions, two serotype specific PCR products, 1026 bp for Mass and 896 bp for Ark, respectively, were amplified and detected by agarose gel electrophoreses. The specificity of the technique was verified by using 20 different strains and isolates of IBV, and other avian bacterial and viral pathogens. Using a serial 10-fold dilution of the artificial mixture of both Mass and Ark samples, the detection limit was found to be 5 pg RNA after 35 cycles of PCR. The multiplex PCR was able to detect and differentiate both serotypes in embryonated eggs that were co-infected with different EID50 virus titers of Mass 41 and Ark 99. The multiplex PCR developed in this study will be valuable for rapid identification, differential diagnosis, and epidemiological studies of these two serotypes of IBV infections.","Infectious bronchitis virus (IBV); Multiplex PCR; Primers; Serotype differentiation","primer DNA; animal disease; article; bronchitis; controlled study; Coronavirus; differential diagnosis; gel electrophoresis; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; serotype; virus characterization; Animalia; Aves; Avian infectious bronchitis virus; Bacteria (microorganisms); Coronavirus; Gallus gallus; RNA viruses","Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 90-93. , (Siddell, S. G., ed.) New York, USA: Plenum Press; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry, 10th Edition, pp. 511-526. , (Calnek, B. W., ed.) Ames, Iowa, USA: Iowa State University Press; Cook, J.K.A., Huggins, M.B., Newly isolated serotypes of infectious bronchitis virus: Their role in disease (1986) Avian Pathology, 15, pp. 129-138; Gelb J., Jr., Wolff, J.B., Moron, C.A., Variant serotypes of IBV isolated from commercial layers and broiler chickens (1991) Avian Diseases, 35, pp. 82-87; Gelb J., Jr., Infectious bronchitis (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 3rd Edition, , (Purchase, H. G., Arp, C. H. & Pearson, J. E., eds). American Association Avian Pathologists; Gelb J., Jr., Killian, S.L., Serum antibody responses of chickens following sequential inoculations with infectious bronchitis virus serotypes (1987) Avian Diseases, 31, pp. 513-522; Karaca, K., Naqi, S., Gelb J., Jr., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Diseases, 36, pp. 903-915; Anderson, J.R., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Diseases, 35, pp. 216-220; Kwon, H.M., Jackwood, M.W., Gelb J., Jr., Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Disease, 37, pp. 194-202; Lin, Z., Kato, A., Kudou, Y., Ueda, S., A new typing method for the avian infectious bronchitis virus using polymerase chain reaction and restriction fragment length polymorphism (1991) Archive of Virology, 116, pp. 19-31; Keeler, C.L.J., Reed, K.L., Nix, W.A., Gelb J., Jr., Serotype identification of avian infectious bronchitis virus by RT-PCR of the peplomer(S-1) gene (1998) Avian Diseases, 42, pp. 275-284; Way, J.S., Josephson, K.L., Pillai, S.D., Abbaszadegan, M., Gerba, C.P., Pepper L. II, Specific detection of Salmonella spp. By multiplex polymerase chain reaction (1993) Applied and Environmental Microbiology, 59, pp. 1473-1479; Lawrence, L.M., Gilmour, A., Incidence of Listeria spp. and Listeria monocytogenes in a poultry processing environment and in poultry products and their confirmation by multiplex PCR (1994) Applied and Environmental Microbiology, 60, pp. 4600-4604; Kulski, J.K., Khinsoe, C., Pryce, T., Christiansen, K., Use of multiplex PCR to detect and identify Mycobacterium avium and M. intercellulare in blood culture fluids of AIDS patients (1995) Journal of Clinical Microbiology, 33, pp. 668-674; Wang, H., Fadl, A.A., Khan, M.I., Multiplex PCR for avian pathogenic mycoplasmas (1997) Molecular and Cellular Probes, 11, pp. 211-216; Karlsen, F., Kalantari, M., Jenkins, A., Petersen, E., Kristensen, G., Holm, R., Johansson, B., Hagmar, B., Use of multiplex PCR primer sets for optimal detection of human papillomavirus (1996) Journal of Clinical Microbiology, 34, pp. 2095-2100; Van Der Heide, L., Kalbac, M., Brustolon, M., Lawson, M.G., Pathogenicity for chickens of a reovirus isolated from turkeys (1980) Avian Disease, 24, pp. 989-997; Frey, M.L., Hanson, R.P., Anderson, D.P., A medium for the isolation of avian mycoplasmas (1968) American Journal of Veterinary Research, 29, pp. 2163-2171; Chomezynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analytic Biochemistry, 162, pp. 156-159; Niester, H.G., Lenstra, J.A., Spaan, W.J., The peplomer protein sequence of the M 41 strain of coronavirus IBV and its comparison with Beaudette strains (1986) Virus Research, 5, pp. 253-263; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Kwon, H.M., Jackwood, M.W., Molecular cloning and sequence comparison of the S1 glycoprotein of the Gray and JMK strains of avian infectious bronchitis virus (1995) Virus Genes, 9, pp. 219-229; Wang, L., Junker, D., Hock, L., Ebiary, E., Collisson, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Research, 34, pp. 327-338; Binns, M.M., Boursnell, M.E., Tomley, F.M., Brown, D.K., Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) Journal of General Virology, 67, pp. 2825-2831; Wang, L., Yuan, X., Collisson, E.W., Experimental confirmation of recombination upstream of S1 hypervariable region of IBV (1997) Virus Research, 49, pp. 139-145; Altschul, S.F., Gish, W., Miller, E., Lipman, D., Basic local alignment search tool (1990) Journal of Molecular Biology, 215, pp. 403-410; Reed, E.J., Muench, H., A simple method for estimating fifty percent end points (1938) American Journal of Hygiene, 27, pp. 493-497; Kwok, S., Kellogg, D.E., McKinney, N., Spasic, D., Goda, L., Levenson, C., Sninsky, J.J., Effects of primer-template mismatches on the polymerase chain reaction: Human immunodeficiency virus type 1 model studies (1990) Nucleic Acid Research, 18, pp. 999-1005; Warren, W.M., Snyder, D.B., Epidemiology of infectious bronchitis in the United States (1991) International Symposium on Infectious Bronchitis, pp. 53-57. , Rauishholzhausen, Germany","Khan, M.I.; Department of Pathobiology, University of Connecticut, U-89, 61 North Eagleville Road, Storrs, CT 06269-3089, United States; email: mkhan@canr1.cag.uconn.edu",,"Academic Press",08908508,,MCPRE,"10024427","English","Mol. Cell. Probes",Article,"Final",,Scopus,2-s2.0-0033083454
"Bendali F., Bichet H., Schelcher F., Sanaa M.","6602415971;6602968267;7006601789;55907687000;","Pattern of diarrhoea in newborn beef calves in south-west France",1999,"Veterinary Research","30","1",,"61","74",,47,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032610229&partnerID=40&md5=7d26ed9d655c417f912a04b4333a600d","Lab. d'Epidemiol. et de Gestion D., Ecl. Natl. Veterinaire D'alfort, 7, avenue du General de Gaulle, 94704 Maisons-Alfort cedex, France; Reseau d'Epidemiosurveillance VEGA, rue de las Escoumes, Foix Cedex, France; Pathol. Reproduction des Ruminants, Ecl. Natl. Veterinaire de Toulouse, URA Inra, 23, chemin des capelles, 31076 Toulouse Cedex, France","Bendali, F., Lab. d'Epidemiol. et de Gestion D., Ecl. Natl. Veterinaire D'alfort, 7, avenue du General de Gaulle, 94704 Maisons-Alfort cedex, France; Bichet, H., Reseau d'Epidemiosurveillance VEGA, rue de las Escoumes, Foix Cedex, France; Schelcher, F., Pathol. Reproduction des Ruminants, Ecl. Natl. Veterinaire de Toulouse, URA Inra, 23, chemin des capelles, 31076 Toulouse Cedex, France; Sanaa, M.","A prospective study was carried out on 94 randomly selected beef herds in the Midi-Pyrénées region in France. The objective was to describe diarrhoea and mortality in beef calves from birth to 30 days of age. Calves (3080) were followed from December 1995 to April 1996, and a total of 700 visits allowed records of herd management practices, individual data and environmental conditions to be collected. The incidence rate for diarrhoea during the neonatal period was 14.6 %, and varied markedly between herds. Eighteen herds did not suffer from diarrhoea, while five herds had an incidence of more than 50% Results indicate that 52 % of diarrhoea appears during the first week and only 15% after the second week of life. The greatest risk of diarrhoea for a calf was during the first and second weeks of life (7.9 and 6.5 times, respectively). The month of birth was also significantly associated with morbidity, the highest incidence was observed in December and March (17.6 and 23.6%, respectively). Escherichia coli was isolated from 20.3% of faecal samples and appeared earlier during the first days of life Rotavirus was frequently isolated (47.4%) from samples. Coronavirus was positive for only 16.5% but was significantly associated with diarrhoea. Cryptosporidium was less frequent (15.6%) The global mortality rate was 3.6 % and was two-times higher in December than in other months. Forty per cent of herds did not exhibit mortality, and 10% had mortality rates greater than 10%. This study confirms previously reported data, and with greater precision and details on diarrhoea and mortality incidences among herds, age and month of birth in suckling beef calves. ©Inra/Elsevier, Paris.","Beef calf; Diarrhoea; Epidemiology; Mortality","Coronavirus; Cryptosporidium; Escherichia coli; Rotavirus; animal; animal disease; article; cattle; cattle disease; cryptosporidiosis; diarrhea; Enterobacter infection; France; incidence; meat; mortality; newborn; prospective study; risk factor; standard; Animals; Animals, Newborn; Cattle; Cattle Diseases; Cryptosporidiosis; Diarrhea; Escherichia coli Infections; France; Incidence; Meat; Prospective Studies; Risk Factors","Acres, S., Enterotoxigenic escherichia coli infections in newborn calves: A review (1985) J. Dairy Sci., 68, pp. 229-256; Bichet, H., L'activité vétérinaire passée au peigne fin, réseau VEGA (1994) Revue d'Épidémiosurveillance Animale, 7, pp. 4-14; Bonal, C., Moussa, A., Les entérites néonatales virales du veau (1993) Le Point Vétérinaire, 25, pp. 33-38; Bruning-Fann, C., Kaneene, J.B., Environmental and management risk factors associated with morbidity and mortality in perinatal and pre-weaning calves: A review from an epidemiological perspective (1992) Vet. Bull., 62, pp. 399-413; Busato, A., Steiner, L., Martin, S.W., Shoukri, M.M., Gaillard, C., Calf health in cow-calf herds in Switzerland (1997) Prev. Vet. Med., 30, pp. 9-22; Clement, J.C., King, M.E., Salman, M.D., Wittum, T.E., Casper, H.H., Odde, K.G., Use of epidemio-logic principles to identify risk factors associated with the development of diarrhoea in calves in five beef herd (1995) J. Am. Vet. Med. Assoc., 207, pp. 1334-1338; Combeau, H., Résultats du contrôle des performances bovins allaitants (1996) Compte Rendu Annuels, 2610, pp. 5-47. , Institut de l'élevage bovin; Curtis, C.R., Erb, H.N., White, M.E., Descriptive epidemiology of calfhood morbidity and mortality in New York Holstein herds (1988) Prev. Vet. Med., 5, pp. 293-307; Debnath, N.C., Sil, B.K., Selim, S.A., Prodhan, M.A.M., Howlader, M.M.R., A retrospective study of calf mortality and morbidity on smalholder traditional farms in Bangladesh (1990) Prev. Vet. Med., 9, pp. 1-7; Derycke, J., Bernard, S., Laporte, J., Naciri, M., Popof, M.R., Rodolakis, A., Prevalence of various enteropathogens in the feces of diarrheic and healthy calves (1986) Ann. Rech. Vét., 17, pp. 159-168; Desjouis, G., Millet, A., Les gastro-entérites néonatales du veau (1989) La Dépêche Vétérinaire, 4, pp. 2-14; Fassi-Fehri, M.M., Johnson, D.W., Taoudi, A., Berrada, J., Épidémiologie des diarrhées à Escherichia coli et à rotavirus chez, le veau et l'agneau au Maroc (1988) Ann. Rech. Vet., 19, pp. 59-64; Fourichon, C., Seegers, H., Beaudeau, F., Élevage des veaux et risque de mortalité et de troubles de santé en exploitations laitiéres (1996) Rencontres Recherches Ruminants, 3, pp. 143-148; Franck, N.A., Kaneene, J.B., Management risk factors associated with calf diarrhoea in Michigan herds (1993) J. Dairy Sci., 76, pp. 1313-1323; Gouet, P., The etiology, pathology and epidemiology of gastro-enteritis in calves and piglets (1983) Ann. Rech. Vet., 14, pp. 391-394; Martin, S.W., Schwabe, C.W., Franti, C.E., Dairy calf mortality rate: Characteristic of calf mortality rates in Tulare County, California (1975) Am. J. Vet. Res., 36, pp. 1099-1104; Quigley, J.D., Martin, K.R., Bemis, D.A., Potgieter, L.N.D., Reinemerger, C.R., Rohrbach, B.W., Dowlen, H.H., Lamar, K.C., Effects of housing and colostrum feeding on serum immunoglobulins, growth, and fecal scores of Jersey calves (1995) J. Dairy. Sci., 78, pp. 893-901; (1990) SAS/STAT User's Guide, Version 6, 4th Ed., , Carry, NC; Schumann, F.J., Townsend, H.G.G., Naylor, J.M., Risk factors for mortality from diarrhoea in beef calves in Alberta (1990) Can. J. Vet. Res., 54, pp. 336-372; Sivula, N.J., Ames, T.R., Marsh, W.E., Werdin, R.E., Descriptive epidemiology of morbidity and mortality in Minnesota dairy heifer calves (1996) Prev. Vet. Med., 27, pp. 155-171; Snodgrass, D.R., Evaluation of combined rotavirus and enterotoxigenic Escherichia coli vaccine in cattle (1986) Vet. Rec., 119, pp. 39-42; (1990) Sudaan User's Manual, Professional Software for Survey Data Analysis for Multistage Designs Release 6.0, , Research Inst., Research Triangle Park, NC; Vallet, A., Grenet, N., Gauthier, D., Influence des conditions d'élevage sur la fréquence des diarrhées de veau nouveau-nés et sur l'efficacité de leur traitement par voie orale (1985) Ann. Rech. Vét., 16, pp. 297-303; Waltner-Toews, D., Martin, S.W., Meek, A.H., Dairy calf management, morbidity and mortality in Ontario Holstein herds (1986) Prev. Vet. Med., 4, pp. 103-171; Wells, S.J., Dargatz, D.A., Ott, S.L., Factors associated with mortality to 21 days of life in dairy heifers in the United States (1996) Prev. Vet. Med., 29, pp. 9-19; Wells, S.J., Garber, L.P., Hill, G.W., Health status of preweaned dairy heifers in the United States (1996) Prev. Vet. Med., 29, pp. 185-199","Bendali, F.; Lab. d'Epidemiol. et de Gestion D., Ecl. Natl. Veterinaire D'alfort, 7, avenue du General de Gaulle, 94704 Maisons-Alfort cedex, France; email: bendali@vel-alfort.fr",,"EDP Sciences",09284249,,VEREE,"10081113","English","Vet. Res.",Article,"Final",,Scopus,2-s2.0-0032610229
"Thomas P.D., Pollok R., Gazzard B.G.","57207717677;6603865038;34874678500;","Enteric viral infections as a cause of diarrhoea in the acquired immunodeficiency syndrome",1999,"HIV Medicine","1","1",,"19","24",,41,"10.1046/j.1468-1293.1999.00004.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033206875&doi=10.1046%2fj.1468-1293.1999.00004.x&partnerID=40&md5=d7fdaabc0fa5cbd86e37f648cb3dee03","Department of HIV/GUM Medicine, Chelsea and Westminster Hospital, 369 Fiilham Road, London SW10 9NH, United Kingdom; St Bartholomew's and the Royal London School of Medicine and Dentistry, Digestive Diseases Research Centre, Turner Street, London El 2AD, United Kingdom","Thomas, P.D., Department of HIV/GUM Medicine, Chelsea and Westminster Hospital, 369 Fiilham Road, London SW10 9NH, United Kingdom, St Bartholomew's and the Royal London School of Medicine and Dentistry, Digestive Diseases Research Centre, Turner Street, London El 2AD, United Kingdom; Pollok, R., Department of HIV/GUM Medicine, Chelsea and Westminster Hospital, 369 Fiilham Road, London SW10 9NH, United Kingdom, St Bartholomew's and the Royal London School of Medicine and Dentistry, Digestive Diseases Research Centre, Turner Street, London El 2AD, United Kingdom; Gazzard, B.G., Department of HIV/GUM Medicine, Chelsea and Westminster Hospital, 369 Fiilham Road, London SW10 9NH, United Kingdom, St Bartholomew's and the Royal London School of Medicine and Dentistry, Digestive Diseases Research Centre, Turner Street, London El 2AD, United Kingdom","Background and aims The role of non-cytomegalovirus (CMV) enteric viral infection in causing diarrhoea in patients with human immunodeficiency virus (HIV) is poorly understood. We aimed to investigate the prevalence of these infections in acute and chronic diarrhoea. Methods Stool specimens from 377 HIV-infected patients presenting with diarrhoea were studied prospectively for evidence of non-CMV enteric viral infection. Patients with diarrhoea underwent investigation for gastrointestinal pathogens, including electron microscopic examination of stool for enteric viruses. We collected data on patients in whom enteric virus was identified and examined the association of enteric virus infection with diarrhoeal symptomatology. Results Eighty-nine (10.3°/o) stool specimens from 60 (15.9%) HIV+ individuals were positive for coronavirus (n=13, 22%), rotavirus (n=11, 18%), adenovirus (n = 30, 50%) and small round structured viruses (n = 5, 8%) or dual infection (n = 2, 3%). Thirty-four of 52 (65%) patients available for analysis had acute diarrhoea, and 18/52 (35%) had chronic diarrhoea. Twenty-three of 52 (44%) patients had a concurrent gut pathogen. After exclusion of concurrent pathogens enteric viral infections were found to be significantly associated with acute as opposed to chronic diarrhoea (P = 0.004). The presence of adenovirus colitis was significantly more likely to be associated with chronic diarrhoea (15/21 cases) than adenovirus isolated from stool alone (9/23 cases) (P=0.03). There was a trend towards an association between adenovirus colitis and colonie cytomegalovirus infection (P=0.06). Conclusion Enteric viral infection is strongly associated with acute diarrhoea in patients with HIV. Light microscopic examination of large bowel biopsies can identify adenovirus colitis which is significantly associated with chronic diarrhoea, and in addition may facilitate gastrointestinal coinfection with CMV. © 1999 British HIV Association.","Adenovirus, colitis, diarrhoea, electron microscopy, enteric virus, hiv","acute disease; adult; AIDS related complex; article; chronic disease; diarrhea; enteropathy; human; immunology; prevalence; prospective study; United Kingdom; virology; Acute Disease; Adult; AIDS-Related Opportunistic Infections; Chronic Disease; Diarrhea; Great Britain; HIV Enteropathy; Human; Middle Age; Prevalence; Prospective Studies","Smith, P.D., Lane, H.C., Gill, V.J., Intestinal infections in patients with the acquired immunodeficiency syndrome (AIDS); etiology and response to therapy (1988) Ann Intern Med, 108, pp. 328-333; Laughon, B.E., Drukman, D.A., Vernon, A., Prevalence of enteric pathogens in homosexual men with and without acquired immunodeficiency syndrome (1988) Gastroenterology, 94, pp. 984-993; Blanshard, C., Gazzard, B.G., Natural history and prognosis of diarrhoea of unknown cause in patients with acquired immunodeficiency syndrome (AIDS) (1991) Gut, 36, pp. 283-286; Batman, P.A., Aro, M., Sedgwick, P.M., Hiv, E.A., (1991) AIDS, 5, pp. 1247-1252; Budhraja, M.D., Levendoglu, H., Kocka, F., Duodenal mucosal T cell subpopulation and bacterial cultures in acquired immune deficiency syndrome (1987) Am J Gastroenterol, 82, pp. 427-431; Belitsos, P.C., Greenson, J.K., Yardley, J.H., Association of gastric hypoacidity with opportunistic infections inpatients with AIDS (1992) J Infect Dis, 166, pp. 277-284; Neson, J.A., Wiley, C.A., Reynolds-Kohler, C., Human immunodeficiency virus detected in the bowel epithelium from patients with gastrointestinal symptoms (1988) Lancet, 1, pp. 259-262; Blacklow, N.R., Cukor, G., Viral gastroenteritis (1981) N Engl J Med, 304, pp. 397-406; Dolin, R., Treanor, J.J., Madore, H.P., Novel agents of viral enteritis in humans (1987) J Infect Dis, 155, pp. 365-376; Saulsbury, F.T., Winkelstein, J.A., Yolken, R.H., Chronic rotavirus infection in immunodeficiency (1980) J Paediatr, 97, pp. 61-65; Yolken, R.H., Bishop, C.A., Townsend, T.R., Infectious gastroenteritis in bone marrow recipients (1982) N Eng J Med, 306, pp. 1009-1012; Hierholzer, J.C., Adenoviruses in the immunocompromised host (1992) Clin Microbiol Reviews, 5, pp. 262-274; Grohman, G.S., Glass, R.I., Pereira, H.G., Enteric viruses and diarrhoea in HIV infected patients (1993) N Engl J Med, 329, pp. 14-20; Cunningham, A.L., Grohman, G.S., Harkness, J., Gastrointestinal infections in men who were symptomatic and seropositive for human immunodeficiency virus (1988) J Infect Dis, 158, pp. 386-391; Kaljot, K.T., Ling, J.P., Jwm, G., Prevalence of Acute Enteric Viral Pathogens in Acquired Immunodeficiency Syndrome; Durepaire, N., Ranger-Rogez, S., Gandji, J.A., Enteric prevalence of adenovirus in human immunodeficiency virus seropositive patients (1995) JAfed Virol, 45, pp. 56-60; Thea, D.M., Glass, R., Grohman, O.S., Prevalence of enteric viruses amoung hospital patients with AIDS in Kinshasa (1993) Zaire Trans Roy Soc Trop Med Hygiene, 87, pp. 263-266; Schmidt, W., Schneider, Heise, W., Stool viruses, co-infection, and diarrhoea in HIV infected patients (1996) JAccquir Immune Defic Syndr Hum Retrovirol, 13 (1), pp. 33-38; Janoff, E.N., Orenstein, J.M., Manischewitz, J.F., Adenovirus colitis in the acquired immunodeficiency syndrome (1991) Gastroenterology, 100, pp. 976-979; Maddox, A., Francis, N., Moss, J., Blanshard, C., Gazzard, B., Adenovirus infection of the large bowel in HIV positive patients (1992) J Clin Path, 45, pp. 684-688; Blanshard, C., Francis, N., Gazzard, B.G., Investigation of chronic diarrhoea in acquired immunodeficiency syndrome (1996) A Prospective Study of 155 Patients. Gut, 39, pp. 824-832; Somekh, E., Berry, C.D., Ellison, R.T., Adenovirus isolation from the stools of HIV-infected patients (1991) Abstract of the XXXI Interscience Conference on Antimicrobial Agents and Chemotherapy, Chicago, Illinois, Pp. 190; Albrecht, H., Stellbrink, H.J., Fenske, S., Rotavirus antigen detection in patients with HIV infection and diarrhoea (1993) ScandJ Gastroenterol, 28, pp. 307-310; Dionisio, D., Arista, S., Vizzi, E., Chronic intestinal infection due to subgenus F type 40 adenovirus in patients with AIDS (1997) Scand J Infect Dis, 29, pp. 305-307; Crawford-Miksza, L., Schnurr, D.P., Seroepidemiology of new AlDS-associated adenoviruses among the San Francisco Men's Health Study (1996) JAfed Virol, 50, pp. 230-236; Parkin, J., Tyms, S., Roberts, A., Cytomegalovirus colitis (1987) Can It Be Caused by Adenovirus? III Int ConfAIDS, 1, p. 159; Wold, W.S., Hermiston, T.W., Tollefson, A.E., Adenovirus proteins that subvert host defences (1994) Trends Microbiol, 2 (11), pp. 437-443","Thomas, P.D.; Department of HIV/GUM Medicine, Chelsea and Westminster Hospital, 369 Fiilham Road, London SW10 9NH, United Kingdom",,"Blackwell Publishing Ltd.",14642662,,HMIEA,"11737325","English","HIV Med.",Article,"Final",,Scopus,2-s2.0-0033206875
"Rakes G.P., Arruda E., Ingram J.M., Hoover G.E., Zambrano J.C., Hayden F.G., Platts-Mills T.A.E., Heymann P.W.","6701487484;7004935664;7102464401;7004454691;7004252878;7103233446;7102024608;7005133665;","Rhinovirus and respiratory syncytial virus in wheezing children requiring emergency care: IgE and eosinophil analyses",1999,"American Journal of Respiratory and Critical Care Medicine","159","3",,"785","790",,358,"10.1164/ajrccm.159.3.9801052","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032985772&doi=10.1164%2fajrccm.159.3.9801052&partnerID=40&md5=42f6bc8da416e0a7e854ee0d7e1b0c7b","Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; MR-4 Building, Box 29, Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA 22908, United States","Rakes, G.P., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States, MR-4 Building, Box 29, Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA 22908, United States; Arruda, E., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Ingram, J.M., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Hoover, G.E., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Zambrano, J.C., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Hayden, F.G., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Platts-Mills, T.A.E., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States; Heymann, P.W., Dept. of Pediat., Int. Med.,/Pathol., Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA, United States","This cross-sectional emergency department study of 70 wheezing children and 59 control subjects (2 mo to 16 yr of age) examined the prevalence of respiratory viruses and their relationship to age, atopic status, and eosinophil markers. Nasal washes were cultured for respiratory viruses, assayed for respiratory syncytial virus (RSV) antigen, and tested for coronavirus and rhinovirus RNA using reverse transcription-PCR (RT-PCR). Also evaluated were eosinophil numbers and eosinophil cationic protein (ECP) in both nasal washes and serum, along with total IgE and specific IgE antibody in serum. Respiratory viruses were detected in 82% (18 of 22) of wheezing infants younger than 2 yr of age and in 83% (40 of 48) of older wheezing children. The predominant pathogens were RSV in infants (detected in 68% of wheezing subjects) and rhinovirus in older wheezing children (71%), and both were strongly associated with wheezing (p < 0.005). RSV was largely limited to wheezing children younger than 24 mo of age, but rhinovirus was detected by RT-PCR in 41% of all infants and in 35% of nonwheezing control subjects older than 2 yr of age. After 2 yr of age the strongest odds for wheezing were observed among those who had a positive RT-PCR test for rhinovirus together with a positive serum radioallergosorbent testing (RAST), nasal eosinophilia, or elevated nasal ECP (odds ratios = 17, 21, and 25, respectively). Results from this study demonstrate that a large majority of emergent wheezing illnesses during childhood (2 to 16 yr of age) can be linked to infection with rhinovirus, and that these wheezing attacks are most likely in those who have rhinovirus together with evidence of atopy or eosinophilic airway inflammation.",,"eosinophil cationic protein; immunoglobulin E; adolescent; airway resistance; antibody blood level; article; atopy; child; controlled study; disease marker; eosinophil; female; human; infant; inflammation; major clinical study; male; prevalence; priority journal; Respiratory syncytial pneumovirus; reverse transcription polymerase chain reaction; Rhinovirus; risk factor; treatment outcome; virus detection; virus infection; wheezing","Duff, A.L., Pomeranz, E.S., Gelber, L.E., Price, G.W., Farris, H., Hayden, F., Platts-Mills, T.A.E., Heymann, P.W., Risk factors for acute wheezing in infants and children: Viruses, passive smoke, and IgE antibodies to inhalant allergens (1993) Pediatrics, 92, pp. 535-540; Pattemore, P.K., Johnston, S.L., Bardin, P.G., Viruses as precipitants of asthma symptoms: I. Epidemiology (1992) Clin. Exp. Allergy, 22, pp. 325-336; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L., Symington, P., Holgate, S.T., A community study of the role of viral infections in exacerbations of asthma in 9-11 year old children (1995) B.M.J., 310, pp. 1225-1229; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) B.M.J., 307, pp. 982-986; Sporik, R., Holgate, S.T., Platts-Mills, T.A.E., Cogswell, J.J., Exposure to housedust mite allergen (Der p I ) and the development of asthma in childhood (1990) N. Engl. J. Med., 323, pp. 502-507; Squillace, S.P., Sporik, R.B., Rakes, G., Couture, N., Lawrence, A., Merriam, S., Zhang, J., Platts-Mills, T.A.E., Sensitization to dust mites as a dominant risk factor for asthma among adolescents living in Central Virginia (1997) Am. J. Respir. Crit. Care Med., 156, pp. 1760-1764; Freeman, G.L., The role of allergy in viral respiratory tract infections (1962) Am. J. Dis. Child., 104, pp. 44-48; Frick, O.L., Effect of respiratory and other virus infection on IgE immunoregulation (1986) J. Allergy Clin. Immunol., 78, pp. 1013-1018; Skoner, D.P., Doyle, W.J., Tanner, E.P., Kiss, J., Fireman, P., Effect of rhinovirus 39 (RV-39) infection on immune and inflammatory parameters in allergic and non-allergic subjects (1995) Clin. Exp. Allergy, 25, pp. 561-567; Lemanske R.F., Jr., Dick, E.C., Swenson, C.A., Vrtis, R.F., Busse, W.W., Rhinovirus upper respiratory infection increases airway hyperreactivity and late asthmatic reactions (1989) J. Clin. Invest., 83, pp. 1-10; Calhoun, W.J., Dick, E.C., Schwartz, L.B., Busse, W.W., A common cold virus, rhinovirus 16, potentiates airway inflammation after segmental antigen bronchoprovocation in allergic subjects (1994) J. Clin. Invest., 94, pp. 2220-2228; Fraekel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and asthmatic subjects (1995) Am. J. Respir. Crit. Care Med., 151, pp. 879-886; Garafalo, R., Kimpkin, J.L., Welliver, R.C., Ogra, P.L., Eosinophil degranulation in the respiratory tract during naturally acquired respiratory syncytial virus infection (1992) J. Pediatr., 120, pp. 28-32; Ingram, J.M., Rakes, G.P., Hoover, G.E., Platts-Mills, T.A.E., Heymann, P.W., Eosinophil cationic protein in serum and nasal washes from wheezing infants and children (1995) J. Pediatr., 127, pp. 558-564; Pitkaranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR (1997) J. Clin. Microbiol., 35, pp. 1791-1793; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings by PCR (1993) Mol. Cell. Probes, 7, pp. 373-379; Gwaltney J.M., Jr., Hendley, J.O., Simon, G., Jordan W.S., Jr., Rhinovirus infections in an industrial population: I. The occurrence of illness (1966) N. Engl. J. Med., 275, pp. 1261-1268; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am. J. Respir. Crit. Care Med., 155, pp. 1159-1161; Winther, B., Effects on the nasal mucosa of upper respiratory viruses (common cold) (1994) Dan. Med. Bull., 41, pp. 193-204; Halperin, S.A., Eggleston, P.A., Beasley, P., Suratt, P., Hendley, J.O., Groshel, D.H.M., Gwaltney, J.M., Exacerbations of asthma in adults during experimental rhinovirus infection (1985) Am. Rev. Respir. Dis., 132, pp. 976-980; Grunberg, K., Timmers, M.C., Smits, H.H., De Klerk, E.P., Dick, E.C., Spaan, W.J.M., Hiemstra, P.S., Sterk, P.J., Effect of experimental rhinovirus 16 colds on airway hyperresponsiveness to histamine and interleukin-8 in nasal lavage in asthmatic subjects in vivo (1996) Clin. Exp. Allergy, 27, pp. 36-45; Cheung, D., Dick, E.C., Timmers, M.C., DeKlerk, E.P.A., Spaan, W.J.M., Sterk, P.J., Rhinovirus inhalation causes long-lasting excessive airway narrowing in response to methacholine in asthmatic subjects in vivo (1995) Am. J. Respir. Crit. Care Med., 152, pp. 1490-1496; Gern, J.E., Calhoun, W., Swenson, C., Shen, G., Busse, W.W., Rhinovirus infection preferentially increases lower airway responsiveness in allergic subjects (1997) Am. J. Respir. Crit. Care Med., 155, pp. 1872-1876; Gern, J.E., Vrtis, R., Kelly, E.A., Dick, E.C., Busse, W.W., Rhinovirus produces nonspecific activation of lymphocytes through a monocyte-dependent mechanism (1996) J. Immunol., 157, pp. 1605-1612; Srikiatkhachorn, A., Braciale, T.J., Virus-specific memory and effector T lymphocytes exhibit different cytokine responses to antigens during experimental murine respiratory syncytial virus infection (1997) J. Virol., 71, pp. 678-685; Openshaw, P.J.M., Clarke, S.L., Record, F.M., Pulmonary eosinophilic response to respiratory syncytial virus infection in mice sensitized to the major surface glycoprotein G (1992) Int. Immunol., 4, pp. 493-500; Kim, H.W., Canchola, J.G., Brandt, C.D., Pyles, C.D., Chanock, R.M., Jensen, K., Parrott, R.H., Respiratory syncytial virus disease in infants despite prior administration of antigenic inactivated vaccine (1969) Am. J. Epidemiol., 89, pp. 422-434; Koller, D.Y., Wojnarowski, C., Herkner, K.R., Weinlander, G., Raderer, M., Eichler, I., Frischer, T., High levels of eosinophil cationic protein in wheezing infants predict the development of asthma (1997) J. Allergy Clin. Immunol., 99 (6 PT. 1), pp. 752-756","Rakes, G.P.; MR-4 Building, Box 29, Univ. of Virginia Hlth. Sci. Center, Charlottesville, VA 22908, United States",,"American Lung Association",1073449X,,AJCME,"10051251","English","Am. J. Respir. Crit. Care Med.",Article,"Final",,Scopus,2-s2.0-0032985772
"Carmichael L.E.","7101757988;","Canine viral vaccines at a turning point-A personal perspective",1999,"Advances in Veterinary Medicine","41","C",,"289","307",,35,"10.1016/S0065-3519(99)80022-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032621002&doi=10.1016%2fS0065-3519%2899%2980022-6&partnerID=40&md5=b5963df770b32ae8c2287510344ad3b5","James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Carmichael, L.E., James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","The most important canine viral infections are distemper and CPV-2. Problems of variable CD vaccine safety and efficacy persist, but CD vaccines have greatly reduced the prevalence of disease and cases in vaccinated dogs are now rare. Canine hepatitis (ICH, CAV-1 infection) also has been controlled well by vaccines for more than 35 years and it is now rare; the sporadic cases seen in the 1990s have usually occurred in unvaccinated dogs. CAV-2 vaccines should, therefore, continue to be given since they have proved to be safe and effective, and prevent hepatitis as well as adenoviral tracheobronchitis. Failure to vaccinate would likely result in increase in cases of ICH, a serious disease, but never as significant as distemper and CPV infection. ""Are we vaccinating too often?"" The question is complex, but the dominant opinion is ""yes"" (Smith, 1995). The question cannot be responded to unequivocally, however, since manufacturers employ different strains that vary in their immunizing capacity and, probably, duration of immunity. This question was frequent with distemper in the 1960s. At that time, many veterinarians tested batches of the vaccine they used by providing pre- and postvaccinal sera to competent diagnostic laboratories. That practice appeared to benefit veterinarians and dogs, as well as the quality of vaccines. Unfortunately, many owners and some veterinarians seem to hold the view that infectious diseases such as parvovirus infection can be controlled by frequent vaccination alone. The common practice of dog breeders of vaccinating their animals several times each year is senseless. Revaccination for distemper and parvovirus infection is suggested at 1 year of age, but recommendations regarding the frequency of most vaccinations given after that time are unclear. Since most distemper and CPV-2 vaccines probably provide immunity that endures several years, vaccination at 3- to 5-year intervals, after the first year, seems a reasonable practice until more data on duration of immunity become available. ""Are too many kinds of vaccines being promoted for dogs?"" Distemper and parvovirus vaccines are essential; canine adenovirus vaccines are recommended since the few cases brought to our attention in recent years have been in unvaccinated dogs. Vaccination against respiratory infections is recommended for most dogs, especially those in kennels, or if they are to be boarded. Need has not been clearly established for coronavirus vaccines; Lyme disease vaccines (see below) are useful in preventing illness in areas where the disease exists, but are unnecessary elsewhere since dogs respond rapidly to appropriate antibiotics; current Leptospira bacterins are without benefit since they contain serovars that fail to protect in most areas (noted below). Lyme disease (LD) was not considered here, but newer recombinant (OspA) vaccines are now available that appear to be safe and effective for at least 1 year and they have not caused vaccine-induced postvaccinal lameness, which has been documented with certain whole-cell Lyme disease bacterins. Lyme disease vaccines should be restricted to dogs in, or entering, endemic areas where infested ticks reside. More than 85% of LD cases occur in the mid-Atlantic and Northeastern States, about 10% in six Midwestern states (Michigan, Minnesota, and Wisconsin), and a smaller percentage in restricted areas of northern California and the Pacific Northwest. Leptospirosis also was not discussed here, but vaccines are commonly reported as a cause of anaphylaxis and current vaccines do not contain the serovars prevalent in most regions. The vast majority of cases diagnosed at the New York State Diagnostic Lab at Cornell are grippotyphosa and pomona serovars and there have been no recent cases caused by canicola or icterohemorrhagiae serovars. Because leptospirosis is an important disease of dogs, there is an urgent need for more research and the development of safer vaccines that contain the prevalent serovars. In Mexico, dogs may be infected with several serovars and some canine vaccines contain 8-10 serovars. The conditio sine qua non is the availability of consistently good vaccines. Without standardization of vaccines, it seems difficult to formulate general vaccine recommendations. Effort should be directed to improving and standardizing the important vaccines in current use, not the development of new products, unless need is demonstrated. The public is becoming increasingly aware of vaccine problems, perhaps even more so than the benefits of vaccination. The reality that all vaccines carry some risk is not fully perceived by many owners and veterinarians. Alternative veterinary medicine is now a growing reality; such practices are being taught in some veterinary colleges and questions pertaining to vaccine safety and efficacy will continue to vex veterinarians, vaccinologists, and vaccine producers. They will have to be addressed. There is a need for better appreciation of the risk of adverse reactions (Duval and Giger, 1996). Finally, the issues that have been discussed, or recommendations that might be made, will have little influence unless biologics manufacturers and regulatory officials exercise greater responsibility in controlling vaccine quality. This could be encouraged by the appointment of a committee of unbiased experts to review vaccines for each disease and provide recommendations based on available evidence. This view has been discussed at meetings on several occasions during the past 30 years, but it has been largely neglected because of considerations that involve industry interests, indifferent or overburdened government authorities, and the trust by veterinarians and dog owners in advertising. Vaccines and vaccination guidelines for physicians are supervised by the American Academy of Pediatric's Committee on Infectious Diseases and the Advisory Committee on Immunization Practices who advise the medical profession and regulatory authorities (Holmes, 1996). Until the veterinary profession insists on a responsible advisory council, concerns and questions regarding vaccines will continue to be met by conflicting opinions and open the door to ""Nosodes"" and ""Thuja""-whose benefits seem to be understood only by those who use and profit from them. © 1999 Elsevier Inc. All rights reserved.",,"virus vaccine; animal; animal disease; Coronavirus; dog; dog disease; immunology; Parvovirus; review; vaccination; virology; virus infection; Animals; Coronavirus Infections; Coronavirus, Canine; Distemper; Dog Diseases; Dogs; Parvoviridae Infections; Parvovirus; Vaccination; Viral Vaccines; Virus Diseases","Appel, M., Reversion to virulence of attenuated canine distemper virus in vivo and in vitro (1978) J. Gen. Virol., 41, pp. 385-390; Appel, M., (1987) Virus Infections of Vertebrates, 1, pp. 29-160. , Horzinek M.C. (Ed), Elsevier, Amsterdam; Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet. Med., 83, pp. 360-366; Appel, M.J.G., Gillespie, J.H., Canine distemper virus (1972) Virol. Monogr., 11, pp. 27-48; Baker, J.A., Robson, D.S., Carmichael, L.E., Gillespie, J.H., Hildreth, B., Control procedures for infectious diseases of dogs (1961) Proc. Anim. Care Panel, 11, pp. 234-244; Baker, J.A., Robson, D.S., Hildreth, B., Pakkala, B., Breed response to distemper vaccination (1962) Proc. Anim. Care Panel, 12, pp. 157-162; Binn, L.N., Lazar, E.C., Keenan, Recovery and characterization of a coronavirus from military dogs with diarrhea (1975) Proc. 78th Annu. Meet., U.S. Anim. Health Assoc., pp. 359-366. , Roanoke, VA, 1974; Brunner, C.J., Swango, L.J., Canine parvovirus infection: Effects on the immune system and factors that predispose to severe disease (1985) Compend. Contin. Educ. Vet. Pract., 7, pp. 979-988; Carmichael, L.E., Immunization strategies in puppies-why failures? (1983) Compend. Contin. Educ. Pract. Vet., 5, pp. 1043-1051; Carmichael, L.E., Canine parvovirus immunization: ""Myths and realities."" (1989) Am. Kennel Club Gaz., Decembers, pp. 94-102; Carmichael, L.E., Canine parvovirus type-2: An evolving pathogen of dogs (1994) Ann. Med. Vét., 138, pp. 459-464; Carmichael, L.E., Vaccines for dogs (1997) Veterinary Vaccinology, pp. 327-331. , Pastoret P.-P., Balncou J., Vannier P., and Vereschueren C. (Eds), Elsevier, Amsterdam; Carmichael, L.E., Pollock, R.H.V., Joubert, J.C., A modified live canine parvovirus strain with novel plaque characteristics. II: Immune response (1983) Cornell Vet., 71, pp. 13-29; Coyne, M.J., May, S.W., Considerations in using a canine coronavirus vaccine (1995) Top. Vet. Med., 6, pp. 32-34; Dodds, W.J., Vaccine safety and efficacy (1991) Kennel Hotline, 8, pp. 2-4; Duval, D., Giger, U., Vaccine-associated immune-mediated hemolytic anaemia in the dog (1996) J. Vet. Intern. Med., 10, pp. 290-295; Edwards, B.G., Fulker, R.H., Acree, W.M., Evaluating a canine coronavirus vaccine through antigen extinction and challenge studies (1985) Vet. Med., 80, pp. 28-33; Fulker, R., Wasmoen, T., Atchison, H.-J., Acree, W., Efficacy of an inactivated vaccine against clinical disease caused by canine coronavirus (1995) Corona- and Related Viruses, , Talbot P.J., and Levy G.A. (Eds), Plenum, New York; Gorham, J.R., Duration of vaccination immunity and the influence on subsequent prophylaxis (1966) J. Am. Vet. Med. Assoc., 149, pp. 699-704; Holmes, S.J., Review of recommendations of the Advisory Committee on Immunization Practices. Centers for Disease Control and Prevention (1996) J. Infect. Dis., 174, pp. S342-S344; Hoskins, J.D., Taylor, H.W., Gourley, K.R., Challenge trial of a new attenuated canine parvovirus vaccine (1995) Proc. Annu. Vet. Med. Forum Am. Coll. Vet. Intern. Med., 13, p. 1012; Larson, L.J., Schultz, R.D., High-titer canine parvovirus vaccine: Serologic response and challenge-of-immunity study (1996) Vet. Med., March, pp. 1-5; Luff, P.R., Wood, G.W., Thornton, P.H., Canine parvovirus serology: Collaborative assay (1987) Vet. Rec., 120, pp. 270-273; Martin, M.L., Canine coronavirus enteritis and a recent outbreak following modified live virus vaccination (1985) Compend. Contin. Educ. Pract. Vet., 7, pp. 1012-1017; Pastoret, P.-P., Les infections digestives d'origin viral chez le chien (1984) Ann. Med. Vet., 128, pp. 473-483; Phillips, T.R., Schultz, R.D., Failure of vaccine or virulent strains of canine parvovirus to induce immunosuppressive effects on the immune system of the dog (1987) Viral Immunol., 1, pp. 135-144; Pitcairn, R.H., (1995) Dr. Pitcairn's Complete Guide to Natural Health for Dogs & Cats. 2nd ed, , Rodale Press, Emmaus, PA; Pollock, R.H.V., Carmichael, L.E., Enteric viruses (1990) Infectious Diseases of the Dog and Cat, pp. 226-283. , Greene C.E. (Ed), Saunders, Philadelphia; Priest, S.A., Holistic remedies are getting a shot in the arm. Homeopathic nosodes are being examined by some vets as an option to yearly vaccines (1996) Dog World, January, pp. 24-30; Prydie, J., Persistence of antibodies following vaccination against canine distemper and effect of revaccination (1966) Vet. Rec., 78, pp. 486-488; Rikula, U., Sihvonen, L., Voipio, H.M., Serum antibody response to canine distemper virus vaccines in beagle dogs (1995) Front. Lab. Anim. Sci., p. 199; Rimmelzwaan, G., Application of enzyme-linked immunosorbant assay systems for the serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in The Netherlands. Canine Parvovirus Infection: Novel Approaches to Diagnosis and Immune Prophylaxis (1990) Thesis, pp. 39-56. , State University of Utrecht, The Netherlands; Rockborn, G., Lannek, N., Norby, E., Comparison between the immunizing effect in dogs and ferrets of living distemper vaccines attenuated in dog tissue culture and embryonated eggs (1965) Res. Vet. Sci., 6, p. 423; Schultz, R.D., Emerging issue: Vaccines strategies for canine viral enteritis (1995) Proc. Int. Gastroenter. Symp. North Am. Vet. Conf., pp. 19-24; Schultz, R.D., Canine distemper: Comparison of the leading multi-component commercial vaccines (1996) Infect. Dis. Bull., pp. 1-2. , Intervet, Millsboro, DE; Smith, C.A., Current concepts: Are we vaccinating too much? (1995) J. Am. Vet. Med. Assoc., 207, pp. 421-425; Starita-Mehan, D., The Dangers of Vaccinations, and the Advantages of Nosodes for Disease Prevention. Nosode Vaccination (1997) County Way Veterinary Care, Boring, OR; Taura, Y., Ishi, K., Nagami, M., Changes in lymphoproliferation and DTH responses after vaccination immediately before surgery in puppies (1995) J. Vet. Med. Sci., 57, pp. 899-904; Taylor, J., Tartaglia, J., Riviere, Applications of canarypox (ALVAC) vectors in human and veterinary vaccines (1994) Dev. Biol. Stand., 82, pp. 131-135; Tennant, B.J., Gaskell, R.M., Jones, R.C., Studies on the epizootiology of canine coronavirus (1993) Vet. Rec., 132, pp. 7-11; Tizzard, I., Risks associated with the use of live vaccines (1990) J. Am. Vet. Med. Assoc., 196, pp. 1851-1858; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine and human coronavirus in serogrup I (1996) J. Virol., pp. 8669-8674; Vieler, E., Herbst, W., electron microscopic determination of viruses in feces of dogs with diarrhea (1995) Tieraerztl. Prax., 23, pp. 66-69; Wilbur, L.A., Abortion and death in pregnant bitches associated with a canine vaccine contaminated with bluetongue virus (1994) J. Am. Vet. Med. Assoc., 204, pp. 1762-1765; Wilson, R.B., Holladay, J.A., Cave, J.A., A neurologic syndrome associated with use of a canine coronavirus-parvovirus vaccine in dogs (1986) Compend. Contin. Educ. Pract. Vet., 8, pp. 117-124; Yarnall, C., (1995) Cat Care Naturally, , Tuttle, Rutland, VT; Schultz, R.D., Current and future canine and feline vaccination programs (1998) Vet. Med., 93 (3), pp. 233-254; Schultz, R.D., Vaccine immunity challenges for the 21st century (1998) Suppl. Compend. Contin. Educ. Pract. Vet., 20 (5 B), pp. 5-18","Carmichael, L.E.; James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States",,"Academic Press Inc.",1093975X,,,"9890023","English","Adv. Vet. Med.",Book Chapter,"Final",,Scopus,2-s2.0-0032621002
"De La Fuente R., Luzón M., Ruiz-Santa-Quiteria J.A., García A., Cid D., Orden J.A., García S., Sanz R., Gómez-Bautista M.","6507240946;6602384929;6701468772;54406740900;6701327952;6506947568;7201561300;7006843232;6701627325;","Cryptosporidium and concurrent infections with other major enterophatogens in 1 to 30-day-old diarrheic dairy calves in central Spain",1999,"Veterinary Parasitology","80","3",,"179","185",,81,"10.1016/S0304-4017(98)00218-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032890386&doi=10.1016%2fS0304-4017%2898%2900218-0&partnerID=40&md5=5c2e1de6eef9f6c04fc94aeacacb6a3d","Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain","De La Fuente, R., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Luzón, M., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Ruiz-Santa-Quiteria, J.A., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; García, A., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Cid, D., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Orden, J.A., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; García, S., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Sanz, R., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain; Gómez-Bautista, M., Depto. Patología Animal I, Fac. de Vet., Univ. Complutense, 28040 Madrid, Spain","Faeces samples from 218, 1 to 30-day-old, diarrheic dairy calves in 65 dairy herds were screened for the presence of Cryptosporidium and concurrent infections with rotavirus, coronavirus, F5+ Escherichia coli and Salmonella spp. Calves were grouped according to their age as follows: 1-7, 8-14, 15-21 and 22-30 days. Cryptosporidium infection was detected in 43.8%, 71.9%, 63.2% and 6.9% of the calves in the respective age groups. Significant differences in the detection rate of Cryptosporidium were found between the age group 22-30 days and all other age groups, and between the age group 1-7 days and the age groups 8-14 days and 15-21 days. Cryptosporidium was the only enteropathogen detected in 60 of the 114 (52.6%) diarrheic calves. Concurrent infections with other enteropathogen(s) were detected in 64.3%, 46.3%, 39.5% and 0% of the Cryptosporidium-infected calves in the age groups 1-7, 8-14, 15-21 and 22-30 days, respectively. A significant age-associated decrease in the detection rate of mixed infections (p&lt;0.05) was found. The detection rates of the other enteropathogens considered in calves with Cryptosporidium infection were 87% for rotavirus, 11.1% for coronavirus, 27.8% for F5+ E. coli and 1.8% for Salmonella. Copyright (C) 1999 Elsevier Science B.V.","Cattle-protozoa; Coronavirus; Cryptosporidium sp.; Escherichia coli; Neonatal calf diarrhea; Rotavirus; Salmonella","age; article; coronavirus; cryptosporidiosis; cryptosporidium; diarrhea; enzyme linked immunosorbent assay; escherichia coli; feces analysis; nonhuman; rotavirus; salmonella; spain; superinfection; Agglutination Tests; Animals; Animals, Suckling; Cattle; Cattle Diseases; Coronavirus; Coronavirus Infections; Cryptosporidiosis; Cryptosporidium; Diarrhea; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Escherichia coli Infections; Feces; Female; Gastroenteritis; Rotavirus; Rotavirus Infections; Salmonella; Salmonella Infections, Animal; Spain; Bos taurus; Coronavirus; Cryptosporidium; Cryptosporidium sp.; Escherichia coli; Protozoa; Rotavirus; Salmonella","Bellinzoni, R.C., Blackhall, J., Terzolo, H.R., Moreira, A.R., Auza, N., Mattion, N., Micheo, G.L., Scodeller, E.A., Microbiology of diarrhoea in young beef and dairy calves in Argentina (1990) Rev. Argent. Microbiol., 22, pp. 130-137; Brenner, J., Elad, D., Markovics, A., Grinberg, A., Trainin, Z., Epidemiological study of neonatal calf diarrhoea in Israel - A one-year survey of faecal samples (1993) Isr. J. Vet. Med., 48, pp. 113-116; Bulgin, M.S., Anderson, B.C., Ward, A.C.S., Evermann, J.F., Infectious agents associated with neonatal calf disease in southwestern Idaho and eastern Oregon (1982) J. Am. Vet. Med. Assoc., 180, pp. 1222-1226; Casemore, D.P., Armstrong, M., Sands, R.L., Laboratory diagnosis of cryptosporidiosis (1985) J. Clin. Pathol., 38, pp. 1337-1341; Contrepois, M., Martel, J.L., Bordas, C., Hayers, F., Millet, A., Ramisse, J., Sendral, R., Fréquence des pili FY et K99 parmi des souches de Escherichia coli isolées de veaux diarrhéiques en France (1985) Ann. Rech. Vét., 16, pp. 25-28; Dean, A.G., Dean, J.A., Coulombier, D., Brendel, K.A., Smith, D.C., Burton, A.H., Dicker, R.C., Arner, T.G., (1994) Epi Info Version 6: A Word Processing, Database, and Statistics Program for Epidemiology on Microcomputers, , Centers for Disease Control and Prevention, Atlanta, Georgia, USA; Fagan, J.G., Dwyer, P.J., Quinlan, J.G., Factors that may affect the occurrence of enteropathogens in the faeces of diarrhoeic calves in Ireland (1995) Irish Vet. J., 48, pp. 17-21; Fayer, R., Ungar, B.L.P., Cryptosporidium spp. and cryptosporidiosis (1986) Microbiol. Rev., 50, pp. 458-483; Fletcher, R.H., Fletcher, S.W., Wagner, E.H., (1996) Clinical Epidemiology - The Essentials, , Williams and Wilkins, Baltimore MD, 276pp; Garber, L.P., Salman, M.D., Hurd, H.S., Keefe, T., Schlater, J.L., Potential risk factors for Cryptosporidium infection in dairy calves (1994) Am. J. Vet. Med. Assoc., 205, pp. 86-91; Heine, J., Eine einfache Nachweismethode für Krytosporidiosen im Kot (1982) Zentralbl. Veterinaermed. Reihe B, 29, pp. 324-327; Herring, A.J., Inglis, N.F., Ojeh, C.K., Snodgrass, D.R., Menzies, J.D., Rapid diagnosis of rotavirus infection by direct detection of viral nucleic acid in silver-stained polyacrylamide gels (1982) J. Clin. Microbiol., 16, pp. 473-477; Markovics, A., Pipano, E., Shedding of cryptosporidial oocysts by naturally infected calves (1987) Isr. J. Vet. Med., 43, pp. 46-49; Martín, S., Ortega, L.M., Pilar, M., Rojo, F.A., Pereira, J., Pevalencia de la infección por Cryptosporidium parvum en terneros en la provincia de León (1995) IV Congreso Ibérico Parasitología, pp. 118-119. , Santiago de compostela, Spain; McDonough, S.P., Stull, C.L., Osburn, B.I., Enteric pathogens in intensively reared veal calves (1994) Am. J. Vet. Res., 55, pp. 1516-1520; Moore, D.A., Zeman, D.H., Cryptosporidiosis in neonatal calves: 277 cases (1986-1987) (1991) J. Am. Vet. Med. Assoc., 198, pp. 1969-1971; Morin, M., Lariviee, S., Lallier, R., Begin, M.E., Ethier, R., Roy, R.S., Tremblay, A., Diarrhoea of newborn calves. II. Agents responsible for the disease on Quebec dairy farms (1980) Med. Vét. Quebec, 10, pp. 60-65; Morris, J.A., Thorns, C.J., Wells, G.A.H., Scott, A.C., Sojka, W.J., The Production of F41 fimbriae by piglet strains of enterotoxigenic Escherichia coli that lack K88, K99 and 987P fimbriae (1983) J. Gen. Microbiol., 129, pp. 2753-2759; O'Donoghue, P., Cryptosporidium and cryptosporidiosis in man and animals (1995) Int. J. Parasitol., 25, pp. 139-195; Otto, V.P., Elschner, M., Günther, H., Schulze, F., Vergleichende Untersuchungen zum nachweis von Rotaviren, Coronaviren, Kryptosporidien und enterotoxigenen E. coli im Kot durchfallkranker Kälber (1995) Tierärztl Umschau, 50, pp. 80-86; Quílez, J., Sánchez-Acebo, C., Del Cacho, E., Clavel, A., Causapé, A.C., Prevalence of Cryptosporidium and Giardia infections in cattle in Aragón (northeastern Spain) (1996) Vet. Parasitol., 66, pp. 139-146; Reynolds, D.J., Morgan, J.H., Chanter, N., Jones, P.W., Bridger, J.C., Debney, T.G., Bunch, K.J., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec., 119, pp. 34-39; Rosati, S., Dondo, A., Guercio, A., Maglione, E., Masoero, L., Rotavirosi bovina in Piamonte: Indagine virologica e sierologica in allevamenti con sindrome enterica in atto (1991) Atti Della Società Italiana di Buiatria, 23, pp. 165-170; Sherwood, D., Snodgrass, D.R., Lawson, G.H.K., Prevalence of enterotoxigenic Escherichia coli in calves in Scotland and northern England (1983) Vet. Rec., 113, pp. 208-212; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Tzipori, S., Smith, M., Halpin, C., Angus, K.W., Sherwood, D., Campbell, I., Experimental cryptosporidiosis in calves: Clinical manifestations and pathological finding (1983) Vet. Rec., 112, pp. 116-120; Zrelli, M., Messadi, L., Ben Miled, L., Jemli, M.H., Haddad, N., Les agents infectieux associés aux diarrhées néonatales du veau en Tunisie (1990) Revue Méd. Vét., 141, pp. 861-872","De la Fuente, R.; Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; email: rifuente@eucemax.sim.ucm.es",,,03044017,,VPARD,"9950342","English","Vet. Parasitol.",Article,"Final",,Scopus,2-s2.0-0032890386
"Izeta A., Smerdou C., Alonso S., Penzes Z., Mendez A., Plana-Durán J., Enjuanes L.","6602523425;6602856664;57210695335;55761804900;36823007700;6604038063;7006565392;","Replication and packaging of transmissible gastroenteritis coronavirus- derived synthetic minigenomes",1999,"Journal of Virology","73","2",,"1535","1545",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032948952&partnerID=40&md5=651442c37bf1a043ea20d51c4346a7d8","Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Fort Dodge Veterinaria, Vall de Bianya, 17813 Girona, Spain","Izeta, A., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Smerdou, C., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Alonso, S., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Penzes, Z., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Mendez, A., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain; Plana-Durán, J., Fort Dodge Veterinaria, Vall de Bianya, 17813 Girona, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Ctro. Natl. de Biotecnología, Campus Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain","The sequences involved in the replication and packaging of transmissible gastroenteritis virus (TGEV) RNA have been studied. The structure of a TGEV defective interfering RNA of 9.7 kb (DI-C) was described previously (A. Mendez, C. Smerdou, A. Izeta, F. Gebauer, and L. Enjuanes, Virology 217: 495- 507, 1996), and a cDNA with the information to encode DI-C RNA was cloned under the control of the T7 promoter. The molecularly cloned DI-C RNA was replicated in trans upon transfection of helper virus-infected cells and inhibited 20-fold the replication of the parental genome. A collection of 14 DI-C RNA deletion mutants (TGEV minigenomes) was synthetically generated and tested for their ability to be replicated and packaged. The smallest minigenome (M33) that was replicated by the helper virus and efficiently packaged was 3.3 kb. A minigenome of 2.1 kb (M21) was also replicated, but it was packaged with much lower efficiency than the M33 minigenome, suggesting that it had lost either the sequences containing the main packaging signal or the required secondary structure in the packaging signal due to alteration of the flanking sequences. The low packaging efficiency of the M21 minigenome was not due to minimum size restrictions. The sequences essential for minigenome replication by the helper virus were reduced to 1,348 nt and 492 nt at the 5' and 3' ends, respectively. The TGEV-derived RNA minigenomes were successfully expressed following a two-step amplification system that couples pol II-driven transcription in the nucleus to replication supported by helper virus in the cytoplasm, without any obvious splicing. This system and the use of the reporter gene β-glucuronidase (GUS) allowed minigenome detection at passage zero, making it possible to distinguish replication efficiency from packaging capability. The synthetic minigenomes have been used to design a helper-dependent expression system that produces around 1.0 μg/106 cells of GUS.",,"animal cell; article; coronavirus; DNA flanking region; helper virus; nonhuman; nucleotide sequence; open reading frame; priority journal; promoter region; protein secondary structure; RNA replication; RNA structure; virus genome; virus replication; Animals; Base Sequence; Cell Line; DNA, Viral; Gene Expression; Genes, Viral; Helper Viruses; Molecular Sequence Data; RNA, Viral; Swine; Transmissible gastroenteritis virus; Virus Assembly; Virus Replication","Ball, L.A., Cellular expression of a functional nodavirus RNA replicon from vaccinia virus vectors (1992) J. Virol., 64, pp. 2335-2345; Ball, L.A., Requirements for the self-directed replication of flock house virus RNA I (1995) J. 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Virol., 9, pp. 173-180; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Semin. Virol., 8, pp. 101-111; Bronstein, I., Fortin, J., Stanley, P.E., Stewart, G.S.A.B., Kricka, L.J., Chemiluminescent and bioluminescent reporter gene assays (1994) Anal. Biochem., 219, pp. 169-181; Bronstein, I., Fortin, J.J., Voyta, J.C., Juo, R.-R., Edwards, B., Olenses, C.E.M., Lijam, N., Kricka, L.J., Chemiluminescent reporter gene assays: Sensitive detection of the GUS and SEAP gene products (1994) BioTechniques, 17, pp. 172-177; Bronstein, I., Martin, C.S., Fortin, J.J., Olesen, C.E.M., Voyta, J.C., Chemiluminescence: Sensitive detection technology for reporter gene assays (1996) Clin. Chem., 42, pp. 1542-1546; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. 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Virol., 71, pp. 824-827; Zhou, M., Collisson, E.W., Determination of RNA binding domains in the IBV nucleocapsid protein (1998) Fifth International Symposium on Positive Strand RNA Viruses, , St. Petersburg, Fla","Enjuanes, L.; Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, CSIC, Canto Blanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,0022538X,,JOVIA,"9882359","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032948952
"Verinaud L., Camargo I.J.B., Vassallo J., Sakurada J.K., Rangel H.A.","6602378213;6603667046;7005637352;7004164464;7003471453;","Lymphoid organ alterations enhanced by sub-lethal doses of coronaviruses in experimentally induced Trypanosoma cruzi infection in mice",1999,"Laboratory Animal Science","49","1",,"35","41",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033002592&partnerID=40&md5=ab114ae18e76f151ea303ee09ce7fa97","Dept. of Microbiology and Immunology, Institute of Biology, Unicamp, Campinas, São Paulo, Brazil; Department of Pathology, Medical School, Unicamp, Campinas, São Paulo, Brazil; Depto. de Microbiologia e Imunologia, Instituto de Biologia, UNICAMP, C.P. 6109, Campinas, São Paulo, Brazil","Verinaud, L., Dept. of Microbiology and Immunology, Institute of Biology, Unicamp, Campinas, São Paulo, Brazil, Depto. de Microbiologia e Imunologia, Instituto de Biologia, UNICAMP, C.P. 6109, Campinas, São Paulo, Brazil; Camargo, I.J.B., Dept. of Microbiology and Immunology, Institute of Biology, Unicamp, Campinas, São Paulo, Brazil; Vassallo, J., Department of Pathology, Medical School, Unicamp, Campinas, São Paulo, Brazil; Sakurada, J.K., Dept. of Microbiology and Immunology, Institute of Biology, Unicamp, Campinas, São Paulo, Brazil; Rangel, H.A., Dept. of Microbiology and Immunology, Institute of Biology, Unicamp, Campinas, São Paulo, Brazil","The effect of sub-lethal doses of coronaviruses on the course of disease in CBA mice experimentally infected with a mildly pathogenic strain of Trypanosoma cruzi was investigated. Mice were inoculated with either T. cruzi, 0.1 median lethal dose (LD50) of coronavirus (mouse hepatitis virus [MHV-3] or virus X), or both pathogens. Levels of parasitemia, mortality, and the extent of pathologic alterations in lymphoid organs were determined. Mice inoculated with T. cruzi had mild alterations in their lymphoid organs and survived infection. In contrast, mice inoculated with both pathogens died, and had significantly higher levels of parasitemia and profound alterations in lymphoid organs. These results indicate that the pathologic profile of T. cruzi infection can be profoundly altered by subclinical infection with coronaviruses.",,"animal cell; animal model; animal tissue; article; cell survival; controlled study; coronavirus; disease course; female; histopathology; ld 50; lymphoid cell; male; mouse; nonhuman; pathogenesis; trypanosoma cruzi; Animals; Bone Marrow Cells; Cell Count; Chagas Disease; Coronavirus Infections; Female; Hematopoietic Stem Cells; Lymph Nodes; Lymphoid Tissue; Male; Mice; Mice, Inbred BALB C; Mice, Inbred CBA; Organ Size; Parasitemia; Spleen; Thymus Gland; Trypanosoma cruzi","Control of Chagas' disease (1991) W.H.O., 187, pp. 1-99; Brener, Z., Immunity to Trypanosoma cruzi (1980) Adv. Parasitol., 18, pp. 247-291; Reed, S.G., Inverso, J.A., Roters, S.B., Suppressed antibody responses to sheep erythrocytes in mice with chronic Trypanosoma cruzi infections are restored with interleukin 2 (1984) J. 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Parasitol., 34, pp. 168-180; Midoro, K., Nakanaga, K., Kyuwa, S., Immunopathology of chronic progressive hepatitis in nude mice infected with low-virulent mouse hepatitis virus (1989) Microbiol. Immunol., 33, pp. 669-682","Verinaud, L.; Depto. de Microbiologia e Imunologia, Instituto de Biologia, UNICAMP, C.P. 6109, Campinas, São Paulo, Brazil",,,00236764,,LBASA,"10090092","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0033002592
"Schoenike B., Franta A.K., Fleming J.O.","7801352811;36966675300;7401457370;","Quantitative sense-specific determination of murine coronavirus RNA by reverse transcription polymerase chain reaction",1999,"Journal of Virological Methods","78","1-2",,"35","49",,5,"10.1016/S0166-0934(98)00167-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032977675&doi=10.1016%2fS0166-0934%2898%2900167-0&partnerID=40&md5=8750e49f6ce25897a24ceae6541ddb22","Depts. Neurol. Med. Microbiol. I., Univ. of Wisconsin, 1300 Univ. Ave., Madison, WI 53906, United States; William s. Middleton Vet. Hospital, Madison, WI 53792, United States","Schoenike, B., Depts. Neurol. Med. Microbiol. I., Univ. of Wisconsin, 1300 Univ. Ave., Madison, WI 53906, United States, William s. Middleton Vet. Hospital, Madison, WI 53792, United States; Franta, A.K., Depts. Neurol. Med. Microbiol. I., Univ. of Wisconsin, 1300 Univ. Ave., Madison, WI 53906, United States, William s. Middleton Vet. Hospital, Madison, WI 53792, United States; Fleming, J.O., Depts. Neurol. Med. Microbiol. I., Univ. of Wisconsin, 1300 Univ. Ave., Madison, WI 53906, United States, William s. Middleton Vet. Hospital, Madison, WI 53792, United States","In many applications, it is useful to know the sense and amount of viral RNAs present in a sample. In theory, sense-specific measurement of viral RNAs may be achieved by reverse transcription polymerase chain reaction (RT-PCR) assays which utilize primers of defined polarity during the RT step. However, in practice, it has been shown that such assays are prone to artifacts, such as non-specific priming, which drastically diminish their reliability. Using murine coronavirus MHV-4 as a model, we describe and validate several modifications of the RT-PCR procedure which eliminate these artifacts. Key RT-PCR parameters which were optimized include the design of tagged primers, DNase treatment of in vitro transcribed RNA standards, specification of temperature differences between RT and PCR annealing steps, and use of competitive RNA templates for quantitative assays. The assays described may be used to determine the sense and abundance of any viral or host RNA of interest in complex biological specimens. Copyright (C) 1999 Elsevier Science B.V.","Coronaviruses; Mouse hepatitis virus; PCR; Sense-specific RNA determination","virus RNA; accuracy; article; coronavirus; nucleotide sequence; priority journal; quantitative assay; reverse transcription polymerase chain reaction; RNA analysis; RNA sequence; sequence homology; technique; temperature; Animals; Coronavirus Infections; DNA, Antisense; Male; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Plasmids; Reproducibility of Results; Reverse Transcriptase Polymerase Chain Reaction; RNA, Antisense; RNA, Viral; Sensitivity and Specificity; Transcription, Genetic; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus strain 4","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1994) Current Protocols in Molecular Biology, p. 4912. , (Eds.), Wiley, New York; Bauer, P., Rolfs, A., Regitz-Zagrosek, V., Hildebrandt, A., Fleck, E., Use of maganese in RT-PCR eliminates PCR artifacts resulting from DNase I digestion (1997) BioTechniques, 22, pp. 1128-1132; Blumberg, D.D., Creating a ribonuclease-free environment (1987) Methods Enzymol., 152, pp. 20-24; Busch, M.P., Wilber, J.C., Johnson, P., Tobler, L., Evans, C.S., Impact of specimen handling and storage on detection of hepatitis C virus RNA (1992) Transfusion, 32, pp. 420-425; Chaves, R.L., Graff, J., Normann, A., Flehmig, B., Specific detection of minus strand hepatitis A virus RNA by Tail-PCR following reverse transcription (1994) Nucleic Acids Res., 22, pp. 1919-1920; Cheley, S., Anderson, R., Cupples, M.J., Lee Chan, E.C.M., Morris, V.L., Intracellular murine hepatitis virus-specific RNAs contain common sequences (1981) Virology, 112, pp. 596-604; Chou, Q., Russell, M., Birch, D., Raymond, J., Bloch, W., Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplifications (1992) Nucleic Acids Res., 20, pp. 1717-1723; Farkas, D.H., Kaul, K.L., Wiedbrauk, D.C., Kiechle, F.L., Specimen collection and storage for diagnostic molecular pathology investigation (1996) Arch. Pathol. Lab. Med., 120, pp. 591-596; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Foley, K.P., Leonard, M.W., Engel, J.D., Quantitation of RNA using the polymerase chain reaction (1993) Trends Genet., 9, pp. 380-385; Gill, S.S., Aubin, R.A., Bura, C.A., Curran, I.H.A., Matula, T.I., Ensuring recovery of intact RNA from rat pancreas (1996) Mol. Biotech., 6, pp. 359-362; Gilland, G., Perrin, S., Bunn, H.F., Competitive PCR for quantitation of mRNA (1990) PCR Protocols, pp. 60-69. , M.A. Innis, D.H. Gelfand, J.J. Sninsky, & T.J. White. San Diego: Academic Press; Gunji, T., Kato, N., Hijikata, M., Hayashi, K., Saitoh, S., Shimotohno, K., Specific detection of positive and negative stranded hepatitis C viral RNA using chemical RNA modification (1994) Arch. 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NeuroVirol., 2, pp. 361-376; Jagus, R., Hybrid selection of mRNA and hybrid arrest of translation (1987) Methods Enzymol., 152, p. 567572; Köhler, T., Lassner, D., Rost, A.-K., Thamm, B., Pustowoit, B., Remke, H., (1995) Quantification of Mrna by Polymerase Chain Reaction, , (Eds.), Springer, Berlin; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lanford, R.E., Sureau, C., Jacob, J.R., White, R., Fuerst, T.R., Demonstration of in vitro infection of chimpanzee hepatocytes with hepatitis C virus using strand-specific RT-PCR (1994) Virology, 202, pp. 606-614; Lerat, H., Berby, F., Traubaud, M.-A., Vidalin, O., Major, M., Trépo, C., Inchauspé, G., Specific detection of hepatitis C virus minus strand RNA in hematopoietic cells (1996) J. Clin. Invest., 97, pp. 845-851; McGuinness, P.H., Bishop, G.A., McCaughan, G.W., Trowbridge, R., Gowans, E.J., False detection of negative-strand hepatitis C virus RNA (1994) Lancet, 343, pp. 551-552; Mullis, K., The polymerase chain reaction in an anemic mode: How to avoid cold oligodeoxyribonuclear fusion (1991) PCR Methods Appl., 1, pp. 1-4; Prediger, E., RNA isolation: New ways to handle tissue and store RNA (1998) Ambion TechNotes, 5, pp. 1-16; Rock, R.C., Technical evaluation of laboratory studies (1994) Laboratory Medicine: The Selection and Interpretation of Clinical Laboratory Studies, pp. 15-26. , D.A. Noe, & R.C. Rock. Baltimore: Williams and Wilkins; Saag, M.S., Quantification of HIV viral load: A tool for clinical practice (1997) The Medical Management of AIDS, pp. 57-74. , M.A. Sande, & P.A. Volberding. Philadelphia: W.B. Saunders; Schneeberger, C., Speiser, P., Kury, F., Zeillinger, R., Quantitative detection of reverse transcriptase-PCR products by means of a novel and sensitive DNA stain (1995) PCR Methods Appl., 4, pp. 234-238; Silver, J., Limjoco, T., Feinstone, S., Site-specific mutagenesis using the polymerase chain reaction (1995) PCR Strategies, pp. 179-188. , M.A. Innis, D.H. Gelfand, & J.J. Sninsky. San Diego: Academic Press; Tsai, S.-J., Wiltbank, M.C., Quantification of mRNA using competitive RT-PCR with standard curve methodology (1996) BioTechniques, 21, pp. 862-866; Wang, A.M., Doyle, M.V., Mark, D.F., Quantitation of mRNA by the polymerase chain reaction (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 9717-9721; Wang, F.I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Willems, M., Moshage, H., Yap, S.H., PCR and detection of negative HCV RNA strands (1993) Hepatology, 17, p. 526; Yokoi, H., Natsuyama, S., Iwai, M., Noda, Y., Mori, T., Mori, K.J., Fujita, K., Fujita, J., Non-radioisotopic quantitative RT-PCR to detect changes in mRNA levels during early mouse embryo development (1993) Biochem. Biophys. Res. Commun., 195, pp. 769-775; Zazzi, M., Romano, L., Peruzzi, F., Toneatto, S., De Milito, A., Botta, G., Valensin, P.E., Optimal conditions for detection of human immunodeficiency virus type 1 DNA by polymerase chain reaction with nested primers (1993) Mol. Cell. Probes, 7, pp. 431-437","Fleming, J.O.; Department of Neurology, University of Wisconsin, 1300 University Avenue, Madison, WI 53906, United States; email: fleming@neurology.wisc.edu",,,01660934,,JVMED,"10204695","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0032977675
"Sigari G., Losi E.","6603105311;6701432273;","Gastroenteritis and hepatitis A viruses in mussels [Virus delle gastroenteriti e dell'epatite a (HAV) nei mitili]",1999,"Igiene Moderna","111","3",,"225","238",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0039622698&partnerID=40&md5=79f9ddce50d44b4cd2e4156d67025890","Sezione di Igiene e Med. Preventiva, Dipartimento di Scienze della Salute, Univ. degli Studi di Genova, Via Pastore, 1, 16132 Genova, Italy","Sigari, G., Sezione di Igiene e Med. Preventiva, Dipartimento di Scienze della Salute, Univ. degli Studi di Genova, Via Pastore, 1, 16132 Genova, Italy; Losi, E.","The presence of enteroviruses and hepatitis A virus in mussels of the Arenzano Gulf coast was monitored over a period of 5 months (from May to September 1996). Viruses were detected in mussel samples obtained from four areas. The fluid of the mussels was concentrated in Microton-100 (Amicon) and viruses were detected by electron microscopy (EM). Results indicated that hepatitis A-like virus (HAV) and Norwalk-like viruses were more persistent during July and August. Adenovirus enteric, Coronavirus-like and Parvovirus-like were also detected. The increase of virus was considered to be a reflection of the increased human population during July and August, and was probably dependent upon the enviromental concentration. The occurence of enterovirus in marine water, which met current bacteriological standards, indicates that these standards do not reflect the occurrence of enteroviruses in mussels in the same water.","Concentration; Gastroenteritis virus; HAV; Mussels; Persistence",,"Atmar, R.L., Metcalf, T.G., Neill, F.H., Estes, M.K., Detection of enteric viruses in oysters by using the polimerase chain reaction (1993) Appl. Environ. Microbiol., 59, pp. 631-635; Bostock, A.D., Mepham, P., Phillips, S., Hepatitis A infection associated with the consumption of mussels (1979) J. Infect, 1, pp. 171-177; Desenclos, J.C.A., Klontz, K.C., Wilder, M.H., Nainan, O.V., Margolis, S., Gunn, R.A., A multistate outbreak of hepatitis A caused by the consumption of raw oysters (1991) Am. J. Public Health, 81, pp. 1268-1272; Dowell, S.F., Groves, C., Kirkland, K.B., Cicirello, H.G., Ando, T., Jin, Q., Gentsch, J.R., Glass, R.I., A multistate outbreak of oyster-associated gastroenteritis: Implications for interstate tracing of contaminated shellfish (1995) J. Inf. Dis., 171, pp. 1497-1503; Enriquez, R., Frosner, G.G., Hochstein-Mintzel, V., Riedemann, S., Reinhardt, G., Accumulation and persistence of hepatitis A virus in mussels (1992) J. Med. Virol., 37, pp. 174-179; G.U. no 7 del 11-1-'93; G.U. no 41 del 19-2-'92; G.U. no 203 del 26-7-'82; Garin, D., Fuchs, F., Crance, J.M., Rouby, Y., Chapalain, J.C., Lamarque, D., Gounot, A.M., Aymard, M., Exposure to enteroviruses and hepatitis A virus among divers in environmental waters in France, first biological and serological survey of a controlled cohort (1994) Epidemiol. Infect, 113, pp. 541-549; Gerba, C.P., Goyal, S.M., Labelle, R.L., Cech, I., Bodgan, G.F., Failure of indicator bacteria to reflect the occurence of enteroviruses in marine waters (1979) Am. J. Public Health, 69, pp. 1116-1119; Gill, O.N., Cubitt, W.D., Mcswiggan, D.A., Watney, B.M., Bartlett, C.L.R., Epidemic of gastroenteritis caused by oysters contaminated with small round structured viruses (1983) Br. Med. J., 287, pp. 1532-1534; Grohmann, G.S., Greenberg, H.B., Welch, B.M., Murphy, A.M., Oyster-associated gastroenteritis in Australia: The detection of Norwalk virus and its antibody by immune electron microscopy and radioimmunoassay (1980) J. Med. Virol., 6, pp. 11-19; Grohmann, G.S., Murphy, A.M., Christopher, P.J., Norwalk virus gastroenteritis in volunteers consuming depurated oysters (1981) Aust. J. Exp. Biol. Med. Sci., 59 (2 PART), pp. 219-228; Gunn, R.A., Janowski, H.T., Lieb, S., Prather, E.C., Greenberg, H.B., Norwalk virus gastroenteritis following raw oyster consumption (1982) Am. J. Epid., 115, pp. 348-351; Halliday, M.L., Kang, L.Y., Zhou, T.K., Hu, M.D., Pan, Q.C., Fu, T.Y., Huang, Y.S., Hu, S.L., An epidemic of hepatitis A attributable to the ingestion of raw clams in Shanghai, China (1991) J. Infect. Dis., 164, pp. 852-859; Kohn, M.A., Farley, T.A., Ando, T., Curtis, M., Wilson, S.A., Jin, Q., Monroe, S.S., Glass, R.I., An outbreak of Norwalk virus gastroenteritis associated with eating raw oysters. Implications for maintaining safe oyster beds (1995) JAMA, 273, pp. 466-471; Le Guyader, F., Dubois, E., Menard, D., Pommepuy, M., Detection of hepatitis A, rotavirus, and enterovirus in naturally contaminated shellfish and sediment by reverse transcription-seminested PCR (1994) Appl. Environ. Microbiol., 60, pp. 3665-3671; Lewis, D., Lightfoot, N., Pether, J., Solid-phase immune electron microscopy with human immunoglobulin M for serotyping of Norwalk-life viruses (1988) J. Clinical Microbiol., 26 (5), pp. 938-942; Mele, A., Rastelli, M.G., Gill, O.N., Di Bisceglie, D., Rosmini, F., Pardelli, G., Valtriani, C., Patriarchi, P., Recurrent epidemic hepatitis A associated with consumption of raw shellfish, probably controlled through public health measures (1989) Am. J. Epidemiol., 130, pp. 540-546; (1993) Multistate Outbreak of Viral Gastroenteritis Related to Consumption of Oysters-Louisiana, Maryland, Mississipi, and North Carolina, 42, pp. 945-948. , 1993; Multistate outbreak of viral gastroenteritis related to consumption of oysters-1993 (1994) JAMA, 271, pp. 183-185; (1994) Viral Gastroenteritis Associated with Consumption of Raw Oysters-Florida, 43 (24), pp. 446-449. , 1993; Multistate outbreak of viral gastroenteritis associated with consumption of oysters-Apalachicola Bay (1995) JAMA, 273, p. 452. , Florida, december 1994-january 1995; Sigari, G., Losi, E., Lo Monaco, R., Cuneo Crovari, P., (1995) Ruolo Dell'acqua Quale Veicolo di Infezione Delle Gastrointeriti Virali, pp. 455-464. , A / VIII Congrsso Internazionale Igiene dell'ambiente e del territorio (Isola Capo Rizzuto); Sigari, G., Losi, E., Cuneo Crovari, C., An electron microscopical investigation of small round viruses in non-bacterial gastroenteritis (1997) J. Biol. Res., 73 (1-2), pp. 31-38; Wyer, M.D., Fleisher, J.M., Gough, J., Kay, D., Merrett, H., An investigation into parametric relationships between enterovirus and faecal indicator organisms in the coasta waters of England and Wales (1995) Water Res., 29, pp. 1863-1868","Sigari, G.; Sezione di Igiene e Med. Preventiva, Dipartimento di Scienze della Salute, Univ. degli Studi di Genova, Via Pastore, 1, 16132 Genova, Italy",,,00191655,,IGMPA,,"Italian","Ig. Mod.",Article,"Final",,Scopus,2-s2.0-0039622698
"O'Connor J.B., Brian D.A.","55433538800;7006460232;","The major product of porcine transmissible gastroenteritis coronavirus gene 3b is an integral membrane glycoprotein of 31 kDa",1999,"Virology","256","1",,"152","161",,8,"10.1006/viro.1999.9640","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033616516&doi=10.1006%2fviro.1999.9640&partnerID=40&md5=e1b7df1dfb9fd55610f21d0773828f78","Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States","O'Connor, J.B., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States","The open reading frame potentially encoding a polypeptide of 27.7 kDa and located as the second of three ORFs (gene 3b) between the S and M genes in the genome of the Purdue strain of porcine transmissible gastroenteritis coronavirus (TGEV) was cloned and expressed in vitro to examine properties of the protein. Gene 3b has a postulated role in pathogenesis, but its truncated form in some laboratory-passaged strains of TGEV has led to the suggestion that it is not essential for virus replication. During synthesis in vitro in the presence of microsomes, the 27.7-kDa polypeptide became an integral membrane protein, retained its postulated hydrophobic N-terminal signal sequence, and underwent glycosylation on apparently two asparagine linkage sites to attain a final molecular mass of 31 kDa. A 20-kDa N-terminally truncated, nonglycosylated, nonanchored form of the protein was also made via an unknown mechanism. The existence of both transmembrane and soluble forms of the gene 3 product in the cell is suggested by immunofluorescence patterns showing both a punctated perinuclear and diffuse intracytoplasmic distribution. No gene 3b product was found on gradient-purified Purdue TGEV by a Western blotting procedure that would have detected as few as 4 molecules/virion, indicating the protein probably is not a structural component of the virion.",,"asparagine; gene product; membrane protein; signal peptide; virus protein; amino terminal sequence; article; Coronavirus; immunofluorescence; molecular weight; nonhuman; open reading frame; priority journal; protein glycosylation; protein synthesis; virus gene; virus pathogenesis; virus replication","Anderson, D.J., Blobel, G., Immunoprecipitation of proteins from cell-free translations (1983) Methods Enzymol, 96, pp. 111-120; Bergmann, C.C., Maass, D., Poruchynsky, M.S., Atkinson, P.H., Bellamy, A.R., Topology of the non-structural rotavirus receptor glycoprotein in the rough endoplasmic reticulum (1989) EMBO J., 8, pp. 1695-1703; Brian, D.A., Dennis, D.E., Guy, J.S., Genome of porcine transmissible gastroenteritis virus (1980) J. 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Virol., 105, pp. 165-178; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Cavanagh, D., Brian, D.A., Enjuanes, L., Holmes, K.V., Lai, M.M.C., Laude, H., Siddell, S.G., Talbot, P.J., Recommendations of the coronavirus study group for the nomenclature of the structural proteins, mRNAs and genes of coronaviruses (1990) Virology, 176, pp. 306-307; Chen, C.-M., Cavanagh, D., Britton, P., Cloning and sequencing of a 8.4 kb region from the 3′ end of a Taiwanese virulent field isolate of the coronavirus transmissible gastroenteritis virus (TGEV) (1995) Virus Res., 38, pp. 83-89; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF (1994) Virology, 198, pp. 466-476; Engelman, D.M., Steitz, T.A., Goldman, A., Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins (1986) Annu. Rev. Biophys. Biophys. Chem., 15, pp. 321-353; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology (1995) The Coronaviridae, , New York: Plenum. p. 337-376; Fujiki, Y., Hubbard, A.L., Fowler, S., Lazarow, P.B., Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum (1982) J. Cell Biol., 93, pp. 97-102; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF 4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Hogue, B.G., King, B., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J. Virol., 51, pp. 384-388; Horshburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. 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Eng., 10, pp. 1-6; Page, K.W., Mawditt, K.L., Britton, P., Sequence comparison of the 5′ end of mRNA 3 from transmissible gastroenteritis virus and porcine respiratory coronavirus (1991) J. Gen. Virol., 72, pp. 579-587; Titus, D., (1991) Promega Protocols and Application Guide, , Promega Corporation, Madison, WI; Queen, C., Korn, L.J., A comprehensive sequence analysis program for the IBM personal computer (1984) Nucleic Acids Res., 12, pp. 581-599; Raabe, T., Siddell, S., Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 and mRNA 5 unique regions (1989) Nucleic Acids Res., 14, p. 6387; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochimie (Paris), 69, pp. 591-600; Risco, C., Anton, I.M., Sune, C., Pedregosa, A.M., Martin-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, , Ames: Iowa State University Press. p. 362-386; Senanayake, S.D., Brian, D.A., Precise large deletions by the PCR-based overlap extension method (1995) Molecular Bio/Technology, 4, pp. 13-15; Sethna, P.B., Brian, D.A., Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes (1997) J. 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Biochem., 133, pp. 17-21; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Brian, D.A.; Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,"Academic Press Inc.",00426822,,VIRLA,"10087235","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0033616516
"Stephensen C.B., Casebolt D.B., Gangopadhyay N.N.","7005417177;6602311055;56694672100;","Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay",1999,"Virus Research","60","2",,"181","189",,99,"10.1016/S0168-1702(99)00017-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032972895&doi=10.1016%2fS0168-1702%2899%2900017-9&partnerID=40&md5=c7aded187b3ded6ed2985b828645c792","Department of International Health, Sch. Pub. Hlth., Univ. Alabama B., Birmingham, AL 35294, United States; Department of Comparative Medicine, University of Alabama at Birmingham, Birmingham, AL 95616, United States","Stephensen, C.B., Department of International Health, Sch. Pub. Hlth., Univ. Alabama B., Birmingham, AL 35294, United States; Casebolt, D.B., Department of Comparative Medicine, University of Alabama at Birmingham, Birmingham, AL 95616, United States; Gangopadhyay, N.N., Department of International Health, Sch. Pub. Hlth., Univ. Alabama B., Birmingham, AL 35294, United States","Viruses in the genus Coronavirus are currently placed in three groups based on antigenic cross-reactivity and sequence analysis of structural protein genes. Consensus polymerase chain reaction (PCR) primers were used to obtain cDNA, then cloned and sequenced a highly conserved 922 nucleotide region in open reading frame (ORF) 1b of the polymerase (pol) gene from eight coronaviruses. These sequences were compared with published sequences for three additional coronaviruses. In this comparison, it was found that nucleotide substitution frequencies (per 100 nucleotides) varied from 46.40 to 50.13 when viruses were compared among the traditional coronavirus groups and, with one exception (the human coronavirus (HCV) 229E), varied from 2.54 to 15.89 when compared within these groups. (The substitution frequency for 229E, as compared to other members of the same group, varied from 35.37 to 35.72.) Phylogenetic analysis of these pol gene sequences resulted in groupings which correspond closely with the previously described groupings, including recent data which places the two avian coronaviruses-infectious bronchitis virus (IBV) of chickens and turkey coronavirus (TCV)-in the same group [Guy, J.S., Barnes, H.J., Smith L.G., Breslin, J., 1997. Avian Dis. 41:583-590]. A single pair of degenerate primers was identified which amplify a 251 bp region from coronaviruses of all three groups using the same reaction conditions. This consensus PCR assay for the genus Coronavirus may be useful in identifying as yet unknown coronaviruses. Copyright (C) 1999 Elsevier Science B.V.","Consensus PCR; Coronavirus; Polymerase gene","complementary DNA; primer DNA; article; avian infectious bronchitis virus; chicken; consensus sequence; controlled study; coronavirus; gene sequence; molecular cloning; nonhuman; phylogeny; polymerase chain reaction; priority journal; sequence analysis; structural gene; turkey (bird); Amino Acid Sequence; Animals; Base Sequence; Conserved Sequence; Coronavirus; Coronavirus 229E, Human; DNA, Complementary; Evolution, Molecular; Genes, pol; Humans; Molecular Sequence Data; Phylogeny; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid","Astori, G., Arzese, A., Pipan, C., De Villiers, E.M., Botta, G.A., Characterization of a putative new HPV genomic sequence from a cervical lesion using L1 consensus primers and restriction fragment length polymorphism (1997) Virus Res., 50, pp. 57-63; Bernard, H.U., Chan, S.Y., Manos, M.M., Ong, C.K., Villa, L.L., Delius, H., Peyton, C.L., Wheeler, C.M., Identification and assessment of known and novel human papillomaviruses by polymerase chain reaction amplification, restriction fragment length polymorphisms, nucleotide sequence, and phylogenetic algorithms (1994) J. 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Fields, D.M. Knipe, & P.M. Howley. New York: Raven Press; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., Lamonica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Myint, S.H., Human coronavirus infections (1995) The Coronaviridae, pp. 389-402. , S.G. Siddell. 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Virol., 72, pp. 1659-1666","Stephensen, C.B.; Department of Nutrition, 3243 Meyer Hall, University of California, One Shields Avenue, Davis, CA 95616, United States; email: cstephensen@ucdavis.edu",,,01681702,,VIRED,"10392726","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0032972895
"Arbour N., Ekandé S., Côté G., Lachance C., Chagnon F., Tardieu M., Cashman N.R., Talbot P.J.","6602762564;6504317670;8776263100;57210675095;57196797991;55412346900;16169124200;7102670281;","Persistent infection of human oligodendrocytic and neuroglial cell lines by human coronavirus 229E",1999,"Journal of Virology","73","4",,"3326","3337",,54,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033052720&partnerID=40&md5=5bb99bb4bf387d74a63bcacf9e35ff2f","Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Laboratoire de Neurovirologie, Université Paris XI, Kremlin Bicêtre, France; Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Que. H3A 2B4, Canada; INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Arbour, N., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Ekandé, S., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Côté, G., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Lachance, C., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Chagnon, F., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Tardieu, M., Laboratoire de Neurovirologie, Université Paris XI, Kremlin Bicêtre, France; Cashman, N.R., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Que. H3A 2B4, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Human coronaviruses (HuCV) cause common colds. Previous reports suggest that these infectious agents may be neurotropic in humans, as they are for some mammals. With the long-term aim of providing experimental evidence for the neurotropism of HuCV and the establishment of persistent infections in the nervous system, we have evaluated the susceptibility of various human neural cell lines to acute and persistent infection by HuCV-229E. Viral antigen, infectious virus progeny and viral RNA were monitored during both acute and persistent infections. The astrocytoma cell lines U-87 MG, U-373 MG, and GL-15, as well as neuroblastoma SK-N-SH, neuroglioma H4, and oligodendrocytic MO3.13 cell lines, were all susceptible to an acute infection by HuCV-229E. The CHME-5 immortalized fetal microglial cell line was not susceptible to infection by this virus. The MO3.13 and H4 cell lines also sustained a persistent viral infection, as monitored by detection of viral antigen and infectious virus progeny. Sequencing of the S1 gene from viral RNA after ~130 days of infection showed two point mutations, suggesting amino acid changes during persistent infection of MO3.13 cells but none for H4 cells. Thus, persistent in vitro infection did not generate important changes in the S1 portion of the viral spike protein, which was shown for murine coronaviruses to bear hypervariable domains and to interact with cellular receptor. These results are consistent with the potential persistence of HuCV-229E in cells of the human nervous system, such as oligodendrocytes and possibly neurons, and the virus's apparent genomic stability.",,"virus RNA; amino acid substitution; antigen detection; article; astrocyte; cell line; controlled study; coronavirus; gene amplification; glia cell; human; human cell; microglia; neurotropism; nonhuman; nucleotide sequence; oligodendroglia; persistent virus infection; point mutation; priority journal; sequence analysis; virus genome; Astrocytoma; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Disease Susceptibility; Glioma; Humans; Neuroblastoma; Oligodendroglia; Organ Specificity; Tumor Cells, Cultured","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, K., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Arbour, N., Côté, G., Lachance, C., Tardieu, M., Cashman, N.R., Talbot, P.J., Acute and persistent infection of human neural cell lines by human coronavirus OC43 (1999) J. 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Virol., 78, pp. 747-756; Sun, N., Grzybicki, D., Castro, R.F., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Sun, N., Perlman, S., Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes (1995) J. Virol., 69, pp. 633-641; Taguchi, F., Massa, P.T., Ter Meulen, V., Characterization of a variant virus isolated from neural cell culture after infection of mouse coronavirus JHMV (1986) Virology, 155, pp. 267-270; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brains after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; Takahashi, K., Goto, N., Ishida, T., Katami, K., Fujiwara, K., Acute demyelination in mice inoculated intraspinally with mouse hepatitis virus. JHM strain (1981) Jpn. J. Exp. Med., 51, pp. 323-330; Talbot, P.J., Dionne, G., Lacroix, M., Vaccination against lethal coronavirus-induced encephalitis with a synthetic decapcptide homologous to a domain in the predicted peplomer stalk (1988) J. Virol., 62, pp. 3032-3036; Talbot, P.J., Salmi, A.A., Knobler, R.L., Buchmeier, M.J., Topographical mapping of epitopes on the glycoproteins of murine hepatitis virus-4 (strain JHM): Correlation with biological activities (1984) Virology, 131, pp. 250-260; Talbot, P.J., Ékandé, S., Cashman, N.R., Mounir, S., Stewart, J.N., Neurotropism of human coronavirus 229E (1994) Adv. Exp. Med. Biol., 342, pp. 339-346; Talbot, P.J., Paquette, J.S., Ciurli, C., Antel, J.P., Ouellet, F., Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis (1996) Ann. Neurol., 39, pp. 233-240; Tardieu, M., Boespflug, O., Barbé, T., Selective tropism of a neurotropic coronavirus for ependymal cells, neurons, and meningeal cells (1986) J. Virol., 60, pp. 574-582; Watanabe, R., Wege, H., Ter Meulen, V., Comparative analysis of coronavirus JHM-induced demyelinating encephalomyelitis in Lewis and Brown Norway rats (1987) Lab. Investig., 57, pp. 375-384; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Talbot, P.J.; INRS, Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,,0022538X,,JOVIA,"10074187","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0033052720
"Arbour N., Côté G., Lachance C., Tardieu M., Cashman N.R., Talbot P.J.","6602762564;8776263100;57210675095;55412346900;16169124200;7102670281;","Acute and persistent infection of human neural cell lines by human coronavirus OC43",1999,"Journal of Virology","73","4",,"3338","3350",,65,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344859876&partnerID=40&md5=fbff0e3f5f7debca985925088aea5ef1","Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Laboratoire de Neurovirologie, Université Paris XI, Kremlin Bicêtre, France; Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Que. H3A 2B4, Canada; INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Arbour, N., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Côté, G., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Lachance, C., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada; Tardieu, M., Laboratoire de Neurovirologie, Université Paris XI, Kremlin Bicêtre, France; Cashman, N.R., Neuroimmunology Unit, Montreal Neurological Institute, McGill University, Montréal, Que. H3A 2B4, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Human Health Research Center, University of Quebec, Laval, Que. H7V 1B7, Canada, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Human coronaviruses (HuCV) are recognized respiratory pathogens. Data accumulated by different laboratories suggest their neurotropic potential. For example, primary cultures of human astrocytes and microglia were shown to be susceptible to an infection by the OC43 strain of HuCV (A. Bonavia, N. Arbour, V. W. Yong, and P. J. Talbot, J. Virol. 71:800-806, 1997). We speculate that the neurotropism of HuCV will lead to persistence within the central nervous system, as was observed for murine coronaviruses. As a first step in the verification of our hypothesis, we have characterized the susceptibility of various human neural cell lines to infection by HuCV-OC43. Vital antigen, infectious virus progeny, and viral RNA were monitored during both acute and persistent infections. The astrocytoma cell lines U-87 MG, U- 373 MG, and GL-15, as well as neuroblastoma SK-N-SH, neuroglioma H4, oligodendrocytic MO3.13, and the CHME-5 immortalized fetal microglial cell lines, were all susceptible to an acute infection by HuCV-OC43. Viral antigen and RNA and release of infectious virions were observed during persistent HuCV-OC43 infections (~130 days of culture) of U-87 MG, U-373 MG, MO3.13, and H4 cell lines. Nucleotide sequences of RNA encoding the putatively hypervariable viral S1 gene fragment obtained after 130 days of culture were compared to that of initial virus input. Point mutations leading to amino acid changes were observed in all persistently infected cell lines. Moreover, an in-frame deletion was also observed in persistently infected H4 cells. Some point mutations were observed in some molecular clones but not all, suggesting evolution of the viral population and the emergence of viral quasispecies during persistent infection of H4, U-87 MG, and MO3.13 cell lines. These results are consistent with the potential persistence of HuCV- OC43 in cells of the human nervous system, accompanied by the production of infectious virions and molecular variation of vital genomic RNA.",,"monoclonal antibody; virus antigen; antigen detection; article; astrocyte; astrocytoma cell; cell line; controlled study; coronavirus; human; human cell; infection sensitivity; microglia; nerve cell; neurotropism; nonhuman; nucleotide sequence; oligodendroglia; persistent infection; point mutation; priority journal; virion; virus genome; virus infection; virus particle; Cell Line; Coronavirus; Coronavirus Infections; Coronavirus OC43, Human; Disease Susceptibility; Genome, Viral; Humans; Nerve Tissue; Point Mutation; Variation (Genetics)","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Ahmed, R., Hahn, C.S., Somasundaram, T., Villarete, L., Matloubian, M., Strauss, J.H., Molecular basis of organ-specific selection of viral variants during chronic infection (1991) J. 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Virol., 60, pp. 574-582; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Semin. Immunopathol., 17, pp. 133-148; Wege, H., Winter, J., Meyermaan, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J. Gen. Virol., 69, pp. 87-98; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199","Talbot, P.J.; INRS, Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@iaf.uquebec.ca",,,0022538X,,JOVIA,"10074188","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0344859876
"Tibbles K.W., Cavanagh D., Brown T.D.K.","6507790687;26642890500;56248391000;","Activity of a purified His-tagged 3C-like proteinase from the coronavirus infectious bronchitis virus",1999,"Virus Research","60","2",,"137","145",,7,"10.1016/S0168-1702(99)00011-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033010840&doi=10.1016%2fS0168-1702%2899%2900011-8&partnerID=40&md5=4b408bd5ed706775e723e3b4f1ee2028","Division of Virology, Dept. Pathol., Univ. Cambridge, T., Cambridge, United Kingdom; Institute for Animal Health, Compton Laboratory, Berks RG20 7NN, Newbury, United Kingdom","Tibbles, K.W., Division of Virology, Dept. Pathol., Univ. Cambridge, T., Cambridge, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Berks RG20 7NN, Newbury, United Kingdom; Brown, T.D.K., Division of Virology, Dept. Pathol., Univ. Cambridge, T., Cambridge, United Kingdom","Previous studies in vitro of the processing of cloned polyprotein fragments from the coronavirus infectious bronchitis virus (IBV) large open reading frame (ORF1), confirmed the activity of a predicted 3C-like proteinase (3CLP) domain and suggested that the proteinase is released autocatalytically from the polyprotein in the form of a 35 kDa protein, 3CLpro, capable of further cleavages in trans. In order to identify such cleavages within the ORF1 polyprotein mediated by 3CLpro, the proteinase was expressed in bacteria, purified and used in trans cleavage assays with polyprotein fragments lacking the 3CLP domain as targets. The proteinase was expressed as a polyprotein fragment which was able to process during expression in bacterial cells, releasing mature 3CLpro. A histidine (His6) tag was introduced close to the C-terminus of the proteinase to aid purification. Processing demonstrated by the tagged proteinase was indistinguishable from that of the wild-type enzyme indicating that the site chosen for the tag was permissive. From these studies we were able to demonstrate trans cleavages consistent with the use of most of the previously predicted or identified sites within the open reading frame of gene 1. This tentatively completes the processing map for the ORF1 region with respect to 3CLpro. Copyright (C) 1999 Elsevier Science B.V.","3CLproteinase; Bacterial expression; Coronavirus; His-tagged; Trans processing","histidine; protein; proteinase; virus enzyme; article; avian infectious bronchitis virus; bacterium; carboxy terminal sequence; controlled study; coronavirus; enzyme activity; enzyme purification; nonhuman; priority journal; protein degradation; protein expression; protein processing; Animals; Binding Sites; Catalysis; Cysteine Endopeptidases; Escherichia coli; Gene Expression Regulation, Enzymologic; Histamine; Infectious bronchitis virus; Mutagenesis, Site-Directed; Protein Processing, Post-Translational; Proteins; Recombinant Proteins; Viral Proteins","Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57 (4), pp. 537-547; Brown, T.D.K., Brierley, I., The coronavirus non-structural proteins (1995) The Coronaviridae, pp. 191-217. , S.G. Siddell. New York: Plenum Press; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids. Res., 17 (12), pp. 4847-4861; Grotzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E (1996) Virology, 222 (1), pp. 227-235; Herold, J., Raabe, T., Schelle Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195 (2), pp. 680-691; Heusipp, G., Grotzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78, pp. 2789-2794; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., 71 (7), pp. 5631-5634; Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein (1982) J. Mol. Biol., 157 (1), pp. 105-132; Lama, J., Carrasco, L., Screening for membrane-permeabilizing mutants of the poliovirus protein 3AB (1996) J. Gen. Virol., 77 (9), pp. 2109-2119; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180 (2), pp. 567-582; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68 (9), pp. 5772-5780; Liu, D.X., Shen, S., Xu, H.Y., Wang, S.F., Proteolytic mapping of the coronavirus infectious bronchitis virus 1b polyprotein: Evidence for the presence of four cleavage sites of the 3C-like proteinase and identification of two novel cleavage products (1998) Virology, 246, pp. 288-297; Liu, D.X., Tibbles, K.W., Cavanagh, D., Brown, T.D.K., Brierley, I., Identification, expression, and processing of an 87-kDa polypeptide encoded by ORF 1a of the coronavirus infectious bronchitis virus (1995) Virology, 208, pp. 48-57; Liu, D.X., Xu, H.Y., Brown, T.D., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71 (3), pp. 1814-1820; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 2, pp. 375-382. , issn: 0042-6822; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69 (6), pp. 3554-3559; Netzer, W.J., Hartl, F.U., Recombination of protein domains facilitated by co-translational folding in eukaryotes (1997) Nature, 388 (6640), pp. 343-349; Ng, L.F., Liu, D.X., Identification of a 24-kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites (1998) Virology, 243 (2), pp. 388-395; Ryan, M.D., Flint, M., Virus-encoded proteinases of the picornavirus super-group (1997) J. Gen. Virol., 78 (4), pp. 699-723; Seybert, A., Ziebuhr, J., Siddell, S.G., Expression and characterization of a recombinant murine coronavirus 3C-like proteinase (1997) J. Gen. Virol., 78 (1), pp. 71-75; Smith, D.B., Johnson, K.S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase (1988) Gene, 67 (1), pp. 31-40; Studier, F.W., Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system (1991) J. Mol. Biol., 219 (1), pp. 37-44; Studier, F.W., Rosenberg, A.H., Dunn, J.J., Dubendorff, J.W., Use of T7 RNA polymerase to direct expression of cloned genes (1990) Methods Enzymol., 185, pp. 60-89; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70 (3), pp. 1923-1930; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., A region of the infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate (1995) J. Gen. Virol., 76, pp. 3059-3070; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69 (7), pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71 (5), pp. 3992-3997","Tibbles, K.W.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; email: kwt@mole.bio.cam.ac.uk",,,01681702,,VIRED,"10392722","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0033010840
"Teng H., Piñón J.D., Weiss S.R.","55424332900;35870444000;57203567044;","Expression of murine coronavirus recombinant papain-like proteinase: Efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides",1999,"Journal of Virology","73","4",,"2658","2666",,23,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344628701&partnerID=40&md5=4ee9d5380386ad4c576cec6fc7ee5978","Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Department of Microbiology, University of Pennsylvania, School of Medicine, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Teng, H., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Piñón, J.D., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States, Department of Microbiology, University of Pennsylvania, School of Medicine, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Proteolytic processing of the replicase gene product of mouse hepatitis virus (MHV) is essential for viral replication. In MHV strain A59 (MHV-A59), the replicase gene encodes two predicted papain-like proteinase (PLP) domains, PLP-1 and PLP-2. Previous work using vital polypeptide substrates synthesized by in vitro transcription and translation from the replicase gene demonstrated both cis and trans cleavage activities for PLP-1. We have cloned and overexpressed the PLP-1 domain in Escherichia coli by using a T7 RNA polymerase promoter system or as a maltose-binding protein (MBP) fusion protein. With both overexpression systems, the recombinant PLP-1 exhibited trans cleavage activity when incubated with in vitro-synthesized vital polypeptide substrates. Subsequent characterization of the recombinant PLP-1 revealed that in vitro trans cleavage is more efficient at 22°C than at higher temperatures. Using substrates of increasing lengths, we observed efficient cleavage by PLP-1 requires a substrate greater than 69 kDa. In addition, when PLP-1 was expressed as a polypeptide that included additional viral sequences at the carboxyl terminus of the predicted PLP-1 domain, a fivefold increase in proteolytic activity was observed. The data presented here support previous data suggesting that in vitro and in vivo cleavage of the ORF 1a polyprotein by PLP-1 can occur in both in cis and in trans. In contrast to the cleavage activity demonstrated for PLP-1, no in vitro cleavage in cis or in trans could be detected with PLP-2 expressed either as a polypeptide, including flanking vital sequences, or as an MBP fusion enzyme.",,"hybrid protein; maltose binding protein; papain like proteinase; proteinase; recombinant protein; unclassified drug; article; carboxy terminal sequence; DNA cleavage; enzyme purification; enzyme substrate complex; escherichia coli; gene replication; murine hepatitis coronavirus; nonhuman; priority journal; promoter region; protein analysis; protein degradation; protein expression; protein synthesis; site directed mutagenesis; virus replication; Animals; Base Sequence; Cloning, Molecular; Coronavirus; Mice; Molecular Sequence Data; Papain; Recombinant Proteins; Substrate Specificity","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1987) Current Protocols in Molecular Biology, pp. 1011-1013. , Greene Publishing Associates and Wiley-Interscience, New York, N.Y; Baker, S.C., Shieh, C.K., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene a polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenja, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like proteinase of murine coroavirus (1993) J. Virol., 67, pp. 6056-6063; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Piñón, J.D., Weiss, S.R., Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus MHV-A59 (1997) J. Virol., 71, pp. 900-909; Den Boon, J.A., Faaberg, K.S., Meulenberg, J.J.M., Wassenaar, A.L.M., Plagemann, P.G.W., Gorbalenya, A.E., Snijder, E.J., Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: Identification of two papain-like cysteine proteases (1995) J. Virol., 69, pp. 4500-4505; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Denison, M.R., Kim, J.C., Ross, T., Inhibition of coronavirus MHV-A59 replication by proteinase inhibitors (1995) Corona- and Related Viruses, pp. 391-397. , P. J. Talbot and G. A. Levy (ed.). Plenum Press, New York, N.Y; Denison, M.R., Perlman, S., Translation and processing of mouse hepatitis virus virion RNA in a cell-free system (1986) J. Virol., 60, pp. 12-18; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Dong, S., Baker, S.C., Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Gao, H.-Q., Schiller, J.J., Baker, S.C., Identification of the polymerase polyprotein products p72 and p65 of the murine coronavirus MHV-JHM (1996) Virus Res., 45, pp. 101-109; Gorbalenya, A.E., Koonin, E.V., Comparative analysis of amino-acid sequences of key enzymes of replication and expression of positive-strand RNA viruses: Validity of approach and functional and evolutionary implications (1993) Sov. Sci. Rev. Sect. D, 11, pp. 1-84; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Snijder, E.J., Viral cysteine proteinases (1996) Perspect. Drug Discov. Des., 6, pp. 64-86; Hardy, W.R., Strauss, J.H., Processing the nonstructural polypeptides of Sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and trans (1989) J. Virol., 63, pp. 4653-4664; Herold, J., Gorbalenya, A.E., Thiel, V., Schelle, B., Siddell, S.G., Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate (1998) J. Virol., 72, pp. 910-918; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d (1995) Virology, 208, pp. 1-8; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., LaMonica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence of the murine coronavirus gene 1 encoding the putative protease and RNA polymerase (1991) Virology, 180, pp. 567-582; Lim, K.P., Liu, D.X., Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein (1998) Virology, 245, pp. 303-312; Medina, M., Domingo, E., Brangwyn, J.K., Belsham, G.J., The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities (1993) Virology, 194, pp. 355-359; Nagal, K., Thøgersen, H.C., Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli (1987) Methods Enzymol., 153, pp. 461-481; Rodríguez, P.L., Carrasco, L., Improved factor Xa cleavage of fusion proteins containing maltose binding protein (1995) BioTechniques, 18, pp. 238-243; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Snijder, E.J., Meulenberg, J.J.M., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Studier, W.F., Rosenberg, A.H., Dunn, J.J., Dubendorf, J.W., Use of T7 polymerase to direct the expression of cloned genes (1990) Methods Enzymol., 185, pp. 60-89; Weiss, S.R., Hughes, S.A., Bonilla, P.J., Leibowitz, J.L., Denison, M.R., Coronavirus polyprotein processing (1994) Arch. Virol., 9, pp. 349-358","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"10074111","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0344628701
"Daginakatte G.C., Chard-Bergstrom C., Andrews G.A., Kapil S.","6506142137;6602711643;7202160819;7003293348;","Production, characterization, and uses of monoclonal antibodies against recombinant nucleoprotein of elk coronavirus",1999,"Clinical and Diagnostic Laboratory Immunology","6","3",,"341","344",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032912383&partnerID=40&md5=6c740408cc1000df9c25098e6406721a","Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Manhattan, KS 66506, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, 1800 Denison Ave., Manhattan, KS 66506, United States","Daginakatte, G.C., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Manhattan, KS 66506, United States; Chard-Bergstrom, C., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Manhattan, KS 66506, United States; Andrews, G.A., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Manhattan, KS 66506, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Manhattan, KS 66506, United States, Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, 1800 Denison Ave., Manhattan, KS 66506, United States","This is the first report of the production of monoclonal antibodies against elk coronavirus. The nucleoprotein gene of elk coronavirus was amplified by PCR and was cloned and expressed in a prokaryotic expression vector. Recombinant nucleocapsid protein was used to immunize mice for the production of hybridomas. Twelve hybridomas that produced monoclonal antibodies against the nucleocapsid protein of elk coronavirus were selected by an indirect fluorescent-antibody test, an enzyme-linked immunosorbent assay, and a Western blot assay. Ten of the monoclonal antibodies were of the immunoglobulin G1 (IgG1) isotype, one was IgG2a, and one was IgM. All had kappa light chains. By immunohistochemistry four monoclonal antibodies detected bovine coronavirus and elk coronavirus in formalin-fixed intestinal tissues. Antinucleoprotein monoclonal antibodies were found to be better at ruminant coronavirus detection than the anti-spike protein monoclonal antibodies. Because nucleoprotein is a more abundant antigen than spike protein in infected cells, this was not an unexpected finding.",,"monoclonal antibody; nucleoprotein; virus antibody; antibody production; antigen antibody complex; article; coronavirus; enteritis; enzyme linked immunosorbent assay; gene amplification; gene expression; human; human cell; immunohistochemistry; open reading frame; pneumonia; priority journal; protein analysis; virus infection; Animals; Antibodies, Monoclonal; Antibodies, Viral; Blotting, Western; Cattle; Cattle Diseases; Colon; Coronavirus; Coronavirus Infections; Coronavirus, Bovine; Deer; Enzyme-Linked Immunosorbent Assay; Immunohistochemistry; Mice; Mice, Inbred BALB C; Nucleocapsid Proteins; Recombinant Proteins","Baszler, T.V., Evermann, J.F., Kaylor, P.S., Diagnosis of naturally occurring bovine viral diarrhea virus infections in ruminants using monoclonal antibody-based immunohistochemistry (1995) Vet. Pathol., 32, pp. 609-618; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 49, pp. 51-70; Corapi, W.V., Darteil, R.J., Audonnet, J.C., Chappuis, G.E., Localization of antigenic sites of feline infectious peritonitis virus involved in neutralization and antibody-dependent enhancement (1995) J. Virol., 69, pp. 2858-2862; Crouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture enzyme-linked immunosorbent assay for detection of bovine enteric coronavirus (1984) J. Clin. Microbiol., 19, pp. 388-393; Dar, A.M., Kapil, S., Goyal, S.M., Comparison of immunohistochemistry, electron microscopy, and direct fluorescent antibody test for the detection of bovine coronavirus (1998) J. Vet. Diagn. Invest., 10, pp. 152-157; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Guy, J.S., Brian, D.A., Bovine coronavirus genome (1979) J. Virol., 29, pp. 293-300; Kapil, S., Chard-Bergstrom, C., Bolin, P., Landers, D., Plaque variations in clinical isolates of bovine coronavirus (1995) J. Vet. Diagn. Invest., 7, pp. 538-539; Kapil, S., Richardson, K.L., Radi, C., Chard-Bergstrom, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J. Vet. Diagn. Invest., 8, pp. 96-99; King, B., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Majhdi, F., Minocha, H.C., Kapil, S., Isolation and characterization of a coronavirus from elk calves with diarrhea (1997) J. Clin. Microbiol., 35, pp. 2937-2942; Nakanaga, K., Yamanouchi, K., Fujiwara, K., Protective effect of monoclonal antibodies on lethal mouse hepatitis virus infection in mice (1986) J. Virol., 59, pp. 168-171; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-112; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Reed, H.H., Saif, L.J., Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J. Clin. Microbiol., 33, pp. 3264-3269; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Minocha, H.C., Kapil, S., Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalin-fixed intestines (1997) J. Clin. Microbiol., 35, pp. 2964-2965","Kapil, S.; Dept. of Diagnostic Med.-Pathobiol., College of Veterinary Medicine, 1800 Denison Ave., Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,1071412X,,CDIME,"10225833","English","Clin. Diagn. Lab. Immunol.",Article,"Final",,Scopus,2-s2.0-0032912383
"Gamet Y.","57214541220;","Feline infectious peritonitis 1-Etiology, epidemiology and pathogeny [La péritonite infectieuse féline 1-Etiologie, épidémiologie et pathogénie]",1999,"Point Veterinaire","30","199",,"269","272",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-17944386887&partnerID=40&md5=001363013b4a387f2a7983a12ab9f081","Cros de la Mûre, 84100 Uchaux, France","Gamet, Y., Cros de la Mûre, 84100 Uchaux, France","The coronavirus responsible for feline infectious peritonitis (FIPCo), is not antigenically detectable from feline enteric coronaviruses (FECo), therefore the serology tests have a poor diagnostic value The genetic study of coronaviruses tends to show that the FIPCo results from mutations of FECo. Transmission follows the orofaecal route Infection by FECo provokes the destruction of enterocytes. Often asymptomatic, it can induce digestive disorders, fever and neutropenia, The pathogen power of the FIPCo is linked with their particular capacity to infect macrophages (3 figures, 22 references).","Cat; Epidemiology; Feline infectious peritonitis; Pathogeny; Virus",,"Addie, D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; Addie, D., Risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) Am. J. Vet. Res., 56 (4), pp. 429-433; Addie, D., The risk of typical and antibody enhanced feline infectious peritonitis among cats from feline coronavirus endemic households (1995) Fel. Pract., 23 (3), pp. 24-26; Barlough, J., Cats, coronaviruses and coronavirus antibody tests (1985) J. Small Anim. Pract., 13, p. 567; Evermann, J., Henry, C., Marks, S., Feline infectious peritonitis (1995) J. Am. Vet. Med. Assoc., 206 (8), pp. 1130-1134; Fehr, D., Evaluation of the safety and efficacy of a modified live vaccine under field conditions (1995) Fel. Pract., 23 (3), pp. 83-88; Foley, J.E., Pedersen, N., The inheritance of susceptibility to feline infections peritonitis in purebred catteries (1996) Fel. Pract., 24, pp. 14-22; Foley, J.E., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Am. Vet. Med. Assoc., 210 (9), pp. 1307-1312; Foley, J.E., Risk factors for feline infectious peritonitis among cats in multiple-cat environments (1997) J. Am. Vet. Med. Assoc., 210 (9), pp. 1313-1318; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) J. Am. Vet. Med. Assoc., 209 (6), pp. 1117-1120; Hickman, M., Elimination of feline coronavirus infection from a large experimentale specific pathogen-free cat breeding colony by serologic testing and isolation (1995) Fel. Pract., 23 (3), pp. 96-102; Hohdatsu, T., The prevalence of type I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54 (3), pp. 557-562; Horzinek, M., Herrewegh, A., De Groot, R., Perspectives on feline coronavirus evolution (1995) Fel. Pract., 23 (3), pp. 34-38; Hoskins, J., Coronavirus infection in cats (1991) Comp. Cont. Educ. Pract. Vet., 3 (4), pp. 567-586; Hoskins, J.D., Update on feline coronavirus disease (1997) Consultations in Feline Internal Medicine, pp. 44-50. , August J.R., 1, Philadelphia, WB Saunders Co; Mc Ardle, F., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; Pedersen, N., The history and interpretation of feline coronavirus serology (1995) Fel.Pract., 23 (3), pp. 46-51; Pedersen, N., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Fel. Pract, 23 (3), pp. 7-20; Postorino Reeves, N., Vaccination against naturally occuring FIP in a single large cat shelter (1995) Fel. Pract., 23 (3), pp. 81-82; Scott, F., Olsen, C., Corapi, W., Antibody-dependent enhancement of feline infectious peritonitis virus infection (1995) Fel.Pract., 23 (3), pp. 77-80; Vennema, H., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Fel. Pract., 23 (3), pp. 40-44; Zenger, E., Newer diagnostic testing methodology for infectious agents (1997) Consultations in Feline Internal Medicine, pp. 37-43. , August J.R., Philadelphia, WB Saunders Co","Gamet, Y.; Cros de la Mûre, 84100 Uchaux, France",,,03354997,,,,"French","Point Vet.",Article,"Final",,Scopus,2-s2.0-17944386887
"Fradin-Ferme M., Prélaud P.","6508005746;7003722562;","Feline infectious peritonitis [La péritonite infectieuse féline]",1999,"Pratique Medicale et Chirurgicale de l'Animal de Compagnie","34","SUPPL. 3",,"309","319",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041708505&partnerID=40&md5=0a7afc01dd1061d746e8abc09abd3b8f","Clinique Vétérinaire, 85 ter Boulevard Soult, 75012 Paris, France; CERI, 8, rue de Saintonge, 75003 Paris, France","Fradin-Ferme, M., Clinique Vétérinaire, 85 ter Boulevard Soult, 75012 Paris, France; Prélaud, P., CERI, 8, rue de Saintonge, 75003 Paris, France","The absence of serologie tests capable of exhibiting anti-Coronavirus antibodies is an impediment for both practitioners in their diagnostic procedure and for breeders in the setting up of preventive measures. As it is, the modifications of biological parameters are clear enough and easy enough to be highlighted for the diagnosis of FIP disease to be easily implemented as a routine examination by using both a haemogramme and a protein electrophoresis, and by considering young cats either living together or having recently been subjected to stress or been exposed to animals presenting a risk. The sophisticated nature of the biological tests proposed has not led to a significant improvement of the diagnosis. Basically, in order to achieve the control and prevention of the infection, there must be screening tests for the detection of seropositive cats and stringent hygiene must be enforced in breeders' establishments and at shows.","Cat; Coronavirus; Electrophoresis; Feline infectious peritonitis; Peritonitis; Serology",,"Vennema, H., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Stoddart, M.E., The sites of early viral replication in feline infectious peritonitis (1988) Vet Microbiol, 18, pp. 259-271; Stoddart, M.E., Virus shedding and immune responses in cats inoculated with cell culture-adapted feline infectious peritonitis virus (1988) Vet Microbiol, 16, pp. 145-158; Pedersen, N.C., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) Amer J Vet Res, 42, pp. 368-376; Scott, F.W., The immune response to FIP in cats (1989) Feline Health Topics, 3, pp. 1-3; Kass, P.H., Dent, T.H., The epidemiology of feline infectious peritonitis in catteries (1995) Feline Pract, 23, pp. 27-32; McKiernan, A.J., Evermann, J.F., Isolation of feline coronaviruses from two cats with diverse disease manifestations (1981) Feline Pract, 11, pp. 16-20; Addie, D.D., Jarrett, O., A study of naturally occuring feline coronavirus infections in kittens (1992) Vet Record, 130, pp. 133-137; Herrewegh, A.A.P.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv Exp Med Biol, 218, pp. 529-550; Pedersen, N.C., Animal virus infections that defy vaccination: Equine infectious anemia, caprine arthritis-encephalitis, maedi-visna, and feline infectious peritonitis (1989) Adv Vet Sci Comp Med, 33, pp. 413-428; Ingersoll, J.D., Wylie, D.E., Identification of virual antigens that induce antibody responses on exposure to coronaviruses (1988) Amer J Vet Res, 49, pp. 1467-1471; Gonon, V., Eloit, M., Péritonite infectieuse féline (1998) Médecine Générale, p. 1700. , Encyclopédie Vétérinaire, Elsevier, Paris; Foley, J.E., Risk factors for feline infectious peritonitis among cats in multiple cat environments with endemic feline enteric coronavirus (1997) J Amer Vet Med Assn, 210, pp. 1313-1318; Pedersen, N.C., An overview of feline enteritic coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-19; Foley, J., Pedersen, N.C., The inheritance susceptibility in feline infectious peritonitis in purebred catteries (1996) Feline Pract, 24, pp. 14-22; Addie, D.D., Jarrett, O., Control of feline coronavirus infections in breeding catteries by serotesting, isolation, and early weaning (1995) Feline Pract, 23, pp. 92-95; Rous, A., A new spectrofluorometric procedure for sexing birds (1994) Vet Record, 135, p. 437; Addie, D.D., Jarrett, O., Feline coronavirus antibodies in cats (1992) Vet Record, 130, p. 202; Poland, A.M., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteritic Coronavirus (1996) J Clin Microbiol, 34, pp. 3180-3184; Reinacher, M., Theilen, G., Frequency and significance of feline leukemia virus infection in necropsied cats (1987) Amer J Vet Res, 48, pp. 939-945; Fehr, D., Evaluation of the safety and efficacy of a modified live FIPV vaccine under field conditions (1995) Feline Pract, 23, pp. 83-88; Scott, F.W., Evaluation of the safety and efficacy of primucell-FIP vaccine (1992) Feline Health Topics, 7, pp. 6-8; Shell, L.G., Feline infectious peritonitis viral meningoencephalomyelitis (1997) Feline Pract, 25, pp. 24-25; Harvey, C.J., An uncommon intestinal manifestation of feline infectious peritonitis (1996) J Amer Vet Med Assn, 209, pp. 1117-1120; Kipar, A., Feline infectious peritonitis presenting as a tumour in the abdominal cavity (1999) Vet Record, 144, pp. 118-122; Sparkes, A.H., An appraisal of the value of laboratory tests in the diagnosis of feline infectious peritonitis (1994) J Amer Anim Hosp Assn, 30, pp. 345-350; Rohrer, C., The diagnosis of feline infectious peritonitis (FIP): A retrospective and prospective study (1993) Kleintierpraxis, 38, pp. 379-389; Sparkes, A.H., Coronavirus serology in healthy pedigree cats (1992) Vet Record, 31, pp. 35-36; Kipar, A., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Vet Immunol Immunopathol, 65, pp. 243-257; Cammarata Parodi, G., Using direct immunofluorescence to detect coronaviruses in peritoneal and pleural effusions (1993) J Small Anim Pract, 34, pp. 609-613; Telford, D., PCR-based diagnosis of feline infectious peritonitis (1997) Vet Record, 140, pp. 379-380; Jagger, T., Interpretation of tests results for feline infectious peritonitis (1997) Vet Record, 140, p. 320; Li, X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chaine reaction (1994) Vet Microbiol, 42, pp. 65-77; Addie, D.D., Feline coronavirus in the intestinal contents of cats with feline infectious peritonitis (1996) Vet Record, 139, pp. 522-523; Herrewegh, A.A.P.M., Polymerase chain reaction (PCR) for the diagnosis of naturally occurring feline coronavirus infections (1995) Feline Pract, 23, pp. 56-60; Gut, M., One-tube fluorogenic reverse transcription-polymerase chain reaction for the quantitation of feline coronaviruses (1999) J Virol Methods, 77, pp. 37-46; McReynolds, C., Macy, D., Feline infectious peritonitis. Part I. Etiology and diagnosis (1997) Comp Cont Educ Pract Vet, 19, pp. 1007-1016; Weiss, R.C., Treatment of feline infectious peritonitis with immunomodulating agents and antiviral drugs: A review (1995) Feline Pract, 23, pp. 103-106; McReynolds, C., Macy, D., Feline infectious peritonitis. Part II. Treatment and prevention (1997) Comp Cont Educ Pract Vet, 19, pp. 1111-1116; Pedersen, N.C., The history and interpretation of feline coronavirus serology (1995) Feline Pract, 23, pp. 46-51","Fradin-Ferme, M.; Clinique Vétérinaire, 85 ter Boulevard Soult, 75012 Paris, France",,,07581882,,,,"French","Prat. Med. Chir. Anim. Cie.",Article,"Final",,Scopus,2-s2.0-0041708505
"Yuan S., Nelsen C.J., Murtaugh M.P., Schmitt B.J., Faaberg K.S.","7403273072;56955164800;7005137127;7202241192;6701827490;","Recombination between North American strains of porcine reproductive and respiratory syndrome virus",1999,"Virus Research","61","1",,"87","98",,85,"10.1016/S0168-1702(99)00029-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033063134&doi=10.1016%2fS0168-1702%2899%2900029-5&partnerID=40&md5=31cf7d5f87066e8ccbbb4a6e5c0a65ce","Dept. of Veterinary PathoBiology, Univ. of Minnesota, 1971 Cmw. Avenue, St. Paul, MN 55108, United States; Natl. Vet. Services Laboratories, 1800 Dayton Avenue, Ames, IA 50010, United States","Yuan, S., Dept. of Veterinary PathoBiology, Univ. of Minnesota, 1971 Cmw. Avenue, St. Paul, MN 55108, United States; Nelsen, C.J., Dept. of Veterinary PathoBiology, Univ. of Minnesota, 1971 Cmw. Avenue, St. Paul, MN 55108, United States; Murtaugh, M.P., Dept. of Veterinary PathoBiology, Univ. of Minnesota, 1971 Cmw. Avenue, St. Paul, MN 55108, United States; Schmitt, B.J., Natl. Vet. Services Laboratories, 1800 Dayton Avenue, Ames, IA 50010, United States; Faaberg, K.S., Dept. of Veterinary PathoBiology, Univ. of Minnesota, 1971 Cmw. Avenue, St. Paul, MN 55108, United States","Porcine reproductive and respiratory syndrome virus (PRRSV), a recently discovered arterivirus swine pathogen, was shown to undergo homologous recombination. Co-infection of MA-104 cells with two culture-adapted North American PRRSV strains resulted in recombinant viral particles containing chimeric ORF 3 and ORF 4 proteins. Nucleotide sequence analysis of cloned recombinant PCR products, encompassing 1182 bases of the 15.4 kb viral genome, revealed six independent recombination events. Recombinant products persisted in culture for at least three passages, indicating continuous formation of recombinant viruses, growth of recombinant viruses in competition with parental viruses, or both. The frequency of recombination was estimated from <2% up to 10% in the 1182 b fragment analyzed, which is similar to recombination frequencies observed in coronaviruses. An apparent example of natural ORF 5 recombination between naturally occurring wild type viruses was also found, indicating that recombination is likely an important genetic mechanism contributing to PRRSV evolution. Copyright (C) 1999 Elsevier Science B.V.","Differential RT-PCR; Porcine reproductive and respiratory syndrome virus; Viral recombination","arterivirus; article; cell culture; in vitro study; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; virus recombinant; virus replication; Amino Acid Sequence; Animals; Base Sequence; DNA, Viral; Molecular Sequence Data; North America; Porcine respiratory and reproductive syndrome virus; Recombination, Genetic; Swine","Andreyev, V.G., Wesley, R.D., Mengeling, W.L., Vorwald, A.C., Lager, K.M., Genetic variation and phylogenetic relationships of 22 porcine reproductive and respiratory syndrome virus (PRRSV) field strains based on sequence analysis of open reading frame 5 (1997) Arch. Virol., 142, pp. 993-1001; Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Cavanagh, D., Davis, P., Cook, J., Li, D., Molecular basis of the variation exhibited by avian infectious bronchitis coronavirus (IBV) (1990) Adv. Exp. Med. Biol., 276, pp. 369-372; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Chirnside, E.D., Wearing, C.M., Binns, M.M., Mumford, J.A., Comparison of M and N gene sequences distinguishes variation amongst equine arteritis virus isolates (1994) J. Gen. Virol., 75, pp. 1491-1497; Collins, J.E., Benfield, D.A., Christianson, W.T., Isolation of swine infertility and respiratory syndrome virus (isolate ATCC VR-2332) in North America and experimental reproduction of the disease in gnotobiotic pigs (1992) J. Vet. Diagn. Invest., 4, pp. 117-126; Faaberg, K.S., Elam, M.R., Nelsen, C.J., Murtaugh, M.P., Subgenomic RNA7 is transcribed with different leader-body junction sites in PRRSV (strain VR2332) infection of CL2621 cells (1998) Adv. Exp. Med. Biol., 440, pp. 275-279; Faaberg, K.S., Plagemann, P.G.W., The envelope proteins of lactate dehydrogenase-elevating virus and their membrane topography (1995) Virology, 212, pp. 512-525; Godeny, E.K., De Vries, A.A., Wang, X.C., Smith, S.L., De Groot, R.J., Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: Evidence for gene duplication during arterivirus evolution (1998) J. Virol., 72, pp. 862-867; Hubner, A., Kruhoffer, M., Grosse, F., Krauss, G., Fidelity of human immunodeficiency virus type I reverse transcriptase in copying natural RNA (1992) J. Mol. Biol., 223, pp. 595-600; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Kapur, V., Elam, M.R., Pawlovich, T.M., Murtaugh, M.P., Genetic variation in porcine reproductive and respiratory syndrome virus isolates in the midwestern United States (1996) J. Gen. Virol., 77, pp. 1271-1276; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Lai, M.M., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Lai, M.M., Recombination in large RNA viruses: Coronaviruses (1996) Semin. Virol., 7, pp. 381-388; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Mardassi, H., Massie, B., Dea, S., Intracellular synthesis, processing, and transport of proteins encoded by ORFs 5 to 7 of porcine reproductive and respiratory syndrome virus (1996) Virology, 221, pp. 98-112; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Meulenberg, J.J.M., Hulst, M.M., De Meijer, E.J., Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS), is related to LDV and EAV (1993) Virology, 192, pp. 62-72; Murtaugh, M.P., Elam, M.R., Kakach, L.T., Comparison of the structural protein coding sequences of the VR-2332 and Lelystad virus strains of the PRRS virus (1995) Arch. Virol., 140, pp. 1451-1460; Murtaugh, M.P., Faaberg, K.S., Laber, J., Elam, M., Kapur, V., Genetic variation in the PRRS virus (1998) Adv. Exp. Med. Biol., 440, pp. 787-794; Nagy, P.D., Simon, A.E., New insights into the mechanisms of RNA recombination (1997) Virology, 235, pp. 1-9; Nelsen, C.J., Murtaugh, M.P., Faaberg, K.S., Porcine reproductive and respiratory syndrome virus comparison: Divergent evolution on two continents (1999) J. Virol., 73, pp. 270-280; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J., Comparison of the genome organization of toro- And coronaviruses: Evidence for two non-homologous RNA recombination events during Berne virus evolution (1991) Virology, 180, pp. 448-452; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wang, L., Junker, D., Hock, L., Ebiary, E., Collisson, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Res., 34, pp. 327-338; Ward, C.D., Stokes, M.A., Flanegan, J.B., Direct measurement of the poliovirus RNA polymerase error frequency in vitro (1988) J. Virol., 62, pp. 558-562; Wensvoort, G., Terpstra, C., Pol, J.M.A., Mystery swine disease in the Netherlands: The isolation of Lelystad virus (1991) Vet. Q., 13, pp. 121-130","Faaberg, K.S.; Department of Veterinary PathoBiol., University of Minnesota, 1971 Commonwealth Avenue, St. Paul, MN 55108, United States; email: kay@lenti.med.umn.edu",,,01681702,,VIRED,"10426212","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0033063134
"Klausegger A., Strobl B., Regl G., Kaser A., Luytjes W., Vlasak R.","6602254232;6701482578;6506171579;7004029860;6701683324;56244751900;","Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus",1999,"Journal of Virology","73","5",,"3737","3743",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032901056&partnerID=40&md5=d8b5a390c4dfb1aabb2c0da4bfea49f9","Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria; University of Leiden, Institute of Microbiology, Department of Virology, 2300 AH Leiden, Netherlands; Institute of Molecular Biology, Austrian Academy of Sciences, Billroth Str. 11, A-5020 Salzburg, Austria","Klausegger, A., Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria; Strobl, B., Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria; Regl, G., Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria; Kaser, A., Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria; Luytjes, W., University of Leiden, Institute of Microbiology, Department of Virology, 2300 AH Leiden, Netherlands; Vlasak, R., Institute of Molecular Biology, Austrian Academy of Sciences, A-5020 Salzburg, Austria, Institute of Molecular Biology, Austrian Academy of Sciences, Billroth Str. 11, A-5020 Salzburg, Austria","We have characterized the hemagglutinin-esterase (HE) of puffinosis virus (PV), a coronavirus closely related to mouse hepatitis virus (MHV). Analysis of the cloned gene revealed approximately 85% sequence identity to HE proteins of MHV and approximately 60% identity to the corresponding esterase of bovine coronavirus. The HE protein exhibited acetylesterase activity with synthetic substrates p-nitrophenyl acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate. In contrast to other viral esterases, no activity was detectable with natural substrates containing 9- O-acetylated sialic acids. Furthermore, PV esterase was unable to remove influenza C virus receptors from human erythrocytes, indicating a substrate specificity different from HEs of influenza C virus and bovine coronavirus. Solid-phase binding assays revealed that purified PV was unable to bind to sialic acid-containing glycoconjugates like bovine submaxillary mucin, mouse α1 macroglobulin or bovine brain extract. Because of the close relationship to MHV, possible implications on the substrate specificity of MHV esterases are suggested.",,"esterase; hemagglutinin; animal cell; article; coronavirus; enzyme activity; enzyme specificity; enzyme substrate; genetic analysis; influenza virus c; molecular cloning; molecular recognition; mouse; nonhuman; priority journal; protein expression; receptor binding; virus characterization; Amino Acid Sequence; Animals; Base Sequence; Cattle; Cloning, Molecular; Coronavirus; Coronavirus, Bovine; DNA, Viral; Genes, Viral; Glycoconjugates; Glycoproteins; Hemagglutinins, Viral; Humans; Influenzavirus C; L Cells (Cell Line); Mice; Molecular Sequence Data; N-Acetylneuraminic Acid; Sequence Homology, Amino Acid; Substrate Specificity; Viral Fusion Proteins; Viral Proteins","Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995) The Coronaviridae, pp. 165-179. , S. Siddell (ed.), Plenum Press, Inc., New York, N.Y; Cornelissen, L.A.H.M., Wierda, C.M.H., Van Der Meer, F.J., Herrewegh, A.A.P.M., Horzinek, M.C., Egberink, H.F., De Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J. Virol., 71, pp. 5277-5286; Dveksler, G.S., Basile, A.A., Cardellichio, C.B., Holmes, K.V., Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain (1995) J. Virol., 69, pp. 543-546; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Ekia, P.E., Holmes, K.V., Mouse coronavirus MHV-a59 and blocking anti-receptor monoclonal antibody bind to the N-terminal domain of cellular receptor MHVR (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Formanowski, F., Meier-Ewert, H., Isolation of the influenza C virus glycoprotein in a soluble form by bromelain digestion (1988) Virus Res., 10, pp. 177-192; Gagneten, S., Gout, O., Duois-Dalcq, M., Rottier, P., Rossen, J., Holmes, K.V., Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for interaction with an MHV strain that expresses the hemagglutinin-esterase glycoprotein (1995) J. Virol., 69, pp. 889-895; Garcia-Sastre, A., Villar, E., Manuguerra, J.C., Hannoun, C., Cabezas, J.A., Activity of influenza C virus O-acetylesterase with O-acetyl-containing compounds (1991) Biochem. J., 273, pp. 435-441; Gubler, U., Hoffman, B.J., A simple and very efficient method for generating cDNA libraries (1983) Gene, 25, pp. 263-269; Herrler, G., Dükop, I., Becht, H., Klenk, H.-D., The glycoprotein of influenza C virus is the hemagglutinin, esterase and fusion factor (1988) J. Gen. 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Virol., 73, pp. 901-906; Schultze, B., Wahn, K., Klenk, H.-D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Shieh, C.K., Lee, H.J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol., 63, pp. 3729-3736; Siddell, G.S., Coronavirus JHM: Tryptic fingerprinting of virion proteins intracellular polypeptides (1982) J. Gen. 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USA, 88, pp. 5533-5536; Yokomori, K., Banner, L.R., Lai, M.M.C., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Yokomori, K., Baker, S.C., Stohlman, S.A., Lai, M.M.C., Hemagglutinin-esterase-specific monoclonal antibodies alter the neuropathogenicity of mouse hepatitis virus (1992) J. Virol., 66, pp. 2865-2874; Yokomori, K., La Monica, N., Makino, S., Shieh, C.K., Lai, M.M.C., Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus (1989) Virology, 173, pp. 683-691; Yoo, D., Graham, F.L., Prevec, L., Parker, M.D., Benkö, M., Zamb, T., Babiuk, L.A., Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus (1992) J. Gen. Virol., 73, pp. 2591-2600; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.-L., Lai, M.M.C., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183; Zimmer, G., Reuter, G., Schauer, R., Use of influenza C virus for detection of 9-O-acetylated sialic acids on immobilized glycoconjugates by esterase activity (1992) Eur. J. Biochem., 204, pp. 209-215","Vlasak, R.; Institute of Molecular Biology, Austrian Academy of Sciences, Billroth Str. 11, A-5020 Salzburg, Austria; email: rvlasak@oeaw.ac.at",,,0022538X,,JOVIA,"10196267","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032901056
"Napthine S., Liphardt J., Bloys A., Routledge S., Brierley I.","7801637219;57204947749;6507341759;6506737619;7004639098;","The role of RNA pseudoknot stem 1 length in the promotion of efficient -1 ribosomal frameshifting",1999,"Journal of Molecular Biology","288","3",,"305","320",,64,"10.1006/jmbi.1999.2688","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033532080&doi=10.1006%2fjmbi.1999.2688&partnerID=40&md5=94491d1e057af5a4357c9ec00b55c64e","Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","Napthine, S., Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Liphardt, J., Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Bloys, A., Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Routledge, S., Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom; Brierley, I., Div. of Virol. Dept. of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, United Kingdom","The ribosomal frameshifting signal present in the genomic RNA of the coronavirus infectious bronchitis virus (IBV) contains a classic hairpin-type RNA pseudoknot that is believed to possess coaxially stacked stems of 11 bp (stem 1) and 6 bp (stem 2). We investigated the influence of stem 1 length on the frameshift process by measuring the frameshift efficiency in vitro of a series of IBV-based pseudoknots whose stem 1 length was varied from 4 to 13 bp in single base-pair increments. Efficient frameshifting depended upon the presence of a minimum of 11 bp; pseudoknots with a shorter stem 1 were either non-functional or had reduced frameshift efficiency, despite the fact that a number of them had a stem 1 with a predicted stability equal to or greater than that of the wild-type IBV pseudoknot. An upper limit for stem 1 length was not determined, but pseudoknots containing a 12 or 13 bp stem 1 were fully functional. Structure probing analysis was carried out on RNAs containing either a ten or 11 bp stem 1; these experiments confirmed that both RNAs formed pseudoknots and appeared to be indistinguishable in conformation. Thus the difference in frameshifting efficiency seen with the two structures was not simply due to an inability of the 10 bp stem 1 construct to fold into a pseudoknot. In an attempt to identify other parameters which could account for the poor functionality of the shorter stem 1-containing pseudoknots, we investigated, in the context of the 10 bp stem 1 construct, the influence on frameshifting of altering the slippery sequence-pseudoknot spacing distance, loop 2 length, and the number of G residues at the bottom of the 5'-arm of stem 1. For each parameter, it was possible to find a condition where a modest stimulation of frameshifting was observable (about twofold, from seven to a maximal 17%), but we were unable to find a situation where frameshifting approached the levels seen with 11 bp stem 1 constructs (48-57%). Furthermore, in the next smaller construct (9 bp stem 1), changing the bottom four base-pairs to G·C (the optimal base composition) only stimulated frameshifting from 3 to 6%, an efficiency about tenfold lower than seen with the 11 bp construct. Thus stem 1 length is a major factor in determining the functionality of this class of pseudoknot and this has implications for models of the frameshift process.","Coronavirus; Retrovirus; Ribosomal frameshifting; RNA pseudoknot; RNA structure probing","virus RNA; article; Avian infectious bronchitis virus; base pairing; controlled study; Coronavirus; gene construct; nonhuman; priority journal; ribosomal frameshifting; RNA conformation; RNA structure","Arnott, S., Hukins, D.W., Dover, S.D., Fuller, W., Hodgson, A.R., Structures of synthetic polynucleotides in the A-RNA and A′-RNA conformations: X-ray diffraction analyses of the molecular conformations of polyadenylic acid-polyuridylic acid and polyinosinic acid-polycytidylic acid (1973) J. Mol. Biol., 81, pp. 107-122; Bidou, L., Stahl, G., Grima, B., Liu, H., Cassan, M., Rousset, J.-P., In vivo HIV-1 frameshift efficiency is directly related to the stability of the stem-loop stimulatory signal (1997) RNA, 10, pp. 1153-1158; Brierley, I., Ribosomal frameshifting on viral RNAs (1995) J. Gen. Virol., 76, pp. 1885-1892; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterisation of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 57, pp. 537-547; Brierley, I., Rolley, N.J., Jenner, A.J., Inglis, S.C., Mutational analysis of the RNA pseudoknot component of a coronavirus ribosomal frameshifting signal (1991) J. Mol. Biol., 220, pp. 889-902; Brierley, I., Jenner, A.J., Inglis, S.C., Mutational analysis of the ""slippery sequence"" component of a coronavirus ribosomal frameshifting signal (1992) J. Mol. Biol., 227, pp. 463-479; Chen, X., Chamorro, M., Lee, S.I., Shen, L.X., Hines, J.V., Tinoco I., Jr., Varmus, H.E., Structural and functional studies of retroviral RNA pseudoknots involved in ribosomal frameshifting: Nucleotides at the junction of the two stems are important for efficient ribosomal frameshifting (1995) EMBO J., 14, pp. 842-852; Chen, X.Y., Kang, H.S., Shen, L.X., Chamorro, M., Varmus, H.E., Tinoco, I., A characteristic bent conformation of RNA pseudoknots promotes -1 frameshifting during translation of retroviral RNA (1996) J. Mol. Biol., 260, pp. 479-483; Dinman, J.D., Ruiz-Echevarria, M.J., Czaplinski, K., Peltz, S.W., Peptidyl-transferase inhibitors have antiviral properties by altering programmed -1 ribosomal frameshifting efficiencies: Development of model systems (1997) Proc. 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Biol., 53, pp. 131-196; Krzyzosiak, W.J., Marciniec, T., Wiewiorowski, M., Romby, P., Ebel, J.-P., Giege, R., Characterisation of the lead (II)-induced cleavages in tRNAs in solution and effect of the Y-base removal in yeast tRNA Phe (1988) Biochemistry, 27, pp. 5771-5777; Kunkel, T.A., Rapid and efficient site-specific mutagenesis without phenotypic selection (1985) Proc. Natl Acad. Sci. USA, 82, pp. 488-492; Liphardt, J., Napthine, S., Kontos, H., Brierley, I., Evidence for an RNA pseudoknot loop-helix interaction essential for efficient -1 ribosomal frameshifting (1999) J. Mol. Biol., 288, pp. 321-335; Melton, D.A., Krieg, P.A., Robagliati, M.R., Maniatis, T., Zinn, K., Green, M.R., Efficient in vitro synthesis of biologically active RNA and RNA hybridisation probes from plasmids containing a bacteriophage SP6 promoter (1984) Nucl. Acids Res., 12, pp. 7035-7056; Pleij, C.W.A., Rietveld, K., Bosch, L., A new principle of RNA folding based on pseudoknotting (1985) Nucl. 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Chem., 17, pp. 167-192; Van Belkum, A., Verlaan, P., Bing, K.J., Pleij, C., Bosch, L., Temperature-dependent chemical and enzymatic probing of the tRNA-like structure of TYMV RNA (1988) Nucl. Acids Res., 16, pp. 1931-1950; Vlassov, V.V., Zuber, G., Felden, B., Behr, J.-P., Giege, R., Cleavage of tRNA with imidazole and spermine imidazole constructs: A new approach for probing RNA structure (1995) Nucl. Acids Res., 23, pp. 3161-3167; Wills, N.M., Gesteland, R.F., Atkins, J.F., Evidence that a downstream pseudoknot is required for translational readthrough of the Moloney murine leukaemia virusgag stop codon (1991) Proc. Natl Acad. Sci. USA, 88, pp. 6991-6995; Wyatt, J.R., Puglisi, J.D., Tinoco, I., RNA pseudoknots: Stability and loop size requirements (1990) J. Mol. Biol., 214, pp. 455-470; Young, J.F., Desselberger, U., Graves, P., Palese, P., Shatzman, A., Rosenberg, M., Cloning and expression of influenza virus genes (1983) The Origin of Pandemic Influenza Viruses, pp. 129-138. , W. G. Laver. Amsterdam: Elsevier Science","Brierley, I.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; email: ib103@mole.bio.cam.ac.uk",,"Academic Press",00222836,,JMOBA,"10329144","English","J. Mol. Biol.",Article,"Final",,Scopus,2-s2.0-0033532080
"Tråvén M., Björnerot L., Larsson B.","6603563444;6506686423;7202678840;","Nationwide survey of antibodies to bovine coronavirus in bulk milk from Swedish dairy herds",1999,"Veterinary Record","144","19",,"527","529",,19,"10.1136/vr.144.19.527","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033535644&doi=10.1136%2fvr.144.19.527&partnerID=40&md5=8eabdfc496b25ab03dba2faa90bcb613","Dept. Ruminant Med. and Epidemiol., University of Agricultural Sciences, Uppsala, Sweden; Division of Epizootiology, National Veterinary Institute, Uppsala, Sweden","Tråvén, M., Dept. Ruminant Med. and Epidemiol., University of Agricultural Sciences, Uppsala, Sweden; Björnerot, L., Division of Epizootiology, National Veterinary Institute, Uppsala, Sweden; Larsson, B., Division of Epizootiology, National Veterinary Institute, Uppsala, Sweden","Bulk milk samples from 2236 dairy herds randomly selected throughout Sweden in proportion to region and herd size were analysed for antibodies to bovine coronavirus (BCV) in an ELISA. The results were expressed as optical density (OD) values and an OD>0·04 was considered positive. Eighty-nine per cent of the samples were antibody-positive and 52 per cent had high levels of antibodies to BCV (an OD>0·70). There were significantly higher OD values (P<0·001) and fewer antibody-negative samples (P<0·001) from larger herds than from smaller herds. There were also significantly higher OD values and fewer antibody-negative samples from herds in southern Sweden than from herds in northern Sweden (P<0·001 and P<0·001, respectively). These results indicate a higher frequency of BCV infections in larger herds and in herds in southern Sweden.",,"virus antibody; animal; animal disease; article; cattle; cattle disease; Coronavirus; enzyme linked immunosorbent assay; immunology; isolation and purification; milk; prevalence; randomization; Sweden; virology; virus infection; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; Milk; Prevalence; Random Allocation; Sweden","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Veterinaria Scandinavica, 32, pp. 163-170; Battaglia, M., Lutz, H., Wyler, R., Serologische Übersichtsuntersuchung uber die Verbreitung des bovinen Coronavirus in der Schweiz (1986) Schweizer Archiv fur Tierheilkunde, 128, pp. 213-218; Campbell, S.G., Cookingham, C.A., The enigma of winter dysentery (1978) Cornell Veterinarian, 68, pp. 423-441; Mcnulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Veterinary Microbiology, 9, pp. 425-434; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Veterinary Pathology, 10, pp. 45-64; Möstl, K.V., Burki, F., Ursachliche Beteiligung boviner Coronaviren an respiratorischen Krankheitsausbrüchen bei Kalbern und pathologisch-immunologischer Uberlegungen hierzu (1987) Deutsche Tierarztliche Wochenschrift, 95, pp. 19-22; Roberts, S.J., Winter dysentery in dairy cattle (1957) Cornell Veterinarian, 47, pp. 372-388; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Veterinarian, 80, pp. 303-311; Stair, E.L., Rhodes, M.B., White, R.G., Amebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) American Journal of Veterinary Research, 33, pp. 1147-1156; Storz, J.V., Rott, R., Über die Verbreitung der Coronavirusinfektion bei Rindern in ausgewalten Gebieten Deutschlands: Antikorpernachweis durch Mikroimmundiffusion und Neutralisation (1980) Deutsche Tierärtzliche Wochenschrift, 87, pp. 252-254; Thomas, L.H., Gourlay, R.N., Stott, E.J., Howard, C.J., Bridger, J.C., A search for new microorganisms in calf pneumonia by the inoculation of gnotobiotic calves (1982) Research in Veterinary Science, 33, pp. 170-182; Tråvén, M., Sundberg, J., Larsson, B., Niskamen, R., Winter dysentery diagnosed by farmers in dairy herds in central Sweden: Incidence, clinical signs and protective immunity (1993) Veterinary Record, 133, pp. 315-318; White, M.E., Schukken, Y.H., Tanksley, B., Space-time clustering of, and risk factors for, farmer-diagnosed winter dysentery in dairy cattle (1989) Canadian Veterinary Journal, 30, pp. 948-951","Tråvén, M.; Dept. Ruminant Med. and Epidemiol., University of Agricultural Sciences, Uppsala, Sweden",,"British Veterinary Association",00424900,,VETRA,"10378280","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0033535644
"Marini R.P., Li X., Harpster N.K., Dangler C.","7007004908;7501700707;6602178472;35876999200;","Cardiovascular pathology possibly associated with ketamine/xylazine anesthesia in dutch belted rabbits",1999,"Laboratory Animal Science","49","2",,"153","160",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032891033&partnerID=40&md5=3d3a2926f256488d03db6088140454b3","Division of Comparative Medicine, Massachusetts Inst. of Technology, Cambridge, MA, United States; Animal Resources Center, University of Chicago, Chicago, IL, United States; Angell Memorial Hospital, Boston, MA, United States","Marini, R.P., Division of Comparative Medicine, Massachusetts Inst. of Technology, Cambridge, MA, United States; Li, X., Animal Resources Center, University of Chicago, Chicago, IL, United States; Harpster, N.K., Angell Memorial Hospital, Boston, MA, United States; Dangler, C., Division of Comparative Medicine, Massachusetts Inst. of Technology, Cambridge, MA, United States","Background and Purpose: After myocardial necrosis and fibrosis was observed in five rabbits which had been anesthetized a variable number of times, the potential relationship of these lesions and anesthesia was evaluated in 35 other rabbits. Methods: Anesthesia was induced by intramuscular administration of ketamine and xylazine followed by infusion of lactated Ringer's solution also containing ketamine and xylazine. Group A rabbits (n = 9) were subjected to multiple anesthesias and were evaluated by echocardiography, thoracic radiography, electrocardiography, determination of serum coronavirus titer, vitamin E concentration, and complete necropsy. Prior to a single acute procedure followed by necropsy, group B rabbits (n = 11) were evaluated by echocardiography only. Group C rabbits (n = 10) had never been anesthetized and were necropsied after euthanasia. Group D rabbits (n = 5) had intermediate anesthesia exposure history and were evaluated by echocardiography only. Myocardial fibrosis was scored semi-quantitatively on a scale of 0 to 4. Results: Canine coronavirus test results were negative; hypovitaminosis E was evident, and fibrosis scores were significantly increased in group A, compared with group B or group C, rabbits. Conclusion: Etiologic differentials included α2-agonist-mediated coronary vasoconstriction with associated myocardial hypoperfusion, hypovitaminosis E and free radical injury, and other anesthetic-induced physiologic trespass.",,"alpha 1 adrenergic receptor stimulating agent; alpha tocopherol; free radical; ketamine; Ringer lactate solution; xylazine; alpha tocopherol deficiency; anesthesia; animal experiment; animal tissue; article; cardiovascular disease; controlled study; coronary artery constriction; coronavirus; echocardiography; electrocardiogram; female; heart muscle fibrosis; heart muscle necrosis; intramuscular drug administration; male; nonhuman; rabbit; thorax radiography; virus titration; Anesthesia; Anesthetics; Animals; Antibodies, Viral; Cardiovascular Diseases; Coronavirus; Echocardiography; Fibrosis; Ketamine; Myocarditis; Myocardium; Organ Size; Rabbits; Specific Pathogen-Free Organisms; Vitamin E; Xylazine","Weisbroth, S.H., Flatt, R.E., Kraus, A.L., (1974) The Biology of the Laboratory Rabbit, 1st Ed., , Academic Press, San Diego; Edwards, S., Small, J.D., Geratz, J.D., An experimental model for myocarditis and congestive heart failure after rabbit coronavirus infection (1992) J. 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Heart J., 120, pp. 233-236; Magid, N.M., Opio, G., Wallerson, D.C., Heart failure due to chronic experimental aortic regurgitation (1994) Am. J. Physiol., 267, pp. 556-562; Tomlinson, C.W., Dhalla, N.S., Alterations in myocardial function during bacterial infective cardiomyopathy (1976) Am. J. Cardiol., 37, pp. 373-381; Fein, F.S., Miller-Green, B., Zola, B., Reversibility of diabetic cardiomyopathy with insulin in rabbits (1986) Am. Physiol. Soc., pp. H108-H113; Khan, M.Y., Radiation-induced cardiomyopathy (1973) Am. J. Pathol., 73, pp. 131-140; Khan, M.Y., Radiation-induced cardiomyopathy in rabbits: An ultrastructural study (1971) Radiat. Res., 47, pp. 268-269; O'Hara, P.J., Pierce, K.R., A toxic cardiomyopathy caused by Cassia occidentalis I. Morphological studies in poisoned rabbits (1974) Vet. Pathol., 11, pp. 97-109; O'Hara, P.J., Pierce, K.R., A toxic cardiomyopathy caused by Cassia occidentalis II. Biochemical studies in poisoned rabbits (1974) Vet. Pathol., 11, pp. 110-124; Lee, J.C., Downing, S.E., Ventricular performance in diabetic rabbits with norepinephrine cardiomyopathy (1986) Soc. Exp. Bio. Med., 181, pp. 345-350; Downing, S.E., Chen, V., Myocardial injury following endogenous catecholamine release in rabbits (1985) J. Mol. Cell. Cardiol., 17, pp. 377-387; Simons, M., Downing, S.E., Coronary vasoconstriction and catecholamine cardiomyopathy (1985) Am. Heart J., 109, pp. 297-304; Lee, J.C., Sponenberg, D.P., Role of α-1-adrenoceptors in norepinephrine-induced cardiomyopathy (1985) Am. J. Pathol., 121, pp. 316-321; Lurie, K.G., Bristow, M.R., Minobe, W.A., 6-hydroxydopamine mediated cardiotoxicity in rabbits (1988) Am. J. Cardiovasc. Pathol., 2, pp. 181-191; Khan, M.Y., Haider, B., Thind, I.S., Emetine-induced cardiomyopathy in rabbits (1983) J. Submicrosc. Cytol., 15, pp. 495-507; Friesen, J.M., Ferris, J.A.J., Rabkin, S.S., Pathological features of cantharidin-induced toxic cardiomyopathy: Lack of correlation between electron-microscopic and histopathologic myocardial damage (1979) Forensic Sci. Int., 13, pp. 187-192; Dodd, D.A., Atkinson, J.B., Olson, R.D., Doxorubicin cardiomyopathy is associated with a decrease in calcium release channel of the sarcoplasmic reticulum in a chronic rabbit model (1993) J. Clin. Invest., 91, pp. 1697-1705; Jaenke, R.S., Deprez-DeCampeneere, D., Troust, A., Cardiotoxicity and comparative pharmacokinetics of six anthracyclines in the rabbit (1980) Cancer Res., 40, pp. 3530-3536; Li, X., Murphy, J.C., Lipman, N.S., Eisenmenger's syndrome in a New Zealand White rabbit (1995) Lab. Anim. Sci., 45, pp. 618-620; Weber, H.W., VanderWalt, J.J., Cardiomyopathy in crowded rabbits (1973) S. Afr. Med. J., 47, pp. 1591-1595; Hesselton, R.M., Yang, W.C., Medveczky, P., Pathogenesis of Herpesvirus svlvilagus infection in cottontail rabbits (1988) Am. J. Pathol., 133, pp. 639-647; Palmore, W.P., A fatal response to xylazine and ketamine in a group of rabbits (1990) Vet. Res. Commun., 14, pp. 91-98; Teng, B., Muir, W.W., Mason, D.E., Segmental response of canine coronary arteries to alpha-2 agonists, xylazine and medetomidine (1995) Vet. Surg., 24, p. 537; Flores, N.A., Davies, R.L., Penny, W.J., Coronary microangiograpby in the guinea pig, rabbit, and ferret (1984) Int. J. Cardiol., 6, pp. 459-471; Maxwell, M.P., Hearse, D.J., Yellon, D.M., Species variation in the coronary collateral circulation during regional myocardial ischaemia: A critical determinant of the rate of evolution and extent of myocardial infarction (1987) Cardiovasc. Res., 21, pp. 737-746; Bosso, F.J., Allman, F.D., Pilati, C.F., Myocardial work load is a major determinant of norepinephrine-induced left ventricular dysfunction (1994) Am. Physiol. Soc., pp. H531-H539; Maze, M., Tranquilli, W., Alpha-2 adrenoceptor agonists: Defining the role in clinical anesthesia (1991) Anesthesiology, 74, pp. 581-605; Marini, R.P., Avison, D.L., Corning, B.F., Ketamine/xylazine/butorphanol: A new anesthetic combination for rahbits (1992) Lab. Anim. Sci., 42, pp. 57-62; Hobbs, B.A., Rolhall, T.G., Sprenkel, T.L., Comparisons of several combinations for anesthesia in rabbits (1991) Am. J. Vet. Res., 52, pp. 669-674; Lipman, N.S., Marini, R.P., Erdman, S.E., Comparison of ketamine/xylazine and ketamine/xylazine/ acepromazine anesthesia in the rabbit (1990) Lab. Anim. Sci., 40, pp. 395-398; Peeters, M.E., Gil, D., Teske, E., Four methods for general anesthesia in the rabbit: A comparative study (1988) Lab. Animals, 22, pp. 355-360; Popilskis, S.J., Oz, M.C., Gorman, P., Comparison of xylazine with tiletamine-zolazepam (TelazolR) and xylazine-ketamine anesthesia in rabbits (1991) Lab. Anim. Sci., 41, pp. 51-53; Sanford, T.D., Colby, E.D., Effect of xylazine and ketamine on blood pressure, heart rate and respiratory rate in rabbits (1980) Lab. Anim. Sci., 30, pp. 519-523; Wyatt, J.D., Scott, R.A.W., Richardson, M.E., Effects of prolonged ketamine-xylazine intravenous infusion on arterial blood pH, blood gases, mean arterial blood pressure, heart and respiratory rates, rectal temperature and reflexes in the rabbit (1989) Lab. Anim. Sci., 39, pp. 411-416; Herman, E.H., Zhang, J., Chadwick, D.P., Age dependence of the cardiac lesions induced by minoxidil in the rat (1996) Toxicology, 110, pp. 71-83; Roberts, R., Morris, D., Pratt, C.M., Pathophysiology, recognition, and treatment of acute myocardial infarction and its complications (1994) The Heart, Arteries and Veins, 8th Ed., pp. 1107-1112. , R. C. Schlant and R. W. Alexander (ed.), McGraw-Hill, Inc., New York; Van Vleet, J.F., Greenwood, L., Ferrans, V.J., Effect of selenium-vitamin E on adriamycin-induced cardiomyopathy in rabbits (1978) Am. J. Vet. Res., 39, pp. 997-1010; De Jong, J.W., Van Der Meer, P., Nieukoop, A.S., Xanthine oxidoreductase activity in perfused hearts of various species, including humans (1990) Circ. Res., 67, pp. 770-773; Jiang, J.P., Chen, V., Downing, S.E., Modulation of catecholamine cardiomyopathy by allopurinol (1991) Am. Heart J., 122, pp. 115-121; Bertazzoli, C., Sala, L., Solcia, E., Experimental adriamycin cardiotoxicity prevented by ubiquinone in vivo in rabbits (1975) Int. Res. Commun. Syst-Med. Sci., 3, p. 468; Amouzadeh, H.R., Sangiah, S., Qualls, C.W., Xylazine-induced pulmonary edema in rats (1991) Toxicol. Appl. Pharmacol., 108, pp. 417-427; Amouzadeh, H.R., Qualls, C.W., Wyckoff, J.H., Biochemical and morphological alterations in xylazine-induced pulmonary edema (1993) Toxicol. Pathol., 21, pp. 562-571; Borgman, R.F., The effects of feeding rabbits a vitamin E-low diet containing oleic acid (1966) Am. J. Vet. Res., 27, pp. 809-813; Zalkin, H., Tappel, A.L., Studies of the mechanism of vitamin E action. IV. Lipid peroxidation in the vitamin E-deficient rabbit (1960) Arch. Biochem. Biophys., 88, pp. 113-117; Yamini, B., Stein, S., Abortion, stillbirth, neonatal death, and nutritional myodegeneration in a rabbit breeding colony (1989) J. Am. Vet. Med. Assoc., 194, pp. 561-562; Bragdon, J.H., Levine, H.D., Myocarditis in vitamin E-deficient rabbits (1949) Am. J. Pathol., 25, pp. 265-271; Innes, J.R.M., Yevich, P.P., So-called nutritional muscular dystrophy as a cause of ""paralysis"" in rabbits (1954) Am. J. Pathol., 30, pp. 555-565; Ringler, D.H., Abrams, G.D., Laboratory diagnosis of vitamin E deficiency in rabbits fed a faulty commercial ration (1971) Lab. Anim. Sci., 21, pp. 383-388; Nielsen, J.N., Carlton, W.W., Colobomatous microphthalmos in a New Zealand White rabbit, arising from a colony with suspected vitamin E deficiency (1995) Lab. Anim. Sci., 45, pp. 320-322; Hunt, C.E., Harrington, D.D., Nutrition and nutritional diseases of the rabbit (1974) The Biology of the Laboratory Rabbit, , S. H. Weisbroth, R. E. Flatt, and A. L. Kraus (ed.), Academic Press, Inc., New York; Gatz, A.J., Houchin, O.B., Histological observations on the vitamin E-deficient rabbit heart (1947) Anat. Rec., 97, p. 337; Gatz, A.J., Houchin, O.B., The histology of vitamin E-deficient rabbit hearts (1947) Anat. Rec., 97, p. 462","Marini, R.P.; Division of Comparative Medicine, Massachusetts Inst. of Technology, Cambridge, MA, United States",,,00236764,,LBASA,"10331545","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0032891033
"McGoldrick A., Lowings J.P., Paton D.J.","6603456332;6602003410;7103157927;","Characterisation of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a",1999,"Archives of Virology","144","4",,"763","770",,37,"10.1007/s007050050541","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032948720&doi=10.1007%2fs007050050541&partnerID=40&md5=30d702c52926dbb4475644ac41b7d215","Virology Department, Veterinary Laboratories Agency, Addlestone, United Kingdom; Vet. Labs. Agency (Weybridge), Woodham Lane, Addlestone KT15 3NB, United Kingdom","McGoldrick, A., Virology Department, Veterinary Laboratories Agency, Addlestone, United Kingdom; Lowings, J.P., Virology Department, Veterinary Laboratories Agency, Addlestone, United Kingdom; Paton, D.J., Virology Department, Veterinary Laboratories Agency, Addlestone, United Kingdom, Vet. Labs. Agency (Weybridge), Woodham Lane, Addlestone KT15 3NB, United Kingdom","Analyses of transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) isolates have suggested that tropism and pathogenicity are influenced by the spike protein and ORF 3. In general, enteric viruses (TGEV) have been shown to contain intact spike and ORF 3 genes, whilst respiratory isolates (PRCV) have major deletions within both regions. Virulence has been correlated to a functional ORF 3. Here, sequence analysis of a recent isolate of virulent TGEV, revealed a variant with an intact spike gene, but a large deletion in ORF 3a. This suggests that ORF 3a is not essential for enteric virulence.",,"deletion mutant; gastroenteritis virus; open reading frame; porcine respiratory coronavirus; united kingdom; viral genetics; virus transmission; virus virulence; Animals; Base Sequence; Coronavirus; DNA Primers; Gastroenteritis, Transmissible, of Swine; Great Britain; Membrane Glycoproteins; Molecular Sequence Data; Open Reading Frames; Phylogeny; Polymerase Chain Reaction; Sequence Deletion; Swine; Transmissible gastroenteritis virus; Variation (Genetics); Viral Envelope Proteins; Virulence; Coronavirus; Porcine respiratory coronavirus; Staphylococcus phage 3A; Suidae; Transmissible gastroenteritis virus","Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies amino-peptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus feline infectious peritonitis virus and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J Gen Virol, 76, pp. 2235-2241; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res, 18, pp. 71-80; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res, 21, pp. 181-198; Britton, P., Kottier, S., Chen, C.M., Pocock, D.H., Salmon, H., Aynaud, J.M., The use of PCR genome mapping for the characterisation of TGEV strains (1993) Adv Exp Med Biol, 342, pp. 29-34; Chen, C.-M., Cavanagh, D., Britton, P., Cloning and sequencing of a 84-kb region from the 3′-end of a Taiwanese virulent isolate of the coronavirus transmissible gastroenteritis virus (1995) Virus Res, 38, pp. 83-89; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus II Domains in the peplomer glycoprotein (1986) J Gen Virol, 67, pp. 1405-1418; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J Virol, 64, pp. 5367-5375; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus (TGEV) epidemiology (1995) The Coronaviridae, pp. 337-376. , Siddell SG (ed) Plenum, New York; Felsenstein, J., PHYLIP: Phylogenetic inference package (version 3.2) (1989) Cladistics, 5, pp. 164-166; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J Virol, 68, pp. 8008-8016; Jones, T.O., Paton, D.J., Classical transmissible gastroenteritis returns (1996) Vet Rec, 138, pp. 166-716; Jones, T.O., Pritchard, G.C., Paton, D.J., Transmissible gastroenteritis of pigs (1997) Vet Rec, 141, pp. 427-428; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J Virol, 71, pp. 3285-3287; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Noda, M., Koide, F., Asagi, M., Inaba, Y., Physicochemical properties of transmissible gastroenteritis virus hemagglutinin (1988) Arch Virol, 99, pp. 163-172; Paton, D.J., Lowings, P., Discrimination between transmissible gastroenteritis virus isolates (1997) Arch Virol, 142, pp. 1703-1711; Paton, D.J., Ibata, G., Sands, J., McGoldrick, A., Detection of transmissible gastroenteritis virus by RT-PCR and differentiation from porcine respiratory coronavirus (1997) J Virol Methods, 66, pp. 303-309; Paul, P.S., Vaughn, E.M., Halbur, P.G., Pathogenicity and sequence analysis studies suggest potential role of gene 3 in virulence of swine enteric and respiratory coronaviruses (1997) Adv Exp Med Biol, 412, pp. 317-321; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Pritchard, G.C., Paton, D.J., Wibberley, G., Transmissible gastroenteritis in Britain: A changing situation? (1998) Proceedings of the 15th IPVS Congress, p. 218. , Birmingham, England, 5-9 July, 1998; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus but not the related porcine respiratory coronavirus has a sialic acid (N-glycolylncuraminic acid) binding activity (1996) J Virol, 70, pp. 5634-5637; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet Microbiol, 36, pp. 333-347; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J Clin Microbiol, 32, pp. 1809-1812; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S 3 and 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus antigenically similar to transmissible gastroenteritis virus in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J Virol, 64, pp. 4761-4766; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373","Paton, D.J.; Veterinary Lab. Agency (Weybridge), Woodham Lane, Addlestone, Surrey KT15 3NB, United Kingdom",,,03048608,,ARVID,"10365166","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0032948720
"Herold J., Siddell S.G., Gorbalenya A.E.","7006838690;7005260816;7005626044;","A human RNA viral cysteine proteinase that depends upon a unique Zn2+- binding finger connecting the two domains of a papain-like fold",1999,"Journal of Biological Chemistry","274","21",,"14918","14925",,50,"10.1074/jbc.274.21.14918","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033591345&doi=10.1074%2fjbc.274.21.14918&partnerID=40&md5=5f0f216e55dda70551b8096de445c2a5","Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Advanced Biomedical Computing Center, SAIC/NCI-Frederick Cancer R. D. Ctr., National Institutes of Health, Frederick, MD 21702-1201, United States; Leiden University Medical Center, AZL P4-22, P.O. BOX 9600, 2300RC Leiden, Netherlands; M. P. Chumakov Inst. P., Russian Academy of Medical Sciences, 142782 Moscow, Russian Federation; Dept. of Microbiology and Immunology, Box 0414, University of California, San Francisco, CA 94143-0414, United States; SAIC/NCI-FCRDC, 430 Miller Dr, Frederick, MD 21702-1201, United States","Herold, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany, Dept. of Microbiology and Immunology, Box 0414, University of California, San Francisco, CA 94143-0414, United States; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacher Strasse 7, 97078 Würzburg, Germany; Gorbalenya, A.E., Advanced Biomedical Computing Center, SAIC/NCI-Frederick Cancer R. D. Ctr., National Institutes of Health, Frederick, MD 21702-1201, United States, Leiden University Medical Center, AZL P4-22, P.O. BOX 9600, 2300RC Leiden, Netherlands, M. P. Chumakov Inst. P., Russian Academy of Medical Sciences, 142782 Moscow, Russian Federation, SAIC/NCI-FCRDC, 430 Miller Dr, Frederick, MD 21702-1201, United States","A cysteine proteinase, papain-like proteinase (PL1pro), of the human coronavirus 229E (HCoV) regulates the expression of the replicase polyproteins, pp1a and ppa1ab, by cleavage between Gly111 and Asn112, far upstream of its own catalytic residue Cys1054. In this report, using bioinformatics tools, we predict that, unlike its distant cellular homologues, HCoV PL1pro and its coronaviral relatives have a poorly conserved Zn2+ finger connecting the left and right hand domains of a papain-like fold. Optical emission spectrometry has been used to confirm the presence of Zn2+ in a purified and proteolytically active form of the HCoV PL1pro fused with the Escherichia coli maltose-binding protein. In denaturation/renaturation experiments using the recombinant protein, its activity was shown to be strongly dependent upon Zn2+, which could be partly substituted by Co2+ during renaturation. The reconstituted, Zn2+- containing PL1pro was not sensitive to 1,10-phenanthroline, and the Zn2+- depleted protein was not reactivated by adding Zn2+ after renaturation. Consistent with the proposed essential structural role of Zn2+, PL1pro was selectively inactivated by mutations in the Zn2+ finger, including replacements of any of four conserved Cys residues predicted to co-ordinate Zn2+. The unique domain organization of HCoV PL1pro provides a potential framework for regulatory processes and may be indicative of a nonproteolytic activity of this enzyme.",,"cysteine proteinase; virus enzyme; zinc finger protein; article; coronavirus; enzyme inactivation; enzyme regulation; nonhuman; priority journal; protein domain; protein expression; protein folding; RNA virus; Amino Acid Sequence; Coronavirus; Coronavirus 229E, Human; Humans; Models, Molecular; Molecular Sequence Data; Papain; Protein Structure, Tertiary; Viral Proteins; Zinc Fingers","Neurath, H., (1984) Science, 224, pp. 350-357; Hartley, B.S., (1960) Annu. Rev. Biochem., 29, pp. 45-72; Rawlings, N.D., Barrett, A.J., (1993) Bicchem. J., 290, pp. 205-218; Gorbalenya, A.E., Blinov, V.M., Donchenko, A.P., (1986) FEBS Lett., 194, pp. 253-257; Bazan, J.F., Fletterick, R.J., (1988) Proc. Natl. Acad. Sci. U. S. 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Biol., 141, pp. 441-484; Joshua-Tor, L., Xu, H.E., Johnston, S.A., Rees, D.C., (1995) Science, 269, pp. 945-950","Gorbalenya, A.E.; SAIC, NCI-FCRDC, 430 Miller Dr., Frederick, MD 21702-1201, United States; email: gorbalen@ncifcrf.gov",,,00219258,,JBCHA,"10329692","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0033591345
"Breslin J.J., Smith L.G., Fuller F.J., Guy J.S.","7004753945;37109180900;7006216552;7202723649;","Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus",1999,"Intervirology","42","1",,"22","29",,28,"10.1159/000024956","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032990712&doi=10.1159%2f000024956&partnerID=40&md5=0178f384abdbb5429e7ae53b293d6719","Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC, United States; North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States","Breslin, J.J., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC, United States; Smith, L.G., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC, United States; Fuller, F.J., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC, United States; Guy, J.S., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC, United States, North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States","A reverse transcriptase, polymerase chain reaction (RT-PCR) procedure was used to amplify a segment of the genome of turkey coronavirus (TCV) spanning portions of the matrix and nucleocapsid (MN) protein genes (approximately 1.1 kb). The MN gene region of three epidemiologically distinct TCV strains (Minnesota, NC95, Indiana) was amplified, cloned into pUC19, and sequenced, TCV MN gene sequences were compared with published sequences of other avian and mammalian coronaviruses. A high degree of similarity (> 90%) was observed between the nucleotide, matrix protein, and nucleocapsid protein sequences of TCV strains and published sequences of infectious bronchitis virus (IBV). The matrix and nucleocapsid protein sequences of TCV had limited homology (< 30%) with MN sequences of mammalian coronaviruses. These results demonstrate a close genetic relationship between the avian coronaviruses, IBV and TCV.","Coronavirus; Infectious bronchitis virus; Polymerase chain reaction; Turkey coronavirus","article; coronavirus; gene sequence; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; sequence analysis; virus gene; virus nucleocapsid; Amino Acid Sequence; Animals; Base Sequence; Coronavirus; Coronavirus, Turkey; Genotype; Infectious bronchitis virus; Molecular Sequence Data; Phylogeny; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sequence Alignment; Sequence Homology; Viral Matrix Proteins","Robb, J.A., Bond, C.W., Coronaviridae (1979) Comprehensive Virology, 14, pp. 193-247. , Fraenkel-Conrat H, Wagner RR (eds): New York, Plenum Press; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Siddell, S.G., The Coronaviridae - An Introduction (1995) Coronaviridae, pp. 1-9. , Siddell SG (ed): New York, Plenum Press; 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Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J Gen Virol, 72, pp. 1659-1666; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis, 41, pp. 583-590; Pomeroy, B.S., Nagaraja, K.V., Coronaviral enteritis of turkeys (bluecomb disease) (1991) Diseases of Poultry, pp. 745-752. , Calnek BW, Barnes HJ, Beard CW, Reid WM, Yoder HW Jr (eds): Ames, Iowa State University Press; Andreasen J.R., Jr., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis, 35, pp. 216-220; Jackwood, M.W., Kwon, H.M., Hilt, D.A., Infectious bronchitis virus detection in allantoic fluid using the polymerase chain reaction and a DNA probe (1992) Avian Dis, 36, pp. 403-409; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; 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Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Res, 25, pp. 213-222; Savoysky, E., Boireau, P., Finance, C., Laporte, J., Sequence and analysis of BECV F15 matrix protein (1990) Res Virol, 141, pp. 411-425; Pfleiderer, M., Skinner, M.A., Siddell, S.G., Coronavirus MHV-JHM: Nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res, 14, p. 6338; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Britton, P., Carmenes, R.S., Page, K.W., Garwes, D.J., The integral membrane protein from a virulent isolate of transmissible gastroenteritis virus: Molecular characterization, sequence and expression in Escherichia coli (1988) Mol Microbiol, 2, pp. 497-505. , published erratum appears in Mol Microbiol 1988 Sep;2(5):687; Laude, H., Rasschaert, D., Huet, J.C., Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastroenteritis virus (1987) J Gen Virol, 68, pp. 1687-1693; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res, 21, pp. 181-198; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J Gen Virol, 71, pp. 2599-2607; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J Gen Virol, 73, pp. 2849-2862; Jouvenne, P., Richardson, C.D., Schreiber, S.S., Lai, M.M., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus 229E (1990) Virology, 174, pp. 608-612; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J Gen Virol, 73, pp. 2731-2736; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335","Guy, J.S.; North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States; email: Jim-Guy@ncsu.edu",,,03005526,,IVRYA,"10393500","English","Intervirology",Article,"Final",,Scopus,2-s2.0-0032990712
"Pratelli A., Tempesta M., Greco G., Martella V., Buonavoglia C.","7004884960;7005599031;7101640307;7003300496;7005623145;","Development of a nested PCR assay for the detection of canine coronavirus",1999,"Journal of Virological Methods","80","1",,"11","15",,60,"10.1016/S0166-0934(99)00017-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032994568&doi=10.1016%2fS0166-0934%2899%2900017-8&partnerID=40&md5=4b798477d16d52f156409dd32deda17f","Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy","Pratelli, A., Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy; Tempesta, M., Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy; Greco, G., Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy; Martella, V., Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy; Buonavoglia, C., Dept. of Health and Animal Welfare, Fac. Vet. Med., Univ. Bari, S., Valenzano, Bari, Italy","A diagnostic test for canine coronavirus (CCV) infection based on a nested polymerase chain reaction (n-PCR) assay was developed and tested using the following coronavirus strains: CCV (USDA strain), CCV (45/93, field strain), feline infectious peritonitis virus (FIPV, field strain), trasmissible gastroenteritis virus (TGEV, Purdue strain), bovine coronavirus (BCV, 9WBL-77 strain), infectious bronchitis virus (IBV, M-41 strain) and fecal samples of dogs with CCV enteritis. A 230-bp segment of the gene encoding for transmembrane protein M of CCV is the target sequence of the primer. The test described in the present study was able to amplify both CCV and TGEV strains and also gave positive results on fecal samples from CCV infected dogs. n-PCR has a sensitivity as high as isolation on cell cultures, and can therefore be used for the diagnosis of CCV infection in dogs. Copyright (C) 1999 Elsevier Science B.V.","Canine coronavirus; Dogs; Nested-polymerase chain reaction","animal model; animal tissue; article; coronavirus; dog; enteritis; nonhuman; polymerase chain reaction; priority journal; technique; virus characterization; virus infection; Animals; Cats; Cattle; Coronavirus Infections; Coronavirus, Canine; Diarrhea; Dog Diseases; Dogs; Polymerase Chain Reaction; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline infectious peritonitis virus; Transmissible gastroenteritis virus","Appel, M.J., Canine coronavirus (1987) Virus Infections of Vertebrates, pp. 115-122. , In: Appel, M.J. (Ed), Virus infections of carnivores. Horzinek, M.C. (Series Ed.) Elsevier Science, Amsterdam; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, B.S., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc. 78th Ann. Mtg. USAHA, pp. 359-366; Buonavoglia, C., Marsilio, F., Cavalli, A., Tiscar, P.G., L'infezione da coronavirus del cane: Indagine sulla presenza del virus in Italia (1994) Notiziario Farmaceutico Veterinario, , Nr. 2/94, ed. SCIVAC; Buonavoglia, C., Sagazio, P., Cirone, F., Tempesta, M., Marsilio, F., Isolamento e caratterizzazione di uno stipite di virus della peritonite infettiva felina (1995) Veterinaria Anno, 9 (1), pp. 91-94; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35, pp. 673-675; Herrewegh, A.A., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72 (5), pp. 4508-4514; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 Kb sequence from the 3′-end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histochemical and immunofluorescent techiques (1976) Am. J. Vet. Res., 37 (3), pp. 247-256; Porter-Jordan, K., Rosenberg, E.I., Keiser, J.F., Gross, J.D., Ross, A.M., Nasim, S., Garret, C.T., Nested polymerase chain reaction assay for the detection of cytomegalovirus overcomes false positives caused by contamination with fragmented DNA (1990) J. Med. Virol., 30, pp. 85-91","Tempesta, M.; Department Health and Animal Welfare, Faculty of Veterinary Medicine, University of Bari, Strada per Casamassima km 3, 70010 Valenzano, Bari, Italy; email: m.tempesta@veterinarian.uniba.it",,,01660934,,JVMED,"10403671","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0032994568
"Hirano N., Suzuki Y., Haga S.","7101604276;57206758980;35430103200;","Pigs with highly prevalent antibodies to human coronavirus and swine haemagglutinating encephalomyelitis virus in the Tohoku district of Japan",1999,"Epidemiology and Infection","122","3",,"545","551",,6,"10.1017/S0950268899002332","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032799039&doi=10.1017%2fS0950268899002332&partnerID=40&md5=2715883bcbe5fb668955968a73c72055","Dept. of Veterinary Microbiology, Iwate University, Morioka 020, Japan","Hirano, N., Dept. of Veterinary Microbiology, Iwate University, Morioka 020, Japan; Suzuki, Y., Dept. of Veterinary Microbiology, Iwate University, Morioka 020, Japan; Haga, S., Dept. of Veterinary Microbiology, Iwate University, Morioka 020, Japan","From 1985 to 1988, a total of 2496 swine sera from 60 farms in the Tohoku District of the Honshu Island of Japan were examined for antibodies to swine haemagglutinating encephalomyelitis virus (HEV), human coronavirus (HCV) and bovine coronavirus (BCV) by haemagglutination-inhibition (HI) test. Antibodies to HEV 67N strain and HCV OC43 strain were highly prevalent with positivity rates of 82.1 and 91.4%, respectively, while seropositivity rate to BCV Kakegawa strain was 44.2%. No clinical signs of HEV infection were noticed in any farms including farms with relatively high seropositivity. The results suggested that HCV or antigenitically related virus(es) as well as HEV might be perpetuated in swine in the Tohoku District.",,"virus antibody; animal experiment; antibody detection; article; controlled study; coronavirus; hemagglutination inhibition; Japan; male; mouse; nonhuman; prevalence; RNA virus; swine disease; swine haemagglutinating encephalomyelitis virus; virus replication; Animals; Animals, Suckling; Antibodies, Viral; Cattle; Coronavirus; Coronavirus Infections; Coronavirus OC43, Human; Cross Reactions; Encephalomyelitis; Hemagglutination Tests; Humans; Japan; Mice; Mice, Inbred ICR; Seroepidemiologic Studies; Specific Pathogen-Free Organisms; Swine; Swine Diseases","Wege, H., Siddell, S.T., Ter Meulen, V., The biology and pathogenesis of cornaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Roe, C.K., Alexander, T.J.L., A disease of nursing pigs previously unreported in Ontario (1958) Conad J Comp Med, 22, pp. 305-307; Mitchell, D., Encephalomyelitis of swine caused by hemagglutinating virus. I. Case histories (1963) Res Vet Sci, 4, pp. 506-510; Greig, A.S., Girard, A., Enchephalomyelitis of swine caused by a hemagglutinating virus. II. Virological studies (1963) Res Vet Sci, 4, pp. 511-517; Alexander, T.J.L., Sanders, C.N., Vomiting and wasting disease of piglets (1969) Vet Rec, 84, p. 178; Cartright, S.F., Lucas, M., Cavill, J.P., Gush, A.F., Blandford, T.B., Vomiting and wasting disease of piglets. Virological and epidemiological studies (1970) Vet Rec, 86, pp. 278-279; Mengeling, W.L., Bloothe, A.D., Richte, A.E., Characterization of coronavirus (strain 67N) of pigs (1972) Am J Vet Res, 33, pp. 297-308; Girard, A., Greig, A.S., Mitchell, D., Encephalomyelitis of swine caused by a hemagglutinating virus. III. Serological studies (1964) Res Vet Sci, 5, pp. 294-302; Mcferren, J.B., Clarke, J.K., Cornner, T.J., Norx, E.R., Serological evidence of the presence of hemagglutinating encephalomyelitis virus in Northern Ireland (1971) Vet Rec, 88, pp. 339-340; Chang, C.N., Hsu, F.S., Shen, Y.M., Yen, C.C., A serological survey on hemagglutinating encephalomyelitis virus infection in pigs of Taiwan Sugar Corporation. Taiwan (1978) Annual Research Report of Animal Research Institute, pp. 157-163. , Taiwan Sugar Corporation; Hirai, K., Chang, C.N., Shimakura, S., A serological survey on hemagglutinating encephalomyelitis virus infection in Japan (1974) Jpn J Vet Sci, 36, pp. 375-382; Mengeling, W.L., Incidence of antibody for hemagglutinating encephalomyelitis virus in serum from swine in the United States (1975) Am J Vet Res, 36, pp. 821-825; Hirahara, T., Yasuhara, H., Kodama, K., Nakai, M., Sasaki, N., Isolation of hemagglutinating encephalomyelitis virus from respiratory tract of pig in Japan (1987) Jpn J Vet Sci, 49, pp. 85-93; Takahashi, A., Inaba, Y., Sato, K., Epizootic dairrhea of adult cattle associated with coronavirus like agent (1980) Vet Microbiol, 5, pp. 151-154; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Chanock, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc Natl Acad Sci, 57, pp. 933-940; Hirano, N., Ono, K., Takasawa, H., Murakami, T., Haga, S., Replication and plaque formation of swine hemagglutinating encephalomyelitis virus (67N) in swine cell line, SK-K culture (1990) J Virol Meth, 27, pp. 91-100; Hirano, N., Sada, Y., Tsuchiya, K., Ono, K., Murakami, T., Plaque assay of bovine coronavirus in BEK-1 cells (1985) Jpn J Vet Sci, 47, pp. 679-681; Kaye, H.S., Yarbrough, W.R., Reed, C.J., Harrison, A.K., Antigenic relationship between human coronavirus strain OC43 and hemagglutinating encephalomyelitis virus 67N strain. Antibody responses in human and animal sera (1977) J Infect Dis, 135, pp. 201-209; Pensaert, M.B., Debouck, P., Reynolds, D.J., An immunoelectron microscopic and immunofluorescent study on the antigenic relationship between the coronavirus-like agent, CV777, and several coronaviruses (1981) Arch Virol, 68, pp. 45-52; Kaye, H.S., March, H.B., Dowdle, W.R., Seroepidemiologic survey of corona-virus (strain OC 43) related infections in a children's population (1971) Am J Epidemiol, 94, pp. 43-49; Kawana, R., Matsumoto, I., Clinical virology of rhinovirus and coronavirus infection in man (1975) Modern Media, 21, pp. 158-172; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol, 169, pp. 169-176; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 44, pp. 152-161","Hirano, N.; Department Veterinary Microbiology, Iwate University, Morioka 020, Japan",,,09502688,,EPINE,"10459660","English","Epidemiol. Infect.",Article,"Final",Open Access,Scopus,2-s2.0-0032799039
"Wesley R.D.","7103154080;","The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus",1999,"Virus Research","61","2",,"145","152",,35,"10.1016/S0168-1702(99)00032-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032791654&doi=10.1016%2fS0168-1702%2899%2900032-5&partnerID=40&md5=653f49ac224fd404ad4540074064c6c6","Virology Swine Research Unit, Natl. Anim. Dis. Ctr., USDA, A., Ames, IA 50010, United States","Wesley, R.D., Virology Swine Research Unit, Natl. Anim. Dis. Ctr., USDA, A., Ames, IA 50010, United States","To gain insight into the genetic relationships among six canine coronavirus (CCV) strains, the variable region of the spike (S) protein gene was sequenced. The CCV strains were: two ATCC reference strains, the Insavc-1 vaccine strain, the National Veterinary Services Laboratories (Ames, IA) challenge strain, and two California field isolates (UCD-1 and UCD-2) from the 1970s. All six strains, downstream of the nucleocapsid (N) protein gene, had sufficient size for an ORF 7b, and thus, none were transmissible gastroenteritis virus (TGEV)-like since TGEV lacks ORF 7b. By sequence analysis of the variable domain at the 5' end of the S gene, five of the six CCV strains had a high degree of identity with feline infectious peritonitis virus (FIPV). However, one CCV field isolate (UCD-1) was different and had a high degree of identity with the 5' end of the TGEV S gene. This suggests that RNA recombination occurred at this site between antigenically related coronaviruses. The low passage field isolates, UCD-1 and UCD-2, varied in their initial infectivity for swine testicular cells suggesting that sequence differences in the variable domain of the S gene may account for biological variation among CCVs. Copyright (C) 1999 Elsevier Science B.V.","Coronavirus; RT-PCR; UCD-1","nucleocapsid protein; recombinant RNA; animal cell; article; cat; controlled study; coronavirus; gene sequence; genetic recombination; hepatitis virus; nonhuman; open reading frame; priority journal; reverse transcription polymerase chain reaction; strain difference; swine; virus strain; Amino Acid Sequence; Animals; Antigens, Viral; Cats; Cells, Cultured; Coronavirus, Canine; Coronavirus, Feline; Dogs; Fluorescent Antibody Technique; Molecular Sequence Data; Phylogeny; Reverse Transcriptase Polymerase Chain Reaction; RNA Viruses; Sequence Alignment; Sequence Analysis; Transmissible gastroenteritis virus; Viral Proteins; Canine coronavirus; Coronavirus; Felidae; Feline infectious peritonitis virus; Sus scrofa; Transmissible gastroenteritis virus","Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc. Annu. Mtg. U.S. Anim. Health Assoc., 78, pp. 359-366; Binn, L.N., Marchwicki, R.H., Stephenson, E.H., Establishment of a canine cell line: Derivation, characterization, and viral spectrum (1980) Am. J. Vet. Res., 41 (6), pp. 855-860; Crandell, R.A., Fabricant, C.G., Nelson-Rees, W.A., Development, characterization and viral susceptibility of a feline (Felis catus) renal cell line (CrFK) (1973) In Vitro, 9, pp. 176-185; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , S.G. Siddell. New York: Plenum Press; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J.M., Sequence analysis of the 3′ end of the feline coronavirus FIPV 79-1146 genome: Comparison with the porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoconal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Horsburgh, B.C., Brown, T.D.K., Cloning, sequencing and expression of the S protein gene from two geographically distinct strains of canine coronavirus (1995) Virus Res., 39, pp. 63-74; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline and canine coronaviruses (1982) Infect. Immunol., 37, pp. 1148-1155; Jacobs, L., De Groot, R., Van Der Zeijst, B.A.M., Horzinek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res., 8 (4), pp. 363-371; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from TGE (1966) Can. J. Comp. Med., 30 (2), pp. 190-198; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Reynolds, D.J., Garwes, D.J., Lucey, S., Differentiation of canine coronavirus and porcine transmissible gastroenteritis virus by neutralization with canine, porcine and feline sera (1980) Vet. Microbiol., 5, pp. 283-290; Ruitenberg, E.J., Ristic, M., Vonlehmden-Maslin, A.A., Characterization and development in tissue culture of a virus of transmissible gastroenteritis of swine (1969) Cornell Vet., 59, pp. 76-89; Siddell, S.G., The coronaviridae, an introduction (1995) The Coronaviridae, pp. 1-10. , S.G. Siddell. New York: Plenum Press; Welter, C.J., TGE of swine. I. Propagation of virus in cell cultures and development of a vaccine (1965) Vet. Med. Small Animal Clin., 60 (10), pp. 1054-1058; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794; Woods, R.D., Studies of enteric coronaviruses in a feline cell line (1982) Vet. Microbiol., 7, pp. 427-435; Woods, R.D., Pedersen, N.C., Cross-protection studies between feline infectious peritonitis and porcine transmissible gastroenteritis viruses (1979) Vet. Microbiol., 4, pp. 11-16; Woods, R.D., Wesley, R.D., Immune response in sows given transmissible gastroenteritis virus or canine coronavirus (1986) Am. J. Vet. Res., 47, pp. 1239-1242; Woods, R.D., Wesley, R.D., Cultivation techniques for animal coronaviruses: Emphasis on feline infectious peritonitis virus, canine coronavirus, transmissible gastroenteritis virus, and porcine hemagglutinating encephalomyelitis virus (1988) J. Tiss. Cult. Meth., 11, pp. 95-100; Woods, R.D., Wesley, R.D., Seroconversion of pigs in contact with dogs exposed to canine coronavirus (1992) Can. J. Vet. Res., 56, pp. 78-80; Woods, R.D., Cheville, N.F., Gallegher, J.E., Lesions in the small intestine of newborn pigs inoculated with porcine, feline, and canine coronaviruses (1981) Am. J. Vet. Res., 42, pp. 1163-1169","Wesley, R.D.; Virology Swine Research Unit, National Animal Disease Center, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010, United States; email: rwesley@nadc.ars.usda.gov",,,01681702,,VIRED,"10475084","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0032791654
"Regl G., Kaser A., Iwersen M., Schmid H., Kohla G., Strobl B., Vilas U., Schauer R., Vlasak R.","6506171579;7004029860;6505820932;57196741516;6602278772;6701482578;6507502550;7102195839;56244751900;","The hemagglutinin-esterase of mouse hepatitis virus strain S is a sialate-4-O-acetylesterase",1999,"Journal of Virology","73","6",,"4721","4727",,49,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033060753&partnerID=40&md5=66f1f7e15a6e731799e6ae97474beae2","Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria; Institute of Biochemistry, University of Kiel, D-24098 Kiel, Germany; Austrian Academy of Sciences, Institute of Molecular Biology, Billrothstr. 11, A-5020 Salzburg, Austria","Regl, G., Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria; Kaser, A., Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria; Iwersen, M., Institute of Biochemistry, University of Kiel, D-24098 Kiel, Germany; Schmid, H., Institute of Biochemistry, University of Kiel, D-24098 Kiel, Germany; Kohla, G., Institute of Biochemistry, University of Kiel, D-24098 Kiel, Germany; Strobl, B., Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria; Vilas, U., Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria; Schauer, R., Institute of Biochemistry, University of Kiel, D-24098 Kiel, Germany; Vlasak, R., Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria, Austrian Academy of Sciences, Institute of Molecular Biology, Billrothstr. 11, A-5020 Salzburg, Austria","By comparative analysis of the hemagglutinin-esterase (HE) protein of mouse hepatitis virus strain S (MHV-S) and the HE protein of influenza C virus, we found major differences in substrate specificities. In striking contrast to the influenza C virus enzyme, the MHV-S esterase was unable to release acetate from bovine submandibulary gland mucin. Furthermore, MHV-S could not remove influenza C virus receptors from erythrocytes. Analysis with free sialic acid derivatives revealed that the MHV-S HE protein specifically de-O-acetylates 5-N-acetyl-4-O-acetyl sialic acid (Neu4,5Ac2) but not 5-N- acetyl-9-O-acetyl sialic acid (Neu5,9Ac2), which is the major substrate for esterases of influenza C virus and bovine coronaviruses. In addition, the MHV-S esterase converted glycosidically bound Neu4,5Ac2 of guinea pig serum glycoproteins to Neu5Ac. By expression of the MHV esterase with recombinant vaccinia virus and incubation with guinea pig serum, we demonstrated that the vital HE possesses sialate-4-O-acetylesterase activity. In addition to observed enzymatic activity, MHV-S exhibited affinity to guinea pig and horse serum glycoproteins. Binding required sialate-4-O-acetyl groups and was abolished by chemical de-O-acetylation. Since Neu4,5Ac2 has not been identified in mice, the nature of potential substrates and/or secondary receptors for MHV-S in the natural host remains to be determined. The esterase of MHV-S is the first example of a vital enzyme with high specificity and affinity toward 4-O-acetylated sialic acids.",,"acetylesterase; esterase; sialic acid derivative; virus enzyme; virus hemagglutinin; animal cell; article; binding affinity; enzyme activity; enzyme specificity; enzyme substrate; erythrocyte; guinea pig; influenza virus c; murine hepatitis coronavirus; nonhuman; priority journal; vaccinia virus; virus recombinant; Acetylation; Acetylesterase; Animals; Hemagglutinins, Viral; Mice; Murine hepatitis virus; N-Acetylneuraminic Acid; Receptors, Virus; Vaccinia virus; Viral Fusion Proteins; Viral Proteins","Brian, D.A., Hogue, B.G., Kienzle, T.E., (1995) The Coronavirus Hemagglutinin Esterase Glycoprotein, pp. 165-179. , S. Siddell (ed.), The coronaviridae. Plenum Press Inc., New York, N.Y; Cornelissen, L.A.H.M., Wierda, C.M.H., Van Der Meer, F.J., Herrewegh, A.A.P.M., Horzinek, M.C., Egberink, H.F., De Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J. Virol., 71, pp. 5277-5286; Dea, S., Verbeek, A.J., Tijssen, P., Antigentc and genomic relationships among turkey and bovine enteric coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Falkner, F.G., Moss, B., Escherichia coli gpt gene provides dominant selection for vaccinia virus open reading frame expression vectors (1988) J. 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J. Biochem., 294, pp. 209-215; Zimmer, G., Suguri, T., Reuter, G., Yu, R.K., Schauer, R., Herrler, G., Modification of sialic acids by 9-O-acetylation is detected in human leucocytes using the lectin property of influenza C virus (1994) Glycobiology, 4, pp. 343-349","Vlasak, R.; Austrian Academy of Sciences, Institute of Molecular Biology, Billrothstr. 11, A-5020 Salzburg, Austria; email: rvlasak@oeaw.ac.at",,,0022538X,,JOVIA,"10233932","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0033060753
"Hsue B., Masters P.S.","7801347035;7006234572;","Insertion of a new transcriptional unit into the genome of mouse hepatitis virus",1999,"Journal of Virology","73","7",,"6128","6135",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033033638&partnerID=40&md5=2672e25e5ba210530ae9c5f0c03da23f","Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Hsue, B., Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Masters, P.S., Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","The subgenomic mRNAs of the coronavirus mouse hepatitis virus (MHV) are composed of a leader sequence, identical to the 5' 70 nucleotides of the genome, joined at distant downstream sites to a stretch of sequence that is identical to the 3' end of the genome. The points of fusion occur at intergenic sequences (IGSs), loci on the genome that contain a tract of sequence homologous to the 3' end of the leader RNA. We have constructed a mutant of MHV-A59 containing an extra IGS inserted into the genome immediately downstream of the 3'-most gene, that encoding the nucleocapsid (N) protein. We show that in cells infected with the mutant, there is synthesis of an additional leader-containing subgenomic RNA of the predicted size. Our study demonstrates that (i) an IGS can be a sufficient cis-acting element to dictate MHV transcription, (ii) the relative efficiency of an IGS must be influenced by factors other than the nucleotides immediately adjacent to the 5'AAUCUA AAC3' core consensus sequence or its position relative to the 3' end of the genome, (iii) a downstream IGS can exert a polar attenuating effect on upstream IGSs, and (iv) unknown factors prevent the insertion of large exogenous elements between the N gene and the 3' untranslated region of MHV. These results confirm and extend conclusions previously derived from the analysis of defective interfering RNAs.",,"messenger RNA; animal cell; article; gene locus; gene sequence; mouse; murine hepatitis coronavirus; nonhuman; priority journal; RNA analysis; virus gene; virus transcription; 5' Untranslated Regions; Animals; Base Sequence; Cell Line; DNA, Viral; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutagenesis, Insertional; RNA, Viral; Transcription, Genetic; Virus Replication","An, S., Makino, S., Characterizations of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency (1998) Virology, 243, pp. 198-207; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. 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Plenum Press, New York, N.Y; Van Marle, G., Luytjes, W., Van Der Most, R.G., Van Der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Williams, G.D., Chang, R.-Y., Brian, D.A., Evidence for a pseudoknot in the 3′ untranslated region of the bovine coronavirus genome (1995) Advances in Experimental Medicine and Biology, Vol. 380. Corona-and Related Viruses, 380, pp. 511-514. , P. J. Talbot and G. A. Levy (ed.). Plenum Press, New York, N.Y; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"10364371","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0033033638
"Kapil S., Richardson K.L., Maag T.R., Goyal S.M.","7003293348;19636522900;6603019250;7202441793;","Characterization of bovine coronavirus isolates/from eight different states in the USA",1999,"Veterinary Microbiology","67","3",,"221","230",,11,"10.1016/S0378-1135(99)00042-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033051455&doi=10.1016%2fS0378-1135%2899%2900042-5&partnerID=40&md5=7736dfa64ff445393051f5239c3d9d13","Dept. Diagn. Med.-Pathobiology C., Kansas Stt. Univ., 1800 Denison Ave., Manhattan, KS 66506, United States; Dept. of Vet. Diagnostic Medicine, Coll. Vet. Med., Univ. of Minnesota, St. Paul, MN 55108, United States","Kapil, S., Dept. Diagn. Med.-Pathobiology C., Kansas Stt. Univ., 1800 Denison Ave., Manhattan, KS 66506, United States; Richardson, K.L., Dept. Diagn. Med.-Pathobiology C., Kansas Stt. Univ., 1800 Denison Ave., Manhattan, KS 66506, United States; Maag, T.R., Dept. Diagn. Med.-Pathobiology C., Kansas Stt. Univ., 1800 Denison Ave., Manhattan, KS 66506, United States; Goyal, S.M., Dept. of Vet. Diagnostic Medicine, Coll. Vet. Med., Univ. of Minnesota, St. Paul, MN 55108, United States","Bovine coronavirus isolates from eight different states of the USA were compared for their antigenic properties and susceptibility to hygromycin B. Antigenic differences were observed among the isolates in a one-way hemagglutination-inhibition (HI) test using a polyclonal antiserum against the Mebus bovine coronavirus isolate. Differences were observed on isoelectric focusing among viral proteins with isoelectric points between 4.45-4.65. Most of the BCV isolates were susceptible to hygromycin B (0.5mM) whereas a few hygromycin B resistant isolates were also found. Copyright (C) 1999 Elsevier Science B.V.","Antigenic subtypes; Bovine coronavirus; Hygromycin B","hygromycin b; virus antibody; virus antigen; virus protein; virus vaccine; animal cell; antiviral activity; article; controlled study; coronavirus; erythrocyte; hemagglutination inhibition; isoelectric focusing; mouse; nonhuman; virus characterization; virus hemagglutination; virus purification; virus virulence; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Hemagglutination Inhibition Tests; Hemagglutination Tests; Humans; Hygromycin B; Isoelectric Focusing; Mice; Tumor Cells, Cultured; United States; Viral Proteins; Bovinae; Bovine coronavirus; Coronavirus","Clark, M.A., Campbell, I., El-Ghorr, A.A., Snodgrass, D.R., A comparison of bovine coronavirus trains using monoclonal antibodies (1990) Adv. Exp. Med. Biol., 276, pp. 461-466; Clark, M.A., Bovine coronavirus (1993) Br. Vet. 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Invest., 7, pp. 538-539; Kapil, S., Richardson, K.L., Radi, C., Chard-Bergstrom, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J. Vet. Diagn. Invest., 8, pp. 96-99; Kapil, S., Tent, A.M., Goyal, S.M., Excretion and persistence of bovine coronavirus in neonatal calves (1990) Arch. Virol., 115, pp. 127-132; King, B., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Lai, M.M.C., Transcription, replication, and engineering of coronavirus genes (1995) Adv. Expt. Med. Biol., 380, pp. 463-478; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch. Virol, 131, pp. 455-465; Oleszak, E.L., Knisley, T., Rodkey, L.S., Leibowitz, J.L., Microheterogeneity of S-glycoprotein of mouse hepatitis virus temperature-sensitive mutants (1992) J. Virol. Meth., 38, pp. 103-112; Sadasiv, E.C., Yeh, T.T., Chang, P.W., PI alteration related to strain variation of infectious bronchitis virus, an avian coronavirus (1991) J. Virol. Meth., 33, pp. 115-125; Saif, L.J., (1993) Coronavirus Immunogens. Vet. Microbiol., 37, pp. 285-295; Sato, K., Inaba, Y., Kurogi, H., Hemagglutination by calf diarrhea coronavirus (1977) Vet. Microbiol., 2, pp. 83-87; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor destroying and acetylesterase activities of avirulent and virulent coronavirus strains (1992) Arch. Virol., 125, pp. 193-204; Thurber, E.T., Bass, E.P., Beckenhauer, W.H., Field trial evaluation of a reo-coronavirus calf diarrhea vaccine (1977) Can. J. Comp. Med., 41, pp. 131-136; Tsunemitsu, H., Saif, L.F., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol., 140, pp. 1303-1311; Vautherot, J.F., Laporte, J., Utilization of monoclonal antibodies for antigenic characterization of coronaviruses (1983) Ann. Rech. Vet., 14, pp. 437-444; Virtala, A.K., Mechor, G.D., Grohn, Y.T., Ereb, H.N., Morbidity from nonrespiratory diseases and mortality in dairy heifers during the first three months of life (1996) JAVMA, 208, pp. 2043-2046; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852","Kapil, S.; Dept. Diagnostic Medicine-Pathobiol., College of Veterinary Medicine, Kansas State University, 1800 Denison Avenue, Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,03781135,,VMICD,"10418876","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0033051455
"Bandai C., Ishiguro S., Masuya N., Hohdatsu T., Mochizuki M.","6506323730;35589050100;6506308704;57197786893;7403050664;","Canine Coronavirus Infections in Japan: Virological and Epidemiological Aspects",1999,"Journal of Veterinary Medical Science","61","7",,"731","736",,38,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033159575&partnerID=40&md5=57da7a78ec3876e68fab5668ffee72d1","Central Laboratories, Kyoritsu Shoji Corporation, 2-9-22 Takamihara, Kukisaki, Ibaraki 300-1252, Japan; Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034-0021, Japan; Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, Tokyo 102-0073, Japan; Lab. of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyodaku, Tokyo 102-0073, Japan","Bandai, C., Central Laboratories, Kyoritsu Shoji Corporation, 2-9-22 Takamihara, Kukisaki, Ibaraki 300-1252, Japan; Ishiguro, S., Central Laboratories, Kyoritsu Shoji Corporation, 2-9-22 Takamihara, Kukisaki, Ibaraki 300-1252, Japan; Masuya, N., Central Laboratories, Kyoritsu Shoji Corporation, 2-9-22 Takamihara, Kukisaki, Ibaraki 300-1252, Japan; Hohdatsu, T., Dept. of Vet. Infectious Diseases, Sch. of Vet. Med. and Anim. Sciences, Kitasato University, Towada, Aomori 034-0021, Japan; Mochizuki, M., Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, Tokyo 102-0073, Japan, Lab. of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyodaku, Tokyo 102-0073, Japan","Ten strains, eight field and two reference laboratory strains, of canine coronavirus (CCV) were comparatively examined with respect to antigenic relationships and pathogenic potential in dogs. With monoclonal antibodies and hyperimmune antisera to feline coronavirus and CCV, respectively, varying degrees of antigenic diversities were found among the strains by neutralization and immunofluorescence assays, but it was felt that they belong to one serotype. Specific-pathogen-free puppies experimentally inoculated with some CCV strains manifested clinical symptoms, but there was a difference in their virulence. In order to elucidate the prevalence of CCV infections in dogs in Japan, we tested for neutralizing antibodies to CCV in 467 field dogs, and found a prevalence of 44.1%. Moreover, by using nested reverse transcriptase - polymerase chain reaction on rectal swabs of 100 diarrheic dogs recently presented in veterinary clinics, evidence of CCV in 16% of these specimens was found. The results suggested that CCV infection is more widespread than expected in dogs, and that CCV is a significant etiologic factor in canine diarrhea also in Japan.","Canine; Canine coronavirus; Diarrhea; Enteritis","Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline coronavirus; virus antibody; virus antigen; animal; animal disease; antigenic variation; article; blood; cat; classification; comparative study; Coronavirus; diarrhea; dog; dog disease; Japan; methodology; pathogenicity; prevalence; reverse transcription polymerase chain reaction; virology; virulence; virus infection; Animals; Antibodies, Viral; Antigenic Variation; Antigens, Viral; Cats; Coronavirus; Coronavirus Infections; Coronavirus, Canine; Diarrhea; Dog Diseases; Dogs; Japan; Prevalence; Reverse Transcriptase Polymerase Chain Reaction; Virulence","Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet. Med., 83, pp. 360-366; Appel, M.J.G., Cooper, B.J., Greisen, H., Carmichael, L.E., Status report: Canine viral enteritis (1978) J. Am. Vet. Med. Assoc., 173, pp. 1516-1518; Appel, M.J.G., Cooper, B.J., Greisen, H., Scott, F., Carmichael, L.E., Canine viral enteritis. I. Status report on corona- And parvo-like viral enteritides (1979) Cornell Vet., 69, pp. 123-133; Appel, M., Meunier, P., Pollock, R., Greisen, H., Carmichael, L., Glickman, L., Canine viral enteritis (1980) Canine Prac., 7, pp. 22-36; Barlough, J.E., Jacobson, R.H., Scott, F.W., Macrotiter assay for coronavirus-neutralizing activity in cats using a canine continuous cell line (A-72) (1983) Lab. Anim. Sci., 33, pp. 567-570; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc.78th Ann. Meeting us Anim. Health Assoc., pp. 359-366; Binn, L.N., Alford, J.P., Marchwicki, R.H., Keefe, T.J., Beattie, R.J., Wall, H.G., Studies of respiratory disease in random-source laboratory dogs: Viral infections in unconditioned dogs (1979) Lab. Anim. Sci., 29, pp. 48-52; Carmichael, L.E., Infectious canine enteritis caused by a coronaviral-type virus (1978) J. Am. Vet. Med. Assoc., 173, pp. 247-248; Carmichael, L.E., Binn, L.N., New enteric viruses in the dog (1981) Adv. Vet. Sci. Comp. Med., 25, pp. 1-37; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Golucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35, pp. 673-675; Heifer-Baker, C., Evermann, J.F., Mckeirnan, A.J., Morrison, W.B., Slack, R.L., Miller, C.W., Serological studies on the incidence of canine enteritis viruses (1980) Canine Prac., 7, pp. 37-42; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (MAbs): Preparation of MAbs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Vet. Microbiol, 28, pp. 13-24; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Arch. Virol., 117, pp. 85-95; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect. Immu., 37, pp. 1148-1155; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologie, histochemical, and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Kennedy, M.A., Brenneman, K., Millsaps, R.K., Black, J., Potgieter, L.N.D., Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis (1998) J. Vet. Diag. Invest., 10, pp. 93-97; Marshall, J.N., Healey, D.S., Studdert, M.J., Scott, P.C., Kennett, M.L., Ward, B.K., Gust, I.D., Viruses and virus-like particles in the faeces of dogs with and without diarrhoea (1984) Aust. Vet. J., 61, pp. 33-38; Mochizuki, M., Diarrhea causing viruses of dogs and cats (1996) J. Jpn. Vet. Med. Assoc., 49, pp. 293-300; Mochizuki, M., Sugiura, R., Akuzawa, M., Microneutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Pedersen, N.C., Ward, J., Mexgeling, W.L., Antigenic relationship of the feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., Mckeirnan, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Roseto, A., Lema, F., Cavalieri, F., Dianoux, L., Sitbon, M., Ferchal, F., Lasneret, J., Peries, J., Electron microscopy detection and characterization of viral particles in dog stools (1980) Arch. Virol., 66, pp. 89-93; Takeuchi, A., Binn, L.N., Jervis, H.R., Keenan, K.P., Hildebrandt, P.K., Valas, R.B., Bland, F.F., Electron microscope study of experimental enteric infection in neonatal dogs with a canine coronavirus (1976) Lab. Invest., 34, pp. 539-549; Vennema, H., Poland, A., Foley, J., Pederson, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike(S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen.Virol., 75, pp. 1789-1794; Yasoshima, A., Fujinami, F., Doi, K., Kojima, A., Takada, H., Okaniwa, A., Case report on mixed infection of canine parvovirus and canine coronavirus - Electron microscopy and recovery of canine coronavirus (1983) Jpn. J. Vet. Sci., 45, pp. 217-225","Mochizuki, M.; Lab. of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyodaku, Tokyo 102-0073, Japan",,,7653697,,,"10458093","English","J. Vet. Med. Sci.",Article,"Final",,Scopus,2-s2.0-0033159575
"Fukutomi T., Tsunemitsu H., Akashi H.","7103130680;7004628959;7103188256;","Detection of bovine coronaviruses from adult cows with epizootic diarrhea and their antigenic and biological diversities",1999,"Archives of Virology","144","5",,"997","1006",,23,"10.1007/s007050050562","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033056982&doi=10.1007%2fs007050050562&partnerID=40&md5=c941325c57cafaf32603eef01f3ce4e4","Okayama Pref. Vet. Diagn. Laboratory, Mitsu-cho, Okayama, Japan; Shichinohe Research Unit, National Institute of Animal Health, Shichinohe, Aomori, Japan; National Institute of Animal Health, Kannondai, Tsukuba, Ibaraki, Japan; National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-0856, Japan","Fukutomi, T., Okayama Pref. Vet. Diagn. Laboratory, Mitsu-cho, Okayama, Japan; Tsunemitsu, H., Shichinohe Research Unit, National Institute of Animal Health, Shichinohe, Aomori, Japan; Akashi, H., National Institute of Animal Health, Kannondai, Tsukuba, Ibaraki, Japan, National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-0856, Japan","Bovine coronavirus (BCV) was detected by reverse transcriptase-PCR, immune electron microscopy or virus isolation from adult cows at 6 out of 6 outbreak of epizootic diarrhea in Japan. Six BCVs isolated in feces, intestinal content or tracheal exudate of the cows were analyzed for their antigenic properties by cross virus neutralization (VN) tests. The isolates were divided into two groups, one of which had closely related antigenecity with the reference Mebus and Kakegawa strains of BCV, and another which showed significant differences in VN antibody titers from the reference strains. Two isolates in the latter group, which were from the enteric and respiratory tracts of the same cows, respectively, were distinguished from each other by ELISA using monoclonal antibodies against the Kakegawa strain. The isolates showed various hemagglutination and receptor destroying enzyme titers against chicken or mouse erythrocytes.",,"coronavirus; cow; diarrhea; electron microscopy; enzyme linked immunosorbent assay; monoclonal antibody; reverse transcription polymerase chain reaction; virus isolation; Animals; Antibody Formation; Antigenic Variation; Antigens, Viral; Cattle; Cattle Diseases; Chickens; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Disease Outbreaks; Enzyme-Linked Immunosorbent Assay; Erythrocytes; Feces; Female; Gastrointestinal Contents; Guinea Pigs; Hemagglutination Tests; Japan; Mice; Neutralization Tests; Receptors, Virus; Trachea; Variation (Genetics)","Akashi, H., Inaba, Y., Miura, Y., Tokuhisa, S., Satoda, K., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet Microbiol, 5, pp. 265-276; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Bridger, J.C., Woode, G.N., Meyling, A., Isolation of coronaviruses from neonatal calf diarrhea in Great Britain and Denmark (1978) Vet Microbiol, 3, pp. 101-113; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Dca, S., Roy, R.S., Elazhary, M.A., Antigenic variation among calf diarrhea coronaviruses by immunodiffusion and counterimmuno electrophoresis (1982) Ann Rech Vet, 13, pp. 351-356; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; Heckert, R.A., Saif, L.J., Myers, G.W., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immunofluoresccnce of nasal epithelial cells (1989) Vet Microbiol, 19, pp. 217-231; Horner, G.W., Hunter, R., Kirkbrid, C.A., A coronavirus-like agent present in faeces of cows with diarrhea (1975) N Z Vet J, 33, p. 98; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike protein distinguish between vaccine and wildtype strains (1991) Virology, 183, pp. 442-445; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am J Vet Res, 34, pp. 145-150; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nuclecocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-434; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.F., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of coronavirus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Morin, M., Lamothe, P., Gagnon, A., Malo, R., A case of viral neonatal calf diarrhea in a Quebec dairy herd (1974) Can J Comp Med, 38, pp. 236-242; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J.H., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Redman, D.R., Moodrhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Sato, M., Akashi, H., Hirai, S., Kimura, Y., Takahashi, M., Production of monoclonal antibodies against the Kakegawa strain of bovine coronavirus and their characterization (1991) J Vet Med Sci, 53, pp. 147-148; Sato, K., Inaba, Y., Kurogi, H., Takahashi, E., Satoda, K., Omori, T., Matsumoto, M., Hemagglutination by calf diarrhea coronavirus (1977) Vet Microbiol, 2, pp. 83-87; Schltze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrhea coronavirus (1976) Am J Vet Res, 37, pp. 1031-1041; Stair, E.L., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am J Vet Res, 33, pp. 1147-1156; Storz, J., Stine, L., Liem, A., Anderson, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) JAVMA, 208, pp. 1452-1455; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Takahashi, E., Inaba, Y., Sato, K., Ito, Y., Kurogi, H., Akashi, H., Satoda, K., Omori, T., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Tompkins, W.A., Watrach, A.M., Schmale, J.D., Shults, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 1101-1110; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Tsunemitsu, H., Yoncmichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; White, M.E., Schukken, Y.H., Tanksley, B., Space-time clustering of, and risk factors for, farmer-diagnosed winter dysentery in dairy cattle (1989) Can Vet J, 30, pp. 948-951","Akashi, H.; National Institute of Animal Health, 3-1-1 Kannondai, Tsukuba, Ibaraki 305-0856, Japan",,,03048608,,ARVID,"10416381","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033056982
"Gaber F., Kapil S.","6602697455;7003293348;","Development of an antigen spot test for detection of coronavirus in bovine fecal samples",1999,"Clinical and Diagnostic Laboratory Immunology","6","4",,"542","544",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032798036&partnerID=40&md5=5e1efabe7b24f92b245da9a62db7c2b9","Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Gaber, F., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States, Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","We have developed a rapid and sensitive microimmunodot blot assay, the antigen spot test (AST), for the detection of bovine coronavirus (BCV) antigen from neonatal calf fecal samples. The AST procedure can be completed in 3.5 h, whereas the previously reported immunodot blot assays require 10 to 12 h. Ninety-six samples can be tested per membrane, and 10 membranes (960 samples) may be processed by a single technologist in 1 working day. The effects of detergents, oxidizing chemicals, chaotropic agents, and enzyme substrates in improving the sensitivity and signal-to-noise ratio of the AST were studied. Finally, the sensitivity and specificity of AST for the detection of BCV antigen were compared to those of a sandwich enzyme-linked immunosorbant assay (ELISA) and a hemagglutination assay (HA). Of 347 field samples tested by all three methods, 94.2% were positive by AST, 91.4% were positive by ELISA, and 86.7% were positive by HA. The sensitivity of the AST was determined to be 100% compared to the results of the ELISA reference method. The specificity of the AST was 67%, which reflects a lower limit of detection of 104 viral particles per ml in a 10% fecal suspension.",,"antigen detection; article; controlled study; coronavirus; diarrhea; enzyme linked immunosorbent assay; feces analysis; hemagglutination; immunoblotting; laboratory test; nonhuman; priority journal; signal noise ratio; virus infection; Animals; Antigens, Viral; Cattle; Coronavirus; Enzyme-Linked Immunosorbent Assay; Feces; Hemagglutination Tests; Immunoblotting; Reference Standards; Sensitivity and Specificity","Akashi, H., Inaba, Y., Miura, Y., Tokuhisa, S., Sato, K., Satoda, K., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet. Microbiol., 5, pp. 265-276; Bridger, J.C., Woode, G.N., Meyling, A., Isolation of coronavirus from neonatal call diarrhea in Britain and Denmark (1978) Vet. Microbiol., 3, pp. 101-113; Carpenter, A.B., Enzyme-linked immunoassays (1997) Manual of Clinical Laboratory Immunology, 5th Ed., pp. 20-29. , N. R. Rose, E. Conway de Macario, J. D. Folds, H. C. Lane, and R. M. Nakamura (ed.), American Society for Microbiology, Washington, D.C; Crouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture enzyme-linked immunosorbent assay for detection of bovine enteric coronavirus (1984) J. Clin. Microbiol., 19, pp. 388-393; Czeruy, C.P., Eichhorn, W., Characterization of monoclonal and polyclonal antibodies to bovine enteric coronavirus: Establishment of an efficient ELISA for antigen detection in feces (1989) Vet. Microbiol., 20, pp. 111-122; Daginakatte, G.C., Chard-Bergstrom, C., Andrews, G.A., Kapil, S., Production, characterization, and uses of monoclonal antibodies against recombinant nueleoprotein of elk coronavirus (1999) Clin. Diagn. Lab. Immunol., 6, pp. 341-344; Goding, J., Purification, fragmentation and isotopic labelling of monoclonal antibodies (1996) Monoclonal Antibodies Principles and Practice, pp. 104-141. , J. W. Goding (ed.), Academic Press, Inc., San Diego, Calif; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., A longitudinal study of bovine coronavirus enteric and respiratory infection in dairy calves in two herds in Ohio (1990) Vet. Microbiol., 22, pp. 187-201; Heckert, R.A., Saif, L.J., Myers, G.W., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immuno-fluorescence of nasal epithelial cells (1989) Vet. Microbiol., 19, pp. 217-231; Herbrink, P., Van Bussel, F.J., Warnaar, S.O., The antigen spot test (AST): A highly sensitive assay for the detection of antibodies (1982) J. Immunol. Methods, 48, pp. 293-298; House, J.A., Economics of the rotavirus and other neonatal disease agents of animals (1978) J. Am. Vet. Med. Assoc., 173, pp. 573-576; Kapil, S., Pomeroy, K.A., Goyal, S.M., Trent, A.M., Experimental infection with a virulent pneumoenteric isolate of bovine coronavirus (1991) J. Vet. Diagn. Invest., 3, pp. 88-89; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral entritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am. J. Vet. Res., 40, pp. 1476-1478; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet. Microbiol., 9, pp. 425-434; Noorduyn, L.A., Meddens, M.J., Lindeman, J., Van-Dijk, W.C., Herbrink, P., Favorable effect of detergent on antigen detection and comparison of enzyme linked detection systems in an ELISA for Chlamydia trachomatis (1989) J. Immunoassay, 10, pp. 429-448; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch. Virol., 85, pp. 71-83; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infection in calves: Viral replication in the respiratory and intestinal tracts (1986) Am. J. Vet. Res., 47, pp. 1426-1432; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet. Res., 123, pp. 300-301; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved (1990) Cornell Vet., 80, pp. 303-311; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet. Rec., 128, pp. 447-449; Schoenthaler, S.L., Kapil, S., Development and application of a bovine coronavirus antigen detection enzyme-linked immunosorbent assay (1999) Clin. Diagn. Lab. Immunol., 6, pp. 130-132; Stair, L.E., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am. J. Vet. Res., 33, pp. 1147-1156; Tahir, R.A., Pomeroy, K.A., Goyal, S.M., Evaluation of shell vial cell culture technique for the detection of bovine coronavirus (1995) J. Vet. Diagn. Invest., 7, pp. 301-304; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Reed, H.H., Saif, L.J., Isolation of coronavirus antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J. Clin. Microbiol., 33, pp. 3264-3269; Vanrompay, D., Van Nerom, A., Ducatelle, R., Haesebrouck, F., Evaluation of live immuno-assays for detection of Chlamydia psittaci in cloacal and conjunctival specimens from turkeys (1994) J. Clin. Microbiol., 32, pp. 1470-1474; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Minocha, H.C., Kapil, S., Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalin-fixed intestines (1997) J. Clin. Microbiol., 35, pp. 2964-2965","Kapil, S.; Diagnostic Med.-Pathobiology Dept., College of Veterinary Medicine, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States; email: kapil@vet.ksu.edu",,,1071412X,,CDIME,"10391859","English","Clin. Diagn. Lab. Immunol.",Article,"Final",,Scopus,2-s2.0-0032798036
"Dessau R.B., Lisby G., Frederiksen J.L.","6603866036;6603928311;7102315536;","Coronaviruses in spinal fluid of patients with acute monosymptomatic optic neuritis",1999,"Acta Neurologica Scandinavica","100","2",,"88","91",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032783042&partnerID=40&md5=ccda37b9df73f789c554771982b3acfd","Department of Clinical Microbiology, Herlev University Hospital, Herlev Ringvej, DK-2720 Herlev, Denmark; Department of Neurology, Glostrup University Hospital, Ndr. Ringvej, DK-2600 Glostrup, Denmark; Dept of Clinical Microbiology, Aalborg University Hospital, PO Box 365, DK-9000 Aalborg, Denmark","Dessau, R.B., Department of Clinical Microbiology, Herlev University Hospital, Herlev Ringvej, DK-2720 Herlev, Denmark, Dept of Clinical Microbiology, Aalborg University Hospital, PO Box 365, DK-9000 Aalborg, Denmark; Lisby, G., Department of Clinical Microbiology, Herlev University Hospital, Herlev Ringvej, DK-2720 Herlev, Denmark; Frederiksen, J.L., Department of Neurology, Glostrup University Hospital, Ndr. Ringvej, DK-2600 Glostrup, Denmark","Acute monosymptomatic optic neuritis (AMON) may be an initial symptom of multiple sclerosis (MS). Coronaviruses have been implicated in the etiology of MS. The objective of the present study was to look for coronaviral RNA in AMON, which could be present in the initial stages of the development of MS. Material and methods - Spinal fluids from 37 patients with AMON and 15 surgical control patients with protrusion of the intervertebral disk were assayed with a nested multiplex polymerase chain reaction with primers specific for human coronaviruses strain (HCV) 229E and OC43. Results - Four patients and 1 control were positive for HCV-229E. No evidence of HCV-OC43 was found. The frequency of positive samples was low and there was no statistical difference between AMON and controls. Conclusion - This study does not provide evidence for an etiological role of human coronaviruses in acute monosymptomatic optic neuritis.","Human coronavirus; Multiple sclerosis; Optic neuritis; Polymerase chain reaction","article; clinical article; controlled study; Coronavirus; human; human cell; human tissue; intervertebral disk disease; optic nerve disease; polymerase chain reaction; RNA analysis; strain difference; Acute Disease; Adolescent; Adult; Cerebrospinal Fluid; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus OC43, Human; Female; Humans; Male; Middle Aged; Optic Neuritis; Reverse Transcriptase Polymerase Chain Reaction; RNA; RNA, Viral","Wray, S.H., Optic neuritis (1997) Clinical and Pathogenetic Basis, pp. 21-30. , Raine CS et al., eds. Multiple sclerosis. London: Chapman and Hall Medical; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann Neurol, 31, pp. 525-533; Cristallo, A., Gambaro, F., Biamonti, G., Ferrante, P., Battaglia, M., Cereda, P.M., Human coronavirus poly-adenylated RNA sequences in cerebrospinal fluid from multiple sclerosis patients (1997) New Microbiol, 20, pp. 105-114; Southern, E.M., Detection of specific sequences among DNA fragments separated by gel electrophoresis (1975) J Mol Biol, 98, p. 503; Wisconsin Package, Version 9.1, , Genetics Computer Group (GCG) 575 Science Drive, Madison, Wisconsin, USA 53711; Schreiber, J., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Myint, S., Harmsen, D., Raabe, T., Siddell, S., Human coronavirus mRNA for nucleocapsid protein (1993) Genbank, , Acc. X51325; Eckert, K.A., Kunkel, T.A., The fidelity of DNA polymerases used in the polymerase chain reactions (1991) PCR. A Practical Approach, pp. 225-244. , McPherson MJ et al. Oxford: IRL Press at Oxford University Press; Krawczak, M., Reiss, J., Schmidtke, J., Rösler, U., Polymerase chain reaction: Replication errors and reliability of gene diagnosis (1989) Nucleic Acids Res, 17, pp. 2197-2201; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res, 12, pp. 1-9; Cruciere, C., Laporte, J., Sequence and analysis of bovine enteritic coronavirus (1988) Ann Inst Pasteur Virol, 139, pp. 123-138","Dessau, R.B.; Dept. of Clinical Microbiology, Aalborg University Hospital, PO Box 365, DK-9000 Aalborg, Denmark",,,00016314,,ANRSA,"10442448","English","Acta Neurol. Scand.",Article,"Final",,Scopus,2-s2.0-0032783042
"Xue S., Sun N., Van Rooijen N., Perlman S.","7202791284;57214909902;35428581800;7102708317;","Depletion of blood-borne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus",1999,"Journal of Virology","73","8",,"6327","6334",,44,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032813555&partnerID=40&md5=78a8b6018d1f488ff062cec65b95630f","Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Dept. of Cell Biology and Immunology, Medical Faculty, Vrije Universiteit, Amsterdam, Netherlands; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Xue, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Sun, N., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Van Rooijen, N., Dept. of Cell Biology and Immunology, Medical Faculty, Vrije Universiteit, Amsterdam, Netherlands; Perlman, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Mice infected with the neurotropic coronavirus mouse hepatitis virus strain JHM (MHV-JHM) develop a chronic demyelinating disease with symptoms of hindlimb paralysis. Histological examination of the brains and spinal cords of these animals reveals the presence of large numbers of activated macrophages/microglia. In two other experimental models of demyelination, experimental allergic encephalomyelitis and Theiler's murine encephalomyelitis virus-induced demyelination, depletion of hematogenous macrophages abrogates the demyelinating process. In both of these diseases, early events in the demyelinating process are inhibited by macrophage depletion. From these studies, it was not possible to determine whether infiltrating macrophages were required for late steps in the process, such as myelin removal. In this study, we show that when macrophages are depleted with either unmodified or mannosylated liposomes encapsulating dichloromethylene diphosphate, the amount of demyelination detected in MHV- infected mice is not affected. At a time when these cells were completely depleted from the liver, approximately equivalent numbers of macrophages were present in the spinal cords of control and drug-treated animals. These results suggest that blood-borne macrophages are not required for MHV- induced demyelination and also suggest that other cells, such as perivascular macrophages or microgila, perform the function of these cells in the presence of drug.",,"liposome; major histocompatibility antigen class 1; major histocompatibility antigen class 2; allergic encephalitis; animal experiment; animal model; animal tissue; antigen expression; article; cell loss; controlled study; coronavirus; demyelination; hindlimb; immunohistochemistry; inoculation; macrophage; microglia; mouse; neuropathology; neurotropism; nonhuman; paralysis; priority journal; virus load; virus strain; Animals; Central Nervous System; Chronic Disease; Clodronic Acid; Coronavirus; Coronavirus Infections; Demyelinating Diseases; Histocompatibility Antigens Class I; Histocompatibility Antigens Class II; Macrophages; Mice; Mice, Inbred BALB C; Microglia; Murine hepatitis virus; Time Factors","Bauer, J., Huitinga, I., Zhao, W., Lassmann, H., Hickley, W.F., Dijkstra, C.D., The role of macrophages, perivascular cells, and microglial cells in the pathogenesis of experimental autoimmune encephalomyelitis (1995) Glia, 15, pp. 437-446; Biewenga, J., Van Der Ende, M.B., Kristi, L.F.G., Borst, A., Ghufron, M., Macrophage depletion in the rat after intraperitoneal administration of liposome-encapsulated clodronate: Depletion kinetics and accelerated repopulation of peritoneal and omental macrophages by administration of Freund's adjuvant (1995) Cell Tissue Res., 280, pp. 189-196; Ciavarra, R.P., Buhrer, K., Van Rooijen, N., Tedeschi, B., T cell priming against vesicular stomatitis virus analyzed in situ (1997) J. Immunol., 158, pp. 1749-1755; Cserr, H.F., Knopf, P.M., Cervical lymphatics, the blood-brain barrier and the immunoreactivity of the brain: A new view (1992) Immunol. Today, 13, pp. 507-512; Ford, A.L., Goodsall, A.L., Hickey, W.F., Sedgwick, J.D., Normal adult ramified microglia separated from other central nervous system macrophages by flow cytometric sorting (1995) J. Immunol., 154, pp. 4309-4321; Hickey, W., Kimura, H., Perivascular microglial cells of the CNS are bone marrow-derived and present antigen in vivo (1988) Science, 239, pp. 290-292; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Huitinga, I., Damoiseaux, J.G.M.C., Van Rooijen, N., Dopp, E.A., Dykstra, C.D., Liposome mediated affection of monocytes (1992) Immunobiology, 185, pp. 11-19; Huitinga, I., Ruuls, S.R., Jung, S., Van Rooijen, N., Hartung, H.-P., Dijkstra, C.D., Macrophages in T cell line-mediated, demyelinating, and chronic relapsing experimental autoimmune encephalomyelitis in Lewis rats (1995) Clin. Exp. Immunol., 100, pp. 344-351; Huitinga, I., Van Rooijen, N., De Groot, C.J.A., Uitdehaag, B.M.J., Dijkstra, C.D., Suppression of experimental allergic encephalomyelitis in Lewis rats after elimination of macrophages (1990) J. Exp. Med., 172, pp. 1025-1033; Knobler, R., Haspel, M., Oldstone, M.B.A., Mouse hepatitis virus type-4 (JHM strain) induced fatal nervous system disease. I. Genetic control and the murine neuron as the susceptible site of disease (1981) J. Exp. Med., 153, pp. 832-843; Lampert, P.W., Sims, J.K., Kniazeff, A.J., Mechanism of demyelination in JHM virus encephalomyelitis (1973) Acta Neuropathol., 24, pp. 76-85; Lampson, L.A., Interpreting MHC class I expression and class I/class II reciprocity in the CNS: Reconciling divergent findings (1995) Microsc. Res. Tech., 32, pp. 267-285; Lipton, H.L., Twaddle, G., Jelachich, M.L., The predominant virus antigen burden is present in macrophages in Theiler's murine encephalomyelitis virus-induced demyelinating disease (1995) J. Virol., 69, pp. 2525-2533; Lynch, F., Doherty, P.C., Ceredig, R., Phenotypic and functional analysis of the cellular response in regional lymphoid tissue during an acute virus infection (1989) J. Immunol., 142, pp. 3592-3598; Martiney, J.A., Rajan, A.J., Charles, P.C., Cerami, A., Ulrich, P.C., Machphail, S., Tracey, K.J., Brosnan, C.F., Prevention and treatment of experimental autoimmune encephalomyelitis by CNI-1493, a macrophage-deactivating agent (1998) J. Immunol., 160, pp. 5588-5595; McKnight, A.J., Macfarlane, A.J., Dri, P., Turlety, L., Willis, A.C., Molecular cloning of F4/80, a murine macrophage-restricted cell surface glycoprotein with homology to the G protein-linked transmembrane 7 hormone receptor family (1996) J. Biol. Chem., 271, pp. 486-489; McLean, I.W., Nakane, P.K., Periodate-lysine-paraformaldehyde fixative: A new fixative for immunoelectron microscopy (1974) J. Histochem. Cytochem., 22, pp. 1077-1083; Perlman, S., Ries, D., The astrocyte is a target cell in mice persistently infected with mouse hepatitis virus, strain JHM (1987) Microb. Pathog., 3, pp. 309-314; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating encephalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog., 2, pp. 185-194; Pewe, L., Wu, G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Pewe, L., Xue, S., Perlman, S., Infection with cytotoxic T-lymphocyte escape mutants results in increased mortality and growth retardation in mice infected with a neurotropic coronavirus (1998) J. Virol., 72, pp. 5912-5918; Polman, C.H., Dijkstra, C.D., Sminia, T., Koetsier, J.C., Immunohistochemical analysis of macrophages in the central nervous system of Lewis rats with acute experimental allergic encephalomyelitis (1986) J. Neuroimmunol., 11, pp. 215-222; Raine, C.S., Multiple sclerosis: Immune system molecule expression in the central nervous system (1994) J. Neuropathol. Exp. Neurol., 53, pp. 328-337; Rossi, C.P., Delcroix, M., Huitinga, I., McAllister, A., Van Rooijen, N., Claassen, E., Brahic, M., Role of macrophages during Theiler's virus infection (1997) J. Virol., 71, pp. 3336-3340; Sedgwick, J.D., Ford, A.L., Foulcher, E., Airriess, R., Central nervous system microglial cell activation and proliferation follows direct interaction with tissue-infiltrating T cell blasts (1998) J. Immunol., 160, pp. 5320-5330; Sedgwick, J.D., Schwender, S., Imrich, H., Dorries, R., Butcher, G., Ter Meulen, V., Isolation and direct characterization of resident microglial cells from the normal and inflamed central nervous system (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 7438-7442; Sorensen, O., Perry, D., Dales, S., In vivo and in vitro models of demyelinating diseases. III. JHM virus infection of rats (1980) Arch. Neurol., 37, pp. 478-484; Stevenson, P., Freeman, S., Bangham, C.R.M., Hawke, S., Virus dissemination through the brain parenchyma without immunologic control (1997) J. Immunol., 159, pp. 1876-1884; Stevenson, P.G., Hawke, S., Sloan, D.J., Bangham, C.R.M., The immunogenicity of intracerebral virus infection depends on anatomical site (1997) J. Virol., 71, pp. 145-151; Stohlman, S.A., Bergmann, C.C., Perlman, S., Persistent infection by mouse hepatitis virus (1998) Persistent Viral Infections, pp. 537-557. , R. Ahmed and I. Chen (ed.). John Wiley & Sons, Inc., New York, N.Y; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Sun, N., Grzybicki, D., Castro, R., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Tran, E.H., Hoesktra, K., Van Rooijen, N., Dijkjstra, C.D., Owens, T., Immune invasion of the central nervous system parenchyma and experimental allergic encephalomyelitis, but not leukocyte extravasation from blood, are prevented in macrophage-depleted mice (1998) J. Immunol., 161, pp. 3767-3775; Van Rooijen, N., Bakker, J., Sanders, A., Transient suppression of macrophage functions by liposome-encapsulated drugs (1997) Trends Biotechnol., 15, pp. 178-185; Van Rooijen, N., Kors, N., Kraal, G., Macrophage subset repopulation in the spleen: Differential kinetics after liposome-mediated elimination (1989) J. Leukoc. Biol., 45, pp. 97-104; Van Rooijen, N., Sanders, A., Liposome mediated depletion of macrophages: Mechanism of action, preparation of liposomes and applications (1994) J. Immunol. Methods, 174, pp. 83-93; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wijburg, O.L.C., Heemskerk, M.H.M., Boog, C.J.P., Van Rooijen, N., Role of spleen macrophages in innate and acquired immune responses against mouse hepatitis virus strain A59 (1997) Immunology, 92, pp. 252-258","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"10400724","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032813555
"Freymuth F., Vabret A., Brouard J., Toutain F., Verdon R., Petitjean J., Gouarin S., Duhamel J.-F., Guillois B.","7103410207;7003959575;7005417717;6603726795;55898524800;7006379234;56107903900;7102076710;7005164878;","Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae infections in exacerbations of asthma in children",1999,"Journal of Clinical Virology","13","3",,"131","139",,177,"10.1016/S1386-6532(99)00030-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032797581&doi=10.1016%2fS1386-6532%2899%2900030-X&partnerID=40&md5=69061a04af70e0a4f892f88009898034","Lab. of Human and Molecular Virology, Univ. Hosp., Av. G. C., Caen, France; Department of Paediatry, Univ. Hosp., Av. G. C., Caen, France; Department of Infectious Diseases, Univ. Hosp., Av. G. C., Caen, France","Freymuth, F., Lab. of Human and Molecular Virology, Univ. Hosp., Av. G. C., Caen, France; Vabret, A., Lab. of Human and Molecular Virology, Univ. Hosp., Av. G. C., Caen, France; Brouard, J., Department of Paediatry, Univ. Hosp., Av. G. C., Caen, France; Toutain, F., Department of Paediatry, Univ. Hosp., Av. G. C., Caen, France; Verdon, R., Department of Infectious Diseases, Univ. Hosp., Av. G. C., Caen, France; Petitjean, J., Lab. of Human and Molecular Virology, Univ. Hosp., Av. G. C., Caen, France; Gouarin, S., Lab. of Human and Molecular Virology, Univ. Hosp., Av. G. C., Caen, France; Duhamel, J.-F., Department of Paediatry, Univ. Hosp., Av. G. C., Caen, France; Guillois, B., Department of Paediatry, Univ. Hosp., Av. G. C., Caen, France","Background: A high frequency of virus infections has been recently pointed out in the exacerbations of asthma in children. Objectives: To confirm this, using conventional and molecular detection methods, and expanding the study to younger children. Study design: One hundred and thirty-two nasal aspirates from 75 children hospitalized for a severe attack of asthma were studied (32 infants, mean age 9.1 months; and 43 children, mean age 5.6 years). According to the virus, a viral isolation technique, immunofluorescence assays (IFA) or both were used for the detection of rhinovirus, enterovirus, respiratory syncytial (RS) virus, adenovirus, coronavirus 229E, influenza and parainfluenza virus. Polymerase chain reaction (PCR) assays were used for the detection of rhinovirus, enterovirus, RS virus, adenovirus, coronavirus 229E and OC43, Chlamydia pneumoniae and Mycoplasma pneumoniae. Results: Using IFA and viral isolation techniques, viruses were detected in 33.3% of cases, and by PCR techniques, nucleic acid sequences of virus, Chlamydia pneumoniae and Mycoplasma pneumoniae were obtained in 71.9% of cases. The combination of conventional and molecular techniques detects 81.8% of positive samples. Two organisms were identified in the same nasal sample in 20.4% of the cases. The percentage of detections was higher (85.9%) in the younger group than in the other (77%). The most frequently detected agents were rhinovirus (46.9%) and RS virus (21.2%). Using PCR rather than conventional techniques, the detection rates were increased 5.8- and 1.6-fold in rhinovirus and RS virus infections, respectively. The detection levels of the other organisms are as follows: 9.8, 5.1, 4.5, 4.5, 4.5, 3.7, and 2.2% for enterovirus, influenza virus, Chlamydia pneumoniae, adenovirus, coronavirus, parainfluenza virus, and Mycoplasma pneumoniae, respectively. Conclusion: These results confirm the previously reported high frequency of rhinovirus detection in asthmatic exacerbations in children. They also point out the frequency of RS virus detection, and emphasize the fact that PCR assays may be necessary to diagnose respiratory infections in asthma.","Asthma; Chlamydia; Mycoplasma; Respiratory syncytial virus; Rhinovirus","Adenovirus; adolescent; article; aspiration; asthma; child; Chlamydophila pneumoniae; Coronavirus; Enterovirus; human; immunofluorescence test; infant; major clinical study; Mycoplasma pneumoniae; nucleotide sequence; Parainfluenza virus; polymerase chain reaction; priority journal; Respiratory syncytial pneumovirus; Rhinovirus; virus detection; virus infection; Adolescent; Asthma; Child; Child, Preschool; Chlamydia Infections; Chlamydophila pneumoniae; Fluorescent Antibody Technique; Humans; Infant; Mycoplasma pneumoniae; Picornaviridae Infections; Pneumonia, Mycoplasma; Polymerase Chain Reaction; Respiratory Tract Infections; Virus Diseases; Viruses","De Barbeyrac, B., Bernet-Poggi, C., Febrer, F., Fenaudin, H., Dupon, M., Bebear, C., Detection of Mycoplasma pneumoniae and Mycoplasma genitalium in clinical samples by PCR (1993) Clin Infect Dis, 17 (SUPPL1), pp. 83-89; Douglas, R.G., Cate, T.R., Gerone, P.J., Couch, R.B., Quantitative rhinovirus shedding in volunteers (1966) Am Rev Respir Dis, 94, pp. 159-167; Freymuth, F., Petitjean, J., Pothier, P., Norrby, E., Prevalence of respiratory syncytial virus subgroups A and B in France, 1982 to 1990 (1991) J Clin Microbiol, 29, pp. 653-655; Freymuth, F., Quibriac, M., Petitjean, J., Pierre, C., Duhamel, J.F., Denis, A., Legoas, C., Rhinovirus et infections respiratoires aigues du nourrisson (1986) Arch Fr Pédiatr, 43, pp. 677-679; Freymuth, F., Quibriac, M., Petitjean, J., Daon, F., Amiel, M.L., Les virus responsables d'infections respiratoires en pédiatrie. Bilan de 3480 aspirations nasales réalisées chez l'enfant en une période de six ans (1987) Ann Pédiatr (Paris), 34, pp. 493-501; Freymuth, F., Eugene, G., Vabret, A., Petitjean, J., Gennetay, G., Brouard, J., Duhamel, J.F., Guillois, B., Detection of respiratory syncytial virus by reverse transcription-PCR and hybridization with DNA enzyme immunoassay (1995) J Clin Microbiol, 33, pp. 3352-3355. , [Erratum, J Clin Microbiol 1996;34:1601]; Freymuth, F., Vabret, A., Galateau-Salle, F., Ferey, J., Eugene, G., Petitjean, J., Gennetay, E., Guillois, B., Detection of respiratory syncytial virus, parainfluenzavirus 3, adenovirus and rhinovirus in respiratory tract of infants by PCR and hybridization (1997) Clin Diagn Virol, 8, pp. 31-40; Gama, R.E., Horsnell, P.R., Hughes, P.J., North, C., Bruce, C.B., Al Nakib, W., Stanway, G., Amplification of rhinovirus specific nucleic acids from clinical samples using the PCR (1989) J Med Virol, 28, pp. 73-77; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimenally-induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Hall, C.B., Douglas, R.G., Geiman, G.M., Respiratory syncytial virus infections in infants: Quantitation and duration of shedding (1976) J Pediatr, 89, pp. 11-15; Hierholzer, J.C., Halonen, P.E., Dahlen, P.O., Bingham, P.G., McDonough, M.M., Detection of adenovirus in clinical specimens by PCR and liquid-phase hybridization quantited by time-resolved fluorometry (1993) J Clin Microbiol, 31, pp. 1886-1891; Hyypïa, T., Auvinen, P., Maaronen, M., PCR for human picornaviruses (1989) J Gen Virol, 70, pp. 3261-3268; Jennings, L.C., Barns, G., Dawson, K.P., The association of viruses with acute asthma (1987) N Z Med J, 10, pp. 488-490; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Lambden, P.R., Holgate, S.T., Use of PCR for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 11-117; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L., Symington, P., Holgate, S.T., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) Br. Med J, 310, pp. 1225-1229; Kellner, G., Popow-Kraupp, T., Kundi, M., Binder, C., Kunz, C., Clinical manifestations of respiratory tract infections due to respiratory syncytial virus and rhinoviruses in hospitalized children (1989) Acta Paediatr Scand, 78, pp. 390-394; Mammes, O., (1994) Intérêts et Limites de la PCR Dans Le Diagnostic des Bronchiolites à Rhinovirus Chez Le Nourrisson, , Thesis Pharm, Paris, 5199494PA05PI82; Midulla, F., Villani, A., Panuska, J.R., Dab, I., Kolls, J.K., Merolla, R., Ronchetti, R., Respiratory syncytial virus lung infection in infants: Immunoregulatory role of infected alveolar macrophages (1993) J Infect Dis, 168, pp. 1515-1519; Nadel, J.A., Busse, W.W., Asthma (1998) Am J Respir Crit Care Med, 157, pp. 130-S138; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) Br Med J, 307, pp. 982-986; Pattemore, P.K., Johnston, S.L., Bardin, P.G., Viruses as precipitants of asthma symptoms. I. Epidemiology (1992) Clin Exp Allergy, 22, pp. 325-336; Petitjean, J., Vincent, F., Fretigny, M., Vabret, A., Poveda, J.D., Brun, J., Freymuth, F., Comparison of two serological methods and a PCR-enzyme immunoassay for the diagnosis of acute respiratory infections with Chlamydia pneumoniae in adults (1998) J Med Microbiol, 47, pp. 615-621","Freymuth, F.; Laboratory Human Molecular Virology, University Hospital, av. G. Clemenceau, 14033 Caen, France; email: freymuth-f@chu-caen.fr",,,13866532,,JCVIF,"10443789","English","J. Clin. Virol.",Article,"Final",,Scopus,2-s2.0-0032797581
"Foley J.E., Foley P., Pedersen N.C.","7402872921;7101667257;7202299909;","The persistence of a SIS disease in a metapopulation",1999,"Journal of Applied Ecology","36","4",,"555","563",,11,"10.1046/j.1365-2664.1999.00427.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032862888&doi=10.1046%2fj.1365-2664.1999.00427.x&partnerID=40&md5=f21ac8aa949d5989c98455320eeee0aa","School of Veterinary Medicine, Center for Companion, Animal Health, University of California, Davis, CA 95616, United States","Foley, J.E., School of Veterinary Medicine, Center for Companion, Animal Health, University of California, Davis, CA 95616, United States; Foley, P.; Pedersen, N.C.","1. Deterministic models predict that susceptible-infective-susceptible (SIS) disease, where there is no immunity to reinfection following recovery, will become infinitely persistent in a host population. We explored the incorporation of stochasticity into SIS models; modelled interacting host-disease agents in metapopulations; and examined model predictions in a real system involving viral infection in domestic cats. 2. SIS models incorporating stochasticity predicted that disease persistence would be finite and dependent on the host population size, provided the host population was isolated. However, the disease may persist by dynamic spread among interacting host metapopulations. 3. Feline enteric coronavirus (FECV) dynamics in domestic cats were well predicted by stochastic metapopulation models. 4. The models we present are mathematically tractable, generalizable, and mechanistically realistic. The findings from the cat-virus system are immediately applicable to the management of cattery populations and could be adapted to inform eradication programmes for other infectious diseases in animal and human populations. The most practical methods to eradicate feline enteric coranovirus would be to remove small catteries (islands) from interactions with large catteries (mainlands) and to convert mainlands to islands by depopulation.","Birth and death processes; Feline enteric coronavirus; Infectious disease; Spatial spread of disease","disease spread; ecological modeling; host-pathogen interaction; metapopulation; persistence","Bailey, N., (1975) The Mathematical Theory of Infectious Diseases and Its Applications, , Griffin, London, UK; Bartlett, M., Deterministic and stochastic models for recurrent epidemics (1956) Proceedings of the Third Berkeley Symposium on Mathematical Statistics and Probability, 4, pp. 81-109. , (ed. J. Neyman), University of California Press, Berkeley, CA; Bharucha-Reid, A., On the stochastic theory of epidemics (1956) Proceedings of the Third Berkeley Symposium on Mathematical Statistics and Probability, 4, pp. 111-119. , (ed. J. Neyman), University of California Press, Berkeley, CA; Van Den Bosch, F., Metz, A., Diekmann, O., The velocity of spatial population expansion (1990) Journal of Mathematical Biology, 28, pp. 529-565; Dietz, R., Heide-Jorgensen, M.-P., Harkonen, T., Mass deaths of harbor seals (Phoca vitulina) in Europe (1989) Ambio, 18, pp. 258-264; Durrett, R., Levin, S., Stochastic spatial models: A user's guide to ecologica applications (1994) Philosophical Transactions of the Royal Society of London, Series B, 343, pp. 329-350; Edelstein-Keshet, L., (1988) Mathematical Models in Biology, , Random-House, New York, NY; Feller, W., (1971) An Introduction to Probability Theory and Its Applications, 2. , Wiley, New York, NY; Ferguson, N., May, R., Anderson, R., Measles: Persistence and synchronicity in disease dynamics (1997) Spatial Ecology: The Role of Space in Population Dynamics and Interspecific Interactions, pp. 137-157. , (eds D. Tilman & P. Kareiva), Princeton University Press, Princeton, NJ; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) Journal of the American Veterinary Medical Association, 210, pp. 1307-1312; Gardiner, C., (1985) Handbook of Stochastic Methods, , Springer, New York, NY; Grenfell, B., Bolker, B., Kleckowski, A., Seasonality, demography and the development dynamics of measles in developed countries (1995) Epidemic Models: Their Structure and Relation to Data, pp. 248-268. , (ed. D. Mollison), Cambridge University Press, Cambridge, UK; Gyllenberg, M., Hanski, I., Hastings, A., Structured metapopulation models (1997) Metapopulation Biology, pp. 93-122. , (eds I. Hanski & M. Gilpin), Academic Press, San Diego, CA; Hanski, I., Single-species metapopulation dynamics: Concepts, models and observations (1991) Bulletin of Journal of Linnaean Society, 42, pp. 17-38; Hanski, I., Foley, P., Hassell, M., Random walks in a metapopulation: How much density dependence is necessary for long-term persistence? (1996) Journal of Animal Ecology, 65, pp. 274-282; Harrison, S., Local extinction in a metapopulation context: An empirical evaluation (1991) Metapopulation Dynamics: Empirical and Theoretical Investigations, pp. 73-88. , (eds M. Gilpin & I. Hanski), Academic Press, London, UK; Harrison, S., Quinn, J., Correlated environments and the persistence of metapopulations (1959) Oikos, 56, pp. 293-298; Harrison, S., Taylor, A., Empirical evidence for metapopulation dynamics (1997) Metapopulation Dynamics: Empirical and Theoretical Investigations, pp. 27-42. , (eds M. Gilpin & I. Hanski), Academic Press, London, UK; Hethcote, H., Qualitative analyses of communicable disease models (1976) Mathematical Biosciences, 28, pp. 335-356; Ims, R., Yoccoz, N., Studying transfer processes in metapopulations. Emigration, migration, and colonization (1997) Metapopulation Biology. Ecology, Genetics, and Evolution, pp. 247-265. , (eds I. Hanski & M. Gilpin), Academic Press, San Diego, CA; Johnson, N.L., Kotz, S., Balakrishnan, N., (1994) Continuous Univariate Distributions, 1. , Wiley, New York, NY; Karlin, S., Taylor, H., (1975) A First Course in Stochastic Processes, , Academic Press, London, UK; Kermack, W., McKendrick, A., Contributions to the mathematical theory of epidemics (1927) Royal Statistical Society Journal, 115, pp. 700-721; Lajmanovich, A., Yorke, J., A deterministic model for gonorrhea in a nonhomogeneous population (1976) Mathematical Biosciences, 28, pp. 221-236; Levins, R., Some demographic and genetic consequences of environmental heterogeneity for biological control (1969) Bulletin of Entomological Society of America, 15, pp. 237-240; MacArthur, R., Wilson, E., (1967) The Theory of Island Biogeography, , Princeton University Press, Princeton, NJ; May, R., Anderson, R., Spatial heterogeneity and the design of immunization programs (1984) Mathematical Biosciences, 72, pp. 83-111; Mollison, D., The importance of demographic stochasticity in population dynamics (1981) The Mathematical Theory of the Dynamics of Biological Populations II, pp. 99-107. , (eds R. Hiorns & D. Cooke), Academic Press, London, UK; Mollison, D., Dependence of epidemic and population velocities on basic parameters (1991) Mathematical Biosciences, 107, pp. 255-287; Mollison, D., Kuulasmaa, K., Spatial epidemic models: Theory and simulations (1985) Population Dynamics of Rabies in Wildlife, pp. 291-309. , (ed. P. Bacon), Academic Press, London, UK; Murray, J., (1989) Mathematical Biology, , Springer, New York, NY; Nisbet, R., Gurney, W., (1982) Modelling Fluctuating Populations, , Wiley, New York, NY; Paul, J., Freese, H., An epidemiological study of the 'common cold' in an isolated arctic community (Spitzbergen) (1933) American Journal of Hygiene, 17, p. 517; Pedersen, N., The history and interpretation of feline coronavirus serology (1995) Feline Practice, 23, pp. 46-52; Pedersen, N.C., Boyle, J.F., Floyd, K., Fudge, A., Barker, A., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) American Journal of Veterinary Research, 42, pp. 368-477; Poland, A., Vennema, H., Foley, J.E., Pedersen, N.C., Feline infectious peritonitis is caused by simple mutants of feline enteric coronavirus (FECV) that arise frequently during the course of primary FECV infection (1996) Journal of Clinical Microbiology, 34, pp. 3180-3184; Shibli, M., Gooch, S., Lewis, H., Tyrrell, D., Common colds on Tristan da Cunha (1971) Journal of Hygiene, Cambridge, 69, pp. 255-262; Sjogren Gulve, P., Distribution and extinction patterns within a northern metapopulation case of the pool frog, Rana lessonae (1994) Ecology, 75, pp. 1357-1367; Thomas, C., Hanski, I., Butterfly metapopulation (1997) Metapopulation Biology, pp. 359-386. , (eds I. Hanski & M. Gilpin), Associated Press, San Diego, CA","Foley, J.E.; School of Veterinary Medicine, Center for Companion, Animal Health, University of California, Davis, CA 95616, United States; email: jefoley@ucdavis.edu",,,00218901,,JAPEA,,"English","J. Appl. Ecol.",Article,"Final",,Scopus,2-s2.0-0032862888
"Brun A., Rodríguez F., Parra F., Sobrino F., Escribano J.M.","7202745069;18435465400;7005551438;7006219133;55402647000;","Design and construction of African swine fever virus chimeras incorporating foreign viral epitopes",1999,"Archives of Virology","144","7",,"1287","1298",,3,"10.1007/s007050050587","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032782149&doi=10.1007%2fs007050050587&partnerID=40&md5=b42302070935eb245f335fa2e2d19326","Ctro. de Investigacion en Sanid. A., Valdeolmos, Madrid, Spain; Depto. de Bioquimica y Biologia M., Instituto Univ. Biotecnologia de A., Universidad de Oviedo, Oviedo, Spain; Ctro. Biologia Molec. Severo Ochoa, Cantoblanco, Madrid, Spain; Depto. Mejora Genetica Biotecnologia, Madrid, Spain; Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA, United States; Depto. Mejora Genetica Biotecnologia, INIA, Ctra. de La Coruña, Km7, 28040 Madrid, Spain","Brun, A., Ctro. de Investigacion en Sanid. A., Valdeolmos, Madrid, Spain; Rodríguez, F., Ctro. de Investigacion en Sanid. A., Valdeolmos, Madrid, Spain, Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA, United States; Parra, F., Depto. de Bioquimica y Biologia M., Instituto Univ. Biotecnologia de A., Universidad de Oviedo, Oviedo, Spain; Sobrino, F., Ctro. de Investigacion en Sanid. A., Valdeolmos, Madrid, Spain, Ctro. Biologia Molec. Severo Ochoa, Cantoblanco, Madrid, Spain; Escribano, J.M., Depto. Mejora Genetica Biotecnologia, Madrid, Spain, Depto. Mejora Genetica Biotecnologia, INIA, Ctra. de La Coruña, Km7, 28040 Madrid, Spain","In the present work we have studied the feasibility of introducing foreign epitopes into the African swine fever virus (ASFV) particle by genetic manipulation of the virus. For this purpose, we developed specific transfer vectors containing the gene encoding for the highly antigenic structural ASFV protein p54 in which foreign sequences were introduced. DNA sequences encoding continuous linear epitopes, the antigenic site A from foot-and-mouth disease virus (FMDV) VP1 protein and the DA3 antigenic determinant from transmissible gastroenteritis coronavirus (TGEV) nucleoprotein N, were separately cloned into the p54 gene, in a region encoding a non-essential domain of the protein. Chimeric p54 genes were inserted by homologous recombination into the thymidine kinase (TK) locus of ASFV genome. The resulting recombinant viruses efficiently expressed both chimeric proteins under transcriptional control of the p54 promoter, and the chimeric gene products were recognized by antibodies to both p54 and foreign epitopes. The modified p54 proteins were also found in the viral particles and complemented the function of the wild-type p54, since deletion of the p54 gene from recombinant viruses did not affected virus replication in Vero cells. This work demonstrates for the first time the feasibility of incorporating foreign amino acid sequences (up to 18 residues) into a protein component of the ASFV particle without affecting virus viability.",,"African swine fever virus; amino acid sequence; chimera; epitope; foot and mouth disease virus; gene transfer; vector; African Swine Fever Virus; Amino Acid Sequence; Animals; Base Sequence; Capsid; Capsid Proteins; Cercopithecus aethiops; Chimera; Epitopes; Molecular Sequence Data; Nucleocapsid Proteins; Recombinant Fusion Proteins; Recombination, Genetic; Vero Cells; African swine fever virus; Animalia; Classical swine fever virus; Coronavirus; Foot-and-mouth disease virus; Sus scrofa","Alcaraz, C., Brun, A., Ruiz-Gonzalvo, F., Escribano, J.M., Cell culture propagation modifies the African swine fever replicative phenotype in macrophages and generates viral subpopulations differing in protein p54 (1992) Virus Res, 23, pp. 173-182; Borca, M.V., Carrillo, C., Zsak, L., Laegreid, W.W., Kutish, G.F., Neilan, J.G., Burrage, T.G., Rock, D.L., Deletion of a CD2-like gene, 8-DR, from African swine fever virus affects viral infection in domestic swine (1988) J Virol, 72, pp. 2881-2889; Brookes, S.M., Sun, H., Dixon, L.K., Parkhouse, R.M., Characterization of African swine fever virion proteins j5R and j13L: Immuno-localization in virus particles and assembly sites (1998) J Gen Virol, 79, pp. 1179-1188; Carrascosa, A.L., Del Val, M., Santarén, J.F., Viñuela, E., Purification and properties of African swine fever virus (1985) J Virol, 54, pp. 337-344; Casal, I., Enjuanes, L., Viñuela, E., Porcine leukocyte cellular subsets sensitive to ASFV in vitro (1984) J Virol, 52, pp. 37-46; García, R., Almazán, F., Rodríguez, J.M., Alonso, M., Viñuela, E., Rodríguez, J.F., Vectors for the genetic manipulation of African swine fever virus (1995) J Biotechnol, 40, pp. 121-131; Gómez-Puertas, P., Rodríguez, F., Ortega, A., Oviedo, J.M., Alonso, C., Escribano, J.M., Improvement of African swine fever virus neutralization assay using recombinant viruses expressing chromogenic marker genes (1995) J Virol Methods, 55, pp. 271-279; Gómez Puertas, P., Rodríguez, F., Oviedo, J.M., Ramiro-Ibáñez, F., Ruiz-Gonzalvo, F., Alonso, C., Escribano, J.M., Neutralizing antibodies to different proteins of African swine fever virus inhibit both virus attachment and internalization (1996) J Virol, 70, pp. 5689-5694; Gómez-Puertas, P., Rodríguez, F., Oviedo, J.M., Brun, A., Alonso, C., Escribano, J.M., The African swine fever virus proteins p54 and p30 are involved in two distinct steps of virus attachment and both contribute to the antibody-mediated protective immune response (1998) Virology, 243, pp. 461-471; Martín Alonso, J.M., Balbín, M., Garwes, D.J., Enjuanes, L., Gascón, S., Parra, F., Antigenic structure of transmissible gastroenteritis virus nucleoprotein (1992) Virology, 188, pp. 168-174; Mateu, M.G., Rocha, E., Vicente, O., Vayreda, F., Navalpotro, C., Andreu, D., Pedroso, E., Domingo, E., Reactivity with monoclonal antibodies of viruses from an episode of foot-and-mouth disease (1987) Virus Res, 8, pp. 261-274; Mateu, M.G., Martínez, M.A., Rocha, E., Andreu, D., Parejo, J., Sobrino, F., Domingo, E., Implication of a quasispecies genome structure: Effect of frequent, naturally occurring amino acid substitutions on the antigenicity of foot-and-mouth disease virus (1989) Proc Natl Acad Sci USA, 86, pp. 5883-5887; Neilan, J.G., Lu Kutish, G.F., Zsak, L., Lewis, T.L., Rock, D.L., A conserved African swine fever virus IΚ-B homolog, 5EL, is non-essential for growth in vitro and virulence in domestic pigs (1997) Virology, 235, pp. 377-385; Onisk, D.V., Borca, M.V., Kutish, G., Kramer, E., Irusta, P., Rock, D.L., Passively transferred African swine fever virus antibodies protect swine against lethal infection (1994) Virology, 198, pp. 350-354; Ramiro-Ibáñez, F., Escribano, J.M., Alonso, C., Application of a monoclonal antibody recognizing protein p30 to detect African swine fever virus infected cells in peripheral blood (1995) J Virol Methods, 55, pp. 339-345; Ramiro-Ibáñez, F., Ortega, A., Brun, A., Escribano, J.M., Alonso, C., Apoptosis: A mechanism of cell killing and lymphoid organ impairment during acute African swine fever virus infection (1996) J Gen Virol, 77, pp. 2209-2219; Rodríguez, J.M., Almazán, F., Viñuela, E., Rodríguez, J.F., Genetic manipulation of African swine fever virus: Construction of recombinant virus expressing the β-galactosidase gene (1992) Virology, 188, pp. 67-76; Rodríguez, F., Alcaraz, C., Eiras, A., Yáñez, R.J., Rodríguez, J.M., Alonso, C., Rodríguez, J.F., Escribano, J.M., Characterization and molecular basis of heterogeneity of the African swine fever virus envelope protein p54 (1994) J Virol, 68, pp. 7244-7252; Rodríguez, F., Ley, V., Gómez-Puertas, P., García, R., Rodríguez, J.F., Escribano, J.M., The structural protein p54 is essential for African swine fever virus viability (1996) Virus Res, 40, pp. 161-167; Ruiz-Gonzalvo, F., Carnero, M.E., Bruyel, V., Immunological responses of pigs to partially attenuated African swine fever virus and their resistance to virulent homologous and heterologous viruses (1983) FAO/CEC Expert Consultation in African Swine Fever Research Sardinia, pp. 206-216. , Wilkinson PJ (ed); Sun, H., Jacobs, S.C., Smith, G.L., Dixon, L.K., Parkhouse, R.M., African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats (1995) J Gen Virol, 76, pp. 1117-1127; Viñuela, E., African swine fever virus (1985) Curr Top Microbiol Immunol, 116, pp. 151-170; Wardley, R.C., Norley, S.G., Martins, C.V., Lawman, M.J.P., The host response to African swine fever virus (1987) Prog Med Virol, 34, pp. 180-192; Wilkinson, P.J., African swine fever virus (1989) Virus Infection of Porcines, pp. 17-37. , Pensaert MB (ed). Elsevier, Amsterdam; Zsak, L., Onisk, D.V., Afonso, C.L., Rock, D.L., Virulent African swine fever virus isolates are neutralized by swine serum and by monoclonal antibody recognizing a 72 kDa viral protein (1993) Virology, 196, pp. 596-602; Zsak, L., Caler, E., Lu, Z., Kutish, G.F., Neilan, J.G., Rock, D.L., A nonessential African swine fever virus gene UK is a significant virulence determinant in domestic swine (1997) J Virol, 72, pp. 1028-1035","Escribano, J.M.; Depto. de Mejora Gen. y Biotecnol., INIA, Ctra. de La Coruna, Km7, 28040 Madrid, Spain",,,03048608,,ARVID,"10481737","English","Arch. Virol.",Article,"Final",,Scopus,2-s2.0-0032782149
"An S., Chen C.-J., Yu X., Leibowitz J.L., Makino S.","55107136200;56288577100;57196945883;7006843902;7403067550;","Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer",1999,"Journal of Virology","73","9",,"7853","7859",,83,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032816080&partnerID=40&md5=3725012c82c0cea7cce3deafda320fd3","Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States; Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77555-1019, United States; Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Hlth. Sci. Ctr., College Station, TX 77843-1114, United States; Dept. of Microbiology and Immunology, Stanford University, Stanford, CA 94305, United States; Department of Biology, California Institute of Technology, Pasadena, CA 91125, United States","An, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Stanford University, Stanford, CA 94305, United States; Chen, C.-J., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77555-1019, United States; Yu, X., Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Hlth. Sci. Ctr., College Station, TX 77843-1114, United States, Department of Biology, California Institute of Technology, Pasadena, CA 91125, United States; Leibowitz, J.L., Dept. of Pathol. and Lab. Medicine, Texas A and M Univ. Hlth. Sci. Ctr., College Station, TX 77843-1114, United States; Makino, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77555-1019, United States","We demonstrated that infection of 17Cl-1 cells with the murine coronavirus mouse hepatitis virus (MHV) induced caspase-dependent apoptosis. MHV-infected DBT cells did not show apoptotic changes, indicating that apoptosis was not a universal mechanism of cell death in MHV-infected cells. Expression of MHV structural proteins by recombinant vaccinia viruses showed that expression of MHV E protein induced apoptosis in DBT cells, whereas expression of other MHV structural proteins, including S protein, M protein, N protein, and hemagglutinin-esterase protein, failed to induce apoptosis. MHV E protein-mediated apoptosis was suppressed by a high level of Bcl-2 oncogene expression. Our data showed that MHV E protein is a multifunctional protein; in addition to its known function in coronavirus envelope formation, it also induces apoptosis.",,"protein bcl 2; virus protein; animal cell; apoptosis; article; controlled study; gene expression; murine hepatitis coronavirus; nonhuman; oncogene; priority journal; protein expression; RNA virus infection; virus expression; Animals; Apoptosis; Caspase 3; Caspases; Cell Line; DNA Fragmentation; Mice; Murine hepatitis virus; Proto-Oncogene Proteins c-bcl-2; Viral Envelope Proteins","Afonso, C.L., Neilan, J.G., Kutish, G.F., Rock, D.L., An African swine fever virus Bcl-2 homolog, 5-HL, suppresses apoptotic cell death (1996) J. Virol., 70, pp. 4858-4863; Bailey, O., Pappenheimer, A.M., Cheever, F.S., Daniels, J.B., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin. II. Pathology (1949) J. 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"De Haan C.A.M., Smeets M., Vernooij F., Vennema H., Rottier P.J.M.","7003682643;57201814214;57193314302;7003697291;7006145490;","Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein",1999,"Journal of Virology","73","9",,"7441","7452",,62,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032874344&partnerID=40&md5=311954b415b92dbb79423899171f8a9a","Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","De Haan, C.A.M., Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Smeets, M., Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Vernooij, F., Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Vennema, H., Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infec. Dis. and Immunology, Utrecht University, Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","The coronavirus membrane (M) protein is the key player in virion assembly. One of its functions is to mediate the incorporation of the spikes into the vital envelope. Heterotypic interactions between M and the spike (S) protein can be demonstrated by coimmunoprecipitation and by immunofluorescence colocalization, after coexpression of their genes in eukaryotic cells. Using these assays in a mutagenetic approach, we have mapped the domains in the M protein that are involved in complex formation between M and S. It appeared that the 25-residue luminally exposed amino- terminal domain of the M protein is not important for M-S interaction. A 15- residue deletion, the insertion of a His tag, and replacement of the ectodomain by that of another coronavirus M protein did not affect the ability of the M protein to associate with the S protein. However, complex formation was sensitive to changes in the transmembrane domains of this triple-spanning protein. Deletion of either the first two or the last two transmembrane domains, known not to affect the topology of the protein, led to a considerable decrease in complex formation, but association was not completely abrogated. Various effects of changes in the part of the M protein that is located at the cytoplasmic face of the membrane were observed. Deletions of the extreme carboxy-terminal tail appeared not to interfere with M-S complex formation. However, deletions in the amphipathic domain severely affected M-S interaction. Interestingly, changes in the amino-terminal and extreme carboxy-terminal domains of M, which did not disrupt the interaction with S, are known to be fatal to the ability of the protein to engage in virus particle formation (C. A.M. de Haan, L. Kuo, P.S. Masters, H. Vennema, and P. J. M. Rottier, J. Virol. 72:6838-6850, 1998). Apparently, the structural requirements of the M protein for virus particle assembly differ from the requirements for the formation of M-S complexes.",,"membrane protein; virus protein; article; complex formation; coronavirus; immunofluorescence; immunoprecipitation; mutagenesis; nonhuman; peptide mapping; priority journal; protein assembly; protein domain; protein protein interaction; protein structure; structure activity relation; Animals; Binding Sites; Cats; Cell Line; Cell Membrane; Chromosome Mapping; Cricetinae; Membrane Glycoproteins; Murine hepatitis virus; Mutagenesis; Precipitin Tests; Viral Envelope Proteins; Viral Matrix Proteins","Bos, E.C., Luytjes, W., Van Der Meulen, H.V., Koerten, H.K., Spaan, W.J., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995) The Coronaviridae, pp. 165-179. , S. 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Virol., 64, pp. 3051-3055","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands; email: P.Rottier@vet.uu.nl",,,0022538X,,JOVIA,"10438834","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032874344
"Sánchez C.M., Izeta A., Sánchez-Morgado J.M., Alonso S., Sola I., Balasch M., Plana-Durán J., Enjuanes L.","57193985365;6602523425;6602349176;57210695335;7003336781;6602693824;6604038063;7006565392;","Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence",1999,"Journal of Virology","73","9",,"7607","7618",,157,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344069787&partnerID=40&md5=e528c568512a30924b5d25a9097f3ac7","Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain","Sánchez, C.M., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sánchez-Morgado, J.M., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Alonso, S., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Balasch, M., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Plana-Durán, J., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Enjuanes, L., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Targeted recombination within the S (spike) gene of transmissible gastroenteritis coronavirus (TGEV) was promoted by passage of helper respiratory virus isolates in cells transfected with a TGEV-derived defective minigenome carrying the S gene from an enteric isolate. The minigenome was efficiently replicated in trans and packaged by the helper virus, leading to the formation of true recombinant and pseudorecombinant viruses containing the S proteins of both enteric and respiratory TGEV strains in their envelopes. The recombinants acquired an enteric tropism, and their analysis showed that they were generated by homologous recombination that implied a double crossover in the S gene resulting in replacement of most of the respiratory, attenuated strain S gene (nucleotides 96 to 3700) by the S gene of the enteric, virulent isolate. The recombinant virus was virulent and rapidly evolved in swine testis cells by the introduction of point mutations and in-phase codon deletions in a domain of the S gene (nucleotides 217 to 665) previously implicated in the tropism of TGEV. The helper virus, with an original respiratory tropism, was also found in the enteric tract, probably because pseudorecombinant viruses carrying the spike proteins from the respiratory strain and the enteric virus in their envelopes were formed. These results demonstrated that a change in the tropism and virulence of TGEV can be engineered by sequence changes in the S gene.",,"article; coronavirus; gastroenteritis; gene sequence; gene targeting; genetic recombination; genetic transfection; nonhuman; point mutation; priority journal; virogenesis; virulence; virus replication; Animals; Culture Techniques; Genes, Viral; Intestine, Small; Recombination, Genetic; Swine; Swine, Miniature; Transmissible gastroenteritis virus; Tropism; Viral Proteins; Virulence; Virus Replication","Bai, M., Campisi, L., Freimuth, P., Vitronectin receptor antibodies inhibit infection of HeLa and A549 cells by adenovirus type 12 but not by adenovirus type 2 (1994) J. 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"Phillips J.J., Chua M.M., Lavi E., Weiss S.R.","7404582468;7006092803;7006986911;57203567044;","Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence",1999,"Journal of Virology","73","9",,"7752","7760",,130,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344500898&partnerID=40&md5=9d773328c259d25ac056e4084d56640e","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Department of Pathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Department of Microbiology, University of Pennsylvania, 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Phillips, J.J., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Chua, M.M., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Lavi, E., Department of Pathology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States, Department of Microbiology, University of Pennsylvania, 203A Johnson Pavilion, 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","The mouse hepatitis virus (MHV) spike glycoprotein, S, has been implicated as a major determinant of viral pathogenesis. In the absence of a full-length molecular clone, however, it has been difficult to address the role of individual vital genes in pathogenesis. By using targeted RNA recombination to introduce the S gene of MHV4, a highly neurovirulent strain, into the genome of MHV-A59, a mildly neurovirulent strain, we have been able to directly address the role of the S gene in neurovirulence. In cell culture, the recombinants containing the MHV4 S gene, S4R22 and S4R21, exhibited a small-plaque phenotype and replicated to low levels, similar to wild-type MHV4. Intracranial inoculation of C57BL/6 mice with S4R22 and S4R21 revealed a marked alteration in pathogenesis. Relative to wild-type control recombinant viruses (wtR13 and wtR9), containing the MHV-A59 S gene, the MHV4 S gene recombinants exhibited a dramatic increase in virulence and an increase in both viral antigen staining and inflammation in the central nervous system. There was not, however, an increase in the level of viral replication in the brain. These studies demonstrate that the MHV4 S gene alone is sufficient to confer a highly neurovirulent phenotype to a recombinant virus deriving the remainder of its genome from a mildly neurovirulent virus, MHV-A59. This definitively confirms previous findings, suggesting that the spike is a major determinant of pathogenesis.",,"virus antigen; virus protein; animal cell; animal experiment; animal model; article; cell culture; central nervous system infection; immunohistochemistry; mouse; murine hepatitis coronavirus; nonhuman; priority journal; virogenesis; virus pathogenesis; virus recombinant; virus replication; virus virulence; Animals; Antigens, Viral; Brain; Cell Line; Coronavirus Infections; Liver; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Reassortant Viruses; Viral Envelope Proteins; Virulence; Virus Replication","Bailey, O.T., Pappenheimer, A.M., Cheever, F.S., Daniels, J.B., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin. II. Pathology (1949) J. Exp. 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"Van Der Meer Y., Snijder E.J., Dobbe J.C., Schleich S., Denison M.R., Spaan W.J.M., Locker J.K.","7005678965;7006058325;6602684547;6602811199;7101971810;7007172944;6602308258;","Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication",1999,"Journal of Virology","73","9",,"7641","7657",,144,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032816239&partnerID=40&md5=815ccbd878ea402bc3dd5866f6e891e7","Department of Virology, Leiden University Medical Center, 2300 RC Leiden, Netherlands; EMBL, 69117 Heidelberg, Germany; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232, United States; Dept. of Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, United States; Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States; EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany","Van Der Meer, Y., Department of Virology, Leiden University Medical Center, 2300 RC Leiden, Netherlands; Snijder, E.J., Department of Virology, Leiden University Medical Center, 2300 RC Leiden, Netherlands; Dobbe, J.C., Department of Virology, Leiden University Medical Center, 2300 RC Leiden, Netherlands; Schleich, S., EMBL, 69117 Heidelberg, Germany; Denison, M.R., Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232, United States, Dept. of Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, United States, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States; Spaan, W.J.M., Department of Virology, Leiden University Medical Center, 2300 RC Leiden, Netherlands; Locker, J.K., EMBL, 69117 Heidelberg, Germany, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany","The aim of the present study was to define the site of replication of the coronavirus mouse hepatitis virus (MHV). Antibodies directed against several proteins derived from the gene 1 polyprotein, including the 3C-like protease (3CLpro), the putative polymerase (POL), helicase, and a recently described protein (p22) derived from the C terminus of the open reading frame 1a protein (CT1a), were used to probe MHV-infected cells by indirect immunofluorescence (IF) and electron microscopy (EM). At early times of infection, all of these proteins showed a distinct punctate labeling by IF. Antibodies to the nucleocapsid protein also displayed a punctate labeling that largely colocalized with the replicase proteins. When infected cells were metabolically labeled with 5-bromouridine 5'-triphosphate (BrUTP), the site of viral RNA synthesis was shown by IF to colocalize with CT1a and the 3CLpro. As shown by EM, CT1a localized to LAMP-1 positive late endosomes/lysosomes while POL accumulated predominantly in multilayered structures with the appearance of endocytic carrier vesicles. These latter structures were also labeled to some extent with both anti-CT1a and LAMP-1 antibodies and could be filled with fluid phase endocytic tracers. When EM was used to determine sites of BrUTP incorporation into vital RNA at early times of infection, the vital RNA localized to late endosomal membranes as well. 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Virol., 69, pp. 4331-4338","Locker, J.K.Meyerhofstrasse 1, 69117 Heidelberg, Germany; email: KRIJNSE@EMBL-Heidelberg.DE",,,0022538X,,JOVIA,"10438855","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032816239
"Mochizuki M., Osawa N., Ishida T.","7403050664;7007183248;7403962144;","Feline Coronavirus Participation in Diarrhea of Cats",1999,"Journal of Veterinary Medical Science","61","9",,"1071","1073",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033195242&partnerID=40&md5=b9d0817931c6e418a7a632ec9803fc24","Akasaka Animal Hospital, 4-1-29 Akasaka, Minato-ku, Tokyo 107-0052, Japan; Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan","Mochizuki, M., Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan; Osawa, N., Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan; Ishida, T., Akasaka Animal Hospital, 4-1-29 Akasaka, Minato-ku, Tokyo 107-0052, Japan","Fecal samples were examined for viruses participated in gastrointestinal disorders of cats, especially focusing on feline coronavirus (FCoV) by a reverse transcriptase-polymerase chain reaction assay. It was found that a primary viral pathogen was feline panleukopenia parvovirus (FPLV; 28.5% of the positive rate) and the secondary was FCoV (10.7%). Commonly reported clinical signs of cats of which feces were FCoV-positive were vomiting, diarrhea and dehydration with an exception of one serious case with concurrent FPLV infection.","Coronavirus; Diarrhea; Feline","Coronavirus; Felidae; Feline coronavirus; feline panleukopenia parvovirus; Feline panleukopenia virus; Felis catus; Parvovirus; monoclonal antibody; virus DNA; animal; animal disease; article; cat; cat disease; chemistry; Coronavirus; diarrhea; DNA sequence; feces; Feline panleukopenia virus; fluorescent antibody technique; gastrointestinal disease; genetics; molecular genetics; nucleotide sequence; pathogenicity; reverse transcription polymerase chain reaction; sequence homology; virology; virus infection; Animals; Antibodies, Monoclonal; Base Sequence; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; Diarrhea; DNA, Viral; Feces; Feline Panleukopenia; Feline panleukopenia virus; Fluorescent Antibody Technique, Indirect; Gastrointestinal Diseases; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; Sequence Analysis, DNA; Sequence Homology, Nucleic Acid","Addie, D.D., Toth, S., Herrewegh, A.A.P.M., Jarrett, O., (1996) Vet. Rec., 139, pp. 522-523; Dea, S., Roy, R.S., Elazhary, M.A.S.Y., (1982) Can. Vet. J., 23, pp. 153-155; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., (1997) J. Am. Vet. Med. Assoc., 210, pp. 1307-1312; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., (1997) J. Clin. Microbiol., 35, pp. 673-675; Gaskell, R.M., Bennett, M., (1996) Feline and Canine Infectious Diseases, , (Gaskell, R. M. and Bennett, M. ed.), Blackwell Science, Oxford; Gunnmoore, D.A., Gruffydd-Jones, T.J., Harbour, D.A., (1998) Vet. Microbioi., 62, pp. 193-205; Hashimoto, H., Roerink, F., Tohya, Y., Mochizuki, M., (1999) J. Vet. Med. Sci., 61, pp. 603-608; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (1998) J. Viral., 72, pp. 4508-4514; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (1995) Virology, 212, pp. 622-631; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., (1992) J. Vet. Med. Sci., 54, pp. 557-562; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., (1991) Vet. Microbiol., 28, pp. 13-24; Jacobse-Geels, H.E.L., Horzinek, M.C., (1983) J. Gen. Virol., 64, pp. 1859-1866; Kennedy, M.A., Brenneman, K., Millsaps, R.K., Black, J., Potgieter, L.N.D., (1998) J. Vet. Diagn. Invest., 10, pp. 93-97; Kipar, A., Kremendahl, J., Addie, D.D., Leukert, W., Grant, C.K., Reinacher, M., (1998) J. Comp. Pathol., 119, pp. 1-14; Li, X., Scott, F.W., (1994) Vet. Microbiol., 42, pp. 65-77; Loeffler, D.G., Ott, R.L., Evermann, J.F., Alexander, J.E., (1978) Feline Pract., 8, pp. 43-47; McKeirnan, A.J., Evermann, J.F., Hargis, A., Miller, L.M., Ott, R., (1981) Feline Pract., 11, pp. 16-20; Mochizuki, M., (1996) J. Jpn. Vet. Med. Assoc., 49, pp. 293-300. , in Japanese; Mochizuki, M., Horiuchi, M., Hiragi, H., San Gabriel, M.C., Yasuda, N., Uno, T., (1996) J. Clin. Microbiol., 34, pp. 2101-2105; Mochizuki, M., Hsüan, S.-W., (1984) Jpn. J. Vet. Sci., 46, pp. 905-908; Mochizuki, M., Konishi, S., Ajiki, M., Akaboshi, T., (1989) Jpn. J. Vet. Sci., 51, pp. 264-272; Mochizuki, M., San Gabriel, M.C., Nakatani, H., Yoshida, M., (1993) Res. Vet. Sci., 55, pp. 60-63; Mochizuki, M., Sugiura, R., Akuzawa, M., (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., (1996) Microbiol. Immunol., 40, pp. 425-433; Pedersen, N.C., (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeirnan, A.J., Ott, R.L., (1984) Adv. Exp. Med. Biol., 173, pp. 365-380; Pedersen, N.C., Boyle, J.F., Floyd, K., (1981) Am. J. Vet. Res., 42, pp. 363-367; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., (1992) Vet. Rec., 131, pp. 35-36; Truyen, U., Evermann, J.F., Vieler, E., Parrish, C.R., (1996) Virology, 215, pp. 186-189; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., (1995) Feline Pract., 23, pp. 40-44; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., (1998) Virology, 243, pp. 150-157","Mochizuki, M.; Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan",,,7653697,,,"10535517","English","J. Vet. Med. Sci.",Article,"Final",,Scopus,2-s2.0-0033195242
"Rottier P.J.M.","7006145490;","The molecular dynamics of feline coronaviruses",1999,"Veterinary Microbiology","69","1-2",,"117","125",,19,"10.1016/S0378-1135(99)00099-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032819499&doi=10.1016%2fS0378-1135%2899%2900099-1&partnerID=40&md5=0955c3954960894b2c8746538dd22b0b","Veterinary Faculty, Utrecht Univ., Dept. Infect. Dis. I., Utrecht, Netherlands","Rottier, P.J.M., Veterinary Faculty, Utrecht Univ., Dept. Infect. Dis. I., Utrecht, Netherlands","Feline coronaviruses are widespread and come in different flavors. There are two main serotypes both of which occur in two pathotypes, the avirulent enteric viruses and the virulent, usually fatal peritonitis viruses, the latter in turn occurring either in a 'wet' or exudative form or in a 'dry' or proliferative form. In this paper a concise overview is given of the molecular features of these viruses. Special attention is given to the genetic dynamics of the viruses as these now allow us to begin to understand the origin of the different phenotypes, in particular the genesis of virulence during persistent infection. As discussed, the surprising new insights obtained over the last few years call for a critical reevaluation of strategies for protection. Copyright (C) 1999 Elsevier Science B.V.","Coronavirus persistence; Feline coronavirus; Feline infectious peritonitis","virus vaccine; conference paper; coronavirus; evolution; molecular dynamics; nonhuman; persistent virus infection; polymerase chain reaction; serotype; vaccination; viral genetics; virus characterization; virus shedding; virus virulence; Animals; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; Polymerase Chain Reaction; Coronavirus; Felidae; Feline coronavirus","De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-309. , In: Siddell, S.G. (Ed.), Plenum Press, New York; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Godet, M., L'Haridon, R., Vautherot, J.-F., Laude, H., TGEV coronavirus ORF 4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Apoptosis and T-cell depletion during feline infectious peritonitis (1996) J. Virol., 70, pp. 8977-8983; Herrewegh, A.A.P.M., (1997) Molecular Genetics, Persistence and Evolution of FCoV, , Thesis (ISBN 90-393-1972-3), Utrecht University, Utrecht; Herrewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A.P.M., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Polymerase chain reaction (PCR) for the diagnosis of naturally occurring feline coronavirus infections (1995) Feline Practice, 23, pp. 56-60; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains FECV 79-1683 and FIPV 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J.Virol., 72, pp. 4508-4514; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer integral membrane and nucleocapsid proteins of feline canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeiman, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Molecular Biology and Pathogenesis of Coronaviruses, pp. 365-380. , In: Rottier, P.J.M., van der Zeijst, B.A.M., Spaan, W.J.M., Horzinek, M.C. (Eds), Plenum Press, New York; Pedersen, N.C., Floyd, K., Experimental studies with three new strains of feline infectious peritonitis virus: FIPV-UCD2, FIPV-UCD4, and FIPV-UCD4 (1985) Compend.Contin. Educ. Pract. Vet., 7, pp. 1001-1011; Rossen, J.W.A., Bekker, C.P.J., Strous, G.J.A.M., Horzinek, M.C., Dveksler, G.S., Holmes, K.V., Rottier, P.J.M., A murine and a porcine coronavirus are released from opposite surfaces of the same epithelial cells (1996) Virology, 224, pp. 345-351; Rossen, J.W.A., Horzinek, M.C., Rottier, P.J.M., Coronavirus infection of polarized epithelial cells (1995) Trends in Microbiol., 3, pp. 486-490; Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Van Der Ende, A., Strous, G.J.A.M., Rottier, P.J.M., MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally (1995) Virology, 210, pp. 54-66; Vennema, H., Godeke, G.-j., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by coexpression of viral envelope proteins (1996) EMBO J., 15, pp. 2020-2028; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44","Rottier, P.J.M.; Veterinary Faculty, Dept. Infectious Diseases, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",,,03781135,,VMICD,"10515281","English","Vet. Microbiol.",Conference Paper,"Final",Open Access,Scopus,2-s2.0-0032819499
"Naciri M., Paul Lefay M., Mancassola R., Poirier P., Chermette R.","7006479183;6504210563;6601957111;7006516209;7003280357;","Role of Cryptosporidium parvum as a pathogen in neonatal diarrhoea complex in suckling and dairy calves in France",1999,"Veterinary Parasitology","85","4",,"245","257",,77,"10.1016/S0304-4017(99)00111-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344223308&doi=10.1016%2fS0304-4017%2899%2900111-9&partnerID=40&md5=2750e63d4b28fd3304ee0493f6a300ce","INRA, U. Pathol. Aviaire Parasitol., 37380, Nouzilly, France; Hoechst Roussel Vet, 140 Avenue Jean Lolive, 93695 Cedex, Pantin, France; Société Protocole, Les Algorithmes, Immeuble H., Saint Aubin, France; Ecl. Natl. Veterinaire d'Alfort, UMR Biol. Molec. Immunol. P., Maisons-Alfort, France","Naciri, M., INRA, U. Pathol. Aviaire Parasitol., 37380, Nouzilly, France; Paul Lefay, M., Société Protocole, Les Algorithmes, Immeuble H., Saint Aubin, France; Mancassola, R., INRA, U. Pathol. Aviaire Parasitol., 37380, Nouzilly, France; Poirier, P., Hoechst Roussel Vet, 140 Avenue Jean Lolive, 93695 Cedex, Pantin, France; Chermette, R., Ecl. Natl. Veterinaire d'Alfort, UMR Biol. Molec. Immunol. P., Maisons-Alfort, France","This study was carried out to find the importance of Cryptosporidium parvum in diarrhoea of neonatal calves in two types of breeding - suckling and dairy calves - in France. Different agents causing neonatal diarrhoea, E. coli, rotavirus, coronavirus, Salmonella and Cryptosporidium were systematically researched in faeces. 1. Suckling calves: In 40 livestock farms selected for diarrhoea, 311 calves 4 to 10 days old which had diarrhoea for less than 24h or no diarrhoea, were included in the study. A prophylaxis of neonatal diarrhoea had been carried out in 21 of the 40 livestock farms. On D0 (inclusion day), the mean age was 6 days, 82% presented a good initial general condition and 76.2% had a good appetite; 48.6% were diarrhoeic but 91.3% presented no sign of dehydration. Only 6.1% were infected by E. coli K99, 14.3% by rotavirus, 6.8% by coronavirus, 0.3% by Salmonella but 50% excreted C. parvum oocysts. This later percentage increases up to 84% and 86% by D3 and D7, respectively . We note that 16% of the 4-day-old calves on D0 are excreting oocysts and this percentage increases as a function of the age of the calf on D0 to reach 90% to 95% by the age of 8 days. 10 out of 12 dead calves excreted C. parvum oocysts. From D0 to D14 the other pathogen agents show a relative or a decreasing stability. 2. Dairy calves: 382 calves which had diarrhoea for less than 24h or no diarrhoea, aged 8 to 15 days coming from six industrial livestock farms were included in the study. On D0, 99% of the calves presented a good initial general condition, 99.7% had a good appetite and no calf was dehydrated. At this date (D0), 16.8% of the calves excreted cryptosporidia. This percentage increases up to 23% and 51.8% on D3 and D8, respectively, then decreases to 31.9% on D14. The pressure of the other pathogenic agents remains relatively stable, excepted for rotavirus on D7 (from 9.9% on D0 to 27.2% on D7, then 12.6% on D14) which does not explain the concomitant peak in diarrhoea because the infection by rotavirus on D7 is more frequent in non-diarrhoeic calves than in diarrhoeic calves. Our results show that Cryptosporidium prevalence is higher in suckling than in dairy calves and C. parvum constitutes actually in both cases the major aetiological agent of neonatal diarrhoea. Copyright (C) 1999 Elsevier Science B.V.","Cattle-protozoa; Coronavirus; Cryptosporidium parvum; Escherichia coli; Neonatal calf diarrhoea; Rotavirus; Salmonella sp.","animal model; animal tissue; article; cattle; coronavirus; cryptosporidium parvum; diarrhea; diet; enzyme linked immunosorbent assay; escherichia coli; feces analysis; immunohistochemistry; newborn; nonhuman; oocyst; rotavirus; salmonella; suckling; Animals; Animals, Newborn; Cattle; Cattle Diseases; Coronavirus, Bovine; Cryptosporidiosis; Cryptosporidium parvum; Diarrhea; Escherichia coli; Feces; Female; France; Rotavirus; Salmonella","Anderson, B.C., Patterns of shedding of cryptosporidial oocysts in Idaho calves (1981) J. Am. Vet. Med. Assoc., 178, pp. 982-984; Angus, K.W., Cryptosporidiosis in ruminants (1990) Cryptosporidiosis of Man and Animals, pp. 83-99. , In: Dubey, J.P., Speer, C.A., Fayer, R. (Eds.) CRC Press, Boca Raton; Aurich, J.E., Dobrinski, I., Grunert, E., Intestinal cryptosporidiosis in calves on a dairy farm (1990) Vet. Rec., 127, pp. 380-381; Blewett, D.A., Quantitative techniques in Cryptosporidium research (1989) Cryptosporidiosis: Proceedings of the First International Workshop, pp. 85-95. , In: Angus, K.W., Blewett, D.A. (Eds.), Moredun Research Institute, Edinburgh; Bukhari, Z., Smith, H.V., Cryptosporidium parvum: Oocyst excretion and viability patterns in experimentally infected lambs (1997) Epidemiol. Infect., 119, pp. 105-108; Chermette, R., Polack, B., Boufassa, S., Bariaud, F., Tarnau, C., Couderc, O., Creuzon, F., (1984) Cryptosporidies Chez Les Animaux Adultes en France: Rôle Épidémiologique, , Commun. Congrès SFP, Rennes, France; De La Fuente, R., Garcia, A., Ruiz-Santa-Quiteria, J.A., Luzon, M., Cid, D., Garcia, S., Orden, J.A., Gomez-Bautista, M., Proportional morbidity rates of enteropathogens among diarrheic dairy calves in central Spain (1998) Prev. Vet. Med., 36, pp. 145-152; De La Fuente, R., Luzon, M., Garcia, A., Cid, D., Orden, J.A., Garcia, S., Sanz, R., Gomez-Bautista, M., Cryptosporidium and concurrent infections with other major enteropathogens in 1 to 30-day-old diarrheic dairy calves in central Spain (1999) Vet. Parasitol., 80, pp. 179-185; Du Pont, H.L., Chappell, C.L., Sterling, C.R., Okhuysen, P.C., Rose, J.B., Jakubowski, W., The infectivity of Cryptosporidium parvum in healthy volunters (1995) New Engl. J. Med., 332, pp. 855-859; Fayer, R., Ungar, B.L.P., Cryptosporidium spp. and cryptosporidiosis (1986) Microbiol. Rev., 50, pp. 458-483; Fayer, R., Gasbarre, L., Pasquali, P., Canals, A., Almeria, S., Zarlenga, D., Cryptosporidium parvum infection in bovine neonates: Dynamic clinical, parasitic, parasitic and immunologic patterns (1998) Int. J. Parasitol., 28, pp. 49-56; Garber, L.P., Salman, M.D., Hurd, H.S., Keefe, T., Schlater, J., Potential risk factors for Cryptosporidium infection in dairy calves (1994) J. Am. Vet. Med. Assoc., 205, pp. 86-91; Henriksen, S.A., Grogh, H.V., Bovine cryptosporidiosis in Denmark I. Prevalence, age, distribution, and seasonal variation (1985) Nord. Vet. Med., 37, pp. 34-41; Lorenzo-Lorenzo, M.J., Ares-Mazas, E., Villacorta Martinez De Maturana, I., Detection of oocysts and IgG antibodies to Cryptosporidium parvum in asymptomatic adult cattle (1993) Vet. Parasitol., 47, pp. 9-15; McCluskey, B.J., Cryptosporidium parvum oocyst shedding in Florida dairy calves (1992) Anim. Health Insight USDA: APHIS: VS Rep N010.1192, pp. 1-5; Mann, E.D., Sekla, L.H., Nayar, G.P.S., Koschik, C., Infection with Cryptosporidium spp. in human and cattle in Manitoba (1986) Can. J. Vet. Res., 50, pp. 174-178; Moore, J.A., Blagburn, B.L., Lindsay, D.S., Cryptosporidiosis in animals including humans (1988) Compend. Cont. Ed. Small Anim. Pract., 10, pp. 275-281; Moore, D.A., Zeman, D.H., Cryptosporidiosis in neonatal calves: 277 cases (1986-1987) (1991) J. Am. Vet. Med. Assoc., 198, pp. 1969-1971; Morin, M., Larivière, S., Lallier, R., Pathological and microbiological observations made on spontaneous cases of acute neonatal calf diarrhea (1976) Can. J. Comp. Med., 40, pp. 228-240; Naciri, M., Mancassola, R., Yvoré, P., Peeters, J.E., The effect of halofuginone lactate on experimental Cryptosporidium parvum infections in calves (1993) Vet. Parasitol., 45, pp. 199-207; O'Donoghue, P.J., Cryptosporidium and cryptosporidiosis in man and animals (1995) Int. J. Parasitol., 25, pp. 139-195; Otto, V.P., Elschner, M., Günther, H., Schulze, F., Vergleichende Untersuchungen zum nachweis von Rotaviren, Coronaviren Kryptosporidien und enterotoxinogen E. coli im Kot durchfallkranker Kälber (1995) Tierärztl Umschau, 50, pp. 80-86; Panciera, R.J., Thomassen, R.W., Garner, F.M., Cryptosporidial infection in a calf (1971) Vet. Pathol., 8, pp. 479-484; Pavlasek, I., Dynamics of the release of oocysts of Cryptosporidium spp. in spontaneously infected calves (1982) Folia Parasitol., 29, pp. 295-296; Peeters, J.E., Villacorta, I., Vanopdenbosch, E., Vandergheynst, D., Naciri, M., Ares-Mazas, E., Yvoré, P., Cryptosporidium parvum in calves: Kinetics and immunoblot analysis of specific serum and local antibody responses (immunoglobulin A (IgA), IgG and IgM) after natural and experimental infections (1992) Infect. Immun., 60, pp. 2309-2316; Quilez, J., Ares-Mazas, E., Sanchez-Acedo, C., Del Cacho, E., Clavel, A., Causapé, A.C., Comparison of oocyst shedding and the serum immune response to Cryptosporidium parvum in cattle and pigs (1996) Parasitol. Res., 82, pp. 529-534; Quilez, J., Sanchez-Acedo, C., Del Cacho, E., Clavel, A., Causapé, A.C., Prevalence of Cryptosporidium and Giardia infections in cattle in Aragon (northeastern Spain) (1996) Vet. Parasitol., 66, pp. 139-146; Reynolds, D.J., Morgan, J.H., Chanter, N., Jones, P.W., Bridger, J.C., Debney, T.G., Bunch, K.J., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec., 119, pp. 34-39; Sandford, S.A., Josephson, G.K.A., Bovine cryptosporidiosis: Clinical and pathological findings in fortytwo scouring neonatal calves (1982) Can. Vet. J., 23, pp. 340-343; Scott, C.A., Smith, H.V., Gibbs, H.A., Excretion of Cryptosporidium parvum by a herd of beef suckler cows (1994) Vet. Rec., 34, p. 172; Scott, C.A., Smith, H.V., Mtambo, M.M.A., Gibbs, H.A., An epidemiological study of Cryptosporidium parvum in two herds of adult beef cattle (1995) Vet. Parasitol., 57, pp. 277-288; Stein, V.E., Boch, J., Heine, J., Henkel, G., Der Verlauf naturlicher Cryptosporidium-infektionen in vier Rinderzuchtbetrieben (1983) Berl. Münch. Tieräztl. Wochenschr., 96, pp. 222-225; Schulz, V.W., Die bovine Kryptosporidiose: Nachweis und Bedeutung. Monatsschr (1986) Vet. Med., 41, pp. 330-335; Villacorta, I., Ares-Mazas, E., Lorenzo, M.J., Cryptosporidium parvum in cattle, sheep and pigs in Galicia (N.W. Spain) (1991) Vet. Parasitol., 38, pp. 249-252; Xiao, L., Herd, R.P., Infection patterns of Cryptosporidium and Giardia in calves (1994) Vet. Parasitol., 55, pp. 257-262","Naciri, M.; INRA, Unite Pathologie Aviaire/Parasitol., 3780 Nouzilly, France; email: naciri@tours.inra.fr",,,03044017,,VPARD,"10488727","English","Vet. Parasitol.",Article,"Final",,Scopus,2-s2.0-0344223308
"Robitaille J., Izzi L., Daniels E., Zelus B., Holmes K.V., Beauchemin N.","55937939300;6603083058;7101961843;6602571243;7201657724;7005461095;","Comparison of expression patterns and cell adhesion properties of the mouse biliary glycoproteins Bgp1 and Bgp2",1999,"European Journal of Biochemistry","264","2",,"534","544",,29,"10.1046/j.1432-1327.1999.00660.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033199905&doi=10.1046%2fj.1432-1327.1999.00660.x&partnerID=40&md5=052483fa582eedf34948b889a17d330b","McGill Cancer Centre, McGill University, Montreal, Que., Canada; Department of Biochemistry, McGill University, Montreal, Que., Canada; Department Anatomy and Cell Biology, McGill University, Montreal, Que., Canada; Department Oncology and Medicine, McGill University, Montreal. Que., Canada; Department of Microbiology, Univ. of Colorado Hlth. Sci. Centre, Denver, CO, United States; McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Drummond St., Montreal, Qué H3G 1Y6, Canada","Robitaille, J., McGill Cancer Centre, McGill University, Montreal, Que., Canada; Izzi, L., McGill Cancer Centre, McGill University, Montreal, Que., Canada, Department of Biochemistry, McGill University, Montreal, Que., Canada; Daniels, E., Department Anatomy and Cell Biology, McGill University, Montreal, Que., Canada; Zelus, B., Department of Microbiology, Univ. of Colorado Hlth. Sci. Centre, Denver, CO, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Centre, Denver, CO, United States; Beauchemin, N., McGill Cancer Centre, McGill University, Montreal, Que., Canada, Department of Biochemistry, McGill University, Montreal, Que., Canada, Department Oncology and Medicine, McGill University, Montreal. Que., Canada, McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Drummond St., Montreal, Qué H3G 1Y6, Canada","Biliary glycoproteins are members of the carcinoembryonic antigen (CEA) family and behave as cell adhesion molecules. The mouse genome contains two very similar Bgp genes, Bgp1 and Bgp2, whereas the human and rat genomes contain only one BGP gene. A Bgp2 isoform was previously identified as an alternative receptor for the mouse coronavirus mouse hepatitis virus. This isoform consists of two extracellular immunoglobulin domains, a transmembrane domain and a cytoplasmic tail of five amino acids. In this report, we have examined whether the Bgp2 gene can express other isoforms in different mouse tissues. We found only one other isoform, which has a long cytoplasmic tail of 73 amino acids. The long cytodomain of the Bgp2 protein is highly similar to that of the Bgp1/4L isoform. The Bgp2 protein is expressed in low amounts in kidney and in a rectal carcinoma cell line. Antibodies specific to Bgp2 detected a 42-kDa protein, which is expressed at the cell surface of these samples. Bgp2 was found by immunocytochemistry in smooth muscle layers of the kidney, the uterus, in gut mononuclear cells and in the crypt epithelia of intestinal tissues. Transfection studies showed that, in contrast with Bgp1, the Bgp2 glycoprotein was not directly involved in intercellular adhesion. However, this protein is found in the proliferative compartment of the intestinal crypts and in cells involved in immune recognition. This suggests that the Bgp2 protein represents a distinctive member of the CEA family; its unusual expression patterns in mouse tissues and the unique functions it may be fulfilling may provide novel clues about the multiple functions mediated by a common BGP protein in humans and rats.","Biliary glycoprotein (BGP); C-CAM; Carcinoembryonic antigen; CD66; Cell adhesion","amino acid; carcinoembryonic antigen; cell adhesion molecule; glycoprotein; animal tissue; antigen recognition; article; cell adhesion; gene expression; hepatobiliary system; immunocytochemistry; mouse; nonhuman; priority journal; protein analysis; protein expression; protein localization; tissue distribution; Amino Acid Sequence; Animals; Antigens, CD; Cell Adhesion; Cell Adhesion Molecules; Cell Line; Cloning, Molecular; Gene Expression Regulation; Glycoproteins; Immunohistochemistry; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Sequence Alignment; Animalia; Coronavirus; Murine hepatitis virus; Rodentia","Stanners, C.P., (1998) Cell Adhesion and Communication Mediated by the CEA Family, pp. 1-302. , Stanners C.P., ed. Harwood Press, Amsterdam; Robbins, J., Robbins, P.F., Kosak, C.A., Callahan, R., The mouse biliary glycoprotein gene (Bgp): Partial nucleotidesequence, expression, and chromosomal assignment (1991) Genomics, 10, pp. 583-587; Nédellec, P., Turbide, C., Beauchemin, N., Characterization and transcriptional activity of the mouse biliary glycoprotein 1 gene, a carcinoembryonic antigen-related gene (1995) Eur. J. Biochem., 231, pp. 104-114; Nédellec, P., Dveksler, G.S., Daniels, E., Turbide, C., Chow, B., Basile, A.A., Holmes, K.V., Beauchemin, N., Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis viruses (1994) J. Virol., 68, pp. 4525-4537; McCuaig, K., Rosenberg, M., Nédellec, P., Turbide, C., Beauchemin, N., Expression of the Bgp gene and characterization of mouse colon biliary glycoprotein isoforms (1993) Gene, 127, pp. 173-183; Dveksler, G.S., Dieffenback, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Rojas, M., Fuks, A., Stanners, C.P., Biliary glycoprotein, a member of the immunoglobulin supergene family, functions in vitro as a Ca2+-dependent intercellular adhesion molecule (1990) Cell Growth Differ., 1, pp. 527-533; Ocklind, C., Öbrink, B., Intercellular adhesion of rat hepatocytes (1982) J. Biol. 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Dynamics, 206, pp. 272-290; Kunath, T., Ordoñez-Garcia, C., Turbide, C., Beauchemin, N., Inhibition of colonic tumor cell growth by biliary glycoprotein (1995) Oncogene, 11, pp. 2375-2382; Hsieh, J.-T., Luo, W., Song, W., Wang, Y., Van Kleinerman, D.I.N.T., Lin, S.-H., Tumor suppressive role of an androgen-regulated epithelial cell adhesion molecule (C-CAM) in prostate carcinoma cell revealed by sense and antisense approaches (1995) Cancer Res., 55, pp. 190-197; Tanaka, K., Hinoda, Y., Takahashi, H., Sakamoto, H., Nakajima, Y., Imai, K., Decreased expression of biliary glycoprotein in hepatocellular carcinomas (1997) Int. J. Cancer, 74, pp. 15-19; Rietdorf, L., Lisboa, B.W., Henkel, U., Naumann, M., Wagener, C., Loning, T., Differential expression of CD66a (BGP), a cell adhesion molecule of the carcinoembryonic antigen family, in benign, premalignant and malignant lesions of the human mammary gland (1997) J. Histochem. Cytochem., 45, pp. 957-963; Bamberger, A.M., Rietdorf, L., Nollau, P., Naumann, M., Erdmann, I., Gotze, J., Brummer, J., Loning, T., Dysregulated expression of CD66a (BGP, C-CAM), an adhesion molecule of the CEA family, in endometrial cancer (1998) Am. J. Pathol., 152, pp. 1401-1406; Beauchemin, N., Kunath, T., Robitaille, J., Chow, B., Turbide, C., Daniels, E., Veillette, A., Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells (1997) Oncogene, 14, pp. 783-790; Huber, M., Izzi, L., Grondin, P., Houde, C., Kunath, T., Veillette, A., Beauchemin, N., The carboxy-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells (1999) J. Biol. Chem., 274, pp. 335-344; Skubitz, K.M., Campbell, K.D., Ahmed, K., Skubitz, A.P.N., CD66 family members are associated with tyrosine kinase activity in human neutrophils (1995) J. Immunol., 151, pp. 5382-5390; Hauck, C.R., Meyer, T.F., Lang, F., Gulbins, E., CD66-mediate phagocytosis of Opa52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase- and Rac 1-dependent signalling pathway (1998) EMBO J., 17, pp. 443-454; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl Acad. Sci. USA, 74, pp. 5463-5467; Rosenberg, M., Nédellec, P., Jothy, S., Fleiszer, D., Turbide, C., Beauchemin, N., The expression of mouse biliary glycoprotein, a carcinoembryonic antigen-related gene, is down-regulated in malignant mouse tissues (1993) Cancer Res., 53, pp. 4938-4945; Southern, P.J., Berg, P., Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter (1982) J. Mol. Appl. Genet., 1, pp. 314-327; Sambrook, J., Firtsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Tarn, J.P., Synthetic peptide vaccine design: Synthesis and properties of a high-density multiple antigenic peptide system (1988) Proc. Natl Acad. Sci. USA, 85, pp. 5409-5413; Smith, D.B., Johnson, K.S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase (1988) Gene, 67, pp. 31-40; Edlund, M., Wikstrom, K., Toomik, R., Ek, P., Öbrink, B., Characterization of protein kinase C-mediated phosphorylation of the short cytoplasmic domain isoform of C-CAM (1998) FEBS Lett., 425, pp. 166-170; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Knobler, R., Coutelier, J.P., Dubois-Dalcq, M., Holmes, K.V., Tissue and cellular distribution of an adhesion molecule in the carcino-embryonic antigen family that serves as a receptor for the mouse hepatitis virus (1995) Lab. Invest., 73, pp. 615-627; Watt, S.M., Fawcett, J., Murdoch, S.J., Teixeira, A.M., Gschmeissner, S.E., Hajibagheri, N.M.A.N., Simmons, D.L., CD66 identifies the biliary glycoprotein (BGP) adhesion molecule: Cloning, expression, and adhesion functions of the BGPc splice variant (1994) Blood, 84, pp. 200-210; Izzi, L., Turbide, C., Houde, C., Kunath, T., Beauchemin, N., Cis-determinants in the cytoplasmic domain of CEA-CAM1 responsible for its tumor inhibitory function (1999) Oncogene, , in press; Cheung, P.H., Luo, W., Qiu, Y., Zhang, X., Earley, K., Millirons, P., Lin, S.H., Structure and function of C-CAM1. The first immunoglobulin domain is required for intercellular adhesion (1993) J. Biol. Chem., 268, pp. 24303-24310; Turbide, C., Kunath, T., Daniels, E., Beauchemin, N., Optimal ratios of biliary glycoprotein isoforms required for inhibition of colonic tumor cell growth (1997) Cancer Res., 57, pp. 2781-2788; Formisano, P., Najjar, S.M., Gross, C.N., Philippe, N., Oriente, F., Kern-Buell, C.L., Accili, D., Gorden, P., Receptor-mediated internalization of insulin (1995) J. Biol. Chem., 270, pp. 24073-24077; Cheung, P.H., Thompson, N.L., Early, K., Culic, O., Hixson, S., Lin, S.-L., Cell-CAM105 isoforms with different adhesion functions are coexpressed in adult rat tissues and during liver development (1993) J. Biol. Chem., 268, pp. 6139-6146; Thompson, N.L., Panzica, M.A., Hill, G., Lin, S.H., Curran, T.R., Gruppuso, P.A., Baum, O., Hixson, D., Spatiotemporal expression of two cell-cell adhesion molecule 105 isoforms during liver development (1993) Cell Growth Differ., 4, pp. 257-268; Hunter, I., Lindh, M., Öbrink, B., Differential regulation of C-CAM isoforms in epithelial cells (1994) J. Cell Sci., 107, pp. 1205-1216; Wikstrom, K., Kjellstrom, G., Öbrink, B., Homophilicintercellular adhesion mediated by C-CAM is due to a domain 1-domain 1 reciprocal binding (1996) Exp. Cell Res., 227, pp. 360-366; Cheng, H., Leblond, C.P., Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine. V. Unitarian theory of the origin of the four epithelial cell types (1974) Am. J. Pathol., 141, pp. 537-561","Beauchemin, N.; McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Drummond St., Montreal, Que. H3G 1Y6, Canada; email: nicoleb@med.mcgill.ca",,,00142956,,EJBCA,"10491101","English","Eur. J. Biochem.",Article,"Final",,Scopus,2-s2.0-0033199905
"Vennema H.","7003697291;","Genetic drift and genetic shift during feline coronavirus evolution",1999,"Veterinary Microbiology","69","1-2",,"139","141",,33,"10.1016/S0378-1135(99)00102-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032819744&doi=10.1016%2fS0378-1135%2899%2900102-9&partnerID=40&md5=29b12469a311c6dbc34080c3e8f181fb","Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Vennema, H., Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",[No abstract available],,"cat disease; conference paper; coronavirus; enzyme linked immunosorbent assay; gene sequence; genetic drift; genetic variability; molecular genetics; nonhuman; phenotype; viral genetics; virus mutation; virus neutralization; Animals; Cats; Coronavirus; Coronavirus Infections; Coronavirus, Feline; Evolution, Molecular; Gene Frequency; Coronavirus; Felidae; Feline coronavirus; Felis catus",,"Vennema, H.; Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: h.vennema@vet.uu.nl",,,03781135,,VMICD,"10515284","English","Vet. Microbiol.",Conference Paper,"Final",Open Access,Scopus,2-s2.0-0032819744
"Williams G.D., Chang R.-Y., Brian D.A.","7406083594;36725275000;7006460232;","A phylogenetically conserved hairpin-type 3' untranslated region pseudoknot functions in coronavirus RNA replication",1999,"Journal of Virology","73","10",,"8349","8355",,79,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032827591&partnerID=40&md5=0142eec7fff451c82c7b7c5ca30296bd","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Building, Knoxville, TN 37996-0845, United States; National Dong-Hwa University, Hualien, Taiwan","Williams, G.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Chang, R.-Y., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, National Dong-Hwa University, Hualien, Taiwan; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Building, Knoxville, TN 37996-0845, United States","Secondary and tertiary structures in the 3' untranslated region (UTR) of plus-strand RNA viruses have been postulated to function as control elements in RNA replication, transcription, and translation. Here we describe a 54- nucleotide (nt) hairpin-type pseudoknot within the 288-nt 3' UTR of the bovine coronavirus genome and show by mutational analysis of both stems that the pseudoknotted structure is required for the replication of a defective interfering RNA genome. The pseudoknot is phylogenetically conserved among coronaviruses both in location and in shape but only partially in nucleotide sequence, and evolutionary covariation of bases to maintain G · U pairings indicates that it functions in the plus strand. RNase probing of synthetic transcripts provided additional evidence of its tertiary structure and also identified the possible existence of two conformational states. These results indicate that the 3' UTR pseudoknot is involved in coronavirus RNA replication and lead us to postulate that it functions as a regulatory control element.",,"ribonuclease; virus RNA; article; coronavirus; nonhuman; nucleotide sequence; phylogeny; priority journal; RNA replication; RNA structure; RNA transcription; RNA translation; structure analysis; transcription regulation; 3' Untranslated Regions; Animals; Base Sequence; Cattle; Conserved Sequence; Coronavirus; Molecular Sequence Data; Nucleic Acid Conformation; Phylogeny; RNA, Viral; Virus Replication","Auron, P.E., Weber, L.D., Rich, A., Comparison of transfer ribonucleic acid structures using cobra venom and S1 endonucleases (1982) Biochemistry, 21, pp. 4700-4706; Baer, M.L., Houser, F., Loesch-Fries, L.S., Gehrke, L., Specific RNA binding by amino-terminal peptides of alfalfa mosaic virus coat protein (1994) EMBO J., 13, pp. 727-735; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Blackwell, J.L., Brinton, M.A., BHK cell proteins that bind to the 3′ stem-loop structure of the West Nile virus genome RNA (1995) J. Virol., 69, pp. 5650-5658; Blight, K.J., Rice, C.M., Secondary-structure determination of the conserved 98-base sequence at the 3′ terminus of hepatitis C virus genome RNA (1997) J. Virol., 71, pp. 7345-7352; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Brian, D.A., Dennis, D.E., Guy, J.S., Genome of porcine transmissible gastroenteritis virus (1980) J. Virol., 34, pp. 410-415; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Semin. Virol., 8, pp. 101-111; Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus (1993) J. Gen. Virol., 74, pp. 1795-1804; Chang, R.-Y., Brian, D.A., cis-requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Chang, R.-Y., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. 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Virol., 69, pp. 3744-3751; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Williams, G.D., Chang, R.-Y., Brian, D.A., Evidence for a pseudoknot in the 3′ untranslated region of the bovine coronavirus genome (1995) Adv. Exp. Med. Biol., 380, pp. 511-514; Wyatt, J.R., Puglisi, J.D., Tinoco, I., RNA pseudoknots: Stability and loop size requirements (1990) J. Mol. Biol., 214, pp. 455-470; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′ end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023","Brian, D.A.; Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Building, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,,0022538X,,JOVIA,"10482585","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032827591
"Senanayake S.D., Brian D.A.","7004008817;7006460232;","Translation from the 5' untranslated region (UTR) of mRNA 1 is repressed, but that from the 5' UTR of mRNA 7 is stimulated in coronavirus- infected cells",1999,"Journal of Virology","73","10",,"8003","8009",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032844923&partnerID=40&md5=8dba8b18d2ae6d25a22210aa03a04df8","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Bldg., Knoxville, TN 37996-0845, United States","Senanayake, S.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Bldg., Knoxville, TN 37996-0845, United States","Viral gene products are generally required in widely differing amounts for successful virus growth and assembly. For coronaviruses, regulation of transcription is a major contributor to these differences, but regulation of translation may also be important. Here, we examine the possibility that the 5' untranslated regions (UTRs), unique for each of the nine species of mRNA in the bovine coronavirus and ranging in length from 70 nucleotides (nt) to 210 nt (inclusive of the common 5'-terminal 65-nt leader), can differentially affect the rate of protein accumulation. When the natural 77-nt 5' UTR on synthetic transcripts of mRNA 7 (mRNA for N and I proteins) was replaced with the 210-nt 5' UTR from mRNA 1 (genomic RNA, mRNA for viral polymerase), approximately twofold-less N, or (N) CAT fusion reporter protein, was made in vitro. Twofold less was also made in vivo in uninfected cells when a T7 RNA polymerase-driven transient-transfection system was used. In coronavirus- infected cells, this difference surprisingly became 12-fold as the result of both a stimulated translation from the 77-nt 5' UTR and a repression of translation from the 210-nt 5' UTR. These results reveal that a differential 5' UTR-directed regulation of translation can occur in coronavirus-infected cells and lead us to postulate that the direction and degree of regulation is carried out by viral or virally induced cellular factors acting in trans on cis-acting elements within the 5' UTR.",,"cis acting element; gene product; hybrid protein; RNA polymerase; trans acting factor; animal cell; article; cattle; coronavirus; genetic transfection; mouse; nonhuman; priority journal; transcription regulation; translation regulation; virogenesis; virus assembly; virus infection; 5' Untranslated Regions; Animals; Base Sequence; Cats; Cattle; Cell Line; Coronavirus; Coronavirus Infections; Gene Expression Regulation, Viral; Humans; Molecular Sequence Data; Protein Biosynthesis; RNA, Messenger","Ali, N., Siddiqui, A., The La antigen binds 5′ noncoding region of the hepatitis C virus RNA in the context of the initiator AUG codon and stimulates internal ribosome entry site-mediated translation (1997) Proc. 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Virol., 65, pp. 6194-6204; Senanayake, S.D., Brian, D.A., Precise large deletions by the PCR-based overlap extension method (1995) Mol. Biotechnol., 4, pp. 13-15; Senanayake, S.D., Brian, D.A., Bovine coronavirus I protein synthesis follows ribosomal scanning on the bicistronic N mRNA (1997) Virus Res., 48, pp. 101-105; Senanayake, S.D., Hofmann, M.A., Maki, J.L., Brian, D.A., The nucleocapsid protein gene of the bovine coronavirus is bicistronic (1992) J. Virol., 66, pp. 5277-5283; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Svitkin, Y.V., Pause, A., Sonenberg, N., La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA (1994) J. Virol., 68, pp. 7001-7007; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Tahara, S.M., Dietlin, T.A., Nelson, G.W., Stohlman, S.A., Manno, D.J., Mouse hepatitis virus nucleocapsid protein as a translational effector of viral mRNAs (1998) Adv. Exp. Med. Biol., 440, pp. 313-318; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5 (1994) J. Gen. Virol., 75, pp. 3041-3046","Brian, D.A.; Department of Microbiology, University of Tennessee, M409 Walters Life Sciences Bldg., Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,,0022538X,,JOVIA,"10482548","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032844923
"Luo Z., Matthews A.M., Weiss S.R.","55460270800;57197974935;57203567044;","Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion",1999,"Journal of Virology","73","10",,"8152","8159",,48,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032827589&partnerID=40&md5=1c335c6306b6ee24a4360c60d8e2fee7","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","Luo, Z., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Matthews, A.M., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","The murine coronavirus spike (S) protein contains a leucine zipper domain which is highly conserved among coronaviruses. To assess the role of this leucine zipper domain in S-induced cell-to-cell fusion, the six heptadic leucine and isoleucine residues were replaced with alanine by site-directed mutagenesis. The mutant S proteins were analyzed for cell-to-cell membrane fusion activity as well as for progress through the glycoprotein maturation process, including intracellular glycosylation, oligomerization, and cell surface expression. Single-alanine-substitution mutations had minimal, if any, effects on S-induced cell-to-cell fusion. Significant reduction in fusion activity was observed, however, when two of the four middle heptadic leucine or isoleucine residues were replaced with alanine. Double alanine substitutions that involved either of the two end heptadic leucine residues did not significantly affect fusion. All double-substitution mutant S proteins displayed levels of endoglycosidase H resistance and cell surface expression similar to those of the wild-type S. However, fusion-defective double-alanine-substitution mutants exhibited defects in S oligomerization. These results indicate that the leucine zipper domain plays a role in S- induced cell-to-cell fusion and that the ability of S to induce fusion may be dependent on the oligomeric structure of S.",,"alanine; leucine; mutant protein; virus protein; amino acid substitution; animal cell; article; cell fusion; controlled study; coronavirus; glycosylation; mouse; nonhuman; oligomerization; priority journal; protein domain; protein expression; protein structure; site directed mutagenesis; Amino Acid Sequence; Amino Acid Substitution; Animals; Cell Fusion; Cell Line; Coronavirus; Leucine Zippers; Membrane Glycoproteins; Mice; Molecular Sequence Data; Point Mutation; Viral Envelope Proteins; Virus Replication","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1989) Current Protocols in Molecular Biology, , Wiley-Interscience, New York, N.Y; Bernstein, H.B., Tucker, S.P., Kar, S.R., McPherson, S.A., McPherson, D.T., Dubay, J.W., Lebowitz, J., Hunter, E., Oligomerization of the hydrophobic heptad repeat of gp41 (1995) J. 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"Salanueva I.J., Carrascosa J.L., Risco C.","6506074528;35481302900;56251715300;","Structural maturation of the transmissible gastroenteritis coronavirus",1999,"Journal of Virology","73","10",,"7952","7964",,48,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032845105&partnerID=40&md5=ff98c1c98654b11a1f7108b3add69062","Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnologia (CSIC), Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Salanueva, I.J., Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Carrascosa, J.L., Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Risco, C., Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain, Dept. of Macromolecular Structure, Ctro. Nac. de Biotecnologia (CSIC), Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","During the life cycle of the transmissible gastroenteritis coronavirus (TGEV), two types of virus-related particles are detected in infected swine testis cells: large annular viruses and small dense viruses. We have studied the relationships between these two types of particles. Immunoelectron microscopy showed that they are closely related, since both large and small particles reacted equally with polyclonal and monoclonal antibodies specific for TGEV proteins. Monensin, a drug that selectively affects the Golgi complex, caused an accumulation of large annular viral particles in perinuclear elements of the endoplasmic reticulum-Golgi intermediate compartment. A partial reversion of the monensin blockade was obtained in both the absence and presence of cycloheximide, a drug that prevented the formation of new viral particles. After removal of monensin, the Golgi complex recovered its perinuclear location, and a decrease in the number of perinuclear large viral particles was observed. The release of small dense viral particles into secretory vesicles and the extracellular medium was also observed, as was a partial recovery of infectivity in culture supernatants. Small viral particles started to be seen between the third and the fourth Golgi cisternae of normally infected cells. All of these data strongly indicate that the large annular particles are the immature precursors of the small dense viruses, which are the infectious TGEV virions. 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Virol., 62, pp. 2762-2772","Risco, C.; Dept. of Macromolecular Structure, Centro Nacional Biotecnologia (CSIC), Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; email: crisco@cnb.uam.es",,,0022538X,,JOVIA,"10482542","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032845105
"Wu G.F., Perlman S.","7404976255;7102708317;","Macrophage infiltration, but not apoptosis, is correlated with immune- mediated demyelination following murine infection with a neurotropic coronavirus",1999,"Journal of Virology","73","10",,"8771","8780",,98,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032845113&partnerID=40&md5=e091b79e9d46e25391e1b77e2d424933","Program in Neuroscience, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, 2042 Medical Labs., Iowa City, IA 52242, United States","Wu, G.F., Program in Neuroscience, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Program in Neuroscience, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, 2042 Medical Labs., Iowa City, IA 52242, United States","Mice infected with mouse hepatitis virus strain JHM (MHV-JHM) develop a chronic demyelinating encephalomyelitis that is in large part immune mediated. Potential mechanisms of immune activity were assessed using an adoptive transfer system. Mice deficient in recombinase-activating gene function (RAGI(-/-)), defective in B- and T-cell maturation, become persistently infected with MHV but do not develop demyelination. Adoptive transfer of splenocytes from mice immunized to MHV into RAG1(-/-) mice infected with an attenuated strain of the virus results in the rapid and progressive development of demyelination. Most striking, adoptive transfer resulted, within 5 to 6 days, in extensive recruitment of activated macrophages/microglia to sites of demyelination within the spinal cord. Clearance of virus antigen occurred preferentially from the gray matter of the spinal cord. Apoptotic cells were identified in both the gray and white matter of the central nervous system (CNS) from RAG1(-/-) mice before and after adoptive transfer, with a moderate increase in number, but not distribution, of apoptotic cells following the development of demyelination. These results suggest that apoptosis following MHV-JHM infection of the murine CNS is not sufficient to cause demyelination. These results, showing that macrophage recruitment and myelin destruction occur rapidly after immune reconstitution of RAG(-/-) mice, suggest that this will be a useful system for investigating MHV-induced demyelination.",,"virus antigen; animal cell; animal experiment; animal model; article; b lymphocyte; cell maturation; controlled study; coronavirus; demyelination; gene function; macrophage migration; mouse; murine hepatitis coronavirus; nonhuman; priority journal; spleen cell; t lymphocyte; Animals; Antigens, Viral; Apoptosis; Cell Movement; Coronavirus Infections; Demyelinating Diseases; Macrophage Activation; Mice; Murine hepatitis virus","Barac-Latas, V., Suchanek, G., Breitschopf, H., Stuehler, A., Wege, H., Lassmann, H., Patterns of oligodendrocyte pathology in coronavirus-induced subacute demyelinating encephalomyelitis in the Lewis rat (1997) Glia, 19, pp. 1-12; Bauer, J., Bradl, M., Hickey, W.F., Forss-Petter, S., Breitschopf, H., Linington, C., Wekerte, H., Lassmann, H., T-cell apoptosis in inflammatory brain lesions: Destruction of T cells does not depend on antigen recognition (1998) Am. 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Immunol., 6, pp. 1061-1070; Monastra, G., Cabrelle, A., Zambon, A., Rosato, A., Macino, B., Collavo, D., Zanovello, P., Membrane form of TNF alpha induces both cell lysis and apoptosis in susceptible target cells (1996) Cell. Immunol., 171, pp. 102-110; Nicotera, P., Bonfoco, E., Brune, B., Mechanisms for nitric oxideinduced cell death: Involvement of apoptosis (1995) Adv. Neuroimmunol., 5, pp. 411-420; Njenga, M.K., Asakura, K., Wettsetin, P., Pease, L.R., Rodriguez, M., The immune system preferentially clears Theiler's virus from the gray matter of the central nervous system (1997) J. Virol., 71, pp. 8592-8601. , H. S. F; Nonoyama, S., Ochs, H.D., Immune deficiency in SCID mice (1996) Int. Rev. Immunol., 13, pp. 289-300; Oberhaus, S.M., Smith, R.L., Clayton, G.H., Dermody, T.S., Tyler, K.L., Reovirus infection and tissue injury in the mouse central nervous system are associated with apoptosis (1997) J. 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Virol., 69, pp. 5898-5903; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Sun, N., Grzybicki, D., Castro, R.F., Murphy, S.P., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Tran, E.H., Hoekstra, K., Van Rooijen, N., Dijkstra, C.D., Owens, T., Immune invasion of the central nervous system parenchyma and experimental allergic encephalomyelitis, but not leukocyte extravasation from blood, are prevented in macrophage-depleted mice (1998) J. Immunol., 161, pp. 3767-3775; Waldner, H., Sobel, R.A., Howard, E., Kuchroo, V.K., Fas- and FasL-deficient mice are resistant to induction of autoimmune encephalomyelitis (1997) J. Immunol., 159, pp. 3100-3103; Wang, F.-I., Hinton, D.R., Gilmore, W., Trousdale, M.D., Fleming, J.O., Sequential infection of glial cells by the murine hepatitis virus JHM strain (MHV-4) leads to a characteristic distribution of demyelination (1992) Lab. Investig., 66, pp. 744-754; Wang, F.-I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Xue, S., Sun, N., Van Rooijen, N., Perlman, S., Depletion of bloodborne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus (1999) J. Virol., 73, pp. 6327-6334","Perlman, S.; Department of Pediatrics, University of Iowa, 2042 Medical Labs, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"10482631","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032845113
"Hasoksuz M., Lathrop S.L., Gadfield K.L., Saif L.J.","6603236044;36836780500;6508283179;7102226747;","Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses",1999,"American Journal of Veterinary Research","60","10",,"1227","1233",,50,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033205818&partnerID=40&md5=9de5e4ca3c42245c08d81233513db6be","Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Istanbul University, Veterinary Faculty, Department of Microbiology, Avcilar, 34851, Istanbul, Turkey","Hasoksuz, M., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States, Istanbul University, Veterinary Faculty, Department of Microbiology, Avcilar, 34851, Istanbul, Turkey; Lathrop, S.L., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Gadfield, K.L., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Saif, L.J., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States","Objective - To isolate bovine coronaviruses from the respiratory tracts of feedlot cattle and compare antigenic and biological properties of these strains with bovine enteric coronaviruses. Animals - 5- to 8-month-old mixed-breed cattle at 4 feedlots. Procedure - Samples were obtained from the nasal passages for testing. The 13 samples with the highest magnitude of positive values for bovine coronavirus (BCV) were cultured. Ten strains of bovine respiratory coronavirus (BRCV) were adapted successfully to serial passage. After observation of cytopathic effects (CPE) and confirmation of BRCV by immune electron microscopy and immunofluorescence testing, cell culture-adapted strains were cloned by limiting dilution. These isolates then were compared with a panel of bovine enteric coroaviruses (BECV), using hemagglutination (HA), receptor-destroying enzyme activity (RDE), hemagglutination inhibition (HI), and virus neutralization (VN) assays. Antigenic relatedness values then were calculated. Results - The BRCV were detected in 105 of 488 (21.5%) of the cattle tested. Of 13 strains tested, 10 were isolated in cell culture. Six of the BRCV strains were similar to 2 strains obtained from neonatal calves with diarrhea and 2 strains from adult cattle with winter dysentery. The other 4 BRCV isolates had high RDE activity against mouse erythrocytes but differed from other strains of BECV. Nine of 10 BRCV isolates had properties similar to the 2 BECV subtypes. Conclusions and Clinical Relevance - The BRCV can be isolated from nasal passages of cattle entering feedlots. Most BRCV were similar to BECV strains, although a few had unique properties. Vaccines developed to protect against enteric strains also may protect against respiratory tract strains.",,"virus antigen; animal; animal disease; article; cattle; cattle disease; cell culture; classification; comparative study; Coronavirus; diarrhea; dysentery; enzyme linked immunosorbent assay; hemagglutination test; human; immunoelectron microscopy; isolation and purification; mouse; newborn; nose mucosa; rectum tumor; respiratory tract infection; virology; virus infection; Animals; Animals, Newborn; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Dysentery; Enzyme-Linked Immunosorbent Assay; Hemagglutination Tests; Humans; Mice; Microscopy, Immunoelectron; Nasal Mucosa; Rectal Neoplasms; Respiratory Tract Infections; Tumor Cells, Cultured","Benfield, D.A., Saif, L.J., Cell culture propagation of coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies between the relationship between coronavirus from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Heckert, R.A., Miller, K.L., Cell culture propagation of bovine coronaviruses (1988) J Tiss Cul Meth, 11, pp. 139-145; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Carman, P.S., Haclett, M.J., Bovine coronavirus infection in Ontario, 1990-91 (1992) Can Vet J, 33, pp. 812-814; Jactel, B., Espinasse, J., Viso, M., An epidemiological study of winter dysentery in fifteen herds in France (1990) Vet Res Commun, 14, pp. 367-369; Jimenez, C., Herbst, W., Bierman, V., Isolation in tissue culture of coronavirus from respiratory diseased calves in the FRG (1989) Zentralbl Veterinarmed [B], 36, pp. 635-638; Pinto, G.B., Hawkes, P., Zabal, O., Viral antibodies in bovine fetuses in Argentina (1993) Res Vet Sci, 55, pp. 385-388; Hasey, D., Reynolds, D.J., Bridger, J.C., Identification of coronaviruses in exotic species of bovidae (1984) Vet Rec, 115, pp. 602-603; Majhdi, F., Minocha, C., Kapil, S., Isolation and characterization of a coronavirus from elk calves with diarrhea (1997) J Clin Virol, 35, pp. 2937-2942; Tsunemitsu, H., El-Kanawati, Z., Smith, D., Isolation of coronavirus antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J Clin Microbiol, 33, pp. 3264-3269; Dea, S., Michaud, L., Milane, G., Comparison of BCV isolates associated with neonatal calf diarrhea and winter dysentery in adult dairy cattle in Quebec (1995) J Gen Virol, 76, pp. 1263-1270; Heckert, R.A., Saif, L.J., Myers, G.W., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am J Vet Res, 52, pp. 845-851; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Cavanagh, D., Brian, D.A., Enjuanes, L., Recommendations of the coronavirus study group for the nomenclature of the structural proteins, mRNAs, and genes of coronaviruses (1990) Virology, 176, pp. 306-307; Degert, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-2877; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advan Virus Res, 48, pp. 1-100; Parker, M.D., Yoo, D., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) J Gen Virol, 71, pp. 263-270; Degert, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Kapil, S., Bergstom, C.C., Botin, P., Plaque variations in clinical isolates of bovine coronavirus (1995) J Vet Invest, 7, pp. 538-539; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J Gen Virol, 73, pp. 901-906; Sato, K., Inaba, Y., Kurogi, H., Hemagglutination by calf diarrhea coronavirus (1977) Vet Microbiol, 2, pp. 83-87; Milane, G., Kourtesis, A.B., Dea, S., Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates (1997) J Clin Microbiol, 35, pp. 33-40; Milane, G., Michaud, L., Dea, S., Biological and molecular differentiation between coronaviruses associated with neonatal calf diarrhea and winter dysentery in adult cattle (1995) Corona and Related Viruses, pp. 29-33. , Tajbot PJ, Levy GA, eds. New York: Plenum Press; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Zhang, X., Herbst, W., Kousoulas, K.G., Comparison of the s genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 134, pp. 421-426; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Smith, D.R., Tsunemitsu, H., Heckert, R.A., The evaluation of two antigen capture ELISAs, employing monoclonal antibodies for detecting coronavirus (1995) J Vet Diagn Invest, 8, pp. 99-105; Fernandez, F.M., Conner, M.E., Parwani, A.V., Isotype-specific antibody responses to rotavirus and virus proteins in cows inoculated with subunit vaccines composed of recombinant SA11 rotavirus core-like particles (CLP) or virus-like particles (VLP) (1996) Vaccine, 14, pp. 1303-1312; Saif, L.J., Bohl, E.H., Kohler, E.M., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Reed, L.J., Muench, H.A., A simple method for estimating fifty percent endpoint (1938) Am J Hyg, 27, pp. 493-497; Archetti, I., Horsfall, F.L., Persistent antigenic variation of influenza A viruses after incomplete neutralization in ovo with heterologous immune serum (1950) J Exp Med, 92, pp. 441-462; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 83, pp. 442-445; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., A serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; McNulty, M.S., Bryson, D.G., Allan, G.M., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-435","Saif, L.J.; Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States",,,00029645,,AJVRA,"10791935","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0033205818
"Harpold L.M., Legendre A.M., Kennedy M.A., Plummer P.J., Millsaps K., Rohrbach B.","7801516412;7005586574;7402308045;13007916200;21641045400;7004280369;","Fecal shedding of feline coronavirus in adult cats and kittens in an Abyssinian cattery",1999,"Journal of the American Veterinary Medical Association","215","7",,"948","951",,21,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033209898&partnerID=40&md5=0a384e8159c1ccb5f98fff83202dbec6","Dept. of Small Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Dept. of Large Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Mesa Veterinary Hospital Ltd., 858 N Country Club Dr, Mesa, AZ 85201, United States","Harpold, L.M., Dept. of Small Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States, Mesa Veterinary Hospital Ltd., 858 N Country Club Dr, Mesa, AZ 85201, United States; Legendre, A.M., Dept. of Small Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Kennedy, M.A., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Plummer, P.J., Dept. of Small Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Millsaps, K., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States; Rohrbach, B., Dept. of Large Anim. Clin. Sciences, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901, United States","Objective - To determine patterns of fecal shedding of feline coronavirus (FCV) by cats, age at which kittens first began to shed FCV in their feces, and whether there was any relationship between fecal shedding of FCV and serum antibody titers in adult cats or kittens. Design - Prospective observational study. Animals - 15 adult cats and 18 kittens from a single cattery. Procedure - Blood and fecal samples were collected from adult cats every other month for 13 months. Serum FCV antibody titers were measured by use of an indirect immunofluorescence assay. A reverse-transcriptase, nested polymerase chain reaction assay was used to detect FCV in feces. Blood and fecal samples were collected from kittens at approximately 2-week intervals from 3 weeks to 15 weeks of age. Results - Adult cats shed FCV intermittently. All adult cats shed virus in their feces at least once during the year, and 4 of 15 shed virus > 75% of the time. Serum antibody titer was not significantly associated with shedding of FCV. For the kittens, median age at the time FCV was first detected in feces was 67 days (range, 33 to 78 days). All except 1 of the kittens was found to be shedding virus in their feces before or at the time of seroconversion. Conclusions and Clinical Relevance - Results suggest that serum FCV antibody titers are not a good indicator of shedding of FCV in the feces. Kittens may shed FCV in their feces before they seroconvert, and all kittens in a cattery in which FCV infection is endemic may be infected before 12 weeks of age.",,"virus antibody; animal; animal disease; article; blood; cat; cat disease; Coronavirus; feces; female; immunology; isolation and purification; newborn; physiology; suckling; vaccination; virology; virus infection; Animals; Animals, Newborn; Animals, Suckling; Antibodies, Viral; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; Feces; Female; Vaccination","Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-22; Vennema, H., Poland, A., Hawkins, K.F., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-46; Poland, A.M., Vennema, H., Foley, J.E., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J Clin Microbiol, 34, pp. 3180-3184; Vennema, H., Poland, A., Foley, J., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Foley, J.E., Poland, A., Carlson, J., Patterns of feline coronavirus infections and fecal shedding from cats in multiple-cat environments (1997) J Am Vet Med Assoc, 210, pp. 1307-1312; Addie, D.D., Jannett, L., Control of feline coronavirus infections in breeding catteries by serotesting, isolation, and early weaning (1995) Feline Pract, 23, pp. 92-95; Herrewegh, A., DeGroot, R.J., Cepica, A., Detection of feline coronavirus RNA in feces, tissue, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Herrewegh, A., Egberink, H.F., Horsinek, M.C., Polymerase chain reaction (PCR) for the diagnosis of naturally occurring feline coronavirus infections (1995) Feline Pract, 23, pp. 56-60; Schlesselman, J.J., (1982) Case-control Studies, pp. 203-206. , New York: Oxford University Press; Meta, C.R., Patel, N.R., A network algorithm for performing Fisher's exact test in rXc contingency tables (1983) J Am Stat Assoc, 78, pp. 427-434; Foley, J.E., Poland, A., Carlson, J., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) J Am Vet Med Assoc, 210, pp. 1313-1319; Herrewegh, A.A., Mahler, M., Hedrich, H.J., Persistence and evolution of feline corona virus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363","Harpold, L.M.; Mesa Veterinary Hospital Ltd., 858 N Country Club Dr, Mesa, AZ 85201, United States",,,00031488,,JAVMA,"10511857","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0033209898
"Van Marle G., Dobbe J.C., Gultyaev A.P., Luytjes W., Spaan W.J.M., Snijder E.J.","6603893383;6602684547;6701385719;6701683324;7007172944;7006058325;","Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences",1999,"Proceedings of the National Academy of Sciences of the United States of America","96","21",,"12056","12061",,163,"10.1073/pnas.96.21.12056","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032718485&doi=10.1073%2fpnas.96.21.12056&partnerID=40&md5=8ff4684ada0611fd2965f4eab9da5241","Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Sect. Theor. Biol. and Phylogenetics, Inst. of Evol. and Ecol. Sciences, Leiden University, Leiden, Netherlands; Natl. Inst. Pub. Hlth. the Environ., Bilthoven, Netherlands; Department of Virology, Leiden University Medical Center, LUMC P4-26, P.O. Box 9600, 2300 RC, Leiden, Netherlands","Van Marle, G., Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Dobbe, J.C., Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Gultyaev, A.P., Sect. Theor. Biol. and Phylogenetics, Inst. of Evol. and Ecol. Sciences, Leiden University, Leiden, Netherlands; Luytjes, W., Department of Virology, Leiden University Medical Center, Leiden, Netherlands, Natl. Inst. Pub. Hlth. the Environ., Bilthoven, Netherlands; Spaan, W.J.M., Department of Virology, Leiden University Medical Center, Leiden, Netherlands; Snijder, E.J., Department of Virology, Leiden University Medical Center, Leiden, Netherlands, Department of Virology, Leiden University Medical Center, LUMC P4-26, P.O. Box 9600, 2300 RC, Leiden, Netherlands","To generate an extensive set of subgenomic (sg) mRNAs, nidoviruses (arteriviruses and coronaviruses) use a mechanism of discontinuous transcription. During this process, mRNAs are generated that represent the genomic 5' sequence, the so-called leader RNA, fused at specific positions to different 3' regions of the genome. The fusion of the leader to the mRNA bodies occurs at a short, conserved sequence element, the transcription- regulating sequence (TRS), which precedes every transcription unit in the genome and is also present at the 3' end of the leader sequence. Here, we have used site-directed mutagenesis of the infectious cDNA clone of the arterivirus equine arteritis virus to show that sg mRNA synthesis requires a base-pairing interaction between the leader TRS and the complement of a body TRS in the viral negative strand. Mutagenesis of the body TRS of equine arteritis virus RNA7 reduced sg RNA7 transcription severely or abolished it completely. Mutations in the leader TRS dramatically influenced the synthesis of all sg mRNAs. The construction of double mutants in which a mutant leader TRS was combined with the corresponding mutant RNA7 body TRS resulted in the specific restoration of mRNA7 synthesis. The analysis of the mRNA leader-body junctions of a number of mutants with partial transcriptional activity provided support for a mechanism of discontinuous minus-strand transcription that resembles similarity-assisted, copy-choice RNA recombination.",,"messenger RNA; animal cell; arterivirus; article; cell strain bhk; controlled study; equine viral arteritis virus; messenger RNA synthesis; nonhuman; nucleotide sequence; priority journal; RNA sequence; site directed mutagenesis; transcription regulation; virus genome; virus transcription; 5' Untranslated Regions; Arterivirus; Base Pairing; Base Sequence; Gene Expression Regulation, Viral; Models, Genetic; Molecular Sequence Data; Mutagenesis; RNA, Antisense; RNA, Messenger; RNA, Viral; Sequence Analysis, RNA; Transcription, Genetic; Transfection","McKnight, S.L., Yamamoto, K.R., (1992) Transcriptional Regulation, , Cold Spring Harbor Lab. Press, Plainview, NY; Von Hippel, P.H., (1998) Science, 281, pp. 660-665; Adkins, S., Stawicki, S.S., Faurote, G., Siegel, R.W., Kao, C.C., (1998) RNA, 4, pp. 455-470; Siegel, R.W., Bellon, L., Beigelman, L., Kao, C.C., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 11613-11618; Lai, M.M.C., Cavanagh, D., (1997) Adv. Virus Res., 48, pp. 1-100; Snijder, E.J., Meulenberg, J.J.M., (1998) J. Gen. Virol., 79, pp. 961-979; Jacobs, L., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., (1981) J. Virol., 39, pp. 401-406; Baric, R.S., Stohlman, S.A., Lai, M.M.C., (1983) J. Virol., 48, pp. 633-640; Spaan, W.J.M., Delius, H., Skinner, M., Armstrong, J., Rottier, P.J.M., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., (1983) EMBO J., 2, pp. 1839-1844; Den Boon, J.A., Spaan, W.J.M., Snijder, E.J., (1995) Virology, 213, pp. 364-372; Sethna, P.B., Hung, S.L., Brian, D.A., (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Sethna, P.B., Hofmann, M.A., Brian, D.A., (1991) J. Virol., 65, pp. 320-325; Den Boon, J.A., Kleijnen, M.F., Spaan, W.J.M., Snijder, E.J., (1996) J. Virol., 70, pp. 4291-4298; Sawicki, S.G., Sawicki, D.L., (1990) J. Virol., 64, pp. 1050-1056; Schaad, M.C., Baric, R.S., (1994) J. Virol., 68, pp. 8169-8179; Sawicki, S.G., Sawicki, D.L., (1995) Corona- and Related Viruses, pp. 499-505. , eds. Talbot, P. J. & Levy, G. A. (Plenum, New York); Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; De Vries, A.A.F., Chirnside, E.D., Bredenbeek, P.J., Gravestein, L.A., Horzinek, M.C., Spaan, W.J.M., (1990) Nucleic Acids Res., 18, pp. 3241-3247; Van Der Meer, Y., Van Tol, H., Krijnse Locker, J., Snijder, E.J., (1998) J. Virol., 72, pp. 6689-6698; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., (1994) J. Virol., 68, pp. 5755-5764; Glaser, A.L., De Vries, A.A.F., Dubovi, E.J., (1995) J. Gen. Virol., 76, pp. 2223-2233; MacLachlan, N.J., Balasuriya, U.B., Hedges, J.F., Schweidler, T.M., McCollum, W.H., Timoney, P.J., Hullinger, P.J., Patton, J.F., (1998) J. Vet. Diagn. Invest., 10, pp. 229-236; Van Marle, G., Van Dinten, L.C., Luytjes, W., Spaan, W.J.M., Snijder, E.J., (1999) J. Virol., 73, pp. 5274-5281; Van Batenburg, F.H.D., Gultyaev, A.P., Pleij, C.W.A., (1995) J. Theor. Biol., 174, pp. 269-280; Gultyaev, A.P., Van Batenburg, F.H.D., Pleij, C.W.A., (1995) J. Mol. Biol., 250, pp. 37-51; Li, H.P., Zhang, X., Duncan, R., Comai, L., Lai, M.M.C., (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9544-9549; Li, H.P., Huang, P., Park, R.S., Lai, M.M.C., (1999) J. Virol., 73, pp. 772-777; Brian, D.A., Spaan, W.J.M., (1997) Semin. Virol., 8, pp. 101-111; Baker, S.C., Lai, M.M.C., (1990) EMBO J., 9, pp. 4173-4179; White, K.A., Morris, T.J., (1995) RNA, 1, pp. 1029-1040; Nagy, P.D., Simon, A.E., (1997) Virology, 235, pp. 1-9; Chang, R.Y., Krishnan, R., Brian, D.A., (1996) J. Virol., 70, pp. 2720-2729; Wagner, E.G.H., Simons, R.W., (1994) Annu. Rev. Microbiol., 48, pp. 713-742; Gerdes, K., Gultyaev, A.P., Franch, T., Pedersen, K., Mikkelsen, N.D., (1997) Annu. Rev. Genet., 31, pp. 1-31; Makino, S., Joo, M., Makino, J.K., (1991) J. Virol., 65, pp. 6031-6041; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., (1994) J. Virol., 68, pp. 8223-8231","Snijder, E.J.; Department of Virology, Leiden University Medical Center, LUMC P4-26, PO Box 9600, 2300 RC Leiden, Netherlands; email: Snijder@virology.azl.nl",,,00278424,,PNASA,"10518575","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0032718485
"Maeda J., Maeda A., Makino S.","23135329700;7201779383;7403067550;","Release of coronavirus E protein in membrane vesicles from virus- infected cells and E protein-expressing cells",1999,"Virology","263","2",,"265","272",,55,"10.1006/viro.1999.9955","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033604298&doi=10.1006%2fviro.1999.9955&partnerID=40&md5=2d0acfe66f1c248fa9e463abe68d436f","Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States; Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77551-1019, United States","Maeda, J., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77551-1019, United States; Maeda, A., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77551-1019, United States; Makino, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas at Austin, Austin, TX 78712, United States, Dept. of Microbiology and Immunology, Univ. of Texas Med. Br. at Galveston, Galveston, TX 77551-1019, United States","Coronavirus E protein is a small viral envelope protein that plays an essential role in coronavirus assembly; coexpression of coronavirus M and E proteins results in the production of virus-like particles. The present study demonstrated that mouse hepatitis virus (MHV) E protein was released as an integral membrane protein in lipid vesicles from E-protein-expressing mammalian cells, in the absence of other MHV proteins. Furthermore, our data indicated that the E-protein-containing vesicles, which had a slightly lighter buoyant density than that of MHV, were released from MHV-infected cells. These data implied that E protein alone can drive the production and release of coronavirus envelope in the absence of M protein.",,"M protein; virus protein; article; Coronavirus; lipid vesicle; membrane vesicle; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; protein secretion; virus envelope; virus infection; Animalia; Coronavirus; Mammalia; Murinae; Murine hepatitis virus; RNA viruses","Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, , San Diego: Academic Press. p. 1-100; Bos, E.C., Luytjes, W., Van Der Meulen, H.V., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Kim, K.H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J. Virol., 71, pp. 3922-3931; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Bredenbeek, P.J., Frolov, I., Rice, C.M., Schlesinger, S., Sindbis virus expression vectors: Packaging of RNA replicons by using defective helper RNAs (1993) J. Virol., 67, pp. 6439-6446; Lustig, S., Jackson, A.C., Hahn, C.S., Griffinn, D.E., Strauss, E.G., Strauss, J.H., Molecular basis of Sindbis virus neurovirulence in mice (1988) J. Virol., 62, pp. 2329-2336; Yu, X., Bi, W., Weiss, S.R., Leibowits, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Hirano, N., Hino, S., Fujiwara, K., Physico-chemical properties of mouse hepatitis virus (MHV-2) grown on DBT cell culture (1978) Microbiol. Immunol., 22, pp. 377-390; Zhang, J., Lamb, R.A., Characterization of the membrane association of the influenza virus matrix protein in living cells (1996) Virology, 225, pp. 255-266; Fujiki, Y., Hubbard, A.L., Fowler, S., Lazarow, P.B., Isolation of intracellular membrane by means of sodium carbonate treatment: Application to endoplasmic reticulum (1982) J. Cell. Biol., 93, pp. 97-102; Li, Y., Luo, L., Schubert, M., Wagner, R.R., Kang, C.Y., Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus (1993) J. Virol., 97, pp. 4415-4420; Wills, J.W., Cameron, C.E., Wilson, C.B., Xiang, Y., Bennett, R.P., Leis, J., An assembly domain of the Rous sarcoma virus Gag protein required late in budding (1994) J. Virol., 68, pp. 6605-6618; Garnier, L., Wiills, J.W., Verderame, M.F., Sudol, M., WW domains and retrovirus budding (1996) Nature (London), 381, pp. 744-745; Xiang, Y., Cameron, C.E., Wills, J.W., Leis, J., Fine mapping and characterization of the Rous sarcoma virus Pr76gag late assembly domain (1996) J. Virol., 70, pp. 5695-5700; Harty, R.N., Paragas, J., Sudol, M., Palese, P., A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding (1999) J. Virol., 73, pp. 2921-2929; Craven, R.C., Harty, R.N., Paragas, J., Palese, P., Wills, J.W., Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras (1999) J. Virol., 73, pp. 3359-3365; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462","Makino, S.; Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77551-1019, United States; email: shmakino@utmb.edu",,"Academic Press Inc.",00426822,,VIRLA,"10544100","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0033604298
"Piñón J.D., Teng H., Weiss S.R.","35870444000;55424332900;57203567044;","Further requirements for cleavage by the murine coronavirus 3C-like proteinase: Identification of a cleavage site within ORF1b",1999,"Virology","263","2",,"471","484",,11,"10.1006/viro.1999.9954","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344994525&doi=10.1006%2fviro.1999.9954&partnerID=40&md5=7c8b156e6d6dc695197a0f55589e7669","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","Piñón, J.D., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Teng, H., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States","The coronavirus mouse hepatitis virus strain A59 (MHV-A59) encodes a 3C- like proteinase (3CLpro) that is proposed to be responsible for the majority of the processing events that take place within the replicase polyproteins pp1a and pp1ab. In this study we demonstrate that the Q939↓S940 peptide bond, located between the polymerase and Zn-finger regions of pp1ab (the POL↓Zn site), is processed by the 3CLpro, albeit inefficiently. Mutagenesis of the POL↓Zn site, as well as the previously identified HD1↓3C site in the 1a region of pp1a and pp1ab, demonstrated that the amino acid residues at the P2 and P1 positions of the cleavage site, occupied by L and Q, respectively, were important determinants of 3CLpro substrate specificity. Finally, a direct comparison of the 3CLpro-mediated cleavages at the HD1↓3C and POL↓Zn sites was made by determining the rate constants using synthetic peptides. The results show that while a larger polypeptide substrate carrying the HD1↓3C site was processed more efficiently than a polypeptide substrate carrying the POL↓Zn site, cleavage of the synthetic peptide substrates containing these two cleavage sites occurred at similar efficiencies. This indicates that the overall conformation of a large polyprotein substrate is important in the accessibility of the cleavage site to the proteinase.",,"amino acid; proteinase; virus enzyme; zinc finger protein; article; chemical binding; enzyme specificity; Murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; protein conformation; protein degradation; site directed mutagenesis; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Baker, S.C., Shieh, C.K., Chang, M.F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Piñon, J.D., Weiss, S.R., Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site (1995) Virology, 209, pp. 489-497; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res., 18, pp. 1825-1832; Brierley, I., Boursnell, M.E.G., Binns, M.M., Billimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Cavanagh, D., A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 20, pp. 316-320; Denison, M.R., Spaan, W.J.M., Van Der Meer, Y., Gibson, C.A., Sims, A.C., Prentice, E., Lu, X.T., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) J. Virol., 73, pp. 6862-6871; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, J.L., Weiss, S.R., Intracellular processing of the N-terminal ORF 1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59 (1991) J. Virol., 65, pp. 3076-3082; De Vries, A.A.F., Horzinek, F.M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. 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Virol., 78, pp. 71-75; Sims, A.C., Lu, X.T., Denison, M.R., Expression, purification, and activity of recombinant MHV-A59 3CLpro (1998) Adv. Exp. Med. Biol., 440, pp. 129-134; Teng, H., Piñón, J.D., Weiss, S.R., Expression of murine coronavirus recombinant papain-like proteinase: Efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides (1999) J. Virol., 73, pp. 2658-2666; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Van Dinten, L.C., Sietske, R., Gorbalenya, A.E., Snijder, E.J., Proteolytic processing of the open reading frame 1b-encoded part of the arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication (1999) J. Virol., 73, pp. 2027-2037; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase assay (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185","Weiss, S.R.; 203A Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"10544119","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0344994525
"Reddy P.S., Idamakanti N., Chen Y., Whale T., Babiuk L.A., Mehtali M., Tikoo S.K.","16943768100;6602833966;57196264442;6504629265;35427029400;56607974600;7005561263;","Replication-defective bovine adenovirus type 3 as an expression vector",1999,"Journal of Virology","73","11",,"9137","9144",,84,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032853359&partnerID=40&md5=ba79d0b50547d3a465f4976ded0edb6b","Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Gene Therapy Department, Transgene, S.A., 67000 Strasbourg, France; Genetic Therapy, Inc., Gaithersburg, MD 20878, United States; VIDO, University of Saskatchewan, 120 Veterinary Rd., Saskatoon, Sask. S7N 5E3, Canada","Reddy, P.S., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada, Genetic Therapy, Inc., Gaithersburg, MD 20878, United States; Idamakanti, N., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Chen, Y., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Whale, T., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Babiuk, L.A., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Mehtali, M., Gene Therapy Department, Transgene, S.A., 67000 Strasbourg, France; Tikoo, S.K., Virology Group, Vet. Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada, VIDO, University of Saskatchewan, 120 Veterinary Rd., Saskatoon, Sask. S7N 5E3, Canada","Although recombinant human adenovirus (HAV)-based vectors offer several advantages for somatic gene therapy and vaccination over other viral vectors, it would be desirable to develop alternative vectors with prolonged expression and decreased toxicity. Toward this objective, a replication- defective bovine adenovirus type 3 (BAV-3) was developed as an expression vector. Bovine cell lines designated VIDO R2 (HAV-5 E1A/B-transformed fetal bovine retina cell [FBRC] line) and 6.93.9 (Madin-Darby bovine kidney [MDBK] cell line expressing E1 proteins) were developed and found to complement the E1A deletion in BAV-3. Replication-defective BAV-3 with a 1.7-kb deletion removing most of the E1A and E3 regions was constructed. This virus could be grown in VIDO R2 or 6.93.9 cells but not in FBRC or MDBK cells. The results demonstrated that the E1 region of HAV-5 has the capacity to transform bovine retina cells and that the E1A region of HAV-5 can complement that of BAV-3. A replication-defective BAV-3 vector expressing bovine herpesvirus type 1 glycoprotein D from the E1A region was made. A similar replication-defective vector expressing the hemagglutinin-esterase gene of bovine coronavirus from the E3 region was isolated. Although these viruses grew less efficiently than the replication-competent recombinant BAV-3 (E3 deleted), they are suitable for detailed studies with animals to evaluate the safety, duration of foreign gene expression, and ability to induce immune responses. In addition, a replication-competent recombinant BAV-3 expressing green fluorescent protein was constructed and used to evaluate the host range of BAV-3 under cell culture conditions. The development of bovine E1A-complementing cell lines and the generation of replication-defective BAV-3 vectors is a major technical advancement for defining the use of BAV-3 as vector for vaccination against diseases of cattle and somatic gene therapy in humans.",,"virus vector; Adenovirus; animal cell; article; cattle; gene therapy; nonhuman; priority journal; virus replication; Adenovirus E1A Proteins; Animals; Blotting, Western; Cattle; Cell Line; Defective Viruses; Genetic Vectors; Green Fluorescent Proteins; Hemagglutinins, Viral; Humans; Luminescent Proteins; Mastadenovirus; Plasmids; Precipitin Tests; Recombinant Proteins; Sequence Deletion; Transfection; Viral Proteins; Virus Replication","Baca-Estrada, M.E., Liang, X., Babiuk, L.A., Yoo, D., Induction of mucosal immunity in cotton rats to hamagglutinin-esterase glycoprotein of bovine coronavirus by recombinant adenovirus (1995) Immunology, 86, pp. 134-140; Ball, A.O., Williams, M.E., Spindler, K.R., Identification of mouse adenovirus type 1 early region 1: DNA sequence and a conserved transactivating function (1988) J. 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Virol., 77, pp. 1-9; Mittal, S.K., Papp, Z., Tikoo, S.K., Baca-Esrada, M.E., Yoo, D., Benko, M., Babiuk, L.A., Induction of systemic and mucosal immune responses in cotton rats immunized with human adenovirus type 5 recombinants expressing the full length and truncated forms of bovine herpesvirus type 1 glycoprotein gD (1996) Virology, 222, pp. 299-309; Papp, Z., Middleton, D., Mittal, S.K., Babiuk, L.A., Baca-Estrada, M.E., Mucosal immunization with recombinant adenoviruses:Induction of immunity and protection of cotton rats against respiratory bovine herpesvirus type 1 infection (1997) J. Gen. Virol., 78, pp. 2933-2943; Parker, M.D., Cox, G.J., Deregt, D., Fitzpatrick, D.R., Babiuk, L.A., Cloning and in vitro expression of the gene for the E3 haeagglutinin glycoprotein of bovine coronavirus (1989) J. Gen. Virol., 70, pp. 155-164; Reddy, P.S., Idamakanti, N., Babiuk, L.A., Tikoo, S.K., (1999), Unpublished data; Reddy, P.S., Chen, Y., Idamakanti, N., Pyne, C., Babiuk, L.A., Tikoo, S.K., Characterization of early region 1 and pIX of bovine adenovirus-3 (1999) Virology, 253, pp. 299-308; Reddy, P.S., Idamakanti, N., Hyun, B., Tikoo, S.K., Babiuk, L.A., Development of porcine adenovirus-3 as an expression vector (1999) J. Gen. Virol., 80, pp. 563-570; Reddy, P.S., Idamakanti, N., Zakhartchouk, A.N., Baxi, M.K., Lee, J.B., Pyne, C., Babiuk, L.A., Tikoo, S.K., Nucleotide sequence, genome organization and transcription map of bovine adenovirus type 3 (1998) J. Virol., 72, pp. 1394-1402; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: a Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Tikoo, S.K., Fitzpatrick, D.R., Babiuk, L.A., Zamb, T.J., Molecular cloning, sequencing and expression of functional bovine herpesvirus 1 glycoprotein gIV in transfected bovine cells (1990) J. Virol., 64, pp. 5132-5142; Tikoo, S.K., Campos, M., Babiuk, L.A., Bovine herpesvirus 1(BHV-1): Biology, pathogenesis and control (1995) Adv. Virus Res., 45, pp. 191-223; Van Drunen Littel-Van Den Hurk, S., Parker, M.D., Massie, B., Van Den Hurk, J.V., Harland, R., Babiuk, L.A., Zamb, T.J., Protection of cattle from BHV-1 infection by immunization with recombinant glycoprotein gIV (1993) Vaccine, 11, pp. 25-35; Van Drunen Littel-Van Den Hurk, S., Tikoo, S.K., Liang, X., Babiuk, L.A., Bovine herpesvirus vaccines (1993) Immunol. Cell Biol., 71, pp. 405-420; Wicham, T.J., Filardo, E.J., Cheresh, D.A., Nemerow, G.R., Integrin-alpha-v-beta and integrin-alpha-v-beta-5 promote adenovirus internalization but not virus attachment (1993) Cell, 73, pp. 309-319; Worgall, S., Wolf, G., Falck-Pedersen, E., Crystal, R.G., Innate immune mechanisms dominate elimination of adenoviral vectors following in vivo administration (1997) Hum. Gene Ther., 8, pp. 37-44; Xu, Z.Z., Both, G.W., Altered tropism of an ovine adenovirus carrying the fiber protein cell binding domain of human adenovirus type 5 (1998) Virology, 248, pp. 156-163; Xu, Z.Z., Hyatt, A., Boyle, D.B., Both, G.W., Construction of ovine adenovirus recombinants by gene insertion or deletion of related terminal region sequences (1997) Virology, 230, pp. 62-71; Yates, W.D.G., A review of infectious bovine rhinotracheitis, shipping fever pneumonia and viral-bacterial synergism in respiratory diseases of cattle (1982) Can J. Comp. Med., 46, pp. 225-263; Zakhartchouk, A.N., Pyne, C., Mutwiri, G.K., Papp, Z., Baca-Estrada, M., Griebel, P., Babiuk, L.A., Tikoo, S.K., Mucosal immunization of calves with recombinant bovine adenovirus-3: Induction of protective immunity to bovine herpesvirus-1 (1999) J. Gen. Virol., 80, pp. 1263-1269; Zakhartchouk, A.N., Reddy, P.S., Baxi, M., Baca-Estrada, M.E., Mehtali, M., Babiuk, L.A., Tikoo, S.K., Construction and characterization of E3 deleted bovine adenovirus type 3 expressing full-length and truncated form of bovine herpesvirus type 1 glycoprotein gD (1998) Virology, 250, pp. 220-229; Zheng, B., Mittal, S.K., Graham, F.L., Prevec, L., The El sequence of bovine adenovirus type 3 and complementation of human adenovirus type 5 E1A function in bovine cells (1994) Virus Res., 31, pp. 163-186","Tikoo, S.K.; VIDO, University of Saskatchewan, 120 Veterinary Rd., Saskatoon, Sask. S7N 5E3, Canada; email: tikoo@sask.usask.ca",,,0022538X,,JOVIA,"10516020","English","J. Virol.",Article,"Final",,Scopus,2-s2.0-0032853359
"Dee S.","7006501484;","Viral Respiratory Diseases of Nursery Pigs",1999,"Compendium on Continuing Education for the Practicing Veterinarian","21","11",,"S258","S263",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347156612&partnerID=40&md5=ebc799baf203a4c67af20336787ff6d7","University of Minnesota, United States; Swine Medicine Faculty, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States; Amer. Coll. of Vet. Microbiologists, United States","Dee, S., University of Minnesota, United States, Swine Medicine Faculty, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States, Amer. Coll. of Vet. Microbiologists, United States","As pig production intensifies, so does the role of the respiratory virus. This article describes three viral pathogens - pseudorabies virus, swine influenza virus, and porcine respiratory coronavirus - known to be significant contributors to respiratory disease problems experienced in nursery pig production. (Although porcine reproductive and respiratory syndrome virus is not described in this article, several references are provided for interested readers.) An overview of the cause, epidemiology, clinical signs, diagnosis, and control measures of each virus is provided.",,"Arterivirus; Coronavirus; herpetovirus; Influenza virus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Suid herpesvirus 1; Suidae; Sus scrofa; Swine influenza virus","Kluge, J.P., Beran, G.W., Hill, H.T., Platt, K.B., Pseudorabies (Aujeszky's disease) (1992) Diseases of Swine, Ed 7, pp. 312-323. , Leman AD, Straw BE, Glock RD (eds) Ames, IA, Iowa State University Press; Schoenbaum, M.A., Zimmermann, J.J., Beran, G.W., Murphy, D.P., Survival of pseudorabies virus in aerosols (1990) Am J Vet Res, 51, pp. 331-333; Davies, E.B., Beran, G.W., Influence of environmental factors upon the survival of Aujeszky's disease virus (1981) Res Vet Sci, 31, pp. 32-36; Iglesias, G., Pijoan, C., Molitor, T., Interactions of pseudorabies virus with swine alveolar macrophages: Effects of virus infection on cell functions (1989) J Leukoc Biol, 45, pp. 410-415; Osorio, F.A., Latency of Aujeszky's disease virus (1999) Proc 3rd Int Symp PRRS and Aujeszky's Dis, p. 322; Davies, E.B., Beran, G.W., Spontaneous shedding of pseudorabies virus from a clinically recovered post parturient sow (1980) JAVMA, 176, pp. 1345-1347; Annelli, J.F., Morrison, R.B., Goyal, S.M., Pigs having a single reactor to serum antibody tests to Aujeszky's disease virus (1991) Vet Rec, 128, pp. 49-53; Corner, A.H., Pathology of experimental Aujeszky's disease in piglets (1965) Res Vet Sci, 6, pp. 337-343; Dow, C., Mcferran, J.B., The neuropathology of Aujeszky's disease in the pig (1962) Res Vet Sci, 3, pp. 436-442; Murphy, B.R., Webster, R.G., Influenza viruses (1990) Virology, pp. 1091-1154. , Fields B (ed) New York, Raven Press; Easterday, B.C., Hinshaw, V.S., Swine influenza (1992) Diseases of Swine, Ed 7, pp. 349-357. , Leman AD, Straw BE, Glock RD, et al (eds) Ames, IA, Iowa State University Press; Halbur, P.G., Viral contributions to the porcine respiratory disease complex (1993) Proc AASP, pp. 343-350; Hinshaw, V.S., Swine influenza virus in the U.S (1994) Proc AASP, pp. 243-245; Morin, M., Robinson, Y., Causes of mystery swine disease (1992) Can Vet J, 33, p. 6; Pensaert, M.B., Cox, E., Porcine respiratory coronavirus is related to transmissible gastroenteritis virus (1989) Agri Pract, 10, pp. 17-21; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus antigenically similar to transmissible gastroenteritis virus in the United States (1990) J Vet Diagn Invest, 2, pp. 312-317; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19","Dee, S.; Swine Medicine Faculty, College of Veterinary Medicine, University of Minnesota, St. Paul, MN, United States",,,01931903,,,,"English","Compend. Contin. Educ. Pract. Vet.",Article,"Final",,Scopus,2-s2.0-0347156612
"Packer C., Altizer S., Appel M., Brown E., Martenson J., O'Brien S.J., Roelke-Parker M., Hofmann-Lehmann R., Lutz H.","7103089793;6701756957;7101857422;7404129662;7006232043;7402355306;6603020361;7003867023;57202819852;","Viruses of the Serengeti: Patterns of infection and mortality in African lions",1999,"Journal of Animal Ecology","68","6",,"1161","1178",,134,"10.1046/j.1365-2656.1999.00360.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032752225&doi=10.1046%2fj.1365-2656.1999.00360.x&partnerID=40&md5=7aa4c99206996e4e666045bcfb5ca703","Department of Ecology, Evolution and Behaviour, University of Minnesota, St. Paul, MN, United States; James Baker Inst. of Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States; Laboratory of Viral Carcinogetiesis, National Cancer Institute, Frederick, MD, United States; Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Zurich, Switzerland; Department of Ecology, Evolution and Behavior, University of Minnesota, 1987 Upper Buford Circle, St Paul, MN 55108, United States","Packer, C., Department of Ecology, Evolution and Behaviour, University of Minnesota, St. Paul, MN, United States, Department of Ecology, Evolution and Behavior, University of Minnesota, 1987 Upper Buford Circle, St Paul, MN 55108, United States; Altizer, S., Department of Ecology, Evolution and Behaviour, University of Minnesota, St. Paul, MN, United States; Appel, M., James Baker Inst. of Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States; Brown, E., Laboratory of Viral Carcinogetiesis, National Cancer Institute, Frederick, MD, United States; Martenson, J., Laboratory of Viral Carcinogetiesis, National Cancer Institute, Frederick, MD, United States; O'Brien, S.J., Laboratory of Viral Carcinogetiesis, National Cancer Institute, Frederick, MD, United States; Roelke-Parker, M., Laboratory of Viral Carcinogetiesis, National Cancer Institute, Frederick, MD, United States; Hofmann-Lehmann, R., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Zurich, Switzerland; Lutz, H., Clinical Laboratory, Dept. of Int. Veterinary Medicine, University of Zurich, Zurich, Switzerland","1. We present data on the temporal dynamics of six viruses that infect lions (Panthera leo) in the Serengeti National Park and Ngorongoro Crater, Tanzania. These populations have been studied continuously for the past 30 years, and previous research has documented their seroprevalence for feline herpesvirus, feline immunodeficiency virus (FIV), feline calicivirus, feline parvovirus, feline coronavirus and canine distemper virus (CDV). A seventh virus, feline leukaemia virus (FeLV), was absent from these animals. 2. Comprehensive analysis reveals that feline herpesvirus and FIV were consistently prevalent at high levels, indicating that they were endemic in the host populations. Feline calici-, parvo- and coronavirus, and CDV repeatedly showed a pattern of seroprevalence that was indicative of discrete disease epidemics: a brief period of high exposure for each virus was followed by declining seroprevalence. 3. The timing of viral invasion suggests that different epidemic viruses are associated with different minimum threshold densities of susceptible hosts. Furthermore, the proportion of susceptibles that became infected during disease outbreaks was positively correlated with the number of susceptible hosts at the beginning of each outbreak. 4. Examination of the relationship between disease outbreaks and host fitness suggest that these viruses do not affect birth and death rates in lions, with the exception of the 1994 outbreak of canine distemper virus. Although the endemic viruses (FHV and FIV) were too prevalent to measure precise health effects, there was no evidence that FIV infection reduced host longevity.","Epidemic; Population density; Seroprevalence; Susceptibles; Virulence","disease spread; epidemic; felid; mortality; virus; Tanzania; Panthera leo","Alexander, K.A., Appel, M.J.G., African wild dogs (Lycaon pictus) endangered by a canine-distemper epizootic among domestic dogs near the Masai-Mara National Reserve, Kenya (1994) Journal of Wildlife Diseases, 30, pp. 481-485; Alexander, K.A., Kat, P.W., Frank, L.G., Holekamp, K.E., Smale, L., House, C., Appel, M.J.G., Evidence of canine distemper virus infection among free-ranging spotted hyenas (Crocuta crocuta) in the Masai Mara, Kenya (1995) Journal of Zoo and Wildlife Medicine, 26, pp. 201-206; Allison, A.C., Coevolution between hosts and infectious disease agents, and its effects on virulence (1982) Population Biology of Infections Diseases, pp. 245-268. , eds R. M. Anderson & R. M. May, Springer-Verlag, New York; Anderson, R.M., May, R.M., Population biology offectious diseases. Part I (1979) Nature, 280, pp. 361-367; Anderson, R.M., May, R.M., Population biology offectious diseases. Part II (1979) Nature, 280, pp. 455-461; Anderson, R.M., May, R.M., Directly transmitted infectious diseases: Control by vaccination (1982) Science, 215, pp. 1053-1060; Anderson, R.M., May, R.M., (1991) Infectious Diseases of Humans: Dynamics and Control, , Oxford University Press, Oxford; Ballard, W.B., Krausman, P.R., Occurrence of rabies in wolves of Alaska (1997) Journal of Wildlife Diseases, 33, pp. 242-245; Brown, E.W., Yuhki, N., Packer, C., O'Brien, S.J., A lion lentivirus related to feline immunodeficiency virus: Epidemiologic and phylogenetic aspects (1994) Journal of Virology, 68, pp. 5953-5968; Carpenter, M.A., O'Brien, S.J., Coadaptation and immunodeficiency virus: Lessons from the Felidae (1995) Current Opinion in Genetics and Development, 5, pp. 739-745; Cleaveland, S., (1996) The Epidemiology of Rabies and Canine Distemper in the Serengeti, Tanzania, , PhD Thesis, University of London; Courchamp, F., Suppo, C., Fromont, E., Bouloux, C., Dynamics of two feline retroviruses (FIV and FeLV) within one population of cats (1997) Proceedings of the Royal Society of London B, 264, pp. 785-794; Courchamp, F., Yoccoz, N.G., Artois, M., Pontier, D., At-risk individuals in feline immunodeficiency virus epidemiology: Evidence from a multivariate approach in a natural population of domestic cats (Felis catus) (1998) Epidemiology and Infection, 121, pp. 227-236; Creel, S., Creel, N.M., Munson, L., Sanderlin, D., Appel, M.J.G., Serosurvey for selected viral diseases and demography of African wild dogs in Tanzania (1997) Journal of Wildlife Diseases, 33, pp. 823-832; Dobson, A.P., Hudson, P.J., Microparasites: Observed patterns in wild animal populations (1995) Ecology of Infectious Diseases in Natural Populations, pp. 52-89. , eds A. P. Dobson & B. T. Grenfell, Cambridge University Press, Cambridge; Dobson, A.P., McCallum, H., Detecting disease and parasite threats to endangered species and ecosystems (1995) Trends in Ecology and Evolution, 10, pp. 190-193; Dobson, A.P., Meagher, M., The population dynamics of brucellosis in the Yellowstone National Park (1996) Ecology, 77, pp. 1026-1036; Ewald, P., Host-parasite relations, vectors, and the evolution of disease severity (1983) Annual Review of Ecological Systems, 14, pp. 465-485; Grenfell, B.T., Gulland, M.D., Introduction: Ecological impact of parasitism on wildlife host populations (1995) Parasitology, 111, pp. S3-S14; Hanby, J.P., Bygott, J.D., Population changes in lions and other predators (1995) Serengeti: Dynamics of An Ecosystem, pp. 249-262. , eds A. R. E. Sinclair & M. Norton-Griffiths, University of Chicago Press, Chicago; Hanby, J.P., Bygott, J.D., Packer, C., Ecology, demography and behavior of lions in two contrasting habitats: Ngorongoro Crater and the Serengeti Plains (1995) Serengeti II: Research, Management and Conservation of An Ecosystem, pp. 315-331. , eds P. Arcese & A. R. E. Sinclair, University of Chicago Press, Chicago; Herre, E.A., Population structure and the evolution of virulence in nematode parasites of fig wasps (1993) Science, 259, pp. 1442-1445; Hofmann-Lehmann, R., Fehr, D., Grob, M., Elgizoli, M., Packer, C., O'Brien, S.J., Lutz, H., Prevalence of antibodies to feline parvovirus, calicivirus, herpesvirus, coronavirus and feline immunodeficiency virus in sera from lions in East Africa (1996) Clinical and Diagnostic Laboratory Immunology, 3, pp. 554-562; Jaenike, J., On the capacity of macroparasites to control insect populations (1998) American Naturalist, 151, pp. 84-96; Jaffee, B., Phillips, R., Muldoon, A., Mangel, M., Density-dependent host-pathogen dynamics in soil microcosms (1992) Ecology, 73, pp. 495-506; Kaare, M., Cleaveland, S., Targeting rabies control in the Serengeti: The rationale and design of a domestic dog vaccination campaign (1997) Proceedings of the Southern and Eastern African Rabies Group Meeting, Nairobi, Kenva 4-6 March 1997, , eds B. D. Perry, P. Kitala & A. A. King. Editions Foundation Marcel Merieux, Lyon, France; Kat, P.W., Alexander, K.A., Smith, J.S., Munson, L., Rabies and African wild dogs in Kenya (1995) Proceedings of the Royal Society of London B, 262, pp. 229-233; Laurenson, K., Sillero-Zubiri, C., Thompson, H., Shiferaw, F., Thirgood, S., Malcolm, J., Disease as a threat to endangered species: Ethiopian wolves, domestic dogs and canine pathogens (1998) Animal Conservation, 1, pp. 273-280; Lenski, R.E., May, R.M., The evolution of virulence in parasites and pathogens: Reconciliation between two competing hypotheses (1994) Journal of Theoretical Biology, 169, pp. 253-265; Levin, B.R., The evolution and maintenance of virulence in microparasites (1996) Emerging Infectious Diseases, 2, pp. 93-102; Macdonald, D.W., (1980) Rabies and Wildlife, , Oxford University Press, Oxford; Malik, R., Kendall, K., Cridlands, J., Coulston, S., Stuart, A.J., Snow, D., Love, D.N., Prevalence of feline leukemia virus and feline immunodeficiency virus infections in cats in Sydney (1997) Australian Veterinary Journal, 75, pp. 323-327; May, R.M., Parasitic infections as regulators of animal populations (1983) American Scientist, 71, pp. 36-45; O'Brien, S.J., Martenson, J.S., Packer, C., Herbst, L., De Voss, V., Jocelyn, P., Ott-Jocelyn, J., Bush, M., Biochemical genetic variation in geographically isolated populations of African and Asiatic lions (1987) National Geographic Research, 3, pp. 114-124; Olmsled, R.A., Langley, R., Roelke, M., Goeken, R.M., Johnson, D.A., Goff, J., Albert, J., O'Brien, S.J., Worldwide prevalence of lentivirus infection of wild felidae species: Epidemiologic and genetic aspects (1992) Journal of Virology, 66, pp. 6008-6018; Onstad, D.W., Carruthers, R.I., Epizootiological models of insect diseases (1990) Annual Review of Entomology, 35, pp. 399-419; Osterhaus, A., Vedder, E.J., Identification of virus causing recent seal deaths (1988) Nature, 335, p. 20; Packer, C., Herbst, L., Pusey, A.E., Bygott, J.D., Hanby, J.P., Cairns, S.J., Borgerhoff-Mulder, M., Reproductive success of lions (1988) Reproductive Success, pp. 363-383. , ed T. H. Clutton-Brock, University of Chicago Press, Chicago; Packer, C., Pusey, A.E., Rowley, H., Gilbert, D.A., Martenson, J., O'Brien, S.J., Case study of a population bottleneck: Lions of Ngorongoro Crater (1991) Conservation Biology, 5, pp. 219-230; Packer, C., Gilbert, D., Pusey, A.E., O'Brien, S.J., A molecular genetic analysis of kinship and cooperation in African lions (1991) Nature, 351, pp. 562-565; Packer, C., Pusey, A.E., Should a lion change its spots? (1993) Nature, 362, p. 595; Packer, C., Tatar, M., Collins, A., Reproductive cessation in female mammals (1998) Nature, 392, pp. 807-811; Pedersen, N.C., Ho, E.W., Brown, M.L., Yamamoto, J.K., Isolation of a T-lymphocyte virus from domestic cats with an immunodeficiency like syndrome (1987) Science, 235, pp. 790-793; Plowright, W., The effects of rinderpest and rinderpest control on wildlife in Africa (1982) Symposium of the Zoological Society of London, 50, pp. 1-28; Poli, A., Abramo, F., Cavicchio, P., Bandecchi, E., Ghelardi, E., Pistello, M., Lentivirus infection in an African lion: A clinical, pathologic and virologic study (1995) Journal of Wildlife Diseases, 51, pp. 70-74; Pusey, A.E., Packer, C., Non-offspring nursing in social carnivores: Minimizing the costs (1994) Behavioral Ecology, 5, pp. 362-374; Rigby, M.A., Holmes, E.C., Pistello, M., MacKay, A., Leigh-Brown, A.J., Neil, J.C., Evolution of structural patterns of feline immunodeficiency virus: Molecular epidemiology and evidence of selection for change (1993) Journal of General Virology, 74, pp. 425-436; Roelke-Parker, M.E., Munson, L., Packer, C., Kock, R., Cleaveland, S., Carpenter, M., O'Brien, S.J., Appel, M.J.G., A canine distemper virus epidemic in Serengeti lions (Panthera leo) (1996) Nature, 379, pp. 441-445; Schaller, G.B., (1972) The Serengeti Lion, , University of Chicago Press, Chicago; Sillero, Z.C., King, A.A., McDonald, D.W., Rabies and mortality in Ethiopian wolves (Canis simensis) (1996) Journal of Wildlife Diseases, 32, pp. 80-86; Spencer, J.A., Morkel, P., Serological survey of sera from lions in Etosha National Park (1993) S -Afr Tydskr Natuurnav, 23, pp. 60-61; Thorne, E.T., Williams, E.S., Disease and endangered species: The black-footed ferret as a recent example (1988) Conservation Biology, 1, pp. 66-74; Torten, M., Franchini, M., Barlough, J.W., Mozes, E., Lutz, H., Pedersen, N.C., Progressive immune function in cats experimentally infected with feline immunodeficiency virus (1991) Journal of Virology, 65, pp. 2225-2230; Weiler, G.J., Garner, G.W., Ritter, D.O., Occurrence of rabies in a wolf population in northeastern Alaska (1995) Journal of Wildlife Diseases, 31, pp. 79-82; Yamamoto, J.K., Hansen, H., Ho, E.W., Morishita, T.Y., Okuda, T., Sawa, T.R., Nakamura, R.M., Pedersen, N.C., Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission (1989) Journal of the American Veterinary Medical Association, 194, pp. 213-220; Yamamoto, J.K., Sparger, E., Ho, E.W., Anderson, P.R., O'connor, T.P., Mandell, C.P., Lavenstine, L., Pedersen, N.C., Pathogenesis of experimentally induced feline immunodeficiency virus infection in cats (1988) American Journal of Veterinary Research, 49, pp. 1246-1258; Young, T.P., Natural die-offs of large mammals: Implications for conservation (1994) Conservation Biology, 8, pp. 410-418","Packer, C.; Dept. of Ecology, Evolution/Behavior, University of Minnesota, 1987 Upper Buford Circle, St Paul, MN 55108, United States; email: packer@biosci.umn.edu",,,00218790,,JAECA,,"English","J. Anim. Ecol.",Article,"Final",,Scopus,2-s2.0-0032752225
"Compton S.R., Vivas-Gonzalez B.E., Macy J.D.","7102893878;6507307536;7005966543;","Reverse transcriptase polymerase chain reaction-based diagnosis and molecular characterization of a new rat coronavirus strain",1999,"Laboratory Animal Science","49","5",,"506","513",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032710137&partnerID=40&md5=36126a01b9be1347a439172d6337e2d7","Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States; Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States","Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States, Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Vivas-Gonzalez, B.E., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States; Macy, J.D., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States","Background and Purpose: Rat coronaviruses (RCV) are highly infectious and spread rapidly through laboratory rat colonies, causing sneezing, nasal and ocular discharges, photophobia, and cervical swelling. Current diagnostic methods include serologic testing and histologic examination. During a recent rat coronavirus outbreak, we tested a rapid, noninvasive method of RCV diagnosis that involved use of reverse transcriptase-polymerase chain reaction (RT-PCR) analysis to detect RCV RNA on cages housing infected rats. Methods: The RT-PCR was used to detect RCV RNA in tissues from infected rats and on cages housing infected rats and to amplify portions of the RCV N, M, and S genes for molecular characterization. Results: The RT-PCR detected RCV RNA on cages and in tissues from infected rats. The RCV-NJN gene is most closely related to the MHV-Y N gene. The M proteins of RCV-NJ and RCV-SDA are 99% homologous, and the six RCV S protein fragments are 97 to 100% homologous. Conclusions: Use of RT-PCR with cage-swab specimens was capable of diagnosing RCV infection in and viral excretion from rats. Additionally, molecular characterization of the N, M, and S genes of RCV-NJ provided baseline information that can be used in performing further epidemiologic studies.",,"RNA; article; coronavirus; DNA sequence; gene amplification; histology; male; nonhuman; nucleotide sequence; rat; reverse transcription polymerase chain reaction; RNA analysis; sequence analysis; serodiagnosis; virus characterization; virus diagnosis; Amino Acid Sequence; Animals; Base Sequence; Coronavirus Infections; Coronavirus, Rat; DNA Restriction Enzymes; Drug Stability; Male; Molecular Sequence Data; Nucleocapsid; Nucleocapsid Proteins; Plastics; Rats; Rats, Sprague-Dawley; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Rodent Diseases; Viral Matrix Proteins; Viral Proteins","LaRegina, M., Woods, L., Klender, P., Transmission of sialodacryoadenitis virus (SDAV) from infected rats to rats and mice through handling, close contact, and soiled bedding (1992) Lab. Anim. Sci., 42, pp. 344-346; Bhatt, P.N., Jacoby, R.O., Experimental infection of adult axenic rats with Barker's rat coronavirus (1977) Arch. Virol., 54, pp. 345-352; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Pathogenesis of sialodacryoadenitis in gnotobiotic rats (1975) Vet. Pathol., 12, pp. 196-209; Jacoby, R.O., Rat coronavirus (1986) Viral and Mycoplasmal Infections of Rodents, pp. 625-638. , P. N. Bhatt, R. O. Jacoby, H. C. Morse, et al. (ed.), Academic Press, Inc., New York; Homberger, F.R., Smith, A.L., Barthold, S.W., Detection of rodent coronaviruses in tissues and cell cultures by polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Yamada, Y.K., Yabe, M., Yamada, A., Detection of mouse hepatitis virus by the polymerase chain reaction and its application to the rapid diagnosis of infection (1993) Lab. Anim. Sci., 43, pp. 285-290; Herrewegh, A.A.P.M., DeGroot, R.J., Cepica, A., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Kwon, H.M., Jackwood, M.W., Brown, T.P., Polymerase chain reaction and a biotin-labeled probe for detection of infectious bronchitis virus in chickens (1993) Avian Dis., 37, pp. 149-156; Li, X., Scott, F.W., Detection of feline coronaviruses in cell culture and in fresh and fixed feline tissues using polymerase chain reaction (1994) Vet. Microbiol., 43, pp. 65-77; Paton, D., Ibata, G., Sands, J., Detection of transmissible gastroenteritis virus by RT-PCR and differentiation from porcine respiratory coronavirus (1997) J. Virol. Methods, 66, pp. 303-307; Ishikawa, K., Sekiguchi, H., Ogino, T., Direct and rapid detection of porcine epidemic diarrhea virus by RT-PCR (1997) J. Virol. Methods, 69, pp. 191-195; Casebolt, D.B., Qian, B., Stephensen, C.B., Detection of enterotropic mouse hepatitis virus fecal excretion by polymerase chain reaction (1997) Lab. Anim. Sci., 47, pp. 6-10; Goto, K., Kunita, S., Terada, E., Comparison of polymerase chain reaction and culture methods for detection of Mycoplasma pulmonis from nasal, tracheal and oral swabs samples of rats (1994) Exp. Anim., 43, pp. 413-415; Gaertner, D.J., Compton, S.R., Winograd, D.F., Environmental stability of rat coronaviruses (RCVs) (1993) Lab. Anim. Sci., 43, pp. 403-404; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 1-14; Gagneten, S., Scanga, C.A., Dveksler, G.S., Attachment glycoproteins and receptor specificity of rat coronaviruses (1996) Lab. Anim. Sci., 46, pp. 159-166; Gaertner, D.J., Compton, S.R., Winograd, D.F., Growth characteristics and protein profiles of prototype and wild-type rat coronavirus isolates grown in a cloned subline of mouse fibroblasts (1996) Virus Res., 41, pp. 55-68; Barker, M.G., Percy, D.H., Hovland, D.J., Preliminary characterization of the structural proteins of the coronaviruses, sialodacryoadenitis virus and Parker's rat coronavirus (1994) Can. J. Vet. Res., 58, pp. 99-103; Wege, H., Siddell, S., TerMeulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol., 99, pp. 165-200; Kunita, S., Mori, M., Terada, E., Sequence analysis of the nucleocapsid protein gene of rat coronavirus SDAV-681 (1993) Virology, 193, pp. 520-523; Paturzo, F., Transmission of sialodacryoadenitis virus in rats (1987) Lab. Anim. Sci., 37, p. 580; Bhatt, P.N., Jacoby, R.O., Jonas, A.M., Respiratory infection of mice with sialodacryoadenitis virus, a coronavirus of rats (1977) Infect. Immun., 18, pp. 823-827; Barthold, S.W., DeSouza, M., Smith, A.L., Susceptibility of laboratory mice to intranasal and contact infection with coronaviruses of other species (1990) Lab. Anim. Sci., 40, pp. 481-485; Yokomori, K., Asanaka, M., Stohlman, S.A., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56; Asanaka, M., Lai, M.M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Hornberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res., 31, pp. 39-56; Kunita, S., Zhang, L., Hornberger, F.R., Molecular characterization of the S proteins of two enterotropic murine coronavirus strains (1995) Virus Res., 35, pp. 277-289","Compton, S.R.; Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States",,,00236764,,LBASA,"10551451","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0032710137
"Compton S.R., Smith A.L., Gaertner D.J.","7102893878;57203012240;7004631465;","Comparison of the pathogenicity in rats of rat coronaviruses of different neutralization groups",1999,"Laboratory Animal Science","49","5",,"514","518",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032710138&partnerID=40&md5=c1cb882039f542df25322a37003bc4c0","Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States; Dept. of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, United States; Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Department of Pathology, Stritch School of Medicine, Loyola University, Maywood, IL 60153, United States","Compton, S.R., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States, Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States; Smith, A.L., Section of Comparative Medicine, Yale University School of Medicine, New Haven, CT, United States, Department of Pathology, Stritch School of Medicine, Loyola University, Maywood, IL 60153, United States; Gaertner, D.J., Dept. of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, United States","Background and Purpose: Rat coronaviruses (RCVs) are common natural pathogens of rats that cause clinical illness, necrosis, and inflammation of respiratory, salivary, and lacrimal organs. The aim of the study was to determine whether antigenically different strains of RCV vary in their pathogenic potential in rats. Methods: Neutralization groups were identified by use of RCV strain-specific antisera. Sprague Dawley rats were inoculated oronasally with RCV-SDA, RCV-BCMM, or RCV-W. Histologic examination, immunohistochemical analysis, and reverse transcriptase-polymerase chain reaction analysis were performed on tissues from infected rats. Results: Clinical illness was not evident in any of the inoculated rats. The RCV-SDA strain caused mild lesions in the exorbital gland of one rat. The RCV-BCMM strain caused severe lesions in the Harderian and parotid glands and mild lesions in the exorbital glands, lungs, and nasal mucosa. The RCV-W strain caused severe lesions in the Harderian, exorbital, and parotid glands and mild lesions in the submandibular glands, lungs, and nasal mucosa. The RNA concentration was highest in the Harderian, parotid, and exorbital glands of RCV-BCMM- and RCV-W-infected rats at postinoculation day 7. Conclusions: Although RCV-SDA, RCV-BCMM, and RCV-W caused different degrees and patterns of lesions, neutralization groups are not useful for predicting the pathogenic potential of a new RCV isolate.",,"RNA; virus antigen; animal tissue; article; clinical feature; coronavirus; histopathology; immunohistochemistry; lung; male; nonhuman; nose mucosa; parotid gland; rat; reverse transcription polymerase chain reaction; RNA analysis; rodent disease; strain difference; submandibular gland; virus pathogenesis; virus strain; Animals; Antigens, Viral; Coronavirus Infections; Coronavirus, Rat; Harderian Gland; Lung; Nasal Mucosa; Parotid Gland; Rats; Rats, Sprague-Dawley; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Rodent Diseases; Submandibular Gland","Bhatt, P.N., Jacoby, R.O., Experimental infection of adult axenic rats with Parker's rat coronavirus (1977) Arch. Virol., 54, pp. 345-352; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Pathogenesis of sialodacryoadenitis in gnotobiotic rats (1975) Vet. Pathol., 12, pp. 196-209; Jacoby, R.O., Rat coronavirus (1986) Viral and Mycoplasmal Infections of Rodents, pp. 625-638. , P. N. Bhatt, R. O. Jacoby, H. C. Morse, et al. (ed.), Academic Press, Inc., New York; Wege, H., Siddell, S., Termeulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol., 99, pp. 165-200; Gaertner, D.J., Compton, S.R., Winograd, D.F., Growth characteristics and protein profiles of prototype and wild-type rat coronavirus isolates grown in a cloned subline of mouse fibroblasts (1996) Virus Res., 41, pp. 55-68; Barker, M.G., Percy, D.H., Hovland, D.J., Preliminary characterization of the structural proteins of the coronaviruses, sialodacryoadenitis virus and Parker's rat coronavirus (1994) Can. J. Vet. Res., 58, pp. 99-103; Gagneten, S., Scanga, C.A., Dveksler, G.S., Attachment glycoproteins and receptor specificity of rat coronaviruses (1996) Lab. Anim. Sci., 46, pp. 159-166; Weir, E.C., Jacoby, R.O., Paturzo, F.X., Infection of SDAV-immune rats with SDAV and rat coronavirus (1990) Lab. Anim. Sci., 40, pp. 363-366; Percy, D.H., Bond, S.J., Paturzo, F.X., Duration of protection from reinfection following exposure to sialodacryoadenitis virus in Wistar rats (1990) Lab. Anim. Sci., 40, pp. 144-149; Bhatt, P.N., Percy, D.H., Jonas, A.M., Characterization of the virus of sialodacryoadenitis in rats: A member of the coronavirus group (1972) J. Infect. Dis., 126, pp. 123-130; Parker, J.C., Cross, S.S., Rowe, W.P., Rat coronavirus (RCV): A prevalent, naturally occurring pneumotropic virus of rats (1970) Arch. Gesamte Virusforsch., 31, pp. 293-302; Gaertner, D.J., Smith, A.L., Paturzo, F.X., Susceptibility of rodent cell lines to rat coronaviruses and differential enhancement by trypsin and DEAE-dextran (1991) Arch. Virol., 118, pp. 57-66; Gaertner, D.J., Winograd, D.F., Compton, S.R., Development and optimization of plaque assays for rat coronaviruses (1993) J. Virol. Methods, 43, pp. 53-64; Paturzo, F., Transmission of sialodacryoadenitis virus in rats (1987) Lab. Anim. Sci., 37, p. 580; Macy, J.D., Weir, E.C., Barthold, S.W., Reproductive abnormalities associated with a coronavirus infection of rats (1996) Lab. Anim. Sci., 46, pp. 129-132; Kohn, D.F., Barthold, S.W., Biology and diseases of rats (1984) Laboratory Animal Medicine, pp. 91-112. , J. G. Fox, B. J. Cohen, and F. M. Loew (ed.), Academic Press, Inc., New York; Jacoby, R.O., Bhatt, P.N., Jonas, A.M., Viral diseases (1979) The Laboratory Rat, Vol. 1: Biology and Diseases, 1, pp. 272-306. , H. J. Baker, J. R. Lindsey, and S. H. Weisbroth (ed.), Academic Press, Inc., New York; Kojima, A., Okaniwa, A., Antigenic heterogeneity of sialodacryoadenitis virus isolates (1991) J. Vet. Med. Sci., 53, pp. 1059-1063","Compton, S.R.; Section of Comparative Medicine, Yale University School of Medicine, P.O. Box 208016, New Haven, CT 06520-8016, United States",,,00236764,,LBASA,"10551452","English","Lab. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0032710138
"Koetters P.J., Hassanieh L., Stohlman S.A., Gallagher T., Lai M.M.C.","10840800300;8062278100;35502534500;7202310503;7401808497;","Mouse hepatitis virus strain JHM infects a human hepatocellular carcinoma cell line",1999,"Virology","264","2",,"398","409",,13,"10.1006/viro.1999.9984","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033604580&doi=10.1006%2fviro.1999.9984&partnerID=40&md5=7423e9554e1f1d36efbdd581f7d2de6e","Dept. Molec. Microbiol. and Immunol., Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States; Howard Hughes Medical Institute, Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States; Loyola University Medical Center, Maywood, IL 60153, United States","Koetters, P.J., Dept. Molec. Microbiol. and Immunol., Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States; Hassanieh, L., Dept. Molec. Microbiol. and Immunol., Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States; Stohlman, S.A., Dept. Molec. Microbiol. and Immunol., Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States; Gallagher, T., Loyola University Medical Center, Maywood, IL 60153, United States; Lai, M.M.C., Dept. Molec. Microbiol. and Immunol., Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States, Howard Hughes Medical Institute, Univ. S. California Keck Sch. Med., Los Angeles, CA 90033, United States","Mouse hepatitis virus (MHV) strain JHM is a coronavirus that causes encephalitis and demyelination in susceptible rodents. The known receptors for MHV are all members of the carcinoembryonic antigen family. Although human forms of the MHV receptor can function as MHV receptors in some assays, no human cell line has been identified that can support wild-type MHV infection. Here we describe the infection of a human hepatocellular carcinoma cell line, HUH-7, with MHV. HUH-7 cells were susceptible to strains JHM-DL and JHM-DS, yielding virus titers nearly identical to those seen in mouse DBT cells. In contrast, HUH-7 cells were only marginally susceptible or completely resistant to infection by other MHV strains, including A59. JHM produced a strong cytopathic effect in HuH-7 cells with the formation of round plaques. Studies of various recombinant viruses between JHM and A59 strains suggested that the ability of JHM to infect HUH-7 cells was determined by multiple viral genetic elements. Blocking the viral spike (S) protein with a neutralizing antibody or a soluble form of the MHV receptor inhibited infection of HUH-7 cells, suggesting that infection is mediated through the S protein. Transfection with the prototype mouse receptor, biliary glycoprotein, rendered HUH-7 cells susceptible to infection by other MHV strains as well, suggesting that JHM uses a receptor distinct from the classical MHV receptor to infect HUH-7 cells. Possible implications for human disease are discussed.",,"carcinoembryonic antigen; neutralizing antibody; antibody titer; article; Coronavirus; demyelination; hepatitis virus; human; human cell; Human immunodeficiency virus 1; liver cell carcinoma; priority journal; protein analysis; receptor binding; rodent; T lymphocyte","Asanaka, M., Lai, M.M.C., Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry (1993) Virology, 197, pp. 732-741; Baric, R.S., Sullivan, E., Hensley, L., Yount, B., Chen, W., Persistent infection promotes cross-species transmissibility of mouse hepatitis virus (1999) J. 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USA, 92, pp. 12095-12099; Chen, W., Yount, B., Hensley, L., Baric, R.S., Receptor homologue scanning functions in the maintenance of MHV-A59 persistence in vitro (1998) Adv. Exp. Med. Biol., 440, pp. 743-750; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses [published erratum appears in Lab. Anim. Sci., 1993, 43, 203] (1993) Lab. Anim. Sci., 43, pp. 15-28; Dalgleish, A.G., Viruses and multiple sclerosis (1997) Acta. Neurol. Scand. Suppl., 169, pp. 8-15; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; Dveksler, G.S., Dieffenbach, C.W., Cardellichio, C.B., McCuaig, K., Pensiero, M.N., Jiang, G.S., Beauchemin, N., Holmes, K.V., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. 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Rev., 56, pp. 61-79; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: MRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lai, M.M.C., Stohlman, S.A., Comparative analysis of RNA genomes of mouse hepatitis viruses (1981) J. Virol., 38, pp. 661-670; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease [see comments] (1997) Trends Microbiol., 5, pp. 9-14; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139, pp. 138-151; Moore, J.P., Trkola, A., Dragic, T., Co-receptors for HIV-1 entry [see comments] (1997) Curr. Opin. 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Invest., 33, pp. 440-445; Schickli, J.H., Zelus, B.D., Wentworth, D.E., Sawicki, S.G., Holmes, K.V., The murine coronavirus mouse hepatitis virus strain A59 from persistently infected murine cells exhibits an extended host range (1997) J. Virol., 71, pp. 9499-9507; Selinka, H.C., Huber, M., Pasch, A., Klingel, K., Aepinus, C., Kandolf, R., Coxsackie B virus and its interaction with permissive host cells (1998) Clin. Diagn. Virol., 9, pp. 115-123; Smith, G.L., Vanderplasschen, A., Extracellular enveloped vaccinia virus: Entry, egress, and evasion (1998) Adv. Exp. Med. Biol., 440, pp. 395-414; Stohlman, S.A., Brayton, P.R., Fleming, J.O., Weiner, L.P., Lai, M.M.C., Murine coronaviruses: Isolation and characterization of two plaque morphology variants of the JHM neurotropic strain (1982) J. Gen. Virol., 63, pp. 265-275; Tanaka, R., Iwasaki, Y., Koprowski, H., Intracisternal virus-like particles in brain of a multiple sclerosis patient (1976) J. Neurol. Sci., 28, pp. 121-126; Thoulouze, M.I., Lafage, M., Schachner, M., Hartmann, U., Cremer, H., Lafon, M., The neural cell adhesion molecule is a receptor for rabies virus (1998) J. Virol., 72, pp. 7181-7190; Wang, F.I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wang, J., Chou, C.H., Blankson, J., Satoh, M., Knuth, M.W., Eisenberg, R.A., Pisetsky, D.S., Reeves, W.H., Murine monoclonal antibodies specific for conserved and non-conserved antigenic determinants of the human and murine Ku autoantigens (1993) Mol. Biol. Rep., 18, pp. 15-28; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Weiss, S.R., Coronaviruses SD and SK share extensive nucleotide homology with murine coronavirus MHV-A59, more than that shared between human and murine coronaviruses (1983) Virology, 126, pp. 669-677; Williams, R.K., Jiang, G.S., Snyder, S.W., Frana, M.F., Holmes, K.V., Purification of the 110-kilodalton glycoprotein receptor for mouse hepatitis virus (MHV)-A59 from mouse liver and identification of a nonfunctional, homologous protein in MHV-resistant SJL/J mice (1990) J. Virol., 64, pp. 3817-3823; Yamamoto, T., Suda, M., Moriwaki, Y., Takahashi, S., Higashino, K., Novel apoprotein A-I-containing lipoprotein produced by a human hepatoma-derived cell line HuH-7 (1990) Biochim. Biophys. Acta, 1047, pp. 49-56; Yokomori, K., Asanaka, M., Stohlman, S.A., Lai, M.M.C., A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry (1993) Virology, 196, pp. 45-56; Yokomori, K., Asanaka, M., Stohlman, S.A., Makino, S., Shubin, R.A., Gilmore, W., Weiner, L.P., Lai, M.M.C., Neuropathogenicity of mouse hepatitis virus JHM isolates differing in hemagglutinin-esterase protein expression [see comments] (1995) J. Neurovirol., 1, pp. 330-339; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus infection utilizes more than one receptor and requires an additional cellular factor (1993) Adv. Exp. Med. Biol., 342, pp. 273-277; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus receptors: More than a single carcinoembryonic antigen (1994) Arch. Virol. Suppl., 9, pp. 461-471; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.L., Lai, M.M.C., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Lai, M.M.C.; Dept. of Molec. Microbiol./Immunol., Howard Hughes Medical Institute, University of Southern California, Los Angeles, CA 90033, United States; email: michlai@hsc.usc.edu",,"Academic Press Inc.",00426822,,VIRLA,"10562501","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0033604580
"Pascalis H., Laude H.","6508265083;7006652624;","As [Les ARN défectifs interférants chez les coronavirus]",1999,"Virologie","3","6",,"455","464",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033378334&partnerID=40&md5=9401ecc805b1b26d0006b31af0767eed","INRA, Unité de Virologie Immunologie Moléculaire, 78350 Jouy-en-Josas, France","Pascalis, H., INRA, Unité de Virologie Immunologie Moléculaire, 78350 Jouy-en-Josas, France; Laude, H., INRA, Unité de Virologie Immunologie Moléculaire, 78350 Jouy-en-Josas, France","Coronaviruses replication goes along with the appearance of genomic RNA molecules, a commonly observed phenomenon in RNA viruses. Theses molecules, resulting from recombination events are likely to interfere, to a more or less efficient extent, with the wild virus replication. Also, when packed they are likely to infect new cells. This article's aim is a synthesis of up to date knowledge about defective interfèrent RNA in coronaviruses. This study proved to be a decisive asset for better understanding the essential aspects of the virus cycle events such as replication, assembly and packaging. Coronaviruses DI RNA are also particularly useful to study the mechanism of high frequency recombination. This contribution has recently been reinforced as it was shown that a shrewed use of synthetic RNAs arising from defective DI RNA, was an efficient means to bring about targeted changes in genomic RNA through an in vivo recombination, thus opening the way to reverse gene-tics in coronaviruses.","Coronavirus; Defective interfèrent RNA; Recombination; Replication; Transcription","virus RNA; Coronavirus; nonhuman; review; RNA synthesis; virus assembly; virus genome; virus recombination; virus replication","Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Baric, R.S., Stohlman, S.A., Lai, M.M., Characterization of replicative intermediate RNA of mouse hepatitis virus : Presence of leader RNA sequences on nascent chains (1993) J Virol, 48, pp. 633-640; Spaan, W.J., Delius, H., Skinner, M., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J, 2, pp. 1839-1844; Baker, S.C., Lai, M.M., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) £A 1BO J, 9, pp. 4173-4179; 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Kim, Y.N., Lai, M.M., Makino, S., Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing (1993) Virology, 194, pp. 244-253; Lin, Y.J., Lai, M.M., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J Virol, 67, pp. 6110-6118; Zhang, X., Lai, M.M., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA : Correlation with the amounts of Subgenomic mRNA transcribed (1995) J Virol, 69, pp. 1637-1644; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′ end of mouse hepatitis virus genomic RNA (1995) J Virol, 69, pp. 2016-2023; Yu, W., Leibowitz, J.L., A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology, 214, pp. 128-138; Hsue, B., Masters, P.S., A bulged stem-loop structure in the 3′ untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J Virol, 71, pp. 7567-7578; Roux, L., Simon, A.E., Holland, J.J., Effects of defective interfering viruses on virus replication and pathogenesis in vitro and m vivo (1991) Adv VmisRes, 40, pp. 181-211; Vennema, H., Godeke, G.J., Rossen, J.W., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J, 15, pp. 2020-2028; Adami, C., Pooley, J., Glomb, J., Evolution of mouse hepatitis virus (MHV) durins chronic infection : Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Maeda, A., Hayashi, M., Ishida, K., Mizutani, T., Watanabe, T., Namioka, S., Characterization of DBT cell clones derived from cells persistently with the JHM strain of mouse hepatitis virus (1995) J Vet Med Sei, 57, pp. 813-817; Sawicki, S.G., Lu, J.H., Holmes, K.V., Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from the epigenetic expression of the MHV receptor (1995) J Virol, 69, pp. 5535-5543; Chen, W., Baric, R., Function of a 5'-end genomic RNA mutation that evolves during persistent mouse hepatitis virus infection m vitro (1995) J Virol, 69, pp. 7529-7540; Meyer, G., Thiel, H.J., Cytopathogenicity of classical fever virus caused by defective interfering particles (1995) J Virol, 69, pp. 3683-3689; Holland, J.J., Delatorre, J.C., Steinhauer, D.A., RNA virus populations as quasispecies (1992) Cnrr Top Microb Immuno, 176, pp. 1-20; Eigen, M., On the nature of virus quasispecies (1996) Trends Microb, 4, pp. 216-218; Morimoto, K., Craig, D., Hooper, D., Rabies virus quasispecies : Implication for pathogenis (1998) Proc Nail Acad Sei USA, 95, pp. 3152-3156; Kirkwood, T.B., Bangham, C.R., Cycles, chaos, and evolution in virus cultures : A model of defective interfering particles (1994) Proc Natl Acad Sei USA, 91, pp. 8685-8689; Morse, S.S., The virus of the future ? Emerging viruses and evolution (1994) The Evolutionary Biology of Viruses, pp. 325-335. , Morse SS, ed. Raven Press, Ltd, NY; Laude, H., Rasschaert, D., Dclmas, B., Eleouet, J.E., Le coronavirus respiratoire porcin PRCV : Un virus émergent pas comme les autres (1998) Virologie, 2, pp. 305-316; Fu, K., Baric, R.S., Map locations of mouse hepatitis virus temperaturesensitive mutants : Confirmation of variable rates of recombination (1994) J Virol, 68, pp. 7458-7466; Makino, S., Lai, M.M., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J Virol, 63, pp. 5285-5292; Brian, D.A., Spaan, W.J., Recombination and coronavirus defective interfering RNAs (1997) Seminars Virol, 8, pp. 101-111; Carpenter, C.D., Oh, J.W., Zhang, C., Simon, A.E., Involment of a stemloop structure in the location of junction sites in viral RNA recombination (1995) J Mol Biol, 245, pp. 608-622; White, A.K., Moris, T.J., RNA determinants of junction site selection in RNA virus recombinants and defective interfering RNAs (1995) RNA, 1, pp. 1029-1040; Nagy, P.D., Bujarski, J.J., Engineering of homologous recombination hotspots with AU-rich sequences in brome mosaic virus (1997) J Virol, 71, pp. 3799-3810; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J Virol, 66, pp. 1841-1848; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J Virol, 68, pp. 328-337; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J Virol, 69, pp. 5475-5484; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed e gene mutants of mouse hepatitis virus confirms a pivotal role for e protein in coronavirus assembly (1998) J Virol, 72, pp. 7885-7894; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targetted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59 : Q159 is a determinant of hepatotropism (1998) J Virol, 72, pp. 9628-9636","Pascalis, H.; INRA, Unité de Virologie Immunologie Moléculaire, 78350 Jouy-en-Josas, France",,,12678694,,VIROF,,"French","Virologie",Article,"Final",,Scopus,2-s2.0-0033378334
"Hasoksuz M., Lathrop S., Al-dubaib M.A., Lewis P., Saif L.J.","6603236044;36836780500;16067981200;56343303500;7102226747;","Antigenic variation among bovine enteric coronaviruses (BECV) and bovine respiratory coronaviruses (BRCV) detected using monoclonal antibodies",1999,"Archives of Virology","144","12",,"2441","2447",,25,"10.1007/s007050050656","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033394544&doi=10.1007%2fs007050050656&partnerID=40&md5=2942329855ea8ba32039f61ff25bfa1e","Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States; Veterinary Faculty, Department of Microbiology, Istanbul University, Istanbul, Turkey; Coll. of Agric. and Vet. Medicine, King Saud University, Burydah, Saudi Arabia; Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, 1680 Madison Avenue, Wooster, 44691-4096 OH, United States","Hasoksuz, M., Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Veterinary Faculty, Department of Microbiology, Istanbul University, Istanbul, Turkey; Lathrop, S., Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Veterinary Faculty, Department of Microbiology, Istanbul University, Istanbul, Turkey; Al-dubaib, M.A., Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Coll. of Agric. and Vet. Medicine, King Saud University, Burydah, Saudi Arabia; Lewis, P., Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States; Saif, L.J., Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, Wooster, OH, United States, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Ohio State University, 1680 Madison Avenue, Wooster, 44691-4096 OH, United States","Bovine coronavirus (BCV) causes neonatal calf diarrhea (CD) and is associated with winter dysentery (WD) in adult dairy cattle. It can also be isolated from the respiratory tracts of cattle entering feedlots. Monoclonal antibodies (MAbs) specific for the hemagglutinin esterase (HE) and spike (S) surface proteins of 2 bovine enteric coronavirus (BECV) strains and two bovine respiratory coronavirus (BRCV) strains were tested against 6 BECV strains and 6 recently isolated BRCV strains, in order to characterize the antigenicity of BCV strains with varied tissue tropisms. All MAbs had high immunofluorescence (IF) titers against BECV and BRCV strains, indicative of conserved cross-reactive epitopes. In hemagglutination inhibition (HI) tests, the S-MAbs were more broadly reactive than HE-MAbs. The BRCV and CD MAbs were more broadly reactive in HI than the WD MAbs. The HA activity of the Mebus vaccine CD strain was not inhibited by any of the MAbs tested. The HI activity of BRCV strain R6 was unique among the 6 BRCV isolates. In virus neutralization assays, MAbs to the BRCV strain R4 neutralized all 6 BECV strains tested. Antigenic variation exists among both BECV and BRCV strains, but it cannot be attributed soley to the clinical origin of the strain.",,"antibody specificity; assay; bovine enteric coronavirus; bovine respiratory coronavirus; epitope; hemagglutinin esterase; immunofluorescence; monoclonal antibody; spike surface protein; virus antigen; virus neutralization assay; Animals; Antibodies, Monoclonal; Antibody Specificity; Antigenic Variation; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Hemagglutination Inhibition Tests; Hemagglutinins, Viral; Membrane Glycoproteins; Neutralization Tests; Respiratory Tract Infections; Viral Envelope Proteins; Viral Fusion Proteins","Benfield, D.A., Saif, L.J., Cell culture propagation of coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoprotein E2 and E3: Demonstration of in vivo virus neutralizing activity (1989) J Gen Virol, 70, pp. 993-998; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; Hasoksuz, M., Lathrop, S., Gadfield, K., Saif, L.J., Isolation of bovine respiratory coronavirus from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronavirus (1999) Am J Vet Res, 60. , in press; Heckert, R.A., Saif, L.J., Myers, G.W., Agnes, A.G., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infection (1991) Am J Vet Res, 52, pp. 563-571; Kang, S.Y., Saif, L.J., Production and characterization of monoclonal antibodies against an avian group A rotavirus (1991) Avian Dis, 35, pp. 563-571; Lathrop, S.L., Wittum, T.E., Morley, P.S., Smith, D., Bingham, H., Saif, L.J., Bovine coronavirus respiratory infections in feedlot cattle (1996) Proceedings of the Conference of Research Workers in Animal Disease, , Chicago, IL, Poster 200; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-435; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variation among the Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Millane, G., Kourtesis, A.B., Dea, S., Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates (1997) J Clin Microbiol, 35, pp. 33-40; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronavirus from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence of an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990) Viral Diarrhea of Man and Animals, pp. 190-199. , Saif LJ,Theil KW (eds). CRC Press, Boca Raton; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-0-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am J Vet Res, 53, pp. 1253-1258; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentry of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Welch, S.K.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity with virulent and attenuated virus (1988) Arch Virol, 101, pp. 221-235; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine virulent and avirulent coronavirus: Sequence and functional comparison between strains (1991) Virology, 185, pp. 847-852","Saif, L.J.; Food Animal Health Research Program, Dept. of Veterinary Preventive Med., Ohio State University, 1680 Madison Avenue, Wooster, OH 44691-4096, United States",,,03048608,,ARVID,"10664396","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033394544
"István K., Sándor K., János T., Klingeborn B.S., Sándor B.","6603849862;6603764465;6603437628;35611673800;56248472000;","Data regarding the molecular biology of feline coronaviruses [Adatok a macska coronavirusainak molekuláris biológiájához]",1999,"Magyar Allatorvosok Lapja","121","5",,"292","297",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347239504&partnerID=40&md5=cde806378bdfc56c3aa3dac9068ea7df","Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; Department of Virology, National Veterinary Institute, Biomedical Center, S-751-23, Uppsala, Sweden","István, K., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; Sándor, K., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; János, T., Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary; Klingeborn, B.S., Department of Virology, National Veterinary Institute, Biomedical Center, S-751-23, Uppsala, Sweden; Sándor, B., Department of Virology, National Veterinary Institute, Biomedical Center, S-751-23, Uppsala, Sweden","The authors give a short review on contemporary knowledge about the molecular biology of feline coronaviruses. Particular attention is paid to the connection between feline enteric coronaviruses (FECV) and feline infectious peritonitis viruses (FIPV). FIP is a leading infectious cause of death among young cats, and occurs worldwide. The disease has a progressive immune-mediated pathogenesis. Diagnosis and control of the disease is difficult since serological investigations are not informative for this purpose, and neither treatment nor reliable vaccines are available at present. Based on in vitro neutralisation, the existence of two serotypes of feline coronaviruses has been shown. They differ mainly in their field prevalence and their in vitro growth characteristics. Feline coronaviruses were divided into two biotypes on the grounds of pathogenicity, i.e. FECV and FIP viruses. FECV may produce mild enteritis, but most infections remain subclinical. However, FECV presents a considerable health risk to cats because it is the precursor of FIPV. FECV can establish persistent infection in cats during natural infection. Asymptomatic FECV-infected carrier cats spread the infection to susceptible animals via the fecal-oral route. FIP viruses arise as a result of deletions and presumably mutations in the FECV genome during the intestinal replicative phase of infection. Deletions occur most specifically in the ORF3c region of the FECV genome. The intact ORF3c presumably suppresses the function of the virulence factor ORF7b in FECVs. However, in their changed FIPV counterparts, where the ORF3c is deleted or truncated, this suppression does not function, therefore the ORF7b may readily contribute to the invasion of the organism and to the development of FIP. In experimentally infected cats, the authors found that the persisting FECV forms in the large intestine a quasi-species population the composition of which varies with tune. The changes affect the structural-protein coding regions of the viruses. Having entered the different organs, this variability is markedly reduced, which is probably due to strong selection. Furthermore, since some of the detected viruses were partly or entirely lacking ORF7b, the existence of other virulence factors cannot be excluded. Thus, the incidence of FIP in a cat population is not the result of the circulation of certain FIP viruses, but rather it is in strict correlation with the mutation rate of FECV to FIPV. Therefore, to learn the probability of occurrence of FIP viruses and the disease itself, it is recommended to monitor a population for the prevalence of the asymptomatic FECV carriers. We suggest using RT-PCR targeting one of the most conservative genomic regions for this purpose. However, the regions ORF3c and ORF7b that are presumably responsible for the evolution of FIP viruses should be also scrutinised in pathogenicity studies. Similarly, the molecular background of natural resistance of some cat breeding-lines against feline coronaviruses would be also well worth investigating.",,,"Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; De Groot, R.J., Ter Haar, R.J., Intracellular RNAs of the feline infectious peritonitis virus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , SIDDELL, S. G. (ed.): Plenum Press. New York; De Vries, A.A.F., Horzinek, M.C., The genome organization of the Nidovirales: Similarities and differences between Arteri-, Toro-, and Coronaviruses (1997) Seminars Virol., 8, pp. 33-47; Evermann, J.F., Mckeirnan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Vet. Microbiol., 28, pp. 243-255; Foley, J.F., Poland, A., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) J. Am. Vet. Med. Ass., 210, pp. 1313-1318; Herrewegh, A.A.P.M., Vennema, H., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 662-1631; Herrewegh, A.A.P.M., Mähler, M., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 214, pp. 349-363; Herrewegh, A.A.P.M., Smeek, I., Feline coronavirus type II strains 79-1638 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Gen. Virol., 79, pp. 4508-4514; Hickman, M.A., Morris, J.G., Elimination of feline coronavirus infection from a large experimental specific pathogen-free cat breeding colony by serologic testing and isolation (1995) Feline Pract., 23, pp. 96-102; Keck, J.G., Matsushima, G.K., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Kiss, I., Ballagi-Pordány, A., Kecskeméti, S., Matiz, K., Tanyi, J., Klingeborn, B.S., Belák, S., Városi macskák coronavirus fertozöttsége (1998) Magy. Állatorv. Lapja, 120, pp. 655-658; Kiss, I., Kecskeméti, S., Tanyi, J., Klingeborn, B.S., Belák, S., Studies on the Invasion and Distribution of Feline Coronaviruses in Naturally and Experimentally Infected Cats, , közlésre benyújtva; Kusters, J.G., Jager, E.J., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, pp. 605-608; Lai, M.M.C., Baric, R.C., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Lai, M.M.C., Genetic recombination in RNA viruses (1992) Curr. Top. Microbiol. Immunol., 176, pp. 21-32; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Seminars Virol., 7, pp. 381-388; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus. Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , SIDDELL, S. G. (ed.): Plenum Press. New York; Mckeirnan, A.J., Evermann, J.F., Isolation of feline coronavirus from two cats with diverse disease manifestations (1981) Feline Pract., 11, pp. 16-20; Mckeirnan, A.J., Evermann, J.F., Comparative properties of feline coronaviruses in vitro (1987) Can. J. Vet. Res., 51, pp. 212-216; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-37; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., Evermann, J.F., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) Am. J. Vet. Res., 45, pp. 2580-2585; Stoddart, M.E., Gaskell, C.J., Feline coronavirus infection (1985) Feline Medicine and Therapeutics, pp. 284-289. , CHANDLER, E. A. et al. (eds): Blackwell Scientific Publications. Oxford; Vennema, H., Rossen, W.A., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Vennema, H., Poland, A., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157","István, K.; Debreceni Allat-egeszsegugyi Intezet, Pf. 51, H-4002 Debrecen, Hungary",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Article,"Final",,Scopus,2-s2.0-0347239504
"Tråvén M., Carlsson U., Lundén A., Larsson B.","6603563444;7006147810;7005154912;7202678840;","Serum Antibodies to Bovine Coronavirus in Swedish Sheep",1999,"Acta Veterinaria Scandinavica","40","1",,"69","74",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032610683&partnerID=40&md5=5cb6ac7970390cc5d4c5afad12583d13","Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, Uppsala, Sweden; Dept. of Veterinary Microbiology, Section of Parasitology, Swed. Univ. of Agricultural Sciences, Uppsala, Sweden; Swedish Board of Agriculture, Jönköping, Sweden; Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, P.O. Box 7019, S-750 07 Uppsala, Sweden","Tråvén, M., Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, Uppsala, Sweden, Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, P.O. Box 7019, S-750 07 Uppsala, Sweden; Carlsson, U., Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, Uppsala, Sweden; Lundén, A., Dept. of Veterinary Microbiology, Section of Parasitology, Swed. Univ. of Agricultural Sciences, Uppsala, Sweden; Larsson, B., Swedish Board of Agriculture, Jönköping, Sweden","Altogether 218 sheep sera from 40 flocks in different parts of Sweden were screened for antibodies to bovine coronavirus (BCV). Nineteen per cent of the sera were positive and there was a significantly higher frequency (p<0.05) of at least one positive sample in flocks with more than 100 adult sheep than in smaller flocks. There was also a significantly higher frequency (p<0.001) of positive samples from sheep older than 4 years than from younger ones. Only a weak relationship between BCV positivity (2 or more positive samples, p<0.05) and cattle contact was demonstrated in this study. Possible transmission routes and other factors that could have affected the result are discussed. In light of our finding that all 5 sheep experimentally exposed to BCV through contact with infectious cow facces seroconverted, we conclude that the antibodies found in Swedish sheep are probably the result of BCV infections directly or indirectly transmitted from cattle.","Age; Cattle contact; Experimental infection; Flock size; Seroconversion; Survey","virus antibody; age; animal; animal disease; article; blood; cattle; Coronavirus; disease transmission; enzyme linked immunosorbent assay; epidemiology; feces; female; immunology; male; sheep; sheep disease; Sweden; virology; virus infection; Age Factors; Animals; Antibodies, Viral; Cattle; Coronavirus Infections; Coronavirus, Bovine; Enzyme-Linked Immunosorbent Assay; Feces; Female; Male; Seroepidemiologic Studies; Sheep; Sheep Diseases; Sweden","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet. Scand., 32, pp. 163-170; Carlsson, U., Border disease in sheep caused by transmission of virus from cattle persistently infected with bovine virus diarrhoea virus (1991) Vet. Rec., 128, pp. 145-147; Carlsson, U., Belák, K., Border disease virus transmitted to sheep and cattle by a persistently infected ewe: Epidemiology and control (1994) Acta Vet. Scand., 35, pp. 79-88; Chengping, L., (1985) Isolierung, Charakterisierung und Epizootiologic Boviner Coronaviren. (Isolation, Characterization and Epidemiology of Bovine Coronavirus.), , Vet. Med. Thesis, University of München, In German; Durham, P.J.K., Stevenson, B.J., Farquharson, B.C., Rotavirus and coronavirus associated diarrhoea in domestic animals (1979) N. Z. Vet. J., 27, pp. 30-32; Elvander, M., Severe respiratory disease in dairy cows caused by infection with bovine respiratory syncytial virus (1996) Vet. Rec., 138, pp. 101-105; Hedström, H., Isaksson, A., Epizootic enteritis in cattle in Sweden (1951) Cornell Vet., 42, pp. 251-253; Liebermann, H.V., Hille, G., Herold, M., Coronavirus infections of sheep (1986) Monatshefte Vet.-Med., 41, pp. 814-815; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet. Microbiol., 9, pp. 425-434; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet. Path., 10, pp. 45-64; Möstl, K.V., Bürki, F., Bovine coronavirus in calf respiratory disease - Pathological and immunological considerations (1987) Dt. Tierärztl. Wschr., 95, pp. 19-22. , In German; Nagy, B., Nagy, G., Pálfi, V., Bozsó, M., Occurence of cryptosporidia, rotavirus, coronavirus-like particles and K99+ Escherichia Coli in goat kids and lambs (1983) Proc. 3rd Int. Symp. Vet. Lab. Diagn., 2, pp. 525-531. , Ames, Iowa, USA; Reinhardt, G., Zamora, J., Tadich, N., Polette, M., Aguilar, M., Riedemann, S., Palisson, J., Diagnosis of coronavirus in sheep in Valdivia province, X region, Chile (1995) Archos Med. Vet., 27, pp. 129-132. , Chile; Roberts, S.J., Winter dysentery in dairy cattle (1957) Cornell Vet., 47, pp. 372-388; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet., 80, pp. 303-311; Sato, K., Inaba, Y., Miura, Y., Tokuhisa, S., Akashi, H., Shinozaki, T., Matumoto, M., Neutralizing antibody to calf diarrhea coronavirus in various animal species in Japan (1981) Microbiol. Immunol., 25, pp. 623-625; Snodgrass, D., Herring, J., Reid, H., Scott, F., Gray, E., Virus infections in cattle and sheep in Scotland 1975-1978 (1980) Vet. Rec., 106, pp. 193-195; Stair, E.L., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1912) Am. J. Vet. Res., 33, pp. 1147-1156; Thomas, L.H., Gourlay, R.N., Stott, E.J., Howard, C.J., Bridger, J.C., A search for new microorganisms in calf pneumonia by the inoculation of gnotobiotic calves (1982) Res. Vet. Sci., 33, pp. 170-182; Tråvén, M., Björnerot, L., Larsson, B., Nation-wide survey of antibodies to bovine coronavirus in Swedish dairy herd bulk milk Vet. Rec., , in press; Tråvén, M., Sundberg, J., Larsson, B., Niskanen, R., Winter dysentery diagnosed by farmers in dairy herds in central Sweden: Incidence, clinical signs and protective immunity (1993) Vet. Rec., 133, pp. 315-318; Tzipori, S., Smith, M., Makin, M.T., McCaughan, C., Enteric coronavirus-like particles in sheep (1978) Austr. Vet. J., 54, pp. 320-321; White, M.E., Schukken, Y.H., Tanksley, B., Space-time clustering of, and risk factors for, farmer-diagnosed winter dysentery in dairy cattle (1989) Can. Vet. J., 30, pp. 948-951","Tråvén, M.; Dept. Ruminant Med. Vet. Epidemiol., Section of Ruminant Medicine, P.O. Box 7019, S-750 07 Uppsala, Sweden; email: madelein.traven@idmed.slu.se",,,0044605X,,AVSCA,"10418197","English","Acta Vet. Scand.",Article,"Final",,Scopus,2-s2.0-0032610683
"Vilmos P.","7003472044;","Winter dysentery in dairy cattle herds caused by bovine coronavirus [Coronavirus okozta, ún. téli hasmenés elofordulása szarvasmarha-állományainkban]",1999,"Magyar Allatorvosok Lapja","121","12",,"733","739",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346909299&partnerID=40&md5=d37e4462cbfc4b19ed36f5c35c4a7e3e","Orszagos Allat-egeszsegugyi Intezet, Tábornok u. 2, H-1149 Budapest, Hungary","Vilmos, P., Orszagos Allat-egeszsegugyi Intezet, Tábornok u. 2, H-1149 Budapest, Hungary","During late winter and early spring in 1997 and 1998, an epizootic diarrhea prevailed among cattle over six months in dairy herds of two regions of Hungary. The disorder showed marked resemblance to the disease literally named 'winter dysentery' that is caused by Bovine Coronavirus (BCV). This disease had never been diagnosed in Hungary before. Investigations were carried out on 4 large and 7 small scale farms. The disease spread very quickly both among and within herds with a sudden onset of symptoms in affected herds. On large scale farms, the infection progressed in 3-4 days and appeared on animals kept in other buildings in 1-2 weeks. In large herds the morbidity was 80 per cent, while in small farms it could reach 100%. The affected animals showed anorexia and fever followed by a watery diarrhea, that became bloody or blood-stripped after 2-3 days. In milking cows, milk production decreased by 50-100 per cent, i.e. there was an overall decrease in excess of 50 per cent at farm level. The severity of symptoms decreased after about 5-6 days with the gradual disappearance of the diarrhea. Milk production returned to normal in 2-4 weeks depending on the size of the herd. In a large herd, losses were between 110-750 liter milk daily during the phase of diarrhea, totaling over 3000 USD. In another herd, the number of cows observed to be in heat decreased from the normal 6,3 to 2,9 per day during the course of the disease. Fecal and blood samples were sent for laboratory investigation from the affected farms. Feces and paired blood samples were tested from 5 herds showing acute symptoms. BCV was detected in feces samples from all five herds, however, only 22 out of 43 samples were positive with a direct ELISA method. Since blood samples were taken at the onset of infection, only three of these 22 BCV positive were positive for BCV antibodies by the HAI method. However, sero-conversion or rising titers specific to BCV were demonstrated in 39 of the 48 paired blood samples. HAI titers of 1:32-≥ 512 were found in 37 of the 40 reconvalescent sera from a total of 7 herds. These results indicate the causative role of BCV in epizootic diarrhea of adult cattle in Hungary.",,,"Akashi, H.Y., Inaba, Y., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet. Microbiol., 5, pp. 265-276; Alenius, S.N., Juntti, R., Epizootic diarrhea (winter dysentery) of dairy cattle in Sweden caused by bovine coronavirus (1988) XV. Congresso Mundial de Buiatria. Palma de Mallorca, 2, pp. 1505-1506; Alenius, S., Niskanen, R., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet. Scand., 32, pp. 163-170; Barber, D.M.L., Nettleton, P.F., Herring, J.A., Disease in a dairy herd associated with the introduction and spread of bovine virus diarrhoea virus (1985) Vet Rec., 117, pp. 459-464; Charton, A., Faye, P., Etude clinique et 7xpérimentale dune entérite hémorragique des bovins associée á la présence dans le tube digestif d'un ultravirus pathogéne (1963) Rec. Méd. Vét., 139, pp. 897-908; Crouch, C.F., Acres, S.D., Prevalence of rotavirus and coronavirus antigens in feces of normal cows (1984) Can. J. Comp. Med., 48, pp. 340-342; Collins, J.K., Riegel, C.A., Shedding of enteric coronavirus in adult cattle (1987) Am. J.Vet. Res., 48, pp. 361-365; Edwards, M.J., Sier, A.M., Bovine epizootic diarrhea in western Australia (1960) Aust. Vet. J., 36, pp. 402-404; Espinasse, J., Viso, M., Winter dysentery: A coronavirus-like agent in the feces of beef and dairy cattle with diarrhea (1982) Vet. Rec., 110, p. 385; Fox, F.H., (1980) Bovine Medicine and Surgery. 2nd Edition, , AMSSTUTZ, H. E. (ed.): Am. Vet. Publ. Inc. Santa Barbara, California, USA; Hedstrom, H., Isaksson, A., Epizootic enteritis in cattle in Sweden (1951) Cornell Vet., 47, pp. 251-253; Horner, G.W., Hunter, R., Kirkbridge, C.A., A coronavirus like agent present in faeces of cows with diarrhea (1976) N. Z. Vet. J., 23, p. 98; Jactel, B., Espinasse, J., An epidemiological study of winter dysentery in fifteen herds in France (1990) Vet. Res. Comm., 74, pp. 367-379; Jones, F.S., Little, R.B., The etiology of infectious diarhhea (winter scours) in cattle (1931) J. Exp. Med., 53, pp. 835-843; Komarov, A., Goldsmit, L., Isolation of a viral agent from winter dysentery of cattle (1959) Refu. Vet., 16, pp. 149-152; Macpherson, L.V., Bovine virus enteritis (winter dysentery) (1957) Can. J. Comp. Med., 21, pp. 184-192; Mcnulty, M., Bryson, D.A., Coronavirus infection of the bovine respiratory tract (1984) Vet. Microbiol., 9, pp. 425-434; Mebus, C.A., Star, E.L., Neonatal calf diarrhea propagation, attenuation and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Nagy, B., Bozsó, M., Coronavirusok hasmenéses borjakban (1983) Magy. Állatorv. Lapja, 38, pp. 717-718; Pinto, G.B., Hawkes, P., Viral antibodies in bovine fetuses in Argentina (1993) Res. Vet. Sci., 55, pp. 385-388; Reynolds, D.J., Debney, T.G., Studies on the relationship between coronaviruses from the intestinal and respiratory tract of calves (1985) Arch. Virol., 85, pp. 71-83; Rollison, D.H.L., Infectious diarrhoea of dairy cows (1948) Vet. Rec., 60, pp. 191-192; Saif, L.J., Redman, D.R., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet. Rec., 123, pp. 300-301; Sato, K., Inaba, Y., Hemagglutination by calf diarrheacoronavirus (1977) Vet. Microbiol., 2, pp. 83-87; Sato, K., Inaba, Y., Neutralizing antibody to calfdiarrhea coronavirus in various animal species in Japan (1981) Microbiol. Immunol., 25, pp. 623-625; Smith, D.R., Fedorka-Cray, P.J., Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle (1998) Am. J. Vet. Res., 59, pp. 994-1001; Traven, M., Silvan, A., Experimental infection with bovine coronavirus (BCV) in lactating cows: Clinical disease, viral excretion, interpheron-alpha and antibody response (1995) Bovine Pract., 29, pp. 64-65; Tsunimetsu, H., El Kanawaki, R., Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J. Clin. Microbiol., 33, pp. 3264-3269; Van Kruiningen, H.J., Hiesand, L., Winter dysentery in dairy cattle: Recent findings (1985) Comp. Cont. Educ. Pract. Vet., 7, pp. 591-598","Vilmos, P.; Orszagos Allat-egeszsegugyi Intezet, Tábornok u. 2, H-1149 Budapest, Hungary; email: vilmos_palfi@oai.hu",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Article,"Final",,Scopus,2-s2.0-0346909299
"Pewe L., Heard S.B., Bergmann C., Dailey M.O., Perlman S.","6603143496;7103177569;35449739000;7005838815;7102708317;","Selection of CTL escape mutants in mice infected with a neurotropic coronavirus: Quantitative estimate of TCR diversity in the infected central nervous system",1999,"Journal of Immunology","163","11",,"6106","6113",,42,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033485955&partnerID=40&md5=3fadb7e05ac1c66f7db39a7eefdbae1d","Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Biological Sciences, University of Iowa, Iowa City, IA 52242, United States; Department of Pathology, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Dept. Interdisc. Prog. in Immunol., University of Iowa, Iowa City, IA 52242, United States; Dept. Neurol. Molec. Microbiol. I., University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Pewe, L., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Heard, S.B., Department of Biological Sciences, University of Iowa, Iowa City, IA 52242, United States; Bergmann, C., Dept. Neurol. Molec. Microbiol. I., University of Southern California, School of Medicine, Los Angeles, CA 90033, United States; Dailey, M.O., Department of Pathology, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Dept. Interdisc. Prog. in Immunol., University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Dept. Interdisc. Prog. in Immunol., University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Variant viruses mutated in the immunodominant cytotoxic T cell epitope surface (S) glycoprotein S-510-518 are selected in mice chronically infected with mouse hepatitis virus, strain JHM. We determined whether this selection occurred in the presence of an oligoclonal or polyclonal T cell response using soluble MHC/peptide tetramers in direct ex vivo analyses of CNS-derived lymphocytes. A total of 42% (range, 29-60%) of CD8 T cells in the CNS of mice with acute encephalitis recognized epitope S-510-518. A total of 34% (range, 18-62%) of cells from mice with hind limb paralysis (and chronic demyelination) were also epitope specific, even though only virus expressing mutated epitope is detected in these animals. Sequence analysis of the β- chain CDR3 of 487 tetramer S-510-518-positive cDNA clones from nine mice showed that a majority of clonotypes were identified in more than one mouse. From these analyses, we estimated that 300-500 different CD8 T cell clonotypes responsive to epitope S-510-518 were present in each acutely infected brain, while 100-900 were present in the CNS of each mouse with chronic disease. In conclusion, a polyclonal CD8 T cell response to an epitope does not preclude the selection of T cell escape mutants, and epitope-specific T cells are still present at high levels even after RNA- encoding wild-type sequence is no longer detectable.",,"cell surface protein; epitope; t lymphocyte receptor; adolescent; animal cell; animal model; antigenic variation; article; cellular immunity; central nervous system infection; controlled study; coronavirus; cytotoxic t lymphocyte; demyelination; mouse; nonhuman; priority journal; receptor density; t lymphocyte subpopulation; virus infection; virus mutant; Acute Disease; Animals; Chronic Disease; Coronavirus Infections; Demyelinating Diseases; Encephalitis, Viral; Genes, T-Cell Receptor beta; Immunodominant Epitopes; Immunoglobulin Variable Region; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Paralysis; Receptors, Antigen, T-Cell; T-Lymphocytes, Cytotoxic; Variation (Genetics); Viral Envelope Proteins","Zinkernagel, R.M., Immunology taught by viruses (1996) Science, 271, p. 173; Stohlman, S.A., Bergmann, C.C., Perlman, S., Persistent infection by mouse hepatitis virus (1998) Persistent Viral Infections, p. 537. , R. 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Med., 188, p. 2205; Steven, N.M., Leese, N.E., Annels, S.P., Rickinson, A.B., Epitope focusing in the primary cytotoxic T cell response to Epstein-Barr virus and its relationship to memory (1996) J. Exp. Med., 184, p. 1801; Ishikawa, T., Kono, D., Chung, J., Fowler, P., Theofilopouos, A., Kakumu, S., Chisari V., F., Polyclonality and multispecificity of the CTL response to a single viral epitope (1998) J. Immunol., 161, p. 5843. , V; Weiner, A., Erickson, A., Kanospon, J., Crawford, K., Muchmore, E., Hughes, A., Houghton, M., Walker, C.M., Persistent hepatitis C virus infection in a chimpanzee is associated with emergence of a cytotoxic T lymphocyte escape variant (1995) Proc. Natl. Acad. Sci. USA, 92, p. 2755; Knopf, P.M., Harling-Berg, C.J., Cserr, H.F., Basu, D., Sirulnick, E., Nolan, S., Park, J., Hickey, W.F., Antigen-dependent intrathecal antibody synthesis in the normal rat brain: Tissue entry and local retention of antigen-specific B cells (1998) J. Immunol., 161, p. 692; Pannetier, C., Evan, J., Kourilsky, P., T-cell repertoire diversity and clonal expansion in normal and clinical samples (1995) Immunol. Today, 16, p. 176; Maryanski, J., Jongeneel, C., Bucher, P., Casanova, J.-L., Walker, P., Single-cell PCR analysis of TCR repertoires selected by antigen in vivo: A high magnitude CD8 response is comprised of very few clones (1996) Immunity, 4, p. 47; Naumov, Y.N., Hogan, K.T., Naumova, E.N., Pagel, J.T., Gorski, J., A class I MHC-restricted recall response to a viral peptide is highly polyclonal despite stringent CDR3 selection: Implications for establishing memory T cell repertoires in ""real world"" conditions (1998) J. Immunol., 160, p. 2842; Lehner, P., Wang, E.C., Moss, P.A., Williams, S., Platt, K., Friedmar, E.M., Bell, J.I., Borysiewicz, Human HLA-A0201-restricted cytotoxic T lymphocyte recognition of influenza a is dominated by T cells bearing the Vβ1'7 gene segment (1993) J. Exp. Med., 181, p. 79; Bousso, P., Casrouge, A., Altman, J.D., Haury, M., Kanellopoulos, J., Abastado, J.-P., Kourilsky, P., Individual variations in the murine T cell response to a specific peptide reflect variability in naive repertoires (1998) Immunity, 9, p. 169; Butz, E.A., Bevan, M.J., Massive expansion of antigen-specific CD8+ T cells during an acute virus infection (1998) Immunity, 8, p. 167","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,00221767,,JOIMA,"10570300","English","J. Immunol.",Article,"Final",,Scopus,2-s2.0-0033485955
"Macfarlane J., Holmes W., Rose D., Weston V.B., Leinonen M., Saikku P., Myint S., Gard P., Macfarlane R.","7201418190;13302597900;7401709610;15074177200;21534996000;7005686722;35479862600;7003546441;7101956481;","Direct and indirect evidence of infection in previously well adults consulting with Lower Respiratory Tract illness (LRTi): A prospective study in primary care",1999,"Thorax","54","SUPPL. 3",,"","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-33751372477&partnerID=40&md5=c63e82f5aa2f529dc1c6316684f735fe","Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom","Macfarlane, J., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Holmes, W., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Rose, D., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Weston, V.B., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Leinonen, M., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Saikku, P., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Myint, S., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Gard, P., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom; Macfarlane, R., Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom","LRTi and acute bronchitis in previously well adults are normally regarded as being viral. We investigated in detail 316 previously well adults consulting their GP with LRTi over the winter period. Viral and bacterial throat swabs, sputum, acute and follow-up serology were obtained in nearly all patients and tested for bacterial, viral and atypical pathogens, using a range of cultural, serological and molecular biological techniques. CXrays were obtained in 92%. Pathogens were identified in 173 patients (55%), of whom 130 had one pathogen, 39 had two, and 4 had time pathogens. Bacterial pathogens found in 82 patients included S.pneumoniae (54) H.influenzae (31) and M.catarrhalis (7). Atypical pathogens in 75 included C.pneumoniae in 55 and M.pneumoniae in 23. Viral pathogens in 61 included influenza A (23), coronavirus (16), rhinovirus (13), influenza B (4), RSV (3) and adenovirus in 2. Twenty-five percent of patients had indirect evidence of infection: CXray changes consistent with infection and/or CRP of =/> 50mg/litre. There was a significant relationship between raised CRP and CXray infection changes. Both of these factors were significantly commoner in those in whom bacterial and/or atypical pathogens had been identified. However, we report elsewhere that outcome was not related to direct or indirect evidence of infection. Conclusion: LRTi in previously well adults is associated with infection in over half of cases, most commonly bacterial and atypical pathogens. However, we also find outcome is not influenced by aetiology.",,,,"Respiratory Infection Group, c/o Nottingham City Hospital, NG5 1PB, United Kingdom",,,00406376,,THORA,,"English","Thorax",Article,"Final",,Scopus,2-s2.0-33751372477
"Pitkäranta A., Nokso-Koivisto J., Jäntti V., Takala A., Kilpi T., Hovi T.","7003331729;6602762108;7006756048;7005326859;7003727621;36152793900;","Lowered yields of virus-induced interferon production in leukocyte cultures and risk of recurrent respiratory infections in children",1999,"Journal of Clinical Virology","14","3",,"199","205",,18,"10.1016/S1386-6532(99)00056-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345148879&doi=10.1016%2fS1386-6532%2899%2900056-6&partnerID=40&md5=b78c1bd5061586cbd9d0108d7abd2bb4","Department of Otorhinolaryngology, Univ. Helsinki, PL 220, 00029 HYKS, Helsinki, Finland; Department of Virology, Natl. Pub. Hlth. Inst., M., Helsinki, Finland; Department of Vaccines, Natl. Pub. Hlth. Inst., M., Helsinki, Finland","Pitkäranta, A., Department of Otorhinolaryngology, Univ. Helsinki, PL 220, 00029 HYKS, Helsinki, Finland; Nokso-Koivisto, J., Department of Otorhinolaryngology, Univ. Helsinki, PL 220, 00029 HYKS, Helsinki, Finland, Department of Virology, Natl. Pub. Hlth. Inst., M., Helsinki, Finland; Jäntti, V., Department of Virology, Natl. Pub. Hlth. Inst., M., Helsinki, Finland; Takala, A., Department of Vaccines, Natl. Pub. Hlth. Inst., M., Helsinki, Finland; Kilpi, T., Department of Vaccines, Natl. Pub. Hlth. Inst., M., Helsinki, Finland; Hovi, T., Department of Virology, Natl. Pub. Hlth. Inst., M., Helsinki, Finland","Objective: To study the correlation between the yield of virus-induced interferon (IFN) production in leukocyte cultures and the risk of recurrent respiratory infections. Methods: A sample of 71 consecutive children enrolled in the Finnish Otitis Media Cohort Study were selected. Children suffering from frequently recurring respiratory infections (FRRIs) were defined as the highest quintile of the entire cohort of 329 children, as regards the number of upper respiratory infections (URIs) and/or episodes of acute otitis media (AOM) during the follow-up period from 2 to 24 months. Results: In the sample of 71 children, there were 18 children with FRRI (≥9 URI and/or ≥4 AOM). Leukocyte cultures, prepared from blood drawn from these 18 children at 6 months of age, produced lower yields of IFN than those of the remaining 53 children, when stimulated with adenovirus (P<0.001), coronavirus (P<0.001) or rhinovirus (P=0.002). The difference in IFN yields was even greater (P<0.001 with all three viruses) if the comparison was made between children with FRRI and those with no or maximally one URI during the follow-up period. When the IFN production capacity induced by rhinovirus was measured at the age of 24 months, a statistically significant difference between the children with FRRI and the others was also seen (P=0.002). Influenza A virus-induced IFN production capacity did not differ between the groups at either age (P=0.209). Conclusions: Lowered IFN responses in children suffering from recurrent URIs and/or AOM may, in a subgroup of the children, be due to a genetic property of the child. However, because of the great interindividual variations, we cannot use the IFN production capacity as such for prediction of forthcoming respiratory infections and/or otitis media. Copyright (C) 1999 Elsevier Science B.V.","Child; Interferon; Otitis media; Respiratory infection; Virus","interferon; adenovirus; article; child; controlled study; coronavirus; drug response; female; follow up; genetic predisposition; human; infant; influenza virus a; interferon production; leukocyte; major clinical study; male; otitis media; priority journal; recurrent infection; respiratory tract infection; rhinovirus; Adenoviruses, Human; Cells, Cultured; Child, Preschool; Coronavirus; Female; Humans; Infant; Influenza A virus; Interferons; Leukocytes, Mononuclear; Male; Otitis Media; Prospective Studies; Recurrence; Respiratory Tract Infections; Rhinovirus; Risk Factors; Viruses","Bondestam, M., Alm, G.V., Foucard, T., Interferon production in children with undue susceptibility to infections (1984) Acta Paediatr. Scand., 73, pp. 197-202; Isaacs, D., Clarke, J.R., Tyrrel, D.A., Webster, A.D.B., Valman, H.B., Deficient production of leukocyte interferon (interferon-α) in vitro and in vivo in children with recurrent respiratory tract infections (1981) Lancet, 31, pp. 950-952; Karma, P., Palva, T., Kouvalainen, K., Kärjä, J., Mäkelä, P.H., Prinssi, V.P., Finnish approach to the treatment of acute otitis media. Report of the Finnish concensus conference (1987) Ann. Otol. Rhinol. Laryngol, 96 (SUPPL.), pp. 1-19; Katschinski, D.M., Neustock, P., Kluter, H., Kirchner, H., Influence of various factors on interferon-α production in culture of human leukocytes (1994) J. Interferon Res., 14, pp. 105-110; Kornman, K.S., Crane, A., Wang, H.-Y., The interleukin-1 genotype as a severity factor in adult periodontal disease (1997) J. Clin. Periodontol., 24, pp. 72-77; Lyall, E.G.H., Eden, O.B., Dixon, R., Sutherland, R., Thomson, A., Assessment of a clinical scoring system for detection of immunodeficiency in children with recurrent infections (1991) Pediatr. Infect. Dis. J., 10, pp. 673-676; McGuire, W., Hill, A.V.S., Allsop, C.E.M., Greenwood, B.M., Kwiatkowski, D., Variation in the TNF-a promoter region associated with susceptibility to cerebral malaria (1994) Nature, 371, pp. 508-511; Muller, U., Steinhoff, U., Reis, L.F.L., Hemmi, S., Pavlovic, J., Zinkernagel, R.M., Functional role of type I and type II interferons in antiviral defense (1994) Science, 264, pp. 1918-1921; Neustock, P., Kruse, A., Bock, S., St. Pierre, B., Kirchner, H., Deficient interferon-alpha response of newborn in comparison to adults (1993) Lymphokine Cytokine Res., 12, pp. 109-114; Pitkäranta, A., Linnavuori, K., Hovi, T., Virus-induced interferon production in human leukocytes: A low responder to one virus can be a high responder to another virus (1991) J. Interferon Res., 11, pp. 17-23; Pitkäranta, A., Karma, P., Hovi, T., Deficiency in interferon production by leukocytes from children with recurrent respiratory infections (1993) Clin. Diagn. Virol., 1, pp. 101-108; Pitkäranta, A., Karma, P., Hovi, T., Virus-induced interferon production in leukocyte cultures from children with recurrent respiratory infections. A follow-up study (1996) Clin. Diagn. Virol., 6, pp. 11-16; Stuber, F., Petersen, M., Bokelmann, F., Schade, U., A genomic polymorphism within the tumor necrosis factor locus influences plasma tumor necrosis factor-a concentrations and outcome of patients with severe sepsis (1996) Crit. Care Med., 24, pp. 381-384; Tupasi, T.E., De Leon, L.E., Lupisan, S., Torres, C.U., Leonor, Z.A., Sunico, M.E.S., Community-based studies of acute respiratory tract infections in young children (1990) Rev. Infect. Dis., 12 (SUPPL. 8), pp. 940-S949; Vanecek, K., Lehovcova, A., Interferon production in children with respiratory diseases (1985) Acta Paediatr. Scand., 74, pp. 118-121; Westbom, L., Kornfält, R., Chronic illness among children in a total population. An epidemiological study in a Swedish primary health care district (1987) Scand. J. Soc. Med., 15, pp. 87-97; Westendorp, R.G.J., Langermans, J.A.M., Huizinga, T.W.J., Genetic influence on cytokine production and fatal meningococcal disease (1997) Lancet, 349, pp. 170-173","Pitkaranta, A.; Department of Otorhinolaryngology, University of Helsinki, 00029 HYKS, Helsinki, Finland; email: anne.pitkaranta@helsinki.fi",,,13866532,,JCVIF,"10614857","English","J. Clin. Virol.",Article,"Final",,Scopus,2-s2.0-0345148879
"Wang Y., Zhang X.","7601495525;55715175900;","The nucleocapsid protein of coronavirus mouse hepatitis virus interacts with the cellular heterogeneous nuclear ribonucleoprotein A1 in vitro and in vivo",1999,"Virology","265","1",,"96","109",,51,"10.1006/viro.1999.0025","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033527903&doi=10.1006%2fviro.1999.0025&partnerID=40&md5=f4b1ca775a4df8512ffc6f333406fa1f","Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States","Wang, Y., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Zhang, X., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States","The nucleocapsid (N) protein of mouse hepatitis virus (MHV) and the cellular heterogeneous nuclear ribonucleoprotein A1 (hnRNP-A1) are RNA- binding proteins, binding to the leader RNA and the intergenic sequence of MHV negative-strand template RNAs, respectively. Previous studies have suggested a role for both N and hnRNP-A1 proteins in MHV RNA synthesis. However, it is not known whether the two proteins can interact with each other. Here we employed a series of methods to determine their interactions both in vitro and in vivo. Both N and hnRNP-A1 genes were cloned and expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins, and their interactions were determined with a GST-binding assay. Results showed that N protein directly and specifically interacted with hnRNP-A1 in vitro. To dissect the protein-binding domain on the N protein, 15 deletion constructs were made by PCR and expressed as GST fusion proteins. Two hnRNP-A1-binding sites were identified on N protein: site A is located at amino acids 1 to 292 and site B at amino acids 392 to 455. In addition, we found that N protein interacted with itself and that the self-interacting domain coincided with site A but not with site B. Using a fluorescence double-staining technique, we showed that N protein colocalized with hnRNP-A1 in the cytoplasm, particularly in the perinuclear region, of MHV-infected cells, where viral RNA replication/transcription occurs. The N protein and hnRNP-A1 were coimmunoprecipitated from the lysates of MHV-infected cells either by an N- or by an hnRNP-A1-specific monoclonal antibody, indicating a physical interaction between N and hnRNP-A1 proteins. Furthermore, using the yeast two-hybrid system, we showed that N protein interacted with hnRNP-A1 in vivo. These results thus establish that MHV N protein interacts with hnRNP-A1 both in vitro and in vivo.",,"nucleocapsid protein; ribonucleoprotein; RNA binding protein; article; in vitro study; in vivo study; Murine hepatitis coronavirus; nonhuman; priority journal; protein domain; protein protein interaction; protein RNA binding; sequence analysis; Animalia; Coronavirus; Escherichia coli; Murinae; Murine hepatitis virus; RNA viruses","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1989) Current Protocols in Molecular Biology, , New York: Wiley; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. Virol., 62, pp. 4280-4287; Baric, R.S., Stohlman, S.A., Razavi, M.K., Lai, M.M.C., Characterization of leader-related small RNAs in coronavirus-infected cells: Further evidence for leader-primed mechanism of transcription (1985) Virus Res., 3, pp. 19-33; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′-end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Cartegni, L., Maconi, M., Morandi, E., Cobianchi, F., Riva, S., Biamonti, G., HnRNP-A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins (1996) J. Mol. Biol., 259, pp. 337-348; Compton, S.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., In vitro replication of mouse hepatitis virus strain A59 (1987) J. Virol., 61, pp. 1814-1820; Denison, M.R., Spaan, W.J.M., Van Der Meer, Y., Gibson, C.A., Sims, A.C., Prentice, E., Lu, X.T., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) J. Virol., 73, pp. 6862-6871; Dreyfuss, G., Matunis, M.J., Pinol-Roma, S., Burd, C.G., HnRNP proteins and the biogenesis of mRNA (1993) Annu. Rev. Biochem., 62, pp. 289-321; Fields, S., Song, O., A novel genetic system to detect protein-protein interactions (1989) Nature, 340, pp. 245-247; Fisher, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Flemming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM(MHV-4) virus (1983) Virology, 131, pp. 296-307; Furuya, T., Lai, M.M.C., Three different cellular proteins bind to the complementary sites on the 5′-end positive- And 3′-end negative-strands of mouse hepatitis virus RNA (1993) J. Virol., 67, pp. 7215-7222; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Lai, M.M.C., Cellular factors in the transcription and replication of viral RNA genomes: A parallel to DNA-dependent RNA transcription (1998) Virology, 244, pp. 1-12; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus-a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lai, M.M.C., Patton, C.D., Baric, R.S., Stohlman, S.A., The presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol., 46, pp. 1027-1033; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzyahdzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Li, H.-P., Zhang, X.M., Duncan, R., Comai, L., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9544-9549; Li, H.-P., Huang, P., Park, S., Lai, M.M.C., Polypyrimidine tract-binding protein binds to the leader RNA of mouse hepatitis virus and serves as a regulator of viral transcription (1999) J. Virol., 73, pp. 772-777; Liao, C.-L., Zhang, X.M., Lai, M.M.C., Coronavirus defective-interfering RNA as an expression vector: The generation of a pseudorecombinant mouse hepatitis virus expressing hemagglutinin-esterase (1995) Virology, 208, pp. 319-327; Makino, S., Lai, M.M.C., Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Arch. Virol., 125, pp. 141-160; McBride, A.E., Schlegel, A., Kirkegaard, K., Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 2296-2301; Nelson, G.W., Stohlman, S.A., Localization of the RNA-binding domain of MHV nucleocapsid protein (1993) J. Gen. Virol., 74, pp. 1975-1979; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus strain A59 (1989) Virology, 171, pp. 141-148; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. Virol., 69, pp. 5475-5484; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., RNA-binding proteins of coronavirus MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) Proc. Natl. Acad. Sci. USA, 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands (1995) Corona- And Related Viruses, pp. 499-506. , P. J. Talbot, & G. A. Levy. New York: Plenum; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shi, S.T., Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Oh, J.W., Lai, M.M.C., Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells (1999) J. Virol., 73, pp. 5957-5969; Shieh, C.K., Lee, H.J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol., 63, pp. 3729-3736; Skinner, M.A., Siddell, S.G., Coronavirus JHM: Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acids Res., 11, pp. 5045-5054; Smith, D.B., Johnson, K.S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase (1988) Gene, 67, pp. 31-40; Spaan, W.J.M., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van Der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Stohlman, S.A., Baric, R.S., Nelson, G.H., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Stohlman, S.A., Lai, M.M.C., Phosphoproteins of murine hepatitis viruses (1979) J. Virol., 32, pp. 672-675; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′-end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J. Med. Virol., 44, pp. 152-161; Zhang, X.M., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in the murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633; Zhang, X.M., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of murine hepatitis virus RNAs: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X.M., Li, H.-P., Xue, W., Lai, M.M.C., Formation of a ribonucleoprotein complex of mouse hepatitis virus involving heterogeneous nuclear ribonucleoprotein A1 and transcription-regulatory elements of viral RNA Virology, 264, pp. 115-124; Zhang, X.M., Liao, C.L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Zhang, X.; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham Street, Little Rock, AR 72205, United States; email: zhangxuming@exchange.uams.edu",,"Academic Press Inc.",00426822,,VIRLA,"10603321","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0033527903
"Breslin J.J., Smith L.G., Fuller F.J., Guy J.S.","7004753945;37109180900;7006216552;7202723649;","Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3' untranslated region identifies the virus as a close relative of infectious bronchitis virus",1999,"Virus Research","65","2",,"187","193",,53,"10.1016/S0168-1702(99)00117-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032697887&doi=10.1016%2fS0168-1702%2899%2900117-3&partnerID=40&md5=a5aebd421837100bf8b3d1ed1dd59f9e","Department of Microbiology, Pathol., Parasitol., N. Carolina S., Raleigh, NC 27606, United States","Breslin, J.J., Department of Microbiology, Pathol., Parasitol., N. Carolina S., Raleigh, NC 27606, United States; Smith, L.G., Department of Microbiology, Pathol., Parasitol., N. Carolina S., Raleigh, NC 27606, United States; Fuller, F.J., Department of Microbiology, Pathol., Parasitol., N. Carolina S., Raleigh, NC 27606, United States; Guy, J.S., Department of Microbiology, Pathol., Parasitol., N. Carolina S., Raleigh, NC 27606, United States","The 3' end of the turkey coronavirus (TCV) genome (1740 bases) including the nucleocapsid (N) gene and 3' untranslated region (UTR) were sequenced and compared with published sequences of other avian and mammalian coronaviruses. The deduced sequence of the TCV N protein was determined to be 409 amino acids with a molecular mass of approximately 45 kDa. The TCV N protein was identical in size and had greater than 90% amino acid identity with published N protein sequences of infectious bronchitis virus (IBV); less than 21% identity was observed with N proteins of bovine coronavirus and transmissible gastroenteritis virus. The 3' UTR showed some variation among the three TCV strains examined, with two TCV strains, Minnesota and Indiana, containing 153 base segments which are not present in the NC95 strain. Nucleotide sequence identity between the 3' UTRs of TCV and IBV was greater than 78%. Similarities in both size and sequence of TCV and IBV N proteins and 3' UTRs provide additional evidence that these avian coronaviruses are closely related.","Infectious bronchitis virus; Nucleocapsid gene; Turkey coronavirus","nucleocapsid protein; article; avian infectious bronchitis virus; controlled study; coronavirus; genetic variability; intron; nonhuman; nucleotide sequence; phylogeny; priority journal; sequence analysis; sequence homology; turkey coronavirus; virus genome; virus strain; 3' Untranslated Regions; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus, Turkey; DNA, Viral; Infectious bronchitis virus; Molecular Sequence Data; Nucleocapsid; Nucleocapsid Proteins; Sequence Alignment; Turkeys; Animalia; Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; Mammalia; RNA viruses; Transmissible gastroenteritis virus; Turkey coronavirus","Boursnell, M.E., Binns, M.M., Foulds, I.J., Brown, T.D., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry 10th Ed., pp. 511-526. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald, & Y.M. Saif. Ames, IA: Iowa State University Press; Collisson, E.W., Williams, A.K., Vonder Harr, R., Li, W., Sneed, L.W., Sequence comparisons of the 3′end of the genomes of five strains of avian infectious bronchitis virus (1990) Coronaviruses and Their Diseases, pp. 373-377. , D. Cavanagh, & T.D.K. Brown. New York: Plenum; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1986) Avian Dis., 30, pp. 319-326; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- And mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fundamental Virology, 3rd Ed., 1, pp. 1075-1093. , In: Fields, B.N., Knipe, D.M., Howly, P.M. (Eds.), 2 vols. Lippincott-Raven, Philadelphia, PA; Hsue, B., Masters, P.S., A bulged stem-loop in the 3′ untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J. Virol., 71, pp. 7567-7578; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , S.G. Siddell. New York: Plenum; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry 10th Ed., pp. 686-692. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald, & Y.M. Saif. Ames, IA: Iowa State University Press; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three-domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Pedersen, N.C., Antigenic relationship of feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol., 58, pp. 45-53; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; Robb, J.A., Bond, C.W., Coronaviridae (1979) Comprehensive Virology, 14, pp. 193-247. , H. Fraenkel-Conrat, Wagner R.R. New York: Plenum; (1989) Molecular Cloning, a Laboratory Manual 2nd Ed., , J. Sambrook, E.F. Fritsch, & T. Maniatis. Cold Spring Harbor: Cold Spring Harbor Laboratory Press; Sapats, S.I., Ashton, F., Wright, P.J., Ignjatovic, J., Novel variation in the N protein of avian infectious bronchitis virus (1996) Virology, 226, pp. 412-417; Siddell, S.G., The coronaviridae an introduction (1995) Coronaviridae, pp. 1-9. , S.G. Siddell. New York: Plenum; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Res., 25, pp. 213-222; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Analysis of a hypervariable region in the 3′ non-coding end of the infectious bronchitis virus genome (1993) Virus Res., 28, pp. 19-27; Zwaagstra, K.A., Van Der Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1992) J. Clin. Microbiol., 30, pp. 79-84","Guy, J.S.; Department of Microbiology, North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States",,,01681702,,VIRED,"10581391","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0032697887
"Kyuwa S., Ohsawa K., Sato H., Urano T.","7006444820;7102526100;35354210200;55183079300;","Replication of Enterotropic and Polytropic Murine Coronaviruses in Cultured Cell Lines of Mouse Origin",2000,"Experimental Animals","49","4",,"251","257",,3,"10.1538/expanim.49.251","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034304116&doi=10.1538%2fexpanim.49.251&partnerID=40&md5=aa4e1c2d580fa29e30abe98e18a3c09f","Div. of Microbiology and Genetics, Ctr. for Anim. Rsrc. and Development, Kumamoto University, Honjo 2-2-1, Kumamoto 960-0811, Japan; Lab. Anim. Ctr. for Biomed. Research, Nagasaki Univ. School of Medicine, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Department of Biomedical Science, Grad. Sch. of Agric. and Life Sci., University of Tokyo, 1-1-1 Yayoi, Bunkyoy-ku, Tokyo 113-8657, Japan","Kyuwa, S., Div. of Microbiology and Genetics, Ctr. for Anim. Rsrc. and Development, Kumamoto University, Honjo 2-2-1, Kumamoto 960-0811, Japan, Department of Biomedical Science, Grad. Sch. of Agric. and Life Sci., University of Tokyo, 1-1-1 Yayoi, Bunkyoy-ku, Tokyo 113-8657, Japan; Ohsawa, K., Lab. Anim. Ctr. for Biomed. Research, Nagasaki Univ. School of Medicine, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Sato, H., Lab. Anim. Ctr. for Biomed. Research, Nagasaki Univ. School of Medicine, Sakamoto 1-12-4, Nagasaki 852-8523, Japan; Urano, T., Div. of Microbiology and Genetics, Ctr. for Anim. Rsrc. and Development, Kumamoto University, Honjo 2-2-1, Kumamoto 960-0811, Japan","To understand the virus-cell interactions that occur during murine coronavirus infection, six murine cell lines (A3-1M, B16, CMT-93, DBT, IC-21 and J774A.1) were inoculated with eight murine coronaviruses, including prototype strains of both polytropic and enterotropic biotypes, and new isolates. All virus strains produced a cytopathic effect (CPE) with cell-to-cell fusion in B16, DBT, IC-21 and J774A.1 cells. The CPE was induced most rapidly in IC-21 cells and was visible microscopically in all cell lines tested. In contrast, the coronaviruses produced little CPE in A3-1M and CMT-93 cells. Although most virus-infected cells, except KQ3E-infected A3-1M, CMT-93 and J774A.1 cells, produced progeny viruses in the supernatants when assayed by plaque formation on DBT cells, the kinetics of viral replication were dependent on both the cell line and virus strain; replication of prototype strains was higher than that of new isolates. There was no significant difference in replication of enterotropic and polytropic strains. B16 cells supported the highest level of viral replication. To determine the sensitivity of the cell lines to murine coronaviruses, the 50% tissue culture infectious dose of the coronaviruses was determined with B16, DBT, IC-21 and J774A.1 cells, and compared to that with DBT cells. The results indicate that IC-21 cells were the most sensitive to murine coronaviruses. These data suggest that B16 and IC-21 cells are suitable for large-scale preparation and isolation of murine coronaviruses, respectively.","B16 cells; IC-21 cells; Murine coronavirus; Replication; TCID50","Coronavirus; Murinae; Murine hepatitis virus; animal; article; cell culture; cell line; Coronavirus; experimental melanoma; kinetics; mouse; Murine hepatitis coronavirus; physiology; rectum tumor; stem cell; virus culture; virus replication; Animals; Cell Line; Coronavirus; Kinetics; Melanoma, Experimental; Mice; Murine hepatitis virus; Plaque Assay; Rectal Neoplasms; Stem Cells; Tumor Cells, Cultured; Virus Replication","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Barthold, S.W., Smith, A.L., Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice (1984) Arch. Virol., 81, pp. 103-112; Barthold, S.W., Smith, A.L., Lord, P.F.S., Jacoby, R.O., Main, A.J., Epizootic coronaviral typhlocolitis in suckling mice (1982) Lab. Anim. Sci., 32, pp. 376-383; Barthold, S.W., Smith, A.L., Pover, M.L., Enterotropic mouse hepatitis virus infection in nude mice (1985) Lab. Anim. Sci., 35, pp. 613-618; Chen, D.S., Asanaka, M., Yokomori, K., Wang, F.I., Hwang, S.B., Li, H.P., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci., 92, pp. 12095-12099; Compton, S.R., Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors (1994) Virology, 203, pp. 197-201; Compton, S.R., Interactions of enterotropic mouse hepatitis viruses with Bgp2 receptor proteins (1998) Adv. Exp. Med. Biol., 440, pp. 25-31; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Compton, S.R., Winograd, D.F., Gaertner, D.J., Optimization of in vitro growth conditions for enterotropic murine coronavirus strains (1995) J. Virol. Methods, 52, pp. 301-307; Franks, L.M., Hemmings, V.J., A cell line from an induced carcinoma of mouse rectum (1978) J. Pathol., 124, pp. 35-38; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamate Virusforsch., 44, pp. 298-302; Homberger, F.R., Enterotropic mouse hepatitis virus (1997) Lab. Anim., 31, pp. 97-115; Homberger, F.R., Zhang, L., Barthold, S.W., Prevalence of enterotropic and polytropic mouse hepatitis virus in enzootically infected mouse colonies (1998) Lab. Anim. Sci., 48, pp. 50-54; Kyuwa, S., Replication of MHV in mouse embryonic stem cell lines in vitro (1997) Exp. Anim., 46, pp. 311-313; Kyuwa, S., Machii, K., Okumura, A., Toyoda, Y., Characterization of T cells expanded in vivo during primary mouse hepatitis virus infection (1996) J. Vet. Med. Sci., 58, pp. 431-437; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Kyuwa, S., Tagawa, Y., Shibata, S., Doi, K., Machii, K., Iwakura, Y., Murine coronavirus-induced subacute fatal peritonitis in C57BL/6 mice deficient in gamma interferon (1998) J. Virol., 72, pp. 9286-9290; Manaker, R.A., Piczak, C.V., Miller, A.A., Stanton, M.F., A hepatitis virus complicating studies with mouse leukemias (1961) J. Nat. Cancer Inst., 27, pp. 29-45; Okumura, A., Machii, K., Azuma, S., Toyoda, Y., Kyuwa, S., Maintenance of pluripotency in mouse embryonic stem cells persistently infected with murine coronavirus (1996) J. Virol., 70, pp. 4146-4149; Silagi, S., Control of pigment production in mouse melanoma cells in vitro. Evocation and maintenance (1969) J. Cell Biol., 43, pp. 263-274; Stohlman, S.A., Brayton, P.R., Fleming, J.O., Weiner, L.P., Lai, M.M., Murine coronaviruses: Isolation and characterization of two plaque morphology variants of the JHM neurotropic strain (1982) J. Gen. Virol., 63, pp. 265-275; Weiland, E., Mussgey, M., Weiland, F., Nonproducer malignant tumor cells with rescuable sarcoma virus genome isolated from a recurrent Moloney sarcoma (1978) J. Exp. Med., 148, pp. 408-423; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yamaguchi, K., Kyuwa, S., Nakanaga, K., Hayami, M., Establishment of cytotoxic T-cell clones specific for cells infected with mouse hepatitis virus (1988) J. Virol., 62, pp. 2505-2507","Kyuwa, S.; Department of Biomedical Science, Grad. Sch. of Agric. and Life Sci., University of Tokyo, 1-1-1 Yayoi, Bunkyoy-ku, Tokyo 113-8657, Japan",,"International Press Editing Centre Incorporation",13411357,,JIDOA,"11109550","English","Exp. Anim.",Article,"Final",Open Access,Scopus,2-s2.0-0034304116
"Cologna R., Hogue B.G.","7801604385;7003393593;","Identification of a bovine coronavirus packaging signal",2000,"Journal of Virology","74","1",,"580","583",,32,"10.1128/JVI.74.1.580-583.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033989552&doi=10.1128%2fJVI.74.1.580-583.2000&partnerID=40&md5=364676bd0d7e023f71764798bac80244","Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States; Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Cologna, R., Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States; Hogue, B.G., Division of Molecular Virology, Baylor College of Medicine, Houston, TX 77030, United States, Dept. of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030, United States, Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","A region of the bovine coronavirus (BCV) genome that functions as a packaging signal has been cloned. The 291-nucleotide clone shares 72% homology with the region of mouse hepatitis coronavirus (MHV) gene 1b that contains the packaging signal. RNA transcripts were packaged into both BCV and MHV virions when the cloned region was appended to a noncoronavirus RNA. This is the first identification of a BCV packaging signal. The data demonstrate that the BCV genome contains a sequence that is conserved at both the sequence and functional levels, thus broadening our insight into coronavirus packaging.",,"animal cell; article; Coronavirus; DNA packaging; encapsulation; genetic conservation; nonhuman; open reading frame; priority journal; signal transduction; virus genome; virus nucleocapsid; virus replication; virus strain","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-300; Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Baric, R.S., Nelson, C.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Virol., 64, pp. 4108-4114; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Mendez, A., Plana-Duran, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Kienzle, R.T.E., Abraham, S., Hogue, B.G., Brian, D.A., Structure and orientation of expressed bovine coronavirus hemagglutinin esterase protein (1990) J. Virol., 64, pp. 1834-1838; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-77; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) J. Virol., 64, pp. 6045-6053; Mathews, D.H., Sabina, J., Zuker, M., Turne, D.H., Expanded sequence dependence of thermodynamic parameters provides robust prediction of RNA secondary structure (1999) J. Mol. Biol., 288, pp. 911-940; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Nguyen, V.-P., Hogue, B.G., Protein interactions during coronavirus assembly (1997) J. Virol., 71, pp. 9278-9284; Owen, K.E., Kuhn, R.J., Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation (1996) J. Virol., 70, pp. 2757-2763; Pattnaik, A.K., Ball, L.A., Legrone, A.W., Wertz, G.W., Infectious defective interfering particles of VSV from transcripts of a cDNA clone (1992) Cell, 69, pp. 1011-1020; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Sethna, P.B., Hung, S.-H., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Siddell, S.G., The coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interactions between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; (1999) Wisconsin Package, Version 10.0, , University of Wisconsin Genetics Computer Group, Madison; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Zhao, S., Shaw, K., Cavanagh, D., Presence of subgenomic mRNAs in virions of coronavirus IBV (1993) Virology, 196, pp. 172-178; Zuker, M., Mathews, D.H., Turner, D.H., Algorithms and thermodynamics for RNA secondary structure prediction (1999) NATO ASI (Adv. Sci. Inst.) Ser. A Life Sci., 1999, pp. 11-43","Hogue, B.G.; Dept. of Microbiology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; email: bhogue@bcm.tmc.edu",,"American Society for Microbiology",0022538X,,JOVIA,"10590153","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033989552
"Kiss I., Kecskeméti S., Tanyi J., Klingeborn B., Belák S.","6603849862;6603764465;6603437628;35611673800;56053373800;","Prevalence and Genetic Pattern of Feline Coronaviruses in Urban Cat Populations",2000,"Veterinary Journal","159","1",,"64","70",,15,"10.1053/tvjl.1999.0402","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033629648&doi=10.1053%2ftvjl.1999.0402&partnerID=40&md5=718a2bc8e47ff00f863d05cc32264e5b","Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","Kiss, I., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Kecskeméti, S., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Tanyi, J., Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary; Klingeborn, B., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Belák, S., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","The prevalence and phylogeny of feline coronaviruses were studied in urban cat populations by sampling of 113 clinically healthy cats. Rectal swab samples were subjected to a nested reverse-transcription polymerase chain reaction, specific for the conservative nucleocapsid region of the virus genome. More than 30% of the sampled animals proved positive for the presence of feline coronaviruses. The nucleotide sequences of amplified 440 bp products were determined, aligned and the phylogenetic analysis revealed noticeable genetic clusters among the prevalent feline coronaviruses in the surveyed geographic area. These findings will hopefully contribute to the elucidation of the epidemiology of feline infectious peritonitis. © 2000 Harcourt Publishers Ltd.","Feline; coronavirus; RT-PCR; prevalence; phylogeny.","Animalia; Coronavirus; Felidae; Felis catus; complementary DNA; animal; article; cat; chemistry; Coronavirus; genetics; isolation and purification; phylogeny; polymerase chain reaction; rectum; reverse transcription polymerase chain reaction; sequence alignment; urban population; virology; Animals; Cats; Coronavirus; DNA, Complementary; Phylogeny; Polymerase Chain Reaction; Rectum; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Urban Population","Addie, D.D., Jarrett, J.O., A study of naturally occurring feline coronavirus infections in kittens (1992) Veterinary Record, 130, pp. 133-137; Addie, D.D., Jarrett, J.O., Feline coronavirus antibodies in cats (1992) Veterinary Record, 131, pp. 202-203; Baric, R.S., Fu, K.F., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map of murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-Van Dillen, P.M.E., Van Der Nooredaa, J., Rapid and simple method for purification of nucleic acid (1990) Journal of Clinical Microbiology, 28, pp. 495-503; Cheung, R.C., Matsui, S., Greenberg, H., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) Journal of Clinical Microbiology, 32, pp. 2593-2597; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A., Intracellular RNAs of the feline infectious peritonitis virus strain 79-1146 (1987) Journal of General Virology, 68, pp. 995-1002; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Siddell, & S.G. New York: Plenum Press; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R., The genome organization of the Nidovirales: Similarities and differences between Arteri-, Toro-, and Coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Evermann, J.F., McKeirnan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Veterinary Microbiology, 28, pp. 243-255; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A., Horzinek, M.C., Lutz, H., Placebo-controlled evaluation of a modified life virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions (1997) Vaccine, 15, pp. 1101-1109; Foley, J.F., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Practice, 24, pp. 14-22; Foley, J.F., Poland, A., Carlson, J., Pedersen, N.C., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) Journal of American Veterinary Medical Association, 210, pp. 1313-1318; Foley, J.F., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) Journal of American Veterinary Medical Association, 210, pp. 1307-1312; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) Journal of Clinical Microbiology, 35, pp. 673-675; Gunn-Moore, D.A., Gruffydd-Jones, T.J., Harbour, D.A., Detection of feline coronaviruses by culture and reverse transcriptase-polymerase chain reaction of blood samples from healthy cats and cats with clinical feline infectious peritonitis (1998) Veterinary Microbiology, 62, pp. 193-205; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) Journal of American Veterinary Medical Association, 209, pp. 1117-1120; Herrewegh, A.A.P.M., De Groot, R., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) Journal of Clinical Microbiology, 33, pp. 684-689; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) Journal of Virology, 72, pp. 4508-4514; Higgins, D.G., Bleasby, A.J., Fuchs, R., Clustal V: Improved software for multiple sequence alignment (1992) CABIOS, 8, pp. 189-191; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Archives of Virology, 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (Mabs): Preparation of Mabs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Veterinary Microbiology, 28, pp. 13-24; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) Journal of Veterinary Medical Science, 54, pp. 557-562; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) Journal of General Virology, 73, pp. 2849-2862; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, S., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) Journal of Virology, 62, pp. 1810-1813; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kusters, J.G., Jager, E.J., Niesters, B.G.M., Zeist, B.A.M., Sequence evidence for RNA recombination in fireld isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M.C., Baric, R.C., Makino, S., Keck, J.G., Engbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) Journal of Virology, 56, pp. 449-456; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Seminars in Virology, 7, pp. 381-388; L.I., X., Scott, F.W., Detection of feline coronaviruses in cell cultures and in fresh and fixed feline tissues using polymerase chain reaction (1994) Veterinary Microbiology, 42, pp. 65-77; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , S.G. 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New York: Plenum Press; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) Journal of Virology, 57, pp. 729-739; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiology and Immunology, 40, pp. 425-433; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Veterinary Microbiology, 36, pp. 1-37; Paltrinieri, S., Parodi Cammarata, M., Cammarata, G., Comazzi, S., Some aspects of humoral and cellular immunity in naturally occuring feline infectious peritonitis (1998) Veterinary Immunology and Immunpathology, 65, pp. 205-220; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) American Journal of Veterinary Research, 37, pp. 1449-1453; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Advances in Experimental Medicine and Biology, 218, pp. 529-550; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1987) Feline Practice, 23, pp. 7-22; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) Journal of Clinical Microbiology, 34, pp. 3180-3184; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) Journal of General Virology, 64, pp. 761-776; Vennema, H., De Groot, R., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) Journal of Virology, 64, pp. 1407-1409; Vennema, H., De Groot R., J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157","Kiss, I.; Veterinary Institute of Debrecen, P.O. Box 51, H-4002 Debrecen, Hungary",,"Bailliere Tindall Ltd",10900233,,VTJRF,"10640412","English","Vet. J.",Article,"Final",Open Access,Scopus,2-s2.0-0033629648
"Guy J.S.","7202723649;","Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses: A review",2000,"Avian Pathology","29","3",,"207","212",,55,"10.1080/03079450050045459","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034211040&doi=10.1080%2f03079450050045459&partnerID=40&md5=a4a74b5d198db80c9bcae5f2433cc82e","Dept. of Microbiol., Pathol., and P., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States","Guy, J.S., Dept. of Microbiol., Pathol., and P., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States","Turkey coronavirus (TCoV) is the cause of an acute highly contagious enteric disease of turkeys. In recent years, TCoV has been increasingly recognized in North America as an important pathogen of young turkeys, resulting in economic loss due to impaired growth and poor feed conversion. While the epidemiology and pathogenesis of TCoV have been extensively studied, TCoV remains one of the least characterized of the known coronaviruses. Avian and mammalian coronaviruses have been subdivided into distinct antigenic/genotypic groups; however, classification of TCoV has been controversial. Previous studies indicated that TCoV was closely related to bovine coronavirus and other group 2 mammalian coronaviruses, but more recent antigenic and genome sequence analyses contradict these findings and, instead, provide evidence that TCoV is closely related to avian infectious bronchitis virus (IBV). Additionally, experimental studies have indicated that the host range of TCoV, once thought to be restricted to turkeys, includes chickens. These studies have raised additional questions regarding the classification of TCoV; particularly, whether IBV and TCoV are taxonomically distinct viruses, or whether TCoV is merely a variant of IBV. Sequence analyses of TCoV have given credence to the idea that TCoV is a variant of IBV, as these studies have shown that TCoV and IBV are very closely related. However, these studies have been limited to only three TCoV strains and relatively small portions of the TCoV genome. TCoV is readily distinguished from IBV based on antigenic and biological differences, and these differences suggest that TCoV should be considered a distinct virus species. Additional studies will be needed to better define the relationship between TCoV and IBV, and to resolve this taxonomic question. Based on our current understanding, it seems prudent to consider TCoV and IBV as distinct virus species that share a close phylogenetic relationship and together comprise group 3 of the coronavirus major antigenic groups.",,"Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; Galliformes; Gallus gallus; Mammalia; Meleagris gallopavo; Turkey coronavirus","Ambali, A.G., Jones, R.C., Early pathogenesis in chicks of infection with anenterotropic strain of infectious bronchitis virus (1990) Avian Diseases, 34, pp. 809-817; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome ('spiking mortality') of turkeys (1997) Diseases of Poultry 10th Edn, pp. 1025-1031. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald & Y.M. Saif (Eds.), Ames, IA: Iowa State University Press; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3 untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry 10th Edn, pp. 511-526. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald & Y.M. Saif (Eds.), Ames, IA: Iowa State University Press; Cavanagh, D., Brian, D.A., Brinton, M.A., Eujuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Archives of Virology, 142, pp. 629-633; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1986) Avian Diseases, 30, pp. 319-326; Dea, S., Garzon, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (bluecomb) coronaviruses in a continuous human rectal adenocarcinoma cell line (1989) American Journal of Veterinary Research, 50, pp. 1310-1318; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) Journal of Virology, 64, pp. 3112-3118; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis from pheasants (1996) The Veterinary Record, 138, pp. 208-209; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis-and mortality syndrome-affected turkeys (1997) Avian Diseases, 41, pp. 583-590; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J.J., Experimental infection of specific-pathogen-free chickens with turkey coronavirus (1999) Western Poultry Disease Conference, Vancouver, B.C., pp. 91-92; Holmes, K.V., Coronaviridae and their replication (1990) Virology, 1, pp. 841-856. , B.N. Fields (Ed.), New York: Raven Press; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fundamental Virology, 1, pp. 1075-1093. , B.N. Fields, D.M. Knipe & P.M. Howly (Eds.), 3rd edn Philadelphia, PA: Lippincott-Raven Publishers; Karaca, K.S., Naqi, S., Gelb J., Jr., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Diseases, 36, pp. 903-915; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Laporte, J., Bobulesco, P., Rossi, F., Une lignee cellulaire particulierement sensible a la replication du coronavirus enteritique bovin: Les cellules HRT-18 (1980) Comptes Rendus Hebdomadaires des Seances de l'Academie des Sciences, 290, pp. 625-626; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein genes of human coronavirus OC43 and evidence of O-glycosylation (1992) Journal of General Virology, 73, pp. 2731-2736; Murphy, F.A., Virus taxonomy (1996) Fundamental Virology, 1, pp. 15-57. , B.N. Fields, D.M. Knipe & P.M. Howly (Eds.), 3rd edn Philadelphia, PA: Lippincott-Raven Publishers; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, pp. 686-692. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald & Y.M. Saif (Eds.), Ames, IA: Iowa State University Press; Naqi, S.A., Panigrahy, B., Hall, C.F., Bursa of Fabricius, a source of bluecomb infectious agent (1972) Avian Diseases, 16, pp. 937-939; Panigrahy, B., Naqi, S.A., Hall, C.F., Isolation and characterization of viruses associated with transmissible enteritis (bluecomb) of turkeys (1973) Avian Diseases, 17, pp. 430-438; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) American Journal of Veterinary Research, 36, pp. 553-554; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of feline infectious peritonitis virus to coronaviruses of other species (1978) Archives of Virology, 58, pp. 45-53; Pomeroy, K.S., Patel, B.C., Larsen, C.T., Pomeroy, B.S., Combined immunofluorescence and transmission electron microscopic studies of sequential intestinal samples from turkey embryos and poults infected with turkey enteritis virus (1978) American Journal of Veterinary Research, 39, pp. 1348-1358; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Diseases, 17, pp. 546-558; Robb, J.A., Bond, C.W., Coronaviridae (1979) Comprehensive Virology, 14, pp. 193-247. , H. Fraenkel-Conrat & R.R. Wagner (Eds.), New York: Plenum Press; Siddell, S.G., The Coronaviridae: An introduction (1995) Coronaviridae, pp. 1-9. , S.G. Siddell (Ed.), New York: Plenum Press; Spackman, D., Cameron, I.D.R., Isolation of infectious bronchitis virus from pheasants (1983) The Veterinary Record, 113, pp. 354-355; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from eleven coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Research, 60, pp. 181-189; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Advances in Virus Research, 28, pp. 35-112; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTAL_X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Research, 25, pp. 4876-4882; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) Journal of General Virology, 72, pp. 1659-1666; Verbeek, A., Dea, S., Tijssen, P., Genomic relationship between turkey and bovine enteric coronaviruses identified by hybridization with BCV or TCOV specific cDNA probes (1991) Archives of Virology, 121, pp. 199-211; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Current Topics in Microbiology and Immunology, 99, pp. 165-200; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Research, 25, pp. 213-222; Zwaagstra, K.A., Van Der Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1992) Journal of Clinical Microbiology, 30, pp. 79-84","Guy, J.S.; Department of Microbiology, North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough Street, Raleigh, NC 27606, United States",,"Carfax Publishing Company",03079457,,AVPAD,,"English","Avian Pathol.",Review,"Final",,Scopus,2-s2.0-0034211040
"Kim L., Chang K.-O., Sestak K., Parwani A., Saif L.J.","7202158982;7404878277;6701814572;7004273180;7102226747;","Development of a reverse transcription-nested polymerase chain reaction assay for differential diagnosis of transmissible gastroenteritis virus and porcine respiratory coronavirus from feces and nasal swabs of infected pigs",2000,"Journal of Veterinary Diagnostic Investigation","12","4",,"385","388",,30,"10.1177/104063870001200418","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034220403&doi=10.1177%2f104063870001200418&partnerID=40&md5=47e57143c29c6e5b71641856446f8a1b","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; School of Veterinary Medicine, Tufts University, North Grafton, MA 01536-1895, United States","Kim, L., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Chang, K.-O., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Sestak, K., School of Veterinary Medicine, Tufts University, North Grafton, MA 01536-1895, United States; Parwani, A., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States","Transmissible gastroenteritis virus (TGEV), a coronavirus, replicates in intestinal enterocytes and causes diarrhea in young pigs. Porcine respiratory coronavirus (PRCV), a spike (S) gene natural deletion mutant of TGEV, has a respiratory tissue tropism and causes mild or subclinical respiratory infections. Conventional antigen-based diagnostic tests fail to differentiate TGEV and PRCV, and a blocking ELISA test to serologically differentiate TGEV/PRCV-infected pigs is conducted on convalescent serum retrospectively after disease outbreaks. A reverse transcription (RT)-nested polymerase chain reaction (PCR) with primers targeted to the S gene deletion region to differentiate TGEV/PRCV was developed. The specificity of the RT-nested PCR was confirmed with reference and recent field strains of TGEV/PRCV, and its sensitivity was analyzed by testing nasal and fecal samples collected from pigs at various days postinoculation (DPI) with TGEV or PRCV. Specific PCR products for TGEV/PRCV were detected only with the homologous reference or field coronaviruses and for 10-14 DPI of pigs with TGEV (feces) or PRCV (nasal samples). The RT-nested PCR assay was more sensitive than antigen-based assays on the basis of duration of virus detection in experimentally infected pigs and was directly applicable to nasal as well as fecal specimens from the field.",,"animal; animal disease; article; differential diagnosis; feces; nose mucus; respiratory tract infection; reverse transcription polymerase chain reaction; sensitivity and specificity; swine; swine disease; Transmissible gastroenteritis virus; virology; virus infection; Animals; Coronavirus Infections; Diagnosis, Differential; Feces; Gastroenteritis, Transmissible, of Swine; Nasal Lavage Fluid; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction; Sensitivity and Specificity; Swine; Transmissible gastroenteritis virus","Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal Biochem, 162, pp. 156-159; Kwon, H.M., Saif, L.J., Jackwood, D.J., Field isolates of transmissible gastroenteritis virus differ at the molecular level from the Miller and Purdue virulent and attenuated strains and from porcine respiratory coronaviruses (1998) J Vet Med Sci., 60, pp. 589-597; Laude, H., Reeth, K.V., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; Park, S., Sestak, K., Hodgins, D., Immune response of sows vaccinated with attenuated transmissible gastroenteritis virus (TGEV) and recombinant TGEV spike protein vaccines and protection of their suckling pigs against virulent TGEV challenge exposure (1998) Am J Vet Res, 59, pp. 1002-1008; Paton, D., Ibata, G., Sands, J., McGoldrick, A., Detection of TGEV by RT-PCR and differentiation from porcine respiratory coronavirus (1997) J Virol Methods, 66, pp. 303-309; Pritchard, G.C., Paton, D.J., Wibberley, G., Ibata, G., Transmissible gastroenteritis and porcine epidemic diarrhoea in Britain (1999) Vet Rec, 144, pp. 616-618; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis and porcine respiratory coronavirus (1999) Diseases of Swine, pp. 295-325. , ed. Straw BE, 8th ed., Iowa State University Press, Ames, IA; Sestak, K., Lanza, I., Park, S.K., Contribution of passive immunity to PRCV to protection against TGEV challenge exposure in suckling pigs (1996) Am J Vet Res, 57, pp. 664-671; Simkins, R.A., Weilnau, P.A., VanCott, J.L., Competition ELISA, using monoclonal antibodies to the transmissible gastroenteritis virus (TGEV) S protein, for serologic differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am J Vet Res, 54, pp. 254-259; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in formalin-fixed paraffin-embedded tissues (1996) J Virol Methods, 56, pp. 149-160; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of PRCV isolates reveals heterogeneity in the S, 3 and 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Vaughn, E.M., Halbur, P.G., Paul, P.S., Use of nonradioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates (1996) J Vet Diagn Invest, 8, pp. 241-244; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J Vet Diagn Invest, 3, pp. 29-32","Kim, L.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"10907874","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0034220403
"Stirrups K., Shaw K., Evans S., Dalton K., Cavanagh D., Britton P.","57210222541;7202206256;7402709581;7006042187;26642890500;57203302770;","Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus",2000,"Journal of General Virology","81","3",,"791","801",,27,"10.1099/0022-1317-81-3-791","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033956460&doi=10.1099%2f0022-1317-81-3-791&partnerID=40&md5=804df58e1766bda5ff31babfefb08cc1","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; University of Cambridge, Department of Haematology, Division of Transfusion Medicine, Long Road, Cambridge CB2 2PT, United Kingdom; Depts. Pathol. Cell Biol. (BML 342), Yale University School of Medicine, 310 Cedar St., New Haven, CT 06510, United States","Stirrups, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom, University of Cambridge, Department of Haematology, Division of Transfusion Medicine, Long Road, Cambridge CB2 2PT, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Evans, S., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Dalton, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom, Depts. Pathol. Cell Biol. (BML 342), Yale University School of Medicine, 310 Cedar St., New Haven, CT 06510, United States; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","A defective RNA (D-RNA), CD-61, derived from the Beaudette strain of the avian coronavirus infectious bronchitis virus (IBV), was rescued (replicated and packaged) using four heterologous strains of IBV as helper virus. Sequence analysis of the genomic RNA from the four heterologous IBV strains (M41, H120, HV10 and D207) identified nucleotide differences of up to 17% within the leader sequence and up to 4.3% within the whole of the adjacent 5' untranslated region (UTR). Analysis of the 5' ends of the rescued D-RNAs showed that the Beaudette leader sequence, present on the initial CD-61, had been replaced with the corresponding leader sequence from the helper IBV strain but the adjacent 5' UTR sequence of the rescued D-RNAs corresponded to the original CD-61 Beaudette sequence. These results demonstrated that the phenomenon of leader switching previously identified for the coronaviruses murine hepatitis virus and bovine coronavirus (BCoV) also occurred during the replication of IBV D-RNAs. Three predicted stem-loop structures were identified within the 5' UTR of IBV. Stem-loop I showed a high degree of covariance amongst the IBV strains providing phylogenetic evidence that this structure exists and is potentially involved in replication, supporting previous observations that a BCoV stem-loop homologue was essential for replication of BCoV defective interfering RNAs.",,"nucleotide; RNA; signal peptide; 5' untranslated region; article; Avian infectious bronchitis virus; Coronavirus; cow; helper virus; Murine hepatitis coronavirus; priority journal; RNA replication; RNA structure; sequence analysis; Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1987) Current Protocols in Molecular Biology, , New York: John Wiley and Sons; Binns, M.M., Boursnell, M.E.G., Cavanagh, D., Pappain, D.J.C., Brown, T.D.K., Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) Journal of General Virology, 66, pp. 719-726; Binns, M.M., Boursnell, M.E.G., Tomley, F.M., Brown, T.D.K., Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) Journal of General Virology, 67, pp. 2825-2831; Bonfield, J.K., Smith, K.F., Staden, R., A new DNA sequence assembly program (1995) Nucleic Acids Research, 24, pp. 4992-4999; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Seminars in Virology, 8, pp. 101-111; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) Journal of Virology, 68, pp. 8223-8231; Chang, R.Y., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) Journal of Virology, 70, pp. 2720-2729; Darbyshire, J.H., Rowell, J.G., Cook, J.K.A., Peters, R.W., Taxonomic studies on strains of avian infectious bronchitis virus using neutralisation tests in tracheal organ cultures (1979) Archives of Virology, 61, pp. 227-238; Davelaar, F.G., Kouwenhoven, B., Burger, A.G., Occurrence and significance of infectious bronchitis virus variant strains in egg and broiler production in the Netherlands (1984) Veterinary Quarterly, 6, pp. 114-120; Devereux, J., Haeberli, P., Smithies, O., A comprehensive set of sequence analysis programs for the VAX (1984) Nucleic Acids Research, 12, pp. 387-395; Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organisation of the Nidovirales: Similarities and differences between arteri-, toro- and coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Feinberg, A.P., Vogelstein, B., A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity (1983) Analytical Biochemistry, 132, pp. 6-13; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts (1995) Journal of Virology, 69, pp. 6219-6227; Hofmann, M.A., Sethna, P.B., Brian, D.A., Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture (1990) Journal of Virology, 64, pp. 4108-4114; Jaeger, J.A., Turner, D.H., Zuker, M., Improved predictions of secondary structures for RNA (1989) Proceedings of the National Academy of Sciences, USA, 86, pp. 7706-7710; Jaeger, J.A., Turner, D.H., Zuker, M., Predicting optimal and suboptimal secondary structure for RNA (1990) Methods in Enzymology, 183, pp. 281-306; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) Journal of Virology, 63, pp. 5285-5292; Makino, S., Stohlman, S.A., Lai, M.M.C., Leader sequences of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA in transcription (1986) Proceedings of the National Academy of Sciences, USA, 83, pp. 4204-4208; Makino, S., Shieh, C., Keck, J.G., Lai, M.M.C., Defective-interfering particles of murine coronavirus: Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Makino, S., Yokomori, K., Lai, M.M.C., Analysis of efficiently packaged defective Interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal (1990) Journal of Virology, 64, pp. 6045-6053; Maruyama, I.N., Rakow, T.L., Maruyama, H.I., cRACE: A simple method for identification of the 5′ end of mRNAs (1995) Nucleic Acids Research, 23, pp. 3796-3797; Matzura, O., Wennborg, A., RNAdraw: An integrated program for RNA secondary structure calculation and analysis under 32-bit Microsoft Windows (1996) Computer Applications in the Biosciences, 12, pp. 247-249; Mendez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Nicholas, K.B., Nicholas H.B., Jr., (1997) GeneDoc: A Tool for Editing and Annotating Multiple Sequence Alignments, 2.4.002 Edn, , http://www.cris.com/~ketchup/genedoc.html, Distributed by author; Niesters, H.G.M., Lenstra, J.A., Spaan, W.J.M., Zijderveld, A.J., Bleumink-Pluym, N.M.C., Hong, F., Van Scharrenburg, G.J.M., Van Der Zeijst, B.A.M., The peplomer protein sequence of the M41 strain of coronavirus IBV and its comparison with Beaudette strains (1986) Virus Research, 5, pp. 253-263; Pénzes, Z., (1995) Defective Replicating RNAs of Coronavirus Infectious Bronchitis Virus: Investigation of Replication and Genome Packaging Signals, , PhD thesis, University of Hertfordshire, UK; Pénzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Pénzes, Z., Wroe, C., Brown, T.D., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) Journal of Virology, 70, pp. 8660-8668; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) Journal of Virology, 64, pp. 1050-1056; Siddell, S.G., The Coronaviridae (1995) The Coronaviridae, pp. 1-10. , Edited by S. G. Siddell. New York: Plenum; Stern, D.F., Kennedy, S.I.T., Coronavirus multiplication strategy. I. Identification and characterization of virus-specific RNA (1980) Journal of Virology, 34, pp. 665-674; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The Clustal X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Research, 25, pp. 4876-4882; Van Der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , Edited by S. G. Siddell. New York: Plenum; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) Journal of Virology, 65, pp. 3219-3226; Zuker, M., Computer prediction of RNA structure (1989) Methods in Enzymology, 180, pp. 262-288; Zuker, M., On finding all suboptimal foldings of an RNA molecule (1989) Science, 244, pp. 48-52; Zuker, M., Stiegler, P., Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information (1981) Nucleic Acids Research, 9, pp. 133-148","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berks. RG20 7NN, United Kingdom; email: paul.britton@bbsrc.ac.uk",,"Society for General Microbiology",00221317,,JGVIA,"10675417","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033956460
"Kiss I., Kecskeméti S., Tanyi J., Klingeborn B., Belák S.","6603849862;6603764465;6603437628;35611673800;56053373800;","Preliminary studies on feline coronavirus distribution in naturally and experimentally infected cats",2000,"Research in Veterinary Science","68","3",,"237","242",,23,"10.1053/rvsc.1999.0368","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033944049&doi=10.1053%2frvsc.1999.0368&partnerID=40&md5=d9408593133d5bfc86fc321fa9c3f2d5","Veterinary Institute of Debrecen, Box 51, H-4002 Debrecen, Hungary; Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","Kiss, I., Veterinary Institute of Debrecen, Box 51, H-4002 Debrecen, Hungary; Kecskeméti, S., Veterinary Institute of Debrecen, Box 51, H-4002 Debrecen, Hungary; Tanyi, J., Veterinary Institute of Debrecen, Box 51, H-4002 Debrecen, Hungary; Klingeborn, B., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Belák, S., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","The shedding, tissue distribution and quasispecies composition of feline coronaviruses were studied in naturally and experimentally infected cats. The infection remained subclinical, but the majority of the animals shed the virus via faeces throughout the experiment. Sequences corresponding to the viral nucleocapsid region were amplified by reverse-transcription polymerase chain reaction from the cortex, dura mater, pancreas, lungs, third eyelid, and the heart muscle in four cases. Interestingly, the ORF7b viral region - a supposed virulence factor - was detected in fewer organs, raising the possibility that this region can be affected by deletions during virus replication in vivo. It is demonstrated that the composition of the viral quasispecies differs between organs, and that genomic regions with different functions undergo distinct processes of selection, which should be considered during the evolution of feline coronaviruses.",,"nucleocapsid protein; virulence factor; animal experiment; article; brain cortex; cat disease; Coronavirus; dura mater; eyelid; female; heart muscle; lung; male; nonhuman; pancreas; reverse transcription polymerase chain reaction; single strand conformation polymorphism; tissue distribution; virus genome; virus infection; virus replication; virus shedding","Baric, R.S., Fu, K.F., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map of murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Belák, S., Ballagi-Pordány, A., Experiences on the application of the polymerase chain reaction in a diagnostic laboratory (1993) Molecular and Cellular Probes, 7, pp. 241-248; Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-Van Dillen, P.M.E., Van Der Nooredaa, J., Rapid and simple method for purification of nucleic acid (1990) Journal of Clinical Microbiology, 28, pp. 495-503; Cheung, R.C., Matsui, S., Greenberg, H., Rapid and sensitive method for detection of hepatitis C virus RNA by using silica particles (1994) Journal of Clinical Microbiology, 32, pp. 2593-2597; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Siddell, S.G. (ed.). Plenum Press, New York, N.Y; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van Der Zeijst, B.A., Intracellular RNAs of the feline infectious peritonitis virus strain 791146 (1987) Journal of General Virology, 68, pp. 995-1002; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A., Horzinek, M.C., Lutz, H., Placebo-controlled evaluation of a modified life virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions (1997) Vaccine, 15, pp. 1101-1109; Foley, J.F., Poland, A., Carlson, J., Pedersen, N.C., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) Journal of the American Veterinary Medical Association, 210, pp. 1313-1318; Foley, J.F., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) Journal of the American Veterinary Medical Association, 210, pp. 1307-1312; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) Journal of the American Veterinary Medical Association, 209, pp. 1117-1120; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 662-1631; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) Journal of Virology, 72, pp. 4508-4514; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronaviruses (1991) Archives of Virology, 117, pp. 85-95; Hohdatsu, T., Sasamoto, T., Okada, S., Koyama, H., Antigenic analysis of feline coronaviruses with monoclonal antibodies (Mabs): Preparation of Mabs which discriminate between FIPV strain 79-1146 and FECV strain 79-1683 (1991) Veterinary Microbiology, 28, pp. 13-24; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) Journal of Veterinary Medical Science, 54, pp. 557-562; Holland, J.J., De La Torre, J.C., Steinhauer, D.A., RNA virus populations as quasispecies (1992) Current Topics in Microbiology and Immunology, 176, pp. 1-20; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Seminars in Virology, 7, pp. 381-388; Lázaro, C., Estivill, X., Mutation analysis of genetic diseases by asymmetric-PCR SSCP and ethidium bromide staining: Application to neurofibromatosis and cystic fibrosis (1992) Molecular and Cellular Probes, 6, pp. 357-359; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , Siddell, S.G. (ed.), Plenum Press, New York. N.Y; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) Journal of Virology, 57, pp. 729-739; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Veterinary Microbiology, 36, pp. 1-37; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1987) Feline Practice, 23, pp. 7-22; Pedersen, N.C., Boyle, J.E., Floyd, K., Fudge, A., Barker, J., An enteric coronavirus infection of cats and its relationship to feline infectious peritonitis (1981) American Journal of Veterinary Research, 42, pp. 368-377; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) Journal of Clinical Microbiology, 34, pp. 3180-3184; Vennema, H., De Groot, R., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) Journal of Virology, 64, pp. 1407-1409; Vennema, H., De Groot, R.J., Harbour, D.A., Horzinek, M.C., Spaan, W.J., Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens (1991) Virology, 181, pp. 327-335; Vennema, H., Rossen, W.A., Wesseling, J., Horzinek, M.C., Rottier, P.J.M., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157","Belak, S.; Department of Virology, The National Veterinary Institute, Biomedical Center, Box 585, S-751 23 Uppsala, Sweden; email: Sandor.Belak@bmc.uu.se",,"British Veterinary Association",00345288,,RVTSA,"10877969","English","Res. Vet. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0033944049
"Evans S., Cavanagh D., Britton P.","7402709581;26642890500;57203302770;","Utilizing fowlpox virus recombinants to generate defective RNAs of the coronavirus infectious bronchitis virus",2000,"Journal of General Virology","81","12",,"2855","2865",,13,"10.1099/0022-1317-81-12-2855","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034529246&doi=10.1099%2f0022-1317-81-12-2855&partnerID=40&md5=6cc96d563dcf2f5f38637613ed990a5b","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Evans, S., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Coronavirus defective RNAs (D-RNAs) have been used as RNA vectors for the expression of heterologous genes and as vehicles for reverse genetics by modifying coronavirus genomes by targetted recombination. D-RNAs based on the avian coronavirus infectious bronchitis virus (IBV) D-RNA CD-61 have been rescued (replicated and packaged into virions) in a helper virus-dependent manner following electroporation of in vitro-generated T7 transcripts into IBV-infected cells. In order to increase the efficiency of rescue of IBV D-RNAs, cDNAs based on CD-61, under the control of a T7 promoter, were integrated into the fowlpox virus (FPV) genome. The 3'-UTR of the D-RNAs was flanked by a hepatitis delta antigenomic ribozyme and T7 terminator sequence to generate suitable 3' ends for rescue by helper IBV. Cells were co-infected simultaneously with IBV, the recombinant FPV (rFPV) containing the D-RNA sequence and a second rFPV expressing T7 RNA polymerase for the initial expression of the D-RNA transcript, subsequently rescued by helper IBV. Rescue of rFPV-derived CD-61 occurred earlier and with higher efficiency than demonstrated previously for electroporation of in vitro T7-generated RNA transcripts in avian cells. Rescue of CD-61 was also demonstrated for the first time in mammalian cells. The rescue of rFPV-derived CD-61 by M41 helper IBV resulted in leader switching, in which the Beaudette-type leader sequence on CD-61 was replaced with the M41 leader sequence, confirming that helper IBV virus replicated the rFPV-derived D-RNA. An rFPV-derived D-RNA containing the luciferase gene under the control of an IBV transcription-associated sequence was also rescued and expressed luciferase on serial passage.",,"complementary DNA; hepatitis delta antigen; luciferase; ribozyme; RNA polymerase; signal peptide; virus RNA; 3' untranslated region; animal cell; article; Avian infectious bronchitis virus; bacteriophage T7; chicken; controlled study; Coronavirus; defective virus; DNA integration; electroporation; Fowlpox virus; helper virus; in vitro study; kidney cell; nonhuman; priority journal; promoter region; regulator gene; RNA replication; RNA sequence; Vero cell; virion; virus genome; virus infection; virus recombinant; virus recombination","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1987), Current Protocols in Molecular Biology. 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Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034529246
"Seybert A., Van Dinten L.C., Snijder E.J., Ziebuhr J.","7004923617;6602437997;7006058325;7003783935;","Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases",2000,"Journal of Virology","74","20",,"9586","9593",,54,"10.1128/JVI.74.20.9586-9593.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033818909&doi=10.1128%2fJVI.74.20.9586-9593.2000&partnerID=40&md5=d1e1670834f6f278cae05ad1c91823dc","Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany","Seybert, A., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Van Dinten, L.C., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Snijder, E.J., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany","The arterivirus equine arteritis virus nonstructural protein 10 (nsp10) has previously been predicted to contain a Zn finger structure linked to a superfamily 1 (SF1) helicase domain. A recombinant form of nsp10, MBP-nsp10, was produced in Escherichia coli as a fusion protein with the maltose-binding protein. The protein was partially purified by affinity chromatography and shown to have ATPase activity that was strongly stimulated by poly(dT), poly(U), and poly(dA) but not by poly(G). The protein also had both RNA and DNA duplex-unwinding activities that required the presence of 5' single-stranded regions on the partial-duplex substrates, indicating a 5'-to-3' polarity in the unwinding reaction. Results of this study suggest a close functional relationship between the arterivirus nsp10 and the coronavirus helicase, for which NTPase and duplex-unwinding activities were recently demonstrated. In a number of biochemical properties, both arterivirus and coronavirus SF1 helicases differ significantly from the previously characterized RNA virus SF1 and SF2 enzymes. Thus, the combined data strongly support the idea that nidovirus helicases may represent a separate group of RNA virus-encoded helicases with distinct properties.",,"adenosine triphosphatase; double stranded DNA; double stranded RNA; helicase; maltose binding protein; zinc finger protein; Arterivirus; article; Coronavirus; enzyme chemistry; enzyme mechanism; Equine viral arteritis virus; nonhuman; priority journal; RNA synthesis; Adenosinetriphosphatase; Arterivirus; Carrier Proteins; Coronavirus; DNA Helicases; DNA, Viral; GTP Phosphohydrolases; Recombinant Fusion Proteins; RNA Helicases; RNA, Viral; Sodium Chloride; Support, Non-U.S. Gov't; Viral Nonstructural Proteins; Zinc Fingers","Bayliss, C.D., Smith, G.L., Vaccinia virion protein I8R has both DNA and RNA helicase activities: Implications for vaccinia virus transcription (1996) J. Virol., 70, pp. 794-800; Bird, L.E., Subramanya, H.S., Wigley, D.B., Helicases: A unifying structural theme? (1998) Curr. Opin. Struct. 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Virol., 81, pp. 853-879","Ziebuhr, J.; Institute of Virology and Immunology, University of Wurzburg, Versbacher Str. 7, 97078 Wurzburg, Germany; email: ziebuhr@vim.uni-wuerzburg.de",,,0022538X,,JOVIA,"11000230","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033818909
"Cowley J.A., Dimmock C.M., Spann K.M., Walker P.J.","7102947876;7004237605;7003711237;7403666485;","Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses",2000,"Journal of General Virology","81","6",,"1473","1484",,111,"10.1099/0022-1317-81-6-1473","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034093105&doi=10.1099%2f0022-1317-81-6-1473&partnerID=40&md5=1277c150d82d0766b0616fbebb376308","Co-Oper. Res. Centre for Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, PMB3, Indooroopilly, QLD 4068, Australia","Cowley, J.A., Co-Oper. Res. Centre for Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, PMB3, Indooroopilly, QLD 4068, Australia; Dimmock, C.M., Co-Oper. Res. Centre for Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, PMB3, Indooroopilly, QLD 4068, Australia; Spann, K.M., Co-Oper. Res. Centre for Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, PMB3, Indooroopilly, QLD 4068, Australia; Walker, P.J., Co-Oper. Res. Centre for Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, PMB3, Indooroopilly, QLD 4068, Australia","A 20089 nucleotide (nt) sequence was determined for the 5' end of the (+)-ssRNA genome of gill-associated virus (GAV), a yellow head-like virus infecting Penaeus monodon prawns. Clones were generated from a ~ 22 kb dsRNA purified from lymphoid organ total RNA of GAV-infected prawns. The region contains a single gene comprising two long overlapping open reading frames, ORF1a and ORF1b, of 4060 and 2646 amino acids, respectively. The ORFs are structurally related to the ORF1a and ORF1ab polyproteins of coronaviruses and arteriviruses. The 99 nt overlap between ORF1a and ORF1b contains a putative AAAUUUU 'slippery' sequence associated with - 1 ribosomal frameshifting. A 131 nt stem-loop with the potential to form a complex pseudoknot resides 3 nt downstream of this sequence. Although different to the G/UUUAAAC frameshift sites and 'H-type' pseudoknots of nidoviruses, in vitro transcription/translation analysis demonstrated that the GAV element also facilitates read-through of the ORF1a/1b junction. As in coronaviruses, GAV ORF1a encodes a 3C-like cysteine protease domain located between two hydrophobic regions. However, its sequence suggests some structural relationship to the chymotrypsin-like serine proteases of arteriviruses. ORF1b encodes homologues of the 'SDD' polymerase, which among (+)-RNA viruses is unique to nidoviruses, as well as metal-ion-binding and helicase domains. The presence of a dsRNA replicative intermediate and ORF1a and ORF1ab polyproteins translated by a - 1 frameshift suggests that GAV represents the first invertebrate member of the Order Nidovirales.",,"amino acid; chymotrypsin; cysteine proteinase; helicase; metal ion; nucleotide; serine proteinase; virus protein; virus RNA; Arterivirus; article; controlled study; Coronavirus; gene structure; genetic code; genetic transcription; gill; hydrophobicity; in vitro study; invertebrate; metal binding; molecular cloning; nonhuman; nucleotide sequence; open reading frame; priority journal; ribosomal frameshifting; RNA translation; virus gene; Arbovirus; Arterivirus; Coronavirus; Decapoda (Crustacea); Gill-associated virus; Invertebrata; Monodon; Nidovirales; Penaeus monodon; Penaeus monodon; RNA viruses","Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Research, 25, pp. 3389-3402; 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Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Detection of Australian gill-associated virus (GAV) and lymphoid organ virus (LOV) of Penaeus monodon by RT-nested PCR (2000) Diseases of Aquatic Organisms, , in press; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arterivirus is not a togavirus but belongs to the coronavirus-like superfamily (1991) Journal of Virology, 65, pp. 2910-2920; De Vries, A.A.F., Chirnside, E.D., Bredenbeek, P.J., Gravestein, L.A., Horzinek, M.C., Spaan, W.J.M., All subgenomic mRNAs of equine arteritis virus contain a common leader sequence (1990) Nucleic Acids Research, 18, pp. 3241-3247; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Dumas, J.B., Edwards, M., Delort, J., Mallet, J., Oligodeoxynucleotide ligation of single-stranded cDNAs: A new tool for cloning 5′ ends of mRNAs and for constructing cDNA libraries by in vitro amplification (1991) Nucleic Acids Research, 19, pp. 5227-5232; 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Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Hodgman, T.C., A new superfamily of replicative proteins (1988) Nature, 333, pp. 22-23; Jacks, T., Madhani, H.D., Masiarz, F.R., Varmus, H.E., Signals for ribosomal frameshifting in the Rous sarcoma virus gag - Pol region (1988) Cell, 55, pp. 447-458; Koonin, E.V., The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses (1991) Journal of General Virology, 72, pp. 2197-2206; Kozak, M., Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes (1986) Cell, 44, pp. 283-292; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annual Review of Microbiology, 44, pp. 303-333; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Lai, M.M.C., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proceedings of the National Academy of Sciences, USA, 81, pp. 3626-3630; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Limsuwan, C., (1991) Handbook for Cultivation of Black Tiger Prawns, , Bangkok: Tansetakit Co. Ltd; Loh, P.C., Tapay, L.M., Lu, Y., Nadala E.C.B., Jr., Viral pathogens of the penaeid shrimp (1997) Advances in Virus Research, 48, pp. 263-312; Meulenberg, J.J., Hulst, M.M., De Meijer, E.J., Moonen, P.L.J.M., Den Besten, A., De Kluyver, E.P., Wensvoort, G., Moormann, R.J.M., Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS), is related to LDV and EAV (1993) Virology, 192, pp. 62-72; Nadala, E.C.B., Tapay, L.M., Loh, P.C., Yellow-head virus: A rhabdovirus-like pathogen of penaeid shrimp (1997) Diseases of Aquatic Organisms, 31, pp. 141-146; Patel, P.H., Preston, B.D., Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends (1994) Proceedings of the National Academy of Sciences, USA, 91, pp. 549-553; Peliska, J.A., Benkovic, S.J., Mechanism of DNA strand transfer reactions catalysed by HIV-1 reverse transcriptase (1992) Science, 258, pp. 1112-1118; Pleij, C.W.A., Bosch, L., RNA pseudoknots: Structure, detection, and prediction (1989) Methods in Enzymalogy, 180, pp. 289-303; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; Shieh, C.K., Soe, L.H., Makino, S., Chang, M.F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genome: Implications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Snijder, E.J., Spaan, W.J.M., The coronaviruslike superfamily (1995) The Coronaviridae, pp. 239-255. , Edited by S. G. Siddell. New York: Plenum Press; Snijder, E.J., Den Boon, J.A., Bredenbeek, P.J., Horzinek, M.C., Rijnbrand, R., Spaan, W.J.M., The carboxyl-terminal part of the putative Berne virus polymerase is expressed by ribosomal frameshifting and contains sequence motifs which indicate that toro- and coronaviruses are evolutionarily related (1990) Nucleic Acids Research, 18, pp. 4535-4542; Snijder, E.J., Horzinek, M.C., Spaan, W.J.M., A 3′-coterminal nested set of independently transcribed mRNAs is generated during Berne virus replication (1990) Journal of Virology, 64, pp. 331-338; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J.M., Characterization of defective interfering Berne virus RNAs (1991) Journal of General Virology, 72, pp. 1635-1643; Snijder, E.J., Wassenaar, A.L.M., Van Dinten, L.C., Spaan, W.J.M., Gorbalenya, A.E., The arterivirus Nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases (1996) Journal of Biological Chemistry, 271, pp. 4864-4871; Sonigo, P., Barker, C., Hunter, E., Wain-Hobson, S., Nucleotide sequence of Mason-Pfizer monkey virus: An immunosuppressive D-type retrovirus (1986) Cell, 45, pp. 375-385; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2952; Spann, K.M., Vickers, J.E., Lester, R.J.G., Lymphoid organ virus of Penaeus monodon from Australia (1995) Diseases of Aquatic Organisms, 23, pp. 127-134; Spann, K.M., Cowley, J.A., Walker, P.J., Lester, R.J.G., Gill-associated virus (GAV), a yellow head-like virus from Penaeus monodon cultured in Australia (1997) Diseases of Aquatic Organisms, 31, pp. 169-179; Tang, K.F.-J., Lightner, D.V., A yellow head virus gene probe: Application to in situ hybridization and determination of its nucleotide sequence (1999) Diseases of Aquatic Organisms, 35, pp. 165-173; Ten Dam, E.B., Pleij, C.W.A., Bosch, L., RNA pseudoknots: Translational frameshifting and readthrough on viral RNAs (1990) Virus Genes, 4, pp. 121-136; Thompson, J.D., Higgins, D.G., Gibson, T.J., Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice (1994) Nucleic Acids Research, 22, pp. 4673-4680; Walker, P.J., Byrne, K.A., Riding, G.A., Cowley, J.A., Wang, Y., McWilliam, S.M., The genome of bovine ephemeral fever rhabdovirus contains two related glycoprotein genes (1992) Virology, 191, pp. 49-61; Walker, P.J., Wang, Y., Cowley, J.A., McWilliam, S.M., Prehaud, C.J.N., Structural and antigenic analysis of the nucleoprotein of bovine ephemeral fever rhabdovirus (1994) Journal of General Virology, 75, pp. 1889-1899; Weiss, M., Steck, F., Horzinek, M.C., Purification and partial characterization of a new enveloped RNA virus (Berne virus) (1983) Journal of General Virology, 64, pp. 1849-1858; Wongteerasupaya, C., Sriurairatana, S., Vickers, J.E., Akrajamorn, A., Boonsaeng, V., Panyim, S., Tassanakajon, A., Flegel, T.W., Yellow-head virus of Penaeus monodon is an RNA virus (1995) Diseases of Aquatic Organisms, 22, pp. 45-50; Zuker, M., On finding all suboptimal foldings of an RNA molecule (1989) Science, 244, pp. 48-52","Cowley, J.A.; Co-operative Res. Ctr. Aquaculture, CSIRO Tropical Agriculture, Long Pocket Laboratories, Indooroopilly, ACT 4068, Australia; email: Jeff.Cowley@tag.csiro.au",,"Society for General Microbiology",00221317,,JGVIA,"10811931","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034093105
"Lathrop S.L., Wittum T.E., Brock K., Loerch S.C., Perino L.J., Bingham H.R., McCollum E.T., Saif L.J.","36836780500;7004009529;7005813632;7004696614;7003801392;7007070595;57213954709;7102226747;","Association between infection of the respiratory tract attributable to bovine coronavirus and health and growth performance of cattle in feedlots",2000,"American Journal of Veterinary Research","61","9",,"1062","1066",,49,"10.2460/ajvr.2000.61.1062","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034277092&doi=10.2460%2fajvr.2000.61.1062&partnerID=40&md5=379af3b1460193af981666551b8dd2f8","Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Department of Animal Science, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Department of Pathobiology, College of Veterinary Medicine, Auburn University, Auburn, AL 36849, United States; Division of Agriculture, West Texas A and M University, Canyon, TX 79106, United States; Texas A and M Res. and Exten. Center, Amarillo, TX 79106, United States","Lathrop, S.L., Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States, Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Brock, K., Department of Pathobiology, College of Veterinary Medicine, Auburn University, Auburn, AL 36849, United States; Loerch, S.C., Department of Animal Science, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Perino, L.J., Division of Agriculture, West Texas A and M University, Canyon, TX 79106, United States; Bingham, H.R., Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; McCollum, E.T., Texas A and M Res. and Exten. Center, Amarillo, TX 79106, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States, Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States","Objective - To determine the association between respiratory tract infection with bovine coronavirus (BCV), treatment for respiratory tract disease, pulmonary lesions at slaughter, and average daily gain in cattle in feedlots. Animals - 837 calves in feedlots in Ohio and Texas. Procedure - Nasal swab specimens were obtained from cattle at arrival in a feedlot (day 0) and at various times during the initial 28 days after arrival. Specimens were tested for BCV, using an antigen-capture ELISA. Serum samples were obtained at arrival and again 28 days after arrival and tested for antibodies to BCV, using an antibody-detection ELISA. Information was collected regarding treatment for cattle with respiratory tract disease and average daily gain during the feeding period. Pulmonary lesions were evaluated at slaughter. Results - Cattle shedding BCV from the nasal cavity and developing an antibody response against BCV were 1.6 times more likely to require treatment for respiratory tract disease than cattle that did not shed the virus or develop an immune response against BCV. Additionally, cattle that shed BCV from the nasal cavity were 2.2 times more likely to have pulmonary lesions at slaughter than cattle that did not shed the virus. The BCV shedding or seroconversion status did not affect average daily gain. Conclusions and Clinical Relevance - Bovine coronavirus infects feedlot cattle and is associated with an increased risk for cattle developing respiratory tract disease and pulmonary lesions. Development of appropriate control measures could help reduce the incidence of respiratory tract disease. (Am J Vet Res 2000;61:1062-1066).",,"animal; animal disease; article; cattle; cattle disease; enzyme linked immunosorbent assay; lung; nose cavity; pathology; pathophysiology; respiratory tract infection; virology; virus infection; Animals; Cattle; Cattle Diseases; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Lung; Nasal Cavity; Respiratory Tract Infections","Saif, L.J., Heckert, R., Enteropathogenic coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , Saif LJ, Theil KW, eds. Boca Raton, Fla: CRC Press; Stair, E.L., Rhodes, M.B., White, R.G., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am J Vet Res, 33, pp. 1147-1156; Mebus, C.A., Stair, E.L., Rhodes, M.B., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of coronavirus-like agents (1973) Am J Vet Res, 34, pp. 145-150; Heckert, R.A., Saif, L.J., Hoblet, K.H., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in 2 herds in Ohio (1990) Vet Microbiol, 22, pp. 187-201; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; McNulty, M.S., Bryson, D.G., Allan, G.M., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-434; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Thomas, L.H., Gourlay, R.N., Stott, E.J., A search for new microorganisms in calf pneumonia by the inoculation of gnotobiotic calves (1982) Res Vet Sci, 33, pp. 170-182; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Antibody titers against bovine coronavirus and shedding of the virus via the respira-tory tract in feedlot cattle (2000) Am J Vet Res, 61, pp. 1049-1053; Wittum, T.E., Woollen, N.E., Perino, L.J., Relationships among treatment for respiratory tract disease, pulmonary lesions evident at slaughter, and rate of weight gain in feedlot cattle (1996) J Am Vet Med Assoc, 209, pp. 814-818; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Hasoksuz, M., Lathrop, S., Gadfield, K., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biologic and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Smith, D.R., Nielsen, P.R., Gadfield, K.L., Further validation of antibody-capture and antigen-capture enzyme-linked immunosorbent assays for determining exposure of cattle to bovine coronavirus (1998) Am J Vet Res, 59, pp. 956-960; Martin, S.W., Nagy, E., Shewen, P.E., The association of titers to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261","Saif, L.J.; Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States",,"American Veterinary Medical Association",00029645,,AJVRA,"10976737","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0034277092
"Lathrop S.L., Wittum T.E., Loerch S.C., Perino L.J., Saif L.J.","36836780500;7004009529;7004696614;7003801392;7102226747;","Antibody titers against bovine coronavirus and shedding of the virus via the respiratory tract in feedlot cattle",2000,"American Journal of Veterinary Research","61","9",,"1057","1061",,38,"10.2460/ajvr.2000.61.1057","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034276545&doi=10.2460%2fajvr.2000.61.1057&partnerID=40&md5=46d5a8468d47e6ca216e57ec65bd3ca6","Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Department of Animal Science, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Division of Agriculture, West Texas A and M University, Canyon, TX 79106, United States","Lathrop, S.L., Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States, Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Loerch, S.C., Department of Animal Science, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States; Perino, L.J., Division of Agriculture, West Texas A and M University, Canyon, TX 79106, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States, Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States","Objective - To describe patterns of seroconversion to bovine coronavirus (BCV) and shedding of BCV from the respiratory tract in feedlot cattle. Animals - 1,074 calves in feedlots in Ohio, Texas, and Nebraska. Procedure - Nasal swab specimens were obtained at time of arrival (day 0) and at various times during the initial 28 days after arrival at feedlots. Specimens were tested for BCV, using an antigen-capture ELISA. Serum samples were obtained at time of arrival and again 28 days after arrival; sera were analyzed for antibodies to BCV, using an antibody-detection ELISA. Results - Samples from 12 groups of cattle entering 7 feedlots during a 3-year period revealed that 78 of 1,074 (7.3%) cattle were shedding BCV (range, O to 35.9% within specific groups). At time of arrival, 508 of 814 (62.4%) cattle had low (< 50) or undetectable BCV antibody titers. Seroconversion to BCV during the initial 28 days after arrival was detected in 473 of 814 (58%) cattle tested (range, 20.3 to 84.1% within specific groups). In cattle shedding BCV from the nasal passages, 49 of 68 (72.1%) seroconverted, and 472 of 746 (63.3%) cattle that were not shedding the virus seroconverted. Conclusions and Clinical Relevance - Bovine coronavirus can be detected in populations of feedlot cattle in the form of viral shedding as well as seroconversion to the virus. Although only a few cattle were shedding the virus at the time of arrival at a feedlot, most of the cattle seroconverted to BCV by 28 days after arrival. (Am J Vet Res 2000;61:1057-1061).",,"animal; animal disease; article; cattle; cattle disease; Coronavirus; disease transmission; enzyme linked immunosorbent assay; isolation and purification; respiratory system; serodiagnosis; virology; virus infection; virus shedding; Animals; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Disease Transmission, Vertical; Enzyme-Linked Immunosorbent Assay; Neutralization Tests; Respiratory System; Virus Shedding","Rosenquist, B.D., Viruses as etiologic agents of bovine respiratory disease (1984) Bovine Respiratory Disease - a Symposium, pp. 363-376. , Loan RW, ed. College Station, Tex: Texas AM University Press; Thomson, R.G., Pathology and pathogenesis of the common disease of the respiratory tract of cattle (1974) Can Vet J, 15, pp. 249-251; Dyer, R.M., The bovine respiratory disease complex: Infectious agents (1981) Compend Contin Educ Pract Vet, 3, pp. S374-S382; Frank, G.H., Bacteria as etiologic agents in bovine respiratory disease (1984) Bovine Respiratory Disease - a Symposium, pp. 347-362. , Loan RW, ed. College Station, Tex: Texas A&M University Press; (1995) Cattle on Feed Evaluation, pp. 1-20. , Fort Collins. CO: APHIS-National Animal Health Monitoring System; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Lathrop, S.L., Wittum, T.E., Brock, K.V., Association between infection of the respiratory tract attributable to bovine coronavirus and health and growth performance of cattle in feedlots (2000) Am J Vet Res, 61, pp. 1054-1058; Hasoksuz, M., Lathrop, S., Gadfield, K., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Smith, D.R., Nielsen, P.R., Gadfield, K.L., Further validation of antibody-capture and antigen-capture enzyme-linked immunosorbent assays for determining exposure of cattle to bovine coronavirus (1998) Am J Vet Res, 59, pp. 956-960; Saif, L.J., Heckert, R.A., Miller, K.L., Cell culture propagation of bovine coronavirus (1988) J Tissue Cult Methods, 11, pp. 139-145; Martin, S.W., Nagy, E., Shewen, P.E., The association of titers to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261; Ribble, C.S., Meek, A.H., Shewen, P.E., Effect of pretransit mixing on fatal fibrinous pneumonia in calves (1995) J Am Vet Med Assoc, 207, pp. 616-619; Martin, S.W., Bateman, K.G., Shewen, P.E., The frequency, distribution, and effects of antibodies, to seven putative respiratory pathogens, on respiratory disease and weight gain in feedlot calves in Ontario (1989) Can J Vet Res, 53, pp. 355-362; Martin, S.W., Bateman, K.G., Shewen, P.E., A group-level analysis of the associations between antibodies to seven putative pathogens and respiratory disease and weight gain in Ontario feedlot calves (1990) Can J Vet Res, 54, pp. 337-342","Saif, L.J.; Food Animal Health Research Program, Ohio Agric. R. and D. Center (OARDC), Ohio State University, Wooster, OH 44691-4096, United States",,"American Veterinary Medical Association",00029645,,AJVRA,"10976736","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0034276545
"Pratelli A., Buonavoglia D., Martella V., Tempesta M., Lavazza A., Buonavoglia C.","7004884960;7004335810;7003300496;7005599031;35339480400;7005623145;","Diagnosis of canine coronavirus infection using nested-PCR",2000,"Journal of Virological Methods","84","1",,"91","94",,29,"10.1016/S0166-0934(99)00134-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033990760&doi=10.1016%2fS0166-0934%2899%2900134-2&partnerID=40&md5=0090daf0034280af2067b3002af8748f","Dept. of Health and Animal Welfare, Fac. Vet. Med., Strada per C., Bari, Italy; Institute of Infectious Diseases, Faculty of Veterinary Medicine, Messina, Italy; Istituto Zooprofilattico, Brescia, Italy","Pratelli, A., Dept. of Health and Animal Welfare, Fac. Vet. Med., Strada per C., Bari, Italy; Buonavoglia, D., Institute of Infectious Diseases, Faculty of Veterinary Medicine, Messina, Italy; Martella, V., Dept. of Health and Animal Welfare, Fac. Vet. Med., Strada per C., Bari, Italy; Tempesta, M., Dept. of Health and Animal Welfare, Fac. Vet. Med., Strada per C., Bari, Italy; Lavazza, A., Istituto Zooprofilattico, Brescia, Italy; Buonavoglia, C., Dept. of Health and Animal Welfare, Fac. Vet. Med., Strada per C., Bari, Italy","The results of polymerase chain reaction (PCR) and nested polymerase chain reaction (n-PCR) assays for the diagnosis of canine coronavirus (CCV) infection, and the comparison with other diagnostic techniques, such as electron microscopy (EM) and virus isolation using A-72 cell line are reported. The study was carried out on 71 faecal samples of pups with enteritis. Of 71 samples examined 14 were positive in PCR, whereas 30 samples resulted positive in the n-PCR assay. CCV was detected by EM examination in only four out of 45 samples, and by virus isolation in three out of 30 samples n-PCR positive.","Canine coronavirus; Diagnosis; Nested-polymerase chain reaction","article; coronavirus; dog; electron microscopy; feces analysis; nonhuman; polymerase chain reaction; priority journal; virus infection; virus isolation; Animals; Base Sequence; Coronavirus Infections; Coronavirus, Canine; DNA Primers; Dog Diseases; Dogs; Feces; Gastroenteritis; Microscopy, Electron; Polymerase Chain Reaction; Sensitivity and Specificity; Virology; Canine coronavirus; Canis familiaris; Coronavirus; RNA viruses","Appel, M.J., Canine coronavirus (1987) Virus Infections of Vertebrates, pp. 115-122. , in: Appel, M.J. (Ed.), Virus Infections of Carnivores, in: Horzinek, M.C., (Ed.), Elsevier Science, Amsterdam; Athanssious, R., Marsolais, G., Assaf, R., Dea, S., Descoteaux, J.P., Dulude, S., Montpetit, C., Detection of bovine coranavirus and type A rotavirus in neonatal calf diarrhea and winter dyssentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can. Vet. J., 35, pp. 163-169; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, B.S., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proceedings of the Seventy Eight Annual Meeting of the USAHA, pp. 359-366; Herrewegh, A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72 (5), pp. 4508-4514; Hyatt, A.D., The application of electron microscopy to veterinary virus diagnosis (1989) Aust. Vet. J., 66, pp. 445-449; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: studies by virologic, histologic, histochemical, and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Mochizuchi, M., Viruses isolated from feces of dogs and cats in Japan (1998) First International Meeting of Virology of Carnivores, pp. 58-59. , Utrecht, The Netherlands 13-15 May; Naeem, K., Goyal, S.M., Comparison of virus isolation immunofluorescence and electron microscopy for diagnosis of animal viruses (1988) Microbiologica, 11, pp. 355-362; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR assay for the detection of canine coronavirus (1999) J. Virol. Meth., 80, pp. 11-18; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Vet. Microbiol., 42, pp. 255-259; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Gaskell, C.J., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18","Buonavoglia, C.; Dept. of Health and Animal Welfare, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70 010 Valenzano, Bari, Italy; email: c.buonavoglia@veterinaria.uniba.it",,,01660934,,JVMED,"10644090","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0033990760
"Lin X.Q., Chouljenko V.N., Kousoulas K.G., Storz J.","36768282000;6603655227;7003476092;7006694594;","Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses",2000,"Journal of Medical Microbiology","49","12",,"1119","1127",,5,"10.1099/0022-1317-49-12-1119","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033662425&doi=10.1099%2f0022-1317-49-12-1119&partnerID=40&md5=a382f519b5c38ab6d33ff3ddfeb2db13","Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Lin, X.Q., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Chouljenko, V.N., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Kousoulas, K.G., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Storz, J., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Numerous respiratory bovine coronaviruses (RBCV) were isolated recently from nasal swab samples and lung tissues of feedlot cattle with acute respiratory tract disease. These newly emerging RBCV isolates exhibited distinct phenotypic features that differentiated them from enteropathogenic bovine coronaviruses (EBCV). The RBCV strains had a receptor-destroying enzyme function mediated by acetylesterase (AE) activity of the haemagglutinin-esterase (HE) glycoprotein. The HE genes of wild-type EBCV strain LY138 and RBCV strains OK-0514 (OK) and LSU-94LSS-051 (LSU) were cloned, sequenced and transiently expressed in COS-7 cells. The enzymic properties of HE proteins in COS-7 cellular extracts and in purified virus preparations were assayed at room temperature, 37°C and 39°C by two different assays. One assay used ρ-nitrophenyl acetate (PNPA) as substrate and detected serine-esterase activity; the second assay monitored AE function with bovine submaxillary mucin (BSM) as substrate. The PNPA tests confirmed that HE proteins of EBCV and RBCV were functionally expressed in transfected COS-7 cells. Time-dependent determination of the AE activity of purified RBCV OK and LSU particles showed lower AE activity at 39°C than at 37°C, whereas the purified EBCV LY particles retained full AE activity at both 37°C and 39°C. Transiently expressed RBCV HE exhibited a marked reduction of AE activity after 40 min of assay time at 37°C. In contrast, the AE activity of the transiently expressed EBCV HE remained stable beyond 40 min. The deduced amino-acid sequences of the HE proteins specified by the RBCV strains OK and LSU contained specific amino-acid changes in comparison with the EBCV LY strain, which may be responsible for the observed enzymic differences. These results are consistent with the hypothesis that RBCV strains have evolved to selectively replicate in respiratory tissues and that HE may play a role in this tissue tropism.",,"acetylesterase; esterase; glycoprotein; mucin; virus hemagglutinin; virus receptor; acute respiratory tract disease; amino acid sequence; animal cell; article; cattle; cell strain COS1; Coronavirus; enzyme activity; lung parenchyma; nonhuman; nose smear; priority journal; temperature sensitivity; virus expression; virus isolation; virus strain","Spaan, W., Cavanagh, D., Horzinek, M.C., Coronavirus: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995), pp. 165-179. , Siddell SG (ed) The Coronaviridae. New York, Plenum Press; Brown, T.D.K., Brierley, I., The coronavirus nonstructural proteins (1995), pp. 191-217. , Siddell SG (ed) The Coronaviridae. New York, Plenum Press; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-2877; Hogue, B.G., Kienzle, T.E., Brian, D.A., Synthesis and processing of the bovine enteric coronavirus haemagglutinin protein (1989) J Gen Virol, 70, pp. 345-352; Herrler, G., Durkop, I., Becht, H., Klenk, H.-D., The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor (1988) J Gen Virol, 69, pp. 839-846; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J Virol, 51, pp. 384-388; King, B., Potts, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Res, 2, pp. 53-59; Strobl, B., Vlasak, R., The receptor-destroying enzyme of influenza C virus is required for entry into target cells (1993) Virology, 192, pp. 679-682; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J Virol, 62, pp. 4686-4690; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529; Vlasak, R., Muster, T., Lauro, A.M., Powers, J.C., Palese, P., Influenza C virus esterase: Analysis of catalytic site, inhibition, and possible function (1989) J Virol, 63, pp. 2056-2062; Herrler, G., Rott, R., Klenk, H.-D., Muller, H.D., Shukla, A.K., Schauer, R., The receptor-destroying enzyme of influenza C virus is neuraminidate-O-acetylesterase (1985) EMBO J, 4, pp. 1503-1506; Herrler, G., Szepanski, S., Schultze, B., 9-O-acetylated sialic acid, a receptor determinant for influenza C virus and coronaviruses (1991) Behring Inst Mitt, 1, pp. 177-184; Hirst, G.K., The relationship of the receptors of a new strain of virus to those of the mumps-NDV-influenza group (1950) J Exp Med, 91, pp. 177-184; Klenk, E., Faillard, H., Lempfrid, H., Uber die enzymatische wirkung von influenza-virus (1955) Z Physiol Chem, 301, pp. 235-246; Herrler, G., Klenk, H.-D., The surface receptor is a major determinant of the cell tropism of influenza C virus (1987) Virology, 159, pp. 102-108; Deregt, D., Gifford, G.A., Ijaz, M.K., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J Gen Virol, 70, pp. 993-998; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-Oacetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J Gen Virol, 73, pp. 901-906; Parker, M.D., Yoo, D., Babiuk, L.A., Expression and secretion of bovine coronavirus haemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses (1990) J Virol, 64, pp. 1625-1629; Yoo, D., Graham, F.L., Prevec, L., Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus (1992) J Gen Virol, 73, pp. 2591-2600; Schultze, B., Gross, H.-J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a haemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Schultze, B., Wahn, K., Klenk, H.-D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Shieh, C.-K., Lee, H.-J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J Virol, 63, pp. 3729-3736; Storz, J., Respiratory disease of cattle associated with coronavirus infections (1999), pp. 291-293. , Howard JL, Smith RA (eds) Current veterinary therapy: Food animal practice 4. Philadelphia, WB Saunders; Storz, J., Lin, X.Q., Purdy, C.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans' criteria for causation (2000) J Clin Microbiol, , in press; Storz, J., Lin, X.Q., Purdy, C.W., Loan, R.W., Novel diagnostics for defining virus infections in shipping fever pneumonia: Emergence of respiratory bovine coronaviruses (1999), pp. 54-60. , Proceedings of the Ninth International Symposium on World Association of Veterinary Laboratory Diagnosticians: College Station, TX, USA; Storz, J., Purdy, C.W., Lin, X.Q., Isolation of respiratory bovine coronavirus, other cytocidal viruses and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J Am Vet Med Assoc, 216, pp. 1599-1604; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Chouljenko, V.N., Kousoulas, K.G., Lin, X.Q., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3' genomic portion (9.5kb) of respiratory bovine corona-viruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Lin, X.Q., Burrell, M., Storz, J., (1995) Haemagglutinin and receptor destroying functions of newly recognized bovine respiratory coronaviruses, , Annual Meeting of American Society for Microbiology - South Central Branch: Little Rock, AK, USA. Abstract 4/27; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 44, pp. 152-161; Storz, J., Rott, R., Distribution of bovine coronavirus infection in selected areas of Germany: Detection of antibodies by microimmunodiffusion and neutralization (1980) DTW Dtsch Tierarztl Wochenschr, 87, pp. 252-254; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol, 169, pp. 169-178; Storz, J., Herrler, G., Snodgrass, D.R., Monoclonal antibodies differentiate between the hemagglutinating and the receptor-destroying activities of bovine coronavirus (1991) J Gen Virol, 72, pp. 2817-2820; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852; Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Gottschalk, A., Neuraminidase: The specific enzyme of influenza virus and Vibrio cholerae (1957) Biochim Biophys Acta, 23, pp. 645-646; Palese, P., Tobita, K., Ueda, M., Compans, R.W., Characterization of temperature sensitive influenza virus mutants defective in neuraminidase (1974) Virology, 61, pp. 397-410; Hausman, J., Kretzschmar, E., Ohuchi, M., Garten, W., Klenk, H.D., N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemagglutinin activity (1993), p. 34. , Proceedings of the Twelfth Annual Meeting of the American Society for Virology: Davis, CA, USA; Laver, W.G., Colman, P.M., Webster, R.G., Hinshaw, V.S., Air, G.M., Influenza virus neuraminidase with haemagglutinin activity (1984) Virology, 137, pp. 314-323; Parker, M.D., Cox, G.J., Deregt, D., Fitzpatrick, D.R., Babuik, L.A., Cloning and in vitro expression of the gene for the E3 haemagglutinin glycoprotein of bovine coronavirus (1989) J Gen Virol, 70, pp. 155-164; Doughri, A.M., Storz, J., Hajer, I., Fernando, H.S., Morphology and morphogenesis of a coronavirus infecting intestinal epithelial cells of newborn calves (1976) Exp Mol Pathol, 25, pp. 355-370; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet Rec, 123, pp. 300-301","Storz, J.; Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",,"Lippincott Williams and Wilkins",00222615,,JMMIA,"11129725","English","J. Med. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0033662425
"Yu M., Ismail M.M., Qureshi M.A., Dearth R.N., Barnes H.J., Saif Y.M.","55475801200;36793864500;7202876162;6701743424;7102581732;35563198200;","Viral agents associated with poult enteritis and mortality syndrome: The role of a small round virus and a turkey coronavirus",2000,"Avian Diseases","44","2",,"297","304",,58,"10.2307/1592543","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034131303&doi=10.2307%2f1592543&partnerID=40&md5=5d9a7be9685f3594a1dd2b9067769efe","Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States; Dept. Farm Anim. Hlth. Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States","Yu, M., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Ismail, M.M., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Qureshi, M.A., Department of Poultry Science, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States; Dearth, R.N., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Barnes, H.J., Dept. Farm Anim. Hlth. Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States; Saif, Y.M., Food Animal Health Research Program, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","Intestinal samples from turkey poults affected with poult enteritis and mortality syndrome (PEMS) were examined for viruses by immune electron microscopy and double-stranded RNA virus genome electropherotyping. Turkey coronavirus (TCV), avian rotaviruses, reovirus, and a yet undefined small round virus (SRV) were detected. The SRV and TCV were isolated and propagated in turkey embryos. Challenge of specific-pathogen-free turkey poults with SRV, TCV, or both resulted in mortality and clinical responses similar to those of natural PEMS. Our experiments indicate that SRV and TCV are possibly important agents in the etiology of PEMS and the combination of these infections might result in outbreaks with high mortality. The severity of clinical signs and mortality of PEMS are postulated to be partly related to the virus agents involved in individual outbreaks.","Poult enteritis and mortality syndrome; Small round virus; Turkey coronavirus","disease detection; double stranded RNA; immunoelectron microscopy; phenotyping; poult enteritis and mortality syndrome; Reovirus; Rotavirus; Small round structured virus; turkey; turkey coronavirus; virus infection; virus RNA; Animalia; Aves; Coronavirus; Reovirus sp.; RNA viruses; Rotavirus; Small round structured virus; Turkey coronavirus","Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry, 10th ed., pp. 1025-1031. , B. W. Calnek., H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Brown, T.P., Glisson, J.R., Villegas, P.V., Acute enteritis as a cause of ""spiking mortality"" in young turkey poults (1992) Proc. 3rd Eli Lilly Turkey Technical Seminar, pp. 20-29. , Nashville, TN. May 8-10; Edens, F.W., Qureshi, R.A., Parkhurst, C.R., Qureshi, M.A., Havenstein, G.B., Casas, I.A., Characterization of two Escherichia coli isolates associated with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 1665-1673; Goodwin, M.A., Brown, J., Player, E.C., Stiffens, W.L., Heroes, D., Deceit, M.A., Fringed membranous particles and viruses in feces from healthy turkey poults and from poults with putative poult enteritis complex/spiking mortality (1995) Avian Pathol., 24, pp. 497-505; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hayhow, C.S., Parwani, A.V., Saif, Y.M., Single-stranded genomic RNA from turkey enterovirus-like virus (1992) Avian Dis., 37, pp. 558-560; Heggen, C.L., Qureshi, M.A., Edens, F.W., Barnes, H.J., Havenstein, G.B., Alterations in the lymphocytic and mononuclear phagocytic systems of turkey poults associated with exposure to poult enteritis mortality syndrome (1998) Avian Dis., 42, pp. 711-720; McNulty, M.S., Rotavirus infections (1997) Diseases of Poultry, 10th Ed., pp. 692-701. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Qureshi, M.A., Edens, F.W., Havenstein, G.B., Immune system dysfunction during exposure to poults enteritis and mortality syndrome agents (1997) Poult. Sci., 76, pp. 564-569; Qureshi, M.A., Saif, Y.M., Yu, M., Small round virus associated with the poult enteritis and mortality syndrome of turkeys reduced proliferation of lymphocytes (1999) Proc. Southern Conference on Avian Diseases, pp. S125. , Atlanta, GA. January 19-21; Qureshi, M.A., Yu, M., Saif, Y.M., A novel ""small round virus"" inducing poult enteritis and mortality syndrome and associated immune alterations (2000) Avian Dis., 44, pp. 275-283; Reed, L.J., Muench, H., A simple method for estimating fifty percent endpoint (1938) Am. J. Hyg., 27, pp. 493-496; Reynolds, D.L., Saif, Y.M., Astrovirus: A cause of an enteric disease in turkey poults (1986) Avian Dis., 30, pp. 728-735; Reynolds, D.L., Saif, Y.M., Theil, K.W., A survey of enteric viruses of turkey poults (1986) Avian Dis., 31, pp. 89-98; Rosenberger, J.K., Olson, N.O., Viral arthritis (1997) Diseases of Poultry, 10th Ed., pp. 711-719. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Saif, L.J., Jiang, B., Nongroup A rotaviruses of humans and animals (1994) Rotavirus, pp. 339-367. , R. F. Ramig, ed. Springer-Verlag, Berlin and Heidelberg, Germany; Saif, L.J., Saif, Y.M., Theil, K.W., Enteric viruses in diarrheic turkey poults (1985) Avian Dis., 29, pp. 798-811; Swayne, D.E., Radin, M.J., Saif, Y.M., Enteric disease in specific-pathogen-free poults inoculated with a small round turkey-origin enteric virus (1989) Avian Dis., 34, pp. 683-692; Theil, K.W., McCloskey, C.M., Saif, L.J., Redman, D.R., Bohl, E.H., Hancock, D.D., Kohler, E.M., Moorhead, P.D., Rapid, simple method of preparing rotaviral double-stranded ribonucleic acid for analysis by polyacrylamide gel electrophoresis (1981) J. Clin. Microbiol., 14, pp. 273-280; Theil, K.W., Reynolds, D., Saif, Y.M., Comparison of immune microscopy and genome electropherotyping techniques for detection of turkey rotaviruses and rotavirus-like viruses in intestinal contents (1986) J. Clin. Microbiol., 23, pp. 695-699; Villegas, P., Titration of biological suspensions (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 248-253. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Reed, eds. American Association of Avian Pathologists, Kennett Square, PA","Saif, Y.M.; Food Animal Health Research Program, Ohio Agricultural Res./Devt. Center, Ohio State University, Wooster, OH 44691, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"10879909","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0034131303
"Addie D.D., Dennis J.M., Toth S., Callanan J.J., Reid S., Jarrett O.","7003910352;57197606752;57189707374;7004107703;7201777416;7006845693;","Long-term impact on a closed household of pet cats of natural infection with feline coronavirus, feline leukaemia virus and feline immunodeficiency virus.",2000,"The Veterinary record","146","15",,"419","424",,47,"10.1136/vr.146.15.419","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034620885&doi=10.1136%2fvr.146.15.419&partnerID=40&md5=6d9c061cc01f48d09e0d98a75aa1a00f","Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom","Addie, D.D., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom; Dennis, J.M., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom; Toth, S., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom; Callanan, J.J., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom; Reid, S., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom; Jarrett, O., Department of Veterinary Pathology, University of Glasgow Veterinary School, Bearsden, United Kingdom","A closed household of 26 cats in which feline coronavirus (FCoV), feline leukaemia virus (FeLV) and feline immunodeficiency virus (FIV) were endemic was observed for 10 years. Each cat was seropositive for FCoV on at least one occasion and the infection was maintained by reinfection. After 10 years, three of six surviving cats were still seropositive. Only one cat, which was also infected with FIV, developed feline infectious peritonitis (FIP). Rising anti-FCoV antibody titres did not indicate that the cat would develop FIP. The FeLV infection was self-limiting because all seven of the initially viraemic cats died within five years and the remainder were immune. However, FeLV had the greatest impact on mortality. Nine cats were initially FIV-positive and six more cats became infected during the course of the study, without evidence of having been bitten. The FIV infection did not adversely affect the cats' life expectancy.",,"virus antibody; animal; animal disease; animal housing; article; cat; cat disease; cause of death; Coronavirus; disease transmission; enzyme linked immunosorbent assay; Feline immunodeficiency virus; Feline leukemia virus; female; isolation and purification; life expectancy; male; mortality; virus infection; Animals; Antibodies, Viral; Cats; Cause of Death; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Feline Acquired Immunodeficiency Syndrome; Feline Infectious Peritonitis; Female; Housing, Animal; Immunodeficiency Virus, Feline; Leukemia Virus, Feline; Leukemia, Feline; Life Expectancy; Male",,"Addie, D.D.",,,00424900,,,"10811262","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0034620885
"Sizun J., Yu M.W.N., Talbot P.J.","35605340000;16940438900;7102670281;","Survival of human coronaviruses 229E and OC43 in suspension and after drying on surfaces: A possible source of hospital-acquired infections",2000,"Journal of Hospital Infection","46","1",,"55","60",,64,"10.1053/jhin.2000.0795","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033797952&doi=10.1053%2fjhin.2000.0795&partnerID=40&md5=284f1844b43c793d0232e144d8867213","Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, University of Quebec, Laval, Que. H7V 1B7, Canada","Sizun, J., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, University of Quebec, Laval, Que. H7V 1B7, Canada; Yu, M.W.N., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, University of Quebec, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, University of Quebec, Laval, Que. H7V 1B7, Canada","Strains OC43 and 229E of human coronaviruses (HCoV) cause one-third of common colds and hospital-acquired upper respiratory tract HCoV infections have been reported in premature newborns. To evaluate possible sources of infection, virus survival was studied in aqueous suspensions and on absorptive and non-absorptive surfaces representative of a hospital environment. Virus susceptibility to chemical disinfection with standard products was also characterized. Virus survived in saline solution for as long as six days but less in culture medium, with or without added cells. After drying, HCoV-229E infectivity was still detectable after 3 h on various surfaces (aluminum, sterile latex surgical gloves, sterile sponges) but HCoV-OC43 survived 1 h or less. Of the various chemical disinfectants tested, Proviodine® reduced the virus infectious titre by at least 50%. This study suggests that surfaces and suspensions can be considered as possible sources of contamination that may lead to hospital-acquired infections with HCoV and should be appropriately disinfected. (C) 2000 The Hospital Infection Society.","Coronavirus; Disinfection; Hospital-acquired infections; Infectivity; Respiratory infections; Survival; Virus","article; Coronavirus; disinfection; hospital infection; infection control; respiratory tract infection; survival rate; virus culture; virus infection","Myint, S.H., Human coronavirus infections (1995), pp. 389-401. , Siddell SG, ed. The Coronaviridae. New York: Plenum Press; Sizun, J., Soupre, D., Giroux, J.D., Nasal colonization with coronavirus and apnea of the premature newborn (1993) Acta Paediatr, 82, p. 238; Sizun, J., Soupre, D., Legrand, M.C., Neonatal nosocomial respiratory infection with coronavirus: A prospective study in a neonatal intensive care unit (1995) Acta Paediatr, 84, pp. 617-620; Falsey, A.R., McCann, R.M., Hall, W.J., The 'common cold' in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J Amer Geriatr Soc, 45, pp. 706-711; Bradburne, A.F., Bynoe, M.L., Tyrrell, D.A.J., Effects of a new human respiratory virus in volunteers (1967) Brit Med J, 3, pp. 767-769; Larson, H.E., Reed, S.E., Tyrrell, D.A.J., Isolation of rhinovirus and coronaviruses from 38 colds in adults (1980) J Med Virol, 5, pp. 221-229; Ijaz, M.K., Brunner, A.H., Sattar, S.A., Survival characteristics of airborne human coronavirus 229E (1985) J Gen Virol, 66, pp. 2743-2748; Hall, C.B., Douglas, G., Geiman, J.M., Possible transmission by fomites of respiratory syncytial virus (1980) J Infect Dis, 141, pp. 98-102; Hendley, J.O., Wenzel, R.P., Gwaltney, J.M., Transmission of rhinovirus colds by self-inoculation (1973) N Engl J Med, 288, pp. 1361-1364; Jouvenne, P., Mounir, S., Stewart, J.N., Sequence analysis of human coronavirus 229E mRNAs 4 and 5: Evidence for polymorphism and homology with myelin basic protein (1992) Virus Res, 22, pp. 125-141; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene human coronavirus OC43 and evidence for O-glycosylation (1992) J Gen Virol, 73, pp. 2731-2736; Sattar, S.A., Karim, Y.G., Springthorpe, V.S., Johnson-Lussenburg, C.M., Survival of human rhinovirus type 14 dried onto nonporous inanimate surfaces: Effect of relative humidity and suspending medium (1987) Can J Microbiol, 33, pp. 802-806; Sizun, J., Arbour, N., Talbot, P.J., Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture (1998) J Virol Meth, 72, pp. 145-152; Payment, P., Trudel, M., Isolement et identification des virus (1989), pp. 21-44. , Payment P, Trudel M, eds. Manuel de Techniques Virologiques. Quebec: Presses de I' Universite du Quebec; Brady, M.T., Evans, J., Cuartas, J., Survival and disinfection of parainfluenza viruses on environmental surfaces (1990) Amer J Infect Control, 18, pp. 18-23; Ford-Jones, E.L., The special problems of nosocomial infection in the pediatric patient (1993), pp. 812-896. , Wenzel RP, ed. Prevention and Control of Nosocomial Infections. Baltimore: Williams and Wilkins; Lamarre, A., Talbot, P.J., Effect of pH and temperature on the infectivity of human coronavirus 229E (1989) Can J Microbiol, 35, pp. 972-974; Ansari, S.A., Springthorpe, S., Sattar, S.A., Potential role of hands in the spread of respiratory viral infections: Studies with human Parainfluenza virus 3 and Rhinovirus 14 (1991) J Clin Microbiol, 10, pp. 2115-2119; Arbour, N., Ekande, S., Cote, G., Persistent infection of human oligodendrocytic and neuroglial cell lines by human coronavirus 229E (1999) J Virol, 73, pp. 3326-3337; Arbour, N., Cote, G., Lachance, C., Acute and persistent infection of human neural cell lines by human coronavirus OC43 (1999) J Virol, 73, pp. 3338-3350; Bellamy, K., A review of the tests methods used to establish virucidal activity (1995) J Hosp Infect, 30 (SUPPL.), pp. 389-396; Krilov, L.R., Harkness, S.H., Inactivation of respiratory syncytial virus by detergents and disinfectants (1993) Pediatr Infect Dis J, 12, pp. 582-584; Guidelines for prevention of nosocomial pneumonia (1997) MMWR, 46, pp. 1-79","Sizun, J.; Department of Pediatrics, University Hospital, 29609 Brest, France; email: Jacques.Sizun@univ-brest.fr",,"W.B. Saunders Ltd",01956701,,JHIND,"11023724","English","J. Hosp. Infect.",Article,"Final",Open Access,Scopus,2-s2.0-0033797952
"Wang G., Deering C., Macke M., Shao J., Burns R., Blau D.M., Holmes K.V., Davidson B.L., Perlman S., McCray P.B. Jr.","7407150557;7003858436;6602983308;7201361453;57197002035;15729433700;7201657724;7402965653;7102708317;7007180790;","Human coronavirus 229E infects polarized airway epithelia from the apical surface",2000,"Journal of Virology","74","19",,"9234","9239",,39,"10.1128/JVI.74.19.9234-9239.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033808419&doi=10.1128%2fJVI.74.19.9234-9239.2000&partnerID=40&md5=b0ada75793b3dac9dc6bc6c8e8ee6155","Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States","Wang, G., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Deering, C., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Macke, M., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Shao, J., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Burns, R., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Blau, D.M., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Holmes, K.V., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Davidson, B.L., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; McCray P.B., Jr., Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States","Gene transfer to differentiated airway epithelia with existing viral vectors is very inefficient when they are applied to the apical surface. This largely reflects the polarized distribution of receptors on the basolateral surface. To identify new receptor-ligand interactions that might be used to redirect vectors to the apical surface, we investigated the process of infection of airway epithelial cells by human coronavirus 229E (HCoV-229E), a common cause of respiratory tract infections. Using immunohistochemistry, we found the receptor for HCoV-229E (CD13 or aminopeptidase N) localized mainly to the apical surface of airway epithelia. When HCoV-229E was applied to the apical or basolateral surface of well-differentiated primary cultures of human airway epithelia, infection primarily occurred from the apical side. Similar results were noted when the virus was applied to cultured human tracheal explants. Newly synthesized virions were released mainly to the apical side. Thus, HCoV-229E preferentially infects human airway epithelia from the apical surface. The spike glycoprotein that mediates HCoV-229E binding and fusion to CD13 is a candidate for pseudotyping retroviral envelopes or modifying other viral vectors.",,"virus glycoprotein; virus receptor; apical membrane; article; controlled study; Coronavirus; gene transfer; human; human cell; human coronavirus 229e; nonhuman; priority journal; respiratory epithelium; respiratory tract infection; virion; virus adsorption; virus assembly; virus infection; virus pathogenesis; virus vector; Cell Line; Cell Polarity; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Epithelial Cells; Human; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Trachea; Virus Replication","Arbour, N., Ekande, S., Cote, G., Lachance, C., Chagnon, F., Tardieu, M., Cashman, N.R., Talbot, P.J., Persistent infection of human oligodendrocytic and neuroglial cell lines by human coronavirus 229E. J. 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Immunol., 99, pp. 165-200; Welsh, M.J., Gene transfer for cystic fibrosis (1999) J. Clin. Investig., 104, pp. 1165-1166; Yamaya, M., Finkbeiner, W.E., Chun, S.Y., Widdicombe, J.H., Differentiated structure and function of cultures from human tracheal epithelium (1992) Am. J. Physiol., 262, pp. L713-L724; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Zabner, J., Fasbender, A.J., Moninger, T., Poellinger, K.A., Welsh, M.J., Cellular and molecular barriers to gene transfer by a cationic lipid (1995) J. Biol. Chem., 270, pp. 18997-19007; Zabner, J., Zeiher, B.G., Friedman, E., Welsh, M.J., Adenovirusmediated gene transfer to ciliated airway epithelia requires prolonged incubation time (1996) J. Virol., 70, pp. 6994-7003","McCray Jr., P.B.; Department of Pediatrics, Univ. of Iowa College of Medicine, Iowa City, IA 52242, United States; email: paul-mccray@uiowa.edu",,,0022538X,,JOVIA,"10982370","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033808419
"Guy J.S., Smith L.G., Breslin J.J., Vaillancourt J.P., Barnes H.J.","7202723649;37109180900;7004753945;7004505622;7102581732;","High mortality and growth depression experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus",2000,"Avian Diseases","44","1",,"105","113",,39,"10.2307/1592513","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034080644&doi=10.2307%2f1592513&partnerID=40&md5=5047c9e7c7a1881a9f2e7a4b9dff1287","Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Dept. of Food Anim. and Equine Med., North Carolina State University, Raleigh, NC 27606, United States","Guy, J.S., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Smith, L.G., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Breslin, J.J., Dept. Microbiol., Pathol., P., North Carolina State University, Raleigh, NC 27606, United States; Vaillancourt, J.P., Dept. of Food Anim. and Equine Med., North Carolina State University, Raleigh, NC 27606, United States; Barnes, H.J., Dept. of Food Anim. and Equine Med., North Carolina State University, Raleigh, NC 27606, United States","Six-day-old turkeys were inoculated with turkey coronavirus (TCV) and an enteropathogenic Escherichia coli (EPEC) (isolate R98/5) that were isolated from poult enteritis and mortality syndrome (PEMS)-affected turkeys. Turkeys inoculated with only R98/5 did not develop clinically apparent disease, and only mild disease and moderate growth depression were observed in turkeys inoculated with only TCV. Turkeys dually inoculated with TCV and R98/5 developed severe enteritis with high mortality (38/48, 79%) and marked growth depression. R98/5 infection resulted in attaching/effacing (AE) intestinal lesions characteristic of EPEC: adherence of bacterial microcolonies to intestinal epithelium with degeneration and necrosis of epithelium at sites of bacterial attachment. AE lesions were more extensive and were detected for a prolonged duration in dually inoculated turkeys compared with turkeys inoculated with only R98/5. An apparent synergistic effect in dually inoculated turkeys was indicated by increased mortality, enhanced growth depression, and enhanced AE lesion development. The results suggest that TCV promoted intestinal colonization by R98/5; however, R98/5 did not appear to alter TCV infection. The present study provides a possible etiologic explanation for PEMS.","Enteritis; Escherichia coli; Turkey coronavirus","Animalia; Aves; Bacteria (microorganisms); Coronavirus; Enterobacter; Escherichia coli; Meleagris gallopavo; Turkey coronavirus","Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry, 10th Ed., pp. 1024-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Carver, D.K., Vaillancourt, J.P., Stringham, S.M., Descriptive epidemiology of coronavirus in commercial turkeys in North Carolina (1998) Proc. 135th Annual Convention of the American Veterinary Medicine Association, p. 191. , Baltimore, MD; Edens, F.W., Parkhurst, C.R., Quereshi, M.A., Casas, I.A., Havenstein, G.B., Atypical Escherichia coli strains and their association with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 952-960; Edens, F.W., Quereshi, M.A., Parkhurst, C.R., Havenstein, G.B., Casas, I.A., Characterization of two Escherichia coli isolates associated with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 1665-1673; Fisher, J., Maddox, C., Moxley, R., Kinden, D., Miller, M., Pathogenicity of a bovine attaching effacing Escherichia coli isolate lacking shiga-like toxins (1994) Am. J. Vet. Res., 55, pp. 991-999; Fukui, H., Sueyoshi, M., Haritani, M., Nakazawa, M., Naitoh, S., Tani, H., Uda, Y., Natural infection with attaching and effacing Escherichia coli (O 103:H-) in chicks (1995) Avian Dis., 39, pp. 912-918; Gannon, V.P., King, R.K., Kim, J.Y., Thomas, E.J., Rapid and sensitive method for detection of shiga-like toxin-producing Escherichia coli in ground beef using the polymerase chain reaction (1992) Appl. Environ. Microbiol., 58, pp. 3809-3815; Gannon, V.P.J., Rashed, M., King, R.K., Golsteyn-Thomas, E.J., Detection and characterization of the eae gene of shiga-like toxin-producing Escherichia coli using polymerase chain reaction (1991) J. Clin. Microbiol., 31, pp. 1268-1274; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hess, R.G., Bachman, P.A., Baljer, G., Mayr, A., Pospischil, A., Schmid, G., Synergism in experimental mixed infections of newborn colostrum-deprived calves with bovine rotavirus and enterotoxigenic Escherichia coli (ETEC) (1984) Zentralbl. Veterinaermed. B, 31, pp. 585-596; Jerse, A.E., Yu, J., Tall, B.D., Kaper, J.B., A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 7839-7843; Kaper, J.B., McDaniel, T.K., Jarvis, K.G., Gomez-Duarte, O., Genetics of virulence of enteropathogenic E. coli (1997) Mechanisms in the Pathogenesis of Enteric Diseases, pp. 279-287. , P. S. Paul, ed. Plenum Press, New York; Lecce, J.G., Balbaugh, R.K., Clare, D.A., King, M.W., Rotavirus and hemolytic enteropathogenic Escherichia coli in weanling diarrhea of pigs (1982) J. Clin. Microbiol., 16, pp. 715-723; Moon, H.W., Whipp, S.C., Argenzio, R.A., Levine, M.M., Giannella, R.A., Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines (1983) Infect. Immun., 41, pp. 1340-1351; Moxley, R.A., Francis, D.H., Natural and experimental infection with an attaching and effacing strain of Escherichia coli in calves (1986) Infect. Immun., 53, pp. 339-346; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Nakamura, K., Imada, Y., Maeda, M., Lymphocytic depletion of bursa of Fabricius and thymus in chickens inoculated with Escherichia coli (1986) Vet. Pathol., 23, pp. 712-717; Nataro, J.P., Kaper, J.B., Diarrheagenic Escherichia coli (1998) Clin. Microbiol. Rev., 11, pp. 142-201; Newsome, P.M., Coney, K.A., Synergistic rotavirus and Escherichia coli diarrhea infection of mice (1985) Infect. Immun., 47, pp. 573-581; Ojeniyi, B., Ahrens, P., Meyling, A., Detection of fimbrial and toxin genes in Escherichia coli and their prevalence in piglets with diarrhoea. The application of colony hybridization assay, polymerase chain reaction and phenotypic assays (1994) Zentralbl. Vet. Med. B., 41, pp. 49-59; Robins-Browne, R.M., Traditional enteropathogenic Escherichia coli of infantile diarrhea (1987) Rev. Infect. Dis., 9, pp. 28-52; Shivaprasad, H.L., Crespo, R.C., Daft, B., Read, D., Attaching and effacing E. coli associated with enteritis in poultry (1998) Proc. 135th Annual Convention of the American Veterinary Medicine Association, p. 184. , Baltimore, MD; Snedecor, G.W., Cochran, W.G., One-way classifications; analysis of variance (1980) Statistical Methods, 7th Ed., pp. 215-237. , The Iowa State University Press, Ames, IA; Snodgrass, D.R., Smith, M.L., Krautil, F.L., Interaction of rotavirus and enterotoxigenic Escherichia coli in conventionally-reared dairy calves (1982) Vet. Microbiol., 7, pp. 51-60; Turk, J., Maddox, C., Fales, W., Ostlund, E., Miller, M., Johnson, G., Pace, L., Kreeger, J., Examination for heat-labile, heat-stable, and shiga-like toxins and for eaeA gene in Escherichia coli isolates obtained from dogs dying with diarrhea: 122 cases (1992-1996) (1998) J. Am. Vet. Med. Assoc., 212, pp. 1735-1736; Wray, C., Dawson, M., Afshar, A., Lucas, M., Experimental Escherichia coli and rotavirus infection in lambs (1981) Res. Vet. Sci., 30, pp. 379-381; Wray, C., Woodward, M.J., Laboratory diagnosis of Escherichia coli infections (1994) Escherichia Coli in Domestic Animals and Humans, pp. 595-628. , C. L. Gyles, ed. CAB International, Wallingford, United Kingdom","Guy, J.S.; Microbiol., Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"10737650","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0034080644
"Breslin J.J., Smith L.G., Barnes H.J., Guy J.S.","7004753945;37109180900;7102581732;7202723649;","Comparison of virus isolation, immunohistochemistry, and reverse transcriptase-polymerase chain reaction procedures for detection of turkey coronavirus",2000,"Avian Diseases","44","3",,"624","631",,25,"10.2307/1593102","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033827726&doi=10.2307%2f1593102&partnerID=40&md5=c0bc21940cd2780e65c509904584b05c","Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States","Breslin, J.J., Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States; Smith, L.G., Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States; Barnes, H.J., Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States; Guy, J.S., Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States","A reverse transcriptase-polymerase chain reaction (RT-PCR) procedure and two monoclonal antibody (MAb)-based immunohistochemical procedures were developed for detection of turkey coronavirus (TCV) in tissues and intestinal contents/dropping samples. The RT-PCR, MAb-based fluorescent antibody (FA), and MAb-based immunoperoxidase (IP) procedures were compared with virus isolation (VI) for detection of TCV in experimentally infected turkeys. TCV was detected in experimentally infected turkeys as early as day 1 postexposure (PE) by each of the four detection procedures. TCV was detected as late as day 35 PE by FA or IP and days 42 and 49 PE by VI and RT-PCR, respectively. With VI as a reference, sensitivity and specificity of RT-PCR were 93% and 92%, respectively; specificity of both FA and IP was 96%, and sensitivities were 69% and 61%, respectively. Each of the examined procedures was highly specific, but the RT-PCR procedure was also highly sensitive. These findings demonstrate the utility of both immunohistochemistry and RT-PCR for detection of TCV. In addition, the findings indicate that RT-PCR is a highly sensitive and specific alternative to conventional diagnostic procedures.","Reverse transcriptase-polymerase chain reaction; Turkey coronavirus","disease diagnosis; monoclonal antibody; reverse transcription polymerase chain reaction; turkey coronavirus; virus detection; virus isolation","Afshar, A., Dulac, G.C., Bouffard, A., Application of peroxidase labeled antibody assays for detection of porcine IgG antibodies to hog cholera and bovine viral diarrhea viruses (1989) J. Virol Methods, 23, pp. 253-262; Andreasen J.R., Jr., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis., 35, pp. 216-220; Breslin, J.J., Smith, L.G., Fuller, F.G., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Carter, P.B., Beegle, K.H., Gebhard, D.H., Monoclonal antibodies: Clinical use and potential (1986) Vet. Clin. North Am., 16, pp. 1171-1179; Fletcher, R.H., Fletcher, S.W., Wagner, E.H., (1988), Clinical epidemiology - the essentials, 2nd ed. Williams and Wilkins, Baltimore, MD; Guy, J.S., Barnes, H.J., Smith, L.G., Rapid diagnosis of infectious laryngotracheitis using a monoclonal antibody-based immunoperoxidase procedure (1992) Avian Pathol., 21, pp. 77-86; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Jiang, X., Wang, J., Graham, D.Y., Estes, M.K., Detection of Norwalk virus in stool by polymerase chain reaction (1992) J. Clin. Microbiol., 30, pp. 2529-2534; Murphy, F.A., Virus taxonomy (1996), 1, pp. 15-57. , Fundamental virology, 3rd ed.,B. N. Fields, D. M. Knipe, and P. M. Howly, eds. Lippincott-Raven Publishers, Philadelphia, PA; Myint, S., Johnston, S., Sanderson, G., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell Probes, 8, pp. 357-364; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997), pp. 686-692. , Diseases of poultry, 10th ed. B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Reed, L.J., Muench, H., A simple method of estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Schat, K.A., Purchase, H.G., Cell culture methods (1989), pp. 167-175. , A laboratory manual for the isolation and identification of avian pathogens, 3rd ed. H. G. Purchase, L. H. Asp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Senne, D.A., Virus propagation in embryonating eggs (1989), pp. 176-181. , A laboratory manual for the isolation and identification of avian pathogens, 3rd ed. H. G. Purchase, L. H. Asp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Siddell, S.G., The Coronaviridae an introduction (1995), pp. 1-9. , Coronaviridae. S. G. Siddell, ed. Plenum Press, New York; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Tsunemitsu, H., Smith, D.R., Saif, L.J., Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coronavirus in feces by RT-PCR (1999) Arch. Virol., 144, pp. 167-175; Wilde, J., Eiden, J., Yolken, R., Removal of inhibitory substances from human fecal specimens for detection of group A rotaviruses by reverse transcriptase polymerase chain reactions (1990) J. Clin. Microbiol., 28, pp. 1300-1307","Guy, J.S.; Microbiol. Pathol./Parasitol. Dept., North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11007010","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0033827726
"Das Sarma J., Fu L., Tsai J.C., Weiss S.R., Lavi E.","6602813975;7401812822;7403610594;57203567044;7006986911;","Demyelination determinants map to the spike glycoprotein gene of coronavirus mouse hepatitis virus",2000,"Journal of Virology","74","19",,"9206","9213",,74,"10.1128/JVI.74.19.9206-9213.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033808456&doi=10.1128%2fJVI.74.19.9206-9213.2000&partnerID=40&md5=9ea652573d186c38d4f4f7025d930865","University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States","Das Sarma, J., University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States; Fu, L., University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States; Tsai, J.C., University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States; Weiss, S.R., University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States; Lavi, E., University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States","Demyelination is the pathologic hallmark of the human immune-mediated neurologic disease multiple sclerosis, which may be triggered or exacerbated by viral infections. Several experimental animal models have been developed to study the mechanism of virus-induced demyelination, including coronavirus mouse hepatitis virus (MHV) infection in mice. The envelope spike (S) glycoprotein of MHV contains determinants of properties essential for virus-host interactions. However, the molecular determinants of MHV-induced demyelination are still unknown. To investigate the mechanism of MHV-induced demyelination, we examined whether the S gene of MHV contains determinants of demyelination and whether demyelination is linked to viral persistence. Using targeted RNA recombination, we replaced the S gene of a demyelinating virus (MHV-A59) with the S gene of a closely related, nondemyelinating virus (MHV-2). Recombinant viruses containing an S gene derived from MHV-2 in an MHV-A59 background (Penn98-1 and Penn98-2) exhibited a persistence-positive, demyelination-negative phenotype. Thus, determinants of demyelination map to the S gene of MHV. Furthermore, viral persistence is insufficient to induce demyelination, although it may be a prerequisite for the development of demyelination.",,"glycoprotein spike; unclassified drug; virus envelope protein; virus glycoprotein; virus RNA; animal cell; animal experiment; animal model; animal tissue; article; controlled study; demyelination; gene function; gene mapping; genetic recombination; histopathology; mouse; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; persistent virus infection; priority journal; strain difference; virus cell interaction; virus gene; virus pathogenesis; virus recombinant; virus strain; Animal; Coronavirus Infections; Demyelinating Diseases; Gene Expression Regulation, Viral; Human; Membrane Glycoproteins; Mice; Murine hepatitis virus; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Viral Envelope Proteins","Allen, I., Brankin, B., Pathogenesis of multiple sclerosis - The immune diathesis and the role of viruses (1993) J. Neuropathol. Exp. 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Hyg., 27, pp. 493-497; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelinafion in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Suzumura, A., Lavi, E., Bhat, S., Murasko, D.M., Weiss, S.R., Silberberg, D.H., Induction of glial cell MHC antigen expression in neurotropic coronavirus infection: Characterization of the H-2 inducing soluble factor elaborated by infected brain cells (1988) J. Immunol., 140, pp. 2068-2072; Suzumura, A., Lavi, E., Weiss, S.R., Silberberg, D.H., Coronavirus infection induces H-2 antigen expression on oligodendrocytes and astrocytes (1986) Science, 232, pp. 991-993; Wang, F.I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Adv. Virol. Immunol., 99, pp. 165-200; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol., 28, pp. 298-303","Lavi, E.; University of Pennsylvania, Division of Neuropathology, Dept. of Pathology and Lab. Medicine, Philadelphia, PA 19104-6100, United States; email: lavi@mail.med.upenn.edu",,,0022538X,,JOVIA,"10982367","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033808456
"Yu M.W.N., Talbot P.J.","16940438900;7102670281;","Characterization of protection against coronavirus infection by noninternal image antiidiotypic antibody",2000,"Viral Immunology","13","1",,"93","106",,,"10.1089/vim.2000.13.93","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034114809&doi=10.1089%2fvim.2000.13.93&partnerID=40&md5=e70ffece7dffda4be675b98d859c5775","Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que., H7V 1B7, Canada; Laboratory of Neuroimmunovirology, INRS-Institute Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, Que., H7V 1B7, Canada","Yu, M.W.N., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que., H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que., H7V 1B7, Canada, Laboratory of Neuroimmunovirology, INRS-Institute Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, Que., H7V 1B7, Canada","Previously, we have reported protective vaccination of mice against a coronavirus infection using rabbit polyclonal noninternal image Ab2γ ant- idiotypic (anti-Id) antibody specific for a virus-neutralizing and protective monoclonal antibody (mAb) 7-10A against the viral surface S glycoprotein. To characterize further the mechanisms involved in the induction of protective immunity by this noninternal image anti-Id, plasma and splenocytes from Ab2(γ)-immunized BALB/c mice were passively transferred to naive BALB/c mice, followed by viral challenge. A reproducible significant delay in mortality observed in mice to which plasma was passively transferred, together with the presence of specific in vitro neutralizing antiviral Ab3 identified the humoral immune response as the major element responsible for protection. The activation of specific and cross-reactive T lymphocytes by both virus and anti-Id in immunized mice and the absence of adoptive transfer of protection by splenocytes suggested the participation of T helper activity in the induction of protective virus-neutralizing Ab3. To obtain more defined monoclonal reagents for a better understanding of anti-Id-induced protection, mAb2 were generated against the same mAb1 7-10A and characterized. We report the successful generation of mab2 of the γ type. However, unlike the polyclonal Ab2(γ), they were not capable of inducing a protective immune response.",,"idiotypic antibody; neutralizing antibody; adoptive transfer; animal cell; animal experiment; animal model; antibody production; antibody specificity; article; controlled study; drug efficacy; drug mechanism; female; immunoprophylaxis; mouse; nonhuman; spleen cell; T lymphocyte activation; vaccination; virus infection; Animalia; Coronavirus; Formicidae; Oryctolagus cuniculus","Armitage, P., Berry, G., (1987) Statistical Methods in Medical Research. 2nd Ed., pp. 428-433. , Blackwell Scientific Publications, Oxford; Bailey, G.S., Immunodiffusion in gels (1984) Methods in Molecular Biology. Proteins, p. 301. , Walker, J.M. (ed): Humana Press, Clifton, NJ; Billetta, R., Hollingdale, M.R., Zanetti, M., Immunogenicity of an engineered internal image antibody (1991) Proc. Natl. Acad. Sci. 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Virol., 96, pp. 241-248; Daniel, C., Talbot, P.J., Protection from lethal coronavirus infection by affinity-purified spike glycoprotein of murine hepatitis virus, strain A59 (1990) Virology, 174, pp. 87-94; Daniel, C., Lacroix, M., Talbot, P.J., Mapping of linear antigenic sites on the S glycoprotein of a neurotropic murine coronavirus with synthetic peptides: A combination of nine prediction algorithms fails to identify relevant epitopes and peptide immunogenicity is drastically influenced by the nature of the protein carrier (1994) Virology, 202, pp. 540-549; Durrant, L.G., Doran, M., Austin, E.B., Robins, R.A., Induction of cellular immune responses by a murine monoclonal anti-idiotypic antibody recognizing the 791Tgp72 antigen expressed on colorectal, gastric and ovarian human tumours (1995) Int. J. Cancer, 6, pp. 62-66; Fagerberg, J., Steinitz, M., Wigzell, H., Askelöf, P., Mellstedt, H., Human anti-idiotypic antibodies induced a humoral and cellular immune response against a colorectal carcinoma-associated antigen in patients (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 4773-4777; Fung, M.S.C., Sun, C.R.Y., Liou, R.S., Gordon, W., Chang, N.T., Chang, S.-W., Sun, N.-C., Monoclonal anti-idiotypic antibody mimicking the principal neutralization site in HIV-1 GP120 induces HIV-1 neutralizing antibodies in rabbits (1990) J. Immunol., 145, pp. 2199-2206; Heemskerk, M.H.M., Schoemaker, H.M., Spaan, W.J.M., Boog, C.J.P., Predominance of MHC class II-restricted CD4+ cytotoxic T cells against mouse hepatitis virus A59 (1995) Immunology, 84, pp. 521-527; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fields Virology, 3rd Ed., pp. 1075-1093. , Fields, B.N., D.M. Knipe, P.M. Howley et al. 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Virol., 62, pp. 3032-3036; Wege, H., Dörries, R., Wege, H., Hybridoma antibodies to the murine coronavirus JHM: Characterization of epitopes on the peplomer protein (E2) (1984) J. Gen. Virol., 65, pp. 1931-1942; Weiner, L.P., Pathogenesis of demyelination induced by mouse hepatitis virus (JHM virus) (1973) Arch. Neurol., 28, pp. 298-303; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. Neuroimmunol., 32, pp. 1-9; Yang, Y.-F., Thanavala, Y., A comparison of the antibody and T cell response elicited by internal image and noninternal image anti-idiotypes (1995) Clin. Immunol. Immunopathol., 75, pp. 154-158; Yu, M., Talbot, P.J., Induction of a protective immune response to murine coronavirus with non-internal image anti-idiotypic antibodies (1995) Adv. Exp. Med. Biol., 380, pp. 165-172; Yu, M.W.N., Lemieux, S., Talbot, P.J., Genetic control of anti-idiotypic vaccination against coronavirus infection (1996) Eur. J. Immunol., 26, pp. 3230-3233; Zhou, E.-M., Lohman, K.L., Kennedy, R.C., Administration of noninternal image monoclonal anti-idiotypic antibodies induces idiotype-restricted responses specific for human immunodeficiency virus envelope glycoprotein epitopes (1990) Virology, 174, pp. 9-17","Talbot, P.J.; Laboratory of Neuroimmunovirology, Human Health Research Center, Universite du Quebec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@inrs-iaf.uquebec.ca",,"Mary Ann Liebert Inc.",08828245,,VIIME,"10733172","English","Viral Immunol.",Article,"Final",,Scopus,2-s2.0-0034114809
"Krempl C., Ballesteros M.-L., Zimmer G., Enjuanes L., Klenk H.-D., Herrler G.","6602462665;7006110601;7102982629;7006565392;24432172000;7006339246;","Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants",2000,"Journal of General Virology","81","2",,"489","496",,45,"10.1099/0022-1317-81-2-489","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033957648&doi=10.1099%2f0022-1317-81-2-489&partnerID=40&md5=28edf07e1ed25d617d54f0680ea1c027","Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 7, 35037 Marburg, Germany; Centro Nacional de Biotecnologia, Dept. of Cell and Molecular Biology, CSIC Camp. Univ. Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany","Krempl, C., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 7, 35037 Marburg, Germany; Ballesteros, M.-L., Centro Nacional de Biotecnologia, Dept. of Cell and Molecular Biology, CSIC Camp. Univ. Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Zimmer, G., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 7, 35037 Marburg, Germany, Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany; Enjuanes, L., Centro Nacional de Biotecnologia, Dept. of Cell and Molecular Biology, CSIC Camp. Univ. Autonoma de Madrid, Canto Blanco, 28049 Madrid, Spain; Klenk, H.-D., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 7, 35037 Marburg, Germany; Herrler, G., Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Str. 7, 35037 Marburg, Germany, Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany","Transmissible gastroenteritis coronavirus (TGEV) agglutinates erythrocytes of several species by virtue of sialic acid binding activity of the surface protein S. We have isolated and characterized five haemagglutination-defective (HAD) mutants. In contrast to the parental virus, the mutants were unable to bind to porcine submandibulary mucin, a substrate rich in sialic acid. Each of the mutants was found to contain a single point mutation in the S protein (Cys155Phe, Met195Val, Arg196Ser, Asp208Asn or Leu209Pro), indicating that these amino acids are affecting the sialic acid binding site. In four of the HAD mutants a nearby antigenic site is affected in addition to the sialic acid binding site, as indicated by reactivity with monoclonal antibodies. The parental virus was found to have an increased resistance to the detergent octylglucoside compared to the HAD mutants. This effect depended on cellular sialoglycoconjugates bound to the virion. If the binding of sialylated macromolecules was prevented by neuraminidase treatment, the parental virus was as sensitive to octylglucoside as were the HAD mutants. We discuss the possibility that the sialic acid binding activity helps TGEV to resist detergent-like substances encountered during the gastrointestinal passage and thus facilitates the infection of the intestinal epithelium. An alternative function of the sialic acid binding activity - accessory binding to intestinal tissues - is also discussed.",,"monoclonal antibody; sialic acid; sialidase; article; binding affinity; binding site; Coronavirus; erythrocyte; hemagglutination; point mutation; priority journal; virus mutant; Coronavirus; RNA viruses; Suidae; Transmissible gastroenteritis virus","Ballesteros, M.L., Sánchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Bergelson, J.M., Cunningham, J.A., Droguett, G., Kurt-Jones, E.A., Krithivas, A., Hong, J.S., Horwitz, M.S., Finberg, R.W., Isolation of a common receptor for coxsackie B viruses and adenoviruses 2 and 5 (1997) Science, 275, pp. 1320-1323; Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) Journal of General Virology, 76, pp. 2235-2241; Cox, E., Pensaert, M.B., Callebaut, P., Van Deun, K., Intestinal replication of a porcine respiratory coronavirus closely related anti-genically to the enteric transmissible gastroenteritis (1990) Veterinary Microbiology, 23, pp. 237-243; Delmas, B., Gelfi, J., Laude, H., Antigenic structure of transmissible gastroenteritis virus. 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Domains in the peplomer glycoprotein (1986) Journal of General Virology, 67, pp. 1405-1418; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Gebauer, F., Posthumus, W.P., Correa, I., Suñé, C., Smerdou, C., Sánchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virology, 183, pp. 225-238; Hara, S., Yamaguchi, M., Furuhata, K., Ogura, H., Nakamura, M., Determination of mono-o-acetylated N-acetylneuraminic acids in human and rat sera by fluorometric high-performance liquid chromatography (1989) Analytical Biochemistry, 179, pp. 162-166; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) Journal of Virology, 71, pp. 3285-3287; Krempl, C., Ballesteros, M.L., Enjuanes, L., Herrler, G., Isolation of haemagglutination-defective mutants for the analysis of the sialic acid binding activity of transmissible gastroenteritis virus (1998) Advances in Experimental Medicine Ami Biology, 440, pp. 563-568; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. 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Boca Raton, Florida: CRC Press; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., María, J.B., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sá, C.M., Gebauer, F., Suñé, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) Journal of Virology, 73, pp. 7606-7618; Sanger, F., Nicklen, S., Coulson, A.R., DNA sequencing with chain terminating inhibitors (1977) Proceedings of the National Academy of Sciences, USA, 74, pp. 5463-5467; Schauer, R., Chemistry, metabolism, and biological functions of sialic acids (1982) Advances in Carbohydrate Chemistry and Biochemistry, 40, pp. 131-234; Schultze, B., Gross, H.-J., Brossmer, R., Herrler, G., The s protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) Journal of Virology, 65, pp. 6232-6237; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) Journal of Virology, 70, pp. 5634-5637; Suñé, C., Jiménez, G., Correa, I., Bullido, M.J., Gebauer, F., Smerdou, C., Enjuanes, L., Mechanisms of transmissible gastroenteritis coronavirus neutralization (1990) Virology, 177, pp. 559-569; Weiss, R.A., Clapham, P.R., Hot fusion of HIV (1996) Nature, 381, pp. 647-648; Zimmern, D., Kaesberg, P., 3′-Terminal nucleotide sequence of encephylomyocarditis virus RNA determined by reverse transcriptase and chain-terminating inhibitors (1978) Proceedings of the National Academy of Sciences, USA, 75, pp. 4257-4261","Herrler, G.; Institut fur Virologie, Tierarztliche Hochschule Hannover, Bunteweg 17, 30559 Hannover, Germany; email: herrler@viro.tiho-hannover.de",,"Society for General Microbiology",00221317,,JGVIA,"10644848","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033957648
"Stirrups K., Shaw K., Evans S., Dalton K., Casais C., Cavanagh D., Britton P.","57210222541;7202206256;7402709581;7006042187;6602185676;26642890500;57203302770;","Expression of reporter genes from the defective RNA CD-61 of the coronavirus infectious bronchitis virus",2000,"Journal of General Virology","81","7",,"1687","1698",,26,"10.1099/0022-1317-81-7-1687","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033933273&doi=10.1099%2f0022-1317-81-7-1687&partnerID=40&md5=02d372959d93ccb790f82f0782f2ae35","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; University of Cambridge, Department of Haematology, Division of Transfusion Medicine, Long Road, Cambridge CB2 2PT, United Kingdom; Depts. Pathol. Cell Biol. (BML 342), Yale University School of Medicine, 310 Cedar St, New Haven, CT 06510, United States","Stirrups, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom, University of Cambridge, Department of Haematology, Division of Transfusion Medicine, Long Road, Cambridge CB2 2PT, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Evans, S., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Dalton, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom, Depts. Pathol. Cell Biol. (BML 342), Yale University School of Medicine, 310 Cedar St, New Haven, CT 06510, United States; Casais, C., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","The defective RNA (D-RNA) CD-61, derived from the Beaudette strain of the avian coronavirus infectious bronchitis virus (IBV), was used as an RNA vector for the expression of two reporter genes, luciferase and chloramphenicol acetyltransferase (CAT). D-RNAs expressing the CAT gene were demonstrated to be capable of producing CAT protein in a helper-dependent expression system to about 1·6 μg per 106 cells. The reporter genes were expressed from two different sites within the CD-61 sequence and expression was not affected by interruption of the CD-61-specific ORF. Expression of the reporter genes was under the control of a transcription-associated sequence (TAS) derived from the Beaudette gene 5, normally used for the transcription of IBV subgenomic mRNA 5. The Beaudette gene 5 TAS is composed of two tandem repeats of the IBV canonical consensus sequence involved in the acquisition of a leader sequence during the discontinuous transcription of IBV subgenomic mRNAs. It is demonstrated that only one canonical sequence is required for expression of mRNA 5 or for the expression of an mRNA from a D-RNA and that either sequence can function as an acceptor site for acquisition of the leader sequence.",,"chloramphenicol acetyltransferase; luciferase; messenger RNA; signal peptide; virus RNA; article; Avian infectious bronchitis virus; binding site; cloning vector; consensus sequence; controlled study; Coronavirus; gene control; gene expression; nonhuman; open reading frame; priority journal; protein expression; reporter gene; RNA sequence; RNA transcription; tandem repeat; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; DNA viruses; Felis catus; RNA viruses","Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1987) Current Protocols in Molecular Biology, , New York: John Wiley; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) Journal of Virology, 48, pp. 633-640; Binns, M.M., Boursnell, M.E.G., Cavanagh, D., Pappin, D.J.C., Brown, T.D.K., Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) Journal of General Virology, 66, pp. 719-726; Binns, M.M., Boursnell, M.E.G., Tomley, F.M., Brown, T.D.K., Comparison of the spike precursor sequences of coronavirus IBV strains M41 and 6/82 with that of IBV Beaudette (1986) Journal of General Virology, 67, pp. 2825-2831; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of Poultry, 10th Edn, pp. 511-526. , Edited by B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid & H. W. Yoda. 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Identification and characterization of virus-specific RNA (1980) Journal of Virology, 34, pp. 665-674; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Cavanagh, D., Britton, P., Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus (2000) Journal of General Virology, 81, pp. 791-801; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Van Der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) Journal of Virology, 68, pp. 3656-3666; Van Marie, G., Luytjes, W., Van Der Most, R.G., Van Der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) Journal of Virology, 69, pp. 7851-7856; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M., Expression of interferon-gamma by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.-L., Lai, M.M., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; email: Paul.Britton@bbsrc.ac.uk",,"Society for General Microbiology",00221317,,JGVIA,"10859373","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033933273
"Arbour N., Day R., Newcombe J., Talbot P.J.","6602762564;7402617019;8541726600;7102670281;","Neuroinvasion by human respiratory coronaviruses",2000,"Journal of Virology","74","19",,"8913","8921",,102,"10.1128/JVI.74.19.8913-8921.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033808208&doi=10.1128%2fJVI.74.19.8913-8921.2000&partnerID=40&md5=5323c60a9fc26632e77c379db75924ef","Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Arbour, N., Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Day, R., Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Newcombe, J., Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Human coronaviruses (HCoV) cause common colds but can also infect neural cell cultures. To provide definitive experimental evidence for the neurotropism and neuroinvasion of HCoV and its possible association with multiple sclerosis (MS), we have performed an extensive search and characterization of HCoV RNA in a large panel of human brain autopsy samples. Very stringent reverse transcription-PCR with two primer pairs for both viral strains (229E and OC43), combined with Southern hybridization, was performed on samples from 90 coded donors with various neurological diseases (39 with MS and 26 with other neurological diseases) or normal controls (25 patients). We report that 44% (40 of 90) of donors were positive for 229E and that 23% (21 of 90) were positive for OC43. A statistically significant higher prevalence of OC43 in MS patients (35.9%; 14 of 39) than in controls (13.7%; 7 of 51) was observed. Sequencing of nucleocapsid protein (N) gene amplicons revealed point mutations in OC43, some consistently found in three MS patient brains and one normal control but never observed in laboratory viruses. In situ hybridization confirmed the presence of viral RNA in brain parenchyma, outside blood vessels. The presence of HCoV in human brains is consistent with neuroinvasion by these respiratory pathogens. Further studies are needed to distinguish between opportunistic and disease-associated viral presence in human brains.",,"nucleocapsid protein; amino acid sequence; article; controlled study; Coronavirus; human; human cell; human tissue; multiple sclerosis; neuropathology; point mutation; priority journal; strain difference; virus detection; virus infection; Brain; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus OC43, Human; Human; In Situ Hybridization; Multiple Sclerosis; Neurons; Support, Non-U.S. Gov't; Virus Replication","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Andersen, O., Lygner, P.E., Bergstrom, T., Andersson, M., Vahlne, A., Viral infections trigger multiple sclerosis relapses: A prospective sero-epidemiological study (1993) J. 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Virol., 71, pp. 2959-2969; Salmi, A., Ziola, B., Hovi, T., Reunanen, M., Antibodies to coronaviruses OC43 and 229E in multiple sclerosis patients (1982) Neurology, 32, pp. 292-295; Schafer, M.K.-H., Day, R., In situ hybridization techniques to study processing enzyme expression at the cellular level (1994) Methods Neurosci., 23, pp. 16-44; Schreiber, S.S., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Sibley, W.A., Bamford, C.R., Clark, K., Clinical viral infections and multiple sclerosis (1985) Lancet, 1, pp. 1313-1315; Sorensen, O., Collins, A., Flintoff, W., Ebers, G., Dales, S., Probing for the human coronavirus OC43 in multiple sclerosis (1986) Neurology, 36, pp. 1604-1606; Sorensen, O., Coulter-Mackie, M.B., Puchalski, S., Dales, S., In vivo and in vitro models of demyelinating disease. IX. 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Neurol., 39, pp. 233-240; Tanaka, R., Iwasaki, Y., Koprowski, H., Intracisternal virus-like particles in brain of a multiple sclerosis patient (1976) J. Neurol. Sci., 28, pp. 121-126; Weber, T., Major, E.O., Progressive multifocal leukoencephalopathy: Molecular biology, pathogenesis and clinical impact (1997) Intervirology, 40, pp. 98-111; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Semin. Immunopathol., 17, pp. 133-148; White III, F.A., Ishaq, M., Stoner, G.L., Frisque, R.J., JC virus DNA is present in many human brain samples from patients without progressive multifocal leukoencephalopathy (1992) J. Virol., 66, pp. 5726-5734","Talbot, P.J.; Centre de Recherche en Sante Humaine, INRS-Institut Armand-Frappier, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@inrs-iaf.uquebec.ca",,,0022538X,,JOVIA,"10982334","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033808208
"Banerjee S., An S., Zhou A., Silverman R.H., Makino S.","55851941931;55107136200;7202762900;7202370256;7403067550;","RNase L-independent specific 28S rRNA cleavage in murine coronavirus-infected cells",2000,"Journal of Virology","74","19",,"8793","8802",,36,"10.1128/JVI.74.19.8793-8802.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033808358&doi=10.1128%2fJVI.74.19.8793-8802.2000&partnerID=40&md5=b9a2ef7d38546046d1eb7749f8dc1cb2","Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Banerjee, S., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; An, S., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Zhou, A., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Silverman, R.H., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Makino, S., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","We characterized a novel 28S rRNA cleavage in cells infected with the murine coronavirus mouse hepatitis virus (MHV). The 28S rRNA cleavage occurred as early as 4 h postinfection (p.i.) in MHV-infected DBT cells, with the appearance of subsequent cleavage products and a decrease in the amount of intact 28S rRNA with increasing times of infection; almost all of the intact 28S rRNA disappeared by 24 h p.i. In contrast, no specific 18S rRNA cleavage was detected in infected cells. MHV-induced 28S rRNA cleavage was detected in all MHV-susceptible cell lines and all MHV strains tested. MHV replication was required for the 28S rRNA cleavage, and mature cytoplasmic 28S rRNA underwent cleavage. In certain combination of cells and viruses, pretreatment of virus-infected cells with interferon activates a cellular endoribonuclease, RNase L, that causes rRNA degradation. No interferon was detected in the inoculum used for MHV infection. Addition of anti-interferon antibody to MHV-infected cells did not inhibit 28S rRNA cleavage. Furthermore, 28S rRNA cleavage occurred in an MHV-infected mouse embryonic fibroblast cell line derived from RNase L knockout mice. Thus, MHV-induced 28S rRNA cleavage was independent of the activation of RNase L. MHV-induced 28S rRNA cleavage was also different from apoptosis-related rRNA degradation, which usually occurs concomitantly with DNA fragmentation. In MHV-infected 17Cl-1 cells, 28S rRNA cleavage preceded DNA fragmentation by at least 18 h. Blockage of apoptosis in MHV-infected 17Cl-1 cells by treatment with a caspase inhibitor did not block 28S rRNA cleavage. Furthermore, MHV-induced 28S rRNA cleavage occurred in MHV-infected DBT cells that do not show apoptotic signs, including activation of caspase-3 and DNA fragmentation. Thus, MHV-induced 28S rRNA cleavage appeared to differ from any rRNA degradation mechanism described previously.",,"caspase inhibitor; interferon antibody; ribonuclease; RNA 28S; animal cell; animal model; apoptosis; article; DNA degradation; enzyme activation; fibroblast culture; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; RNA analysis; RNA cleavage; RNA degradation; RNA virus infection; virus replication; Animal; Coronavirus Infections; Endoribonucleases; Gene Expression Regulation, Viral; Hepatitis, Viral, Animal; Mice; Murine hepatitis virus; RNA, Ribosomal, 28S; Support, U.S. Gov't, P.H.S.; Virus Replication","An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in routine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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Biochem., 85, pp. 233-240; Zhou, A., Paranjape, J., Brown, T.L., Nie, H., Naik, S., Dong, B., Chang, A., Silverman, R.H., Interferon action and apoptosis are defective in mice devoid of 2',5'-oligoadenylate-dependent RNase L (1997) EMBO J., 16, pp. 6355-6363","Makino, S.; Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,,0022538X,,JOVIA,"10982321","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033808358
"El-Sahly H.M., Atmar R.L., Glezen W.P., Greenberg S.B.","6602970679;7005296248;7004510527;7402294401;","Spectrum of clinical illness in hospitalized patients with “common cold” virus infections",2000,"Clinical Infectious Diseases","31","1",,"96","100",,106,"10.1086/313937","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034457382&doi=10.1086%2f313937&partnerID=40&md5=5abc4ea7e45a40ee8b99238395cea4d8","Deparment of Medicine, Baylor College of Medicine, Houston, TX, United States; Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, United States; Department of Pediatrics, Baylor College of Medicine, Houston, T, United States","El-Sahly, H.M., Deparment of Medicine, Baylor College of Medicine, Houston, TX, United States; Atmar, R.L., Deparment of Medicine, Baylor College of Medicine, Houston, TX, United States, Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, United States; Glezen, W.P., Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, United States, Department of Pediatrics, Baylor College of Medicine, Houston, T, United States; Greenberg, S.B., Deparment of Medicine, Baylor College of Medicine, Houston, TX, United States, Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX, United States","The viruses associated most frequently with the ""common cold"" are rhinoviruses and coronaviruses. The first prospective cohort study to determine the prevalence of rhinovirus and coronavirus infections in patients of all ages hospitalized for acute respiratory illnesses is described. Hospital admissions for acute respiratory illnesses were identified, and cell culture for rhinovirus and serologic assays on paired sera for coronaviruses 229E and OC43 were performed. A total of 61 infections with rhinoviruses and coronaviruses were identified from 1198 respiratory illnesses (5.1%); in addition, 9 additional infections associated with ≥ 1 other respiratory viruses were identified. of those infected with only rhinovirus or coronavirus, underlying cardiopulmonary diseases were present in 35% of the patients aged <5 years, in 93% aged between 5 and 35 years, and in 73% aged >35 years. The predominant clinical syndromes varied by age: pneumonia and bronchiolitis in children aged <5 years; exacerbations of asthma in older children and young adults; and pneumonia and exacerbations of chronic obstructive pulmonary disease and congestive heart failure in older adults. Therefore, rhinovirus and coronavirus infections in hospitalized patients were associated with lower respiratory tract illnesses in all age groups. © 2000 Infectious Diseases Society of America.",,"adolescent; adult; article; child; cohort analysis; common cold; Coronavirus; female; high risk population; hospital admission; hospital care; hospitalization; human; infection prevention; lower respiratory tract infection; major clinical study; male; priority journal; Rhinovirus; seroconversion; virus infection; Adolescent; Adult; Child; Child, Preschool; Common Cold; Coronavirus Infections; Female; Hospitals; Humans; Infant; Male; Prevalence; Prospective Studies; Rhinovirus","Tyrrell, D.A., Hot news on the common cold (1988) Annu Rev Microbiol, 42, pp. 35-47; Arruda, E., Pitkaranta, A., Witek, T.J.J., Doyle, C.A., Hayden, F.G., Frequency and natural history of rhinovirus infections in adults during autumn (1997) J Clin Microbiol, 35, pp. 2864-2868; Makela, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Pelon, W., Mogabgab, W.J., Phillips, I.A., Pierce, W.E., A cytopathogenic agent isolated from naval recruits with mild respiratory illnesses (1957) Proc Soc Exp Biol Med, 94, pp. 262-267; Couch, R.B., Rhinoviruses (1996) Virology. 3d ed., pp. 713-734. , Fields BN, Knipe DM, Howley PM, eds. 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(1999) Clin Infect Dis, 29, pp. 533-535; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Las, H.J., Swanson, V.L., Sudden death of an infant with rhinovirus infection complicating bronchial asthma: Case report (1983) Pediatr Pathol, 1, pp. 319-323; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Am J Respir Crit Care Med, 151, pp. 879-886; Bisno, A.L., Griffin, J.P., Van Epps, K.A., Niell, H.B., Rytel, M.W., Pneumonia and Hong Kong influenza: A prospective study of the 1968-1969 epidemic (1971) Am J Med Sci, 261, pp. 251-263; Schwarzmann, S.W., Adler, J.L., Sullivan, R.J.J., Marine, W.M., Bacterial pneumonia during the Hong Kong influenza epidemic of 1968-1969 (1971) Arch Intern Med, 127, pp. 1037-1041; Couch, R.B., The common cold: Control? (1984) J Infect Dis, 150, pp. 167-173; Samo, T.C., Greenberg, S.B., Couch, R.B., Efficacy and tolerance of intranasally applied recombinant leukocyte A interferon in normal volunteers (1983) J Infect Dis, 148, pp. 535-542; Hayden, F.G., Gwaltney, J.M.J., Intranasal interferon α 2 for prevention of rhinovirus infection and illness (1983) J Infect Dis, 148, pp. 543-550; Higgins, P.G., Phillpotts, R.J., Scott, G.M., Wallace, J., Bernhardt, L.L., Tyrrell, D.A., Intranasal interferon as protection against experimental respiratory coronavirus infection in volunteers (1983) Antimicrob Agents Chemother, 24, pp. 713-715; Hayden, F.G., Albrecht, J.K., Kaiser, D.L., Gwaltney, J.M.J., Prevention of natural colds by contact prophylaxis with intranasal α 2-interferon (1986) N Engl J Med, 314, pp. 71-75; Douglas, R.M., Moore, B.W., Miles, H.B., Prophylactic efficacy of intranasal α 2-interferon against rhinovirus infections in the family setting (1986) N Engl J Med, 314, pp. 65-70; Wiselka, M.J., Nicholson, K.G., Kent, J., Cookson, J.B., Tyrrell, D.A., Prophylactic intranasal α 2-interferon and viral exacerbations of chronic respiratory disease (1991) Thorax, 46, pp. 706-711; Turner, R.B., Wecker, M.T., Pohl, G., Efficacy of tremacamra, a soluble intercellular adhesion molecule 1, for experimental rhinovirus infection: A randomized clinical trial (1999) JAMA, 281, pp. 1797-1804; Hayden, F.G., Hassman, H.A., Coats, T., Menendez, R., Bock, T., Pleconaril treatment shortens duration of picornavirus respiratory illness in adults (1999) Program and abstracts of the 39th Interscience Conference on Antimicrobial Agents and Chemotherapy Addendum (San Francisco), p. 13. , Washington. DC: American Society for Microbiology","Greenberg, S.B.; Deparment of Medicine, Baylor College of Medicine, One Baylor Plaza, 559E, Houston, TX 77030, United States; email: stepheng@bcm.tmc.edu",,,10584838,,,"10913403","English","Clin. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0034457382
"Marin J., Jeler-Kačar D., Levstek V., Maček V.","14058688700;15738467200;15738528300;6602412372;","Persistence of viruses in upper respiratory tract of children with asthma",2000,"Journal of Infection","41","1",,"69","72",,46,"10.1053/jinf.2000.0688","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033836506&doi=10.1053%2fjinf.2000.0688&partnerID=40&md5=dde9bc565a07fe50f8167c4874b5f566","Institute of Microbiology and Immunology, Medical Faculty, University of Ljubljana, Zaloaška 4, 1105 Ljubljana, Slovenia; Department of Paediatrics, University Medical Clinical Centre Ljubljana, Slovenia","Marin, J., Institute of Microbiology and Immunology, Medical Faculty, University of Ljubljana, Zaloaška 4, 1105 Ljubljana, Slovenia; Jeler-Kačar, D., Department of Paediatrics, University Medical Clinical Centre Ljubljana, Slovenia; Levstek, V., Institute of Microbiology and Immunology, Medical Faculty, University of Ljubljana, Zaloaška 4, 1105 Ljubljana, Slovenia; Maček, V., Department of Paediatrics, University Medical Clinical Centre Ljubljana, Slovenia","Objectives: Nasopharyngeal swabs of 50 asthmatic children in the symptom-free period were examined for the presence of adenoviruses, rhinoviruses and coronaviruses. A control group of 20 healthy individuals was included in this study. Methods: A polymerase chain reaction was used to detect adenovirus DNA and rhinovirus and coronavirus complementary DNA. The fragments of amplified genetic material were visualized with the use of agarose gel electrophoresis. Results: Adenovirus DNA was found in 78.4% of asthmatic children, rhinovirus RNA in 32.4% and coronavirus RNA in 2.7%. Adenovirus DNA was detected in one of the 20 nasopharyngeal swabs of healthy controls; the rest of the control samples were negative. Conclusions: The persistent presence of viruses in the upper respiratory tract of asthmatic children shows a possible connection between viral infections and asthma. (C) 2000 The British Infection Society.",,"complementary DNA; virus DNA; Adenovirus; adolescent; agar gel electrophoresis; article; asthma; child; controlled study; Coronavirus; human; nasopharynx; nonhuman; persistent virus infection; polymerase chain reaction; Rhinovirus; throat culture; upper respiratory tract infection","Furlan, J., Kandare, F., Kopriva, S., Kosnik, M., Smernice za obravnavo bolnika z astmo (1995) Zdrav Vest, 64, pp. 89-106; Corne, J., Chanarin, N., Respiratory viruses and asthma (1994) BMJ, 308, pp. 57-63; Johnston, S.L., Pattermore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, S., Role of virus infection in excerbations in children with recurrent wheeze or cough (1993) Thorax, 48, p. 1055; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) BMJ, 307, pp. 982-986; Macek, V., Sorli, J., Kopriva, S., Marin, J., Persistent adenoviral infection and chronic airway obstruction in children (1994) Am J Respir Crit Care Med, 150, pp. 7-10; Hogg, J.C., Persistent and latent viral infections in pathology of asthma (1992) Am Rev Respir Dis, 145, pp. S7-S9; Takeshi, M., Shizu, H., Kazujoshi, K., Hagen, K., Wilfred, A.J., Hogg, J.C., Latent adenoviral infection in the pathogenesis of chronic airways obstruction (1992) Am Rev Respir Dis, 146, pp. 177-184; Pattermore, P.K., Johnston, S.L., Bardin, P.G., Viruses as precipitants of asthma symptoms (1922) Clin Exptl Aller, 22, pp. 325-336; Gern, J.E., Busse, W.W., The effects of rhinovirus infections on allergic airway responses (1995) Am J Respir Crit Care Med, 152, pp. S46-S52; Barnes, P.J., New concepts in the pathogenesis of bronchial hyperrespondsivness and asthma (1989) J Allergy Clin Immunol, 833, pp. 1013-1026; Suskovic, S., Astma (1994) Zdrav Vestn, 63, pp. 149-153; Furlan, J., Mediatorji takosjsnje preobcutljivosti pri astmi (1983) Zdrav Vestn, 52, pp. 267-272; Holgate, S.T., Asthma: Past, present and future (1993) Eur Respir J, 6, pp. 1507-1520; (1995), pp. 12-14. , QIAGEN Gm bH and QIAGEN Inc. Handbook of Blood and Body Fluid Protocol; Becker, Y., Darai, G., (1995), pp. 323-327. , PCR: Protocols for Diagnosis of Human and Animal Virus Diseases. New York: Springer 349-353, 357-366; (1995), pp. 9-11. , QIAGEN GmbH and QIAGEN Inc. Handbook of RNeasy Total RNA Purification Protocol; Beasley, R., Coleman, E.D., Hermon, Y., Holst, P.E., O'Donnell, T.V.O., Tobias, M., Viral respiratory tract infection and excerbations of asthma in adult patients (1988) Thorax, 43, pp. 679-683; Monto, A.S., Sullivan, K.M., Acute respiratory illness in the community. Frequency of illness and the agents involved (1993) Epidemiol Infect, 110, pp. 145-160; Johnston, S.L., Viruses and asthma (1998) Allergy, 53, pp. 922-932; Wege, H., Siddell, S., ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-175; Hendley, J.O., Gwaltney, J.M., Mechanism of transmission of rhinovirus infections (1988) Epidemiol Rev, 10, pp. 242-253; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus colds in normal and asthmatic subjects (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and asthmatic subjects (1995) Am J Respir Crit Care Med, 151, pp. 879-886; Prince, G.A., Porter, D.D., Treatment of parainfluenza type 3 bronchiolitis and pneumonia in a cotton rat model using topical antibody and glucocorticoid (1996) J Infect Dis, 173, pp. 598-608; Hall, C.B., Powell, K.R., MacDonald, N.E., Respiratory syncytial viral infection in children with compromised immune function (1986) New Engl J Med, 315, pp. 77-81","Marin, J.; Institute of Microbiology/Immunology, Medical Faculty, University of Ljubljana, Zaloska 4, 1105 Ljubljana, Slovenia",,"W.B. Saunders Ltd",01634453,,JINFD,"10942643","English","J. Infect.",Article,"Final",,Scopus,2-s2.0-0033836506
"Kimber K.R., Kollias G.V., Dubovi E.J.","6602151124;57210355296;7005099381;","Serologic survey of selected viral agents in recently captured wild north american river otters (lontra canadensis)",2000,"Journal of Zoo and Wildlife Medicine","31","2",,"168","175",,28,"10.1638/1042-7260(2000)031[0168:SSOSVA]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034207931&doi=10.1638%2f1042-7260%282000%29031%5b0168%3aSSOSVA%5d2.0.CO%3b2&partnerID=40&md5=cfe7d22dd3dbfee0bd14b57655ce1b66","Wildlife Health Laboratory, Department of Clinical Sciences, Cornell University, Ithaca, NY 14853, United States; New York State Vet. Diagn. Lab., College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Kimber, K.R., Wildlife Health Laboratory, Department of Clinical Sciences, Cornell University, Ithaca, NY 14853, United States; Kollias, G.V., Wildlife Health Laboratory, Department of Clinical Sciences, Cornell University, Ithaca, NY 14853, United States; Dubovi, E.J., New York State Vet. Diagn. Lab., College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Blood samples were collected from 64 wild North American river otters (Lontra [Lutra] canadensis) from northern and eastern New York State and analyzed for serologic evidence of exposure to selected viral agents during a 1995-1996 translocation program. No clinical signs of disease nor lesions suggestive of prior viral exposure were seen. Titers were detected for antibodies against canine distemper virus, canine herpesvirus-1, and canine parvovirus-2 but not for antibodies against canine adenovirus-1, canine coronavirus, canine parainfluenza virus, rabies virus, feline herpesvirus-1, feline calicivirus, or feline coronavirus. This is the first report of titers for antibodies against canine herpesvirus-1 in North American river otters, and it suggests a low prevalence of antibody titers against most canine viruses in otter populations in northern and eastern New York. Confounding variables in this study could include exposure to domestic dogs associated with the project, prolonged time spent in captivity, and concurrent bacterial or parasitic infection. Stress-associated humoral immune suppression could have altered serologic profiles, especially in otters exposed to dogs after trapping but before venipuncture.","Disease; Lontra canadensis; Otter; Serology; Virus","Adenovirus; animal; animal disease; article; Canine distemper morbillivirus; Carnivora; Coronavirus; dog; dog disease; environmental protection; epidemiology; female; Herpes virus infection; isolation and purification; male; Paramyxovirus; rabies; Rabies virus; serodiagnosis; United States; Varicella zoster virus; virology; virus infection; Adenoviridae; Adenoviridae Infections; Animals; Conservation of Natural Resources; Coronaviridae Infections; Coronavirus; Distemper; Distemper Virus, Canine; Dogs; Female; Herpesviridae Infections; Herpesvirus 1, Canid; Male; Neutralization Tests; New York; Otters; Paramyxoviridae; Paramyxoviridae Infections; Rabies; Rabies virus; Seroepidemiologic Studies","Appel, M., Robson, D.S., A microneutralization test for canine distemper virus (1973) Am. J. Vet. Res., 34, pp. 1459-1463; Barker, I.K., Povey, R.C., Voight, D.R., Response of mink, skunk, red fox, and raccoon, to inoculation with mink virus enteritis, feline panleukopenia, and canine parvovirus and prevalence of antibody to parvovirus in wild carnivores in Ontario (1983) Can. J. Comp. Med., 47, pp. 188-197; Baumgärtner, W., Krakowka, S., Gorham, J.R., Canine parainfluenza virus-induced encephalitis in ferrets (1989) J. Comp. Pathol., 100, pp. 67-76; Budd, J., Distemper (1981) Infectious Diseases of Wild Mammals, 2nd Ed., pp. 31-43. , Davis, J. W., L. H. Karstad, and D. O. Trainer (eds.). Iowa State Univ. Press, Ames, Iowa; Cabasso, V.J., Stebbins, M.R., Norton, T.W., Cox, H.R., Propagation of infectious canine hepatitis virus in tissue culture (1954) Proc. Soc. Exp. Biol. Med., 85, pp. 239-245; Carmichael, L.E., Joubert, J., Pollock, R.V.H., Hemagglutination by canine parvovirus: Serologic studies and diagnostic applications (1980) Am. J. Vet. Res., 41, pp. 784-789; Carpenter, J.W., Appel, M.J.G., Erickson, R.C., Novilla, M.N., Fatal vaccine-induced canine distemper virus infection in black-footed ferrets (1976) J. Am. Vet. Med. Assoc., 169, pp. 961-964; Christian, J., Ratcliffe, H.L., Shock disease in captive wild mammals (1952) Am. J. Pathol., 23, pp. 725-737; Davidson, W.R., Appel, M.J., Doster, G.L., Baker, O.E., Brown, J.F., Diseases and parasites of red foxes, gray foxes, and coyotes from commercial source selling to fox-chasing enclosures (1992) J. Wildl. Dis., 28, pp. 581-589; Dinnes, M.R., Medical care of non-domestic carnivores (1980) Current Veterinary Therapy VII: Small Animal Practice, pp. 710-733. , Kirk, R. W. (ed.). W. B. Saunders Co., Philadelphia, Pennsylvania; Donis, R.O., Dubovi, E.J., Molecular specificity of the antibody responses of cattle naturally infected with cytopathic and noncytopathic bovine viral diarrhea virus biotypes (1987) Am. J. Vet. Res., 48, pp. 1549-1554; Duplaix-Hall, N., River otters in captivity: A review (1975) Breeding Endangered Species in Captivity, pp. 315-327. , Martin, R. D. (ed.). Academic Press, New York, New York; Durchfeld, B., Baumgärtner, W., Krakowka, S., Intranasal infection of ferrets (Mustela putorius furo) with canine parainfluenza virus (1991) J. Vet. Med. Ser. B, 38, pp. 505-512; Forrester, D.J., (1992) Parasites and Diseases of Wild Mammals in Florida, pp. 151-162. , Univ. Press of Florida, Gainesville, Florida; Foster-Turley, P., Macdonald, S., Mason, C., (1990) Otters: An Action Plan for Their Conservation, , International Union for Conservation of Nature and Natural Resources, Gland, Switzerland; Fowler, M.E., (1986) Zoo and Wild Animal Medicine, 2nd Ed., , W B. Saunders Co., Philadelphia, Pennsylvania; Fox, J.G., (1988) Biology and Diseases of the Ferret, , Lea and Febiger, Philadelphia, Pennsylvania; Geisel, V.O., Staupe bei Fischottern (Lutra lutra) (1979) Berl. Muench. Tieracrzl. Wochenschr., 92, p. 304; Harder, T.C., Osterhaus, A.D.M.E., Canine distemper virus - A morbillivirus in search of new hosts? (1997) Trends Microbiol., 5, pp. 120-124; Hoover, J.P., Castro, A.E., Nieves, M.A., Serologic evaluation of vaccinated American river otters (1985) J. Am. Vet. Med. Assoc., 187, pp. 1162-1165; Jalkotzy, M.G., (1985) Reintroduction of River Otters in Kananaskis Country, Alberta, , National Library of Canada, Ottawa, Ontario, Canada; Jamison, R.K., Lazar, E.C., Binn, L.N., Alexander, A.D., Survey for antibodies to canine viruses in selected wild mammals (1973) J. Wildl. Dis., 9, pp. 2-3; Kenyon, A.J., Kenyon, B.J., Hahn, E.C., Protides of the Mustelidae: Immunoresponse of mustelids to Aleutian mink disease virus (1978) Am. J. Vet. Res., 39, p. 1011; Kimber, K.R., (1998) Analysis of Parameters Used to Evaluate Recently Captured North American River Otters (Lontra Canadensis) Involved in a Population Restoration Project, , M.S. Thesis, Cornell Univ., Ithaca, New York; Kollias, G.V., Health assessment, medical management and pre-release conditioning of translocated North American river otters (Lontra canadensis) (1999) Zoo and Wild Animal Medicine: Current Therapy, 4, pp. 443-448. , Miller, R. E., and M. E. Fowler (eds.). W. B. Saunders, Philadelphia, Pennsylvania; Kollias, G.V., McDonough, P., Valentine, B., Hartup, B.K., Abou-Madi, N., Kimber, K.R., Gentz, E., Clostridium perfringens enterotoxicosis in recently captured North American river otters (Lontra canadensis) (1998) Proc. Am. Assoc. Zoo Vet., Am. Assoc. Wildl. Vet., 1998, pp. 61-62. , Omaha, Nebraska; McDonald, K.P., (1989) Survival, Home Range, Movements, Habitat Use, and Feeding Habits of Reintroduced River Otters in Ohio, , M.S. Thesis, Ohio State Univ., Columbus, Ohio; McMaster, G.K., Tratschini, J.D., Siegl, G., Comparison of canine parvovirus with mink enteritis virus by restriction site mapping (1981) J. Virol., 38, pp. 368-371; Monson, R.A., Stone, W.B., Canine distemper in wild carnivores in New York (1976) N. Y. Fish Game J., 23, pp. 149-154; Olsen, G.H., Linhart, S.B., Holmes, R.A., Dasch, G.J., Male, C.B., Injuries to coyotes caught in padded and unpadded steel foothold traps (1986) Wildl. Soc. Bull., 14, pp. 219-223; Parrish, C.R., Emergence, natural history, and variation of canine, mink, and feline parvoviruses (1990) Adv. Virus Res., 38, pp. 403-450; Parrish, C.R., Gorham, J.R., Schwartz, T.M., Carmichael, L.E., Characterization of antigenic variation among mink enteritis virus isolates (1984) Am. J. Vet. Res., 45, pp. 2591-2599; Parrish, C.R., Leathers, C.W., Pearson, R., Gorham, J.R., Comparisons of feline panleukopenia virus, canine parvovirus, raccoon parvovirus, and mink enteritis virus and their pathogenicity for mink and ferrets (1987) Am. J. Vet. Res., 48, pp. 1429-1435; Phillips, M.K., Smith, D.W., (1996) The Wolves of Yellowstone, , Voyageur Press, Stillwater, Minnesota; Ralls, K., Reintroductions (1990) Otters: An Action Plan for Their Conservation, pp. 20-21. , Foster-Turley, P., S. Macdonald, and C. Mason (eds.). Kelvyn Press, Inc., Broadview, Illinois; Roelke, M.E., Jacobson, E.R., Kollias, G.V., Forrester, D.J., Medical Management and Biomedical Findings on the Florida Panther, Felis concolor coryi, July 1, 1985 to June 30, 1986 (1985) Annual Report Presented to the Florida Panther Research Team, Florida Game and Fresh Water Fish Commission, , Gainesville, Florida; Serfass, T.L., Whary, M.T., Peper, R.L., Brooks, R.P., Swimley, T.J., Lawrence, W.R., Rupprecht, C.E., Rabies in a river otter (Lutra canadensis) intended for reintroduction (1995) J. Zoo Wildl. Med., 26, pp. 311-314; Spellman, L.H., North American river otter (Lutra canadensis) translocation in North Carolina 1989-1996 (1998) Proc. Bur. Assoc. Zoo Wildl. Vet., 1998, pp. 461-465. , Chester, United Kingdom; Stanley Price, M.R., A review of mammal re-introductions, and the role of the Re-introduction Specialist Group of IUCN/SSC (1991) Symp. Zool. Soc. Lond., 62, pp. 9-25; Gipps, J.H.W., Beyond Captive Breeding, pp. 9-25. , Oxford Science Publishing, New York, New York; Swango, L.J., Canine viral diseases (1995) Textbook of Veterinary Internal Medicine: Diseases of the Dog and Cat, pp. 398-409. , Ettinger, S. J., and E. C. Feldman (eds.). W. B. Saunders Co., Philadelphia, Pennsylvania; Trimarchi, C.V., Rudd, R.D., Stafford Jr., M., In vitro virus neutralization test for rabies antibodies (1996) Laboratory Techniques in Rabies, 4th Ed., pp. 193-199. , Meslin, F. X., M. M. Kaplan, and H. Koprowski (eds.). World Health Organization, Geneva, Switzerland; Van De Grift, E.R., Possible feline infectious peritonitis in short-clawed otters, Aonyx cinerea (1976) J. Zoo Anim. Med., 7, p. 18; De Van Zyll Jong, C.G., A phylogenetic study of the Lutrinae (Carnivora; Mustelidae) using morphological data (1987) Can. J. Zool., 65, pp. 2536-2544; De Van Zyll Jong, C.G., A systematic review of the nearctic and neotropical river otters (Genus Lutra, Mustelidae, Carnivora) (1972) R. Ont. Mus. Life Sci. Contrib., 80, pp. 1-104; Wallach, J.D., Boever, W.J., (1983) Diseases of Exotic Animals, pp. 495-533. , W. B. Saunders Co., Philadelphia, Pennsylvania; Wells, G.A.H., Suspected Aleutian disease in a wild otter (1989) Vet. Rec., 125, pp. 232-235; Williams, E.S., Thorne, E.T., Appel, M.J.G., Belitsky, D.W., Canine distemper in black-footed ferrets from Wyoming (1988) J Wildl. Dis., 24, pp. 385-398","Kimber, K.R.; Wildlife Health Laboratory, Department of Clinical Sciences, Cornell University, Ithaca, NY 14853, United States",,"American Association of Zoo Veterinarians",10427260,,,"10982127","English","J. Zoo Wildl. Med.",Review,"Final",,Scopus,2-s2.0-0034207931
"Uyar Y., Gunaydin M., Cetin M.","6602749434;16746539800;57212696102;","Investigation of viral etiology in lower respiratory tract infections in children by indirect immunofluorescence method [Alt solunum yolu enfeksiyonu olan cocuklarda viral etiyolojinin indirek immunofloresan yontemiyle arastirilmasi]",2000,"Mikrobiyoloji Bulteni","34","3-4",,"339","345",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033763740&partnerID=40&md5=dd32f0cc032d74fe9e31e9518444d259","Ondokuz Mayis Universitesi, Tip Fakultesi Mikrobiyoloji, Klinik Mikrobiyoloji Anabilim Dali, Samsun, Turkey","Uyar, Y., Ondokuz Mayis Universitesi, Tip Fakultesi Mikrobiyoloji, Klinik Mikrobiyoloji Anabilim Dali, Samsun, Turkey; Gunaydin, M., Ondokuz Mayis Universitesi, Tip Fakultesi Mikrobiyoloji, Klinik Mikrobiyoloji Anabilim Dali, Samsun, Turkey; Cetin, M., Ondokuz Mayis Universitesi, Tip Fakultesi Mikrobiyoloji, Klinik Mikrobiyoloji Anabilim Dali, Samsun, Turkey","In this study, to investigate the viral etiology of lower respiratory tract infections (LRTI) in our region, the nasopharyngeal aspirate (NPA) samples of 124 pediatric patients (age range: 0-5 years) with LRTI were prospectively collected and studied by indirect immunofluorescence assay (IFA) with the use of monoclonal antibodies against Respiratory Syncytial Virus (RSV), Parainfluenza virus type 1, 2, 3, Influenza virus type A and B, Coronavirus and Adenovirus antigens. Of 124 NPA samples, 35 (28.2%) were found positive by means of viral antigens and RSV was the most common etiologic agent with a rate of 40% (14/35), followed by Parainfluenza virus types (10/35, 28.6%), Influenza B virus (4/35, 11.4%), Coronavirus (3/35, 8.6%), Influenza A virus (2/35, 5.7%) and Adenovirus (2/35, 5.7%). Laboratory diagnosis of RSV infections which are very common in winter season, depends on the isolation from tissue cultures that is known to be the gold standard, is time consuming and expensive. Therefore, to search the RSV antigens routinely by IFA method in NPA samples will be more appropriate for rapid diagnosis.","Direct immunofluorescence antibody method; Lower respiratory tract infections; RSV","monoclonal antibody; virus antigen; Adenovirus; article; child; Coronavirus; enzyme immunoassay; human; immunofluorescence; infant; Influenza virus; lower respiratory tract infection; major clinical study; Parainfluenza virus; Respiratory syncytial pneumovirus; tissue culture; virus infection","Grossman, M., Viral repiratory infections, pp: 573-578 (1987), 8. , Rudolph AM (Ed), Pediatrics; Floyd, W., Denny, M.D., Acute respiratory infections in children. Etiology and epidemiology (1987) Pediatr Rev, 9, pp. 135-145; Levy, B.T., Graber, M.A., Respiratory syncytial virus infection in infants and young children (1997) J Fam Pract, 6, pp. 437-481; Adcock, P.M., Stout, G.G., Hauck, M.A., Marshall, G.S., Effect of rapid viral diagnosis on the management of children hospitalized with lower respiratory tract infection (1997) Pediatr Infect Dis J, 16, pp. 842-846; Yilmaz, G., Bozkaya, E., Turkoglu, S., Cesitli viral etkenlerin nazofarinks aspirasyon sivisinda immunofloresan yontemi ile saptanmasi (1991) Klimik Derg, 4 (2), pp. 74-76; Minnich, L.L., Smith, T.F., Ray, C.G., Specter, S., Rapid detection of viruses by immunofluorescence (1988) Cumitech, 24, pp. 1-13; Yilmaz, G., Akut alt solunum yolu infeksiyonlu cocuklarda Respiratory Syncytial Virus (RSV) ile infeksiyon prevalansi ve RSV alt tipleri (1997) Istanbul Universitesi Istanbul Tip Fakultesi, Viroloji Yandal Uzmanlik Tezi, 1997, Istanbul; Miller, H.R., Phipps, P.H., Rossier, E., Reduction of nonspesific fluorescence in respiratory specimens by pretreatment with N-Acetylcysteine (1986) J Clin Microbiol, 24 (3), pp. 470-471; Ahluwalia, G., Embree, J., McNikol, P., Law, B., Hammond, G.W., Comparison of nasopharyngeal aspirate and nasopharyngeal swab specimens for respiratory syncytial virus diagnosis by cell culture, indirect immunofluorescence assay and enzyme-linked immunosorbent assay (1987) J Clin Microbiol, 25, pp. 763-767; Dominguez, E.A., Taber, L.H., Couch, R.B., Comparison of rapid diagnostic techniques for respiratory syncytial and influenza A virus respiratory infections in young children (1993) J Clin Microbiol, 31, pp. 2286-2290; Woo, P.Y.C., Chiu, S.S., Seto, W.H., Peiris, M., Cost-effectiveness of rapid diagnosis of viral respiratory tract infections in pediatric patients (1997) J Clin Microbiol, 35, pp. 1579-1581; Kaul, A., Scott, R., Gallagher, M., Scott, M., Clement, J., Ogra, P.L., Respiratory syncytial virus infection. Rapid diagnosis in children by use of indirect immunofluorescence (1978) Am J Dis Child, 132 (11), pp. 1088-1090; Pothier, P., Denoyel, G.A., Ghim, S., Prudhomme de Saint Maur, G., Freymuth, F., Use of monoclonal antibodies for rapid detection of influenza A virus in nasopharyngeal secretions (1986) Eur J Microbiol, 5 (3), pp. 336-339; McQuillin, J., Madeley, C.R., Kendal, A.P., Monoclonal antibodies for rapid diagnosis of influenza A and B virus by immunofluorescence (1985) Lancet, 26 (2), pp. 911-914; Siqueira, M.M., Ferreira, V., Nascimento, J.P., Respiratory syncytial virus diagnosis: Comparison of isolation, immunofluorescence and enzyme immunoassay (1986) Mem Inst Oswaldo Cruz, 81 (2), pp. 225-232; Swenson, P.D., Kaplan, M.H., Rapid detection of Respiratory Syncytial Virus in nasopharyngeal aspirates by commercial enyzme immunoassay (1986) J Clin Microbiol, 23 (3), pp. 485-488; Koneman, E.W., Allen, S.D., Janda, W.M., Schreckenberger, W.C., Diagnosis of infections caused by viruses, chlamydia, rickettsia, and related organisms (1997), 5, pp. 1252-1253. , Color Atlas and Textbook of Diagnostic Microbiology. 5(th) ed, Lippincott Raven Publishers, Philadelphia; Ozacar, T., Zeytinoglu, A., Ozdogru, E., Aydemir, S., Tanac, R., Bilgic, A., Alt solunum yolu infeksiyonu olan cocuklarda Respiratory Sinsityal Virus antijenlerinin arastirilmasi (1996) Infeks Derg, 10, pp. 25-28; Dereli, D., Ertem, M., Serter, D., Sadiment, M., Coker, M., Tanac, R., Detection of Respiratory Syncytial Virus in children in the 1993-1994 winter season in Izmir, Turkey, by two diagnostic methods (1994) APMIS, 102 (11), pp. 877-879; Sayiner, A.A., Erbaycu, O.O., Yuksel, H., Zeytinoglu, A., Tanac, R., Bilgic, A., Alt solunum yolu infeksiyonlu cocuklarda solunum viruslari antijenlerinin araatirilmasi. 8. (1997) Turk Klinik Mikrobiyoloji ve Infeksiyon Hastaliklari Kongresi, 6-10 Ekim 1997, Antalya. Ozet Kitabi, p. 363; Ozsan, M., Kahraman, H., Klinik olarak alt solunum yolu enfeksiyonu tanisi konulan 0-1 yas, grubu bebeklerde solunum sinsityal virus antijenlerinin arastirilmasi (1998) Mikrobiyol Bult, 32, pp. 51-56; Freymuth, F., Eugene, G., Vabret, A., Detection of Respiratory Syncytial Virus by reverse transcription-PCR and hybridization with a DNA enzyme immunoassay (1995) J Clin Microbiol, 33 (12), pp. 3352-3355; Siqueira, M.M., Nascimento, J.P., Portes, S.A., Schuy, W., Enzyme immunoassay for Respiratory Syncytial Virus: Rapid detection in nasopharyngeal secretions and evaluation of isolates representing different RSV subgroups (1993) J Clin Lab Anal, 7 (2), pp. 130-133; Woodtayakorn, J., Punnarugsa, V., Comparative study of Respiratory Syncytial Virus in nasopharyngeal aspirates using conventional cell culture, shell viral centrifugation culture, immunofluorescence and biotin-avidin enzyme linked immunosorbent assays (1991) Asian Pac J Allergy Immunol, 9 (2), pp. 121-124; John, M., Cherian, T., Christuraj, S., John, T.J., Comparison of immunofluorescence culture for the diagnosis of Respiratory Syncytial Virus infection (1990) Indian J Med Res, 91, pp. 242-244; Grover, S., Watkins, P., Orvell, C., Booth, J., Comparison of direct immunofluorescence of exfoliated cells, tissue culture immunofluorescence and conventional virus isolation for the diagnosis of respiratory virus infection (1990) Serodiagn Immunother Infect Dis, 4, pp. 59-66","Uyar, Y.; Ondokuz Mayis Universitesi, Tip Fakultesi Mikrobiyoloji, Klinik Mikrobiyoloji Anabilim Dali, Samsun, Turkey",,,03749096,,MIBUB,,"Turkish","Mikrobiyol. Bul.",Article,"Final",,Scopus,2-s2.0-0033763740
"Ali A., Reynolds D.L.","57198724268;7401431695;","Characterization of the stunting syndrome agent: Relatedness to known viruses",2000,"Avian Diseases","44","1",,"45","50",,11,"10.2307/1592506","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034023018&doi=10.2307%2f1592506&partnerID=40&md5=1b056ce7f62466a7f067a76eab0acd7a","Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","Ali, A., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States; Reynolds, D.L., Vet. Medical Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States","An enteric disease of young turkeys, referred to as stunting syndrome (SS), causes reduced growth and impaired feed efficiency. A recently isolated virus, stunting syndrome agent, (SSA) has been found to be the etiologic agent of SS. The objective of the present study was to determine relatedness of the SSA with other viral agents. Serologic (viral neutralization and enzyme-linked immunosorbent assay [ELISA]) assays and a reverse transcriptase-polymerase chain reaction (RT-PCR) were used. The antisera against turkey enteric coronavirus (bluecomb agent), bovine coronavirus (BCV), bovine Breda-1 virus, bovine Breda-2 virus, avian infectious bronchitis virus (IBV), avian influenza virus, Newcastle disease virus (NDV), and transmissible gastroenteritis virus (TGEV) of swine were evaluated by dot-immunobinding avidin-biotin-enhanced ELISA and did not react with SSA. The homologous (anti-SSA) antiserum was positive by ELISA. Similarly, anti-SSA antiserum did not react when NDV, IBV, BCV, or TGEV was used as antigen but did react with the homologous (SSA) virus. The virus neutralization assay was performed by inoculating 24-to-25-day-old turkey embryos via the amniotic route and by assessing the embryo infectivity on the basis of gross intestinal lesions and intestinal maltase activity at 72 hr postinoculation. None of the aforementioned antisera neutralized SSA infectivity in embryos except for the homologous anti-SSA antiserum. A RT-PCR was performed with known primers specific for NDV, IBV, BCV, and TGEV. The known primers failed to amplify SSA genome but amplified their respective viral genomes. We concluded that the SSA was distinct from the viral agents that were evaluated.","ELISA; Enteric virus; RT-PCR; Serum virus neutralization; Stunting syndrome; Stunting syndrome agent; Turkey embryos","antibody specificity; Avian infectious bronchitis virus; avian influenza virus; bovine Breda virus 1; bovine Breda virus 2; Coronavirus; Newcastle disease paramyxovirus; serodiagnosis; stunting syndrome; Transmissible gastroenteritis virus; turkey; turkey enteric coronavirus; viral genetics; virus detection; virus genome; virus infectivity; Animalia; Aves; Avian infectious bronchitis virus; Avian influenza virus; Bovinae; Bovine coronavirus; Breda virus; Coronavirus; DNA viruses; Enteric coronavirus; gastroenteritis virus of swine; Influenza virus; Newcastle disease virus; Paramyxoviridae; Sus scrofa; Transmissible gastroenteritis virus; Turkey coronavirus","Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathol., 25, pp. 817-836; Alexander, D.J., Newcastle disease virus and other paramyxoviruses (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 156-163. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Redd, eds. American Association of Avian Pathologists, Kennett Square, PA; Alexander, D.J., Collins, M.S., The structural polypeptides of avian paramyxoviruses (1981) Arch. Virol., 67, pp. 309-323; Ali, A., Reynolds, D.L., Stunting syndrome in turkey poults: Isolation and identification of the etiologic agent (1997) Avian Dis., 41, pp. 870-881; Ali, A., Reynolds, D.L., The in vitro propagation of stunting syndrome agent (1998) Avian Dis., 42, pp. 657-666; Angel, C.R., Sell, J.L., Trampel, D.W., Stunting syndrome in turkeys: Development of an experimental model (1990) Avian Dis., 34, pp. 447-453; Cavanagh, D., Structural characterization of infectious bronchitis virus glycoproteins (1984) Adv. Exp. Med. Biol., 173, pp. 95-108; Cummins, D.R., Reynolds, D.L., Rhoades, K.R., An avidin-biotin enhanced dot-immunobinding assay for the detection of mycoplasma gallisepticum and M. Synoviae serum antibodies in chickens (1990) Avian Dis., 34, pp. 36-43; Dea, S., Verbeek, A.J., Tijssen, P.J., Antigenic and genomic relationship among turkey and bovine enteric coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Gelb J., Jr., Jackwood, M.W., Infectious bronchitis (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 169-174. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Redd, eds. American Association of Avian Pathologists, Kennett Square, PA; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Field's Virology, 3rd Ed., pp. 1075-1093. , B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus, eds. Lippincott-Raven Publ., Philadelphia, PA; James, K., Immunoserology of infectious diseases (1990) Clin. Microbiol. Rev., 3, pp. 132-152; Jestin, V., Jestin, A., Detection of Newcastle disease virus RNA in infected allantoic fluids by in vitro enzymatic amplification (1991) Arch. Virol., 118, pp. 151-161; Lennette, E.H., Halonen, P., Murphey, F.A., Laboratory diagnosis of infectious diseases. Principles and practice (1988) Viral, Rickettsial and Clamydial Diseases, 2. , Springer-Verlag, New York; McLoughlin, M.F., McLoone, D.A., Conner, T.J., Runting and stunting syndrome in turkeys (1987) Vet. Rec., 121, pp. 583-586; Persing, D.H., (1996) PCR-protocols for Emerging Infectious Diseases; a Supplement to Diagnostic Molecular Biology: Principles and Applications, , American Society for Microbiology Press, Washington, DC; Snyder, D.B., Marquardt, W.W., Enzyme immunoassay for poultry disease monitoring (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 3rd Ed., pp. 201-207. , H. G. Purchase, L. H. Arp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Stauber, N., Brechtbuhl, K., Bruchkner, L., Hoffman, M.A., Detection of Newcastle disease virus in poultry vaccine using polymerase chain reaction and direct sequencing of amplified cDNA (1995) Vaccine, 13, pp. 360-364; Thayer, S.G., Beard, C.W., Serologic procedures (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 255-266. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Redd, eds. American Association of Avian Pathologists, Kennett Square, PA; Tijssen, P., Hybridization with nucleic acid probes (1993) Laboratory Techniques in Biochemistry and Molecular Biology, 24. , Elsevier Publ., New York; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J Gen. Virol., 72, pp. 1659-1666; White, B.A., PCR protocols: Current methods and applications (1993) Methods in Molecular Biology, 15. , Humana Press, Totowa, NJ","Reynolds, D.L.; Veterinary Med. Research Institute, College of Veterinary Medicine, Iowa State University, 1802 Elwood Drive, Ames, IA 50011, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"10737643","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0034023018
"Molenkamp R., Greve S., Spaan W.J.M., Snijder E.J.","6603227562;6506902225;7007172944;7006058325;","Efficient homologous RNA recombination and requirement for an open reading frame during replication of equine arteritis virus defective interfering RNAs",2000,"Journal of Virology","74","19",,"9062","9070",,20,"10.1128/JVI.74.19.9062-9070.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033803593&doi=10.1128%2fJVI.74.19.9062-9070.2000&partnerID=40&md5=eadf3263ba5e72b8c188bc73ccec7d7d","Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands","Molenkamp, R., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Greve, S., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Snijder, E.J., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands","Equine arteritis virus (EAV), the prototype arterivirus, is an enveloped plus-strand RNA virus with a genome of approximately 13 kb. Based on similarities in genome organization and protein expression, the arteriviruses have recently been grouped together with the coronaviruses and toroviruses in the newly established order Nidovirales. Previously, we reported the construction of pEDI, a full-length cDNA copy of EAV DI-b, a natural defective interfering (DI) RNa of 5.6 kb (R. Molenkamp et al., J. Virol. 74:3156-3165, 2000). EDI RNA consists of three noncontiguous parts of the EAV genome fused in frame with respect to the replicase gene. As a result, EDI RNA contains a truncated replicase open reading frame (EDI-ORF) and encodes a truncated replicase polyprotein. since some coronavirus DI RNAs require the presence of an ORF for their efficient propagation, we have analyzed the importance of the EDI-ORF in EDI RNA replication. The EDI-ORF was disrupted at different positions by the introduction of frameshift mutations. These were found either to block DI RNA replication completely or to be removed within one virus passage, probably due to homologous recombination with the helper virus genome. Using recombination assays based on EDI-RNA and full-length EAV genomes containing specific mutations, the rates of homologous RNA recombination in the 3'- and 5'-proximal regions of the EAV genome were studied. Remarkably, the recombination frequency in the 5'-proximal region was found to be approximately 100-fold lower than that in the 3'-proximal part of the genome.",,"recombinant RNA; RNA directed RNA polymerase; animal cell; article; Coronavirus; Equine viral arteritis virus; gene mutation; genetic recombination; nonhuman; open reading frame; priority journal; protein expression; sequence homology; Torovirus; virus genome; virus replication; Animal; Arteritis Virus, Equine; Gene Expression Regulation, Viral; Open Reading Frames; Recombination, Genetic; RNA, Viral; Support, Non-U.S. Gov't; Virus Replication","Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Baric, R.S., Schaad, M.C., Wei, T., Fu, K.S., Lum, K., Shieh, C., Stohlman, S.A., Murine coronavirus temperature sensitive mutants (1990) Adv. Exp. Biol. 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Virol., 70, pp. 1588-1595; Molenkamp, R., Rozier, B.C.D., Greve, S., Spaan, W.J.M., Snijder, E.J., Isolation and characterization of an arterivirus defective interfering RNA genome] (2000) J. Virol., 74, pp. 3156-3165; Nagy, P.D., Bujarski, J.J., Genetic recombination in brome mosaic virus: Effect of sequence and replication of RNA on accumulation of recombinants (1992) J. Virol., 66, pp. 6824-6828; Nagy, P.D., Bujarski, J.J., Targeting the site of RNA-RNA recombination in brome mosaic virus with antisense sequences (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 6390-6394; Pedersen, K.W., Van der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) J. 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Exp. Biol. Med., 380, pp. 499-506; Snijder, E.J., Sawicki, D.L., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Snijder, E.J., Van Tol, H., Pedersen, K.W., Raamsman, M.J.B., De Vries, A.A.F., Identification of a novel structural protein of arteriviruses (1999) J. Virol., 73, pp. 6335-6345; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., Proteolytic processing of the replicase ORF1a protein of equine arteritis virus (1994) J. Virol., 68, pp. 5755-5764; Snijder, E.J., Wassenaar, A.L.M., Van Dinten, L.C., Spaan, W.J.M., The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases (1996) J. Biol. Chem., 271, pp. 4864-4871; Spaan, W.J.M., Delius, H., Skinner, M., Armstrong, J., Rottier, P.J.M., Smeekens, S., Van der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Van der Meer, Y., Van Tol, H., Locker, K.J., Snijder, E.J., ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex (1998) J. Virol., 72, pp. 6689-6698; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3' end of the pol gene is essential for encapsidation of coronaviral defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van der Most, R.G., Heijnen, L., Spaan, W.J., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Van der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation which abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Van Dinten, L.C., Rensen, S., Spaan, W.J.M., Gorbalenya, A.E., Snijder, E.J., Proteolytic processing of the ORF1b-encoded part of the arterivirus replicase is mediated by the nsp4 serine protease and is essential for virus replication (1999) J. Virol., 73, pp. 2027-2037; Van Dinten, L.C., Wassenaar, A.L.M., Gorbalenya, A.E., Spaan, W.J.M., Snijder, E.J., Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) J. Virol., 70, pp. 6625-6633; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base-pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA., 96, pp. 12056-12061; Van Marle, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Wassenaar, A.L.M., Spaan, W.J.M., Gorbalenya, A.E., Snijder, E.J., Alternative proteolytic processing of the arterivirus ORF1a polyprotein: Evidence that nsp2 acts as a cofactor for the nsp4 serine protease (1997) J. Virol., 71, pp. 9313-9322; White, C.L., Thomson, M., Dimmock, N.J., Deletion analysis of a defective interfering Semliki Forest virus RNA genome defines a region in the nsp2 sequence that is required for efficient packaging of the genome into virus particles (1998) J. Virol., 72, pp. 4320-4326; Yeh, T.Y., Lin, B.Y., Chang, Y.C., Hsu, Y.H., A defective RNA associated with bamboo mosaic virus and the possible common mechanisms for RNA recombination in potexviruses (1999) Virus Genes, 18, pp. 121-128; Yuan, S., Nelsen, C.J., Murtaugh, M.P., Schmitt, B.J., Faaberg, K.S., Recombination between North American strains of porcine reproductive and respiratory syndrome virus (1999) Virus Res., 61, pp. 87-98","Snijder, E.J.; Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; email: E.J.Snijder@LUMC.nl",,,0022538X,,JOVIA,"10982351","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033803593
"Taguchi F., Shimazaki Y.K.","7103209890;36944983600;","Functional analysis of an epitope in the S2 subunit of the murine coronavirus spike protein: Involvement in fusion activity",2000,"Journal of General Virology","81","12",,"2867","2871",,32,"10.1099/0022-1317-81-12-2867","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034528210&doi=10.1099%2f0022-1317-81-12-2867&partnerID=40&md5=6f3dee3b51d0361cfb408e7dfe91a802","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Shimazaki, Y.K., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","The monoclonal antibody (MAb) 5B 19.2, which has virus-neutralizing and fusion inhibition activities, binds to an epitope (S2A) consisting of nine hydrophobic amino acids in the S2 subunit of the mouse hepatitis virus (MHV) spike (S) protein. This suggests that the S2A epitope may be involved in binding the virus to the MHV receptor and/or in virus-cell fusion. Co-immunoprecipitation analyses demonstrated that while the binding of virus to the receptor was blocked by anti-S1 MAbs, it was not blocked by the S2A antiserum, indicating that S2A was not involved in receptor-binding. The S proteins prepared in this study with mutations in the S2A epitope were either fusogenic or non-fusogenic and their fusogenicity did not correlate with the hydrophobic feature of the S2A epitope. All of these wt and mutated S proteins were similarly transported onto the cell membrane independent of their fusogenicity capability. These results suggest that S2A may mediate the fusion activity of the MHV S protein during virus entry into cells.",,"antiserum; epitope; monoclonal antibody; monoclonal antibody 5b19 2; mutant protein; protein subunit; unclassified drug; virus protein; virus receptor; article; cell fusion; cell membrane transport; controlled study; hydrophobicity; immunoprecipitation; Murine hepatitis coronavirus; mutation; nonhuman; priority journal; receptor binding; virus neutralization","Armstrong, S.J., McInerney, T.L., McLain, L., Wahren, B., Hinkula, J., Levi, M., Dimmock, N.J., Two neutralizing anti-V3 monoclonal antibodies act by affecting different functions of human immuno-deficiency virus type 1 (1996) Journal of General Virology, 77, pp. 2931-2941; Boireau, P., Cruciere, C., Laporte, J., Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) Journal of General Virology, 71, pp. 487-492; Bos, E.C.W., Heijnen, L., Luytjes, W., Spaan, W.J.M., Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion (1995) Virology, 214, pp. 453-463; Bosch, M.L., Earl, P.L., Fargnoli, F., Picciafuoco, S., Giombini, S., Wong-Staal, F., Franchini, G., Identification of the fusion peptide of primate immunodeficiency viruses (1989) Science, 244, pp. 694-697; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion (1982) Virology, 119, pp. 358-371; Daniel, C., Anderson, R., Buchmeier, M.J., Fleming, J.O., Spaan, W.J.M., Wege, H., Talbot, P.J., Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of a complex tridimensional structure (1993) Journal of Virology, 67, pp. 1185-1194; De Groot, R.J., Luytjes, W., Horzinek, M.C., Van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike of coronaviruses (1987) Journal of Molecular Biology, 196, pp. 963-966; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G., Holmes, K.V., Diffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) Journal of Virology, 65, pp. 6881-6891; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesis T7 RNA polymerase (1986) Proceedings of the National Academy of Sciences, USA, 83, pp. 8122-8126; Gallagher, T.M., Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein (1996) Journal of Virology, 70, pp. 4683-4690; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) Journal of Virology, 65, pp. 1916-1928; Gething, J.-J., Doms, R.W., York, D., White, J.M., Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the haemagglutinin of influenza virus (1986) Journal of Cell Biology, 107, pp. 2059-2073; Hernandez, L.D., White, J.M., Mutational analysis of the candidate internal fusion peptide of the avian leukosis and sarcoma virus subgroup A envelope glycoprotein (1998) Journal of Virology, 72, pp. 3259-3263; Koolen, J.J.M., Borst, M.A., Horzinek, J.M.C., Spaan, W.J.M., Immunogenic peptide comprising a mouse hepatitis virus A59 B-cell epitope and an influenza virus T-cell epitope protects against lethal infection (1990) Journal of Virology, 64, pp. 6270-6273; Kubo, H., Takase-Yoden, S., Taguchi, F., Neutralization and fusion inhibition activities of monoclonal antibodies specific for the S1 subunit of the spike protein of neurovirulent murine coronavirus JHMV cl-2 variant (1993) Journal of General Virology, 74, pp. 1421-1425; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) Journal of Virology, 68, pp. 5403-5410; Kunita, S., Zhang, L., Homberger, F.R., Compton, S.R., Molecular characterization of the S proteins of two enterotropic murine coronavirus strains (1995) Virus Research, 35, pp. 277-289; Luo, Z., Weiss, S.R., Roles in cell-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein (1998) Virology, 244, pp. 483-494; Luytjes, W.D., Sturman, L.S., Bredenbeek, P.J., Charite, J., Van der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Luytjes, W., Geerts, D., Posthumus, W., Meleon, R., Spaan, W.J.M., Amino acid sequence of a conserved neutralizing epitope of murine coronavirus (1989) Journal of Virology, 63, pp. 1408-1412; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus OC43 (1993) Journal of General Virology, 74, pp. 1981-1987; Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) Journal of Virology, 68, pp. 5411-5422; Ohtsuka, N., Yamada, Y.K., Taguchi, F., Difference in virus-binding activity of two distinct receptor proteins for mouse hepatitis virus (1996) Journal of General Virology, 77, pp. 1683-1692; Outlaw, M.C., Dimmock, N.J., IgG-neutralization of type A influenza viruses and the inhibition of the endosomal fusion stage of the infectious pathway in BHK cells (1993) Virology, 195, pp. 413-421; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Parker, M.D., Yoo, D., Cox, G.J., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) Journal of General Virology, 71, pp. 263-270; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) Journal of Virology, 71, pp. 9024-9031; Schmidt, I., Skinner, M., Siddell, S., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHVJHM (1987) Journal of General Virology, 68, pp. 47-56; Skinner, M.A., Langlois, A.J., McDanal, C.B., McDougal, J.S., Bolognesi, D.P., Matthews, T.J., Neutralizing antibodies to an immunodominant envelope sequence do not prevent gp 120 binding to CD4 (1988) Journal of Virology, 62, pp. 4195-4200; Sturman, L.S., Ricard, C.A., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) Journal of Virology, 56, pp. 904-911; Suzuki, H., Taguchi, F., Analysis of the receptor-binding site of murine coronavirus spike glycoprotein (1996) Journal of Virology, 70, pp. 2632-2636; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) Journal of Virology, 67, pp. 1195-1202; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor-binding (1995) Journal of Virology, 69, pp. 7260-7263; Taguchi, F., Siddell, S.G., Wege, H., ter Meulen, V., Characterization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) Journal of Virology, 54, pp. 429-435; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) Journal of General Virology, 73, pp. 1065-1072; Talbot, P.J., Buchmeier, M.J., Antigenic variation among murine coronavirus: Evidence for polymorphism on the peplomer glycoprotein, E2 (1985) Virus Research, 2, pp. 317-328; White, J.M., Viral and cellular membrane fusion proteins (1990) Annual Review in Physiology, 52, pp. 675-697; Yamada, Y.K., Yabe, M., Sequence analysis of major structural proteins of newly isolated mouse hepatitis virus (2000) Experimental Animals, 49, pp. 61-66; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; email: taguchi@ncnp.go.jp",,"Society for General Microbiology",00221317,,JGVIA,"11086117","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034528210
"Davis E., Rush B.R., Cox J., DeBey B., Kapil S.","24779379900;7103151000;7404022549;7004363982;7003293348;","Neonatal enterocolitis associated with coronavirus infection in a foal: A case report",2000,"Journal of Veterinary Diagnostic Investigation","12","2",,"153","156",,34,"10.1177/104063870001200210","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034153593&doi=10.1177%2f104063870001200210&partnerID=40&md5=9e6d4fb815c27f35ce83e257adf41a5a","Department of Clinical Sciences, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Davis, E., Department of Clinical Sciences, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Rush, B.R., Department of Clinical Sciences, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Cox, J., Department of Clinical Sciences, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; DeBey, B., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States",[No abstract available],,"virus antigen; animal; animal disease; article; case report; Coronavirus; diarrhea; enterocolitis; enzyme linked immunosorbent assay; feces; female; horse; horse disease; immunohistochemistry; immunology; newborn; pathology; virology; virus infection; Animals; Animals, Newborn; Antigens, Viral; Coronavirus; Coronavirus Infections; Diarrhea; Enterocolitis; Enzyme-Linked Immunosorbent Assay; Feces; Female; Horse Diseases; Horses; Immunohistochemistry","Bass, E.R., Sharpee, R.L., Coronavirus and gastroenteritis in foals (1973) Lancet, 2, p. 822; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Daginakatte, G.C., Chard-Bergstrom, C., Andrews, G.A., Kapil, S., Production, characterization, and application of monoclonal antibodies against nucleoprotein of elk coronaviruses (1999) Clin Diagn Lab Immunol, 6, pp. 341-344; Doughri, A.M., Storz, J., Light and ultrastructural pathologic changes in intestinal coronavirus infection of newborn calves (1977) Zentralbl Veterinaermed, 29, pp. 367-385; Flewett, T.H., Electron microscopy in the diagnosis of infectious diarrhea (1978) J Am Vet Med Assoc, 173, pp. 538-541; Huang, J.C., Wright, S.L., Shipley, W.D., Isolation of coronavirus-like agent from horses suffering from acute equine diarrhoea syndrome (1983) Vet Rec, 113, pp. 262-263; Kapil, S., Richardson, K.L., Radi, C., Chard-Bergstrom, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J Vet Diagn Invest, 8, pp. 96-99; Kapil, S., Trent, A.M., Goyal, S.M., Antibody responses in spiral colon, ileum, and jejunum of bovine coronavirus-infected neonatal calves (1994) Comp Immunol Microbiol Infect, 17, pp. 139-149; Kraaijeveld, C.A., Reed, S.A., Macnaughton, M.R., Enzyme-linked immunosorbent assay for detection of antibody in volunteers experimentally infected with human coronavirus strain 229E (1980) J Clin Microbiol, 12, pp. 493-497; Majhdi, F., Minocha, H.C., Kapil, S., Isolation and characterization of a coronavirus from elk calves with diarrhea (1997) J Clin Microbiol, 35, pp. 2937-2942; McIntosh, K., (1996) Coronaviridae and Their Replication, 3rd Ed., pp. 1095-1102. , B. N. Fields, ed. Lippincott-Raven, Philadelphia, PA; Sackett, D.L., Haynes, B.R., Guyatt, G.H., Tugwell, P., (1991) Clinical Epidemiology, 2nd Ed., , Little Brown and Co., Boston, MA/Toronto, Canada/London, England; Saif, L.J., Heckert, R.A., (1990) Enteropathogenic Coronaviruses, , CRC Press Inc., Boca Raton FL; Schoenthaler, S.L., Kapil, S., Development and applications of a bovine coronavirus antigen detection enzyme-linked immunosorbent assay (1999) Clin Diagn Lab Immunol, 6, pp. 130-132; Slocombe, R.F., Slauson, D.O., Invasive pulmonary aspergillosis of horses: An association with acute enteritis (1988) Vet Pathol, 25, pp. 277-281; Smith, D.R., Fedorka-Cray, P.J., Brock, M.R., Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 994-1001; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Sperlich, A., Kervin, R., Benfield, D.A., Rowland, R.R.R., Nucleolar localization of PRRS virus nucleocapsid protein (1998) Proc 79th Annu Conf Res Work Anim Dis, , Chicago, IL; Sweeney, C.R., Habecker, P.L., Pulmonary aspergillosis in horses: 29 Cases (1974-1997) (1999) J Am Vet Med Assoc, 214, pp. 808-811; Thompson, R.G., (1988) Special Veterinary Pathology, 1st Ed., , BC Decker, Toronto, Canada/Philadelphia, PA; Torres-Medina, A., Schlafer, D.H., Mebus, C.A., (1985) Rota and Coronaviral Diarrhea, 1. , WB Saunders, Philadelphia, PA; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalin-fixed intestines (1997) J Clin Microbiol, 35, pp. 2964-2965","Davis, E.; Department of Clinical Sciences, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"10730946","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0034153593
"Addie D.D.","7003910352;","Clustering of feline coronaviruses in multicat households.",2000,"Veterinary journal (London, England : 1997)","159","1",,"8","9",,20,"10.1053/tvjl.1999.0429","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033631731&doi=10.1053%2ftvjl.1999.0429&partnerID=40&md5=42e36625e66a02f0c9216d6bb1c0c286",,"Addie, D.D.",[No abstract available],,"animal; animal disease; cat; cat disease; immunology; mortality; note; virology; virus infection; Animals; Cat Diseases; Cats; Coronavirus Infections; Feline Infectious Peritonitis",,"Addie, D.D.",,,10900233,,,"10640407","English","Vet. J.",Editorial,"Final",Open Access,Scopus,2-s2.0-0033631731
"Zenner L., Regnault J.-P.","57200423759;57088482000;","Ten-year long monitoring of laboratory mouse and rat colonies in French facilities: A retrospective study",2000,"Laboratory Animals","34","1",,"76","83",,36,"10.1258/002367700780577957","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033958433&doi=10.1258%2f002367700780577957&partnerID=40&md5=df3d2b7563576f0119f333c969926ea4","CDTA, Unité CNRS UPS44, 3B rue de la Férollerie, 45071 Orléans Cedex 2, France; Unité de Recherche INRA 958, Service de Parasitolagie, Ecl. Natl. Veterinarie de Lyon, 1 Avenue Bourgelat, 69280 Marcy l'Etoile, France","Zenner, L., CDTA, Unité CNRS UPS44, 3B rue de la Férollerie, 45071 Orléans Cedex 2, France, Unité de Recherche INRA 958, Service de Parasitolagie, Ecl. Natl. Veterinarie de Lyon, 1 Avenue Bourgelat, 69280 Marcy l'Etoile, France; Regnault, J.-P., CDTA, Unité CNRS UPS44, 3B rue de la Férollerie, 45071 Orléans Cedex 2, France","From 1988 to 1997, a total of 69 mouse colonies and 36 rat colonies were examined for the presence of antibodies to 14 indigenous viruses of mice and rats. Among mouse viruses,high positivity rates were observed with mouse hepatitis virus (MHV). Theiler's encephalomyelitis virus (THEMV), minute virus of mice (MVM), Sendai virus and pneumonia virus of mice (PVM); the prevalence rates were high in rats with Khilam's rat virus (KRV), THEMV, Toolan's H-1 virus, Sendai virus, Parker's rat coronavirus (RCV/SDA) and PVM. During the last decade, the prevalence of some agents such as MHV, Sendai virus, THEMV, PVM and MVM has apparently decreased although they were still present in 1997 (except for PVM). Another point is the constant increase of colonies found free of viruses through this decade, demonstrating the efforts of the French research community to increase the quality of hygiene in laboratory animals.","Epidemiology; Mice; Rats; Virus","antibody; article; Coronavirus; experimental animal; France; hygiene; monitoring; mouse; Murine encephalomyelitis virus; Murine hepatitis coronavirus; nonhuman; Parvovirus; pneumonia; prevalence; rat; retrospective study; Sendai virus; virus infection","Bhatt, P.N., Jacoby, R.O., Morse, H.C., New, A.E., (1986) Viral and Mycoplasma Infections of Laboratory Rodents. Effects on Biomedical Research, , London: Academic Press; Calisher, C.H., Rowe, W.P., Mouse hepatitis, reo-3, and the Theiler viruses (1966) National Cancer Institute Monography, 20, pp. 67-75; Carthew, P., Verstraete, A., A serological survey of accredited breeding colonies in the United Kingdom for common rodent viruses (1978) Laboratory Animals, 12, pp. 29-32; Casebolt, D.B., Lindsey, J.R., Cassel, G.H., Prevalence rates of infectious agents among commercial breeding populations of rats and mice (1988) Laboratory Animal Science, 38, pp. 327-329; Descoteaux, J.P., Grignon-Archambault, D., Lussier, L., Serologic study of the prevalence of murine viruses in five Canadian mouse colonies (1977) Laboratory Animal Science, 27, pp. 621-626; Downs, W.G., Mouse encephalomyelitis virus (1982) The Laboratory Mouse Vol. II: Diseases, 2, pp. 341-352. , (Foster HL, Small JD, Fox JG, eds). New York: Academic Press; Foster, H.L., Small, J.D., Fox, J.G., (1982) The Mouse in Biomedical Research, Vol. II, Diseases, 2. , New York: Academic Press; Fujiwara, K., Takenaka, S., Shumiya, S., Carrier state of antibody and viruses in a mouse breeding colony persistently infected with Sendai and mouse hepatitis viruses (1976) Laboratory Animal Science, 26, pp. 153-159; Fujiwara, K., Tanishima, Y., Tanaka, M., Seromonitoring of laboratory mouse and rat colonies for common murine pathogens (1979) Experimental Animals, 28, pp. 297-306; Gannon, J., Carthew, P., Prevalence of indigenous viruses in laboratory animal colonies in the United Kingdom 1978-1979 (1980) Laboratory Animals, 14, pp. 309-311; Kraft, V., Deeny, A.A., Blanchet, H.M., Recommendations for the health monitoring of mouse, rat, hamster, guineapig and rabbit breeding colonies (1994) Laboratory Animals, 28, pp. 1-12; Kraft, V., Meyer, B., Diagnosis of murine infections in relation to test methods employed (1986) Laboratory Animal Science, 36, pp. 271-276; Kraft, V., Meyer, B., Seromonitoring in small laboratory animal colonies. A five year survey: 1984-1988 (1990) Zeitschrift für Versuchstierkunde, 33, pp. 29-35; Lindsey, J.R., Casebolt, D.B., Cassell, G.H., (1986) Animal Health in Toxicological Research: An Appraisal of Past Performance and Future Prospects, , Princeton: Princeton Scientific; Lussier, G., Descoteaux, J.P., Prevalence of natural virus infections in laboratory mice and rats used in Canada (1986) Laboratory Animal Science, 36, pp. 145-148; Nakagawa, M., Saito, M., Suzuki, E., Nakayama, K., Matsubara, J., Muto, T., Ten-year long survey on pathogen status of mouse and rat breeding colonies (1984) Experimental Animals, 33, pp. 115-120; (1991) Infectious Diseases of Mice and Rats, , Washington DC: National Academic Press; Nicklas, W., Hornberger, F.R., Illgen-Wilcke, B., Implications of infectious agents on results of animal experiment (1999) Laboratory Animals, 33 (1 SUPPL.), pp. 39-87; Pakes, S.P., Lu, Y.S., Meunier, P.C., Factors that complicate animal research (1984) Laboratory Animal Medicine, pp. 649-665. , (Fox JG, Cohen BJ, Loen FM, eds). New York: Academic Press; Parker, J.C., The possibilities and limitations of virus control in laboratory animals (1980) Animal Quality and Models in Research, pp. 161-172. , (Spiegel A, Erichsen S, Solleveld HA, eds). New York: Gustave Fischer Verlag; Parker, J.C., Tennant, R.W., Ward, T.G., Prevalence of viruses in mouse colonies (1966) National Cancer Institute Monography, 20, pp. 25-36; Poiley, J.C., A survey of indigenous murine viruses in a variety of production and research animal facilities (1970) Laboratory Animal Care, 20, pp. 643-650; Rehbinder, C., Baneux, P., Forbes, D., Van Herck, H., Nicklas, W., Rugaya, Z., Winkler, G., FELASA recommendations for the health monitoring of mouse, rat, hamster, gerbil, guineapig and rabbit experimental units (1996) Laboratory Animals, 30, pp. 193-208; Rowe, W.P., Hartley, J.W., Huebner, R.J., Polyoma and other mouse viruses (1963) Laboratory Animal Care, 13, pp. 166-174; Smith, A.L., Serologic tests for detection of antibody to rodent viruses (1986) Viral and Mycoplasmal Infections of Laboratory Rodents: Effects on Biomedical Research, pp. 731-751. , (Bhatt PN, Jacoby RO, Morse III HC, News AE, eds). Orlando: Academic Press; Tennant, R.W., Parker, J.C., Ward, T.G., Respiratory virus infections of mice (1966) National Cancer Institute Monography, 20, pp. 93-104; Van Der Logt, J.T.M., Serological study on the prevalence of murine viruses in laboratory animal colonies in France and in the Netherlands (1981-1984) (1986) Sciences et Techniques de l'Animal de Laboratoire, 11, pp. 197-203","Zenner, L.; Service de Parasitologie, Departement de Sante Publique, Ecole Nationale Veterinaire de Lyon, 1 Avenue Bourgelat, 69280 Marcy l'Etoile, France",,"Royal Society of Medicine Press Ltd",00236772,,LBANA,"10759370","English","Lab. Anim.",Article,"Final",,Scopus,2-s2.0-0033958433
"Masuda T., Rehinarudo H.Y., Suzuki K., Sakai T., Morichi T.","36896500000;6507187253;16048561600;7404832007;6603595157;","The Effect of High Hydrostatic Pressure Treatment on the Preservability and the Immunological Activity of Bovine Colostrum",2000,"Asian-Australasian Journal of Animal Sciences","13","9",,"1323","1328",,4,"10.5713/ajas.2000.1323","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034376839&doi=10.5713%2fajas.2000.1323&partnerID=40&md5=71842e050f002b3ee3a82c867edd9e52","College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan","Masuda, T., College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan; Rehinarudo, H.Y., College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan; Suzuki, K., College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan; Sakai, T., College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan; Morichi, T., College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan","Bovine colostrum, which contains a large quantity of immunoglobulins, is indispensable for newborn animals. The establishment of a new procedure for preserving colostrum without losing the immunological activity is significant. We examined the effect of high hydrostatic pressure treatment (100∼500 MPa) on the preservability and the immunochemical activity of bovine colostrum. When high hydrostatic pressure treatment was 300 MPa or more, the increase of the total viable count, coliforms and psychrotrophic gram-negative bacteria was suppressed effectively. In particular, the number of coliforms in colostrum treated at 300 MPa or more hardly increased for 35 days at 4°C. At 400 MPa or more, both gelling of the colostrum and denaturation of immunoglobulins were observed. However, if the pressure was 300 MPa, immunoglobulins were scarcely influenced and the neutralizing titers against the bovine coronavirus did not decrease. Therefore, it was suggested that 300 MPa was the best pressure for good preservability of colostrum without reducing the immunochemical response.","Bovine Colostrum; High Hydrostatic Pressure; Preservability",,"De Wit, J.N., Klarenbeek, G., Effects of various heat treatments on structure and solubility of whey proteins (1984) J. Dairy Sci., 67, pp. 2701-2710; Hashiguchi, Y., Hatta, T., Studies on effective feeding of colostrum 1. Changes in maternal antibody titers in serum of precololostral calves after feeding of colostrum changes in antibody titers in colostrum supplemented with organic acid in several keeping conditions (1981) J. Jpn. Vet. Med. Assoc., 34, pp. 166-171. , In Japanese with abstract in English; Hayashi, R., Introduction of high pressure to food processing: Referential proteolysis of beta-lactoglobulin in whey (1987) J. Food Sci., 52, pp. 1107-1108; Kadharmestan, C., Baik, B.K., Czuchajowska, Z., Thermal behaviour of whey protein concentrate treated by heat and high hydrostatic pressure and its functionality in wheat dough (1998) Cereal Chem., 75, pp. 785-791; Lambeir, A.M., Heremans, K., Dunford, H.B., High-pressure effect on the equilibrium and kinetics of cyanide binding tochloroperoxidase (1983) Biophys. Chem., 18, pp. 195-201. , Netherlands; Lambin, P., Rochu, D., Fine, M., A new method for determination of molecular weights of proteins by electrophoresis across sodium dodecylsulfate (SDS) polyacrylamide gel (1976) Anal Biochem., 74, pp. 567-575; Mills, G., Earnshaw, R., Patterson, M.F., Effects of high hydrostatic pressure on Clostridium sporogenes spores (1998) Letters in Appl. Microbiol, 26, pp. 227-230; Porter, P., Noakes, D.E., Allen, W.D., Secretory IgA and antibodies to Eschericia coli in porcine colostrum and milk and their significance in the alimentary tract of the young pig (1970) Immunology, 18, pp. 245-247; Raabe, E., Knorr, D., Kinetics of starch hydrolysis with Bacillus amyloliquefaciens α-amylase under high hydrostatic pressure (1996) Starch, 48, pp. 409-414; Raso, J., Barbosa-Canovas, G., Swanson, B.G., Sporulation temperature affects initiation of germination and inactivation by high hydrostatic pressure of Bacillus cereus (1998) J. Appl. Microbiol., 85, pp. 17-24; Roberts, C.M., Hoover, D.G., Sensitivity of Bacillus coagulans spores to combinations of high hydrostatic pressure, heat acidity and risin (1996) J. Appl. Bacteriol., 81, pp. 363-368; Rowland, S.J., The determination of the nitrogen distribution in milk (1938) J. Dairy Res., 9, pp. 42-46; Sakai, T., The characteristic of immunity in newborn calf and the role of colostrum (2) (1994) Kachikushinryo, 372, pp. 35-43. , In Japanese with abstract in English; Takahashi, A., Abe, T., Morichi, T., Maeda, S., Himeno, K., Nakano, S., Studies on replacement on colostrum for piglets. 1. Method for preservation of bovine colostrum, its effect upon newborn piglets, and development of artificial nurses for piglets (1979) Jpn. J. Swine Res., 16, pp. 173-184. , In Japanese with abstract in English; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc, Nati. Acad. Sci., 76, pp. 4350-4354. , USA","Masuda, T.; College of Bioresource Sciences, Nihon University, Fujisawa-shi, Kanagawa 252-8510, Japan; email: Tmasuda@brs.nihon-u.ac.jp",,"Asian-Australasian Association of Animal Production Societies",10112367,,,,"English","Asian-Australas. J. Anim. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0034376839
"Molenkamp R., van Tol H., Rozier B.C.D., van der Meer Y., Spaan W.J.M., Snijder E.J.","6603227562;57213957599;7801352332;7005678965;7007172944;7006058325;","The arterivirus replicase is the only viral protein required for genome replication and subgenomic mRNA transcription",2000,"Journal of General Virology","81","10",,"2491","2496",,82,"10.1099/0022-1317-81-10-2491","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033799819&doi=10.1099%2f0022-1317-81-10-2491&partnerID=40&md5=fc4d28e271a3dcb8918f7b6f8dfb5c20","Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands","Molenkamp, R., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; van Tol, H., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; Rozier, B.C.D., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; van der Meer, Y., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; Snijder, E.J., Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands","Equine arteritis virus (EAV) (Arteriviridae) encodes several structural proteins. Whether any of these also function in viral RNA synthesis is unknown. For the related mouse hepatitis coronavirus (MHV), it has been suggested that the nucleocapsid protein (N) is involved in viral RNA synthesis. As described for MHV, we established that the EAV N protein colocalizes with the viral replication complex, suggesting a role in RNA synthesis. Using an infectious cDNA clone, point mutations and deletions were engineered in the EAV genome to disrupt the expression of each of the structural genes. All structural proteins, including N, were found to be dispensable for genome replication and subgenomic mRNA transcription. We also constructed a mutant in which translation of the intraleader ORF was disrupted. This mutant had a wild-type pheno-type, indicating that, at least in cell culture, the product of this ORF does not play a role in the EAV replication cycle.",,"complementary DNA; gene product; guanine nucleotide binding protein; messenger RNA; RNA directed RNA polymerase; structural protein; virus protein; virus RNA; animal cell; Arterivirus; article; controlled study; Equine viral arteritis virus; gene construct; gene deletion; gene disruption; gene expression; gene function; gene replication; genetic engineering; molecular cloning; mutant; nonhuman; open reading frame; phenotype; point mutation; priority journal; RNA transcription; RNA translation; structural gene; virus genome; virus replication; Animalia; Arterivirus; Coronavirus; Equidae; Equine arteritis virus; Mouse hepatitis coronavirus; Murine hepatitis virus; RNA viruses","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceedings of the National Academy of Sciences, USA, 97, pp. 5516-5521; Balasuriya, U.B., Patton, J.F., Rossitto, P.V., Timoney, P.J., McCollum, W.H., MacLachlan, N.J., Neutralization determinants of laboratory strains and field isolates of equine arteritis virus: Identification of four neutralization sites in the amino-terminal ectodomain of the G(L) envelope glycoprotein (1997) Virology, 232, pp. 114-128; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) Journal of Virology, 62, pp. 4280-4287; Buck, K.W., Comparison of the replication of positive-stranded RNA viruses of plants and animals (1996) Advances in Virus Research, 47, pp. 159-251; Compton, S.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., In vitro replication of mouse hepatitis virus strain A59 (1987) Journal of Virology, 61, pp. 1814-1820; den Boon, J.A., Snijder, E.J., Chirnside, E.D., de Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) Journal of Virology, 65, pp. 2910-2920; de Vries, A.A.F., Chirnside, E.D., Horzinek, M.C., Rottier, P.J.M., Structural proteins of equine arteritis virus (1992) Journal of Virology, 66, pp. 6294-6303; de Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., de Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiology Reviews, 57, pp. 781-822; Glaser, A.L., (1995), Equine arteritis virus: Identification of virus-associated proteins and investigation of antigenic and sequence diversity in the major virion glycoprotein. PhD thesis, Cornell University, USA; Gorbalenya, A.E., Snijder, E.J., Viral cysteine proteases (1996) Perspectives in Drug Discovery and Design, 6, pp. 64-86; Kheyar, A., St Laurent, G., Archambault, D., Sequence determination of the extreme 5' end of equine arteritis virus leader region (1996) Virus Genes, 12, pp. 291-295; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Lamb, R.A., Kolakofski, D., Paramyxoviridae: The viruses and their replication (1996), pp. 577-604. , In Fundamental Virology, Edited by B. N. Fields, D. M. Knipe and P. M. Howley. New York: Raven Press; Lamb, R.A., Krug, R.M., Orthomyxoviridae: The viruses and their replication (1996), pp. 605-648. , In Fundamental Virology, Edited by B. N. Fields, D. M. Knipe and P. M. Howley. New York: Raven Press; Li, H.P., Zhang, X., Duncan, R., Comai, L., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA (1997) Proceedings of the National Academy of Sciences, USA, 94, pp. 9544-9549; MacLachlan, N.J., Balasuriya, U.B., Hedges, J.F., Schweidler, T.M., McCollum, W.H., Timoney, P.J., Hullinger, P.J., Patton, J.F., Serologic response of horses to the structural proteins of equine arteritis virus (1998) Journal of Veterinary Diagnostic Investigation, 10, pp. 229-236; Molenkamp, R., Rozier, B.C.D., Greve, S., Spaan, W.J.M., Snijder, E.J., Isolation and characterization of an arterivirus defective interfering RNA genome (2000) Journal of Virology, 74, pp. 3156-3165; Nelson, G.W., Stohlman, S.A., Tahara, S.M., High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA (2000) Journal of General Virology, 81, pp. 181-188; Niesters, H.G., Strauss, J.H., Defined mutations in the 5' nontranslated sequence of Sindbis virus RNA (1990) Journal of Virology, 64, pp. 4162-4168; Pedersen, K.W., van der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) Journal of Virology, 73, pp. 2016-2026; Quadt, R., Rosdorff, H.J., Hunt, T.W., Jaspars, E.M., Analysis of the protein composition of alfalfa mosaic virus RNA-dependent RNA polymerase (1991) Virology, 182, pp. 309-315; Rowland, R.R., Kervin, R., Kuckleburg, C., Sperlich, A., Benfield, D.A., The localization of porcine reproductive and respiratory syndrome virus nucleocapsid protein to the nucleolus of infected cells and identification of a potential nucleolar localization signal sequence (1999) Virus Research, 64, pp. 1-12; Snijder, E.J., Meulenberg, J.J.M., The molecular biology of arteriviruses (1998) Journal of General Virology, 79, pp. 961-979; Snijder, E.J., van Tol, H., Pedersen, K.W., Raamsman, M.J.B., de Vries, A.A.F., Identification of a novel structural protein of arteriviruses (1999) Journal of Virology, 73, pp. 6335-6345; Stohlman, S.A., Baric, R.S., Nelson, G.W., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) Journal of Virology, 62, pp. 4288-4295; van der Kuyl, A.C., Neeleman, L., Bol, J.F., Deletion analysis of cis- and trans-acting elements involved in replication of alfalfa mosaic virus RNA 3 in vivo (1991) Virology, 183, pp. 687-694; van der Meer, Y., van Tol, H., Krijnse Locker, J., Snijder, E.J., ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex (1998) Journal of Virology, 72, pp. 6689-6698; van der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Krijnse Locker, J., The localization of mouse hepatitis virus nonstructural proteins suggests a role for late endosomes in viral replication (1999) Journal of Virology, 73, pp. 7641-7657; van Dinten, L.C., Wassenaar, A.L.M., Gorbalenya, A.E., Spaan, W.J.M., Snijder, E.J., Proceeding of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains (1996) Journal of Virology, 70, pp. 6625-6633; van Dinten, L.C., den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation which abolishes discontinuous mRNA transcription (1997) Proceedings of the National Academy of Sciences, USA, 94, pp. 991-996; van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base-pairing between sense and antisense transcription-regulating sequences (1999) Proceedings of the National Academy of Sciences, USA, 96, pp. 12056-12061; Wagner, R.R., Rose, J.K., Rhabdoviridae: The viruses and their replication (1996), pp. 561-576. , In Fundamental Virology, Edited by B. N. Fields, D. M. Knipe and P. M. Howley. New York: Raven Press; Wang, Y., Zhang, X., The nucleocapsid protein of coronavirus mouse hepatitis virus interacts with the cellular heterogeneous nuclear ribonucleoprotein A1 in vitro and in vivo (1999) Virology, 265, pp. 96-109; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) Journal of General Virology, 81, pp. 853-879","Snijder, E.J.; Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, Netherlands; email: E.J.Snijder@LUMC.NL",,"Society for General Microbiology",00221317,,JGVIA,"10993938","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033799819
"Enjuanes L., Sola I., Izeta A., Sánchez-Morgado J.M., González J.M., Alonso S., Escors D., Sánchez C.M.","7006565392;7003336781;6602523425;6602349176;57201828108;57210695335;6507259181;57193985365;","Interference with virus and bacteria replication by the tissue specific expression of antibodies and interfering molecules",2000,"Advances in Experimental Medicine and Biology","473",,,"31","45",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034463396&partnerID=40&md5=fb124cdab3c1ef182895b06a11b05b84","Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Enjuanes, L., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sánchez-Morgado, J.M., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; González, J.M., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Alonso, S., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Escors, D., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain; Sánchez, C.M., Department of Molecular and Cell Biology, CSIC, CSIC, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain","Historically, protection against virus infections has relied on the use of vaccines, but the induction of an immune response requires several days and in certain situations, like in newborn animals that may be infected at birth and die in a few days, there is not sufficient time to elicit a protective immune response. Immediate protection in new born could be provided either by vectors that express virus-interfering molecules in a tissue specific form, or by the production of animals expressing resistance to virus replication. The mucosal surface is the largest body surface susceptible to virus infection that can serve for virus entry. Then, it is of high interest to develop strategies to prevent infections of these areas. Virus growth can be interfered intracellularly, extracellularly or both. The antibodies neutralize virus intra- and extracellularly and their molecular biology is well known. In addition, antibodies efficiently neutralize viruses in the mucosal areas. The autonomy of antibody molecules in virus neutralization makes them functional in cells different from those that produce the antibodies and in the extracellular medium. These properties have identified antibodies as very useful molecules to be expressed by vectors or in transgenic animals to provide resistance to virus infection. A similar role could be played by antimicrobial peptides in the case of bacteria. Intracellular interference with virus growth (intracellular immunity) can be mediated by molecules of very different nature: (i) full length or single chain antibodies; (ii) mutant viral proteins that strongly interfere with the replication of the wild type virus (dominant-negative mutants); (iii) antisense RNA and ribozyme sequences; and (iv) the product of antiviral genes such as the Mx proteins. All these molecules inhibiting virus replication may be used to obtain transgenic animals with resistance to viral infection built in their genomes. We have developed two strategies to target into mucosal areas either antibodies to provide immediate protection, or antigens to elicit immune responses in the enteric or respiratory surfaces in order to prevent virus infection. One strategy is based on the development of expression vectors using coronavirus derived defective RNA minigenomes, and the other relies on the development of transgenic animals providing virus neutralizing antibodies in the milk during lactation. Two types of expression vectors are being engineered based on transmissible gastroenteritis coronavirus (TGEV) defective minigenomes. The first one is a helper virus dependent expression system and the second is based on self-replicating RNAs including the information required to encode the TGEV replicase. The minigenomes expressing the heterologous gene have been improved by using a two-step amplification system based on cytomegalovirus (CMV) and viral promoters. Expression levels around 5 μg per 106 cells were obtained. The engineered minigenomes will be useful to understand the mechanism of coronavirus replication and for the tissue specific expression of antigen, antibody or virus interfering molecules. To protect from viral infections of the enteric tract, transgenic animals secreting virus neutralizing recombinant antibodies in the milk during lactation have been developed. Neutralizing antibodies with isotypes IgG1 or IgA were produced in the milk with titers of 106 in RIA that reduced virus infectivity by one million-fold. The recombinant antibodies recognized a conserved epitope apparently essential for virus replication. Antibody expression levels were transgene copy number independent and were related to the transgene integration site. This strategy may be of general use since it could be applied to protect newborn animals against infections of the enteric tract by viruses or bacteria for which a protective MAb has been identified. Alternatively, the same strategy could be used to target the expression of antibiotic peptides to the enteric tract in order to protect against bacterial or virus infections. © Springer Science+Business Media New York 1999.",,"epitope; mutant protein; neutralizing antibody; peptide derivative; recombinant antibody; RNA directed RNA polymerase; virus antibody; virus protein; antibody production; bacterial growth; cellular immunity; conference paper; immune response; infection prevention; infection resistance; infection sensitivity; nonhuman; priority journal; promoter region; tissue specificity; virus infection; virus inhibition; virus replication; virus resistance; Animals; Antibodies, Bacterial; Antibodies, Viral; Bacteria; Humans; Immunity, Mucosal; Intestinal Mucosa; Virus Replication; Animalia; Bacteria (microorganisms); Coronavirus; Cytomegalovirus; Transmissible gastroenteritis virus","Ahmad, I., Perkins, W.R., Lupan, D.M., Selsted, M.E., Janoff, A.S., Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo anti-fungal activity (1995) Biochi. Biophy. Acta., 1237, pp. 109-114; Antón, I.M., Suñé, C., Meloen, R.H., Borrás-Cuesta, F., Enjuanes, L., A transmissible gastroenteritis coronavirus nucleoprotein epitope elicits T helper cells that collaborate in the in vitro antibody synthesis to the three major structural viral proteins (1995) Virology, 212, pp. 746-751; Baghian, A., Jaynes, J., Enright, F., Kousolas, K.G., An amphipathic alpha-helical synthetic peptide analogue of melittin inhibits herpes simplex virus-I (HSV-1)-induced cell fusion and virus spread (1997) Peptides, 18, pp. 177-183; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Bazzo, R., Tappin, M.J., Pastore, A., Harvey, T.S., Carver, J.A., Campbell, I.D., The structure of melittin. A 1H-NMR study in methanol (1988) Eur. J. 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"Gutzwiller A.","6701628224;","Glucose and Galactose Absorption after Ingestion of Milk Containing Hydrolysed Lactose in Calves with Diarrhoea",2000,"Journal of Veterinary Medicine Series A: Physiology Pathology Clinical Medicine","47","8",,"495","500",,2,"10.1046/j.1439-0442.2000.00310.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034297940&doi=10.1046%2fj.1439-0442.2000.00310.x&partnerID=40&md5=c541dda644812044cc46d19602820450","Swiss Fed. Res. Stn. Anim. Prod., 1725 Posieux, Switzerland","Gutzwiller, A., Swiss Fed. Res. Stn. Anim. Prod., 1725 Posieux, Switzerland","Ten calves which had contracted acute diarrhoea caused by rotavirus, coronavirus and Cryptosporidium were used to test the hypothesis that feeding lactose-hydrolysed cow's milk instead of unprocessed cow's milk improves sugar absorption in diarrhoeic calves. The animals were rehydrated with an orally administered solution containing electrolytes and glucose. Thereafter the calves received one test meal of whole fresh cow's milk whose lactose had been hydrolvsed by added lactase and one test meal of unprocessed cow's milk at an interval of 24 h in a cross-over design trial. In comparison with unprocessed milk, the intake of milk containing hydrolysed lactose resulted in a slight decrease of mean breath hydrogen concentration (P=0.18), but also a slight decrease of mean blood galactose concentration (P=0.14). There was no treatment effect on mean plasma glucose concentration. Peak plasma glucose and blood galactose concentration tended to be delayed after the intake of lactose-hydrolysed milk, which implies that gastric emptying was probably delayed. The results show that feeding milk which contains hydrolysed lactose does not significantly improve lactose utilization in calves that are suffering from benign infectious diarrhoea.",,"Animalia; Coronavirus; Cryptosporidium; Rotavirus; beta galactosidase; galactose; glucose; hydrogen; lactase; oral rehydration solution; animal; animal disease; area under the curve; article; blood; cattle; cattle disease; diarrhea; enzymology; female; glucose blood level; male; milk; physiology; Animals; Area Under Curve; beta-Galactosidase; Blood Glucose; Cattle; Cattle Diseases; Diarrhea; Female; Galactose; Glucose; Hydrogen; Lactase; Male; Milk; Rehydration Solutions","Bell, F., Mostaghini, K., Duodenal control of gastric emptying in the milk-fed calf (1975) J. Physiol., 245, pp. 387-407; Bird, P.C., Atwood, Hartmann, P., The response of blood galactose to oral doses of lactose, galactose plus glucose and milk to piglets (1995) Br. J. 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Clin. North Am. Food Anim. Pract., 1, pp. 471-493; Tzipori, S., Smith, M., Halpin, C., Angus, K., Sherwood, D., Campbell, I., Experimental cryptosporidiosis in calves: Clinical manifestations and pathological findings (1983) Vet. Rec., 112, pp. 116-120; Vesa, T., Marteau, P., Briet, F., Boutron-Ruault, M., Rambaud, J., Raising milk energy content retards gastric emptying of lactose in lactose-intolerant humans with little effect on lactose digestion (1997) J. Nutr., 127, pp. 2316-2320","Gutzwiller, A.; Swiss Fed. Res. Stn. Anim. Prod., 1725 Posieux, Switzerland; email: Andreas.Gutzwiller@rap.admin.ch",,"Blackwell Verlag GmbH Berlin",0931184X,,JVMAE,"11075541","English","J. Vet. Med. Ser. A Physiol. Pathol. Clin. Med.",Article,"Final",,Scopus,2-s2.0-0034297940
"Greenberg S.B., Allen M., Wilson J., Atmar R.L.","7402294401;57214159303;56164780300;7005296248;","Respiratory viral infections in adults with and without chronic obstructive pulmonary disease",2000,"American Journal of Respiratory and Critical Care Medicine","162","1",,"167","173",,186,"10.1164/ajrccm.162.1.9911019","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033909359&doi=10.1164%2fajrccm.162.1.9911019&partnerID=40&md5=3ca4598a50a9d9fcaa8f479a49a590ea","Depts. of Med. and Microbiol. and I., Baylor College of Medicine, Houston, TX, United States; Department of Medicine, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Greenberg, S.B., Depts. of Med. and Microbiol. and I., Baylor College of Medicine, Houston, TX, United States, Department of Medicine, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; Allen, M., Depts. of Med. and Microbiol. and I., Baylor College of Medicine, Houston, TX, United States; Wilson, J., Depts. of Med. and Microbiol. and I., Baylor College of Medicine, Houston, TX, United States; Atmar, R.L., Depts. of Med. and Microbiol. and I., Baylor College of Medicine, Houston, TX, United States","A longitudinal cohort study of older adults with chronic obstructive pulmonary disease (COPD) who were stratified by FEV1 at enrollment was done to define the etiology, frequency, severity, and medical-care impact of respiratory tract viral infections (RTVIs). Controls consisted of a group of subjects of comparable age with the patients. RTVIs were documented in 44% of observed acute respiratory illnesses in control subjects and in 27% of COPD subjects, who were followed for mean periods of 35 and 26 mo, respectively. In this heavily influenza-vaccinated cohort (~ 90% vaccinated each year), picornaviruses, parainfluenza viruses, and coronaviruses were most commonly identified. Mean time to return to clinical baseline was approximately 2 wk in each group. Control and COPD subjects with mild airways obstruction (baseline FEV1 ≥ 50% predicted) had few emergency-center visits or hospitalizations. Approximately half of COPD subjects with moderate/severe COPD (baseline FEV1 &lt; 50% predicted) had at least one emergency-center visit and/or hospitalization for acute respiratory illness. RTVIs were documented in 23% of hospitalizations and in 45% of patients admitted between December and March. RTVIs have a major impact on utilization of health care resources for COPD patients with moderate/severe airways obstruction.",,"adult; aged; airway obstruction; article; chronic obstructive lung disease; cigarette smoking; cohort analysis; female; forced expiratory volume; hospitalization; host resistance; human; immune response; major clinical study; male; priority journal; respiratory tract infection; vaccination; virus culture; virus infection","Kramarow, E., Lentzner, H., Rooks, R., Weeks, J., Saydah, S., (1999) Health and Aging Chartbook. Health, United States, 1999, , National Center for Health Statistics, Hyattsville, MD; Mannino, D.M., Brown, C., Giovino, G.A., Obstructive lung disease deaths in the United States from 1979 through 1993: An analysis using multiple-cause mortality data (1997) Am. J. Respir. Crit. 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Virol, 7, pp. 77-84; Frank, A.L., Puck, J., Hughes, B.J., Cate, T.R., Microneutralization test for influenza A and B and parainfluenza 1 and 2 viruses that uses continuous cell lines and fresh serum enhancement (1980) J. Clin. Microbiol., 12, pp. 426-432; Piedra, P.A., Wyde, P.R., Castleman, W.L., Ambrose, M.W., Jewell, A.M., Speelman, D.J., Hildreth, S.W., Enhanced pulmonary pathology associated with the use of formalin-inactivated respiratory syncytial virus vaccine in cotton rats is not a unique viral phenomenon (1993) Vaccine, 11, pp. 1415-1423; Drews, A.L., Atmar, R.L., Glezen, W.P., Baxter, B.D., Piedra, P.A., Greenberg, S.B., Dual respiratory virus infections (1997) Clin. Infect. Dis., 25, pp. 1421-1429; Gill, E.P., Dominguez, E.A., Greenberg, S.B., Atmar, R.L., Hogue, B.G., Baxter, B.D., Couch, R.B., Development and application of an enzyme immunoassay for coronavirus OC43 antibody in acute respiratory illness (1994) J. Clin. Microbiol., 32, pp. 2372-2376; Nicholson, K.G., Kent, J., Hammersley, V., Cancio, E., Acute viral infections of upper respiratory tract in elderly people living in the community: Comparative, prospective, population based study of disease burden (1997) B.M.J., 315, pp. 1060-1064; Walsh, E.E., Falsey, A.R., Hennessey, P.A., Respiratory syncytial and other virus infections in persons with chronic cardiopulmonary disease (1999) Am. J Respir. Crit. Care Med., 160, pp. 791-795; Kraft, M., Cassell, G.H., Henson, J.E., Watson, H., Williamson, J., Marmion, B.P., Gaydos, C.A., Martin, R.J., Detection of Mycoplasma pneumoniae in the airways of adults with chronic asthma (1998) Am. J. Respir. Crit. Care Med., 158, pp. 998-1001; Von Hertzen, L., Alakarppa, H., Koskinen, R., Liippo, K., Surcel, H.M., Leinonen, M., Saikku, P., Chlamydia pneumoniae infection in patients with chronic obstructive pulmonary disease (1997) Epidemiol. Infect., 118, pp. 155-164; Murphy, T.F., Sethi, S., Bacterial infection in chronic obstructive pulmonary disease (1992) Am. Rev. Respir. Dis., 146, pp. 1067-1083; Atmar, R.L., Guy, E., Guntupalli, K.K., Zimmerman, J.L., Bandi, V.D., Baxter, B.D., Greenberg, S.B., Respiratory tract viral infections in inner-city asthmatic adults (1998) Arch. Intern. Med., 158, pp. 2453-2459; Nichol, K.L., Baken, L., Nelson, A., Relation between influenza vaccination and outpatient visits, hospitalization, and mortality in elderly persons with chronic lung disease (1999) Ann. Intern. Med., 130, pp. 397-403; Kessler, R., Faller, M., Fourgaut, G., Mennecier, B., Weitzenblum, E., Predictive factors of hospitalization for acute exacerbation in a series of 64 patients with chronic obstructive pulmonary disease (1999) Am. J. Respir. Crit. Care Med., 159, pp. 158-164; Grasso, M.E., Weller, W.E., Shaffer, T.J., Diette, G.B., Anderson, G.F., Capitation, managed care, and chronic obstructive pulmonary disease (1998) Am. J. Respir. Crit. Care Med., 158, pp. 133-138","Greenberg, S.B.; Department of Medicine, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States; email: stepheng@bcm.tmc.edu",,"American Lung Association",1073449X,,AJCME,"10903237","English","Am. J. Respir. Crit. Care Med.",Article,"Final",,Scopus,2-s2.0-0033909359
"Knotek Z., Toman M., Faldyna M.","56012890700;24073936200;6603774648;","Clinical and immunological characteristics of cats affected by feline infectious peritonitis",2000,"Acta Veterinaria Brno","69","1",,"51","60",,4,"10.2754/avb200069010051","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142172080&doi=10.2754%2favb200069010051&partnerID=40&md5=1976dfd421be28007c4e466eaa97bc76","Univ. Vet. and Pharmaceutical Sci., Brno, Czech Republic; Veterinary Research Institute, Brno, Czech Republic; Small Animal Clinic, Univ. Vet. and Pharmaceutical Sci., Palackého 1-3, 612 42 Brno, Czech Republic","Knotek, Z., Univ. Vet. and Pharmaceutical Sci., Brno, Czech Republic, Small Animal Clinic, Univ. Vet. and Pharmaceutical Sci., Palackého 1-3, 612 42 Brno, Czech Republic; Toman, M., Veterinary Research Institute, Brno, Czech Republic; Faldyna, M., Veterinary Research Institute, Brno, Czech Republic","A set of 180 hospitalized or outdoor feline patients was examined for the presence of antibodies to feline coronavirus (FeCoV) and clinical signs of feline infectious peritonitis (FIP). The numbers of serologically and clinically positive cats were 55 (30.6%) and 35, respectively. The effusive and noneffusive forms of FIP were diagnosed in 24 and 11 animals, respectively. The most apparent signs, irrespective of the form of infection, included anorexia, lethargy, ischemic mucosae, and undernutrition. Hematological and immunological profiles of 14 FIP patients were compared with those found in a control group of 36 clinically normal and FeCoV-negative animals. A significant increase in the number of neutrophilic granulocytes was observed in the FIP patients (FIV-/FeLV-cats with effusive form) and a significant decrease in the number of lymphocytes were observed in the FIP patients. Eosinopenia was also found in patients affected by the effusive form. No alteration of the phagocytic activity (ingestion of particles, chemiluminiscence) due to FIP was demonstrable. The blastic transformation test (stimulation with Con A, PHA, or PWM) showed a marked decrease in the activity of lymphocytes in the FIP patients. Concentrations of immunoglobulins and circulating immune complexes were increased in the affected animals. The expression of the lymphocyte surface antigens CD4, CD5, CD8, and CD21 was studied in a selected subgroup of the patients using flow cytometry. The results indicate an impairment of the activity of the immune system due to FIP. Therefore, treatment of FIP with immunosuppressive drugs is considered inappropriate.","Blastic transformation of lymphocytes; Coronavirus infection; Feline CD antigens; Immune complexes","Animalia; Coronavirus; Felidae; Feline coronavirus; Felis catus","Ackley, C.D., Yamamoto, J.K., Levy, N., Pedersen, N.C., Cooper, M.D., Immunologic abnormalities in pathogen-free cats experimentally infected with feline immunodeficiency virus (1990) J. Virol., 64, pp. 5652-5655; Bech-Nielsen, S., Fulton, R.W., Downing, M.M., Hardy Jr., W.D., Feline Infectious Peritonotis and Viral Respiratory Diseases in Feline Leukemia. Virus Infected Cats (1981) J. Amer. Anim. Hosp. Assoc., 17, pp. 759-765; Evermann, J.F., Henry, C.J., Marks, S.L., Feline infectious peritonitis (1995) J. Amer. Vet. Med. Assoc., 206, pp. 1130-1134; Evermann, J.F., McKiernan, A.J., Ott, R.L., Perspectives on the epizootiology of feline enteric coronavirus and the pathogenesis of feline infectious peritonitis (1991) Vet. Microbiol., 28, pp. 243-255; Faldyna, M., Toman, M., The effect of age on the distribution of lymphocyte and neutrophil granulocyte subsets in the peripheral blood of dog (1998) Vet. Med. - Czech, 43, pp. 193-199; Goitsuka, R., Onda, C., Hirota, Y., Hasegawa, A., Tomoda, I., Feline interleukin 1 production induced by feline infectious peritonitis (1988) Jpn. J. Vet. Sci., 50, pp. 209-214; Goitsuka, R., Hirota, Y., Hasegawa, A., Tomoda, I., Release of interleukin 1 from peritoneal exudate cells of cats with feline infectious peritonitis (1987) Jpn. J. Vet. Sci., 49, pp. 811-818; Goitsuka, R., Ohashi, T., Ono, K., Hirota, Y., Hasegawa, K., Koishibara, Y., Fukui, H., Hasegawa, A., Interleukin 6 activity in feline infectious peritonitis (1990) J. Immunol., 14, pp. 2599-2603; Gunn-Moore, D.A., Caney, S.M.A., Gruffyd-Jones, T.J., Helps, C.R., Harbour, D.A., Antibody and cytokine responses in kittens during the development of feline infectious peritonitis (FIP) (1998) Vet. Immunol. Immunopathol., 65, pp. 221-242; Hájková, V., Pru̇kaz cirkulujících imunokomplexu̇ (1986) Vybrané Diagnostické Metody Lékařské Imunologie, pp. 114-119. , Procházková, J. - John, C. (eds): Praha, Avicenum, in Czech; Hoskins, J.D., Taylor, H.W., Lomax, T.L., Challenge trial of an intranasal feline infectious peritonitis vaccine (1994) Feline Pract., 22, pp. 9-13; Kipar, A., Bellmann, S., Kremendahl, J., Kohler, K., Reinacher, M., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Vet. Immunol. Immunopathol., 65, pp. 243-257; Knotek, Z., Svoboda, M., Jelínek, F., Hájková, P., Felinni infekční peritonitida (1995) Proc. Annu. Confer. CSAVA, pp. 44-46. , Brno in Czech; Knotek, Z., Gojda, M., Svoboda, M., Diagnostika retrovirových infekcí koček v klinické praxi (1997) Veterinářství, 47, pp. 20-22. , in Czech; Knotek, Z., Hájková, P., Svoboda, M., Toman, M., Raška, V., Epidemiology of feline leukaemia and feline immunodeficiency virus infections in the Czech Republic (1999) J. Vet. Med. B, 46, pp. 665-671; Loeffler, D.G., Ott, R.L., Evermann, J.F., Alexander, J.E., The incidence of naturally occurring antibodies against feline infectious peritonitis in selected cat populations (1978) Feline Pract., 8, pp. 43-47; Mathes, L.E., Olsen, R.G., Helebrand, L.C., Abrogation of lymphocyte blastogenesis by feline leukaemia virus protein (1978) Nature, 274, pp. 687-689; McEwan, A.D., Fisher, E.W., Selman, I.E., Penhale, W.J., A turbidity test for estimation of immune globulin levels in neonatal calf serum (1970) Clin. Chim. Acta, 27, pp. 155-163; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-36; Paltrinieri, S., Cammarata Parodi, M., Cammarata, G., Comazzi, S., Some aspects of humoral and cellular immunity in naturally occurring feline infectious peritonitis (1998) Vet. Immunol. Immunopathol., 65, pp. 205-220; Paltrinieri, S., Cammarata Parodi, M., Cammarata, G., Mambretti, M., Type IV hypersensitivity in the pathogenesis of FIPV induced lesions (1998) J. Vet. Med. B, 45, pp. 151-159; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections (1983) Feline Practice, 13, pp. 5-20; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-22; Pedersen, N.C., Virologie an immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Reinacher, M., Diseases associated with spontaneous feline leukemia virus (FeLV) infection in cats (1989) Vet. Immunol. Immunopathol., 21, pp. 85-89; Rohrer, C., Suter, P.F., Lutz, H., Die Diagnostik der felinen infektiosen Peritonitis (FIP): Retrospektive und prospektive Untersuchungen (1993) Kleintierpraxis, 38, pp. 379-389; Rottman, J.B., Tompkins, W.A.F., Tompkins, M.B., A reverse transcription - Quantitative competitive polymerase chain reaction (RT - qcPCR) technique to measure cytokine gene expression in domestic animals (1996) Vet. Pathol., 33, pp. 242-248; Schultz, R.D., Adams, L.S., Immunologic methods for the detection of humoral and cellular immunity (1978) Vet. Clin. North Am., 8, pp. 721-768; Větvička, V., Fornusek, L., Kopeček, J., Phagocytosis of human blood leukocytes: A simple micro-method (1982) Immunol. Lett., 5, pp. 97-100; Weiss, R.C., Dodds, W.J., Scott, F.W., Disseminated intravascular coagulation in experimentally induced feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 663-671; Weiss, R.C., Feline infectious peritonitis and other coronaviruses (1994) The Cat: Diseases and Clinical Management, 2. Ed., pp. 449-477. , Sherding, R. G. (ed): Churchill Livingstone Inc; Wolfe, L.G., Griesemer, R.A., Feline infectious peritonitis (1966) Path. Vet., 3, pp. 255-270","Knotek, Z.; Small Animal Clinic, Univ. Vet. and Pharmaceutical Sci., Palackého 1-3, 612 42 Brno, Czech Republic; email: knotekz@vfu.cz",,"University of Veterinary and Pharmaceutical Sciences",00017213,,,,"English","Acta Vet. Brno",Article,"Final",Open Access,Scopus,2-s2.0-0142172080
"Van Reeth K., Nauwynck H.","57191565576;7007141390;","Proinflammatory cytokines and viral respiratory disease in pigs",2000,"Veterinary Research","31","2",,"187","213",,120,"10.1051/vetres:2000113","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034153670&doi=10.1051%2fvetres%3a2000113&partnerID=40&md5=ec650873220ef3bc466422be6e4133fc","Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium","Van Reeth, K., Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium; Nauwynck, H., Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium","Swine influenza virus (SIV), porcine respiratory coronavirus (PRCV) and porcine reproductive and respiratory syndrome virus (PRRSV) are enzootic viruses causing pulmonary infections in pigs. The first part of this review concentrates on known clinical and pathogenetic features of these infections. SIV is a primary respiratory pathogen; PRCV and PRRSV, on the contrary, tend to cause subclinical infections if uncomplicated but they appear to be important contributors to multifactorial respiratory diseases. The exact mechanisms whereby these viruses cause symptoms and pathology, however, remain unresolved. Classical studies of pathogenesis have revealed different lung cell tropisms and replication kinetics for each of these viruses and they suggest the involvement of different lung inflammatory responses or mediators. The preinflammatory cytokines interferon-α (IFN-α), tumour necrosis factor-α (TNF-α) and interleukin-1 (IL-l) have been shown to play key roles in several respiratory disease conditions. The biological effects of these cytokines and their involvement in human viral respiratory disease are discussed in the second part of this review. The third part summarises studies that were recently undertaken in the authors' laboratory to investigate the relationship between respiratory disease in pigs and bioactive lung lavage levels of IFN-α, TNF-α and IL-1 during single and combined infections with the above viruses. In single SIV infections, typical signs of swine ""flu"" were tightly correlated with an excessive and coordinate production of the 3 cytokines examined. PRCV or PRRSV infections, in contrast, were subclinical and did not induce production of all 3 cytokines. Combined infections with these 2 subclinical respiratory viruses failed to potentiate disease or cytokine production. After combined inoculation with PRCV followed by bacterial lipopolysaccharide, both clinical respiratory disease and TNF-α/IL-1 production were markedly more severe than those associated with the respective single inoculations. Taken together, these data are the first to demonstrate that proinflammatory cytokines can be important mediators of viral respiratory diseases in pigs.","Cytokines; Pathogenesis; Porcine reproductive and respiratory syndrome virus (PRRSV); Porcine respiratory coronavirus (PRCV); Swine influenza virus (SIV)","Bacteria (microorganisms); Coronavirus; Influenza virus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Simian immunodeficiency virus; Suidae; Sus scrofa; Swine influenza virus; cytokine; animal; animal disease; Arterivirus; human; influenza; Influenza virus A; pathophysiology; physiology; respiratory tract infection; review; swine; swine disease; virology; virus infection; Animals; Coronavirus Infections; Cytokines; Humans; Influenza A virus; Influenza, Human; Porcine respiratory and reproductive syndrome virus; Respiratory Tract Infections; Swine; Swine Diseases","Adler, K.B., Fischer, B.M., Wright, D.T., Cohn, L.A., Becker, S., Interactions between respiratory epithelial cells and cytokines: Relationships to lung inflammation (1994) Ann. 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Porcine Fr., 27, pp. 107-116; Albina, E., Porcine reproductive and respiratory syndrome: Ten years of experience (1986-1996) with this undesirable viral infection (1997) Vet. Res., 28, pp. 305-352; Albina, E., Piriou, L., Hutet, E., Cariolet, R., L'Hospitalier, R., Immune responses in pigs infected with porcine reproductive and respiratory syndrome virus (PRRSV) (1998) Vet. Immunol. Immunopathol., 61, pp. 49-66; Arnold, R., Humbert, B., Werchan, H., Gallati, H., Konig, W., Interleukin-8, interleukin-6 and soluble tumour necrosis factor receptor type 1 release from a human pulmonary epithelial cell line (A 549) exposed to respiratory syncytial virus (1994) Immunology, 82, pp. 126-133; Artursson, K., Wallgren, P., Alm, G.V., Appearance of interferon-α in serum and signs of reduced immune function in pigs after transport and installation in a fattening farm (1989) Vet. Immunol. Immunopathol., 23, pp. 345-353; Asai, T., Okada, M., Ono, M., Irisawa, T., Mori, Y., Yokomizo, Y., Sato, S., Increased levels of tumor necrosis factor and interleukin 1 in bronchoalveolar lavage fluids from pigs infected with Mycoplasma hyopneumoniae (1993) Vet. Immunol. Immunopathol., 38, pp. 253-260; Asai, T., Okada, M., Ono, M., Mori, Y., Yokimizo, Y., Sato, S., Detection of interleukin-6 and prostaglandin E2 in bronchoalveolar lavage fluids of pigs experimentally infected with Mycoplasma hyopneumoniue (1994) Vet. Immunol. Immunopathol., 44, pp. 97-102; Baarsch, M.J., Scamurra, R.W., Burger, K., Foss, D.L., Maheswaran, S.K., Murtaugh, M.P., Inflammatory cytokine expression in swine experimentally infected with Actinobacillus pleuropneumoniae (1995) Infect. Immun., 63, pp. 3587-3594; Baron, T., Albina, E., Leforban, Y., Madec, F., Guilmoto, H., Plana Duran, J., Vannier, P., Report on the first outbreaks of the porcine reproductive and respiratory syndrome (PRRS) in France. 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Cancer, 49, pp. 274-278; Bielefeldt-Ohmann, H., Campos, M., Snider, M., Rapin, N., Beskorwayne, T., Popowyck, Y., Lawman, M.J.P., Babiuk, L.A., Effect of chronic administration of recombinant bovine tumor necrosis factor to cattle (1989) Vet. Pathol., 26, pp. 462-472; Bilodeau, R., Archamhault, D., Vezina, S.A., Fournier, M., Dea, S., Persistence of porcine reproductive and respiratory syndrome virus injection in a swine operation (1994) Can. J. Vet. Res., 58, pp. 291-298; Biswas, S., Friedland, J.S., Remick, D.G., Davies, E.G., Sharland, M., Elevated plasma interleukin-8 in respiratory syncytial virus bronchiolitis (1995) Pediatr. Infect. Dis. J., 14, p. 919; Bittleman, D.B., Casale, B.C., Interleukin-8 mediates interleukin-1alpha-induced neutrophil transcellular migration (1995) Am. J. Respir. Cell. Mol. Biol., pp. 323-329; Blecha, F., Reddy, D.N., Chitko-McKown, C.G., McVey, D.S., Chengappa, M.M., Goodband, R.D., Nellsen, J.L., Influence of recombinant bovine interleukin-1 α and interleukin-2 in pigs vaccinated and challenged with Streptococcus suis (1995) Vet. Immunol. Immunopathol., 44, pp. 329-346; Bourgueil, E., Hutet, E., Cariolet, R., Vannier, P., Experimental infection of pigs with the porcine respiratory coronavirus (PRCV): Measure of viral excretion (1992) Vet. Microbiol., 31, p. 1118; Breider, M.A., Kumar, S., Corstvet, R.E., Bovine pulmonary endothelial cell damage mediated by Pasteurella haemolytica pathogenic factors (1990) Infect. Immun., 58, p. 1671; Brown, I.H., Done, S.H., Spencer, Y.I., Cooley, W.A., Harris, P.A., Alexander, D.J., Pathogenicity of a swine influenza HINI virus antigenically distinguishable from classical and European strains (1993) Vet. 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Dis., 177, pp. 1076-1079; Van Reeth, K., Labarque, G., Nauwynck, H., Pensaert, M., Differential production of proinflammatory cytokines in the pig lung during different respiratory virus infections: Correlations with pathogenicity (1999) Res. Vet. Sci, 67, pp. 47-52; Van Reeth, K., Nauwynck, H., Pensaert, M., Porcine respiratory coronavirus synergizes with bacterial lipopolysaccharide in the induction of respiratory disease in pigs: A potential role for tumour necrosis factor-α J. Med. Microbiol., , in press; Vogelzang, P.F.J., Van der Gulden, J.W.J., Folgering, H., Kolk, J.J., Heederik, D., Preller, L., Tielen, M.J.M., Van Schayk, C.P., Endotoxin exposure as a major determinant of lung function decline in pig farmers (1998) Am. J. Respir. Crit. Care Med., 157, pp. 15-18; Wang, Z., Larsson, K., Palmherg, L., Malmberg, P., Larsson, P., Larsson, L., Inhalation of swine dust induces cytokine release in the upper and lower airways (1997) Eur. Respir. J., 10, pp. 381-387; Warren, E.J., Finck, B.N., Scamurra, R.W., Murtaugh, M.P., Johnson, R.W., Behavioral and physiological responses induced by peripheral immune stimulation are mimicked in pigs by central injection of porcine tumor necrosis factorα (1995) J. Anim. Sci., 73 (SUPPL. 1), p. 92; Wesley, R.D., Woods, R.D., Hill, K.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Wesley, R.D., Woods, R.D., Mc Kean, J.D., Senn, M.K., Elazhary, Y., Prevalence of coronavirus antibodies in Iowa swine (1997) Can. J. Vet. Res., 61, pp. 305-308; Wong, G.H.W., Goedel, D.V., Tumor necrosis factors-α and β inhibit virus replication and synergize with interferons (1986) Nature, 323, pp. 819-822; Yoon, I.J., Joo, H.S., Christianson, W.T., Morrison, R.B., Dial, G.D., Persistent and contact infection in nursery pigs experimentally infected with porcine reproductive and respiratory syndrome (PRRS) virus (1993) Swine Health and Production, 1, pp. 5-8; Zeman, D., Neiger, K., Jaeger, M., Nelson, E., Benfield, D., Leslie-Steen, P., Thomson, J., Minehart, M., Laboratory investigation of prrs virus infection in three swine herds (1993) J. Vet. Diagn. Invest., 5, pp. 522-528; Zoja, C., Wang, J.M., Bettoni, S., Sironi, M., Renzi, D., Chiaffarino, F., Abboud, H.E., Remuzzi, G., Interleukin-lβ and tumor necrosis factor-α induce gene expression and production of leucocyte chemotactic factors, colony-stimulating factors, and interleukin-6 in human mesangial cells (1991) Am. J. Pathol., 138, pp. 991-1003; Zhu, Z., Tang, W., Ray, A., Wu, Y., Einarsson, O., Landry, M.L., Gwaltney, J., Elias, J.A., Rhinovirus stimulation of interleukin-6 in vivo and in vitro. Evidence for nuclear factor κ B-dependent transcriptional activation (1996) J. Clin. Invest., 97, pp. 421-430","Van Reeth, K.; Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium; email: kristien.vanreeth@rug.ac.be",,"EDP Sciences",09284249,,VEREE,"10779199","English","Vet. Res.",Article,"Final",Open Access,Scopus,2-s2.0-0034153670
"Qureshi M.A., Yu M., Saif Y.M.","7202876162;55475801200;35563198200;","A novel 'small round virus' inducing poult enteritis and mortality syndrome and associated immune alterations",2000,"Avian Diseases","44","2",,"275","283",,39,"10.2307/1592540","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034047455&doi=10.2307%2f1592540&partnerID=40&md5=555bd789d0778ccde46d64dbb9920f24","Department of Poultry Science, North Carolina State University, Raleigh, NC 27695-7608, United States; OARDC/FAHRP, Ohio State University, Wooster, OH 44691, United States","Qureshi, M.A., Department of Poultry Science, North Carolina State University, Raleigh, NC 27695-7608, United States; Yu, M., OARDC/FAHRP, Ohio State University, Wooster, OH 44691, United States; Saif, Y.M., OARDC/FAHRP, Ohio State University, Wooster, OH 44691, United States","The role of a novel 'small round virus' (SRV) isolated from poult enteritis and mortality syndrome (PEMS) cases in inducing PEMS and associated immune alterations was examined in this study. Specific-pathogen-free and conventional poults were orally challenged with SRV and/or turkey coronavirus and monitored for clinical signs. Intestines, thymus, bursa, and spleens were examined for SRV antigen at various days postinoculation (DPI). Peripheral blood lymphocytes (PBLs), thymocytes, and splenic lymphocytes from inoculated poults or lymphocytes isolated from healthy poults after incubation with SRV in vitro were examined for lymphoproliferative potential against concanavalin A (Con A). The incidence of lymphocyte subpopulations in the peripheral blood and thymic lymphocytes of SRV-challenged poults was examined by flow cytometry. The results of these studies showed that the SRV challenge induced diarrhea, growth suppression, and atrophy of thymus and bursa resembling those of PEMS in field and/or experimental infections. The SRV antigen was detected in intestinal tissues soon after infection (i.e., at 2 and 4 DPI), whereas lymphoid tissues such as thymus, bursa, and spleen were positive for SRV antigen starting at 4 DPI until 8 DPI, suggesting virus translocation to lymphoid organs. The responsiveness of PBLs to Con A at 2 DPI was significantly reduced in all virus challenge groups (e.g., 28% and 22% in the SRV-alone group in studies 1 and 2, respectively) below the uninfected group. However, this suppressed response was no longer evident in the SRV group by 7 DPI. The SRV incubation with normal thymocytes and splenocytes in vitro resulted in significantly reduced lymphoproliferative response against Con A (41.2% and 10.49% reductions at 1: 50 SRV dilution vs. controls in thymocytes and splenocytes, respectively). Flow cytometry analysis revealed a sudden decline at 2 DPI in the numbers of CD4-CD8+ lymphocyte subset in PBLs of SRV-infected poults. However, by 8 DPI, SRV-challenged poults had relatively higher CD4-CD8+ lymphocytes in PBLs. On the contrary, thymocytes had higher percentages of CD4-CD8+ lymphocytes at 2 and 4 DPI and reached comparable levels at 8 DPI in controls and SRV-infected poults. No differences were observed in CD4+CD8- lymphocyte numbers in controls vs. SRV-infected poults. The findings of these studies imply that SRV may be a promising primary etiologic agent of PEMS. Furthermore, the SRV infection may compromise the lymphocyte-mediated immune defenses by reducing lymphoproliferation and the CD4-CD8+ (presumably T-cytotoxic cells) lymphocytes during the acute stage of SRV infection.","Antigen trafficking; Lymphocyte subpopulations; Lymphoproliferation; Poult enteritis and mortality syndrome; Small round virus","Animalia; Aves; Coronavirus; Meleagris gallopavo; Norwalk virus; Turkey coronavirus","Barnes, H.J., Guy, J.S., Poult enteritis -mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry, 10th Ed., pp. 1025-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Barnes, H.J., Guy, J.S., Spiking mortality of turkeys (SMT) and related disorders: An update (1995) Proc. 19th Annual North Carolina Turkey Industry Days Conference, pp. 16-21. , North Carolina State University, Raleigh, NC; Brown, T.P., Howell, D.R., Garcia, A.P., Villegas, P., Histological lesions of spiking mortality of turkeys (SMT): Comparison of lesions induced by SMT organ suspension and cell culture (1996) J. Am. Vet. Med. Assoc., 209, p. 373; Confer, A.W., MacWilliams, P.S., Correlation of hematological changes and serum and monocyte inhibition with the early suppression of phytohemagglutinin stimulation of lymphocytes in experimental infectious bursal disease (1982) Can. J. Comp. Med., 46, pp. 169-175; Edens, F.W., Parkhurst, C.R., Qureshi, M.A., Casas, I.A., Havenstein, G.B., Atypical Escherichia coli strains and their association with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 952-960; Edens, F.W., Qureshi, R.A., Parkhurst, C.R., Qureshi, M.A., Havenstein, G.B., Casas, I.A., Characterization of two Escherichia coli strains associated with poult enteritis and mortality syndrome (PEMS) (1997) Poult. Sci., 76, pp. 1665-1673; Guy, J.S., Virus infections of the gastrointestinal tract of poultry (1998) Poult. Sci., 77, pp. 1166-1175; Heggen, C.L., Qureshi, M.A., Edens, F.W., Barnes, H.J., Alterations in macrophage-produced cytokines and nitrite associated with poult enteritis and mortality syndrome (2000) Avian Dis., 44, pp. 59-65; Heggen, C.L., Qureshi, M.A., Edens, F.W., Barnes, H.J., Havenstein, G.B., Alterations in the lymphocytic and mononuclear phagocytic systems of turkey poults associated with exposure to poult enteritis and mortality syndrome (1998) Avian Dis., 42, pp. 711-720; Qureshi, M.A., Edens, F.W., Havenstein, G.B., Immune system dysfunction during exposure to poult enteritis and mortality syndrome agents (1997) Poult. Sci., 76, pp. 564-569; Sartor, R.B., Cytokines in intestinal inflammation: Pathophysiological and clinical considerations (1994) Gastroenterology, 106, pp. 533-539; Yu, M., Dearth, R.N., Qureshi, M.A., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome (1998) Proc. 79th Annual Conference of Research Workers in Animal Diseases Meeting, p. 42. , Chicago, Ill; Yu, M., Ismail, M.M., Qureshi, M.A., Dearth, R.N., Barnes, H.J., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome: The role of a small round virus and a turkey coronavirus (2000) Avian Dis., 44, pp. 297-304","Qureshi, M.A.; Department of Poultry Science, North Carolina State University, Raleigh, NC 27695-7608, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"10879906","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0034047455
"Marczinke B., Hagervall T., Brierley I.","6602862835;6603606235;7004639098;","The Q-base of Asparaginyl-tRNA is dispensable for efficient - 1 ribosomal frameshifting in eukaryotes",2000,"Journal of Molecular Biology","295","2",,"179","191",,15,"10.1006/jmbi.1999.3361","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034645792&doi=10.1006%2fjmbi.1999.3361&partnerID=40&md5=be1bb71304d24a0189d054ff67cbff46","Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Department of Microbiology, University of Umeå, S-90187 Umeå, Sweden","Marczinke, B., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; Hagervall, T., Department of Microbiology, University of Umeå, S-90187 Umeå, Sweden; Brierley, I., Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom","The frameshift signal of the avian coronavirus infectious bronchitis virus (IBV) contains two cis-acting signals essential for efficient frameshifting, a heptameric slippery sequence (UUUAAAC) and an RNA pseudoknot structure located downstream. The frameshift takes place at the slippery sequence with the two ribosome-bound tRNAs slipping back simultaneously by one nucleotide from the zero phase (U UUA AAC) to the -1 phase (UUU AAA). Asparaginyl-tRNA, which decodes the A-site codon AAC, has the modified base Q at the wobble position of the anticodon (5' QUU 3') and it has been speculated that Q may be required for frameshifting. To test this, we measured frameshifting in cos cells that had been passaged in growth medium containing calf serum or horse serum. Growth in horse serum, which contains no free queuine, eliminates Q from the cellular tRNA population upon repeated passage. Over ten cell passages, however, we found no significant difference in frameshift efficiency between the cell types, arguing against a role for Q in frameshifting. We confirmed that the cells cultured in horse serum were devoid of Q by purifying tRNAs and assessing their Q-content by tRNA transglycosylase assays and coupled HPLC-mass spectroscopy. Supplementation of the growth medium of cells grown either on horse serum or calf serum with free queuine had no effect on frameshifting either. These findings were recapitulated in an in vitro system using rabbit reticulocyte lysates that had been largely depleted of endogenous tRNAs and resupplemented with Q-free or Q-containing tRNA populations. Thus Q-base is not required for frameshifting at the IBV signal and some other explanation is required to account for the slipperiness of eukaryotic asparaginyl-tRNA.","Asparaginyl-tRNA; Q-base; Ribosomal frameshifting; RNA pseudoknot; tRNA anticodon modification","asparagine transfer RNA; glycosyltransferase; queuine; animal cell; article; cell culture; codon; controlled study; Coronavirus; culture medium; fetal calf serum; high performance liquid chromatography; mass spectrometry; nonhuman; priority journal; rabbit; reticulocyte lysate; ribosomal frameshifting; RNA sequence; RNA structure; virus infection; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Equus caballus; Eukaryota; Oryctolagus cuniculus","Agris, P.F., The importance of being modified: Roles of modified nucleosides and Mg2+ in RNA structure and function (1996) Progr. Nucl. Acid Res. Mol. Biol., 53, pp. 79-129; Agris, P.F., Guenther, R., Ingram, P.C., Basti, M.M., Stuart, J.W., Sochacka, E., Malkiewicz, A., Unconventional structure of tRNA(Lys)SUU anticodon explains tRNA's role in bacterial and mammalian ribosomal frameshifting and primer selection by HIV-1 (1997) RNA, 3, pp. 420-428; Björk, G.R., The role of modified nucleosides in tRNA interactions (1992) Transfer RNA in Protein Synthesis, pp. 23-85. , D. L. Hatfield, B. J. Lee, & R. M. Pirtle. Boca Raton: CRC Press; Björk, G.R., Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA (1995) Progr. Nucl. Acid Res. Mol. 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Biol., 227, pp. 463-479; Brierley, I., Meredith, M.R., Bloys, A.J., Hagervall, T.G., Expression of a coronavirus ribosomal frameshift signal in Escherichiacoli: Influence of tRNA anticodon modification on frameshifting (1997) J. Mol. Biol., 270, pp. 360-373; Buck, M., Connick, M., Ames, B.N., Complete analysis of tRNA-modified nucleosides by high performance liquid chromatography: The 29 modified nucleosides of Salmonella typhimurium and Escherichia coli tRNA (1983) Anal. Biochem., 129, pp. 1-13; Carlson, B.A., Kwon, S.Y., Chamorro, M., Oroszlan, S., Hatfield, D.L., Lee, B.J., Transfer RNA modification status influences retroviral ribosomal frameshifting (1999) Virology, 255, pp. 2-8; Cassan, M., Delaunay, N., Vaquero, C., Rousset, J.-P., Translational frameshifting at the gag-pol junction of human immunodeficiency virus type 1 is not increased in infected T-lymphoid cells (1994) J. 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Chromatog., 471, pp. 3-36; Grosjean, H.J., De Henau, S., Crothers, D.M., On the physical basis for ambiguity in genetic coding interactions (1978) Proc. Natl Acad. Sci. USA, 75, pp. 610-614; Grosjean, H., Sprinzl, M., Steinberg, S., Postranscriptionally modified nucleosides in transfer RNA: Their locations and frequencies (1995) Biochimie, 77, pp. 139-141; Hames, B.D., An introduction to polyacrylamide gel electrophoresis (1991) Gel Electrophoresis of Proteins - A Practical Approach, pp. 1-91. , B. D. Hames, & D. Rickwood. Oxford: IRL Press; Hatfield, D., Feng, Y.-X., Lee, B.J., Rein, A., Levin, J.G., Oroszlan, S., Chromatographic analysis of the aminoacyl-tRNAs which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1 and BLV (1989) Virology, 173, pp. 736-742; Hatfield, D., Levin, J.G., Rein, A., Oroszlan, S., Translational suppression in retroviral gene expression (1992) Advan. Virus Res., 41, pp. 193-239; Jacks, T., Varmus, H.E., Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting (1985) Science, 230, pp. 1237-1242; Jacks, T., Madhani, H.D., Masiarz, F.R., Varmus, H.E., Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region (1988) Cell, 55, pp. 447-458; Jackson, R.J., Hunt, T., Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA (1983) Methods Enzymol., 96, pp. 50-74; Kersten, H., Kersten, W., Biosynthesis and function of queuine and queuosine tRNA (1990) Chomatography and Modification of Nucleosides, pp. 69-B108. , C. W. Gehrke, & K. C. T. Kuo. New York and Tokyo, Amsterdam, Oxford: Journal of Chromatography Library, Elsevier; Langgut, W., Changes of phosphorylation of membrane-associated proteins following treatment of HeLa cells with the guanine analogue queuine (1993) BioFactors, 4, pp. 117-122; Langgut, W., Regulation of signalling by receptor tyrosine kinases in HeLa cells involves the Q-base (1995) Biochem. Biophys. Res. Commun., 207, pp. 306-311; Langgut, W., Reisser, T., Involvement of protein kinase C in the control of tRNA modification with queuine in HeLa cells (1995) Nucl. Acids Res., 23, pp. 2488-2491; Langgut, W., Reisser, T., Nishimura, S., Kersten, H., Modulation of mammalian cell proliferation by a modified tRNA base of bacterial origin (1993) FEBS Letters, 336, pp. 137-142; Limbach, P.A., Crain, P.F., Mccloskey, J.A., Summary: The modified nucleosides of RNA (1994) Nucl. 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USA, 74, pp. 5463-5467; Stahl, G., Bidou, L., Rousset, J.-P., Cassan, M., Versatile vectors to study recoding: Conservation of rules between yeast and mammalian cells (1995) Nucl. Acids Res., 23, pp. 1557-1560; Ten, D.E.B., Pleij, C.W.A., Bosch, L., RNA pseudoknots: Translational frameshifting and readthrough on viral RNAs (1990) Virus Genes, 4, pp. 121-136; Ten, D.E., Verlaan, P., Pleij, C., Analysis of the role of the pseudoknot component in the SRV-1 gag-pro ribosomal frameshift signal: Loop lengths and stability of the stem regions (1995) RNA, 1, pp. 146-154; Tsuchihashi, Z., Translational frameshifting in the Escherichia coli dnaX gene in vitro (1991) Nucl. Acids Res., 19, pp. 2457-2462; Tsuchihashi, Z., Brown, P.O., Sequence requirements for efficient translational frameshifting in the Escherichia colidnaX gene and the role of an unstable interaction between tRNALysand an AAG lysine codon (1992) Genes Dev., 6, pp. 511-519; Watanabe, K., Hayashi, N., Oyama, A., Nishikawa, K., Ueda, T., Miura, K., Unusual anticodon loop structure found in E. coli lysine tRNA (1993) Nucl. Acids Res., 22, pp. 79-87; Yokoyama, S., Miyazawa, T., Iitaka, Y., Yamaizumi, Z., Kasai, H., Nishimura, S., Three-dimensional structure of hyper-modified nucleoside Q located in the wobbling position of tRNA (1979) Nature, 282, pp. 107-109","Brierley, I.; Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom; email: ib103@mole.bio.cam.ac.uk",,"Academic Press",00222836,,JMOBA,"10623518","English","J. Mol. Biol.",Article,"Final",,Scopus,2-s2.0-0034645792
"Kuo L., Godeke G.-J., Raamsman M.J.B., Masters P.S., Rottier P.J.M.","7101601942;6603099700;6603137050;7006234572;7006145490;","Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier",2000,"Journal of Virology","74","3",,"1393","1406",,241,"10.1128/JVI.74.3.1393-1406.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033982337&doi=10.1128%2fJVI.74.3.1393-1406.2000&partnerID=40&md5=d9a84ace6fdaae00c33abd1f87e4d179","David Axelrod Institute, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Kuo, L., David Axelrod Institute, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Godeke, G.-J., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Raamsman, M.J.B., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Masters, P.S., David Axelrod Institute, Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands","Coronaviruses generally have a narrow host range, infecting one or just a few species. Using targeted RNA recombination, we constructed a mutant of the coronavirus mouse hepatitis virus (MHV) in which the ectodomain of the spike glycoprotein (S) was replaced with the highly divergent ectodomain of the S protein of feline infectious peritonitis virus. The resulting chimeric virus, designated fMHV, acquired the ability to infect feline cells and simultaneously lost the ability to infect murine cells in tissue culture. This reciprocal switch of species specificity strongly supports the notion that coronavirus host cell range is determined primarily at the level of interactions between the S protein and the virus receptor. The isolation of fMHV allowed the localization of the region responsible for S protein incorporation into virions to the carboxyterminal 64 of the 1,324 residues of this protein. This establishes a basis for further definition of elements involved in virion assembly. In addition, fMHV is potentially the ideal recipient virus for carrying out reverse genetics of MHV by targeted RNA recombination, since it presents the possibility of selecting recombinants, no matter how defective, that have regained the ability to replicate in murine cells.",,"virus glycoprotein; virus RNA; vitronectin; animal cell; article; carboxy terminal sequence; chimera; Coronavirus; genetic recombination; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; protein domain; protein interaction; protein targeting; species difference; virion; virus replication; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Base Sequence; Cats; Cell Line; Coronavirus, Feline; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Neutralization Tests; Plasmids; Receptors, Virus; Recombinant Fusion Proteins; Recombination, Genetic; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Species Specificity; Viral Envelope Proteins; Virion","Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. 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Virol., 70, pp. 8669-8674; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"10627550","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033982337
"Godeke G.-J., De Haan C.A.M., Rossen J.W.A., Vennema H., Rottier P.J.M.","6603099700;7003682643;7005977394;7003697291;7006145490;","Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein",2000,"Journal of Virology","74","3",,"1566","1571",,57,"10.1128/JVI.74.3.1566-1571.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033960161&doi=10.1128%2fJVI.74.3.1566-1571.2000&partnerID=40&md5=453402b5482d56d24b0f575c9fd30c68","Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","Godeke, G.-J., Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands; De Haan, C.A.M., Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands; Rossen, J.W.A., Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands; Vennema, H., Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. Infections Dis. and Immunol., Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","The type I glycoprotein S of coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. Here we demonstrate that incorporation is mediated by the short carboxy-terminal segment comprising the transmembrane and endodomain. To this aim, we used the virus-like particle (VLP) system that we developed earlier for the mouse hepatitis virus strain A59 (MHV-A59) and which we describe now also for the unrelated coronavirus feline infectious peritonitis virus (FIPV; strain 79-1146). Two chimeric MHV-FIPV S proteins were constructed, consisting of the ectodomain of the one virus and the transmembrane and endodomain of the other. These proteins were tested for their incorporation into VLPs of either species. They were found to assemble only into viral particles of the species from which their carboxy-terminal domain originated. Thus, the 64-terminal-residue sequence suffices to draw the 1308 (MHV)- or 1433 (FIPV)-amino-acid-long mature S protein into VLPs. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active. This was indeed confirmed by incorporating one of the proteins into virions which thereby acquired a new host cell tropism, as will be reported elsewhere.",,"glycoprotein; virus protein; article; cell fusion; Coronavirus; nonhuman; peritonitis; priority journal; protein assembly; protein folding; virus cell interaction; virus infection; virus particle; Amino Acid Sequence; Animals; Cats; Cell Fusion; Cell Line; Coronavirus; Coronavirus, Feline; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Recombinant Fusion Proteins; Viral Envelope Proteins; Virion; Virus Assembly","Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. 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Virol., 66, pp. 1579-1589; Siddell, S.G., The small-membrane protein (1995) The Coronaviridae, pp. 181-189. , S. G. Siddell (ed.). Plenum Press. New York, N.Y; Suomalainen, M., Liljeström, P., Garoff, H., Spike protein-nucleocapsid interactions drive the budding of alphaviruses (1992) J. Virol., 66, pp. 4737-4747; Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M.C., Spaan, W.J.M., Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly (1990) J. Virol., 64, pp. 339-346; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nudeocapsid-indepen-dent assembly of coronavirus-like particles by coexpression of viral envelope proteins (1996) EMBO J., 15, pp. 2020-2028; Weismiller, D.G., Sturman, L.S., Buchmeier, M.J., Fleming, J.O., Holmes, K.V., Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identity two subunits and detect a conformational change in the subunit released under mild alkaline conditions (1990) J. Virol., 64, pp. 3051-3055; Zhao, H., Lindqvist, B., Garoff, H., Von Bonsdorff, C.H., Liljeström, P., A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding (1994) EMBO J., 13, pp. 4204-4211","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands; email: P.Rottier@vet.uu.nl",,,0022538X,,JOVIA,"10627571","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033960161
"Yamada Y.K., Yabe M., Ohtsuki T., Taguchi F.","55471420900;7005872003;21737861300;7103209890;","Unique N-linked glycosylation of murine coronavirus MHV-2 membrane protein at the conserved O-linked glycosylation site",2000,"Virus Research","66","2",,"149","154",,9,"10.1016/S0168-1702(99)00134-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034052668&doi=10.1016%2fS0168-1702%2899%2900134-3&partnerID=40&md5=13b5a4bd5e7a0a8f915f35ac569e28e8","Div. of Experimental Animal Research, Natl. Inst. Infect. Dis., 4-7-1 G., Tokyo, Japan; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, K., Tokyo, Japan","Yamada, Y.K., Div. of Experimental Animal Research, Natl. Inst. Infect. Dis., 4-7-1 G., Tokyo, Japan; Yabe, M., Div. of Experimental Animal Research, Natl. Inst. Infect. Dis., 4-7-1 G., Tokyo, Japan; Ohtsuki, T., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, K., Tokyo, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, K., Tokyo, Japan","The membrane (M) proteins of murine coronavirus (MHV) strains have been reported to contain only O-linked oligosaccharides. The predicted O-glycosylation site consisting of four amino acid residues of Ser-Ser-Thr-Thr is located immediately adjacent to the initiator Met and is well conserved among MHV strains investigated so far. We analyzed the nucleotide sequence of a highly virulent strain MHV-2 M-coding region and demonstrated that MHV-2 had a unique amino acid, Asn, at position 2 at the conserved O-glycosylation site. We also demonstrated that this substitution added N-linked glycans to MHV-2 M protein resulting in increment of molecular mass of MHV-2 M protein compared with JHM strain having only O-linked glycans. Copyright (C) 2000 Elsevier Science B.V.","M protein; MHV; Murine coronavirus; N-glycosylation; O-glycosylation","amino acid; asparagine; glycan; M protein; membrane protein; nitrogen; oligosaccharide; oxygen; virus protein; article; controlled study; Coronavirus; nonhuman; nucleotide sequence; priority journal; protein glycosylation; Amino Acid Sequence; Animals; Asparagine; Base Sequence; Blotting, Western; Cloning, Molecular; DNA Primers; Genes, Viral; Glycosylation; Mice; Molecular Sequence Data; Murine hepatitis virus; Proteoglycans; Sequence Alignment; Viral Matrix Proteins; Coronavirus; Murinae; Murine hepatitis virus","Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; De Haan, C.A.M., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J.M., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; De Haan, C.A.M., Roestenberg, P., De Wit, M., De Vries, A.A.F., Nilsson, T., Vennema, H., Rottier, P.J.M., Structural requirements for O-glycosylation of the mouse hepatitis virus membrane protein (1998) J. Biol. Chem., 273, pp. 29905-29914; Hirano, N., Murakami, T., Taguchi, F., Fujiwara, K., Matumoto, M., Comparison of mouse hepatitis virus strains for pathogenicity in weanling mice infected by various routes (1981) Arch. Virol., 70, pp. 69-73; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fields Virology 3rd Ed, pp. 1075-1093. , B.N. Fields, D.M. Knipe, & P.M. Howley. Philadelphia, PA: Lippincott-Raven; Homberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res., 31, pp. 49-56; Kapke, P.A., Tung, F.Y.T., Hogue, B.G., Brian, D.A., Woods, R.D., Wesley, R., The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation (1988) Virology, 165, pp. 367-376; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M.C., RNA recombination of murine coronaviruses: Recombination between fusion-positive mouse hepatitis virus A59 and fusion-negative mouse hepatitis virus 2 (1988) J. Virol., 62, pp. 1989-1998; Kornfeld, R., Kornfeld, S., Assembly of asparagine-linked oligosaccharides (1985) Annu. Rev. Biochem., 54, pp. 631-664; Krijnse Locker, J., Griffiths, G., Horzinek, M.C., Rottier, P.J.M., O-Glycosylation of the coronavirus M protein: Differential localization of sialyltransferases in N- And O-glycosylation (1992) J. Biol. Chem., 267, pp. 14094-14101; Krijnse Locker, J., Rose, J.K., Horzinek, M.C., Rottier, P.J.M., Membrane assembly of the triple-spanning coronavirus M protein (1992) J. Biol. Chem., 267, pp. 21911-21918; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Lavi, E., Kuo, L., Haluskey, J.A., Masters, P.S., Targeted recombination between MHV-2 and MHV-A59 to study neurotropic determinants of MHV (1998) Adv. Exp. Med. Biol., 440, pp. 543-547; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) J. Gen. Virol., 73, pp. 2731-2736; Niemann, H., Geyer, R., Klenk, H.-D., Linder, D., Stirm, S., Wirth, M., The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein E1 (1984) EMBO J., 3, pp. 665-670; Ohtsuka, N., Yamada, Y.K., Taguchi, F., Difference in virus-binding activity of two distinct receptor proteins for mouse hepatitis virus (1996) J. Gen. Virol., 77, pp. 1683-1692; Pfleiderer, M., Skinner, M.A., Siddell, S.G., Coronavirus MHV-JHM: Nucleotide sequence of the mRNA that encodes the membrane protein (1986) Nucleic Acids Res., 14, p. 6338; Rottier, P.J.M., The coronavirus membrane glycoprotein (1995) The Coronaviridae, pp. 115-139. , S.G. Siddell. New York: Plenum; Siddell, S.G., The coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S.G. Siddell. New York: Plenum; Skinner, M.A., Siddell, S.G., Coronavirus JHM: Nucleotide sequence of the mRNA that encodes nucleocapsid protein (1983) Nucleic Acids Res., 11, pp. 5045-5054; Stern, D.F., Sefton, B.M., Coronavirus proteins: Structure and function of the oligosaccharides of the avian infectious bronchitis virus glycoproteins (1982) J. Virol., 44, pp. 804-812; Yamada, Y.K., Yabe, M., Yamada, A., Taguchi, F., Detection of mouse Hepatitis virus by the polymerase chain reaction and its application to the rapid diagnosis of infection (1993) Lab. Anim. Sci., 43, pp. 285-290; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219","Yamada, Y.K.; Division Experimental Animal Res., Natl. Institute Infectious Diseases, 4-7-1 Gakuen, Musashimurayama, Tokyo 208-0011, Japan; email: ykyamada@nih.go.jp",,,01681702,,VIRED,"10725548","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0034052668
"Nokso-Koivisto J., Pitkäranta A., Blomqvist S., Kilpi T., Hovi T.","6602762108;7003331729;7004588653;7003727621;36152793900;","Respiratory coronavirus infections in children younger than two years of age",2000,"Pediatric Infectious Disease Journal","19","2",,"164","166",,15,"10.1097/00006454-200002000-00016","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343851643&doi=10.1097%2f00006454-200002000-00016&partnerID=40&md5=4e433409cb3cb9bfa79d72ce787dc496","Department of Otorhinolaryngology, University of Helsinki, Helsinki, Finland; Department of Virology, Helsinki, Finland; Department of Vaccines, Helsinki, Finland","Nokso-Koivisto, J., Department of Otorhinolaryngology, University of Helsinki, Helsinki, Finland, Department of Virology, Helsinki, Finland; Pitkäranta, A., Department of Otorhinolaryngology, University of Helsinki, Helsinki, Finland; Blomqvist, S., Department of Virology, Helsinki, Finland; Kilpi, T., Department of Vaccines, Helsinki, Finland; Hovi, T., Department of Virology, Helsinki, Finland",[No abstract available],"Children; Human coronavirus; Otitis media; Respiratory infection","antigen antibody reaction; article; common cold; enzyme linked immunosorbent assay; Finland; fluoroimmunoassay; human; hybridization; laboratory test; otitis media; preschool child; priority journal; reinfection; reverse transcription polymerase chain reaction; virus infection; Child, Preschool; Coronavirus; Coronavirus Infections; Ear, Middle; Humans; Infant; Nasopharynx; Nucleic Acid Hybridization; Otitis Media with Effusion; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction","Mäkelä, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Isaacs, D., Flowers, D., Clarke, J.R., Valman, H.B., MacNaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch Dis Child, 58, pp. 500-503; Pitkäranta, A., Virolainen, A., Jero, J., Arruda, E., Hayden, F.G., Detection of rhinovirus, respiratory syncytial virus, and coronavirus infections in acute otitis media by reverse transcriptase polymerase chain reaction (1998) Pediatrics, 102, pp. 291-295; Ukkonen, P., Hovi, T., Von Bonsdorff, Ch., Saikku, P., Penttinen, K., Age-specific prevalence of complement-fixing antibodies to sixteen viral antigens: A computer analysis of 58 500 patients covering a period of eight years (1984) J Med Virol, 13, pp. 131-148; Hovi, T., Kainulainen, H., Ziola, B., Salmi, A., OC43 strain-related coronavirus antibodies in different age groups (1979) J Med Virol, 3, pp. 313-320; Sizun, J., Arbour, N., Talbot, P.J., Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture (1998) J Virol Methods, 72, pp. 145-152; Ieven, M., Goossens, H., Relevance of nucleic acid amplification techniques for diagnosis of respiratory tract infections in the clinical laboratory (1997) Clin Microbiol Rev, 10, pp. 242-256; Pitkäranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR (1997) J Clin Microbiol, 35, pp. 1791-1793; Räty, R., Kleemola, M., Melén, K., Stenvik, M., Julkunen, I., Efficacy of PCR and other diagnostic methods for the detection of respiratory adenoviral infections (1999) J Med Virol, 59, pp. 66-72; Blomqvist, S., Skyttä, A., Roivainen, M., Hovi, T., Rapid detection of human rhinovirus in nasopharyngeal aspirates by microwell reverse transcription-polymerase chain reaction-hybridization assay (1999) J Clin Microbiol, 37, pp. 2813-2816; Kaye, H.S., Marsh, H.B., Dowdle, W.R., Seroepidemiologic survey of coronavirus (strain OC43) related infections in a childrens population (1971) Am J Epidemiol, 94, pp. 43-49; McIntosh, K., Kapikian, A.Z., Turner, H.C., Hartley, J.W., Parrot, R.H., Chanock, R.M., Seroepidemiologic studies of coronavirus infection in adults and children (1070) Am J Epidemiol, 91, pp. 585-592; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, Ma., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Arruda, E., Pitkäranta, A., Witek T.J., Jr., Doyle, C.A., Hayden, F.G., Frequency and natural history of rhinovirus infections in adults during autumn (1997) J Clin Microbiol, 35, pp. 2864-2868","Nokso-Koivisto, J.; Department of Otorhinolaryngology, University of Helsinki, Helsinki, Finland",,,08913668,,PIDJE,"10694007","English","Pediatr. Infect. Dis. J.",Article,"Final",Open Access,Scopus,2-s2.0-0343851643
"Raamsman M.J.B., Krijnse Locker J., De Hooge A., De Vries A.A.F., Griffiths G., Vennema H., Rottier P.J.M.","6603137050;6602308258;6506264528;7202909794;56221617000;7003697291;7006145490;","Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E",2000,"Journal of Virology","74","5",,"2333","2342",,92,"10.1128/JVI.74.5.2333-2342.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342470994&doi=10.1128%2fJVI.74.5.2333-2342.2000&partnerID=40&md5=ecb59df7661b2a7c814e6e2f0e71d276","Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Europ. Molecular Biology Laboratory, Heidelberg, Germany; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","Raamsman, M.J.B., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Krijnse Locker, J., Europ. Molecular Biology Laboratory, Heidelberg, Germany; De Hooge, A., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; De Vries, A.A.F., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Griffiths, G., Europ. Molecular Biology Laboratory, Heidelberg, Germany; Vennema, H., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","The small envelope (E) protein has recently been shown to play an essential role in the assembly of coronaviruses. Expression studies revealed that for formation of the viral envelope, actually only the E protein and the membrane (M) protein are required. Since little is known about this generally low-abundance virion component, we have characterized the E protein of mouse hepatitis virus strain A59 (MHV-A59), an 83-residue polypeptide. Using an antiserum to the hydrophilic carboxy terminus of this otherwise hydrophobic protein, we found that the E protein was synthesized in infected cells with similar kinetics as the other viral structural proteins. The protein appeared to be quite stable both during infection and when expressed individually using a vaccinia virus expression system. Consistent with the lack of a predicted cleavage site, the protein was found to become integrated in membranes without involvement of a cleaved signal peptide, nor were any other modifications of the polypeptide observed. Immunofluorescence analysis of cells expressing the E protein demonstrated that the hydrophilic tail is exposed on the cytoplasmic side. Accordingly, this domain of the protein could not be detected on the outside of virions but appeared to be inside, where it was protected from proteolytic degradation. The results lead to a topological model in which the polypeptide is buried within the membrane, spanning the lipid bilayer once, possibly twice, and exposing only its carboxy-terminal domain. Finally, electron microscopic studies demonstrated that expression of the E protein in cells induced the formation of characteristic membrane structures also observed in MHV-A59-infected cells, apparently consisting of masses of tubular, smooth, convoluted membranes. As judged by their colabeling with antibodies to E and to Rab-1, a marker for the intermediate compartment and endoplasmic reticulum, the E protein accumulates in and induces curvature into these pre-Golgi membranes where coronaviruses have been shown earlier to assemble by budding.",,"envelope protein; membrane protein; animal cell; article; immunofluorescence; kinetics; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein degradation; protein expression; protein synthesis; virus characterization; virus strain; Animals; Cell Line; Cell Membrane; Coronavirus; Fluorescent Antibody Technique; Genetic Vectors; L Cells (Cell Line); Mice; Microscopy, Electron; Murine hepatitis virus; Precipitin Tests; Recombinant Proteins; Transfection; Vaccinia virus; Viral Envelope Proteins; Virus Assembly; Virus Integration","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Bredenbeek, P., (1990) Nucleic Acid Domains and Proteins Involved in the Replication of Coronaviruses, , Ph.D. thesis. Utrecht University, Utrecht, The Netherlands; Budzilowicz, C.J., Weiss, S.R., In vitro synthesis of two polypeptides from a nonstructural gene of coronavirus mouse hepatitis virus strain A59 (1987) Virology, 159, pp. 509-515; David-Ferreira, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) J. Cell Biol., 24, pp. 57-78; De Haan, C.A.M., Roestenberg, P., De Wit, M., De Vries, A.A.F., Nilsson, T., Vennema, H., Rattier, P.J.M., Structural requirements for O-glycosylation of the mouse hepatitis virus membrane protein (1998) J. Biol. Chem., 273, pp. 29905-29914; De Vries, A.A.F., Chirnside, E.D., Horzinek, M.C., Rottier, P.J.M., Structural proteins of equine arteritis virus (1992) J. Virol., 66, pp. 6294-6303; De Vries, A.A.F., Raamsman, M.J.B., Van Dijk, H.A., Horzinek, M.C., Rottier, P.J.M., The small envelope glycoprotein (Gs) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer (1995) J. Virol., 69, pp. 3441-3448; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Elroy-Stein, O., Moss, B., Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6743-6747; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. 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Cell Biol., 18, pp. 795-811; Hobman, T.C., Zhao, B., Chan, H., Farquhar, M.G., Immunoisolation and characterization of a subdomain of the endoplasmic reticulum that concentrates proteins involved in COPII vesicle biogenesis (1998) Mol. Biol. Cell, 9, pp. 1265-1278; Jacobs, L., Spaan, W.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Synthesis of subgenomic mRNAs of mouse hepatitis virus is initiated independently: Evidence from UV transcription mapping (1981) J. Virol., 39, pp. 401-412; Klumperman, J., Krijnse Locker, J., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J.M., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Krijnse Locker, J., Rose, J.K., Horzinek, M.C., Rottier, P.J.M., Membrane assembly of the triple-spanning coronavirus M protein: Individual transmembrane domains show preferred orientation (1992) J. Biol. 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Virol., 38, pp. 20-26; Rottier, P.J.M., Brandenburg, D., Armstrong, J., Van Der Zeijst, B.A.M., Warren, G., Assembly in vitro of a spanning membrane protein of the endoplasmic reticulum: The E1 glycoprotein of coronavirus MHV-A59 (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 1421-1425; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Rottier, P.J.M., Welling, G.W., Welling-Wester, S., Niesters, H.G.M., Lenstra, J.A., Van Der Zeijst, B.A.M., Predicted membrane topology of the coronavirus protein E1 (1986) Biochemistry, 25, pp. 1335-1339; Saraste, J., Lahtinen, U., Goud, B., Localization of the small GTP-binding protein rablp to early compartments of the secondary pathway (1995) J. Cell Sci., 108, pp. 1541-1552; Siddell, S.G., (1995) The Coronaviridae, , Plenum Press, New York, N.Y; Siddell, S.G., The small-membrane protein (1995) The Coronaviridae, pp. 181-189. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Slot, J.W., Geuze, H.G., Gigengack, S., Lienhard, G.E., James, D.E., Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat (1991) J. Cell Biol., 113, pp. 123-135; Smith, A.R., Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Inglis, S.C., Identification of a new membrane-associated polypeptide specified by the coronavirus infectious bronchitis virus (1990) J. Gen. Virol., 71, pp. 3-11; Snijder, E.J., Van Tol, H., Pedersen, K.W., Raamsman, M.J.B., De Vries, A.A.F., Identification of a novel structural protein of arteriviruses (1999) J. Virol., 73, pp. 6335-6345; Spaan, W.J.M., Rottier, P.J.M., Horzinek, M.C., Van Der Zeijst, B.A.M., Isolation and identification of virus specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59) (1981) Virology, 108, pp. 424-434; Sutter, G., Ohlman, M., Erfle, V., Non-replicating vaccinia virus vector efficiently expresses bacteriophage T7 RNA polymerase (1995) FEBS Lett., 371, pp. 9-12; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA5 (1994) J. Gen. Virol., 75, pp. 3041-3046; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in Sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Tooze, S.A., Tooze, J., Warren, G., Site of addition of N-acetylgalactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 (1988) J. Cell Biol., 106, pp. 1475-1487; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by expression of viral envelope proteins (1996) EMBO J., 15, pp. 2020-2028; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands; email: P.Rottier@vet.uu.nl",,,0022538X,,JOVIA,"10666264","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0342470994
"Al-Yousif Y., Al-Majhdi F., Chard-Bergstrom C., Anderson J., Kapil S.","56403260400;16641849700;6602711643;8890406600;7003293348;","Development, characterization, and diagnostic applications of monoclonal antibodies against bovine rotavirus",2000,"Clinical and Diagnostic Laboratory Immunology","7","2",,"288","292",,7,"10.1128/CDLI.7.2.288-292.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034007978&doi=10.1128%2fCDLI.7.2.288-292.2000&partnerID=40&md5=e553b7d078df73c5357577405918b8f8","Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-56061, United States","Al-Yousif, Y., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Al-Majhdi, F., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Chard-Bergstrom, C., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Anderson, J., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States, Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-56061, United States","Hybridomas secreting monoclonal antibodies (MAbs) against the Nebraska calf diarrhea strain of bovine rotavirus (BRV) were characterized. Indirect fluorescent-antibody assay, immunodot assay, and immunoprecipitation were used to select hybridomas that produced anti-BRV MAbs. Seven of the MAbs were shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot assay to be reactive with the BRV outer capsid protein, VP7, which has a molecular mass of 37.5 kDa. None of the seven MAbs were reactive with canine rotavirus, bovine coronavirus, or uninfected Madin-Darby bovine kidney cells. Two clones, 8B4 (immunoglobulin G2a [IgG2a]) and 2B11 (IgG1), were found suitable for use in an antigen capture enzyme-linked immunosorbent assay for detecting BRV in bovine fecal samples. Both were subtype A specific (G6 subtype) but did not react with all isolates of BRV group A.",,"immunoglobulin G; monoclonal antibody; virus antibody; antibody detection; article; cattle; controlled study; hybridoma; immunoprecipitation; immunotherapy; nonhuman; priority journal; Rotavirus; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Capsid; Capsid Proteins; Cattle; Cell Line; Dogs; Mice; Mice, Inbred BALB C; Rotavirus; Rotavirus Infections","Athanassious, R., Marsolias, G., Assaf, R., Dea, S., Descoteaux, J., Dulude, R., Montpetit, C., Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can. Vet. J., 35, pp. 163-169; Birch, C.J., Heath, R.L., Gust, I.D., Use of serotype-specific monoclonal antibodies to study the epidemiology of rotavirus infection (1989) J. Med. Virol., 24, pp. 45-53; Carson, F.L., (1990) Histotechnology, pp. 10-14. , ASCP Press, Chicago, Ill; Crawford, S.E., Estes, M.K., Ciarlet, M., Barone, C., O'Neal, C.M., Chin, J., Conner, M.E., Heterotypic protection and induction of a broad heterotypic neutralization response by rotavirus-like particles (1999) J. Virol., 73, pp. 4813-4822; Czeruy, C.P., Eichhorn, W., Characterization of monoclonal and polyclonal antibodies to bovine enteric coronavirus: Establishment of an efficient ELISA for antigen detection in feces (1989) Vet. Microbiol., 20, pp. 111-122; Estes, M.K., Cohen, D.J., Rotavirus gene structure and function (1989) Microbiol. Rev., 3, pp. 410-449; Goding, J., Purification, fragmentation and isotopic labelling of monoclonal antibodies (1996) Monoclonal Antibodies. Principles and Practice, pp. 104-141. , J. W. Goding (ed.) Academic Press, San Diego, Calif; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immunofluorescence of nasal epithelial cells (1990) Vet. Microbiol., 19, pp. 217-231; Herbrink, P.F., Van Bussel, J., Warnaar, S.O., The antigen spot test (AST): Highly sensitive assay for the detection of antibodies (1982) J. Immunol. Methods, 48, pp. 293-298; Hoshino, M., Ysereno, M., Midthun, K., Flores, J., Kapikian, A.Z., Chanock, R.M., Independent segregation of two antigenic specificities (VP3 and VP7) involved in neutralization of rotavirus infectivity (1984) Proc. Natl. Acad. Sci. USA, 82, pp. 8701-8704; Hussein, H.A., Frost, E., Talbot, B., Shalaby, M., Cornaglia, E., El-Azhary, Y., Comparison of polymerase chain reaction and monoclonal antibodies for G-typing of group A bovine rotavirus directly from fecal material (1996) Vet. Microbiol., 51, pp. 11-17; Ijaz, M.K., Alkarmi, T.O., El-Mekki, A.W., Galadari, S.H., Dar, F.K., Babiuk, L.A., Priming and induction of anti-rotavirus antibody response by synthetic peptides derived from VP7 and VP4 (1995) Vaccine, 13, pp. 3312-3318; Ijaz, M.K., Attah-Poku, S.K., Redmond, M.J., Parker, M.D., Sabara, M.I., Frenchick, P., Babiuk, L.A., Heterotypic passive protection induced by synthetic peptides corresponding to VP7 and VP4 of bovine rotavirus (1991) J. Virol., 65, pp. 3106-3113; Kapikian, A.Z., Flores, J., Hoshino, Y., Glass, R.I., Midthun, K., Gorziglia, M., Chanock, R.M., Rotavirus: The major etiologic agent in severe infantile diarrhea may be controllable by a 'Jennerian' approach to vaccination (1986) J. Infect. Dis., 153, pp. 815-822; Kapikian, A.Z., Hoshino, Y., Chanock, R.M., Perez-Schael, I., Efficacy of a quadrivalent rhesus rotavirus-based human rotavirus vaccine aimed at preventing severe rotavirus diarrhea in infants and young children (1996) J. Infect. Dis., 174, pp. 65-72; Kapil, S., Richardson, K.L., Radi, C., Chard-Bergstrom, C., Factors affecting isolation and propagation of bovine coronavirus in human rectal tumor-18 cell line (1996) J. Vet. Diagn. Investig., 8, pp. 96-99; King, S., Brain, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Kobayashi, N., Taniguchi, K., Urasawa, S., Identification of operationally overlapping and independent cross-reactive neutralization region on human rotavirus VP4 (1990) J. Gen. Virol., 71, pp. 2615-2623; Liu, M., Offitt, P.A., Estes, M.K., Identification of the simian rotavirus SA1I genome segment 3 product (1988) Virology, 163, pp. 26-32; Lucchelli, A., Kang, S.Y., Jayasekera, M.K., Parwani, A.V., Zeman, D.H., Saif, L.J., A survey of G6 and G10 serotypes of group A bovine rotaviruses from diarrheic beef and dairy calves using monoclonal antibodies in ELISA (1994) J. Vet. Diagn. Investig., 6, pp. 175-181; Mackow, E.R., Barne, J.W., Chan, H., Greenberg, H.B., The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant (1989) J. Virol., 63, pp. 1661-1668; Mackow, E.R., Shaw, R.D., Matsui, S.M., Dang, M.N., Greenberg, H.B., The rhesus rotavirus gene encoding protein VP3: Location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region (1988) Proc. Natl. Acad. Sci. USA, 85, pp. 645-649; McNulty, M.S., Todd, D., Allan, G.M., McFerran, J.B., Green, J.A., Epidemiology of rotavirus infection in broiler chicken: Recognition of four serogroups (1984) Arch. Virol., 81, pp. 113-121; Noorduyn, L.A., Meddens, M.J., Lindeman, J., Van-Dijd, W.C., Herbrink, P., Favorable effect of detergent on antigen detection and comparison of enzyme linked detection systems in an ELISA for Chlamydia trachomatis (1989) J. Immunoassay, 10, pp. 429-448; Offitt, P.A., Shaw, R.D., Greenberg, H.B., Passive protection against rotavirus induced diarrhea by monoclonal antibodies to surface protein VP3 and VP7 (1986) J. Virol., 58, pp. 700-703; Rouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture-linked immunosorbent assay for detection bovine enteric comoavirus (1984) J. Clin. Microbiol., 19, pp. 3883-3893; Rugger, F.M., Johnson, K., Basile, G., Kreihenbuhl, J.P., Svensson, L., Anti-rotavirus immunoglobulin A neutralizes virus in vitro after transcystosis through epithelial cells and protects infant mice from diarrhea (1998) J. Virol., 72, pp. 2708-2714; Saif, L.J., Nongroup A rotavirus (1990) Viral Diarrheas of Man and Animals, pp. 73-96. , J. Saif and K. W. Theil (ed.) CRC Press, Inc., Boca Raton, Fla; Schoenthaler, S.L., Kapil, S., Development and application of a bovine coronavirus antigen detection enzyme-linked immunosorbent assay (1998) Clin. Diagn. Lab. Immunol., 6, pp. 130-132; Snodgrass, D.R., Herring, A.J., Campbell, I., Inglis, J.M., Hargreaves, F.D., Comparison of atypical rotaviruses from calves, piglets, lambs and man (1984) J. Gen. Virol., 65, pp. 909-914; Tahir, R.A., Pomeroy, K.A., Goyal, S.M., Evaluation of shell vial cell culture technique for the detection of bovine coronavirus (1995) J. Vet. Diagn. Investig., 7, pp. 301-304; Taniguchi, K., Urasawa, T., Urasawa, S., Species specificity and interspecies relatedness on VP4 genotypes demonstrated by VP4 sequence analysis of equine, feline, and canine rotavirus strains (1994) Virology, 200, pp. 390-400; Taniguchi, K., Maloy, W.L., Nishikawa, K., Green, K.Y., Hoshino, Y., Uraswa, S., Kapikian, A.Z., Gorziglia, M., Identification of cross-reactive and serotype 2-specific neutralization epitopes on VP3 of human rotavirus (1988) J. Virol., 62, pp. 2421-2426; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Reed, H.H., Saif, L.J., Isolation of coronavirus antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J. Clin. Microbiol., 33, pp. 3264-3269; Unicom, L.E., Coulson, B.S., Bishop, R.F., Experience with an enzyme immunoassay for serotyping human group A rotaviruses (1989) J. Clin. Microbiol., 27, pp. 586-588; Vanrompay, D., Van Nerom, A., Ducatelle, R., Haesebrouck, F., Evaluation of five immunoassays for detection of Chlamydia psittaci in cloacal and conjunctival specimens from turkeys (1994) J. Clin. Microbiol., 32, pp. 1470-1474; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Minocha, H.C., Kapil, S., Application of immunohistochemistry and in situ hybridization of bovine coronavirus in paraffin-embedded formalin-fixed intestine (1997) J. Clin. Microbiol., 35, pp. 2964-2965","Kapil, S.; Dept. Diagnostic Med.-Pathobiology, College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506-56061, United States; email: kapil@vet.ksu.edu",,,1071412X,,CDIME,"10702506","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0034007978
"Pennycott T.W.","7004118267;","Causes of mortality and culling in adult pheasants",2000,"Veterinary Record","146","10",,"273","278",,24,"10.1136/vr.146.10.273","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034603574&doi=10.1136%2fvr.146.10.273&partnerID=40&md5=67744769f24b45d968b95c32f67c70e8","Veterinary Science Division, Avian Health Unit, Auchincruive, Ayr KA6 5AE, United Kingdom","Pennycott, T.W., Veterinary Science Division, Avian Health Unit, Auchincruive, Ayr KA6 5AE, United Kingdom","The causes of the deaths or culling of 155 adult pheasants in breeding pens on one site between 1995 and 1997 were investigated. Approximately half the deaths were the result of problems associated with the reproductive tract or trauma, including injuries acquired during fighting or mating. Sinusitis was the commonest infectious cause of mortality or culling, despite medication of the flocks for mycoplasmosis. Marble spleen disease and pheasant coronavirus-associated nephritis, two viral conditions capable of causing high mortality, were diagnosed in a few birds in 1996 and 1997. Histomoniasis (blackhead) contributed to the mortality in 1996. A lymphomatous condition of uncertain aetiology was detected in a small number of birds.",,"animal tissue; article; bird disease; cause of death; Coronavirus; female; fighting; genital system; Gram negative infection; injury; lymphatic system; male; mating; mortality; nephritis; nonhuman; sinusitis; spleen disease; virus infection; Animalia; Aves; Coronavirus; Negibacteria; Phasianidae; Pheasant coronavirus",,"Pennycott, T.W.; Veterinary Science Division, Avian Health Unit, Auchincruive, Ayr KA6 5AE, United Kingdom",,"British Veterinary Association",00424900,,VETRA,"10749040","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0034603574
"Näslund K., Tråvén M., Larsson B., Silván A., Linde N.","8306740800;6603563444;7202678840;6701783135;15723867000;","Capture ELISA systems for the detection of bovine coronavirus-specific IgA and IgM antibodies in milk and serum",2000,"Veterinary Microbiology","72","3-4",,"183","206",,4,"10.1016/S0378-1135(99)00208-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342948674&doi=10.1016%2fS0378-1135%2899%2900208-4&partnerID=40&md5=2ef4d27441cc832bd10ccd2542e821e4","Section of Virology, Natl. Vet. Inst., Box 7073, S-750 07, Uppsala, Sweden; Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. Agric. Sci., B., Uppsala, Sweden","Näslund, K., Section of Virology, Natl. Vet. Inst., Box 7073, S-750 07, Uppsala, Sweden; Tråvén, M., Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. Agric. Sci., B., Uppsala, Sweden; Larsson, B., Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. Agric. Sci., B., Uppsala, Sweden; Silván, A., Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. Agric. Sci., B., Uppsala, Sweden; Linde, N., Section of Virology, Natl. Vet. Inst., Box 7073, S-750 07, Uppsala, Sweden","Isotype-capture ELISAs for BCV-specific IgA and IgM were developed and tested on milk and serum samples from Swedish cattle. The capture ELISAs showed higher sensitivity than indirect ELISAs for detection of BCV-specific IgA and IgM. In the capture ELISAs the agreement between detection in milk and serum samples was 94% for IgA and 86% for IgM. The correlation between log10 titres in milk and serum was r = 0.82 (P &lt; 0.001) for IgA and 0.84 (P &lt; 0.001) for IgM. Milk seemed a better target than serum for diagnosing specific IgA at low levels. There was no variation in the isotype-specific BCV antibody titres between healthy quarters of the same udder, but subclinical mastitis was associated with higher levels of IgA antibodies and weak false IgM positive reactions in undiluted milk. Bovine IgA and IgM antibodies in milk and serum showed high stability towards freezing and thawing and storage at room temperature. The antibody responses to BCV were followed in milk and serum from six dairy cows and in serum from four calves for a period of 1 year after an outbreak of winter dysentery (WD). In this outbreak some animals became reinfected with BCV. The IgA and IgM capture ELISAs differentiated between primarily BCV infected and reinfected animals. In the primarily infected cattle, IgM antibodies were first detected in milk and serum four to nine days after the first WD symptoms observed, and were subsequently detected for at least 2-3 weeks. IgM was also detected in the reinfected cows, but mostly at lower levels and for a shorter period of time than in the primarily infected animals. In milk, however, the IgM response of the reinfected cows was detected for a longer period of time than in serum. Six months after the outbreak, IgA was still detected in both serum and milk of all six cows and also in serum of one calf. The reinfected cows showed higher and more long-lasting peak levels of IgA in milk and serum than the primarily infected cows, indicating boosting of the IgA response. (C) 2000 Elsevier Science B.V.","Bovine coronavirus; Cattle; IgA; IgM; Isotype-capture; Milk; Reinfection","immunoglobulin A antibody; immunoglobulin M antibody; virus antibody; animal experiment; antibody blood level; antibody detection; antibody response; antibody titer; article; cattle; controlled study; Coronavirus; cow; enzyme linked immunosorbent assay; immunoglobulin blood level; mastitis; milk; milk level; nonhuman; Sweden; udder; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Blotting, Western; Cattle; Cattle Diseases; Coronavirus; Coronavirus Infections; Disease Outbreaks; Enzyme-Linked Immunosorbent Assay; Female; Hemagglutination Inhibition Tests; Immunoglobulin A; Immunoglobulin M; Male; Milk; Neutralization Tests; Sensitivity and Specificity; Sweden; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; RNA viruses","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Vet. Scand., 32 (2), pp. 163-170; Atterhem, K., Fossum, C., Tråvén, M., Linde, N., Näslund, K., Larsson, B., Type 1 interferon and virus-specific IgA and IgM antibodies as an aid in the diagnosis of ongoing infections in calves (1996) Swedish J. Agric. Res., 26, pp. 101-104; Butler, J., Bovine immunoglobulins: An augmented review (1983) Vet. Immunol. Immunopath., 4, pp. 43-152; Chantler, S., Diment, J.A., Current status of specific IgM antibody assays (1981) Immunoassays for the 80s, pp. 417-430. , In: Voller, A. (Ed.), MTP Press, Lancaster, England; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Fey, H., Phister, H., Messerli, J., Sturzenegger, N., Grolimund, F., Methods of isolation, purification and quantitation of bovine immunoglobulins: A technical review (1976) Zbl. Vet. Med. B, 23 (4), pp. 269-300; Galfre, G., Milstein, C., Preparation of monoclonal antibodies: Strategies and procedures (1981) Methods Enzymol., 73, pp. 3-46; Guidry, A., Butler, J., Pearson, R., Weinland, B., IgA, IgG1, IgG2, IgM and BSA in serum and mammary secretions throughout lactation (1980) Vet. Immunol. Immunopath., 1, pp. 329-341; Graham, D.A., Mawhinney, K.A., Elvander, M., Adair, B.M., Merza, M., Evaluation of an IgM-specific indirect enzyme-linked immunosorbent assay for serodiagnosis of bovine respiratory syncytial virus infection: Influence of IgM rheumatoid factor on test results with field sera (1998) J. Vet. Diagn. Invest., 10 (4), pp. 331-337; Heckert, R., Saif, L., Mengel, J., Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces and mucosal secretions from experimentally challenge-exposed colostrum-deprived calves (1991) Am. J. Vet. Res., 52 (5), pp. 692-699; Heckert, R., Saif, L., Mengel, J., Mucosal and systemic antibody responses to bovine coronavirus structural proteins in experimentally challenge-exposed calves fed low or high amount of colostral antibodies (1991) Am. J. Vet. Res., 52 (5), pp. 700-708; Heckert, R., Saif, L., Myers, G., Agnes, A., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions or dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am. J. Vet. Res., 52 (6), pp. 845-851; Hedström, H., Isaksson, A., Epizootic enteritis in cattle in Sweden (1951) Cornell Vet., 42, pp. 251-253; Honkanen-Buzalski, T., Sandholm, M., Association of bovine secretory immunoglobulins with milk fat globule membranes (1981) Comp. Immunol. Microbiol. Infect. Dis., 4, pp. 329-342; Hordnes, K., Tynning, T., Brown, T., Haneberg, B., Jonsson, R., Nasal immunization with group B Streptococci can induce high levels of specific IgA antibodies in cervicovaginal secretions of mice (1997) Vaccine, 15, pp. 1244-1251; Hu, K.-F., Ekström, J., Lövgren-Bengtsson, K., Morein, B., Induction of antibody responses in the common mucosal system by an RSV ISCOM and its applications in vaccine formulation (1999) Med. Microbiol. Immunol., 187, pp. 191-198; Hu, K.F., Elvander, M., Merza, M., Åkerblom, L., Brandenburg, A., Morein, B., The immunostimulating complex (ISCOM) is an efficient mucosal delivery system for respiratory syncytial virus (RSV) envelope antigens inducing high local and systemic antibody responses (1998) Clin. Exp. Immunol., 113, pp. 235-243; Kimman, T., Westenbrink, F., Schreuder, B., Straver, P., Local and systemic antibody response to bovine respiratory syncytial virus infection and reinfection in calves with and without maternal antibodies (1987) J. Clin. Microbiol., 25 (6), pp. 1097-1106; Kimman, T.G., Westenbrink, F., Straver, P.J., Zaane, D.V., Schreuder, B.E.C., Isotype-specific ELISAs for the detection of antibodies to bovine respiratory syncytial virus (1987) Res. Vet. Sci., 43, pp. 180-187; Klingenberg, K.D.V., Vågsholm, I., Alenius, S., Incidence of diarrhea after strict closure and eradication of bovine viral diarrhea virus infection in a dairy herd (1999) J. Am. Vet. Med. Assoc., 214, pp. 1824-1828; Lascelles, A., Beh, K., Husband, A., Origin of antibody in mammary secretions with particular reference to the IgA system. In: Butler J.E. (Ed), The Ruminant Immune System (1981) Adv. Exp. Med. Biol., 137, pp. 493-511; Liew, F., Russell, S., Appleyard, G., Brand, C., Beale, J., Cross-protection in mice infected with influenza A virus by the respiratory route is correlated with local IgA antibody rather than serum antibody or cytotoxic T cell reactivity (1984) Eur. J. Immunol., 14, pp. 350-356; McNulty, M.S., Bryson, D.G., Allan, G.M., Logan, E.F., Coronavirus infection of the bovine respiratory tract (1984) Vet. Microbiol., 9, pp. 425-434; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet. Pathol., 10, pp. 45-64; Meurmann, O., Detection of antiviral IgM antibodies and its problems - A review (1983) Curr. Topics Microbiol. Immunol., 104, pp. 101-131; Nakane, P.K., Kawaoi, A., A peroxidase-labeled antibody. A new method of conjugation (1974) J. Histochem. 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Methods, 72, pp. 427-441","Traven, M.; Ruminant Med./Vet. Epidemiol. Dept., Swedish Univ. of Agric. Sciences, Box 7019, S-750 07 Uppsala, Sweden; email: madelein.traven@idmed.slu.se",,,03781135,,VMICD,"10727830","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0342948674
"Bost A.G., Carnahan R.H., Tao Lu X., Denison M.R.","6506678262;7003616850;6504381997;7101971810;","Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly",2000,"Journal of Virology","74","7",,"3379","3387",,85,"10.1128/JVI.74.7.3379-3387.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034054288&doi=10.1128%2fJVI.74.7.3379-3387.2000&partnerID=40&md5=d90f1d67ee588bfbf37415b61343cd9f","Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States; Department of Cell Biology, Vanderbilt University, Nashville, TN 37232, United States; Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Nashville, TN 37232, United States; Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States","Bost, A.G., Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States; Carnahan, R.H., Department of Cell Biology, Vanderbilt University, Nashville, TN 37232, United States; Tao Lu, X., Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Nashville, TN 37232, United States; Denison, M.R., Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States, Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Nashville, TN 37232, United States, Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States","The replicase gene (gene 1) of the coronavirus mouse hepatitis virus (MHV) encodes two co-amino-terminal polyproteins presumed to incorporate all the virus-encoded proteins necessary for vital RNA synthesis. The polyproteins are cotranslationally processed by vital proteinases into at least 15 mature proteins, including four predicted cleavage products of less than 25 kDa that together would comprise the final 59 kDa of protein translated from open reading frame 1a. Monospecific antibodies directed against the four distinct domains detected proteins of 10, 12, and 15 kDa (p1a-10, p1a-12, and p1a-15) in MHV-A59-infected DBT cells, in addition to a previously identified 22-kDa protein (p1a-22). When infected cells were probed by immunofluorescence laser confocal microscopy, p1a-10, -22, -12, and -15 were detected in discrete foci that were prominent in the perinuclear region but were widely distributed throughout the cytoplasm as well. Dual- labeling experiments demonstrated colocalization of the majority of p1a-22 in replication complexes with the helicase, nucleocapsid, and 3C-like proteinase, as well as with p1a-10, -12, and -15. p1a-22 was also detected in separate foci adjacent to the replication complexes. The majority of complexes containing the gene 1 proteins were distinct from sites of accumulation of the M assembly protein. However, in perinuclear regions the gene 1 proteins and nucleocapsid were intercalated with sites of M protein localization. These results demonstrate that the complexes known to be involved in RNA synthesis contain multiple gene 1 proteins and are closely associated with structural proteins at presumed sites of virion assembly.",,"antibody; helicase; M protein; proteinase; RNA directed RNA polymerase; virus protein; virus RNA; antibody labeling; article; confocal laser microscopy; cytoplasm; immunofluorescence; Murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; protein assembly; protein expression; protein localization; RNA synthesis; virion; virus cell interaction; virus gene; virus nucleocapsid; Cell Line; Kinetics; Murine hepatitis virus; Nucleocapsid; Protein Processing, Post-Translational; RNA Replicase; Viral Proteins; Virion; Virus Assembly","Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. 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Cell Biol., 106, pp. 1475-1487; Van Der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Krijnse Locker, J., The localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73, pp. 7641-7657; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185","Denison, M.R.; Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States; email: mark.denison@mcmail.vanderbilt.edu",,,0022538X,,JOVIA,"10708455","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034054288
"O'Connor J.B., Brian D.A.","55433538800;7006460232;","Downstream ribosomal entry for translation of coronavirus TGEV gene 3b",2000,"Virology","269","1",,"172","182",,20,"10.1006/viro.2000.0218","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034732207&doi=10.1006%2fviro.2000.0218&partnerID=40&md5=7ad1e08a6b39b6dcb0eeed6791c5b1ff","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","O'Connor, J.B., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Gene 3b (ORF 3b) in porcine transmissible gastroenteritis coronavirus (TGEV) encodes a putative nonstructural polypeptide of 27.7 kDa with unknown function that during translation in vitro is capable of becoming a glycosylated integral membrane protein of 31 kDa. In the virulent Miller strain of TGEV, ORF 3b is 5'-terminal on mRNA 3-1 and is presumably translated following 5' cap-dependent ribosomal entry. For three other strains of TGEV, the virulent British FS772/70 and Taiwanese TFI and avirulent Purdue-116, mRNA species 3-1 is not made and ORF 3b is present as a non-overlapping second ORF on mRNA 3. ORF 3b begins at base 432 on mRNA 3 in Purdue strain. In vitro expression of ORF 3b from Purdue mRNA 3-like transcripts did not fully conform to a predicted leaky scanning pattern, suggesting ribosomes might also be entering internally. With mRNA 3-like transcripts modified to carry large ORFs upstream of ORF 3a, it was demonstrated that ribosomes can reach ORF 3b by entering at a distant downstream site in a manner resembling ribosomal shunting. Deletion analysis failed to identify a postulated internal ribosomal entry structure (IRES) within ORF 3a. The results indicate that an internal entry mechanism, possibly in conjunction with leaky scanning, is used for the expression of ORF 3b from TGEV mRNA 3. One possible consequence of this feature is that ORF 3b might also be expressed from mRNAs 1 and 2. (C) 2000 Academic Press.","Gene 3b; Porcine transmissible gastroenteritis coronavirus; Ribosomal scanning; Ribosomal shunting","virus protein; animal cell; article; Coronavirus; gene deletion; gene expression; nonhuman; priority journal; ribosome; RNA translation; swine; testis cell; Acronicta leporina; Animalia; Coronavirus; RNA viruses; Staphylococcus phage 3A; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Sequencing of coronavirus IBV genomic RNA: Three open reading frames in the 5′ ""unique"" region of mRNA D (1985) J. Gen. Virol., 66, pp. 2253-2258; Brian, D.A., Dennis, D.E., Guy, J.S., Genome of porcine transmissible gastroenteritis virus (1980) J. 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Virol., 63, pp. 28-35; Yueh, A., Schneider, R.J., Selective translation initiation by ribosome jumping in adenovirus-infected and heat-shocked cells (1996) Genes Dev., 10, pp. 1557-1567","Brian, D.A.; University of Tennessee, Department of Microbiology, Walters Life Science Building, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,"Academic Press Inc.",00426822,,VIRLA,"10725209","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0034732207
"Chang K.W., Sheng Y., Gombold J.L.","57199091715;7202843152;6602901502;","Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein",2000,"Virology","269","1",,"212","224",,38,"10.1006/viro.2000.0219","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034732109&doi=10.1006%2fviro.2000.0219&partnerID=40&md5=1c0e97880c6fc23f655bbdee9d06f990","Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States","Chang, K.W., Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Sheng, Y., Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Gombold, J.L., Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States","The spike glycoprotein of mouse hepatitis virus strain A59 mediates the early events leading to infection of cells, including fusion of the vital and cellular membranes. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail. In this study, we examined the role of these carboxyl-terminal domains in spike-mediated membrane fusion. We show that the cytoplasmic tail is not required for fusion but has the capacity to enhance membrane fusion activity. Chimeric spike protein mutants containing substitutions of the entire transmembrane anchor and cys domain with the herpes simplex virus type 1 glycoprotein D (gD-1) anchor demonstrated that fusion activity requires the presence of the A59 membrane-spanning domain and the portion of the cys domain that lies upstream of the cytoplasmic tail. The cys domain is a required element since its deletion from the wild-type spike protein abrogates fusion activity. However, addition of the cys domain to fusion- defective chimeric proteins was unable to restore fusion activity. Thus, the cys domain is necessary but is not sufficient to complement the gD-1 anchor and allow for membrane fusion. Site-specific mutations of conserved cysteine residues in the cys domain markedly reduce membrane fusion, which further supports the conclusion that this region is crucial for spike function. The results indicate that the carboxyl-terminus of the spike transmembrane anchor contains at least two distinct domains, both of which are necessary for full membrane fusion. (C) 2000 Academic Press.",,"virus glycoprotein; animal cell; article; carboxy terminal sequence; female; membrane fusion; Murine hepatitis coronavirus; nonhuman; priority journal; protein domain; Amino Acid Sequence; Amino Acid Substitution; Animals; beta-Galactosidase; Cell Fusion; Cell Line; Conserved Sequence; Cysteine; Cytoplasm; Genes, Reporter; Kinetics; Membrane Fusion; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Deletion; Transfection; Viral Envelope Proteins; Animalia; Coronavirus; Herpes; Human herpesvirus 1; Murinae; Murine hepatitis virus; RNA viruses","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Bagai, S., Lamb, R.A., Truncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusion (1996) J. 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"Takamura K., Okada N., Ui S., Hirahara T., Shimizu Y.","57192335035;7201736157;7004109542;7004438947;7404067558;","Protection studies on winter dysentery caused by bovine coronavirus in cattle using antigens prepared from infected cell lysates",2000,"Canadian Journal of Veterinary Research","64","2",,"138","140",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034170457&partnerID=40&md5=0912bc5a7c14ef4ff945f2208a02129f","Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan","Takamura, K., Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan; Okada, N., Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan; Ui, S., Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan; Hirahara, T., Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan; Shimizu, Y., Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan","Cells infected with bovine coronavirus (BCV) were solubilized with Triton X-100 to yield a cell lysate (CL) antigen having high hemagglutinating (HA) titers. The antigen gave high HA titers using rat erythrocytes, suggesting that it contained large amounts of hemagglutinin esterase (HE) antigen. The CL antigen, combined with an oil adjuvant, was tested for protective and antibody-inducing activities in cattle. Four groups (2 cattle/group) of cattle were inoculated with CL antigen having HA titers of 16 000, 4000, 1000, and 250. Another group served as untreated controls. Two intramuscular inoculations were given at an interval of 3 wk. The animals were challenged with virus 1 wk after the second inoculation. The groups immunized with the CL antigen having an HA titer of 4000 or 16 000 produced hemagglutination inhibition (HI) antibody titers of > 320 and serum neutralizing (SN) antibody titers of > 1280. These groups of animals showed no clinical abnormalities after challenge. In the groups immunized with CL antigen at an HA titer of 1000 or 250, HI antibody titers were 40 to 160 and SN titers were 80 to 640. The cattle with HI antibody titers of ≥ 160 and the SN titers of ≥ 640 showed no clinical signs, but the cattle with the HI antibody titer < 80 and the SN antibody titer < 160 developed watery diarrhea and fever after challenge. These results indicate that CL antigen with high HA titer induces antibody production in cattle that provides effective protection against winter dysentery.",,"virus antigen; animal; animal disease; article; cattle; cattle disease; Coronavirus; dysentery; hemagglutination test; immunology; rat; season; vaccination; virology; virus infection; Animals; Antigens, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Dysentery; Hemagglutination Tests; Rats; Seasons; Vaccination","Bunn, F.H., Garbay, K.H., Gallop, P.M., The glycosylation of hemoglobin: Relevance to diabetes mellitus (1978) Science, 200, pp. 21-27; Peacock, I., Glycosylated hemoglobin: Measurement and clinical use (1984) J Clin Pathol, 37, pp. 841-851; Wood, P.A., Smith, J.E., Glycosylated hemoglobin and canine diabetes (1980) J Am Vet Med Assoc, 176, pp. 1267-1268; Wood, P.A., Smith, J.E., Elevation rate of glycosylated hemoglobins in dogs after induction of experimental diabetes mellitus (1982) Metabolism, 31, pp. 906-909; Mahaffey, E.A., Cornelius, L.M., Evaluation of a commercial kit for measurement of glycosylated hemoglobin in canine blood (1981) Vet Clin Pathol, 10, pp. 21-24; Smith, J.E., Wood, P.A., Moore, K., Evaluation of a colorimetric method for canine glycosylated hemoglobin (1982) Am J Vet Res, 43, pp. 700-701; Easley, J.R., Glycosylated hemoglobin in dogs: Precision, stability and diagnostic utility (1986) Vet Clin Pathol, 15, pp. 12-15; Mahaffey, E.A., Cornelius, L.M., Glycosylated hemoglobin in diabetic and nondiabetic dogs (1982) J Am Vet Med Assoc, 180, pp. 635-637; Marca, M.C., Loste, A., Glycosylated hemoglobin assay in canine samples (2000) J Small Anim Pract, , In press; Loste, A., Marca, M.C., Estabilidad de fructosamina y hemoglobina glicosilada en muestras caninas (1999) 34th Cong Nac AVEPA, p. 215; Hasegawa, S., Sako, T., Takemura, N., Koyama, H., Motoyoshi, S., Glycated hemoglobin fractions in normal and diabetic dogs measured by high performance liquid chromatography (1991) J Vet Med Sci, 53, pp. 65-68; Jensen, A.L., Glycated proteins in canine diabetes mellitus (1995) Vet Rec, 14, pp. 401-405; Elliot, D.A., Nelson, R.W., Feldman, E.C., Neal, L.A., Glycosylated hemoglobin concentration in the blood of healthy dogs and dogs with naturally developing diabetes mellitus, pancreatic β-cell neoplasia, hyperadrenocorticism and anemia (1997) J Am Vet Med Assoc, 211, pp. 723-727; Miravalles, E., Pascual, T., Irurzun, A., Glycated hemoglobins and fructosamine in patients with anemias (1993) Klin Lab, 39, pp. 1052-1054","Takamura, K.; Division of Veterinary Microbiology, KYOTO-BIKEN Laboratories, 24-16 Makishima-cho, Uji 611-0041, Japan; email: fvgk8253@mb.infoweb.ne.jp",,,08309000,,,"10805255","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0034170457
"Watson D.W., Guy J.S., Stringham S.M.","35568492000;7202723649;35585802200;","Limited transmission of turkey coronavirus in young turkeys by adult Alphitobius diaperinus (Coleoptera: Tenebrionidae)",2000,"Journal of Medical Entomology","37","3",,"480","483",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0012834893&partnerID=40&md5=7ac7f3d6d4dccf89a1db037c048e0901","Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; College of Veterinary Medicine, North Carolina State University, Raleigh, NC, United States","Watson, D.W., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; Guy, J.S., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States, College of Veterinary Medicine, North Carolina State University, Raleigh, NC, United States; Stringham, S.M., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States","We examined the role of lesser mealworm, Alphitobius diaperinus (Panzer), in the transmission of an enteric disease of turkeys caused by a coronavirus. Turkey coronavirus (TCV) from two sources was studied, one isolate (NC95) was embryo propagated, the second was TCV infected material from turkeys diagnosed with poult enteritis mortality syndrome (PEMS). Beetles were fed virus-infected feces mixed with chicken feed. Transmission of virus was effectively halted by surface sterilization of the beetles. Turkey poults administered beetle homogenates infected with TCV+ PEMS that had not been surface sterilized had reduced weight gains and 50% mortality. Mortality and weight gains were not effected in the NC95 group. Virus isolation procedures were performed to determine NC95 viability at varying time intervals. Beetles were dissected and the guts removed 1, 12, and 24 h after the initial viral feeding. Whole beetles were also examined for comparison. Whole beetles and beetle guts were homogenized and injected into turkey eggs for embryo propagation. Direct immunofluorescence was used to determine the presence of TCV. A. diaperinus were capable of mechanical transmission of TCV. However, only turkey embryos receiving whole beetle and beetle gut homogenates within 1 h of feeding on the virus were positive for TCV. Laboratory studies demonstrating PEMS transmission by A. diaperinus are continuing.","Coronavirus; Darkling beetle; Lesser mealworm; Litter beetle; Poult enteritis mortality syndrome; Turkey disease","animal; article; beetle; bird disease; Coronavirus; isolation and purification; pathogenicity; turkey (bird); virology; Animals; Beetles; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Turkeys","Axtell, R.C., The biology and economic importance of the darkling beetle in poultry houses (1994) Poultry Supervisor's Short Course, pp. 8-17. , North Carolina State University, Raleigh, NC; Barnes, H.J., Guy, J.S., Spiking mortality of turkeys (SMT) and related disorders - An update (1995) Proceedings 19th Annual North Carolina Turkey Industry Days Conference, pp. 16-21. , North Carolina State University, Raleigh, NC; Barnes, H.J., Guy, J.S., Brown, T.P., Edens, F.W., Poult enteritis mortality syndrome (SMT) and related disorders - An update (1996) NCSU Quarterly Update to Poultry PEMS Task Force, pp. 1-8. , April. North Carolina State University, Raleigh, NC; De Las Casas, E.R., Harein, P.K., Deshmukh, D.R., Pomeroy, B.S., The relationship between the lesser mealworm and avian viruses. I. Reovirus 24 (1973) Environ. Entomol., 2, pp. 1043-1047; De Las Casas, E.R., Harein, P.K., Deshmukh, D.R., Pomeroy, B.S., Relationship between the lesser mealworm, fowl pox, and Newcastle disease virus in poultry (1976) J. Econ. Entomol., 69, pp. 775-779; Despins, J.L., Axtell, R.C., Rives, D.V., Guy, J.S., Ficken, M.D., Transmission of enteric pathogens of turkeys by darkling beetle larva (Alphitobius diaperinus) (1994) . J. Appl. Poultry Res., 3, pp. 61-65; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Guy, J.S., Barnes, H.J., Breslin, J.J., Vaillancourt, J.P., High mortality and growth depression are experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus (1999) J. Am. Vet. Med. Assoc., 215, p. 1678. , Proc 136th Meeting Am Vet Med Assoc, New Orleans; McAllister, J.C., Steelman, C.D., Newberry, L.A., Skeeles, J.K., Reservoir competence of the lesser mealworm (Coleoptera: Tenebrionidae) for Salmonella typhimurium (Eubacteriales: Enterobacteriaceae) (1994) J. Med. Entomol., 31, pp. 369-372; McAllister, J.C., Steelman, C.D., Newberry, L.A., Skeeles, J.K., Isolation of infectious bursal disease virus from the lesser mealworm, Alphitobius diaperinus (Panzer) (1995) Poultry Sci., 74, pp. 45-49; McAllister, J.C., Steelman, C.D., Skeeles, J.K., Newberry, L.A., Gbur, E.E., Reservoir competence of Alphitobius diaperinus (Coleoptera: Tenebrionidae) for Escherichia coli (Eubacteriales: Enterobacteriaceae) (1996) J. Med. Entomol., 33, pp. 983-987; McNulty, M.S., Allen, G.M., Applications of immunofluorescence in veterinary viral diagnosis (1984) Recent Advances in Virus Diagnosis, pp. 15-26. , M. S. McNulty and J. B. McFerran [eds.], Martinus Nijhoff, The Hague; (1997) User's Guide, Release 11, , Minitab, State College, PA; Pomeroy, B.S., Nagaraja, K.V., Coronaviral enteritis of turkeys (Bluecomb disease) (1991) Diseases of Poultry, 9th Ed., , B. W. Calnek, J. Barnes, C. W. Beard, W. M. Reid, H. W. Yoder, Jr. [eds.], Iowa State University Press, Ames, IA; Qureshi, M.A., Edens, F.W., Havenstein, G.B., Immune system dysfunction during exposure to poult enteritis and mortality syndrome agents (1997) Poultry Sci., 76, pp. 564-569; Rueda, L.M., Axtell, R.C., Arthropods in litter of poultry (broiler chicken and turkey) houses (1997) J. Agric. Entomol., 14, pp. 81-91; Senne, D.A., Virus propagation in embryonating eggs (1989) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 3rd Ed., pp. 176-181. , H. G. Purchase, L. H. Arp, C. H. Domermuth, and J. E. Pearson [eds.], American Association of Avian Pathologists, Kennett Square, PA","Watson, D.W.; Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States",,,00222585,,JMENA,"15535597","English","J. Med. Entomol.",Article,"Final",,Scopus,2-s2.0-0012834893
"Eléouët J.-F., Slee E.A., Saurini F., Castagné N., Poncet D., Garrido C., Solary E., Martin S.J.","6602581440;57194476093;7801420155;6506371286;7003909626;7005285839;7006171387;7404841130;","The viral nucleocapsid protein of transmissible gastroenteritis coronavirus (TGEV) is cleaved by caspase-6 and -7 during TGEV-induced apoptosis",2000,"Journal of Virology","74","9",,"3975","3983",,64,"10.1128/JVI.74.9.3975-3983.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0342313707&doi=10.1128%2fJVI.74.9.3975-3983.2000&partnerID=40&md5=c7c6fc0db99e7f655333679f6f18bc3d","U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Molecular Cell Biology Laboratory, National University of Ireland, Maynooth, County Kildare, Ireland; U.F.R. Médecine et Pharmacie, INSERM U517, 21000 Dijon, France; INRA, U. Virologie Immunol. Moleculaires, 78352 Jouy-en-Josas Cedex, France; Div. of Molecular and Cell Biology, Smurfit Institute of Genetics, Trinity College, Dublin 2, Ireland","Eléouët, J.-F., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France, INRA, U. Virologie Immunol. Moleculaires, 78352 Jouy-en-Josas Cedex, France; Slee, E.A., Molecular Cell Biology Laboratory, National University of Ireland, Maynooth, County Kildare, Ireland, Div. of Molecular and Cell Biology, Smurfit Institute of Genetics, Trinity College, Dublin 2, Ireland; Saurini, F., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Castagné, N., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Poncet, D., U. Virologie Immunol. Moleculaires, Inst. Natl. de la Rech. Agronomique, 78350 Jouy-en-Josas, France; Garrido, C., U.F.R. Médecine et Pharmacie, INSERM U517, 21000 Dijon, France; Solary, E., U.F.R. Médecine et Pharmacie, INSERM U517, 21000 Dijon, France; Martin, S.J., Molecular Cell Biology Laboratory, National University of Ireland, Maynooth, County Kildare, Ireland, Div. of Molecular and Cell Biology, Smurfit Institute of Genetics, Trinity College, Dublin 2, Ireland","The transmissible gastroenteritis coronavirus (TGEV), like many other viruses, exerts much of its cytopathic effect through the induction of apoptosis of its host cell. Apoptosis is coordinated by a family of cysteine proteases, called caspases, that are activated during apoptosis and participate in dismantling the cell by cleaving key structural and regulatory proteins. We have explored the caspase activation events that are initiated upon infection of the human rectal tumor cell line HRT18 with TGEV. We show that TGEV infection results in the activation of caspase-3, -6, -7, -8, and - 9 and cleavage of the caspase substrates eIF4GI, gelsolin, and α-fodrin. Surprisingly, the TGEV nucleoprotein (N) underwent proteolysis in parallel with the activation of caspases within the host cell. Cleavage of the N protein was inhibited by cell-permeative caspase inhibitors, suggesting that this viral structural protein is a target for host cell caspases. We show that the TGEV nucleoprotein is a substrate for both caspase-6 and -7, and using site-directed mutagenesis, we have mapped the cleavage site to VVPD359 ↓. These data demonstrate that viral proteins can be targeted for destruction by the host cell death machinery.",,"caspase; caspase 3; caspase 6; caspase 7; caspase 8; caspase 9; caspase inhibitor; cell protein; fodrin; gelsolin; nucleocapsid protein; unclassified drug; apoptosis; article; binding site; controlled study; Coronavirus; enzyme activation; enzyme activity; enzyme inhibition; enzyme specificity; enzyme substrate; gastroenteritis; human; human cell; nonhuman; peptide mapping; priority journal; protein degradation; reaction analysis; Amino Acid Chloromethyl Ketones; Animals; Antigens, CD13; Apoptosis; Caspase 3; Caspase 6; Caspase 7; Caspase 8; Caspase 9; Caspases; Cell Extracts; Cysteine Proteinase Inhibitors; Cytochrome c Group; Cytosol; Enzyme Activation; Humans; Mitochondria; Nucleocapsid; Nucleocapsid Proteins; Oligopeptides; Receptors, Virus; Transmissible gastroenteritis virus; Tumor Cells, Cultured","An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Bitzer, M., Prinz, F., Bauer, M., Spiegel, M., Neubert, W.J., Gregor, M., Schulze-Osthoff, K., Lauer, U., Sendai virus infection induces apoptosis through activation of caspase-8 (FLICE) and caspase-3 (CPP32) (1999) J. Virol., 73, pp. 702-708; Clouston, W.M., Kerr, J.F., Apoptosis, lymphocytotoxicity and the containment of viral infections (1985) Med. Hypothesis, 18, pp. 399-404; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöstrom, H., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-419; Delmas, B., Gelfi, J., Sjöström, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Adv. Exp. Med. Biol., 342, pp. 293-298; Delmas, B., Kut, E., Gelfi, J., Laude, H., Overexpression of TGEV cell receptor impairs the production of virus particles (1995) Adv. Exp. Med. Biol., 380, pp. 379-385; Devireddy, L.R., Jones, C.J., Activation of caspases and p53 by bovine herpesvirus 1 infection results in programmed cell death and efficient virus release (1999) J. Virol., 73, pp. 3778-3788; Earnshaw, W.C., Martins, L.M., Scott, H., Kaufmann, S.H., Mammalian caspases: Structure, activation, substrates, and functions during apoptosis (1999) Annu. Rev. Biochem., 68, pp. 383-424; Eléouët, J.-F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Eleouet, J.-F., Chilmonczyk, S., Besnardeau, L., Laude, H., Transmissible gastroenteritis coronavirus induces programmed cell death in infected cells through a caspase-dependent pathway (1998) J. Virol., 72, pp. 4918-4924; Enjuanes, L., Van Der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, pp. 337-364. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Erhardt, P., Tomaselli, K.J., Cooper, G.M., Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases (1997) J. Biol. Chem., 272, pp. 15049-15052; Galvan, V., Brandimarti, R., Roizman, B., Herpes simplex virus 1 blocks caspase-3-independent and caspase-dependent pathways to cell death (1999) J. Virol., 73, pp. 3219-3226; Garwes, D.J., Bountiff, L., Millson, G.C., Elleman, C.J., Defective replication of porcine transmissible gastroenteritis virus in a continuous cell line (1984) Adv. Exp. Med. Biol., 178, pp. 79-93; Kluck, R.M., Bossy-Wetzel, E., Green, D.R., Newmeyer, D.D., The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis (1997) Science, 275, pp. 1132-1136; LaCasse, E.C., Baird, S., Korneluk, R.G., MacKenzie, A.E., The inhibitors of apoptosis (IAPs) and their emerging role in cancer (1998) Oncogene, 17, pp. 3247-3259; Laude, H., Chapsal, J.-M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Laude, H., Masters, P., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-158. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S.M., Ahmad, M., Alnemri, E.S., Wang, X., Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade (1997) Cell, 91, pp. 479-489; Martin, S.J., Green, D.R., Protease activation during apoptosis: Death by a thousand cuts? (1995) Cell, 82, pp. 349-352; Martin, S.J., Amarante-Mendes, G.P., Shi, L., Chuang, T.H., Casiano, C.A., O'Brien, G.A., Fitzgerald, P., Green, D.R., The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism (1996) EMBO J., 15, pp. 2407-2416; McFadden, G., Barry, M., How poxviruses oppose apoptosis (1998) Semin. Virol., 8, pp. 429-442; Miller, L.K., White, E., Apoptosis in virus infection (1998) Semin. Virol., 8, pp. 443-444; Miller, L.K., Kaiser, W.J., Seshagiri, S., Baculovirus regulation of apoptosis (1998) Semin. Virol., 8, pp. 445-452; Na, S., Chuang, T.H., Cunningham, A., Turi, T.G., Hanke, J.H., Bokoch, G.M., Danley, D.E., D4-GDI, a substrate of CPP32, is proteolyzed during Fas-induced apoptosis (1996) J. Biol. Chem., 271, pp. 11209-11213; Nicholson, D.W., Thornberry, N.A., Caspases: Killer proteases (1997) Trends Biochem. Sci., 22, pp. 299-306; Piron, M., Vende, P., Cohen, J., Poncet, D., Rotavirus RNA-binding protein NSP3 interacts with elF4GI and evicts the poly(A) binding protein from eIF4F (1998) EMBO J., 17, pp. 5811-5821; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochimie, 69, pp. 591-600; Robbins, S.G., Frana, M.F., McGowan, J.J., Boyle, J.F., Holmes, K.V., RNA-binding proteins of coronavirus MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay (1986) Virology, 150, pp. 402-410; Roulston, A., Marcellus, R.C., Branton, P.E., Viruses and apoptosis (1999) Annu. Rev. Microbiol., 53, pp. 577-628; Salvesen, G.S., Dixit, V.M., Caspases: Intracellular signaling by proteolysis (1997) Cell, 91, pp. 443-446; Siddell, S.G., The coronaviridae: An introduction (1995) The Coronaviridae, p. 1. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Sirinarumitr, T., Kluge, J.P., Paul, P.S., Transmissible gastroenteritis virus induced apoptosis in swine testes cell cultures (1998) Arch. Virol., 143, pp. 2471-2485; Slee, E.A., Harte, M.T., Kluck, R.M., Wolf, B.B., Casiano, C.A., Newmeyer, D.D., Wang, H.G., Martin, S.J., Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner (1999) J. Cell Biol., 144, pp. 281-292; Slee, E.A., Adrain, C., Martin, S.J., Serial killers: Ordering caspase activation events in apoptosis (1999) Cell Death Differ., 6, pp. 1067-1074; Sol, N., Le Junter, J., Vassias, I., Freyssinier, J.M., Thomas, A., Prigent, A.F., Rudkln, B.B., Morinet, F., Possible interactions between the NS-1 protein and tumor necrosis factor alpha pathways in erythroid cell apoptosis induced by human parvovirus B19 (1999) J. Virol., 73, pp. 8762-8770; Sordet, O., Bettaieb, A., Bruey, J.M., Eymin, B., Droin, N., Ivarsson, M., Garrido, C., Solary, E., Selective inhibition of apoptosis by TPA-induced differentiation of U937 leukemic cells (1999) Cell Death Differ., 6, pp. 351-361; Stennicke, H.R., Salvesen, G.S., Biochemical characteristics of caspases-3, -6, -7, and -8 (1997) J. Biol. Chem., 272, pp. 25719-25723; Tepper, C.G., Seldin, M.F., Modulation of caspase-8 and FLICE-inhibitory protein expression as a potential mechanism of Epstein-Barr virus tumorigenesis in Burkitt's lymphoma (1999) Blood, 94, pp. 1727-1737; Thornberry, N.A., Lazebnik, Y., Caspases: Enemies within (1998) Science, 281, pp. 1312-1316; Trapani, J.A., Jans, D.A., Jans, P.J., Smyth, M.J., Browne, K.A., Sutton, V.R., Efficient nuclear targeting of granzyme B and the nuclear consequences of apoptosis induced by granzyme B and perforin are caspase-dependent, but cell death is caspase-independent (1998) J. Biol. Chem., 273, pp. 27934-27938; Villa, P., Kaufmann, S.H., Earnshaw, W.C., Caspases and caspase inhibitors (1997) Trends Biochem. Sci., 22, pp. 388-393; Yang, J., Liu, X., Bhalla, K., Kim, C.N., Ibrado, A.M., Cai, J., Peng, T.I., Wang, X., Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked (1997) Science, 275, pp. 1129-1132; Zhirnov, O.P., Konakova, T.E., Garten, W., Klenk, H.-D., Caspase-dependent N-terminal cleavage of influenza virus nucleocapsid protein in infected cells (1999) J. Virol., 73, pp. 10158-10163","Eleouet, J.-F.; INRA, Unite de Virol./Immunologie Molec., 78352 Jouy-en-Josas Cedex, France; email: eleouet@biotec.jouy.inra.fr",,,0022538X,,JOVIA,"10756009","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0342313707
"Corse E., Machamer C.E.","36957600500;7004585797;","Infectious bronchitis virus E protein is targeted to the Golgi complex and directs release of virus-like particles",2000,"Journal of Virology","74","9",,"4319","4326",,130,"10.1128/JVI.74.9.4319-4326.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033998035&doi=10.1128%2fJVI.74.9.4319-4326.2000&partnerID=40&md5=d6e0cc5ca475c143f16a221816c59cc1","Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, Baltimore, MD 21205, United States; Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","Corse, E., Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, Baltimore, MD 21205, United States; Machamer, C.E., Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, Baltimore, MD 21205, United States, Dept. of Cell Biology and Anatomy, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","The coronavirus E protein is a poorly characterized small envelope protein present in low levels in virions. We are interested in the role of E in the intracellular targeting of infectious bronchitis virus (IBV) membrane proteins. We generated a cDNA clone of IBV E and antibodies to the E protein to study its cell biological properties in the absence of virus infection. We show that IBV E is an integral membrane protein when expressed in cells from cDNA. Epitope-specific antibodies revealed that the C terminus of IBV E is cytoplasmic and the N terminus is translocated. The short luminal N terminus of IBV E contains a consensus site for N-linked glycosylation, but the site is not used. When expressed using recombinant vaccinia virus, the IBV E protein is released from cells at low levels in sedimentable particles that have a density similar to that of coronavirus virions. The IBV M protein is incorporated into these particles when present. Indirect immunofluorescence microscopy showed that E is localized to the Golgi complex in cells transiently expressing IBV E. When coexpressed with IBV M, both from cDNA and in IBV infection, the two proteins are colocalized in Golgi membranes, near the coronavirus budding site. Thus, even though IBV E is present at low levels in virions, it is apparently expressed at high levels in infected cells near the site of virus assembly.",,"complementary DNA; virus protein; animal cell; article; Avian infectious bronchitis virus; Coronavirus; cytology; glycosylation; Golgi complex; human; human cell; immunofluorescence microscopy; nonhuman; priority journal; protein analysis; protein expression; protein localization; protein secretion; protein targeting; Vaccinia virus; virus; virus assembly; virus particle; Animals; Biological Transport; Cell Line; Cell Membrane; Cercopithecus aethiops; Cricetinae; Golgi Apparatus; Hela Cells; Humans; Infectious bronchitis virus; Protein Processing, Post-Translational; Transfection; Vaccinia virus; Vero Cells; Viral Envelope Proteins; Viral Matrix Proteins; Virion; Virus Assembly","Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; An, S., Chen, C.J., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Bos, E.C.W., Luytjes, W., Van Der Meulen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Bock, J.B., Klumperman, J., Davanger, S., Scheller, R.H., Syntaxin 6 functions in trans-golgi network vesicle trafficking (1997) Mol. Biol. Cell, 8, pp. 1261-1271; De Groot, R.J., Van Leen, R.W., Dalderup, M.J.M., Vennema, H., Horzinek, M.C., Spaan, W.J.M., Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice (1989) Virology, 171, pp. 493-502; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. 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Chem., 268, pp. 5768-5801; Pinto, L.H., Holsinger, L.J., Lamb, R.A., Influenza virus M2 protein has ion channel activity (1992) Cell, 69, pp. 517-528; Plutner, H., Davidson, H.W., Saraste, J., Balch, W.E., Morphological analysis of protein transport from the ER to the Golgi membranes in digitonin-permeabilized cells: Role of the p58 containing compartment (1992) J. Cell Biol., 119, pp. 1097-1116; Smith, A.R., Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Inglis, S.C., Identification of a new membrane-associated polypeptide specified by the coronavirus infectious bronchitis virus (1990) J. Gen. Virol., 71, pp. 3-11; Stern, D.F., Sefton, B.M., Coronavirus proteins: Structure and function of the oligosaccharides of the avian infectious bronchitis virus (1982) J. Virol., 44, pp. 804-812; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. 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Virol., 64, pp. 339-346; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Von Heijne, G.A., Gavel, Y., Topogenic signals in integral membrane proteins (1988) Eur. J. Biochem., 174, pp. 671-678; Weisz, O.A., Machamer, C.E., Use of recombinant vaccinia virus vectors for cell biology (1994) Methods Cell Biol., 43, pp. 137-159; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zebedee, S.L., Lamb, R.A., Influenza a virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions (1988) J. Virol., 62, pp. 2762-2772; Zebedee, S.L., Lamb, R.A., Growth restriction of influenza A virus by M2 protein antibody is genetically linked to the M1 protein (1989) Proc. Natl. Acad. Sci. USA, 84, pp. 1061-1065; Zebedee, S.L., Richardson, C.D., Lamb, R.A., Characterization of the influenza virus M2 integral membrane protein and expression at the infected-cell surface from cloned cDNA (1985) J. Virol., 56, pp. 502-511","Machamer, C.E.; Dept. of Cell Biology and Anatomy, Johns Hopkins University, School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States; email: machamer@jhmi.edu",,,0022538X,,JOVIA,"10756047","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033998035
"Almazán F., González J.M., Pénzes Z., Izeta A., Calvo E., Plana-Durán J., Enjuanes L.","6603712040;57201828108;55761804900;6602523425;12801394500;6604038063;7006565392;","Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome",2000,"Proceedings of the National Academy of Sciences of the United States of America","97","10",,"5516","5521",,225,"10.1073/pnas.97.10.5516","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034625066&doi=10.1073%2fpnas.97.10.5516&partnerID=40&md5=10c6bda5fe510525a9c7a8286ba9d733","Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Fort Dodge Veterinaria, 17183 Olot, Spain","Almazán, F., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; González, J.M., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Pénzes, Z., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Calvo, E., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Plana-Durán, J., Fort Dodge Veterinaria, 17183 Olot, Spain; Enjuanes, L., Ctro. Nac. de Biotecnología, Consejo Sup. de Invest. Cie., Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The construction of cDNA clones encoding large-size RNA molecules of biological interest, like coronavirus genomes, which are among the largest mature RNA molecules known to biology, has been hampered by the instability of those cDNAs in bacteria. Herein, we show that the application of two strategies, cloning of the cDNAs into a bacterial artificial chromosome and nuclear expression of RNAs that are typically produced within the cytoplasm, is useful for the engineering of large RNA molecules. A cDNA encoding an infectious coronavirus RNA genome has been cloned as a bacterial artificial chromosome. The rescued coronavirus conserved all of the genetic markers introduced throughout the sequence and showed a standard mRNA pattern and the antigenic characteristics expected for the synthetic virus. The cDNA was transcribed within the nucleus, and the RNA translocated to the cytoplasm. Interestingly, the recovered virus had essentially the same sequence as the original one, and no splicing was observed. The cDNA was derived from an attenuated isolate that replicates exclusively in the respiratory tract of swine. During the engineering of the infectious cDNA, the spike gene of the virus was replaced by the spike gene of an enteric isolate. The synthetic virus replicated abundantly in the enteric tract and was fully virulent, demonstrating that the tropism and virulence of the recovered coronavirus can be modified. This demonstration opens up the possibility of employing this infectious cDNA as a vector for vaccine development in human, porcine, canine, and feline species susceptible to group 1 coronaviruses.",,"article; Coronavirus; molecular cloning; nonhuman; priority journal; RNA virus; virus genome; virus replication; virus virulence; Animals; Cat Diseases; Cats; Cell Line; Cloning, Molecular; Coronavirus; Coronavirus Infections; DNA, Complementary; Dog Diseases; Dogs; Escherichia coli; Genetic Engineering; Genome, Viral; Humans; Male; Molecular Sequence Data; RNA, Viral; Swine; Testis; Transmissible gastroenteritis virus; Viral Vaccines; Bacteria (microorganisms); Coronavirus; Felidae; RNA viruses; Suidae; Sus scrofa","Eniuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Spaan, W.J.M., (1999) Virus Taxonomy, pp. 835-849. , eds. van Regenmortel, M. H. V., Fauquet, C. M., Bishop, D. H. L., Carsten, E. B., Estes, M. K., Lemon, S. M., Mayo, M. A., McGeoch, D. J., Pringle, C. R. & Wickner, R. B. (Academic, New York); Lai, M.M.C., Cavanagh, D., (1997) Adv. Virus Res., 48, pp. 1-100; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., (1992) J. Virol., 66, pp. 1841-1848; Van Der Most, R.G., Heijnen, L., Spaan, W.J.M., Degroot, R.J., (1992) Nucleic Acids Res., 20, pp. 3375-3381; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., (1994) J. Virol., 68, pp. 328-337; Masters, P.S., (1999) Adv. Virus Res., 53, pp. 245-264; Rice, C.M., Grakoui, A., Galler, R., Chambers, T.J., (1989) New Biol., 1, pp. 285-296; Racaniello, V.R., Baltimore, D., (1981) Science, 214, pp. 916-919; Ahlquist, P., French, R., Janda, M., Loesch-Fries, L.S., (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 7066-7070; Rice, C.M., Levis, R., Strauss, J.H., Huang, H.V., (1987) J. Virol., 61, pp. 3809-3819; Lilieström, P., Garoff, H., (1991) Biotechnology, 9, pp. 1356-1361; Satyanarayana, T., Gowda, S., Boyko, V.P., Albiach-Marti, M.R., Mawassi, M., Navas-Castillo, J., Karasev, A.V., Lewandowski, D.J., (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 7433-7438; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Schnell, M.J., Mebatsion, T., Conzelmann, K.-K., (1994) EMBO J., 13, pp. 4195-4203; Fodor, E., Devenish, L., Engelhardt, O.G., Palese, P., Brownlee, G.G., García-Sastre, A., (1999) J. Virol., 73, pp. 9679-9682; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., (1996) Virology, 217, pp. 495-507; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., (1999) J. Virol., 73, pp. 1535-1545; Shizuya, H., Birren, B., Kim, U.J., Mancino, V., Slepak, T., Tachiiri, Y., Simon, M., (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 8794-8797; Messerle, M., Crnkovic, I., Hammerschmidt, W., Ziegler, H., Koszinowski, U.H., (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 14759-14763; Enjuanes, L., Van Der Zeijst, B.A.M., (1995) The Coronaviridae, pp. 337-376. , ed. Siddell, S. G. (Plenum, New York); Enjuanes, L., Siddell, S.G., Spaan, W.J., (1998) Coronaviruses and Arteriviruses, , Plenum, New York; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., (1999) J. Virol., 73, pp. 7607-7618; McClurkin, A.W., Norman, J.O., (1966) Can. J. Comp. Med. Vet. Sci., 30, pp. 190-198; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Escribano, J.M., (1990) Virology, 174, pp. 410-417; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., (1992) Virology, 190, pp. 92-105; Wang, K., Boysen, C., Shizuya, H., Simon, M.I., Hood, L., (1997) BioTechniques, 23, pp. 992-994; Kim, U.-J., Shizuya, H., De Jong, P., Birren, B.W., Simon, M.I., (1992) Nucleic Acids Res., 20, pp. 1083-1085; Solovyev, V.V., Salamov, A.A., Lawrence, C.B., (1994) Nucleic Acids Res., 22, pp. 5156-5163; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, , (Cold Spring Harbor Lab. Press, Plainview, NY), 2nd Ed; Sachs, D., Leight, G., Cone, J., Schwarz, S., Stuart, L., Rosemberg, S., (1976) Transplantation, 22, pp. 559-567; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., (1991) Virology, 183, pp. 225-238; Dubensky, T.W., Driver, D.A., Polo, J.M., Belli, B.A., Latham, E.M., Ibanez, C.E., Chada, S., Mento, S.J., (1996) J. Virol., 70, pp. 508-519; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., (1995) Virology, 206, pp. 817-822; Domingo, E., Holland, J.J., (1997) Annu. Rev. Microbiol., 51, pp. 151-178; Ballesteros, M.L., Sánchez, C.M., Enjuanes, L., (1997) Virology, 227, pp. 378-388","Enjuanes, L.; Centro Nacional de Biotecnologia, Consejo Sup. Investig. Cientificas, Dept. of Molecular and Cell Biology, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,00278424,,PNASA,"10805807","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0034625066
"Storz J., Purdy C.W., Lin X., Burrell M., Truax R.E., Briggs R.E., Frank G.H., Loan R.W.","7006694594;7004943441;36768282000;7006801008;6701356128;57209681724;7401891089;7004131337;","Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp from cattle involved in two natural outbreaks of shipping fever",2000,"Journal of the American Veterinary Medical Association","216","10",,"1599","1604",,66,"10.2460/javma.2000.216.1599","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034656698&doi=10.2460%2fjavma.2000.216.1599&partnerID=40&md5=d4aa37e184d34bcfe86d4a6c6fdbe6b5","Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Conserv. and Prod. Res. Laboratory, USDA, ARS, Bushland, TX 79012, United States; National Animal Disease Center, USDA, ARS, Ames, IA 50010, United States; Dept. of Veterinary Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States","Storz, J., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Purdy, C.W., Conserv. and Prod. Res. Laboratory, USDA, ARS, Bushland, TX 79012, United States; Lin, X., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Burrell, M., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Truax, R.E., Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Briggs, R.E., National Animal Disease Center, USDA, ARS, Ames, IA 50010, United States; Frank, G.H., National Animal Disease Center, USDA, ARS, Ames, IA 50010, United States; Loan, R.W., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, Texas A and M University, College Station, TX 77843, United States","Objective - To identify cytocidal viruses and Pasteurella spp that could be isolated from cattle involved in 2 natural outbreaks of shipping fever. Animals - 105 and 120 castrated male 4- to 8-month-old feedlot cattle involved in 1997 and 1998 outbreaks, respectively. Procedures - Nasal swab specimens and blood samples were collected, and cattle were vaccinated on arrival at an order-buyer barn from 4 local auction houses. Four days later, they were transported to a feedlot, and additional nasal swab specimens and blood samples were collected. Nasal swab specimens were submitted for virus isolation and bacterial culture; blood samples were submitted for measurement of respiratory bovine coronavirus (RBCV) hemagglutinin inhibition titers. Results - 93 of 105 cattle and 106 of 120 cattle developed signs of respiratory tract disease during 1997 and 1998, respectively, and RBCV was isolated from 81 and 89 sick cattle, respectively, while at the order-buyer's barn or the day after arrival at the feedlot. During the 1997 outbreak, bovine herpesvirus 1 was isolated from 2 cattle at the order-buyer's barn and from 5 cattle 7 and 14 days after arrival at the feedlot, and parainfluenza virus 3 was isolated from 4 cattle 14 days after arrival at the feedlot. During the 1998 outbreak, bovine herpesvirus 1 was isolated from 2 cattle at the order-buyer's barn and on arrival at the feedlot and from 5 cattle 7 and 14 days after arrival at the feedlot, and parainfluenza virus 3 was isolated from 1 animal the day of, and from 18 cattle 7 and 14 days after, arrival at the feedlot. Pasteurella spp was cultured from 4 and 6 cattle at the order-buyer's barn and from 92 and 72 cattle on arrival at the feedlot during the 1997 and 1998 outbreaks, respectively. Conclusions and Clinical Relevance - Results suggest that RBCV may play a causative role in outbreaks of shipping fever in cattle. More than 80% of the sick cattle shed RBCV at the beginning of 2 outbreaks when the Pasteurella spp infection rate was low.",,"Animalia; Bacteria (microorganisms); Bos taurus; Bovinae; Bovine coronavirus; Bovine herpesvirus 1; Coronavirus; Herpesviridae; herpesvirus 1; Human parainfluenza virus 3; Pasteurella; virus antibody; animal; animal disease; article; blood; cattle; cattle disease; Coronavirus; epidemic; female; hemagglutination inhibition test; Infectious bovine rhinotracheitis virus; isolation and purification; male; Mannheimia haemolytica; nose cavity; Pasteurella multocida; pathogenicity; serodiagnosis; virology; virus infection; Animals; Antibodies, Viral; Cattle; Coronavirus Infections; Coronavirus, Bovine; Disease Outbreaks; Female; Hemagglutination Inhibition Tests; Herpesvirus 1, Bovine; Male; Mannheimia haemolytica; Nasal Cavity; Neutralization Tests; Pasteurella multocida; Pasteurellosis, Pneumonic","Hoerlein, A.B., Shipping fever (1980) Bovine Medicine and Surgery, pp. 99-106. , Amstutz HE, ed. Santa Barbara, Calif: American Veterinary Publications Inc; Yates, W.D.G., A review of infectious bovine rhinotracheitis, shipping fever pneumonia and viral-bacterial synergism in respiratory disease of cattle (1982) Can J Comp Med, 46, pp. 225-263; McKercher, D.G., Moulton, J.E., Madin, S.H., Infectious bovine rhinotracheitis - A newly recognized virus disease of cattle (1957) Am J Vet Res, 18, pp. 246-256; Reisinger, R.C., Heddleston, K.L., Manthei, C.A., A myxovirus (SF-4) associated with shipping fever of cattle (1959) J Am Vet Med Assoc, 135, pp. 147-154; Baldwin, D.A., Marshall, R.G., Wessman, G.E., Experimental infection of calves with myxovirus parainfluenza-3 and Pasteurella haemolylica (1967) Am J Vet Res, 28, pp. 1773-1782; Rosenquist, B.D., Isolation of respiratory syncytial virus from calves with acute respiratory disease (1974) J Infect Dis, 130, pp. 177-182; Potgieter, L.N.D., McCracken, M.D., Hopkins, F.M., Experimental production of bovine respiratory tract disease with bovine viral diarrhea virus (1984) Am J Vet Res, 45, pp. 1582-1585; Jensen, R., Pierson, R.E., Braddy, P.M., Shipping fever pneumonia in yearling feedlot cattle (1976) J Am Vet Med Assoc, 169, pp. 500-506; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples of cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1456; Storz, J., Respiratory disease of cattle associated with coronavirus infections (1998) Current Veterinary Therapy: Food Animal Practice 4, pp. 291-293. , Howard JL, Smith RA, ed. Philadelphia: WB Saunders Co; Loan, R.W., Purdy, C.W., Tigges, M.G., A tissue culture-derived Pasteurella haemolytica vaccine (1988) 15th World Cong Dis Cattle, pp. 165-170. , Proceedings; Lin, X.Q., O'Reilly, K.L., Storz, J., Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny (1997) Am J Vet Res, 58, pp. 1120-1124; Tompkins, W.A.T., Watrach, A.M., Schmale, J.D., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J Natl Cancer Inst, 52, pp. 904-911; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglulinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Weaver, R.W., Hollis, D.G., Gram-negative bacteria and Francisella tularensis (1980) Manual of Clinical Microbiology. 3rd Ed., pp. 242-262. , Lennette H, Balows A, Hausler WJ, et al, eds. 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Philadelphia: WB Saunders Co; Storz, J., Lin, X.Q., Purdy, C.W., Novel diagnostics for defining virus infections in shipping fever pneumonia: Emergence of respiratory bovine coronaviruses (1999) IX Intern Symp World Assoc Vet Lab Diagnosticians, pp. 54-60. , Proceedings","Storz, J.; Dept. Vet. Microbiol. and Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",,"American Veterinary Medical Association",00031488,,JAVMA,"10825949","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0034656698
"Yu M.W.N., Scott J.K., Fournier A., Talbot P.J.","16940438900;57206879375;7401993674;7102670281;","Characterization of murine coronavirus neutralization epitopes with phage-displayed peptides",2000,"Virology","271","1",,"182","196",,26,"10.1006/viro.2000.0310","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034713350&doi=10.1006%2fviro.2000.0310&partnerID=40&md5=a8b4157fc68bd7d3ee1eda43e712c498","Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada; Inst. of Molec. Biol. and Biochem., Simon Fraser University, Burnaby, BC V5A 1S6, Canada","Yu, M.W.N., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada; Scott, J.K., Inst. of Molec. Biol. and Biochem., Simon Fraser University, Burnaby, BC V5A 1S6, Canada; Fournier, A., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, Que. H7V 1B7, Canada","Phage-displayed peptide libraries were used to map immunologically relevant epitopes on the surface (S) glycoprotein of a neurotropic murine coronavirus (MHV-A59). Three in vitro virus-neutralizing and in vivo protective mAbs against either continuous or discontinuous epitopes on the S glycoprotein were used to screen 12 different peptide libraries expressed on the pVIII major coat protein of the fd filamentous bacteriophage. Consensus sequences that matched short sequences within the S glycoprotein were identified. The sequence of a tight-binding, mAb-selected peptide suggested the location of a discontinuous epitope within the N-terminal S1 subunit. Several tightly binding phage were amplified and used directly as immunogens in BALB/c and C57BL/6 mice. Partial protection of C57BL/6 mice against a lethal acute virus infection was achieved with a phage preparation that displayed a linear epitope. Protection correlated with the presence of sufficient levels of specific antiviral antibodies recognizing the same immunodominant domain and 13-mer peptide, located within the C-terminal S2 subunit, as the selecting mAb. Thus, the direct use of phage-displayed peptides to evaluate protective antiviral immune responses complements their use to characterize antibody-binding epitopes. This is the first evaluation of protective immunization induced by mAb-selected phage-displayed peptides.",,"glycoprotein; amino acid sequence; antibody production; article; Coronavirus; immune response; phage display; priority journal; virus neutralization; Animalia; Coronavirus; Filamentous bacteriophage; Murinae; Murine hepatitis virus; RNA viruses","Armitage, P., Berry, G., (1987) Statistical Methods in Medical Research, , Oxford: Blackwell Sci; Bachmann, M.F., Kalinke, U., Althage, A., Freer, G., Burkhart, C., Roost, H.-P., Aguet, M., Zinkernagel, R.M., The role of antibody concentration and avidity in antiviral protection (1997) Science, 276, pp. 2024-2027; Balass, M., Heldman, Y., Cabilly, S., Givol, D., Katchalski-Katzir, E., Fuchs, S., Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library (1993) Proc. Natl. Acad. Sci. 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"Spagnolo J.F., Hogue B.G.","6508353146;7003393593;","Host protein interactions with the 3' end of bovine coronavirus RNA and the requirement of the poly(A) tail for coronavirus defective genome replication",2000,"Journal of Virology","74","11",,"5053","5065",,76,"10.1128/JVI.74.11.5053-5065.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034122512&doi=10.1128%2fJVI.74.11.5053-5065.2000&partnerID=40&md5=f9eb4f952c0f819bc91d13734cdbd936","Dept. Molec. Virol. and Microbiol., Baylor College of Medicine, Houston, TX 77030, United States; Dept. Molec. Virol. and Microbiol., Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","Spagnolo, J.F., Dept. Molec. Virol. and Microbiol., Baylor College of Medicine, Houston, TX 77030, United States; Hogue, B.G., Dept. Molec. Virol. and Microbiol., Baylor College of Medicine, Houston, TX 77030, United States, Dept. Molec. Virol. and Microbiol., Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States","RNA viruses have 5' and 3' untranslated regions (UTRs) that contain specific signals for RNA synthesis. The coronavirus genome is capped at the 5' end and has a 3' UTR that consists of 300 to 500 nucleotides (nt) plus a poly(A) tail. To further our understanding of coronavirus replication, we have begun to examine the involvement of host factors in this process for two group II viruses, bovine coronavirus (BCV) and mouse hepatitis coronavirus (MHV). Specific host protein interactions with the BCV 3' UTR [287 nt plus poly(A) tail] were identified using gel mobility shift assays. Competition with the MHV 3' UTR [301 nt plus poly(A) tail] suggests that the interactions are conserved for the two viruses. Proteins with molecular masses of 99, 95, and 73 kDa were detected in UV cross-linking experiments. Less heavily labeled proteins were also detected in the ranges of 40 to 50 and 30 kDa. The poly(A) tail was required for binding of the 73-kDa protein. Immunoprecipitation of UV-cross-linked proteins identified the 73-kDa protein as the cytoplasmic poly(A)-binding protein (PABP). Replication of the defective genomes BCV Drep and MHV MIDI-C, along with several mutants, was used to determine the importance of the poly(A) tail. Defective genomes with shortened poly(A) tails consisting of 5 or 10 A residues were replicated after transfection into helper virus-infected cells. BCV Drep RNA that lacked a poly(A) tail did not replicate, whereas replication of MHV MIDI-C RNA with a deleted tail was detected after several virus passages. All mutants exhibited delayed kinetics of replication. Detectable extension or addition of the poly(A) tail to the mutants correlated with the appearance of these RNAs in the replication assay. RNAs with shortened poly(A) tails exhibited less in vitro PABP binding, suggesting that decreased interactions with the protein may affect RNA replication. 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"De Haan C.A.M., Vennema H., Rottier P.J.M.","7003682643;7003697291;7006145490;","Assembly of the coronavirus envelope: Homotypic interactions between the M proteins",2000,"Journal of Virology","74","11",,"4967","4978",,80,"10.1128/JVI.74.11.4967-4978.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034067478&doi=10.1128%2fJVI.74.11.4967-4978.2000&partnerID=40&md5=ae5d19103fdf491f1c8861b51b64effb","Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","De Haan, C.A.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Vennema, H., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands","The viral membrane proteins M and E are the minimal requirements for the budding of coronavirus particles. Since the E protein occurs in particles only in trace amounts, the lateral interactions between the M proteins apparently generate the major driving force for envelope formation. By using coimmunoprecipitation and envelope incorporation assays, we provide extensive evidence for the existence of such M-M interactions. In addition, we determined which domains of the M protein are involved in this homotypic association, using a mutagenetic approach. Mutant M proteins which were not able to assemble into viruslike particles (VLPs) by themselves (C. A. M. de Haan, L. Kuo, P. S. Masters, H. Vennema, and P. J. M. Rottier, J. Virol. 72: 6838-6850, 1998) were tested for the ability to associate with other M proteins and to be rescued into VLPs formed by assembly-competent M proteins. We found that M proteins lacking parts of the transmembrane cluster, of the amphipathic domain, or of the hydrophilic carboxy-terminal tail, or M proteins that had their luminal domain replaced by heterologous ectodomains, were still able to associate with assembly-competent M proteins, resulting in their coincorporation into VLPs. Only a mutant M protein in which all three transmembrane domains had been replaced lost this ability. The results indicate that M protein molecules interact with each other through multiple contact sites, particularly at the transmembrane level. Finally, we tested the stringency with which membrane proteins are selected for incorporation into the coronavirus envelope by probing the coassembly of some foreign proteins. The observed efficient exclusion from budding of the vesicular stomatitis virus G protein and the equine arteritis virus M protein indicates that envelope assembly is indeed a highly selective sorting process. 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Virol., 64, pp. 339-346; Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M.C., Spaan, W.J., Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system using encephalomyocarditis virus 5′-untranslated region sequences (1991) Gene, 108, pp. 201-209; Vogel, R.H., Provencher, S.W., Von Bonsdorff, C.H., Adrian, M., Dubochet, J., Envelope structure of Semliki Forest virus reconstructed from cryo-electron micrographs (1986) Nature, 320, pp. 533-535; Yoshikura, H., Taguchi, F., Mouse hepatitis virus strain MHV-S: Formation of pseudotypes with a murine leukemia virus envelope (1978) Intervirology, 10, pp. 132-136","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508 TD Utrecht, Netherlands; email: P.Rottier@vet.uu.nl",,,0022538X,,JOVIA,"10799570","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034067478
"Ng L.F.P., Liu D.X.","7201477950;57214391633;","Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site",2000,"Virology","272","1",,"27","39",,36,"10.1006/viro.2000.0330","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034691067&doi=10.1006%2fviro.2000.0330&partnerID=40&md5=5d8f0ea01ba07478655fc309ada30062","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Ng, L.F.P., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Coronavirus infectious bronchitis virus (IBV) encodes a trypsin-like proteinase (3C-like proteinase) by ORF 1a, which has been demonstrated to play a pivotal role in proteolytic processing of gene 1-encoded polyproteins. In our previous studies, the proteinase was identified as a 33-kDa protein in IBV-infected cells, and its catalytic center was shown to consist of H2820 and C2922 residues. It is released from the 1a and 1a/1b polyproteins by autoprocessing at two Q-S dipeptide bonds (Q2779- S2780 and Q3086-S3087). In this report, further characterization of the two cleavage sites demonstrates that the N-terminal Q2779- S2780 site is tolerant to mutations at the P1 position. Deletion of the C-terminal region of the proteinase shows that a significant amount of the enzymatic activity is maintained upon deletion of up to 67 amino acids, suggesting that the extreme C-terminal region may be dispensable for the proteolytic activity of the proteinase. Analysis of the autoprocessing kinetics in vitro reveals that proteolysis at the Q2779-S2780 site is the first cleavage event mediated by this proteinase. This is followed by cleavage at the Q3086-S3087 site. The occurrence of both cleavage events in intact cells is potentially rapid and efficient, as no intermediate cleavage products covering the proteinase were detected in either IBV- infected or transfected cells. Immunofluorescence microscopy and subcellular fractionation studies further show differential subcellular localization of the proteinase in IBV-infected cells and in cells expressing the 3C-like proteinase alone, indicating that additional roles in viral replication might be played by this protein. Finally, a Q-A (Q3379-A3380) dipeptide bond encoded by nucleotides 10, 663 to 10, 668 was demonstrated to be a cleavage site of the proteinase. (C) 2000 Academic Press.",,"proteinase; amino terminal sequence; animal cell; article; Avian infectious bronchitis virus; carboxy terminal sequence; cellular distribution; enzyme active site; immunofluorescence microscopy; nonhuman; priority journal; Vero cell; virus replication; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; RNA viruses","Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA (1993) EMBO J., 12, pp. 3587-3598; Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 64, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlise, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus (1993) J. 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Virol., 72, pp. 6689-6698; Van Der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Locker, J.K., Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73, pp. 7641-7657; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185",,,,00426822,,,"10873746","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0034691067
"Sims A.C., Ostermann J., Denison M.R.","7102763252;57210681069;7101971810;","Mouse hepatitis virus replicase proteins associate with two distinct populations of intracellular membranes",2000,"Journal of Virology","74","12",,"5647","5654",,53,"10.1128/JVI.74.12.5647-5654.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034093020&doi=10.1128%2fJVI.74.12.5647-5654.2000&partnerID=40&md5=1b9843a64784c8f2478c50f7090f3f2a","Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States; Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University, Nashville, TN 37232, United States; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, United States; EMBL, 69012 Heidelberg, Germany; Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States","Sims, A.C., Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States, Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University, Nashville, TN 37232, United States; Ostermann, J., Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, United States, Department of Pediatrics, Vanderbilt University Medical Center, D7235 MCN, Nashville, TN 37232-2581, United States; Denison, M.R., Dept. of Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, United States, Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University, Nashville, TN 37232, United States, EMBL, 69012 Heidelberg, Germany","The coronavirus replicase gene (gene 1) is translated into two co-amino- terminal polyproteins that are proteolytically processed to yield more than 15 mature proteins. Several gene 1 proteins have been shown to localize at sites of viral RNA synthesis in the infected cell cytoplasm, notably on late endosomes at early times of infection. However, both immunofluorescence and electron microscopic studies have also dejected gene 1 proteins at sites distinct from the putative sites of viral RNA synthesis or virus assembly. In this study, mouse hepatitis virus (MHV)-infected cells were fractionated and analyzed to determine if gene 1 proteins segregated to more than one membrane population. Following differential centrifugation of lysates of MHV-infected DBT cells, gene 1 proteins as well as the structural N and M proteins were detected almost exclusively in a high-speed small membrane pellet. Following fractionation of the small membrane pellet on an iodixanol density gradient, the gene 1 proteins p28 and helicase cofractionated with dense membranes (1.12 to 1.13 g/ml) that also contained peak concentrations of N. In contrast, p65 and p1a-22 were detected in a distinct population of less dense membranes (1.05 to 1.09 g/ml). Viral RNA was detected in membrane fractions containing helicase, p28, and N but not in the fractions containing p65 and p1a-22. LAMP-1, a marker for late endosomes and lysosomes, was detected in both membrane populations. These results demonstrate that multiple gene 1 proteins segregate into two biochemically distinct but tightly associated membrane populations and that only one of these populations appears to be a site for viral RNA synthesis. The results further suggest that p28 is a component of the viral replication complex whereas the gene 1 proteins p1a-22 and p65 may serve roles during infection that are distinct from viral RNA transcription or replication.",,"RNA directed RNA polymerase; animal cell; article; cell fractionation; concentration response; intracellular membrane; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; RNA transcription; virus replication; Animals; Antigens, CD; Cell Fractionation; Cell Line; Centrifugation, Density Gradient; DNA Helicases; Endoplasmic Reticulum; Endosomes; Fluorescent Antibody Technique; Golgi Apparatus; Intracellular Membranes; Lysosome-Associated Membrane Glycoproteins; Lysosomes; Membrane Glycoproteins; Mice; Microscopy, Confocal; Molecular Weight; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; RNA Replicase; RNA, Viral; Triiodobenzoic Acids; Viral Matrix Proteins; Viral Proteins","Anderson, R., Wong, F., Membrane and phospholipid binding by murine coronaviral nucleocapsid N protein (1993) Virology, 194, pp. 224-232; Balch, W.E., Dunphy, W.G., Braell, W.A., Rothman, J.E., Reconstitution of the transport of proteins between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine (1984) Cell, 39, pp. 405-416; Balch, W.E., Rothman, J.E., Characterization of protein transport between successive compartments of the Golgi apparatus: Asymmetric properties of donor and acceptor activities in a cell-free system (1985) Arch. 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"Andréoletti L., Lesay M., Deschildre A., Lambert V., Dewilde A., Wattré P.","7003617204;57199356828;7004402827;36839007000;7004613991;7007037464;","Differential detection of rhinoviruses and enteroviruses RNA sequences associated with classical immunofluorescence assay detection of respiratory virus antigens in nasopharyngeal swabs from infants with bronchiolitis",2000,"Journal of Medical Virology","61","3",,"341","346",,57,"10.1002/1096-9071(200007)61:3<341::AID-JMV10>3.0.CO;2-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034123488&doi=10.1002%2f1096-9071%28200007%2961%3a3%3c341%3a%3aAID-JMV10%3e3.0.CO%3b2-0&partnerID=40&md5=7473791228313e642e6e0a27c59325fe","Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France; Service de Pédiatrie, Hâpital Jeanne de Flandes, CHRU de Lille, Lille, France; Laboratoire de Virologie, Bâtiment IRFPPS, Ctr. Hosp. Regl. Universitaire, 59037 Lille Cedex, France","Andréoletti, L., Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France, Laboratoire de Virologie, Bâtiment IRFPPS, Ctr. Hosp. Regl. Universitaire, 59037 Lille Cedex, France; Lesay, M., Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France; Deschildre, A., Service de Pédiatrie, Hâpital Jeanne de Flandes, CHRU de Lille, Lille, France; Lambert, V., Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France; Dewilde, A., Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France; Wattré, P., Laboratoire de Virologie CHRU, Bâtiment IRFPPS, Lille, France","To define the role of enteroviruses and human rhinoviruses as etiological agents in childhood bronchiolitis, clinical aspirates from 84 infants admitted to hospital with symptoms of obstructive bronchiolitis were tested by picornavirus RT-PCR assay, adenovirus PCR assay and classical immunofluorescence antigen detection of common respiratory viral agents. Respiratory syncytial viruses (A and B) were detectable in 45 of 84 (53.6%) nasopharyngeal aspirates from infants with bronchiolitis, whereas coronaviruses, influenza viruses, and parainfluenza viruses were not detectable in the same samples. Adenoviruses were detectable by PCR in 11 of 84 (13.1%) nasopharyngeal swabs. By using a picornavirus RT-PCR assay followed by a differential molecular hybridisation, rhinovirus and enterovirus RNA sequences were detected in 16 of 84 (19%) and in 10 of 84 (11.9%) of the nasopharyngeal swabs tested. Positive human rhinovirus or enterovirus RT-PCR assay, however, was the only evidence of respiratory infection in 8 of 84 (9.5%) and in 7 of 84 (8.33%) of the studied patients. Respiratory syncytial viruses, human rhinoviruses, adenoviruses, and enteroviruses occur in dual infections detected in 18 of 84 (21.4%) respiratory samples tested. The median duration of stay in hospital was not significantly different between the patients demonstrating a single viral infection and those with a dual viral infection (6.22 ± 2.07 vs. 5.04 ± 0.95 days; P > 0,05). In summary, combination of molecular and classical detection assays of common viruses can be used to demonstrate enterovirus and human rhinovirus respiratory infection in childhood bronchiolitis, and provides an improved approach to obtain new insights into concomitant viral respiratory tract infection in infants. (C) 2000 Wiley-Liss, Inc.","Bronchiolitis; Differential hybridisation; Enteroviruses; Human rhinoviruses; Lower respiratory tract infection; Picornavirus; Respiratory viruses; RT-PCR","article; bronchiolitis; Enterovirus; female; human; immunofluorescence; infant; major clinical study; male; nonhuman; respiratory tract infection; reverse transcription polymerase chain reaction; Rhinovirus; RNA sequence; sequence analysis; throat culture; virus detection; Antigens, Viral; Bronchiolitis; Enterovirus; Enterovirus Infections; Female; Fluorescent Antibody Technique; Humans; Infant; Male; Nasopharynx; Nucleic Acid Hybridization; Picornaviridae Infections; Reverse Transcriptase Polymerase Chain Reaction; Rhinovirus; RNA, Viral; Sequence Analysis, DNA; Adenoviridae; Enterovirus; Human rhinovirus sp.; Influenza virus; Pneumovirus; Rhinovirus; RNA viruses; Syncytial virus","Andeweg, A.C., Bestebroer, T.M., Huybreghs, M., Kimman, T.G., De Jong, J.C., Improved detection of rhinoviruses in clinical samples by using a newly developed nested reverse transcription-PCR assay (1999) J Clin Microbiol, 37, pp. 524-530; 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Portnoy, B., Eckert, H.L., Salvatore, M.A., Rhinovirus infection in children with acute longer respiratory disease: Evidence against etiological importance (1965) Pediatrics, 35, pp. 899-905; Santti, J., Hyypia, T., Halonen, P., Comparison of PCR primer pairs in the detection of human rhinoviruses in nasopharyngeal aspirates (1997) J Virol Meth, 66, pp. 139-147; Waner, J.L., Mixed viral infections: Detection and management (1994) Clin Microbiol Rev, 7, pp. 143-151","Andreoletti, L.; Laboratoire de Virologie, Batiment IRFPPS, Ctr. Hospitalier Reg. Universitaire, 59037 Lille Cedex, France; email: landreoletti@chru-lille.fr",,,01466615,,JMVID,"10861643","English","J. Med. Virol.",Article,"Final",,Scopus,2-s2.0-0034123488
"Seybert A., Hegyi A., Siddell S.G., Ziebuhr J.","7004923617;6603368848;7005260816;7003783935;","The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity",2000,"RNA","6","7",,"1056","1068",,82,"10.1017/S1355838200000728","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033941814&doi=10.1017%2fS1355838200000728&partnerID=40&md5=30fcd114f8f5679a6863dba4a978033e","Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany; Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","Seybert, A., Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany; Hegyi, A., Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, 97078 Würzburg, Germany, Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","The human coronavirus 229E replicase gene encodes a protein, p66(HEL), that contains a putative zinc finger structure linked to a putative superfamily (SF) 1 helicase. A histidine-tagged form of this protein, HEL, was expressed using baculovirus vectors in insect cells. The purified recombinant protein had in vitro ATPase activity that was strongly stimulated by poly(U), poly(dT), poly(C), and poly(dA), but not by poly(G). The recombinant protein also had both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity. The DNA helicase activity of the enzyme preferentially unwound 5'-oligopyrimidine-tailed, partial-duplex substrates and required a tail length of at least 10 nucleotides for effective unwinding. 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"Yoo D., Pei Y., Christie N., Cooper M.","7103242554;7202306693;57197647856;7404410584;","Primary structure of the sialodacryoadenitis virus genome: Sequence of the structural-protein region and its application for differential diagnosis",2000,"Clinical and Diagnostic Laboratory Immunology","7","4",,"568","573",,8,"10.1128/CDLI.7.4.568-573.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033910862&doi=10.1128%2fCDLI.7.4.568-573.2000&partnerID=40&md5=f2be8572975f9a1329aef04099838d1f","Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Dept. of Lab. Med. and Pathobiology, Faculty of Medicine, University of Toronto, Toronto, Ont., Canada","Yoo, D., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Pei, Y., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Christie, N., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Cooper, M., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada, Dept. of Lab. Med. and Pathobiology, Faculty of Medicine, University of Toronto, Toronto, Ont., Canada","Sialodacryoadenitis virus (SDAV) is a coronavirus that is commonly found in laboratory rats and that causes sialodacryoadenitis and respiratory illness. We cloned and sequenced the 3' terminal 9.8 kb of the genomic RNA and analyzed the structure of the viral genome. As with mouse hepatitis coronaviruses (MHVs), the SDAV genome was able to code for a spike protein, a small membrane protein, a membrane-associated protein, and a nucleocapsid protein. In addition, the hemagglutinin-esterase gene capable of encoding a protein of 439 amino acids (aa) was identified. The putative functional site for acetylesterase activity was present in the HE protein as Phe-Gly-Asp-Ser (FGDS), suggesting that the SDAV HE protein might have retained the esterase activity. Immediately upstream of the HE gene and downstream of the polymerase 1b gene, the NS2 nonstructural-protein gene was identified with a coding capacity of 274 aa. A motif of UCUAAAC was identified as a potential transcription signal for subgenomic mRNA synthesis. Large insertions of 172, 127, and 44 aa were detected in the N-terminal half of the predicted S protein of SDAV when its sequence was compared to the sequences of MHV 2, MHV JITM, and MHV A59, respectively. The sequence information on the SDAV S- protein gene was applied to a differential diagnostic PCR to detect and distinguish the rat coronavirus from mouse coronaviruses. This is the first report on the comprehensive genetic information of any rat coronavirus.",,"acetylesterase; DNA directed DNA polymerase alpha; amino acid sequence; animal cell; article; Coronavirus; differential diagnosis; enzyme activity; molecular cloning; nonhuman; polymerase chain reaction; priority journal; sialodacryoadenitis virus; virus genome; virus morphology; virus nucleocapsid; Amino Acid Sequence; Animals; Cloning, Molecular; Coronavirus; Genome, Viral; Mice; Molecular Sequence Data; Rats; Sequence Alignment; Sequence Analysis; Sialadenitis","Baker, M.G., Percy, D.H., Hovland, D.J., MacInnes, J.I., Preliminary characterization of the structural proteins of the coronaviruses, sialodacryoadenitis virus and Parkers rat coronavirus (1994) Can J. Vet. Res., 58, pp. 99-103; Bhatt, P.N., Percy, D.H., Jonas, A.M., Characterization of the virus of sialodacryoadenitis of rats: A member of the coronavirus group (1972) J. Infect. 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Anim., 33, pp. 115-120; Nunoya, T., Itabashi, M., Kudow, S., Hayashi, K., Tajima, M., An epizootic outbreak of sialodacryoadenitis in rats (1977) Jpn. J. Vet. Sci., 39, pp. 445-450; Parker, M.D., Yoo, D., Cox, G.J., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) J. Gen. Virol., 71, pp. 263-270; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Percy, D.H., Bond, S., MacInnes, J., Replication of sialodacryoadenitis virus in mouse L-2 cells (1989) Arch. Virol., 104, pp. 323-333; Percy, D.H., Williams, K.L., Paturzo, F.X., A comparison of the sensitivity and specificity of sialodacryoadenitis virus, Parker's rat coronavirus, and mouse hepatitis virus-infected cells as a source of antigen for the detection of antibody to rat coronaviruses (1991) Arch. Virol., 119, pp. 175-180; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Schmidt, I., Skinner, M., Siddell, S.G., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Schwarz, B., Routledge, E., Siddell, S.G., Murine coronavirus nonstructural protein NS2 is not essential for virus replication in transformed cells (1990) J. Virol., 64, pp. 4784-4791; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Tsai, C.W., Chang, S.C., Chang, M.F., A 12-amino acid stretch in the hypervariable region of the spike protein S1 subunit is critical for cell fusion activity of mouse hepatitis virus (1999) J. Biol. Chem., 274, pp. 26085-26090; Utsumi, K., Maeda, T., Tatsumi, H., Fujiwara, K., Some clinical and epizootiological observations of infectious sialodacryoadenitis in rats (1978) Exp. Anim., 27, pp. 283-287; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219; Yokomori, K., Stohlman, S.A., Lai, M.M.C., The detection and characterization of multiple hemagglutinin-esterase (HE)-defective viruses in the mouse brain during subacute dymyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-180; Yoo, D., Parker, M.D., Babiuk, L.A., The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells (1991) Virology, 180, pp. 395-399","Yoo, D.; Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; email: dyoo@ovc.uoguelph.ca",,,1071412X,,CDIME,"10882653","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0033910862
"García A., Ruiz-Santa-Quiteria J.A., Orden J.A., Cid D., Sanz R., Gómez-Bautista M., De La Fuente R.","54406740900;6701468772;6506947568;6701327952;7006843232;6701627325;6507240946;","Rotavirus and concurrent infections with other enteropathogens in neonatal diarrheic dairy calves in Spain",2000,"Comparative Immunology, Microbiology and Infectious Diseases","23","3",,"175","183",,55,"10.1016/S0147-9571(99)00071-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034069132&doi=10.1016%2fS0147-9571%2899%2900071-5&partnerID=40&md5=abdd9bac4e52f47b992ae379f9128afe","Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain","García, A., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; Ruiz-Santa-Quiteria, J.A., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; Orden, J.A., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; Cid, D., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; Sanz, R., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; Gómez-Bautista, M., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain; De La Fuente, R., Depto. Patología Animal I, Fac. Vet., Univ. Complutense, 28040, Madrid, Spain","Faeces samples from 218, one to 30 days old, diarrheic dairy calves in 65 dairy herds were screened for the presence of rotavirus and concurrent infections with coronavirus, Cryptosporidium, F5+ Escherichia coli and Salmonella spp. Calves were grouped according to their age as follows: 1-7, 8-14, 15-21 and 22-30 days. Rotavirus infection was detected in 46.9%, 45.6%, 33.8% and 48.3% of the calves in the respective age-groups. No significant differences in the detection rate of rotavirus were found among calves on the different age-groups. Rotavirus was the only enteropathogen detected in 39 of the 93 (41.9%) diarrheic calves positive to this agent. Concurrent infections with other enteropathogen(s) were detected in 31.3%, 33.3%, 20.6% and 3.4% of the rotavirus infected calves in the age-groups 1-7, 8-14, 15-21 and 22-30 d, respectively. A significant age-associated decrease in the detection rate of mixed infections (p &lt; 0.01) was found. The detection rates of the other enteropathogens considered in calves with rotavirus infection were 20.4% for coronavirus, 85.2% for Cryptosporidium, 16.7% for F5+ E. coli and 1.8% for Salmonella. (C) 2000 Elsevier Science Ltd. All rights reserved.","Coronavirus; Cryptosporidium sp; Escherichia coli; Neonatal calf diarrhea; Rotavirus; Salmonella","age; agriculture; article; cattle; controlled study; Coronavirus; Cryptosporidium; diarrhea; Escherichia coli; feces analysis; newborn; nonhuman; Rotavirus; Salmonella; Spain; superinfection; virus detection; Animals; Animals, Newborn; Cattle; Cattle Diseases; Coronavirus Infections; Cryptosporidiosis; Diarrhea; Enterobacteriaceae Infections; Rotavirus Infections; Spain; Animalia; Bos taurus; Coronavirus; Cryptosporidium; Escherichia coli; Negibacteria; RNA viruses; Rotavirus; Salmonella","Radostits, O.M., Leslie, K.E., Fetrow, J., (1994) Herd Health. Food Animal Production Medicine 2nd Ed., , Philadelphia: W.B. Saunders Co; Waltner-Toews, D., Martin, S.W., Meek, A.H., The effect of early calfhood status on survivorship and age at first calving (1986) Can. J. Vet. 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Rec., 119, pp. 31-34; Zrelli, M., Messadi, L., Ben Miled, L., Jemli, M.H., Haddad, N., Les agents infectieux associés aux diarrhées néonatales du veau en Tunisie (1990) Revue Med. Vet., 141, pp. 861-872; Moore, D.A., Zeman, D.H., Cryptosporidiosis in neonatal calves: 277 cases (1986-1987) (1991) J. Am. Vet. Med. Assoc., 198, pp. 1969-1971; Brenner, J., Elad, D., Markovics, A., Grinberg, A., Trainin, Z., Epidemiological study of neonatal calf diarrhoea in Israel - A one-year survey of faecal samples (1993) Isr. J. Vet. Med., 48, pp. 113-116; Rosati, S., Dondo, A., Guercio, A., Maglione, E., Masoero, L., Rotavirosi bovina in Piamonte: Indagine virologica e sierologica in allevamenti con sindrome enterica in atto (1991) Atti Della Società Italiana di Buiatria, 23, pp. 165-170; Fagan, J.G., Dwyer, P.J., Quinlan, J.G., Factors that may affect the occurrence of enteropathogens in the faeces of diarrhoeic calves in Ireland (1995) Irish Vet. J., 48, pp. 17-21; McDonough, S.P., Stull, C.L., Osburn, B.I., Enteric pathogens in intensively reared veal calves (1994) Am. J. Vet. Res., 55, pp. 1516-1520; V. Otto, P., Elschner, M., Günther, H., Schulze, F., Vergleichende Untersuchungen zum nachweis von Rotaviren, Coronaviren, Kryptosporidien und enterotoxigenen E. coli im Kot durchfallkranker Kälber (1995) Tierarztl Umschau., 50, pp. 80-86; Bellinzoni, R.C., Blackhall, J., Terzolo, H.R., Moreira, A.R., Auza, N., Mattion, N., Micheo, G.L., Scodeller, E.A., Microbiology of diarrhoea in young beef and dairy calves in Argentina (1990) Rev. Argent. Microbiol., 22, pp. 130-137; Garcia-Sanchez, J., Corral, C., Halaihel, N.G., Simon, M.C., Alonso, J.L., Muzquiz, J.L., Ortega, C., Girones, O., Survey of rotavirus infection in a dairy herd: Comparison between polyacrylamide gel electrophoresis and two commercial tests (1993) Vet. Microbiol., 34, pp. 321-332; Solana, A., Gómez-Tejedor, C., Marcotegui, M.A., Castro, J.M., Diarrea de los terneros. Estudio preliminar de la incidencia de rotavirus y coronavirus en españa (1985) Med. Vet., 2, pp. 299-304; Herring, A.J., Inglis, N.F., Ojeh, C.K., Snodgrass, D.R., Menzies, J.D., Rapid diagnosis of rotavirus infection by direct detection of viral nucleic acid in silver-stained polyacrylamide gels (1982) J. Clin. Microbiol., 16, pp. 473-477; Heine, J., Eine einfache Nachweismethode für Krytosporidiosen im Kot (1982) Zbl. Vet. Med. B., 29, pp. 324-327; Casemore, D.P., Armstrong, M., Sands, R.L., Laboratory diagnosis of cryptosporidiosis (1985) J. Clin. Pathol., 38, pp. 1337-1341; Morris, J.A., Thorns, C.J., Wells, G.A.H., Scott, A.C., Sojka, W.J., The production of F41 fimbriae by piglet strains of enterotoxigenic Escherichia coli that lack K88, K99 and 987P fimbriae (1983) J. Gen. Microbiol., 129, pp. 2753-2759; Contrepois, M., Martel, J.L., Bordas, C., Hayers, F., Millet, A., Ramisse, J., Sendral, R., Fréquence des pili FY et K99 parmi des souches de Escherichia coli isolées de veaux diarrhéiques en France (1985) Ann. Rech. Vét., 16, pp. 25-28; Dean, A.G., Dean, J.A., Coulombier, D., Brendel, K.A., Smith, D.C., Burton, A.H., Dicker, R.C., Arner, T.G., Epi Info Version 6: A word processing, database and statistics program for epidemiology on microcomputers (1994) Centers for Disease Control and Prevention, , Atlanta, GA; Abraham, G., Roeder, P.L., Zewdu, R., Agents associated with neonatal diarrhoea in ethiopian dairy calves (1992) Trop. Anim. Health Prod., 24, pp. 74-80; Athanassious, R., Marsolais, M., Assaf, R., Dea, S., Descôteaux, J.P., Dulude, S., Montpetit, C., Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dysentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can. Vet. J., 35, pp. 163-169; Gouet, P., Contrepois, M., Dubourguier, H.C., Riou, Y., Scherre, R., Laporte, J., Vautherot, J.F., L'Haridon, R., The experimental production of diarrhea in colostrum deprived axenic and gnotoxenic calves with enteropathogenic Escherichia coli, rotavirus, coronavirus and in a combined infection of rotavirus and E. coli (1978) Ann. Rech. Vet., 9, p. 433; Snodgrass, D.R., Smith, M.L., Krautil, F.L., Interaction of rotavirus and enterotoxigenic Escherichia coli in conventionally-reared dairy calves (1982) Vet. Microbiol., 7, p. 51; Hess, R.G., Bachmann, P.A., Baljer, G., Mayr, A., Pospischil, A., Schmid, G., Synergism in experimental mixed infections of newborn colostrum-deprived calves with bovine rotavirus and enterotoxigenic Escherichia coli (ETEC) (1984) Zbl. Vet. Med. B., 31, pp. 585-596; Runnels, P.L., Moon, H.W., S, M.P.J., Whipp, C., Woode, G.N., Effect of microbial and host variables on the interaction of rotavirus and Escherichia coli infections in gnotobiotic calves (1986) Am. J. Vet. Res., 47, pp. 1542-1550; Morin, M., Lariviee, S., Lallier, R., Begin, M.E., Ethier, R., Roy, R.S., Tremblay, A., Diarrhoea of newborn calves II. Agents responsible for the disease on Quebec dairy farms (1980) Med. Vet. Quebec, 10, pp. 60-65","de la Fuente, R.; Departamento Patologia Animal I, Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain; email: rifuente@eucmax.sim.ucm.es",,,01479571,,CIMID,"10855663","English","Comp. Immunol. Microbiol. Infect. Dis.",Article,"Final",,Scopus,2-s2.0-0034069132
"Freymuth F., Vabret A., Petitjean J., Gouarin S., Gueudin M., Campet M.","7103410207;7003959575;7006379234;56107903900;6603421738;6506923168;","Molecular diagnosis of communal respiratory viral infections [Diagnostic moleculaire des infections virales respiratoires communautaires]",2000,"Virologie","4","4",,"319","328",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033862719&partnerID=40&md5=b9787c3e96a845857a1b325228b00217","Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France","Freymuth, F., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France; Vabret, A., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France; Petitjean, J., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France; Gouarin, S., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France; Gueudin, M., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France; Campet, M., Lab. de Virologie Hum. et Molec., Hôpital Universitaire, 14033 Caen, France","The diagnosis of respiratory viral infections in the community caused by influenza virus, parainfluenza virus (PIV), respiratory syncytial virus (RSV), adenovirus, rhinovirus and coronavirus is based on viral isolation techniques and on direct antigen detection by immunofluorescence assay (IFA) or an immunoenzymatic test (EIA). It has been shown that, in most cases, the molecular methods, i.e. the polymerase chain reaction (PCR) assays, are able to detect more positive cases than the conventional tools. According to the results of three distinctive groups, the detection rate of influenza A viruses, evaluated inside an epidemic period, reaches 57,5, 57,1, 57,7 % and 38,9, 50, 40,9 %, for PCR assays and VIT, respectively. In three distinctive studies of RSV infections, the PCR assays are able to detect 61,3, 62, 62,4 % of VRS-positive samples, whereas there are 65,3, 44, 39,3 % of VIT and/or IF positive samples. For the other respiratory viruses: PIV, AdV, RV, CV few data are available on the PCR results. We have previously shown in epidemiological studies in children, that PCR assays may increase the detection rates of PIV from 4,3 to 8,3 %, of AdV from 9,6 to 15,2 %, and of RV from 15,6 to 39,7 % during a RV outbreak in spring. But if the high sensitivity of the PCR assays and its possible standardization and automatisation, points out the limits of the conventional methods, it remains clear that their use as a diagnostic tool is related to the clinical meaning that will be given to the detection of a viral sequence in a respiratory sample.","Adenovirus; Influenza; Parainfluenza; PCR; Respiratory syncytial virus; Rhinovirus","Adenovirus; antigen detection; Coronavirus; enzyme immunoassay; immunofluorescence test; Influenza virus; nonhuman; Parainfluenza virus; polymerase chain reaction; Respiratory syncytial pneumovirus; respiratory system; review; Rhinovirus; virus diagnosis; virus infection; virus isolation; Adenoviridae; Coronavirus; Influenza A virus; Influenza virus; Respiratory syncytial virus; Rhinovirus; Rice stripe virus; Syncytial virus","Freymuth, F., Vabret, A., Brouard, J., Detection of viral, Chlamydia pneumoniae, Mycoplasma pneumoniae infections in exacerbations of asthma in children (1999) J Clin Virol, 13, pp. 131-139; Gardner, P.S., McQuillin, J., Application of immunofluorescent antibody technique in the rapid diagnosis of respiratory syncytial virus infection (1968) Br Med J, 2, pp. 340-341; Yamada, A., Imanishi, J., Nakajima, E., Nakajima, K., Nakajima, S., Detection of influenza viruses in throat swab by using polymerase chain reaction (1991) Microbiol Immunol, 35, pp. 259-265; Zhang, W., Evans, D.H., Detection and identification of human influenza by the polymerase chain reaction (1991) J Virol Methods, 33, pp. 165-189; Paton, A.W., Paton, J.C., Lawrence, A.J., Goldwater, P.N., Harris, R.J., Rapid detection of respiratory syncytial virus in nasopharyngeal aspirates by reverse transcription and polymerase chain amplification (1992) J Clin Microbiol, 30, pp. 901-904; Cubie, H.A., Ingis, J.M., Leslie, B.E., Edmunds, A.T., Totapally, B., Detection of respiratory syncytial virus in acute bronchiolitis in infants (1992) J Med Virol, 38, pp. 283-287; Bressoud, A., Whitcmob, J., Pourzand, C., Haller, O., Cerutti, P., Rapid detection of influenza virus H1 by the polymerase chain reaction (1990) Biochem Biophys Res Commun, 167, pp. 425-430; Claas, E.C.J., Sprenger, M.J.W., Kleter, G.E.M., Van Beck, R., Quint, W.G.V., Masurel, N., Type-specific identification of influenza viruses A, B and C by the polymerase chain reaction (1992) J Virol Methods, 39, pp. 1-13; Donofrio, J.C., Coonrod, J.D., Davidson, J.N., Betts, R.F., Detection of influenza A and B in respiratory secretions with the polymerase chain reaction (1992) PCR Methods Appl, 1, pp. 263-268; Pisavera, M., Bechtereva, T., Plyusnin, A., Dobretsova, A., Kisselev, O., PCR amplification of influenza A virus specific sequences (1992) Arch Virol, 125, pp. 313-318; Ellis, J.S., Fleming, D.M., Zambon, M.C., Multiplex reverse transcription-PCR for surveillance of influenza A and B viruses in England and Wales in 1995 and 1996 (1997) J Clin Microbiol, 35, pp. 2076-2082; Pregliasco, F., Mensi, C., Camorali, L., Anselmi, G., Comparison of RT-PCR with other diagnostic assays for rapid detection of influenza viruses (1998) J Med Virol, 56, pp. 168-173; Claas, E.C.J., Van Milaan, A.J., Sprenger, M.J.W., Prospective application of reverse transcription polymerase chain reaction for diagnosing influenza infections in respiratory samples from a children's hospital (1993) J Clin Microbiol, 31, pp. 2218-2221; Atmar, R.L., Baxter, B.D., Dominguez, E.A., Taber, L.H., Comparison of reverse transcription-PCR with tissu culture and other rapid diagnosis assays for detection of type A influenza virus (1996) J Clin Microbiol, 34, pp. 2604-2606; Cherian, T., Bobo, L., Steinhoff, M.C., Karron, R.A., Yolken, R.H., Use of PCR-enzyme immunoassay for identification of influenza a virus matrix RNA in clinical samples negative for cultivable virus (1994) J Clin Microbiol, 32, pp. 623-628; Wright, K.E., Wilson, G.A.R., Novosad, D., Dimock, C., Tan, D., Weber, J.M., Typing and subtyping of influenza viruses in clinical samples by PCR (1995) J Clin Microbiol, 33, pp. 1180-1184; Magnard, C., Valette, M., Aymard, M., Lina, B., Comparison of two nested PCR, cell culture, and antigen detection for the diagnosis of upper respiratory tract infections due to influenza viruses (1999) J Med Virol, 59, pp. 215-220; Henkel, J.H., Aberle, S.W., Kundi, M., Popow-Kraupp, T., Improved detection of respiratory syncytial virus in nasal aspirates by semi-nested RT-PCR (1997) J Med Virol, 53, pp. 366-371; Van Milaan, A.J., Sprenger, M.J.W., Rothbarth, P.H., Brandenburg, A.H., Masurel, N., Claas, E.C.J., Detection of respiratory syncytial virus by RNA-polymerase chain reaction and differentiation of subgroups with oligonucleotide probes (1994) J Med Virol, 44, pp. 80-87; Cane, P.R., Pringle, C.R., Respiratory syncytial virus heterogeneity during an epidemic : Analysis by limited nucleotide sequencing (SH gene) and restriction mapping (N gene) (1991) J Gen Virol, 72, pp. 349-357; Freymuth, F., Eugene, G., Vabret, A., Detection of respiratory syncytial virus by reverse transcription-PCR and hybridization with a DNA enzyme immunoassay (1995) J Clin Microbiol, 33, pp. 3352-3355. , Erratum. J Clin Microbiol 1996 ; 34 : 1601; Freymuth, F., Vabret, A., Galateau-Salle, F., Detection of respiratory syncytial virus, parainfluenzavirus 3, adenovirus and rhinovirus sequences in respiratory tract of infants by polymerase chain reaction and hybridization (1997) Clin Diagn Virol, 8, pp. 31-40; Eugene-Ruellan, G., Freymuth, F., Bahloul, C., Badrane, H., Vabret, A., Tordo, N., Detection of respiratory syncytial virus a and B, and parainfluenzavirus 3 sequences in respiratory tract of infants by a single PCR with primers targeted to the L-polymerase gene (1998) J Clin Microbiol, 36, pp. 796-801; Sullender, W.M., Wertz, G.W., Synthetic oligonucleotide probes differentiate respiratory syncytial virus subgroups in a nucleic acid hybridization assay (1991) J Clin Microbiol, 29, pp. 1255-1257; Freymuth, F., Petitjean, J., Pothier, P., Norrby, E., Brouard, J., Prevalence of respiratory syncytial virus subgroups a and B in France, 1982 to 1990 (1991) J Clin Microbiol, 29, pp. 653-655; Echevarria, J.E., Erdmann, D.D., Swierkosz, E.M., Holloway, B.P., Anderson, L.J., Simultaneous detection and identification of human parainfluenza viruses 1, 2, and 3 from clinical samples by multiplex PCR (1998) J Clin Microbiol, 36, pp. 1388-1391; Fan, J., Henrikson, K.J., Rapid diagnosis of human parainfluenzavirus type 1 infection by quantitative reverse transcription-PCR-enzyme hybridization assay (1996) J Clin Microbiol, 34, pp. 1914-1917; Karron, R.A., Froehlich, J.L., Belshe, R.B., Yolken, R.H., Rapid detection of parainfluenza virus type 3 in respiratory specimens : Use of reverse transcription-PCR-enzyme immunoassay (1994) J Clin Microbiol, 32, pp. 484-488; Gwalney, J.M., Rhinoviruses P 593 (1989) Viral Infection of Humans : Epidemiology and Control. 3rd Ed., , Evans AS, ed. Plenum Press, New York; Freymuth, F., Quibriac, M., Petitjean, J., Rhinovirus et infections respiratoires aiguës du nourrisson (1986) Arch Fr Pediatr, 43, pp. 677-679; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infection in exacerbations of asthma in 9-11 year old children (1993) Br Med J, 310, pp. 1225-1229; Gama, R.E., Horsnell, P.R., Hughes, P.J., Amplification of rhinovirus specific nucleic acids from clinical samples using the polymerase chain reaction (1989) J Med Virol, 28, pp. 73-77; Olive, D.M., Al-Mufti, S., Al-Mulla, W., Detection and differentiation of picornaviruses in clinical samples following genomic amplification (1990) J Gen Virol, 71, pp. 2141-2147; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings (1993) Mol Cell Probes, 7, pp. 373-379; Atmar, L., Georghiou, P.L., Classification of respiratory tract picornavirus isolates as enteroviruses or rhinoviruses by using reverse transcription-polymerase chain reaction (1993) J Clin Microbiol, 31, pp. 2544-2546; Johnston, S.L., Sanderson, G., Pattemore, P.K., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Freymuth, F., Vabret, A., Eugene, G., Petitjean, J., Mammes, O., Gennetay, E., (1997) Diagnostic Moléculaire des Infections Respiratoires Communes. 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John Libbey Eurotext, Paris; Mammes, O., (1994) Intérêts et Limites de la PCR Dans le Diagnostic des Bronchiolites à Rhinovirus Chez le Nourrisson, , Thèse Pharm, Paris, 5199494PA05P182; Ireland, D.C., Kent, J., Nicholson, K.G., Improved detection of rhinoviruses in nasal and throat swabs by seminested PCR (1993) J Med Virol, 40, pp. 96-101; Wadell, G., Hammarskjold, M.L., Winberg, G., Varsanyi, T.M., Sundell, G., Genetic variability of adenovirus (1980) Ann NY Acad Sci, 354, pp. 16-42; Allard, A., Girones, R., Juto, P., Wadell, G., Polymerase chain reaction for detection of adenoviruses in stool specimens (1990) J Clin Microbiol, 28, pp. 2659-2667; Hierholzer, J.C., Halonen, P.E., Dahlen, P.O., Bingham, P.G., McDonough, M.M., Detection of adenovirus in clinical specimens by polymerase chain reaction and liquid-phase hybridization quantified by time-resolved fluorometry (1993) J Clin Microbiol, 31, pp. 1886-1891; Wu, T.C., Kanayama, M.D., Hruban, R.H., Au, W.C., Askin, F.B., Hutchins, G.M., Virus associated RNAs (VA-I and VA-II) : An efficient target for the detection of adenovirus infections by in situ hybridization (1992) Am J Pathol, 140, pp. 991-998; Morris, D.J., Cooper, R.J., Barr, T., Bailey, A.S., Polymerase chain reaction for rapid diagnosis of respiratory adenovirus infection (1996) J Infect, 32, pp. 113-117; Matsuse, T., Matsui, H., Shu, C.Y., Adenovirus pulmonary infections identified by PCR and in situ hybridization in bone marrow transplant recipients (1994) J Clin Pathol, 47, pp. 973-977; Kidd, A.H., Jonsson, M., Garwicz, D., Rapid subgenus identification of human adenovirus isolates by a general PCR (1996) J Clin Microbiol, 34, pp. 622-627; Pring-Akerblom, P., Trijssenaar, F.E.J., Adrian, T., Hoyer, H., Multiplex polymerase chain reaction for subgenus-specific detection of human adenoviruses in clinical samples (1999) J Med Virol, 58, pp. 87-92; Vabret, A., Brouard, J., Petitjean, J., Eugene-Ruellan, G., Freymuth, F., Infections à coronavirus humains : Importance et diagnostic (1998) Presse Med, 27, pp. 1813-1817; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Stewart, J.N., Mounir, S., Talbot, J.P., Detection of coronaviruses by the polymerase chain reaction (1995) Diagnosis of Human Viruses by Polymerase Chain Reaction Technology, pp. 317-327. , Becker Y, Darai G eds. Springer-Verlag, New-York; Gilbert, L.L., Dakhama, A., Bone, B.M., Thomas, E.E., Hegele, R.G., Diagnosis of viral respiratory tract infections in children by using a reverse transcription-PCR panel (1996) J Clin Microbiol, 34, pp. 140-143; Fan, J., Henrickson, K.J., Savatski, L.S., Rapid simultaneous diagnosis of infections with respiratory syncytial viruses A and B, influenza viruses A and B, and human parainfluenza virus type 1, 2, and 3 by multiplex quantitative reverse transcription-polymerase chain reaction-enzyme hybridization assay (Hexaplex) (1998) Clin Infect Dis, 26, pp. 1397-1402; Osiowy, C., Direct detection of respiratory syncytial virus, parainfluenza virus, and adenovirus in clinical respiratory specimens by a multiplex reverse transcription-PCR (1998) J Clin Microbiol, 36, pp. 3149-3154; Grondahl, B., Puppe, W., Hoppe, A., Kuhne, I., Weigl, J.A., Schmitt, H.J., Rapid identification of nine microorganisms causing acute respiratory tract infections by single-tube multiplex reverse transcription PCR : Feasibility study (1999) J Clin Microbiol, 37, pp. 1-7","Freymuth, F.; Laboratoire de Virol. Hum. et Mol., Hopital Universitaire, 14033 Caen, France",,,12678694,,VIROF,,"French","Virologie",Review,"Final",,Scopus,2-s2.0-0033862719
"Lim K.P., Ng L.F.P., Liu D.X.","7403175857;7201477950;8972667300;","Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus Avian infectious bronchitis virus and characterization of the cleavage products",2000,"Journal of Virology","74","4",,"1674","1685",,50,"10.1128/JVI.74.4.1674-1685.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033947165&doi=10.1128%2fJVI.74.4.1674-1685.2000&partnerID=40&md5=f29bdcb43df91dd4691ac6d85054816d","Institute of Molecular Agrobiology, National University of Singapore, Singapore 117604, Singapore; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Lim, K.P., Institute of Molecular Agrobiology, National University of Singapore, Singapore 117604, Singapore; Ng, L.F.P., Institute of Molecular Agrobiology, National University of Singapore, Singapore 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, Singapore 117604, Singapore, Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","The coronavirus Avian infectious bronchitis virus (IBV) employs polyprotein processing as a strategy to express its gene products. Previously we identified the first cleavage event as proteolysis at the Gly673- Gly674 dipeptide bond mediated by the first papain-like proteinase domain (PLPD-1) to release an 87-kDa mature protein. In this report, we demonstrate a novel cleavage activity of PLPD-1. Expression, deletion, and mutagenesis studies showed that the product encoded between nucleotides 2548 and 8865 was further cleaved by PLPD-1 at the Gly2265-Gly2266 dipeptide bond to release an N-terminal 195-kDa and a C-terminal 41-kDa cleavage product. Characterization of the cleavage activity revealed that the proteinase is active on this scissile bond when expressed in vitro in rabbit reticulocyte lysates and can act on the same substrate in trans when expressed in intact cells. Both the N- and C-terminal cleavage products were detected in virus- infected cells and were found to be physically associated. Glycosidase digestion and site-directed mutagenesis studies of the 41-kDa protein demonstrated that it is modified by N-linked glycosylation at the Asn2313 residue encoded by nucleotides 7465 to 7467. By using a region-specific antiserum raised against the IBV sequence encoded by nucleotides 8865 to 9786, we also demonstrated that a 33-kDa protein, representing the 3C-like proteinase (3CLP), was specifically immunoprecipitated from the virus- infected cells. Site-directed mutagenesis and expression studies showed that a previously predicted cleavage site (Q2583-G2584) located within the 41-kDa protein-encoding region was not utilized by 3CLP, supporting the conclusion that the 41-kDa protein is a mature vital product.",,"gene product; papain; proteinase; animal cell; article; Avian infectious bronchitis virus; cell lysate; gene deletion; nonhuman; nucleotide sequence; open reading frame; priority journal; protein analysis; protein degradation; protein expression; protein processing; site directed mutagenesis; virus infection; Animals; Binding Sites; Cercopithecus aethiops; Chromosome Mapping; COS Cells; Cysteine Endopeptidases; Dipeptides; Gene Expression; Genes, Viral; Glycine; Glycosylation; Infectious bronchitis virus; Open Reading Frames; Papain; Polyproteins; Protein Biosynthesis; Protein Processing, Post-Translational; Vero Cells; Viral Proteins","Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. Virol., 71, pp. 900-909; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Brierley, I., Boursnell, M.E.G., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D.K., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for a RNA pseudoknot (1989) Cell, 57, pp. 537-547; Cormack, B.P., Valdivia, R.H., Falkow, S., FACS-optimized mutant of the green fluorescent protein (GFP) (1996) Gene, 173, pp. 33-38; Dong, S.H., Baker, S.C., Determination of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus (1994) Virology, 204, pp. 541-549; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. 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USA, 87, pp. 6944-6948; Muylaert, I.R., Chambers, T.J., Galler, R., Rice, C.M., Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: Effects on virus replication and mouse neurovirulence (1996) Virology, 222, pp. 159-168; Ng, L.F.P., Liu, D.X., Identification of a 24 kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites (1998) Virology, 243, pp. 388-395; Ng, L.F.P., Liu, D.X., Further characterization of the coronavirus IBV ORF 1a products encoded by the 3C-like proteinase domain and the flanking regions (1998) Adv. Exp. Med. Biol., 440, pp. 161-171; Pedersen, K.W., Van Der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) J. Virol., 73, pp. 2016-2026; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF 1a (1998) Virology, 242, pp. 288-302; Shi, S.T., Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Oh, J.W., Lai, M.M.C., Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells (1999) J. Virol., 73, pp. 5957-5969; Snijder, E.J., Wassenaar, A.L.M., Spaan, W.J.M., Proteolytic processing of the replicase ORF1a protein of the equine arteritis virus (1994) J. Virol., 68, pp. 5755-5764; Snijder, E.J., Meulenberg, J.J.M., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Localizations of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol., 50, pp. 22-29; Teng, H., Pinon, J.D., Weiss, S.R., Expression of murine coronavirus recombination papain-like proteinase: Efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides (1999) J. Virol., 73, pp. 2658-2666; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D.K., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) J. Virol., 70, pp. 1923-1930; Van Der Meer, Y., Van Tol, H.G., Locker, J.K., Snijder, E.J., ORF1a-encoded replicase subunits are involved in membrane association of the arterivirus replication complex (1998) J. Virol., 72, pp. 6689-6698; Van Der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Locker, J.K., Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73, pp. 7641-7657","Liu, D.X.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; email: liudx@ima.org.sg",,,0022538X,,JOVIA,"10644337","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033947165
"Van Reeth K., Nauwynck H., Pensaert M.","57191565576;7007141390;55905425400;","A potential role for tumour necrosis factor-α in synergy between porcine respiratory coronavirus and bacterial lipopolysaccharide in the induction of respiratory disease in pigs",2000,"Journal of Medical Microbiology","49","7",,"613","620",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033933108&partnerID=40&md5=01eb6eca45c8d5d3ebc784142d291ecc","Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, B-9820 Merelbeke, Belgium","Van Reeth, K., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, B-9820 Merelbeke, Belgium; Nauwynck, H., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, B-9820 Merelbeke, Belgium; Pensaert, M., Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, B-9820 Merelbeke, Belgium","This study examined whether exposure of pigs to both porcine respiratory coronavirus (PRCV) and bacterial lipopolysaccharide (LPS) can potentiate respiratory disease and lung secretion of tumour necrosis factor-α (TNF-α) and interleukin-1 (IL-1). Caesarian-derived colostrum-deprived pigs were inoculated intratracheally with PRCV, with LPS from Escherichia coli 0111:B4 (20 μg/kg), or with a combination of the two, and killed at set times after inoculation. Clinical signs, virus replication and (histo)pathological changes in the lungs, percentage of neutrophils and bioactive TNF-α and IL-1 in broncho-alveolar lavage (BAL) fluids were examined. The effects of separate virus or LPS inoculations were subclinical and failed to induce high and sustained cytokine levels. In a preliminary study, pigs were inoculated with PRCV and then with LPS 24 h later and killed sequentially. Severe respiratory disease and significantly enhanced TNF-α titres (208-3601 U/ml versus 40-89 U/ml after LPS only) were seen during the first 12 h after LPS inoculation. IL-1 levels (106-1631 U/ml versus 28-654 U/ml after LPS only) were also increased, but persisted for longer after clinical recovery than TNF-α. In a second study, pigs were inoculated with PRCV and subsequently with LPS at various time intervals ranging from 0 to 24 h, and killed 5 h after inoculation with LPS. A time interval of at least 12 h between inoculations was necessary for prominent respiratory signs to develop. Production of TNF-α, but not IL-1, was also dependent on the time interval between inoculations and was tightly correlated with disease. Lung neutrophil infiltration and pathological changes were comparable after combined PRCV-LPS and single LPS inoculations, and were not associated with disease. These data show that exposure to high endotoxin concentrations in swine buildings can precipitate respiratory disease in PRCV-infected pigs, and that TNF-α is probably an important mediator of these effects. This is the first in-vivo demonstration of synergy between respiratory viruses and LPS.",,"bacterium lipopolysaccharide; endotoxin; interleukin 1; tumor necrosis factor alpha; animal experiment; animal model; animal tissue; article; controlled study; Coronavirus; cytokine production; disease association; in vivo study; inoculation; lung infiltrate; neutrophil; nonhuman; priority journal; respiratory tract disease; swine; Animals; Bronchoalveolar Lavage Fluid; Coronavirus Infections; Interleukin-1; Lipopolysaccharides; Lung Diseases; Swine; Swine Diseases; Tumor Necrosis Factor-alpha","Pensaert, M., Cox, E., Van Deun, K., Callebaut, P., A sero-epizootiological study of porcine respiratory coronavirus in belgian swine (1993) Vet Q, 15, pp. 16-20; Wesley, R.D., Woods, R.D., McKean, J.D., Senn, M.K., Elazhary, Y., Prevalence of coronavirus antibodies in Iowa swine (1997) Can J Vet Res, 61, pp. 305-308; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res Vet Sci, 48, pp. 165-169; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J Vet Diagn Invest, 5, pp. 184-188; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with 'pneumotropic' porcine coronavirus (1989) Res Vet Sci, 47, pp. 23-29; Rylander, R., Endotoxins (1994) Organic Dusts: Exposure, Effects, and Prevention, 1st Edn., pp. 73-78. , Rylander R, Jacobs RR (eds). Boca Raton, Lewis Publishers; Zejda, J.E., Barber, E., Dosman, J.A., Respiratory health status in swine producers relates to endotoxin exposure in the presence of low dust levels (1994) J Occup Med, 36, pp. 49-56; Liggett, A.D., Harrison, L.R., Farrell, R.L., Acute inflammatory effects of intratracheally instilled Escherichia coli endotoxin and sonicated suspension of Haemophilus pleuropneumoniae in swine (1986) Can J Vet Res, 50, pp. 526-531; Udeze, F.A., Latimer, K.S., Kadis, S., Role of Haemophilus pleuropneumoniae lipopolysaccharide endotoxin in the pathogenesis of porcine Haemophilus pleuropneumoniae (1987) Am J Vet Res, 48, pp. 768-773; Urbain, B., Prouvost, J.-F., Beerens, D., Ansay, M., Gustin, P., Acute effects of endotoxin inhalation on the respiratory tract in pigs: Interaction with ammonia (1996) Inhalation Toxicology, 8, pp. 947-968; Michel, O., Nagy, A.-M., Schroeven, M., Dose-response relationship to inhaled endotoxin in normal subjects (1997) Am J Respir Crit Care Med, 156, pp. 1157-1164; Ulich, T.R., Watson, L.R., Yin, S., The intratracheal administration of endotoxin and cytokines. I. Characterization of LPS-induced IL-1 and TNF mRNA expression and the LPS-, IL-1, and TNF-induced inflammatory infiltrate (1991) Am J Pathol, 138, pp. 1485-1496; Vogelzang, P.F.J., Van Der Gulden, J.W.J., Folgering, H., Endotoxin exposure as a major determinant of lung function decline in pig farmers (1998) Am J Respir Crit Care Med, 157, pp. 15-18; Wang, Z., Larsson, K., Palmberg, L., Malmberg, P., Larsson, P., Larsson, L., Inhalation of swine dust induces cytokine release in the upper and lower airways (1997) Eur Respir J, 10, pp. 381-387; Bielefeldt-Ohmann, H., Role of cytokines in the pathogenesis and treatment of respiratory disease (1995) Cytokines in Animal Health and Disease, pp. 291-332. , Myers MJ, Murtaugh MP (eds). New York, Marcel Dekker; Nain, M., Hinder, F., Gong, J.-H., Tumor necrosis factor-α production of influenza A virus-infected macrophages and potentiating effect of lipopolysaccharides (1990) J Immunol, 145, pp. 1921-1928; Masihi, K.N., Hintelmann, H., Madaj, K., Gast, G., Production of lipopolysaccharide-induced tumour necrosis factor during influenza virus infection in mice coincides with viral replication and respiratory oxidative burst (1995) Mediators of Inflammation, 4, pp. 181-185; Van Reeth, K., Labarque, G., Nauwynck, H., Pensaert, M., Differential production of proinflammatory cytokines in the pig lung during different respiratory virus infections: Correlations with pathogenicity (1999) Res Vet Sci, 67, pp. 47-52; Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus-mediated interference against influenza virus replication in the respiratory tract of feeder pigs (1994) Am J Vet Res, 55, pp. 1275-1281; Chiang, Y.W., Murata, H., Roth, J.A., Activation of bovine neutrophils by recombinant bovine tumor necrosis factor-alpha (1991) Vet Immunol Immunopathol, 29, pp. 329-338; Coe, N.E., Frank, D.E., Roth, J.A., Effect of recombinant human cytokines on porcine neutrophil function (1993) Vet Immunol Immunopathol, 37, pp. 39-47; Sample, A.K., Czuprynski, C.J., Priming and stimulation of bovine neutrophils by recombinant human interleukin-1 alpha and tumor necrosis factor alpha (1991) J Leukoc Biol, 49, pp. 107-115; Strieter, R.M., Kunkel, S.L., Acute lung injury: The role of cytokines in the elicitation of neutrophils (1994) J Investig Med, 42, pp. 640-651; Stephens, K.E., Ishizaka, A., Larrick, J.W., Raffin, T.A., Tumor necrosis factor causes increased pulmonary permeability and edema. Comparison to septic acute lung injury (1988) Am Rev Respir Dis, 137, pp. 1364-1370; Endo, T., Uchida, Y., Matsumota, H., Regulation of endothelin-1 synthesis in cultured guinea pig airway epithelial cells by various cytokines (1992) Biochem Biophys Res Commun, 186, pp. 1594-1599; Kips, J.C., Tavernier, J., Pauwels, R.A., Tumor necrosis factor causes bronchial hyperresponsiveness in rats (1992) Am Rev Respir Dis, 145, pp. 332-336; Thomas, P.S., Yates, D.H., Barnes, P.J., Tumor necrosis factor-α increases airway responsiveness and sputum neutrophilia in normal human subjects (1995) Am J Respir Crit Care Med, 152, pp. 76-80; Bender, A., Sprenger, H., Gong, J.-H., The potentiating effect of LPS on tumor necrosis factor-α production by influenza A virus-infected macrophages (1993) Immunobiology, 187, pp. 357-371; Tanner, W.G., Welborn, M.B., Shepherd, V.L., Tumor necrosis factor-alpha and interleukin-1 alpha synergistically enhance phorbol myristate acetate-induced superoxide production by rat bone marrow-derived macrophages (1992) Am J Respir Cell Mol Biol, 7, pp. 379-384; Caldwell, J., Emerson, S.G., Interleukin-1 alpha upregulates tumor necrosis factor receptors expressed by a human bone marrow stromal cell strain: Implications for cytokine redundancy and synergy (1995) Blood, 86, pp. 3364-3372; Wesselius, L.J., Smimov, I.M., O'Brien-Ladner, A.R., Nelson, M.E., Synergism of intratracheally administered tumor necrosis factor with interleukin-1 in the induction of lung edema in rats (1995) J Lab Clin Med, 125, pp. 618-625; Elbers, A.R.W., De Vries, M., Van Gulick, P., Veterinary practice and occupational health: An epidemiological study of several professional groups of dutch veterinarians. II. Peak expiratory flow variability, dust and endotoxin measurements, use of respiratory protection services, and time distribution of professional activities (1996) Vet Q, 18, pp. 132-136","Van Reeth, K.; Laboratory of Veterinary Virology, Faculty of Veterinary Medicine, University of Ghent, B-9820 Merelbeke, Belgium; email: kristien.vanreeth@rug.ac.be",,,00222615,,JMMIA,"10882086","English","J. Med. Microbiol.",Article,"Final",,Scopus,2-s2.0-0033933108
"Kim L., Hayes J., Lewis P., Parwani A.V., Chang K.O., Saif L.J.","7202158982;57035725700;56343303500;7004273180;7404878277;7102226747;","Molecular characterization and pathogenesis of transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCV) field isolates co-circulating in a swine herd",2000,"Archives of Virology","145","6",,"1133","1147",,41,"10.1007/s007050070114","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033933884&doi=10.1007%2fs007050070114&partnerID=40&md5=cc0bb866d3c2912188587dd227a49525","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Food Animal Research Program, Ohio Agric. Res./Development Center, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","Kim, L., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Hayes, J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Lewis, P., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Parwani, A.V., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Chang, K.O., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio Agric. Res./Development Center, Wooster, OH, United States, Food Animal Research Program, Ohio Agric. Res./Development Center, Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States","TGEV replicates in intestinal enterocytes and causes diarrhea in young pigs. PRCV, a spike (S) gene deletion mutant of TGEV with an altered respiratory tissue tropism, causes mild or subclinical respiratory infections. Comparisons of TGEV and PRCV strains suggest that tropism and pathogenicity are influenced by the S gene and ORF3, respectively. Recently, outbreaks of TGE of reduced virulence were reported in the field. We investigated a similar suspect TGEV outbreak of reduced virulence in nursery pigs from a swine herd in the Midwest. A TGEV strain (BW021898B) was isolated in swine testicular cells from gut contents of a diarrheic pig and three PRCV strains (BW126, BW154, BW155) were isolated from nasal swabs from normal TGEV-seronegative sentinel pigs in contact with the diarrheic pigs. Sequence analysis of the TGEV isolate in the partial S gene and ORF3/3a and ORF3-1/3b revealed high homology with enteropathogenic TGEV strains. Gnotobiotic pig inoculation and histopathological results revealed that this TGEV isolate retained virulence even though in the field outbreak the diarrheal disease was of reduced severity. Sequence analysis of the S gene deletion region of the three PRCV isolates revealed identical deletions between nt 105-752, which differ from deletions previously reported among PRCV strains. The three PRCV isolates had variable sequence changes in ORF 3/3a and ORF 3-1/3b, affecting the ORF size and amino acid sequence. Thus, sequence analysis and pathogenicity studies indicate that this TGEV isolate resembles other enteropathogenic TGEV strains. Therefore, the reduced severity of TGE observed in this herd maybe due to the ongoing PRCV infections, which induce antibodies cross-reactive with TGEV and result in decreased disease severity. The results outlined in this study highlight the need to monitor to monitor the molecular epidemiology of TGEV/PRCV strains with sensitive differential diagnostic assays, followed by sequence analysis of the critical regions to identify changes and pathogenicity studies to confirm the disease potential of the TGEV isolates.",,"diarrhea; differential diagnosis; gene deletion; genetic strain; open reading frame; porcine respiratory coronavirus; S gene; strain difference; swine; tissue tropism; transmissible gastroenteritis coronavirus; United States; virus mutation; virus replication; virus transmission; virus virulence; Amino Acid Sequence; Animal Husbandry; Animals; Coronavirus; Coronavirus Infections; Gastroenteritis, Transmissible, of Swine; Gene Deletion; Germ-Free Life; Membrane Glycoproteins; Molecular Sequence Data; Open Reading Frames; Respiratory Tract Infections; Sequence Analysis, DNA; Swine; Swine Diseases; Transmissible gastroenteritis virus; Viral Envelope Proteins; Virulence","Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminal of the of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J Gen Virol, 76, pp. 2235-2241; Bohl, E.H., Saif, L.J., Theil, K.W., Agnes, A.G., Cross, R.F., Porcine pararotavirus: Detection, differentiation from rotavirus, and pathogenesis in gnotobiotic pigs (1982) J Clin Microbiol, 15, pp. 312-319; Britton, P., Page, K.W., Sequence of the S gene from a virulent British field isolate of transmissible gastroenteritis virus (1990) Virus Res, 18, pp. 71-80; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal Biochem, 162, pp. 156-159; Cox, E., Pensaert, M.B., Callebaut, P., VanDeun, K., Intestinal replication of PRCV closely related antigenically to the enteric transmissible gastroenteritis virus (1990) Vet Microbiol, 23, pp. 237-243; Delmas, B., Rasschaert, D., Godet, M., Gelfi, J., Laude, H., Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of the spike glycoprotein S (1990) J Gen Virol, 71, pp. 1313-1323; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Jacobs, L., Vander Zeijst, B.A.M., Horzinek, M.C., Characterization and translation of transmissible gastroenteritis virus mRNAs (1986) J Virol, 57, pp. 1010-1015; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J Virol, 71, pp. 3285-3287; Kwon, H.M., Saif, L.J., Jackwood, D.J., Field isolates of transmissible gastroenteritis virus differ at the molecular level from the Miller and Purdue virulent and attenuated strains and from porcine respiratory coronaviruses (1998) J Vet Med Sci, 60, pp. 589-597; Laude, H., Reeth, K.V., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet Res, 24, pp. 125-150; 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Pritchard, G.C., Paton, D.J., Wibberley, G., Ibata, G., Transmissible gastroenteritis and porcine epidemic diarrhoea in Britain (1999) Vet Rec, 144, pp. 616-618; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis and porcine respiratory coronavirus (1999) Diseases of Swine 8th Ed., pp. 295-325. , Straw BE, D'Allaire S, Mengeling WL, Taylor DJ (eds) Iowa State University Press, Ames; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronavirus (1992) Virology, 190, pp. 92-105; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-Glycolylneuraminic acid) binding activity (1996) J Virol, 70, pp. 5634-5637; Simkins, R.A., Weilnau, P.A., Bias, J., Saif, L.J., Antigenic variation among transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus.Strains detected with monoclonal antibodies to the S protein of TGEV (1992) Am J Vet Res, 53, pp. 1253-1258; Spaan, W., Cavanagh, D., Horzinek, C., Coronaviruses: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; VanCott, J.L., Brim, T.A., Lunney, J.K., Saif, L.J., Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J Immunol, 152, pp. 3980-3990; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolate reveals heterogenecity in the S, 3 and 3-1 genes (1995) J Virol, 69, pp. 3176-3184; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J Virol, 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J Virol, 64, pp. 4761-4766; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res, 13, pp. 87-100; Wesley, R.D., Nucleotide sequence of the E2-peplomer protein gene and partial nucleotide sequence of the upstream polymerase gene of transmissible gastroenteritis virus (Miller strain) (1991) Adv Exp Med Biol, 276, pp. 301-306","Saif, L.J.; Food Animal Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, 1680 Madison Avenue, Wooster, OH 44691, United States",,,03048608,,ARVID,"10948987","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033933884
"Edwards J.A., Denis F., Talbot P.J.","57199181639;35414314000;7102670281;","Activation of glial cells by human coronavirus OC43 infection",2000,"Journal of Neuroimmunology","108","1-2",,"73","81",,25,"10.1016/S0165-5728(00)00266-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034256082&doi=10.1016%2fS0165-5728%2800%2900266-6&partnerID=40&md5=9646276e38a5f6c63b8ce124e5ff8635","Laboratory of Neuroimmunovirology, Human Health Research Center, Université du Québec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Edwards, J.A., Laboratory of Neuroimmunovirology, Human Health Research Center, Université du Québec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Denis, F., Laboratory of Neuroimmunovirology, Human Health Research Center, Université du Québec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, Human Health Research Center, Université du Québec, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Multiple sclerosis (MS) is an immune-mediated demyelinating disease that could be triggered by a viral infection. Coronaviruses induce an MS-like disease in rodents, are neuroinvasive in humans and can infect primary cultures of human astrocytes and microglia. Infection of the human astrocytic cell line U-373MG by the OC43 strain of human coronavirus caused an upregulation of IL-6, TNF-α, and MCP-1 mRNA expression. This virus also modulated the activity of matrix metalloproteinases-2 and -9 and augmented nitric oxide production in both U-373MG cells and the human microglial cell line CHME-5. Thus, a coronaviral infection of glial cells could lead to the production of inflammatory molecules that have been associated with central nervous system pathologies such as MS. © 2000 Elsevier Science B.V.","Chemokines; Coronavirus; Cytokines; Matrix metalloproteinases; Multiple sclerosis; Nitric oxide","chemokine; cytokine; interleukin 6; matrix metalloproteinase; messenger RNA; nitric oxide; tumor necrosis factor alpha; article; astrocyte; cell activation; controlled study; Coronavirus; glia cell; human; human cell; immunopathology; inflammation; microglia; multiple sclerosis; priority journal; Astrocytes; Cell Line; Chemokine CCL2; Coronavirus; Coronavirus OC43, Human; Gene Expression Regulation; Humans; Interleukin-6; Matrix Metalloproteinase 2; Matrix Metalloproteinase 9; Microglia; Multiple Sclerosis; Neuroglia; Nitric Oxide; RNA, Messenger; Tumor Necrosis Factor-alpha; Up-Regulation","Arbour, N., Côté, G., Lachance, C., Tardieu, M., Cashman, N.R., Talbot, P.J., Acute and persistent infection of human neural cell lines bu human coronavirus OC43 (1999) J. 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"Hsue B., Hartshorne T., Masters P.S.","7801347035;57207534304;7006234572;","Characterization of an essential RNA secondary structure in the 3' untranslated region of the murine coronavirus genome",2000,"Journal of Virology","74","15",,"6911","6921",,53,"10.1128/JVI.74.15.6911-6921.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033927571&doi=10.1128%2fJVI.74.15.6911-6921.2000&partnerID=40&md5=ac73f02385cb8ef9d5f52e87221d6f8f","Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States; Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Ctr. for Immunol. and Microbial Dis., Albany Medical College, Albany, NY 12208, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Hsue, B., Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; Hartshorne, T., Ctr. for Immunol. and Microbial Dis., Albany Medical College, Albany, NY 12208, United States; Masters, P.S., Wadsworth Ctr. for Labs. and Res., New York State Department of Health, Albany, NY 12201, United States, Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","We have previously identified a functionally essential bulged stem-loop in the 3' untranslated region of the positive-stranded RNA genome of mouse hepatitis virus. This 68-nucleotide structure is composed of six stem segments interrupted by five bulges, and its structure, but not its primary sequence, is entirely conserved in the related bovine coronavirus. The functional importance of individual stem segments of this stem-loop was characterized by genetic analysis using targeted RNA recombination. We also examined the effects of stem segment mutations on the replication of mouse hepatitis virus defective interfering RNAs. These studies were complemented by enzymatic and chemical probing of the stem-loop. Taken together, our results confirmed most of the previously proposed structure, but they revealed that the terminal loop and an internal loop are larger than originally thought. Three of the stem segments were found to be essential for vital replication. Further, our results suggest that the stem segment at the base of the stem-loop is an alternative base-pairing structure for part of a downstream, and partially overlapping, RNA pseudoknot that has recently been shown to be necessary for bovine coronavirus replication.",,"virus RNA; animal cell; article; genetic analysis; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; RNA replication; RNA structure; site directed mutagenesis; virus replication; 3' Untranslated Regions; Animals; Base Sequence; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutation; Nucleic Acid Conformation; Plasmids; Recombination, Genetic; Ribonucleases; RNA, Viral; Virus Replication","An, S., Maeda, A., Makino, S., Coronavirus transcription early in infection (1998) J. Virol., 72, pp. 8517-8524; Blackwell, J.L., Brinton, M.A., BHK cell proteins that bind to the 3′ stem-loop structure of the West Nile virus genome RNA (1995) J. 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Siddell (ed.), Plenum Press, New York, N.Y; Van Marie, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Williams, G.D., Chang, R.Y., Brian, D.A., A phylogenetically conserved hairpin-type 3′ untranslated region pseudoknot functions in coronavirus RNA replication (1999) J. Virol., 73, pp. 8349-8355; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′ end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Yu, W., Leibowitz, J.L., A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology, 214, pp. 128-138; Zeng, L., Falgout, B., Markoff, L., Identification of specific nucleotide sequences within the conserved 3′-SL in the dengue type 2 virus genome required for replication (1998) J. Virol., 72, pp. 7510-7522; Zhang, X., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"10888630","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033927571
"Williams B.H., Kiupel M., West K.H., Raymond J.T., Grant C.K., Glickman L.T.","7404502761;7003586822;7401596890;7402362826;7402511447;20134254500;","Coronavirus-associated epizootic catarrhal enteritis in ferrets",2000,"Journal of the American Veterinary Medical Association","217","4",,"526","530",,39,"10.2460/javma.2000.217.526","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034662708&doi=10.2460%2fjavma.2000.217.526&partnerID=40&md5=3ecfff0088f200cf1bd3ae40575aecc1","Department of Veterinary Pathology, Armed Forces Institute of Pathology, Washington, DC 20306-6000, United States; Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47906, United States; Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47906, United States; Prairie Diagnostic Services, 52 Campus Dr, Saskatoon, SK S74 5B4, Canada; Custom Monoclonals International, 813 Harbor Blvd, Ste #284, West Sacramento, CA 95691-2201, United States","Williams, B.H., Department of Veterinary Pathology, Armed Forces Institute of Pathology, Washington, DC 20306-6000, United States; Kiupel, M., Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47906, United States, Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47906, United States; West, K.H., Prairie Diagnostic Services, 52 Campus Dr, Saskatoon, SK S74 5B4, Canada; Raymond, J.T., Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47906, United States, Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47906, United States; Grant, C.K., Custom Monoclonals International, 813 Harbor Blvd, Ste #284, West Sacramento, CA 95691-2201, United States; Glickman, L.T., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47906, United States","Objective - To characterize clinical signs and lesions and identify the etiologic agent associated with epizootic catarrhal enteritis in domestic ferrets. Design - Cross-sectional study. Animals - 119 ferrets with epizootic diarrhea of presumed viral cause and 5 control ferrets. Procedure - Clinical records and biopsy or necropsy specimens of ferrets with presumed epizootic catarrhal enteritis were reviewed, Immunohistochemical staining for coronavirus antigen was performed on paraffin-embedded tissues from approximately 10% of affected ferrets to identify viral antigen and determine its distribution. Transmission electron microscopy was performed on fecal samples and sections of jejunum. Virus isolation studies as well as immunofluorescent tests for other similar viruses were performed. Results - Characteristic microscopic lesions consistent with intestinal coronavirus infection (vacuolar degeneration and necrosis of villus enterocytes; villus atrophy, fusion, and blunting; and lymphocytic enteritis) were consistently detected in affected ferrets. Coronavirus particles were identified in feces and jejunal enterocytes by use of transmission electron microscopy, Immunohistochemical staining of jejunal sections revealed coronavirus antigens. Antigen staining was not detected in healthy ferrets or ferrets with other gastrointestinal tract diseases. Virus isolation was unsuccessful, and other similar viruses were not detected. Conclusions and Clinical Relevance - Results strongly implicate a coronavirus as the causative agent of epizootic catarrhal enteritis in ferrets. Diagnosis may be made on the basis of a combination of historical, clinical, and microscopic findings.",,"animal; animal disease; article; Coronavirus; cross-sectional study; diarrhea; electron microscopy; enteritis; epidemic; ferret; immunohistochemistry; isolation and purification; jejunum; pathology; retrospective study; ultrastructure; virion; virology; virus infection; Animals; Coronavirus; Coronavirus Infections; Cross-Sectional Studies; Diarrhea; Disease Outbreaks; Enteritis; Ferrets; Immunohistochemistry; Jejunum; Microscopy, Electron; Retrospective Studies; Virion","Gorham, J.R., Evermann, J.F., Ward, A., Detection of coronavirus-like particles from mink (1990) Can J Vet Res, 54, pp. 383-384; Kipar, A., Kremendahl, J., Addie, D.D., Fatal enteritis associated with coronavirus infection in cats (1998) J Comp Pathol, 119, pp. 1-14; Kipar, A., Bellmann, S., Kremendahl, J., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Vet Immunol Immunopathol, 65, pp. 243-257; Williams, B.H., Epizootic catarrhal enteritis: A novel diarrheal disease in the ferret (Mustela putorius furo) (1997) Proceedings. 8th Annu Small Mammal Conf, , Baltimore; Keenan, Kp., Jervis, H.R., Marchwicki, R.H., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologie, histologic, histochemical, and immunofluorescent techniques (1976) Am J Vet Res, 37, pp. 247-256; Shen, D.T., Gorham, J.R., Larsen, A.E., Reviewing the transmission of epizootic catarrhal gastroenteritis (1984) Vet Med, 79, pp. 1501-1504; Glass, R.I., Other viral agents of gastroenteritis (1995) Infections of the Gastrointestinal Tract, pp. 1059-1060. , Blaser MJ, ed. New York: Raven Press; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Vet Rec, 132, pp. 7-11; Hoskins, J., Canine viral enteritis (1998) Infectious Diseasts of the Dog and Cat. 3rd Ed., pp. 45-47. , Green CE, ed. Philadelphia: WB Saunders Co; Dea, S., Roy, R.S., Elazhary, M.A., Coronavirus-like particles in the feces of a cat with diarrhea (1982) Can Vet J, 23, pp. 153-155; Pedersen, N.C., Black, J.W., Boyle, J.E., Pathogenic differences between various feline coronavirus isolates (1984) Adv Exp Med Biol, 173, pp. 365-380; Eaton, P., Preliminary observations on enteritis associated with a coronavirus-like agent in rabbits (1984) Lab Anim, 18, pp. 71-74; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Fundamental Virology. 3rd Ed., pp. 541-542. , Fields BN, ed. Philadelphia: Lippincott-Raven Inc; Collins, J.K., Riegal, C.A., Olson, J.D., Shedding of enteric coronavirus in adult cattle (1987) Am J Vet Res, 48, pp. 361-365","Williams, B.H.; Department of Veterinary Pathology, Armed Forces Institute of Pathology, Washington, DC 20306-6000, United States",,"American Veterinary Medical Association",00031488,,JAVMA,"10953717","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0034662708
"Wu G.F., Pewe L., Perlman S.","7404976255;6603143496;7102708317;","Coronavirus-induced demyelination occurs in the absence of inducible nitric oxide synthase",2000,"Journal of Virology","74","16",,"7683","7686",,23,"10.1128/JVI.74.16.7683-7686.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033854596&doi=10.1128%2fJVI.74.16.7683-7686.2000&partnerID=40&md5=abec72e0f6955f352cc69f0ce86bbf24","2042 Medical Labs, University of Iowa, Iowa City, IA 52242, United States","Wu, G.F., 2042 Medical Labs, University of Iowa, Iowa City, IA 52242, United States; Pewe, L., 2042 Medical Labs, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., 2042 Medical Labs, University of Iowa, Iowa City, IA 52242, United States","Demyelination induced by mouse hepatitis virus (MHV), strain JHM, is in large part immune mediated, but little is known about the mechanisms involved in this process. Previous results suggest that inducible nitric oxide synthase (NOS2) contributes transiently to MHV-induced demyelination. Herein, we show that equivalent amounts of demyelination were evident at day 12 after MHV infection in mice genetically deficient in NOS2 (NOS2(-/-)) and in C57BL/6 mice. Furthermore, using an established adoptive transfer model and pharmacological inhibitors of NOS2 function, we could demonstrate no effect on MHV-induced demyelination. These results indicate that NOS2 function is not required for demyelination in mice infected with MHV.",,"nitric oxide synthase; adoptive transfer; animal experiment; animal model; animal tissue; article; controlled study; demyelination; enzyme activity; enzyme induction; enzyme inhibition; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; regulatory mechanism; Adoptive Transfer; Animals; Coronavirus Infections; Demyelinating Diseases; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Nitric Oxide Synthase; Nitric Oxide Synthase Type II; Spinal Cord","Connor, J.R., Manning, P.T., Settle, S.L., Moore, W.M., Jerome, G.M., Webber, R.K., Tjoeng, F.S., Currie, M.G., Suppression of adjuvant-induced arthritis by selective inhibition of inducible nitric oxide synthase (1995) Eur. J. Pharmacol., 273, pp. 15-24; Cross, A.H., Misko, T.P., Lin, R.F., Hickey, W.F., Trotter, J.L., Tilton, R.G., Aminoguanidine, an inhibitor of inducible nitric oxide synthase, ameliorates experimental autoimmune encephalomyelitis in SJL mice (1994) J. Clin. Invest., 93, pp. 2684-2690; Faraci, W.S., Nagel, A.A., Verdries, K.A., Vincent, L.A., Xu, H., Nichols, L.E., Labasi, J.M., Pettipher, E.R., 2-Amino-4-methylpyridine as a potent inhibitor of inducible NO synthase activity in vitro and in vivo (1996) Br. J. Pharmacol., 119, pp. 1101-1108; Fleming, J.O., Trousdale, M.D., El-Zaatari, F., Stohlman, S.A., Wether, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Gold, D., Schroder, K., Powell, H., Kelly, C., Nitric oxide and the immunomodulation of experimental allergic encephalomyelitis (1997) Eur. J. Immunol., 27, pp. 2863-2869; Grzybicki, D., Kwack, K., Perlman, S., Murphy, S., Nitric oxide synthase type II expression by different cell types in MHV-JHM encephalitis suggests distinct roles for nitric oxide in acute versus persistent virus infection (1997) J. Neuroimmunol., 73, pp. 15-27; Horwitz, M., Evans, C., McGavern, D., Rodriguez, M., Oldstone, M., Primary demyelination in transgenic mice expressing interferon-gamma (1997) Nat. Med., 3, pp. 1037-1041; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol., 5, pp. 9-14; Lane, T.E., Fox, H., Buchmeier, M.J., Inhibition of nitric oxide synthase-2 reduces the severity of mouse hepatitis virus-induced demyelination: Implication for NOS2/NO regulation of chemokine expression and inflammation (1998) J. Neurovirol., 5, pp. 48-54; Lane, T.E., Liu, M.T., Chen, B.P., Asensio, V.C., Samawi, R.M., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., A central role for CD4+ T cells and RANTES in virus-induced central nervous system inflammation and demyelination (2000) J. Virol., 74, pp. 1415-1424; Lane, T.E., Paoletti, A.D., Buchmeier, M.J., Dissociation between the in vitro and in vivo effects of nitric oxide on a neurotropic murine coronavirus (1997) J. Virol., 71, pp. 2202-2210; Lin, M.T., Hinton, D., Parra, B., Stohlman, S., Van Der Veen, R., The role of IL-10 in mouse hepatitis virus-induced demyelinating encephalomyelitis (1998) Virology, 245, pp. 270-280; Lin, M.T., Stohlman, S.A., Hinton, D.R., Mouse hepatitis virus is cleared from the central nervous systems of mice lacking perforin-mediated cytolysis (1997) J. Virol., 71, pp. 383-391; MacMicking, J., Xie, Q.-W., Nathan, C., Nitric oxide and macrophage function (1997) Annu. Rev. Immunol., 15, pp. 323-350; Moore, W.M., Webber, R.K., Jerome, G.M., Tjoeng, F.S., Misko, T.P., Currie, M.G., L-N6-(1-iminoethyl)lysine: A selective inhibitor of inducible nitric oxide synthase (1994) J. Med. Chem., 37, pp. 3886-3888; Nathan, C., Xie, Q.-W., Nitric oxide synthases: Roles, tolls, and controls (1994) Cell, 78, pp. 915-918; Parkinson, J.F., Mitrovic, B., Merrill, J., The role of nitric oxide in multiple sclerosis (1997) J. Mol. Med., 75, pp. 174-186; Parra, B., Hinton, D., Marten, N., Bergmann, C., Lin, M.T., Yang, C.S., Stohlman, S.A., IFN-γ is required for viral clearance from central nervous system oligodendroglia (1999) J. Immunol., 162, pp. 1641-1647; Philis-Tsimikas, A., Parthasarathy, S., Picard, S., Palinski, W., Witztum, J.L., Aminoguanidine has both pro-oxidant and antioxidant activity toward LDL (1995) Arteriosclerosis Thrombosis Vasc. Biol., 15, pp. 367-376; Picard, S., Parthasarathy, S., Fruebis, J., Witzhum, J., Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptors (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 6876-6880; Probert, L., Akassogiou, K., Pasparakis, M., Kontogeorgos, G., Kollias, G., Spontaneous inflammatory demyelinating disease in transgenic mice showing central nervous system-specific expression of tumor necrosis factor α (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 11294-11298; Reiss, C.S., Komatsu, T., Does nitric oxide play a critical role in viral infections? (1998) J. Virol., 72, pp. 4547-4551; Rose, J., Hill, K., Wada, Y., Kurtz, C., Tsunoda, I., Fujinami, R., Cross, A., Nitric oxide synthase inhibitor, aminoguanidine, reduces inflammation and demyelination produced by Theiler's virus infection (1998) J. Neuroimmunol., 81, pp. 82-89; Stohlman, S.A., Bergmann, C.C., Perlman, S., Persistent refection by mouse hepatitis virus (1998), pp. 537-557. , R. Ahmed and I. Chen (ed.), Persistent viral infections. John Wiley and Sons, Ltd., New York, N.Y; Stohlman, S.A., Hinton, D.R., Cua, D., Dimacali, E., Sensintaffar, J., Hofman, F.M., Tahara, S.M., Yao, Q., Tumor necrosis factor expression during mouse hepatitis virus-induced demyelinating encephalomyelitis (1995) J. Virol., 69, pp. 5898-5903; Sun, N., Grzybicki, D., Castro, R., Murphy, S., Perlman, S., Acti-vation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wang, F.-I., Hinton, D., Gilmore, W., Trousdale, M., Fleming, J.O., Sequential infection of glial cells by the murine hepatitis virus JHM strain (MHV-4) leads to a characteristic distribution of demyelination (1992) Lab. Invest., 66, pp. 744-754; Wet, X.Q., Charles, I.G., Smith, A., Ure, J., Feug, G.J., Huaug, F.P., Xu, D., Liew, F.Y., Altered immune responses in mice lacking inducible nitric oxide synthase (1995) Nature, 375, pp. 408-411; Wu, G.F., Perlman, S., Macrophage infiltration, but not apoptosis, is correlated with immune-mediated demyelination following murine infection with a neurotropic coronavirus (1999) J. Virol., 73, pp. 8771-8780; Xue, S., Sun, N., Van Rootjen, N., Perlman, S., Depletion of blood-borne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus (1999) J. Virol., 73, pp. 6327-6334","Perlman, S.; 2042 Medical Labs, University of Iowa, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"10906226","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033854596
"Chae C., Kim O., Min K., Choi C., Kim J., Cho W.-S.","36523220500;7202629024;36878789700;7402961450;57191687079;57215232304;","Seroprevalence of porcine respiratory coronavirus in selected Korean pigs",2000,"Preventive Veterinary Medicine","46","4",,"293","296",,4,"10.1016/S0167-5877(00)00154-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034284926&doi=10.1016%2fS0167-5877%2800%2900154-9&partnerID=40&md5=5fe0d660be46dd075c9789c240cc4959","Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea","Chae, C., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; Kim, O., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; Min, K., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; Choi, C., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; Kim, J., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; Cho, W.-S., Department of Veterinary Pathology, College of Veterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea","A total of 446 serum samples from 88 herds in Korea were examined for antibody to porcine respiratory coronavirus (PRCV) using blocking enzyme-linked immunosorbent assay (ELISA). All serum samples were collected from 24- to 26-week-old finishing pigs between December 1998 and June 1999. By ELISA, 237 out of 446 sera tested (53.1%) and 54 out of 88 sampled herds (61.3%) were positive against PRCV. Of 446 sera from 88 herd tested, 185 (41.5%) serum samples from 22 (25%) herds were seronegative against PRCV and transmissible gastroenteritis virus infection. Our data suggested that seropositive herds for PRCV are distributed diffusely throughout South Korea. (C) 2000 Elsevier Science B.V.","Korea; Pig-microbiological disease; Porcine respiratory coronavirus; Prevalence","enzyme linked immunosorbent assay; porcine respiratory coronavirus; serodiagnosis; seroprevalence; South Korea; swine; transmissible gastroenteritis virus; virus infection; Animals; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Female; Korea; Seroepidemiologic Studies; Swine; Swine Diseases","Ahn, K., Chae, C., Kweon, C.-H., Immunohistochemical identification of porcine respiratory coronavirus antigen in the lung of conventional pigs (1997) Vet. Pathol., 34, pp. 167-169; Bernard, S., Bottreau, E., Aynaud, J.M., Have, P., Szymonoky, J., Natural infection with the porcine respiratory coronavirus induces protective lactogenic immunity against transmissible gastroenteritis (1989) Vet. Microbiol., 21, pp. 1-8; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet. Microbiol., 20, pp. 9-19; Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine respiratory coronavirus related to transmissible gastroenteritis virus (1990) Res. Vet. Sci., 48, pp. 165-169; Jabrane, A., Girard, C., Elazhary, Y., Pathogenicity of porcine respiratory coronavirus isolated in Quebec (1994) Can. Vet. J., 35, pp. 86-92; Martin, M., Casal, J., Lanza, I., Rubio, P., Carmenes, P., Porcine respiratory coronavirus spread in Catalunya, Spain, a previously infection-free area (1994) Prev. Vet. Med., 21, pp. 65-74; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with 'pneumotropic' porcine coronavirus (1989) Res. Vet. Sci., 47, pp. 23-29; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Simkins, R.A., Weilnau, P.A., Van Cott, J., Brim, T.A., Saif, L.J., Competition ELISA, using monoclonal antibodies to the transmissible gastroenteritis virus (TGEV) S protein, for serologic differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am. J. Vet. Res., 54, pp. 254-259; Vannier, P., Disorders induced by the experimental infection of pigs with the porcine respiratory coronavirus (PRCV) (1990) J. Vet. Med. B., 37, pp. 177-180; Van Nieuwstadt, A.P., Pol, J.M.A., Isolation of a TGE virus-related respiratory coronavirus causing fatal pneumonia in pigs (1989) Vet. Rec., 124, pp. 43-44; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the US (1990) J. Vet. Diagn. Invest., 2, pp. 312-317","Chae, C.; Dept. Veteterinary Pathology, Coll. Veteterinary Medicine, Seoul National University, Suwon 441-744, Kyounggi-Do, South Korea; email: swine@plaza.snu.ac.kr",,,01675877,,PVMEE,"10960715","English","Prev. Vet. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0034284926
"Narayanan K., Maeda A., Maeda J., Makino S.","7101933409;7201779383;23135329700;7403067550;","Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells",2000,"Journal of Virology","74","17",,"8127","8134",,121,"10.1128/JVI.74.17.8127-8134.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033899980&doi=10.1128%2fJVI.74.17.8127-8134.2000&partnerID=40&md5=358ec2fc193d6f08d555ecec429b0dc6","Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States","Narayanan, K., Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States; Maeda, A., Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States; Maeda, J., Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States; Makino, S., Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States","Coronavirus contains three envelope proteins, M, E and S, and a nucleocapsid, which consists of genomic RNA and N protein, within the viral envelope. We studied the macromolecular interactions involved in coronavirus assembly in cells infected with a murine coronavirus, mouse hepatitis virus (MHV). Coimmunoprecipitation analyses demonstrated an interaction between N protein and M protein in infected cells. Pulse-labeling experiments showed that newly synthesized, unglycosylated M protein interacted with N protein in a pre-Golgi compartment, which is part of the MHV budding site. Coimmunoprecipitation analyses further revealed that M protein interacted with only genomic-length MHV mRNA, mRNA 1, while N protein interacted with all MHV mRNAs. These data indicated that M protein interacted with the nucleocapsid, consisting of N protein and mRNA 1, in infected cells. The M protein-nucleocapsid interaction occurred in the absence of S and E proteins. Intracellular M protein-N protein interaction was maintained after removal of viral RNAs by RNase treatment. However, the M protein-N protein interaction did not occur in cells coexpressing M protein and N protein alone. These data indicated that while the M protein-N protein interaction, which is independent of viral RNA, occurred in the M protein-nucleocapsid complex, some MHV function(s) was necessary for the initiation of M protein-nucleocapsid interaction. The M protein-nucleocapsid interaction, which occurred near or at the MHV budding site, most probably represented the process of specific packaging of the MHV genome into MHV particles.",,"envelope protein; M protein; animal cell; article; cell compartmentalization; Coronavirus; endoplasmic reticulum; Golgi complex; molecular interaction; mouse; nonhuman; priority journal; protein protein interaction; protein RNA binding; virus assembly; virus characterization; virus genome; virus infection; virus nucleocapsid; virus particle; Animals; Cell Line; Coronavirus Infections; Electrophoresis, Polyacrylamide Gel; Membrane Glycoproteins; Mice; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; Precipitin Tests; Protein Binding; Ribonuclease, Pancreatic; RNA, Messenger; RNA, Viral; Viral Envelope Proteins; Viral Matrix Proteins; Virus Assembly","Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Virol., 65, pp. 3219-3226; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Makino, S.; Dept. of Microbiology and Immunology, The Univ. of Texas Med. Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,,0022538X,,JOVIA,"10933723","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033899980
"Crouch C.F., Oliver S., Hearle D.C., Buckley A., Chapman A.J., Francis M.J.","7006793407;55424287900;6508135678;57198294746;57198261437;7201841723;","Lactogenic immunity following vaccination of cattle with bovine coronavirus",2000,"Vaccine","19","2-3",,"189","196",,19,"10.1016/S0264-410X(00)00177-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034666694&doi=10.1016%2fS0264-410X%2800%2900177-8&partnerID=40&md5=17c8806e90509f068140de12f621fd57","Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom","Crouch, C.F., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom; Oliver, S., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom; Hearle, D.C., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom; Buckley, A., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom; Chapman, A.J., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom; Francis, M.J., Schering Plough Animal Health, Breakspear Road South, Harefield, Uxbridge, Middlesex UB9 6LS, United Kingdom","In order to investigate the ability of an oil adjuvanted vaccine containing bovine coronavirus antigen to enhance lactogenic immunity in the calf, pregnant cows and heifers were vaccinated and specific virus neutralising antibody levels determined in serum, colostrum and milk. Pre- existing antibody titres (as a result of natural infection) in the serum of these animals were found to be significantly increased as a result of a single shot vaccination carried out between 2 and 12 weeks before calving. This was reflected in a similar increase in the titre and duration of specific antibody in milk and colostrum that was passed on to the calves. The overall response observed was highly dependent on an adequate antigen payload being incorporated within the single dose vaccine. No abnormal local or systemic reactions were observed as a result of vaccination. It is hoped that this approach will lead to the production of a superior commercial vaccine for the protection of neonatal calves against enteric coronavirus infection. © 2000 Elsevier Science Ltd.","Bovine coronavirus; Cattle; Lactogenic immunity","bacterial antigen; neutralizing antibody; rotavec k99; unclassified drug; virus antigen; virus vaccine; animal model; antibody titer; article; cattle disease; Coronavirus; Escherichia coli; lactation; milk; nonhuman; pregnancy; priority journal; Rotavirus; serum; vaccination; virus infection; Animals; Antibodies, Viral; Antigens, Viral; Cattle; Colostrum; Coronavirus; Dose-Response Relationship, Immunologic; Female; Milk; Pregnancy; Vaccination; Viral Vaccines","Acres, S.D., Laing, C.J., Saunders, J.R., Radostits, O.M., Acute undifferentiated neonatal diarrhea in beef calves 1. Occurrence and distribution of infectious agents Can (1975) J. Comp. Med., 39, pp. 116-132; Moon, H.W., McClurkin, A.W., Isaacson, R.E., Pohlenz, J., Skartedf, S.M., Gillette, K.G., Baetz, A.L., Pathogenic relationships of rotavirus, Escherichia coli, and other agents in mixed infections in calves (1978) J. Am. Vet. Med. Assoc., 173, pp. 577-583; Morin, M., Lariviere, S., Lallier, R., Pathological and microbiological observations made on spontaneous cases of acute neonatal calf diarrhea (1976) Can. J. Comp. Med., 40, pp. 228-240; Mebus, C.A., Stair, E.L., Underdahl, N.R., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a reo-like virus (1971) Vet. Path., 8, pp. 490-505; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a corona-like virus (1973) Vet. Path., 10, pp. 45-64; Crouch, C.F., Acres, S.D., Prevalence of rotavirus and coronavirus antigens in the faeces of normal cows (1984) Can. J. Comp. Med., 19, pp. 340-342; Rodak, L., Babiuk, L.A., Acres, S.D., Radioimmunological (RIA) and enzymimmunological (ELISA) detection of coronavirus antibodies in bovine serum and lacteal secretions (1982) J. Clin. Microbiol., 16, pp. 34-40; Crouch, C.F., Vaccination against enteric rota and coronaviruses in cattle and pigs: Enhancement of lactogenic (1985) Immunity Vaccine, 3, pp. 284-291; Dauvergne, M., Laporte, J., Reynaud, G., Soulebot, J.-P., Brun, A., Espinasse, J., Vaccination of dams with a combined rotavirus-coronavirus vaccine to protect newborn calves against diarrhea (1983) IVth International Symposium, Neonatal Diarrhea, VIDO, Saskatchewan, Canada, pp. 424-432; Wieda, J., Bengelsdorff, H.-J., Bernhardt, D., Hungerer, K.-D., Antibody levels in milk of vaccinated and unvaccinated cows against organisms of neonatal diarrhoea (1987) J. Vet. Med., 34, pp. 495-503; Mostl, K., Burkl, F., Incidence of diarrhoea and of rotavirus- And coronavirus- shedding in calves, whose dams had been vaccinated with an experimental oil-adjuvanted vaccine containing bovine rotavirus and bovine coronavirus (1988) J. Vet. Med., 35, pp. 186-196; Stepanek, J., Salajka, E., Zuffa, A., Mensik, J., Franz, J., New polyvalent vaccine against intestinal infections in newborn calves (1987) Veterinarni-Medicina, 32, pp. 65-80; Kohara, J., Hirai, T., Mori, K., Ishizaki, H., Tsunemitsu, H., Enhancement of passive immunity with maternal vaccine against newborn calf diarrhea (1997) J. Vet. Med. Res., 59, pp. 1023-1025; Deregt, D., Crouch, C.F., Sabara, M., Gilchrist, J., Babiuk, L.A., Hudson, G.R., Preliminary studies of a bovine coronavirus (BCV) antigen responsible for neutralization (1983) IVth International Symposium, Neonatal Diarrhea, VIDO, Saskatchewan, Canada, pp. 117-132; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; Butler, J.E., Synthesis and distribution of immunoglobulins (1973) J. Am.Vet. Med. Assoc., 160, pp. 795-798; Crouch, C.F., Raybould, T.J.G., Comparison of different antigen preparations as substrates for use in passive hemagglutination and enzyme-linked immunosorbent assays for detection of antibody against bovine enteric coronavirus (1983) J. Clin. Microbiol., 18, pp. 146-149; Saif, L.J., Redman, D.R., Smith, K.L., Theil, K.W., Passive immunity to bovine rotavirus in newborn calves fed colostrum supplements from immunised or nonimmunised cows (1983) Infect. Immun., 41, pp. 1118-1131; Bohl, E.H., Gupta, P.K., Olquin, F.M.W., Saif, L.J., Antibody responses in serum, colostrum and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1972) Infect. Immun., 6, pp. 289-301; Snodgrass, D.R., Browning, G., Enteric vaccines for farm animals and horses (1999) In Vaccines for Veterinary Applications, pp. 59-81. , Oxford: Butterworth-Heinemann Ltd",,,,0264410X,,,"10930672","English","Vaccine",Article,"Final",Open Access,Scopus,2-s2.0-0034666694
"Gómez N., Wigdorovitz A., Castañón S., Gil F., Ordá R., Borca M.V., Escribano J.M.","57212697516;6602679344;36089714900;7102457267;55936460800;7004561390;55402647000;","Oral immunogenicity of the plant derived spike protein from swine-transmissible gastroenteritis coronavirus",2000,"Archives of Virology","145","8",,"1725","1732",,51,"10.1007/s007050070087","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033860834&doi=10.1007%2fs007050070087&partnerID=40&md5=5a5c05d6525f1aeced471fd58365d461","Departamento de Mejora Genética y Biotecnologí, INIA, Madrid, Spain; Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Departamento de Biología de Organismos y Sistemas, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, Oviedo, Spain","Gómez, N., Departamento de Mejora Genética y Biotecnologí, INIA, Madrid, Spain; Wigdorovitz, A., Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Castañón, S., Departamento de Biología de Organismos y Sistemas, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, Oviedo, Spain; Gil, F., Departamento de Mejora Genética y Biotecnologí, INIA, Madrid, Spain; Ordá, R., Departamento de Biología de Organismos y Sistemas, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, Oviedo, Spain; Borca, M.V., Instituto de Virología, CICV, INTA-Castelar, Buenos Aires, Argentina; Escribano, J.M., Departamento de Mejora Genética y Biotecnologí, INIA, Madrid, Spain","Transgenic plants represent an inexpensive alternative to classical fermentation systems for production of recombinant subunit vaccines. Transgenic potato plants were created that express the N-terminal domain of the glycoprotein S (N-gS) from Transmissible gastroenteritis coronavirus (TGEV), containing the major antigenic sites of the protein. Extracts from potato tubers expressing N-gS were inoculated intraperitoneally to mice, and the vaccinated mice developed serum IgG specific for TGEV. Furthermore, when potato tubers expressing N-gS were fed directly to mice, they developed serum antibodies specific for gS protein, demonstrating the oral immunogenicity of the plant derived spike protein from TGEV.",,"amino terminal sequence; antibody specificity; glycoprotein S; immunogenicity; immunoglobulin G; mouse; potato; spike protein; transgenic plant; transmissible gastroenteritis coronavirus; vaccination; vaccine production; Administration, Oral; Animals; Antibodies, Viral; Antigens, Viral; Coronavirus; Coronavirus Infections; Enzyme-Linked Immunosorbent Assay; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Plant Proteins; Plants, Genetically Modified; Plasmids; Polymerase Chain Reaction; Recombinant Proteins; Solanum tuberosum; Transformation, Genetic; Vaccines, Synthetic; Viral Envelope Proteins; Viral Vaccines; Animalia; Coronavirus; Solanum tuberosum; Sus scrofa; Transmissible gastroenteritis virus","Arakawa, I., Chong, D.K.X., Langridge, W.H.R., Efficacy of a food plant-based oral cholera toxin B subunit vaccine (1998) Nat Biotech, 16, pp. 292-297; Baulcombe, D.C., Saunders, G.R., Bevan, M.W., Mayo, M.A., Harrison, B.D., Expression of biologically active viral satelite RNA from nuclear genome of transformed plants (1986) Nature, 321, pp. 446-449; Bechtold, N., Ellis, J., Pelletier, G., Agrobacterium mediated gene transfer by infiltration of adult Arabidopsis thaliana plants (1993) C R Acad Sci Paris, 316, pp. 1194-1199; Bohl, E.H., Transmissible gastroenteritis (1981), pp. 195-208. , Leman AD, Glock RD, Mengeling WL, Penny RHC, School E, Straw B (eds) Diseases of swine. 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Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033860834
"Wang Y., Detrick B., Yu Z.-X., Zhang J., Chesky L., Hooks J.J.","56802808200;7003911483;57199729136;7601342242;36966040900;7006661655;","The role of apoptosis within the retina of coronavirus-infected mice",2000,"Investigative Ophthalmology and Visual Science","41","10",,"3011","3018",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033831878&partnerID=40&md5=3d155fcde1f8f191bb1d2dbf964c12cc","NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States","Wang, Y., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; Detrick, B., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; Yu, Z.-X., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; Zhang, J., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; Chesky, L., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; Hooks, J.J., NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States","Purpose. To evaluate the possible roles of apoptosis in the murine retinopathy induced by coronavirus. Methods. Mice were inoculated with virus intravitreally. Mouse eyes harvested at varying times after inoculation were evaluated for apoptotic and immunologic events by hematoxylin and eosin staining, immunohistochemical staining, in situ terminal deoxynucleotidyltransferase dUTP nickend labeling (TUNEL) assay, and electron microscopy. Isolated retinas were analyzed for infectious virus and for expression of apoptosis-associated genes. Results. The number of apoptotic events was significantly elevated in infected eyes from BALB/c and CD-1 mouse strains, reaching a maximum at days 6 through 10, and returning to normal levels at day 20. The majority of apoptotic cells were observed in the outer nuclear layer of the infected retina. In contrast, few apoptotic cells were observed in normal or mock-injected mouse eyes. Apoptotic events within the retina were associated with the presence of viral antigen, infiltration of CD8+ T cells, and clearance of infectious virus. Reverse transcription-polymerase chain reaction (RT-PCR) analysis identified the upregulation of Fas ligand (FasL) and granzyme B mRNAs within the infected retinas. The development of apoptosis, regulative gene expression, and viral clearance were similar in both retinal degeneration-susceptible (BALB/c) and -resistant (CD-1) mice. Conclusions. Retinal apoptosis was associated with retinal inflammation, a decrease in infectious virus, and upregulation of genes associated with CTL killing. These studies indicate that retinal apoptosis may be one of the host mechanisms that contribute to limiting this retinal infection.",,"FAS ligand; granzyme B; virus antigen; animal experiment; animal model; animal tissue; apoptosis; article; controlled study; Coronavirus; cytotoxic T lymphocyte; gene expression; inflammation; mouse; nonhuman; priority journal; retinitis; RNA virus infection; T lymphocyte subpopulation; Animals; Antigens, CD95; Antigens, Viral; Apoptosis; CD8-Positive T-Lymphocytes; Coronavirus Infections; DNA Primers; Eye Infections, Viral; Fas Ligand Protein; Fluorescent Antibody Technique, Indirect; Gene Expression; Granzymes; Hepatitis, Viral, Animal; In Situ Nick-End Labeling; Liver; Male; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Pore Forming Cytotoxic Proteins; Retina; Retinal Diseases; Reverse Transcriptase Polymerase Chain Reaction; Serine Endopeptidases; Up-Regulation; Virus Replication","Madigan, M.C., Penfold, P.L., Human retinoblastoma: A morphological study of apoptotic, leukocytic, and vascular elements (1997) Ultrastruct Pathol, 21, pp. 95-107; 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Advances in Ocular Immunology. Amsterdam: Elsevier; Hooks, J.J., Wang, Y., Detrick, B., The role of immune factors in coronavirus infection of the retina Ocular Infect Hyg, , In press","Hooks, J.J.; NIH/NEI, Building 10, 9000 Rockville Pike, Bethesda, MD 20892, United States; email: jjhooks@helix.nih.gov",,,01460404,,IOVSD,"10967058","English","Invest. Ophthalmol. Vis. Sci.",Article,"Final",,Scopus,2-s2.0-0033831878
"Storz J., Lin X., Purdy C.W., Chouljenko V.N., Kousoulas K.G., Enright F.M., Gilmore W.C., Briggs R.E., Loan R.W.","7006694594;36768282000;7004943441;6603655227;7003476092;35352075200;7004545218;57209681724;7004131337;","Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans' criteria for causation",2000,"Journal of Clinical Microbiology","38","9",,"3291","3298",,65,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033831728&partnerID=40&md5=f34d865966b94921b1b8459cc20f57b7","Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Storz, J., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Lin, X., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Purdy, C.W., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Chouljenko, V.N., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Kousoulas, K.G., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Enright, F.M., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Gilmore, W.C., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Briggs, R.E., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Loan, R.W., Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Respiratory tract infections with viruses and Pasteurella spp. were determined sequentially among 26 cattle that died during two severe epizootics of shipping fever pneumonia. Nasal swab and serum samples were collected prior to onset of the epizootics, during disease progression, and after death, when necropsies were performed and lung samples were collected. Eighteen normal control cattle also were sampled at the beginning of the epizootics as well as at weekly intervals for 4 weeks. Respiratory bovine coronaviruses (RBCV) were isolated from nasal secretions of 21 and 25 cattle before and after transport. Two and 17 cattle nasally shed Pasteurella spp. before and after transport, respectively. RBCV were isolated at titers of 1 x 103 to 1.2 x 107 PFU per g of lung tissue from 18 cattle that died within 7 days of the epizootics, but not from the lungs of the remaining cattle that died on days 9 to 36. Twenty-five of the 26 lung samples were positive for Pasteurella spp., and their CFU ranged between 4.0 x 105 and 2.3 x 109 per g. Acute and subacute exudative, necrotizing lobar pneumonia characterized the lung lesions of these cattle with a majority of pneumonic lung lobes exhibiting fibronecrotic and exudative changes typical of pneumonic pasteurellosis, but other lung lobules had histological changes consisting of bronchiolitis and alveolitis typical of virus-induced changes. These cattle were immunologically naive to both infectious agents at the onset of the epizootics, but those that died after day 7 had rising antibody titers against RBCV and Pasteurella haemolytica. In contrast, the 18 clinically normal and RBCV isolation-negative cattle had high hemagglutinin inhibition antibody titers to RBCV from the beginning, while their antibody responses to P. haemolytica antigens were delayed. Evans' criteria for causation were applied to our findings because of the multifactorial nature of shipping fever pneumonia. This analysis identified RBCV as the primary inciting cause in these two epizootics. These viruses were previously not recognized as a causative agent in this complex respiratory tract disease of cattle.",,"hemagglutination inhibiting antibody; animal tissue; antibody response; antibody titer; article; blood sampling; cattle disease; colony forming unit; controlled study; Coronavirus; disease course; epizootiology; histology; Mannheimia haemolytica; nonhuman; nose smear; pneumonia; priority journal; virus isolation; virus titration; Animals; Antibodies, Bacterial; Antibodies, Viral; Cattle; Coronavirus Infections; Coronavirus, Bovine; Hemagglutination Inhibition Tests; Lung; Mannheimia haemolytica; Nasal Cavity; Pasteurella; Pasteurella multocida; Pasteurellosis, Pneumonic; Virus Shedding; Animalia; Bos taurus; Bovinae; Coronavirus; Mannheimia haemolytica; Negibacteria; Pasteurella; RNA viruses","Appel, G., Heckert, H.-P., Hofmann, W., Uber die Beteiligung von bovinem Coronavirus (BCV) am Rindergrippekomplex in Betrieben Schleswig-Holsteins (1992) Tieraerztl. 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Med., 41, pp. 212-223; Herrler, G., Rott, R., Klenk, H.D., Muller, H.P., Shukla, A.K., Schauer, R., The receptor-destroying enzyme of influenza C virus: Neuraminidate-O-acetyl-esterase (1985) EMBO J., 4, pp. 1503-1506; Hoerlein, A.B., Shipping fever (1980), pp. 99-106. , H. E. Amstutz (ed.), Bovine medicine and surgery. American Veterinary Publications, Inc., Santa Barbara, Calif; Hoerlein, A.B., Saxena, S.P., Mansfield, M.E., Studies on shipping fever of cattle. II. Prevalence of Pasteurella species in nasal secretions from normal calves and calves with shipping fever (1961) Am. J. Vet. Res., 22, pp. 470-472; Jakab, G.J., Mechanisms of virus-induced bacterial superinfection on the lung (1981) Clin. Chest Med., 2, pp. 59-66; Jakab, G.J., Viral-bacterial interaction in pulmonary infections (1982) Adv. Vet. Sci. Comp. Med., 26, pp. 155-171; Jensen, R., Pierson, R.E., Brady, P.M., Saari, D.M., Lauerman, L.H., England, J.J., Keyvanfar, H., Christie, R.M., Shipping fever pneumonia in yearling feedlot cattle (1976) J. Am. Vet. Med. Assoc., 169, pp. 500-506; Jericho, K.W.F., Langford, E.V., Pneumonia in calves produced with aerosols of bovine herpesvirus 1 and Pasteurella haemolytica (1978) Can. J. Comp. Med., 42, pp. 269-277; Lin, X.Q., O'Reilly, K.L., Storz, J., Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny (1997) Am. J. Vet. Res., 58, pp. 1120-1124; Lin, X.Q., O'Reilly, K.L., Storz, J., Purdy, C.W., Loan, R.W., Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis Arch. Virol., , in press; Lin, X.Q., (2000), Isolation and characterization of newly emerging coronaviruses in acute respiratory tract diseases of cattle. Ph.D. dissertation, Louisiana State University, Baton Rouge, La; Magwood, S.E., Barnum, D.A., Thomson, R.G., Nasal bacterial flora of calves in healthy and in pneumonia-prone herds (1969) Can. J. Comp. Med., 33, pp. 237-243; McKercher, D.G., Moulton, J.E., Madin, S.H., Kendrick, J.W., Infectious bovine rhinotracheitis - A newly recognized virus disease of cattle (1957) Am. J. Vet. Res., 18, pp. 246-256; McKercher, D.G., Wada, E.M., Straub, O.C., Distribution and persistence of infectious bovine rhinotracheitis virus in experimentally infected cattle (1963) Am. J. Vet. Res., 24, pp. 510-514; Potgieter, L.N.D., McCracken, M.D., Hopkins, F.M., Walker, R.D., Gay, J.S., Experimental production of bovine respiratory tract disease with bovine viral diarrhea virus (1984) Am. J. Vet. Res., 45, pp. 1582-1585; Reisinger, R.C., Heddleston, K.L., Manthei, C.A., A myxovirus (SF-4) associated with shipping fever of cattle (1959) J. Am. Vet. Med. Assoc., 135, pp. 147-154; Saunders, J.R., Berman, D.T., Epizootiological studies of shipping fever II. Exposure of calves to pasteurellae and parainfluenza 3 virus (1964) Can. J. Comp. Med., 28, pp. 47-62; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples of cattle with signs of respiratory tract disease after shipping (1996) J. Am. Vet. Med. Assoc., 208, pp. 1452-1456; Storz, J., Respiratory disease of cattle associated with coronavirus infections (1998), pp. 291-293. , J. L. Howard and R. A. Smith (ed.), Current veterinary therapy: food animal practice, 4th ed. W. B. Saunders Co. Philadelphia, Pa; Storz, J., Purdy, C.W., Lin, X.Q., Burrell, M., Truax, R.E., Briggs, R.E., Loan, R.W., Isolation of respiratory coronaviruses, other cytocidal viruses and Pasteurella spp from cattle involved in two natural outbreaks of shipping fever (2000) J. Am. Vet. Med. Assoc., 216, pp. 1599-1604; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch. Virol., 125, pp. 193-204; Thomson, R.G., A perspective on respiratory disease of feedlot cattle Can. Vet. J., 21, pp. 181-185; Tompkins, W.A.T., Watrach, A.M., Schmale, J.D., Schultz, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J. Natl. Cancer Inst., 52, pp. 904-911; Weaver, R.E., Hollis, D.G., Gram-negative fermentative bacteria and Francisella tularensis (1980), pp. 242-262. , E. H. Lennette, A. Balows, W. J. Hausler, Jr., and J. P. Truant (ed.), Manual of clinical microbiology, 3rd ed. American Society for Microbiology, Washington, D.C; Whitely, L.O., Maheswaran, S.K., Weiss, D.J., Pasteurella haemolytica A1 and bovine respiratory disease: Pathogenesis (1992) J. Vet. Intern. Med., 6, pp. 11-22; Woolums, A.R., Anderson, M.L., Gunther, R.A., Schlelegle, E.S., La Rochelle, D.R., Singer, R.S., Boyle, G.A., Gershwin, L.J., Evaluation of severe disease induced by aerosol inoculation of calves with bovine respiratory syncytial virus (1999) Am. J. Vet. Res., 60, pp. 473-480; Yates, W.D.G., A review of infectious bovine rhinotracheitis, shipping fever pneumonia and viral-bacterial synergism in respiratory disease of cattle (1982) Can. J. Comp. Med., 46, pp. 225-263","Storz, J.; Dept. of Vet. Microbiol./Parasitol., School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; email: jstorz@mail.vetmed.lsu.edu",,,00951137,,JCMID,"10970373","English","J. Clin. Microbiol.",Article,"Final",,Scopus,2-s2.0-0033831728
"Mizutani T., Repass J.F., Makino S.","56038369800;57186535600;7403067550;","Nascent synthesis of leader sequence-containing subgenomic mRNAs in coronavirus genome-length replicative intermediate RNA",2000,"Virology","275","2",,"238","243",,9,"10.1006/viro.2000.0489","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034734770&doi=10.1006%2fviro.2000.0489&partnerID=40&md5=73b75f827c595c64b6a812900f385984","Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Mizutani, T., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Repass, J.F., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Makino, S., Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Infection with coronavirus results in the accumulation of genomic-sized mRNA and six to eight subgenomic mRNAs that make up a 3' coterminal nested-set structure. Genome-length negative-strand RNA and subgenomic-length negative-strand RNAs, each of which corresponds to each of the subgenomic mRNAs, also accumulate in infected cells. The present study examined whether the genome-length negative-strand RNA serves as a template for subgenomic mRNA synthesis. Genome-length replicative intermediate (RI) RNA was purified by two-dimensional gel electrophoresis of intracellular RNAs from cells infected with mouse hepatitis virus. RNase A treatment of the purified genome-length RI resulted in the production of the genome-length replicative form RNA, indicating that the genome-length RI included genome-length template RNA. RNase protection assays using the purified genome-length RI and two probes, which corresponded to the 5' 300-nt region of mRNA 6 and to the same region of mRNA 7, showed the presence of nascent leader sequence-containing subgenomic mRNAs in the genome-length RI. These data demonstrated that the genome-length negative-strand RNA serves as a template for subgenomic mRNA synthesis. (C) 2000 Academic Press.",,"complementary RNA; messenger RNA; ribonuclease; animal cell; animal model; article; controlled study; messenger RNA synthesis; mouse; Murine hepatitis coronavirus; nonhuman; pathophysiology; priority journal; reaction analysis; RNA analysis; virus cell interaction; virus infection","Lai, M.M., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: mRNA structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39 (3), pp. 823-834; Leibowitz, J.L., Wilhelmsen, K.C., Bond, C.W., The virus-specific intracellular RNA species of two murine coronaviruses: MHV-A59 and MHV-JHM (1981) Virology, 114 (1), pp. 39-51; Stern, D.F., Kennedy, S.I., Coronavirus multiplication strategy. II. Mapping the avian infectious bronchitis virus intracellular RNA species to the genome (1980) J. Virol., 36 (2), pp. 440-449; Lai, M.M., Patton, C.D., Baric, R.S., Stohlman, S.A., Presence of leader sequences in the mRNA of mouse hepatitis virus (1983) J. Virol., 46 (3), pp. 1027-1033; Lai, M.M., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81 (12), pp. 3626-3630; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBQ J., 2 (10), pp. 1839-1844; Jeong, Y.S., Makino, S., Evidence for coronavirus discontinuous transcription (1994) J. Virol., 68 (4), pp. 2615-2623; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86 (14), pp. 5626-5630; Sethna, P.B., Hofmann, M.A., Brian, D.A., Minus-strand copies of replicating coronavirus mRNAs contain antileaders (1991) J. Virol., 65 (1), pp. 320-325; Snijder, E.J., Meulenberg, J.J., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79 (PART 5), pp. 961-979; Baric, R.S., Stohlman, S.A., Lai, M.M., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48 (3), pp. 633-640; Baric, R.S., Yount, B., Subgenomic negative-strand RNA function during mouse hepatitis virus infection (2000) J. Virol., 74 (9), pp. 4039-4046; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64 (3), pp. 1050-1056; Schaad, M.C., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68 (12), pp. 8169-8179; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and anti-sense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96 (21), pp. 12056-12061; An, S., Maeda, A., Makino, S., Coronavirus transcription early in infection (1998) J. Virol., 72 (11), pp. 8517-8524; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139 (1), pp. 138-151; Makino, S., Soe, L.H., Shieh, C.K., Lai, M.M., Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs (1988) J. Virol., 62 (10), pp. 3870-3873; Simmons, D.T., Strauss, J.H., Replication of Sindbis virus. II. Multiple forms of double-stranded RNA isolated from infected cells (1972) J. Mol. Biol., 71 (3), pp. 615-631","Makino, S.; Dept. of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,"Academic Press Inc.",00426822,,VIRLA,"10998322","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0034734770
"Chien Chang Loa, Tsang Long Lin, Ching Ching Wu, Bryan T.A., Thacker H.L., Hooper T., Schrader D.","7409596113;7409626124;7409572853;7005517787;7007150767;7005121335;7007179253;","Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen",2000,"Avian Diseases","44","3",,"498","506",,27,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033831657&partnerID=40&md5=64205c1f212ca00544dd88d4379f00f0","Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Chien Chang Loa, Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Tsang Long Lin, Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Ching Ching Wu, Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T.A., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Thacker, H.L., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","An antibody-capture enzyme-linked immunosorbent assay (ELISA) for detection of antibody to turkey coronavirus (TCV) utilizing infectious bronchitis virus (IBV) antigen was developed. Anti-TCV hyperimmune turkey serum and normal turkey serum were used as positive or negative control serum for optimization of the ELISA system. Goat anti-turkey immunoglobulin G (light plus heavy chains) conjugated with horseradish peroxidase was used as detector antibody. The performance of the ELISA system was evaluated with 45 normal turkey sera and 325 turkey sera from the field and the cutoff point was determined. Serum samples of turkeys experimentally infected with TCV collected sequentially from 1 to 63 days postinfection were applied to the established antibody-capture ELISA using IBV antigens. The optimum conditions for differentiation between anti-TCV hyper-immune serum and normal turkey serum were serum dilution at 1:40 and conjugate dilution at 1:1600. Of the 325 sera from the field, 175 were positive for TCV by immunofluorescent antibody (IFA) assay. The sensitivity and specificity of the ELISA relative to IFA test were 93.1% and 96.7%, respectively, based on the results of serum samples from the field turkey flocks using the optimum cutoff point of 0.18 as determined by the logistic regression method. The ELISA values of all 45 normal turkey sera were completely separated from that of IFA-positive sera. The ELISA results of serum samples collected from turkeys experimentally infected with TCV were comparable to that of the IFA assay. Reactivity of anti-rotavirus, anti-reovirus, anti-adenovirus, or anti-enterovirus antibodies with the IBV antigens coated in the commercially available ELISA plates coated with IBV antigens could be utilized for detection of antibodies to TCV in antibody-capture ELISA.","Coronavirus; Enteritis; Enzyme-linked immunosorbent assay; Infectious bronchitis virus; Turkey","immunoglobulin G; virus antibody; animal; animal disease; article; Avian infectious bronchitis virus; bird disease; blood; chicken; Coronavirus; enzyme linked immunosorbent assay; goat; immunology; isolation and purification; methodology; rabbit; sensitivity and specificity; swine; turkey (bird); Animals; Antibodies, Viral; Chickens; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Enzyme-Linked Immunosorbent Assay; Goats; Immunoglobulin G; Infectious bronchitis virus; Rabbits; Sensitivity and Specificity; Swine; Turkeys","Ali, A., Reynolds, D.L., The in vitro propagation of stunting syndrome agent (1998) Avian Dis., 42, pp. 657-666; Dea, S., Tijssen, P., Detection of turkey enteric coronavirus by enzyme-linked immunosorbent assay and differentiation from other coronaviruses (1989) Am. J. Vet. Res., 50 (2), pp. 226-231; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) Am. J. Vet. Res., 35 (12), pp. 1549-1552; Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis complex/spiking mortality (1995) Avian Pathol., 24, pp. 497-505; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996), pp. 1075-1093. , Fields virology, 3rd ed. B. N. Fields, D. M. Knipe, and P. M. Howley, eds. Lippincott-Raven Publishers, Philadelphia, PA; Karaca, K., Naqi, S., Gelb J., Jr., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Dis., 36, pp. 903-915; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteriti of turkey (bluecomb disease) (1997), pp. 686-692. , Diseases of poultry, 10th ed. B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36 (8), pp. 1265-1267; (1995), SAS institute, Inc. SAS user's guide: statistics, version 6.11 ed. SAS institute, Inc., Cary, NC; Shoukri, M.M., Pause, C.A., (1999), pp. 141-203. , Statistical methods for health sciences, 2nd ed. CRC Press LLC, Boca Raton, FL","Lin, T.L.; Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States",,,00052086,,AVDIA,"11006996","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0033831657
"Uzelac-Keserović B., Vasić D., Ikonomovski J., Bojanić N., Apostolov K.","6508258267;18937799700;6506635041;55398281100;57213866586;","Isolation of a coronavirus from urinary tract tumours of endemic balkan nephropathy patients [3]",2000,"Nephron","86","1",,"93","94",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033828101&partnerID=40&md5=40f521604f60cd56f3ce3f10a007bffd","Institute of Immunobiology and Virology Torlak, Belgrade; Department of Urology, Doboj District Hospital, Doboj, Bosnia and Herzegovina; Department of Nephrology, Clinical Hospital Centre Zvezdara, Belgrade; Institute of Urology and Nephrology, Clinical Centre of Serbia, Belgrade; Biology Section, Macedonian Academy of Arts and Science, Skopje, North Macedonia; Institute of Immunobiology and Virology Torlak, Vojvode Stepe 458, 11221 Belgrade","Uzelac-Keserović, B., Institute of Immunobiology and Virology Torlak, Belgrade, Institute of Immunobiology and Virology Torlak, Vojvode Stepe 458, 11221 Belgrade; Vasić, D., Department of Urology, Doboj District Hospital, Doboj, Bosnia and Herzegovina; Ikonomovski, J., Department of Nephrology, Clinical Hospital Centre Zvezdara, Belgrade; Bojanić, N., Institute of Urology and Nephrology, Clinical Centre of Serbia, Belgrade; Apostolov, K., Biology Section, Macedonian Academy of Arts and Science, Skopje, North Macedonia",[No abstract available],,"neutralizing antibody; animal cell; clinical article; Coronavirus; endemic disease; geographic distribution; human; human tissue; immunofluorescence test; interstitial nephritis; kidney biopsy; letter; lymph node biopsy; lymph node metastasis; nonhuman; priority journal; serodiagnosis; tumor biopsy; urinary tract tumor; Vero cell; virus isolation; Animals; Balkan Nephropathy; Cercopithecus aethiops; Coronavirus; Humans; Urologic Neoplasms; Vero Cells",,"Uzelac-Keserovic, B.; Inst. of Immunobiol./Virol. 'Torlak', Vojvode Stepe 458, 11221 Belgrade, Yugoslavia; email: abn@eunet.yu",,,00282766,,NPRNA,"10971161","English","Nephron",Letter,"Final",,Scopus,2-s2.0-0033828101
"Cho K.-O., Halbur P.G., Bruna J.D., Sorden S.D., Yoon K.-J., Janke B.H., Chang K.-O., Saif L.J.","57193116476;7005935318;7006746374;7003697171;7401607376;7003826275;7404878277;7102226747;","Detection and isolation of coronavirus from feces of three herds of feedlot cattle during outbreaks of winter dysentery-like disease",2000,"Journal of the American Veterinary Medical Association","217","8",,"1191","1194",,35,"10.2460/javma.2000.217.1191","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034667219&doi=10.2460%2fjavma.2000.217.1191&partnerID=40&md5=1680fad047f3bf65e7a052c8d949268b","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States; Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States","Cho, K.-O., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States; Halbur, P.G., Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Bruna, J.D., Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Sorden, S.D., Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Yoon, K.-J., Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Janke, B.H., Veterinary Diagnostic Laboratory, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Chang, K.-O., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States",[No abstract available],,"virus antigen; animal; animal disease; article; cattle; cattle disease; cell culture; Coronavirus; differential diagnosis; dysentery; enzyme linked immunosorbent assay; epidemic; feces; female; immunoelectron microscopy; immunology; isolation and purification; large intestine; lung; lymph node; male; pathology; rectum tumor; respiratory tract infection; ultrastructure; virology; virus infection; Animals; Antigens, Viral; Cattle; Cattle Diseases; Cells, Cultured; Coronavirus Infections; Coronavirus, Bovine; Diagnosis, Differential; Disease Outbreaks; Dysentery; Enzyme-Linked Immunosorbent Assay; Feces; Female; Intestine, Large; Lung; Lymph Nodes; Male; Microscopy, Immunoelectron; Rectal Neoplasms; Respiratory Tract Infections; Tumor Cells, Cultured","Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal anti-bodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Saif, L.J., Bohl, E.H., Kohler, E.M., Immune electron microscopy of transmissible gastroenteritis virus and rotavirus (reovirus-like agent) of swine (1977) Am J Vet Res, 38, pp. 13-20; Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Haines, D.M., Clark, E.G., Dubovi, E.J., Monoclonal antibody-based immunohistochemical detection of bovine viral diarrhea virus in formalin-fixed, paraffin-embedded tissues (1992) Vet Pathol, 29, pp. 27-32; Dar, A.M., Kapil, S., Goyal, S.M., Comparison of immunohisto-chemistry, electron microscopy, and direct fluorescent antibody test for the detection of bovine coronavirus (1998) J Vet Diagn Invest, 10, pp. 151-157; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Durham, P.J.K., Hassard, E.E., Armstrong, K.R., Coronavirus-associated diarrhea (winter dysentery) in adult cattle (1989) Can Vet J, 30, pp. 825-827; Fleetwood, A.J., Edwards, S., Foxell, P.W., Winter dysentery in adult dairy cattle (1989) Vet Rec, 125, pp. 553-554; Traven, M., Silvan, A., Larsson, B., Experimental infection with bovine coronavirus (BCV) in lactating cows: Clinical disease, viral excretion, interferon-α and antibody response (1995) Bovine Pract, 29, pp. 64-65; Espinasse, J., Viso, M., Laval, A., Winter dysentery, a coronavirus-like agent in the feces of beef and dairy cattle with diarrhea (1982) Vet Rec, 110, p. 385; Akashi, H., Inaba, Y., Tokuhisa, S., Properties of a coronavirus isolated from a cow with epizootic diarrhea (1980) Vet Microbiol, 5, pp. 265-276; Akashi, H., Inaba, Y., Miura, Y., Propagation of the Kakegawa strain of bovine coronavirus in suckling mice, rats and hamsters (1981) Arch Virol, 67, pp. 367-370; Durham, P.J., Stevenson, B.J., Farquharson, B.C., Rotavirus and coronavirus associated diarrhea in domestic animal (1979) NZ Vet J, 27, pp. 30-32; Horner, G.W., Hunter, R., Kirkbried, C.A., A coronavirus-like agent present in feces of cows with diarrhea (1975) NZ Vet J, 23, p. 98; Saif, L.J., Redman, D.R., Brock, K.V., Winter dysentery in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet Rec, 123, pp. 300-301; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Takashshi, E., Inaba, Y., Sato, K., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Broes, A., Opdenbosch, E., Wellemans, G., Isolement d'un coronavirus chez des bovins atteints d'enterite hemorragique hivernale (winter dysentery) en belgique (1984) Ann Med Vet, 128, pp. 299-303; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Epidemiologic herd-level assessment of causative agents and risk factors for winter dysentery in dairy cattle (1998) Am J Vet Res, 59, pp. 994-1001; Straub, O.C., Viral respiratory infections of cattle (1995) Bovine Pract, 29, pp. 66-70; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Hasoksuz, M., Lathrop, S.L., Gadfield, K.L., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Antibody titers against bovine coronavirus and sheddine of the virus via the respiratory tract in feedlot cattle (2000) Am J Vet Res, 61, pp. 1057-1061; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am J Vet Res, 57, pp. 48-53; Tsunemitsu, H., Smith, D.R., Saif, L.J., Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coronavirus in feces by RT-PCR (1999) Arch Virol, 144, pp. 167-175","Saif, L.J.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691-4096, United States",,"American Veterinary Medical Association",00031488,,JAVMA,"11043691","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0034667219
"Lee C.-W., Jackwood M.W.","24075183200;7003643324;","Evidence of genetic diversity generated by recombination among avian coronavirus IBV",2000,"Archives of Virology","145","10",,"2135","2148",,87,"10.1007/s007050070044","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033743874&doi=10.1007%2fs007050070044&partnerID=40&md5=cc32933bbd09e0f3d4afe7185a2b20a4","Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States","Lee, C.-W., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Jackwood, M.W., Department of Avian Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States","Previously, we demonstrated that the DE072 strain of IBV is a recombinant which has an IBV strain D1466-like sequence in the S gene. Herein, we analyzed the remaining 3.8 kb 3' end of the genome, which includes Gene 3, Gene 4, Gene 5, Gene 6, and the 3' non-coding region of the DE072 and D1466 strains. Those two viruses had high nucleotide similarity in Gene 4. However, the other individual genes had a much different level of Sequence similarity with the same gene of the other IBV strains. The genome of five IBV strains, of which the complete sequence of the 3' end of the genome has been determined, were divided at an intergenic (IG) consensus sequence (CTGAACAA or CTTAACAA) and compared phylogenetically. Phylogenetic trees of different topology indicated that the consensus IG sequences and the highly conserved sequence around this regions may serve as recombination 'hot spots'. Phylogenetic analysis of selected regions of the genome of the DE072 serotype field isolates further support those results and indicate that isolates within the same serotype may have different amounts of nucleotide sequence similarity with each other in individual genes other than the S gene. Presumably this occurs because the consensus IG sequence serves as the template switching site for the viral encoded polymerase.",,"avian coronavirus; consensus sequence; gene locus; gene switching; genetic diversity; genetic recombination; genetic strain; nucleotide sequence; phylogeny; sequence homology; serotype; virus gene; Animals; Base Sequence; Coronavirus Infections; Genome, Viral; Infectious bronchitis virus; Molecular Sequence Data; Phylogeny; Poultry Diseases; Recombination, Genetic; Sequence Alignment; Sequence Analysis, DNA; Variation (Genetics)","Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J Gen Virol, 68, pp. 57-77; Cavanagh, D., Davis, P.J., Cook, J., Li, D., Kant, A., Koch, G., Location of the amino acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious bronchitis virus (1992) Avian Pathol, 21, pp. 33-43; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997), pp. 511-526. , Calnek BW, Barnes HJ, Beard CW, Reid WM, Yoder HW (eds) Disease of poultry, 10th ed. Iowa State University Press, Ames; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch Virol, 142, pp. 629-633; Davelaar, F.G., Kouwenhoven, B., Burger, A.G., Occurrence and significance of infectious bronchitis virus variant strains in egg and broiler production in the Netherlands (1984) Vet Q, 6, pp. 114-120; Gelb J., Jr., Wolff, J.B., Moran, C.A., Variant serotypes of infectious bronchitis virus isolated from commercial layer and broiler chickens (1991) Avian Dis, 35, pp. 82-87; Gelb J., Jr., Keeler C.L., Jr., Nix, W.A., Rosenberger, J.K., Cloud, S.S., Antigenic and S-1 genomic characterization of the Delaware variant serotypes of infectious bronchitis virus (1997) Avian Dis, 41, pp. 661-669; Jackwood, M.W., Kwon, H.M., Hilt, D.A., Infectious bronchitis virus detection in allantoic fluid using the polymerase chain reaction and a DNA probe (1992) Avian Dis, 36, pp. 403-409; Jarvis, T.C., Kirkegaard, K., Poliovirus RNA recombination: Mechanistic studies in the absence of selection (1992) EMBO J, 11, pp. 3135-3145; Jia, W., Karaca, K., Parrish, D.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch Virol, 140, pp. 259-271; Jia, W., Naqi, S.A., Sequence analysis of gene 3, gene 4 and gene 5 of avian infectious bronchitis virus strain CU-T2 (1997) Gene, 189, pp. 189-193; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kuster, J.G., Niesters, H.M., Bleumink-Pluym, N.M.C., Davelaar, F.G., Horzinek, M.C., Van Der Zeijst, B.A.M., Molecular epidemiology of infectious bronchitis virus in the Netherlands (1987) J Gen Virol, 68, pp. 343-352; Kusters, J.G., Niesters, H., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Kusters, J.G., Jager, E.J., Niesters, H.G.M., Van Der Zeijst, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Kwon, H.M., Jackwood, M.W., Gelb J., Jr., Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction-fragment-length-polymorphism analysis (1993) Avian Dis, 37, pp. 194-202; Lai, M.M.C., Liao, C.-L., Lin, Y.-J., Zhang, X., Coronavirus: How a large RNA viral genome is replicated and transcribed (1994) Infect Agent Dis, 3, pp. 98-105; Lee, C.-W., Jackwood, M.W., Spike gene analysis of the DE072 strain of infectious bronchitis virus: Origin and evolution (2000) Virus Genes; Siddell, S.G., The coronaviridae (1995), pp. 1-49. , Fraenkel-Conrat H, Wagner RR (eds) The viruses. Plenum Press, New York; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Swofford, D.L., (1989) PAUP: Phylogenetic analysis using parsimony, , Version 3. Illinois Natural History Survey, Champaign; Wang, L., Junker, D., Collison, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis viruses and other coronaviruses (1992) Virus Res, 25, pp. 213-222","Jackwood, M.W.; Department of Avian Medicine, University of Georgia, 953 College Station Road, Athens, GA 30602, United States",,,03048608,,ARVID,"11087096","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033743874
"Yount B., Curtis K.M., Baric R.S.","6603564156;7102811088;7004350435;","Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model",2000,"Journal of Virology","74","22",,"10600","10611",,157,"10.1128/JVI.74.22.10600-10611.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033762254&doi=10.1128%2fJVI.74.22.10600-10611.2000&partnerID=40&md5=0767428f3e41d1d9ebbe71c530efb33f","Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","Yount, B., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Curtis, K.M., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; Baric, R.S., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States","A systematic method was developed to assemble functional full-length genomes of large RNA and DNA viruses. Coronaviruses contain the largest single-stranded positive-polarity RNA genome in nature. The ~30-kb genome, coupled with regions of genomic instability, has hindered the development of a full-length infectious cDNA construct. We have assembled a full-length infectious construct of transmissible gastroenteritis virus (TGEV), an important pathogen in swine. Using a novel approach, six adjoining cDNA subclones that span the entire TGEV genome were isolated. Each clone was engineered with unique flanking interconnecting junctions which determine a precise systematic assembly with only the adjacent cDNA subclones, resulting in an intact TGEV cDNA construct of ~28.5 kb in length. Transcripts derived from the full-length TGEV construct were infectious, and progeny virions were serially passaged in permissive host cells. Viral antigen production and subgenomic mRNA synthesis were evident during infection and throughout passage. Plaque-purified virus derived from the infectious construct replicated efficiently and displayed similar plaque morphology in permissive host cells. Host range phenotypes of the molecularly cloned and wild-type viruses were similar in cells of swine and feline origin. The recombinant viruses were sequenced across the unique interconnecting junctions, conclusively demonstrating the marker mutations and restriction sites that were engineered into the component clones. Full-length infectious constructs of TGEV will permit the precise genetic modification of the coronavirus genome. The method that we have designed to generate an infectious cDNA construct of TGEV could theoretically be used to precisely reconstruct microbial or eukaryotic genomes approaching several million base pairs in length.",,"complementary DNA; messenger RNA; virus antigen; virus DNA; virus RNA; article; Coronavirus; DNA modification; gene mutation; molecular cloning; nonhuman; priority journal; RNA synthesis; sequence analysis; virion; virus assembly; virus genome; virus recombinant; virus replication; Animals; Cell Line; Cloning, Molecular; DNA, Viral; Fluorescent Antibody Technique; Genetic Markers; Genome, Viral; Mutagenesis; Mutation; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sequence Analysis, DNA; Swine; Transfection; Transmissible gastroenteritis virus; Virus Assembly","Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic sindbis virus RNA vectors for heterologous gene expression (1998) Proc. Natl. Acad. Sci. 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Virol., 74, pp. 2305-2316; Sosnovtsev, S., Green, K.Y., RNA transcripts derived from a cloned full length copy of the feline calicivirus genome do not require VpG for infectivity (1995) Virology, 210, pp. 383-390; Sumyoshi, H., Hoeke, C.M., Trent, D.W., Infectious Japanese encephalitis virus RNA can be synthesized from in vitro-ligated cDNA templates (1992) J. Virol., 66, pp. 5425-5431; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader effects mRNA efficiency (1994) Virology, 202, pp. 621-630; Tong-Chuan, H., Zhou, S., Da Costa, L.T., Yu, J., Kinzler, K.W., Vogelstein, B., A simplified system for generating recombinant adenoviruses (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 2509-2514; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, porcine, and human coronaviruses in sero-group 1 (1996) J. Virol., 70, pp. 8669-8674; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.-L., Sethna, P.B., Hogue, B.G., Brian, D.A., The 9.1 kilodalton hydrophobic protein encoded at the 3' end of the porcine transmissible gastroenteritis coronavirus genome is membrane associated (1992) Virology, 186, pp. 676-683; Van der Most, R.G., Heijnen, L., Spaan, W.J., De Groot, R.J., Homologous recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious retrovirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Van Zijl, M., Quint, W., Briaire, J., De Rover, T., Gielkens, A., Berns, A., Regeneration of herpesviruses from molecularly cloned subgenomic fragments (1988) J. Virol., 62, pp. 2191-2195; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparisons of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J. Virol., 69, pp. 3176-3184; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Whelan, S., Ball, A., Barr, J., Wertz, G., Efficient recovery of infectious vesicular stomatitis virus entirely from cDNA clones (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 8388-8392","Baric, R.S.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7400, United States; email: rbaric@sph.unc.edu",,,0022538X,,JOVIA,"11044104","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033762254
"Wang Y., Zhang X.","7601495525;55715175900;","The leader RNA of coronavirus mouse hepatitis virus contains an enhancer-like element for subgenomic mRNA transcription",2000,"Journal of Virology","74","22",,"10571","10580",,15,"10.1128/JVI.74.22.10571-10580.2000","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033759913&doi=10.1128%2fJVI.74.22.10571-10580.2000&partnerID=40&md5=babe6b62c7961743332315e7ffb1c05e","Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205, United States","Wang, Y., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205, United States; Zhang, X., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205, United States","While the 5' cis-acting sequence of mouse hepatitis virus (MHV) for genomic RNA replication has been determined in several defective interfering (DI) RNA systems, it remains elusive for subgenomic RNA transcription. Previous studies have shown that the leader RNA in the DI genome significantly enhances the efficiency of DI subgenomic mRNA transcription, indicating that the leader RNA is a cis-acting sequence for mRNA transcription. To further characterize the cis-acting sequence, we made a series of deletion mutants, all but one of which have an additional deletion of the cis-acting signal for replication in the 5' untranslated region. This deletion effectively eliminated the replication of the DI-chloramphenicol acetyltransferase (CAT)-reporter, as demonstrated by the sensitive reverse transcription (RT)-PCR. The ability of these replication-minus mutants to transcribe subgenomic mRNAs was then assessed using the DI RNA-CAT reporter system. Results from both CAT activity and mRNA transcripts detected by RT-PCR showed that a 5'-proximal sequence of 35 nucleotides (nt) at nt 25 to 59 is a cis-acting sequence required for subgenomic RNA transcription, while the consensus repeat sequence of the leader RNA does not have such effect. Analyses of the secondary structure indicate that this 35-nt sequence forms two stem-loops conserved among MHVs. Deletion of this sequence abrogated transcriptional activity and disrupted the predicted stem-loops and overall RNA secondary structure at the 5' untranslated region, suggesting that the secondary structure formed by this 35-nt sequence may facilitate the downstream consensus sequence accessible for the discontinuous RNA transcription. This may provide a mechanism by which the 5' cis-acting sequence regulates subgenomic RNA transcription. The 5'-most 24 nt are not essential for transcription, while the 9 nt immediately downstream of the leader enhances RNA transcription. The sequence between nt 86 and 135 had little effect on transcription. This study thus defines the cis-acting transcription signal at the 5' end of the DI genome.",,"cis acting element; messenger RNA; virus RNA; animal cell; article; deletion mutant; enhancer region; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; reverse transcription polymerase chain reaction; RNA analysis; RNA sequence; RNA transcription; sequence analysis; transcription regulation; 5' Untranslated Regions; Animals; Base Sequence; Chloramphenicol O-Acetyltransferase; Consensus Sequence; Enhancer Elements (Genetics); Gene Deletion; Gene Expression Regulation, Viral; Genome, Viral; Mice; Molecular Sequence Data; Murine hepatitis virus; Nucleic Acid Conformation; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; RNA, Spliced Leader; RNA, Viral; Transcription, Genetic; Transfection; Virus Replication","Baker, S.C., Lai, M.M.C., An in vitro system for the leader-primed transcription of coronavirus mRNAs (1990) EMBO J., 9, pp. 4173-4179; Baric, R.S., Yount, B., Subgenomic negative-strand RNA function during mouse hepatitis virus infection (2000) J. 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Virol., 68, pp. 8131-8140; Lin, Y.J., Zhang, X.M., Wu, R.C., Lai, M.M.C., The 3' untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA (1996) J. Virol., 70, pp. 7236-7240; Luytjes, W., Gerritsma, H., Spaan, W.J.M., Replication of synthetic defective interfering RNAs derived from coronavirus mouse hepatitis virus-A59 (1996) Virology, 216, pp. 174-183; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Lai, M.M.C., Evolution of the 5'-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Makino, S., Lai, M.M.C., High-frequency leader sequence switching during coronavirus defective interfering RNA replication (1989) J. Virol., 63, pp. 5285-5292; Makino, S., Soe, L.H., Shieh, C.K., Lai, M.M.C., Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs (1988) J. Virol., 62, pp. 3870-3873; Makino, S., Stohlman, S.A., Lai, M.M.C., Leader sequences of murine coronavirus mRNAs can be freely reassorted: Evidence for the role of free leader RNA in transcription (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 4204-4208; Pachuk, C., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J.M., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus strain A59 (1989) Virology, 171, pp. 141-148; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shieh, C.K., Lee, H.J., Yokomori, K., La Monica, N., Makino, S., Lai, M.M.C., Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus RNA genome (1989) J. Virol., 63, pp. 3729-3736; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Stohlman, J.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 95, pp. 12056-12061; Williams, G.D., Chang, R.Y., Brian, D.A., A phylogenetically conserved hairpin-type 3' untranslated region pseudoknot functions in coronavirus RNA replication (1999) J. Virol., 73, pp. 8349-8355; Zhang, X.M., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633; Zhang, X.M., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X.M., Lai, M.M.C., A 5'-proximal RNA sequence of murine coronavirus as a potential initiation site for genomic-length mRNA transcription (1996) J. Virol., 70, pp. 705-711; Zhang, X.M., Liao, C.-L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746; Zuker, M., On finding all suboptimal foldings of an RNA molecule (1989) Science, 244, pp. 48-52","Zhang, X.; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205, United States; email: zhangxuming@exchange.uams.edu",,,0022538X,,JOVIA,"11044101","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0033759913
"Reddy P.S., Idamakanti N., Zakhartchouk L.N., Babiuk L.A., Mehtali M., Tikoo S.K.","16943768100;6602833966;6603473850;35427029400;56607974600;7005561263;","Optimization of bovine coronavirus hemagglutinin-estrase glycoprotein expression in E3 deleted bovine adenovirus-3",2000,"Virus Research","70","1-2",,"65","73",,4,"10.1016/S0168-1702(00)00209-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033758904&doi=10.1016%2fS0168-1702%2800%2900209-4&partnerID=40&md5=5d5e99ee1109539542758eba4e1e79e9","Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Gene Therapy Department, Transgene S.A., 67000 Strasbourg, France","Reddy, P.S., Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Idamakanti, N., Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Zakhartchouk, L.N., Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Babiuk, L.A., Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; Mehtali, M., Gene Therapy Department, Transgene S.A., 67000 Strasbourg, France; Tikoo, S.K., Virology Group, Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada","Adenoviral vectors expressing foreign genes have many desirable properties in applications such as vaccination. Recently, we have generated replication-competent (E3 deleted) bovine adenovirus-3 (BAV-3) recombinants expressing significant amounts of glycoprotein D (gD) of bovine herpesvirus-1 (a DNA virus). However, attempts to express the RNA virus genes using the same strategy were not successful. In an effort to optimize the expression, we have constructed several BAV-3 recombinants carrying the hemagglutinin esterase (HE) gene of bovine coronavirus (BCV) in the E3 region with or without exogenous transcription control elements. The expression studies suggest that the introduction of a 137 bp chimeric intron upstream of the HE cDNA is able to increase the level of HE gene expression. The introduction of a SV40 early promoter or human cytomegalovirus (HCMV) immediate early (IE) promoter into the expression cassette changed the kinetics of the HE expression. However, the recombinant BAV-3 containing HE under the HCMV IE promoter replicated less efficiently than the wild-type BAV-3. These studies should prove useful in expression of other RNA viral genes in the E3 region of BAV-3 expression system. (C) 2000 Elsevier Science B.V.","Bovine adenovirus-3; Bovine coronavirus; Gene expression","complementary DNA; esterase; glycoprotein D; hemagglutinin esterase; unclassified drug; virus enzyme; virus glycoprotein; virus vector; Adenovirus; adenovirus 3; article; Coronavirus; gene expression; gene expression system; genetic transfection; Herpes simplex virus 1; Human cytomegalovirus; immediate early gene; intron; nonhuman; nucleotide sequence; priority journal; promoter region; Simian virus 40; virus recombinant; virus replication; Adenovirus E3 Proteins; Animals; Blotting, Northern; Blotting, Southern; Cattle; Cell Line; Coronavirus, Bovine; Gene Deletion; Genetic Vectors; Hemagglutinins, Viral; Humans; Mastadenovirus; Precipitin Tests; Recombinant Proteins; Viral Fusion Proteins","Baca-Estrada, M.E., Liang, L., Babiuk, L.A., Yoo, D., Induction of mucosal immunity in cotton rats to haemagglutinin-esterase glycoprotein of bovine coronavirus by recombinant adenovirus (1995) Immunology, 86, pp. 134-140; Baxi, M.K., Babiuk, L.A., Mehtali, M., Tikoo, S.K., Transcription map and expression of bovine herpesvirus-1 glycoprotein D in early region 4 of bovine adenovirus-3 (1999) Virology, 261, pp. 143-152; Breker-Klassen, M.M., Yoo, D., Mittal, S.K., Sorden, S.D., Haines, D.M., Babiuk, L.A., Recombinant adenovirus type 5 expressing bovine parainfluenza virus type 3 glycoproteins protect Sigmodon hispidus cotton rats from bovine parainfluenza virus type 3 infection (1995) J. Virol., 69, pp. 4308-4315; Carswell, S., Alwine, J.C., Efficiency of utilization of the simian virus 40 late polyadenylation site: Effects of upstream sequences (1989) Mol. Cell. Biol., 9, pp. 4248-4258; Chariter, C., Degryse, E., Gantzer, M., Dieterie, A., Pavirani, A., Mehtali, M., Efficient generation of recombinant adenovirus vectors by homologous recombination in Escherichia coli (1996) J. Virol., 70, pp. 4805-4810; Chomczynski, P., Sacchi, N., Single step method of RNA isolation by acid guanidium thiocynate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoprotein E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; Hirt, B., Selective extraction of polyoma DNA from infection of mouse cultures (1967) J. Mol. Biol., 26, pp. 365-369; Huang, M.T., Gorman, C.M., The simian virus 40 small-t intron, present in many common expression vectors, leads to aberrant splicing (1990) Mol. Cell. Biol., 10, pp. 1805-1810; Idamakanti, N., Reddy, P.S., Babiuk, L.A., Tikoo, S.K., Transcription mapping and characterization of 284R and 121R produced from early region 3 of bovine adenovirus type 3 (1999) Virology, 256, pp. 351-359; Jackson, R.J., Standart, N., Do the poly(A) tail and 3' untranslated region control mRNA translation (1990) Cell, 62, pp. 15-24; King, B.G., Brian, D.A., Bovine coronavirus structural proteins (1982) J. Virol., 42, pp. 700-707; Niiyama, Y., Igarashi, K., Tsukamoto, K., Kurokawa, T., Sugino, Y., Biochemical studies on bovine adenovirus type-3. I. Purification and properties (1975) J. Virol., 16, pp. 621-633; Papp, Z., Middleton, D.M., Mittal, S.K., Babiuk, L.A., Baca-Estrada, M.E., Mucosal immunization with recombinant adenoviruses: Induction of immunity and protection of cotton rats against respiratory bovine herpesvirus type 1 infection (1997) J. Gen. Virol., 78, pp. 2933-2943; Parker, M.D., Cox, G.J., Deregt, D., Fitzpatrick, D.R., Babiuk, L.A., Cloning and in vitro expression of the gene for the E3 haemagglutinin glycoprotein of bovine coronavirus (1989) J. Gen. Virol., 70, pp. 155-164; Reddy, P.S., Idamakanti, N., Chen, Y., Whale, T., Babiuk, L.A., Mehtali, M., Tikoo, S.K., Replication-defective bovine adenovirus type 3 as an expression vector (1999) J. Virol., 73, pp. 9137-9144; Reddy, P.S., Idamakanti, I., Zakhartchouk, A.N., Baxi, M.K., Lee, J.B., Pyne, C., Babiuk, L.A., Tikoo, S.K., Nucleotide sequence, genome organization, and transcription map of bovine adenovirus type 3 (1998) J. Virol., 72, pp. 1394-1402; Reddy, P.S., Nagy, E., Derbyshire, J.B., Restriction endonuclease analysis and molecular cloning of porcine adenovirus type 3 (1993) Intervirol., 36, pp. 161-168; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning: A laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory Press, Cold Spring harbour, NY; Senapathy, P., Shapiro, M.B., Harris, N.L., Splice junctions, branch point sites, and exons: Sequence statistics, identification, and applications to genome project (1990) Meth. Enzymol., 183, pp. 252-278; Tollefson, A.E., Scaria, A., Saha, S.K., Wold, W.S.M., The 11 600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection (1992) J. Virol., 66, pp. 3633-3642; Waltner-Toews, D., Martin, S.W., Meek, A.H., McMillan, I., Crouch, C.F., A field trial to evaluate the efficacy of a combined rotavirus-coronavirus/E. coli vaccine in dairy cattle (1995) Can. J. Comp. Med., 49, pp. 1-7; Yoo, D., Graham, F.L., Prevec, F.L., Parker, M.D., Benko, M., Zamb, T., Babiuk, L.A., Synthesis and processing of haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus (1992) J. Gen. Virol., 73, pp. 2591-2600; Zakhartchouk, A.N., Pyne, C., Mutwiri, G.K., Papp, Z., Baca-Estrada, M., Griebel, P., Babiuk, L.A., Tikoo, S.K., Mucosal immunization of calves with recombinant bovine adenovirus-3: Induction of protective immunity to bovine herpesvirus-1 (1999) J. Gen. Virol., 80, pp. 1263-1269; Zakhartchouk, A.N., Reddy, P.S., Baxi, M., Baca-Estrada, M.E., Mehtali, M., Babiuk, L.A., Tikoo, S.K., Construction and Characterization of E3 deleted bovine adenovirus type 3 expressing full-length and truncated form of bovine herpesvirus type 1 glycoprotein gD (1998) Virology, 250, pp. 220-229; Ziff, E.B., Fraser, N., Adenovirus type 2 late mRNA, structural evidence for 3'-coterminal species (1978) J. Virol., 25, pp. 897-906","Tikoo, S.K.; Virology Group, Veterinary Infect. Dis. Organization, University of Saskatchewan, Saskatoon, Sask. S7N 5E3, Canada; email: tikoo@sask.usask.ca",,,01681702,,VIRED,"11074126","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0033758904
"Cologna R., Spagnolo J.F., Hogue B.G.","7801604385;6508353146;7003393593;","Identification of nucleocapsid binding sites within coronavirus-defective genomes",2000,"Virology","277","2",,"235","249",,34,"10.1006/viro.2000.0611","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034715821&doi=10.1006%2fviro.2000.0611&partnerID=40&md5=2e74602259a956c1623e687ecb4ca416","Baylor College of Medicine, Department of Molecular Virology and Microbiology, Houston, TX 77030, United States; Southwestern Foundation for Biomedical Research, Department of Molecular Virology and Microbiology, San Antonio, TX 78227, United States","Cologna, R., Baylor College of Medicine, Department of Molecular Virology and Microbiology, Houston, TX 77030, United States, Southwestern Foundation for Biomedical Research, Department of Molecular Virology and Microbiology, San Antonio, TX 78227, United States; Spagnolo, J.F., Baylor College of Medicine, Department of Molecular Virology and Microbiology, Houston, TX 77030, United States; Hogue, B.G., Baylor College of Medicine, Department of Molecular Virology and Microbiology, Houston, TX 77030, United States","The coronavirus nucleocapsid (N) protein is a major structural component of virions that associates with the genomic RNA to form a helical nucleocapsid. N appears to be a multifunctional protein since data also suggest that the protein may be involved in viral RNA replication and translation. All of these functions presumably involve interactions between N and viral RNAs. As a step toward understanding how N interacts with viral RNAs, we mapped high-efficiency N-binding sites within BCV- and MHV-defective genomes. Both in vivo and in vitro assays were used to study binding of BCV and MHV N proteins to viral and nonviral RNAs. N-viral RNA complexes were detected in bovine coronavirus (BCV)-infected cells and in cells transiently expressing the N protein. Filter binding was used to map N-binding sites within Drep, a BCV-defective genome that is replicated and packaged in the presence of helper virus. One high-efficiency N-binding site was identified between nucleotides 1441 and 1875 at the 3' end of the N ORF within Drep. For comparative purposes N-binding sites were also mapped for the mouse hepatitis coronavirus (MHV)-defective interfering (DI) RNA MIDI-C. Binding efficiencies similar to those for Drep were measured for RNA transcripts of a region encompassing the MHV packaging signal (nts 3949-4524), as well as a region at the 3' end of the MHV N ORF (nts 4837-5197) within MIDI-C. Binding to the full-length MIDI-C transcript (˜5500 nts) and to an ˜1-kb transcript from the gene 1 a region (nts 935-1986) of MIDI-C that excluded the packaging signal were both significantly higher than that measured for the smaller transcripts. This is the first identification of N-binding sequences for BCV. It is also the first report to demonstrate that N interacts in vitro with sequences other than the packaging signal and leader within the MHV genome. The data clearly demonstrate that N binds coronavirus RNAs more efficiently than nonviral RNAs. The results have implications with regard to the multifunctional role of N. (C) 2000 Academic Press.",,"nucleocapsid protein; nucleotide; virus RNA; article; binding site; Coronavirus; helper virus; Murine hepatitis coronavirus; nonhuman; open reading frame; priority journal; protein expression; protein interaction; RNA replication; RNA transcription; RNA translation; virus genome; virus nucleocapsid","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Abraham, S., Kienzle, T.E., Lapps, W.E., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Virol., 65, pp. 3219-3226; Wang, Y., Zhang, X., The nucleocapsid protein of coronavirus mouse hepatitis virus interacts with the cellular heterogeneous nuclear ribonucleoprotein A1 in vitro and in vivo (1999) Virology, 265, pp. 96-109; Weiss, B., Geigenmuller-Gnirke, U., Schlesinger, S., Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site (1994) Nucleic Acids Res., 22, pp. 780-786; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Yamanaka, K., Ishihama, A., Nagata, K., Reconstitution of influenza virus RNA-nucleoprotein complexes structurally resembling native viral ribonucleoprotein cores (1990) J. Biol. Chem., 265, pp. 11151-11155; Zhang, X., Lai, M.M., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644",,,,00426822,,,"11080472","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0034715821
"Guy J.S., Breslin J.J., Breuhaus B., Vivrette S., Smith L.G.","7202723649;7004753945;6603913949;6604075939;37109180900;","Characterization of a coronavirus isolated from a diarrheic foal",2000,"Journal of Clinical Microbiology","38","12",,"4523","4526",,75,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034459757&partnerID=40&md5=a067fcdee2f59e193887388397abc563","North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States","Guy, J.S., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States; Breslin, J.J., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States; Breuhaus, B., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States; Vivrette, S., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States; Smith, L.G., North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States","A coronavirus was isolated from feces of a diarrheic foal and serially propagated in human rectal adenocarcinoma (HRT-18) cells. Antigenic and genomic characterizations of the virus (isolate NC99) were based on serological comparison with other avian and mammalian coronaviruses and sequence analysis of the nucleocapsid (N) protein gene. Indirect fluorescent-antibody assay procedures and virus neutralization assays demonstrated a close antigenic relationship with bovine coronavirus (BCV) and porcine hemagglutinating encephalomyelitis virus (mammalian group 2 coronaviruses). Using previously described BCV primers, the N protein gene of isolate NC99 was amplified by a reverse transcriptase PCR (RT-PCR) procedure. The RT-PCR product was cloned into pUC19 and sequenced; the complete N protein of NC99 (446 amino acids) was then compared with published N protein sequences of other avian and mammalian coronaviruses. A high degree of identity (89.0 to 90.1%) was observed between the N protein sequence of NC99 and published sequences of BCV (Mebus and F15 strains) and human coronavirus (strain OC43); only limited identity (<25%) was observed with group 1 and group 3 coronaviruses. Based on these findings, the virus has been tentatively identified as equine coronavirus (ECV). ECV NC99 was determined to have close antigenic and/or genetic relationships with mammalian group 2 coronaviruses, thus identifying it as a member of this coronavirus antigenic group.",,"guanine nucleotide binding protein; nucleocapsid protein; virus antigen; amino acid sequence; article; Coronavirus; diarrhea; feces; fowl; gene amplification; gene sequence; nonhuman; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; sequence homology; virus detection; virus isolation; virus neutralization; Amino Acid Sequence; Animals; Capsid; Coronavirus; Coronavirus OC43, Human; Diarrhea; Feces; Horse Diseases; Horses; Humans; Microscopy, Electron; Molecular Sequence Data; Phylogeny; Polymerase Chain Reaction; Aves; Bovinae; Bovine coronavirus; Coronavirus; Equidae; Equine coronavirus; Galliformes; human coronavirus; Mammalia; Porcine hemagglutinating encephalomyelitis virus; RNA viruses; Suidae","Bass, E.P., Sharpee, R.L., Coronavirus and gastroenteritis in foals (1975) Lancet, 2, p. 822; Boursnell, M.E., Binns, M.M., Foulds, I.J., Brown, T.D., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995), pp. 165-179. , S. G. Siddell (ed.),The coronaviridae. Plenum Press, New York, N.Y; Cruciere, C., Laporte, J., Sequence analysis of bovine enteritic coronavirus (F15) genome. I. Sequence of the gene coding the nucleocapsid protein; analysis of the predicted protein (1988) Ann. Inst. Pasteur, 139, pp. 123-138; Davis, E., Rush, B.R., Cox, J., DeBey, B., Kapil, S., Neonatal enterocolitis associated with coronavirus infection in a foal: A case report (2000) J. Vet. Diagn. Investig., 12, pp. 153-156; Durham, P.J.K., Stevenson, B.J., Farquhanson, B.C., Rotavirus and coronavirus associated diarrhea in domestic animals (1979) N. Z. Vet. J., 27, pp. 30-32; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis, 35, pp. 197-203; Gay, J.S., Barnes, H.J., Smith, L.G., Rapid diagnosis of infectious laryngotracheitis using a monoclonal antibody-based immunoperoxidase procedure (1992) Avian Pathol., 21, pp. 77-86; Guy, J.S., Brian, D.A., Bovine coronavirus genome (1979) J. Virol., 29, pp. 293-300; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996), 1, pp. 1075-1093. , B. N. Fields. D M. Knipe, and P. M. Howley (ed.), Fundamental virology, 3rd ed., Lippincott-Raven Publishers, Philadelphia, Pa; Huang, J.C.M., Wright, S.L., Shipley, W.D., Isolation of coronavirus-like agent from horses suffering from acute equine diarrhea syndrome (1983) Vet. Rec., 113, pp. 262-263; Kamahora, T., Soe, L.H., Lai, M.M., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Kapke, P.A., Brian, D.A., Sequence analysis of the porcine transmissible gastroenteritis coronavirus nucleocapsid protein gene (1986) Virology, 151, pp. 41-49; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Mair, T.S., Taylor, F.G.R., Harbour, D.A., Pearson, G.R., Concurrent cryptosporidium and coronavirus infections in an Arabian foal with immunodeficiency syndrome (1990) Vet. Rec., 126, pp. 127-130; Majhdi, F., Mocha, H.C., Kapil, S., Isolation and characterization of a coronavirus from elk calves with diarrhea (1997) J. Clin. Microbiol., 35, pp. 2937-2942; Murphy, F.A., Virus taxonomy (1996), 1, pp. 15-57. , B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fundamental virology, 3rd ed., Lippincott-Raven Publishers, Philadelphia, Pa; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Pedersen, N.C., Antigenic relationship of feline infectious peritonitis virus to coronaviruses of other species (1978) Arch. Virol, 58, pp. 45-53; Robb, J.A., Bond, C.W., Coronaviridae (1979), pp. 193-247. , H. Fraenkel-Conrat and R. R. Wagner (ed.), Comprehensive virology, vol. 14. Plenum Press, New York, NY; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning: a laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y; Schreibner, S.S., Kamahora, T., Lai, M.M., Sequence analysis of the nucleocapsid protein of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Sharpee, R.L., Mebus, C.A., Bass, E.P., Characterization of a calf diarrheal coronavirus (1976) Am. J. Vet. Res., 37, pp. 1031-1041; Siddell, S.G., The Coronaviridae: An introduction (1995) Coronaviridae, pp. 1-9. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Siddell, S.G., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, H.D., Macnaughton, M.R., Pensaert, M., Zeijst, B.A.M.V.D., (1993) Coronaviridae. Intervirology, 20, pp. 181-189; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Res., 25, pp. 4876-4882; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Res., 25, pp. 213-222","Guy, J.S.; North Carolina State University, College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606, United States; email: Jim_Guy@ncsu.edu",,,00951137,,JCMID,"11101590","English","J. Clin. Microbiol.",Article,"Final",,Scopus,2-s2.0-0034459757
"Lin X.Q., O'Reilly K.L., Storz J., Purdy C.W., Loan R.W.","36768282000;7103313844;7006694594;7004943441;7004131337;","Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis",2000,"Archives of Virology","145","11",,"2335","2349",,26,"10.1007/s007050070024","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034520107&doi=10.1007%2fs007050070024&partnerID=40&md5=84feb16c83669f5aca516c87cc3a5679","Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA, United States; Conservation and Production Research Laboratory, USDA, ARS, Bushland, TX, United States; Department of Veterinary Pathobiology, Texas A and M University, College Station, TX, United States","Lin, X.Q., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA, United States; O'Reilly, K.L., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA, United States; Storz, J., Department of Veterinary Microbiology and Parasitology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA, United States; Purdy, C.W., Conservation and Production Research Laboratory, USDA, ARS, Bushland, TX, United States; Loan, R.W., Department of Veterinary Pathobiology, Texas A and M University, College Station, TX, United States","Antibody responses against respiratory bovine coronavirus (RBCV) infections were monitored in cattle from the onset of a naturally occurring severe shipping fever (SF) epizootic to complete recovery of affected cattle or fatal outcomes. The infection with RBCV was detected in nasal secretions of 86 cattle, and 81 of them developed acute respiratory tract disease, including fatal pneumonia. Cattle nasally shedding RBCV at the beginning of the epizootic experienced characteristic primary immune responses with specific antibodies for hemagglutininesterase (HE) and spike (S) glycoproteins. Virus shedding in nasal secretions of the majority of the cattle ceased between days 7 and 14 with the appearance of HE- and S-specific antibodies. Nasal samples and lung tissues from 9 of the 10 fatal cases had high titers of RBCV, but these cattle had only IgM responses to RBCV infections. Cattle remaining negative in RBCV isolation tests entered this epizootic with antibodies against HE and S. Protection against respiratory tract disease was apparently associated with high level of opsonic and virus-neutralizing IgG2. The HE and S glycoproteins were recognized earliest by the bovine immune system while the N protein induced antibody responses during the later stage of initial infection and the early stage of reinfection. The membrane (M) glycoprotein was the least immunogenic of the major viral structural proteins.",,"antibody specificity; bovine coronavirus; cattle disease; cattle; guanine nucleotide binding protein; hemagglutinin esterase; host resistance; immune response; immunoglobulin G2; induced resistance; virus antibody; virus infection; virus infectivity; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Nasal Mucosa; Pasteurellosis, Pneumonic; Respiratory Tract Infections; Viral Structural Proteins; Virus Shedding","Brown, T.D.K., Brierly, I., The coronavirus non-structural proteins (1995), pp. 191-217. , Siddell SG (ed) The Coronaviridae. Plenum Press, New York; Butler, J.E., Bovine immunoglobulins: A review (1969) J Dairy Sci, 52, pp. 1895-1909; Chouljenko, V.N., Kousoulas, K.G., Lin, X.Q., Storz, J., Genetic analysis of respiratory bovine coronavirus strains from fatal pneumonia of cattle (1998) Proceedings of the Seventy-ninth Conference of Research Workers on Animal Diseases, p. 149. , Chicago, Illinois; Chouljenko, V.N., Kousoulas, K.G., Lin, X.Q., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J Gen Virol, 70, pp. 993-998; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-2877; Duncan, J.R., Wilkie, B.N., Hiestand, F., Winter, A.J., The serum and secretory immunoglobulins of cattle: Characterization and quantitation (1972) J Immunol, 108, pp. 965-976; Guidry, A.J., Berning, L.M., Hambleton, C.N., Opsonization of Staphylococcus aureus by bovine immunoglobulin isotypes (1993) J Dairy Sci, 76, pp. 1285-1289; Heckert, R.A., Saif, L.J., Mengel, J.P., Myers, G.W., Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces, and mucosal secretions from experimentally challenge-exposed colostrum-deprived calves (1991) Am J Vet Res, 52, pp. 692-699; Hoerlein, A.B., Shipping fever in bovine medicine and surgery (1980), pp. 99-106. , Amstutz HE (ed) Bovine medicine and surgery. American Veterinary Publications, Santa Barbara; Hogue, B.G., Kienzle, T.E., Brian, D.A., Synthesis and processing of the bovine enteric coronavirus hemagglutinin protein (1989) J Gen Virol, 70, pp. 345-352; Kimman, T.G., Daha, M.R., Brinkhof, J.M.A., Westenbrink, F., Activation of complement by bovine respiratory syncytial virus-infected cells (1989) Vet Immunol Immunopathol, 21, pp. 311-325; Kimman, T.G., Terpstra, G.K., Daha, M.R., Westenbrink, F., Pathogenesis of naturally acquired bovine respiratory syncytial virus infection in calves: Evidence for the involvement of complement and mast cell mediators (1989) Am J Vet Res, 5, pp. 694-700; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu Rev Microbiol, 44, pp. 303-333; LeJan, C., Asso, J., The local and systemic immune response of calves following experimental infection with IBR virus (1980), pp. 677-692. , Butler JE (ed) The ruminant immune system. Plenum Press, New York; Lin, X.Q., Chouljenko, V.N., Kousoulas, K.G., Storz, J., Hemagglutinin-esterase specified by respiratory bovine coronaviruses has temperature-sensitive acetylesterase activity (2000) J Med Microbiol, 49, pp. 849-864; McGuire, T.C., Musoke, A.J., Biologic activities of bovine IgG subclasses (1980), pp. 359-366. , Butler JE (ed) The ruminant immune system. Plenum Press, New York London; McGuire, T.C., Musoke, A.J., Kurtti, T., Functional properties of bovine IgG1 and IgG2: Interaction with complement, macrophages, neutrophils and skin (1979) Immunology, 38, pp. 249-256; McGuire, T.C., Pfeiffer, N.D., Weikel, J.M., Bartsch, R.C., Failure of colostral immunoglobulin transfer in calves dying from infectious disease (1976) J Am Vet Med Assoc, 169, pp. 713-718; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a corona-like agent (1973) Am J Vet Res, 34, pp. 145-150; Nansen, P., (1970) Metabolism of bovine immunoglobulin-G, , Thesis, Royal Veterinary and Agricultural University, Copenhagen; Potgieter, L.N.D., The influence of complement on the neutralization of IBR by globulins derived from early and late bovine antisera (1975) Can J Comp Med, 39, pp. 427-433; Rossi, C.R., Kisesel, G.K., Antibody class and complement requirement of neutralizing antibodies in the primary and secondary response of cattle to IBR vaccines (1976) Arch Virol, 51, pp. 191-196; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet Rec, 123, pp. 300-301; Schmidt, O.W., Kenny, G.E., Polypeptides and functions of antigens from human coronaviruses 229E and OC43 (1982) Infect Immun, 32, pp. 1000-1006; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetyl-neuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J Gen Virol, 74, pp. 901-906; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronavirus: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Stohlman, S.A., Kyuwa, S., Polo, J.M., Brady, D., Lai, M.M.C., Bergmann, C.C., Characterization of mouse hepatitis virus-specific cytotoxic T cells derived from the central nervous system of mice infected with the JHM strain (1993) J Virol, 67, pp. 7050-7059; Storz, J., Respiratory disease of cattle associated with coronavirus infections (1998), pp. 291-293. , Howard JL, Smith RA (ed) Current veterinary therapy: food animal practice 4. WB Saunders, Philadelphia; Storz, J., Lin, X.Q., Purdy, C.W., Loan, R.W., Novel diagnostics for defining virus infections in shipping fever pneumonia: Emergence of respiratory bovine coronaviruses (1999) Proceedings of the Fourth International Symposium of World Association of Veterinary Laboratory Diagnosticians, College Station, pp. 54-60; Storz, J., Lin, X.Q., Purdy, C.W., Chouljenko, V.N., Kousoulas, K.G., Enright, F.M., Gilmore, W.C., Loan, R.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans' criteria of causation (2000) J Clin Microbiol, 38, pp. 3082-3090; Storz, J., Purdy, C.W., Lin, X.Q., Burrell, M., Truax, R.E., Briggs, R.E., Frank, G.H., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp from cattle involved in two natural outbreaks of shipping fever (2000) J Am Vet Med Assoc, 216, pp. 1-6; Storz, J., Rott, R., Über die verbreitung der coronavirusinfektion bei rindern in ausgewählten Gebieten Deutschlands: Antikörpernachweis durch mikroimmundiffusion und neutralisation (1980) Dtsch Tierärztl Wochenschr, 87, pp. 252-254; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med Microbiol Immunol, 169, pp. 169-178; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples of cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1454; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Williams, M.R., Spooner, R.L., Quantitative studies on bovine immunoglobulins (1975) Vet Rec, 96, pp. 81-84; Worku, M., Paape, M.J., Marquardt, W.W., Modulation of Fc receptors for IgG on bovine polymorphonuclear neutrophils by interferon-γ through de novo RNA transcription and protein synthesis (1994) Am J Vet Res, 55, pp. 234-238; Yates, W.D.G., A review of infectious bovine rhinotracheitis, shipping fever pneumonia and viral-bacterial synergism in respiratory disease of cattle (1982) Can J Comp Med, 46, pp. 225-263; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 44, pp. 152-161","Storz, J.; Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Med., Baton Rouge, LA 70803, United States",,,03048608,,ARVID,"11205121","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034520107
"Pfister K., Jaber P., Wolfender F., Carel S.","55539273000;6505847105;57199612258;6603268105;","A new specific immunoglobulin preparation for the prevention of neonatal calf diarrhoea [Ein neues spezifisches Immunglobulinpräparat für die Prophylaxe von neonatalen Kälberdurchfällen]",2000,"Tierarztliche Praxis Ausgabe G: Grosstiere - Nutztiere","28","5",,"260","263",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034365062&partnerID=40&md5=e697f73c18bb7a0fd8d5bc39fe50b6cc","Biokema AG, Crissier/Lausanne, Switzerland; Biokema AG, Ch. de la Chatanerie 2, CH-1023 Crissier/Lausanne, Switzerland","Pfister, K., Biokema AG, Crissier/Lausanne, Switzerland; Jaber, P., Biokema AG, Crissier/Lausanne, Switzerland; Wolfender, F., Biokema AG, Ch. de la Chatanerie 2, CH-1023 Crissier/Lausanne, Switzerland; Carel, S., Biokema AG, Crissier/Lausanne, Switzerland","The preparation is a newly developed, colostrum-derived bovine immunoglobulin concentrate containing ≥2.8 log10/ml specific IgG against E. coli F5 (K99) antigen and IgG antibodies against Rota-and Coronavirus (mean concentration: 2.7 log10/ml, resp. 3.8 log10/ml). The aim of the administration of this specifically concentrated immunoglobulin solution is to provide newborn calves with additional immunoglobulins in order to supplement the protective characteristics of normal colostrum against neonatal calf diarrhoea. The administration of the preparation in a controlled field study with 121 newborn calves (60 ml perorally within the first four and 12 hours post partum, respectively) showed that the product is well accepted and tolerated and does not lead to any adverse reactions or secondary effects. The calves treated with the product showed a decreased frequency of diarrhoea in their first days of life and a slight reduction of the number of ""sick-days"" per calf during the period of examination. Thus, the results clearly indicate that this immunoglobulin concentrate provides an additional protection for the control of the mostly multifactorial neonatal calf-diarrhoea.","Colostrum; Coronavirus; Diarrhoea; E. Coll f5 (k99) antigen; Immunoglobulin; Newborn calves; Prophylaxis; Rotavirus",,"Baljer, G., Wieler, L., Ätiologie, Pathogenese und Immunprophylaxe der neonatalen Durchfallerkrankungen der Kälber (1989) VET 6, 5, pp. 18-26; Berchtold, M., Zaremba, W., Grunert, E., Kälberkrankheiten (1990) Neugeborenen- und Säuglingskunde der Tiere, pp. 260-335. , Walser K, Bostedt H, Hrsg. Stuttgart: Enke; Fey, H., (1972) Colibacillosis in Calves, , Bern: Huber; Heckert, H.P., Bardella, I., Hofmann, W., Oltmer, S., Untersuchung zum Einfluß eines antikörperhaltigen Volleipulvers auf die ak- Tive Immunitätsausbildung bei Kälbern (1999) Dtsch Tierärztl Wschr, 106, pp. 10-14; Leresche, E., Porta, B., Passive protection of calves with an oral immunoglobuline preparation in farms with severe neonatal mortality/morbidity (1988) Proceed. 15th World Congress for Buiatrics, pp. 32-43. , Palma de Mallorca; Luginbühl, A., Pfister, K., Die Kryptosporidiose des Kalbes als schwerwiegendes Bestandsproblem (1996) Schweiz Arch Tierheilk, 138, pp. 195-200; Me Cullogh, W.P., (1996) The Effects of Giving a Colostral Supplement to Newborn Calves before Suckling, , University of Liverpool: BSc Diploma; Meltzer, R., Shpigel, N.Y., Etiologic and epidemiologic aspects of calf diarrhoea in Israeli dairy farms (1996) Proceed BCVA Edinburgh, 1, pp. 93-97; Panier, C.M.L., (1985) Les Gastroentérites Néonatales du Veau. Essai de Prévention de La Colibacillose Entérotoxinogène À Escherichia Coli K99 Par un Immun-sérocolostrum. Suivi Sérologique, , Université Paul Sabatier Toulouse: Thèse doctorat vétérinaire; Rosenberger, G., (1970) Krankheiten Des Rindes, , Berlin, Hamburg: Parey; Schelcher, F., De Rycke, J., Martel, J.L., Diarrhées colibacillaires néonatales du veau (1993) Le Point Vétérinaire, 25, pp. 611-623; Schelcher, F., Bichef, H., Valarcher, J.F., Les vaccinations contre les gastro-entérites diarrhéiques du nouveau-né: Que peut-on en attendre? (1998) Le Point Vétérinaire, 29, pp. 35-42; Spillmann, S.K., Eckert, J., Merk, W., Frey, R., Zum Vorkommen von Kryptosporidien bei Kälbern in der Schweiz (1986) Schweiz Arch Tierheilk, 128, pp. 111-118; White, D.G., Johnson, C.K., Cracknell, V., Comparison of danofloxacin with baguiloprim/sulphadimidine for the treatment of experimentally induced Escherichia coli diarrhoea in calves (1998) Vet Rec, 143, pp. 273-276","Pfister, K.; Biokema AG, Crissier/Lausanne, Switzerland",,,14341220,,,,"German","Tierarztl. Prax. Ausg. G. Grosstiere Nutztiere",Article,"Final",,Scopus,2-s2.0-0034365062
"Aho L.S., Simon I., Bour J.B., Morales-Gineste L., Pothier P., Gouyon J.B.","7006362152;16146955400;6603799482;6508221334;7006986336;24283906900;","Epidemiology of viral nosocomial infections in pediatrics [Épidémiologie des infections nosocomiales virales en pédiatrie]",2000,"Pathologie Biologie","48","10",,"885","892",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034519010&partnerID=40&md5=ec873e0f20c281762f71fd1126403b61","Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France","Aho, L.S., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; Simon, I., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; Bour, J.B., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; Morales-Gineste, L., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; Pothier, P., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; Gouyon, J.B., Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France","Nosocomial viral infections account for at least 5 % of the total of NI and reach 23 % in pediatric wards. The nosocomial infection (NI) incidence rate varies from 0.59 to 0.72 per 100 patients in pediatric wards. Many viruses have been associated with NI in pediatric wards. Rotavirus and respiratory syncytial virus (RSV) are the most frequent. Other viruses frequently identified are : Calicivirus, adenovirus, astrovirus, influenza et para-influenza, rhinovirus and coronavirus. Asymptomatic infections occur frequently. The period of communicability varies and depends on the virus. It often begins before the clinical signs appear and ends after the healing. Viral shedding may be intermittent. Children and hospital environment and less frequently hospital staff are the main source for the virus. Poor handwashing results in direct spread to patient or self-inoculation even for respiratory viruses like RSV and rhinovirus. The main risk factors for NI are prolonged hospital stay, past history of prematurity and low age. Immunocompromised patients constitute a special high-risk group. Understaffing is also a risk factor. Minimal infective doses depend on the route of inoculation and the kind of virus. Low doses are for example sufficient for rotavirus, adenovirus and calicivirus. Viral inactivation is all the more easy when there is an envelope. Handwashing and appropriate isolation (technical and geographical) are the mainstay of prevention of viral NI. Vaccines are promising, especially for rotavirus. © 2000 Éditions scientifiques et médicales Elsevier SAS.","Epidemiology; Nosocomial infections; Pediatric ward; Viral infections","Adenovirus; Astrovirus; Calicivirus; child; Coronavirus; hand washing; high risk population; hospital infection; hospitalization; human; hygiene; immune deficiency; incidence; infant; Influenza virus; Parainfluenza virus; pediatric hospital; Respiratory syncytial pneumovirus; review; Rhinovirus; risk factor; Rotavirus; virus inactivation; virus infection; virus isolation; virus shedding; cross infection; newborn; pediatrics; virology; virus infection; Child; Cross Infection; Humans; Infant; Infant, Newborn; Pediatrics; Respiratory Syncytial Virus Infections; Rotavirus Infections","Ford-Jones, E.L., Mindorff, C.M., Gold, R., Petric, M., The incidence of viral-associated diarrhea after admission to a pediatric hospital (1990) Am J Epidemiol, 131 (SUPPL. 4), pp. 711-718; Glass, R.I., Kilgore, P.E., Holman, R.C., The epidemiology of rotavirus in the United States : Surveillance and estimates of disease burden (1996) J Infect Dis, 174 (SUPPL. 1), pp. 5-11; Valenti, W.M., Menegus, M.A., Hall, C.B., Pincus, P.H., Douglas R.G., Jr., Nosocomial viral infection: I. 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Epidemiologic observations of rhinovirus infections, 1965-1969, in family with young children (1975) Am J Epidemiol, 101, pp. 122-143; Brummitt, C.F., Cherrington, J.M., Katzenstein, D.A., Nosocomial adenovirus infections : Molecular epidemiology of an outbreak due to adenovirus 3a (1988) J Infect Dis, 158 (SUPPL. 2), pp. 423-432; Fox, J.P., Hall, C.E., Cooney, M.K., The Seattle virus watch. VII. Observations of adenovirus infections (1977) Am J Epidemiol, 105, pp. 362-386","Aho, L.S.; Service d'Épidemiologie, Hôpital du Bocage, CHU, BP 1542, 21034 Dijon Cedex, France; email: ludwig.aho@chu-dijon.fr",,,03698114,,PTBIA,"11204919","French","Pathol. Biol.",Review,"Final",,Scopus,2-s2.0-0034519010
"Zhang X., Liu R.","55715175900;55187319300;","Identification of a noncanonical signal for transcription of a novel subgenomic mRNA of mouse hepatitis virus: Implication for the mechanism of coronavirus RNA transcription",2000,"Virology","278","1",,"75","85",,12,"10.1006/viro.2000.0637","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034610251&doi=10.1006%2fviro.2000.0637&partnerID=40&md5=246ad1be641ccf2cab5d177d52cbfec2","Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205-7199, United States","Zhang, X., Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205-7199, United States; Liu, R., Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205-7199, United States","Subgenomic RNA transcription of coronaviruses involves the interaction between the leader (or antileader) and the intergenic (IG) sequences. However, it is not clear how these two sequences interact with each other. In this report, a previously unrecognized minor species of subgenomic mRNA, termed mRNA5-1, was identified in cells infected with mouse hepatitis virus (MHV) strains JHM2c, JHM(2), JHM(3), A59, and MHV-1. Sequence analysis revealed that the leader-body fusion site of the mRNA is located at approximately 150 nucleotides (nt) downstream of the consensus IG sequence for mRNA 5 and did not have sequence homology with any known IG consensus sequences. To determine whether this sequence functions independently as a promoter, we cloned a 140-nt sequence (from ≃70 nt upstream to ≃70 nt downstream of the fusion site) from viral genomic RNA and placed it in front of a reporter gene in the defective-interfering (DI) RNA-chloramphenicol acetyltransferase (CAT) reporter vector. Transfection of the reporter RNA into MHV-infected cells resulted in synthesis of a CAT-specific subgenomic mRNA detected by reverse transcription-polymerase chain reaction (RT-PCR). The strength of this promoter was similar to that of the IG7 (for mRNA 7) as measured by the CAT activity. Deletion analysis showed that the sequence as few as 13 nt was sufficient to initiate mRNA transcription, while mutations within the 13-nt abolished mRNA transcription. In vitro translation study confirmed that the envelope (E) protein was translated from mRNA5-1, which encodes the open reading frame (ORF) 5b at its 5'-end, indicating that mRNA5-1 is a functional message. Furthermore, when the ORF5b was replaced with the CAT gene and placed in the DI in the context of viral mini-genome, CAT was expressed not only from the first ORF of mRNA5-1 but also from the second and third ORF of mRNA5 and genomic DI RNA, respectively, suggesting that more than one mechanism is involved in regulation of ORF5b expression. Our findings thus support the notion that base-pairing between the leader (or antileader) and the IG is not the sole mechanism in subgenomic RNA transcription. (C) 2000 Academic Press.",,"article; Coronavirus; Murine hepatitis coronavirus; nonhuman; priority journal; RNA synthesis; RNA transcription; sequence analysis; signal transduction; Animalia; Coronavirus; DNA viruses; Felis catus; Macropodid herpesvirus type 1; Murinae; Murine hepatitis virus; RNA viruses","Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3'-end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, R.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. 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Plenum, New York; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J.E., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBQ J., 15, pp. 2020-2028; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zhang, X.M., Heterogeneity of subgenomic mRNAs of a mutant mouse hepatitis virus strain JHM2c (2000), The Nidoviruses (E. Lavi et al., Eds.), Plenum, New York; Zhang, X.M., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633; Zhang, X.M., Lai, M.M.C., Interaction between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with amount of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X.M., Liao, C.L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746; Zhang, X.M., Hinton, D.R., Cue, D., Stohlman, S.A., Lai, M.M.C., Expression of gamma interferon by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread and pathogenicity (1997) Virology, 233, pp. 327-338; Zhang, X.M., Hinton, D.R., Parra, B., Park, S., Liao, C.L., Lai, M.M.C., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Zhang, X.; Dept. of Microbiology and Immunology, University of Arkansas for Med. Sci., 4301 W. Markham St., Little Rock, AR 72205, United States; email: zhangxuming@exchange.uams.edu",,"Academic Press Inc.",00426822,,VIRLA,"11112483","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0034610251
"Kennedy M., Citino S., Dolorico T., McNabb A.H., Moffat A.S., Kania S.","7402308045;7004240019;6507361271;7004662201;35978947500;24177256900;","Detection of feline coronavirus infection in captive cheetahs (Acinonyx jubatus) by polymerase chain reaction",2001,"Journal of Zoo and Wildlife Medicine","32","1",,"25","30",,13,"10.1638/1042-7260(2001)032[0025:DOFCII]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042131935&doi=10.1638%2f1042-7260%282001%29032%5b0025%3aDOFCII%5d2.0.CO%3b2&partnerID=40&md5=a12347b073330e4e69ad122bcce48b74","Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States; White Oak Conservation Center, 3823 Owens Road, Yulee, FL 32097-2145, United States; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States","Kennedy, M., Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States, Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States; Citino, S., White Oak Conservation Center, 3823 Owens Road, Yulee, FL 32097-2145, United States; Dolorico, T., Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States; McNabb, A.H., Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States; Moffat, A.S., Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States; Kania, S., Comparative Medicine Department, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States","Feline coronavirus genetic elements were detected by polymerase chain reaction from blood, fecal samples, and effusive fluid collected from 33 cheetahs in the U.S.A. Feline coronavirus-specific serum antibodies were also measured by indirect immunofluorescence. Ten cheetahs were positive for viral shedding by polymerase chain reaction, whereas 13 were seropositive by immunofluorescence. Results of serology did not consistently correlate with shedding of virus, and the capture antigen used for detection of feline coronavirus-specific antibodies had a significant impact on results. Testing of samples from one population over a 1-yr period indicated chronic infection in some animals. These relatively healthy carrier animals were a source of virus for contact animals. Screening programs in cheetah populations for feline coronavirus infection may be most reliable if a combination of serologic analysis and viral detection by polymerase chain reaction is used.","Acinonyx jubatus; Cheetah; Epidemiology; Feline coronavirus; Feline infectious peritonitis; Polymerase chain reaction","Acinonyx jubatus; Animalia; Coronavirus; Felidae; Feline coronavirus; Felis catus; virus antibody; virus RNA; animal; animal disease; article; blood; cheetah; chronic disease; Coronavirus; epidemiology; exudate; feces; female; fluorescent antibody technique; genetics; immunology; isolation and purification; male; methodology; polymerase chain reaction; United States; virology; virus infection; virus shedding; zoo animal; Acinonyx; Animals; Animals, Zoo; Antibodies, Viral; Chronic Disease; Coronaviridae Infections; Coronavirus, Feline; Exudates and Transudates; Feces; Female; Fluorescent Antibody Technique, Indirect; Male; Polymerase Chain Reaction; RNA, Viral; Seroepidemiologic Studies; United States; Virus Shedding","Evermann, J.F., Feline coronavirus infection of cheetahs (1986) Feline Pract., 16, pp. 21-30; Evermann, J.F., Heeney, J.L., McKeirnan, A.J., O'Brien, S.J., Comparative features of a coronavirus isolated from a cheetah with feline infectious peritonitis (1989) Virus Res., 13, pp. 15-28; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Am. Vet. Med. Assoc., 210, pp. 1307-1312; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35, pp. 673-675; Harpold, L.M., Legendre, A.M., Kennedy, M.A., Plummer, P.J., Millsaps, K., Rohrbach, B., Fecal shedding of feline coronavirus in adult cats and kittens in an Abyssinian cattery (1999) J. Am. Vet. Med. Assoc., 215, pp. 948-951; Heeney, J.L., Evermann, J.F., McKeirnan, A.J., Marker-Kraus, L., Roelke, M.E., Bush, M., Wildt, D.E., O'Brien, S.J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) J. Virol., 64, pp. 1964-1972; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., DeGroot, R.J., Feline coronavirus type n strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronavirus: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hoskins, J.D., Coronavirus infection in cats (1993) Veterinary Clinics of North America: Small Animal Practice, pp. 1-16. , Hoskins, J. D., and A. S. Loar (eds.). W. B. Saunders Co., Philadelphia, Pennsylvania; Kennedy, M.A., Brenneman, K., Millsaps, R.K., Black, J., Potgieter, L.N.D., Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis (1998) J. Vet. Diagn. Invest., 10, pp. 93-97; Kennedy, M.A., Dolorico, T., McNabb, A.H., Moffatt, A.S., Stylianides, E., Van Vuuren, M., Kania, S., Genetic detection of feline coronavirus in cheetahs (Acinonyx jubatus) (1999) Proc. Conf. Res. Work. Anim. Dis., 1999, p. 230. , Chicago, Illinois. Iowa State University Press, Ames, Iowa; Kiss, I., Kecskemeti, S., Tanyi, J., Klingeborn, B., Belak, S., Preliminary studies on feline coronavirus distribution in naturally and experimentally infected cats (2000) Res. Vet. Sci., 68, pp. 237-242; O'Brien, S.J., Roelke, M.E., Marker, L., Newman, A., Winkler, C.A., Meltzer, D., Colly, L., Wildt, D.E., Genetic basis for species vulnerability in the cheetah (1985) Science, 227, pp. 1428-1434; Pfeifer, M.L., Evermann, J.F., Roelke, M.E., Gallina, A.M., Ott, R.L., McKeirnan, A.J., Feline infectious peritonitis in a captive cheetah (1983) J. Am. Vet. Med. Assoc., 183, pp. 1317-1319; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Vennema, H., Rossen, J.W.A., Wesseling, J., Horzinek, M.C., Rottier, P.J.M., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 91, pp. 134-140","Kennedy, M.; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37901-1071, United States",,"American Association of Zoo Veterinarians",10427260,,,"12790391","English","J. Zoo Wildl. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0042131935
"Thiel V., Herold J., Schelle B., Siddell S.G.","35238592100;7006838690;6602866326;7005260816;","Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus",2001,"Journal of General Virology","82","6",,"1273","1281",,151,"10.1099/0022-1317-82-6-1273","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034969913&doi=10.1099%2f0022-1317-82-6-1273&partnerID=40&md5=c8b715b013b98c21c4809538c0ac045b","Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","Thiel, V., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Herold, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Schelle, B., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","The coronavirus genome is a positive-strand RNA of extraordinary size and complexity. It is composed of approximately 30 000 nucleotides and it is the largest known autonomously replicating RNA. It is also remarkable in that more than two-thirds of the genome is devoted to encoding proteins involved in the replication and transcription of viral RNA. Here, a reverse-genetic system is described for the generation of recombinant coronaviruses. This system is based upon the in vitro transcription of infectious RNA from a cDNA copy of the human coronavirus 229E genome that has been cloned and propagated in vaccinia virus. This system is expected to provide new insights into the molecular biology and pathogenesis of coronaviruses and to serve as a paradigm for the genetic analysis of large RNA virus genomes. It also provides a starting point for the development of a new class of eukaryotic, multi-gene RNA vectors that are able to express several proteins simultaneously.",,"complementary DNA; protein; virus RNA; virus vector; animal cell; article; controlled study; Coronavirus; genetic analysis; human; human cell; in vitro study; molecular cloning; nonhuman; nucleotide sequence; priority journal; protein expression; RNA transcription; Vaccinia virus; virus genome; virus recombinant; virus strain; Animalia; Coronavirus; Eukaryota; human coronavirus; Human coronavirus 229E; RNA viruses; Vaccinia; Vaccinia virus","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceedings of the National Academy of Sciences, USA, 97, pp. 5516-5521; Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.D., Smith, J.A., Struhl, K., (1987) Current Protocols in Molecular Biology, , (editors) New York: John Wiley; Bredenbeek, P.J., Rice, C.M., Animal RNA virus expression systems (1992) Seminars in Virology, 3, pp. 297-310; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses (2000) Journal of General Virology, 81, pp. 1473-1484; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) Journal of Virology, 71, pp. 5148-5160; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herold, J., Thiel, V., Siddell, S.G., A strategy for the generation of infectious RNAs and autonomously replicating RNAs based on the HCV 229E genome (1998) Advances in Experimental Medicine and Biology, 440, pp. 265-268; Hsue, B., Masters, P.S., Insertion of a new transcriptional unit into the genome of mouse hepatitis virus (1999) Journal of Virology, 73, pp. 6128-6135; Izeta, A., Smerdou, C., Alonso, S., Pénzes, Z., Mendez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) Journal of Virology, 73, pp. 1535-1545; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) Journal of Virology, 74, pp. 1393-1406; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; McIntosh, K., Coronaviruses (1996) Fields Virology, pp. 1095-1103. , 3rd edn, Edited by B.N. Fields, D.M. Knipe & P.M. Howley. Philadelphia: Lippincott-Raven; Mackett, M., Smith, G.L., Moss, B., The construction and characterisation of vaccinia virus recombinant expressing foreign genes (1985) DNA Cloning: A Practical Approach, pp. 191-211. , Edited by D.M. Glover. Oxford: IRL Press; Mandl, C.W., Aberle, J.H., Aberle, S.W., Holzmann, H., Allison, S.L., Heinz, F.X., In vitro-synthesized infectious RNA as an attenuated live vaccine in a flavivirus model (1998) Nature Medicine, 4, pp. 1438-1440; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Advances in Virus Research, 53, pp. 245-264; Mawassi, M., Satyanarayana, T., Gowda, S., Albiach-Marti, M.R., Robertson, C., Dawson, W.O., Replication of heterologous combinations of helper and defective RNA of citrus tristeza virus (2000) Virology, 267, pp. 360-369; Mayr, A., Malicki, K., Attenuation of virulent fowlpox virus in tissue culture and characteristics of the attenuated virus (1966) Zentralblatt für Veterinärmedizin, 13, pp. 1-13. , (in German); Meinkoth, J., Wahl, G., Hybridization of nucleic acids immobilized on solid supports (1984) Analytical Biochemistry, 138, pp. 267-284; Merchlinsky, M., Moss, B., Introduction of foreign DNA into the vaccinia virus genome by in vitro ligation: Recombination-independent selectable cloning vectors (1992) Virology, 190, pp. 522-526; Moss, B., Poxviridae: The viruses and their replication (1996) Fields Virology, pp. 2637-2671. , 3rd edn, Edited by B.N. Fields, D.M. Knipe & P.M. Howley. Philadelphia: Lippincott-Raven; Myint, S., Harmsen, D., Raabe, T., Siddell, S.G., Characterization of a nucleic acid probe for the diagnosis of human coronavirus 229E infections (1990) Journal of Medical Virology, 31, pp. 165-172; Raabe, T., Siddell, S., Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 and mRNA 5 unique regions (1989) Nucleic Acids Research, 17, p. 6387; Raabe, T., Siddell, S.G., Nucleotide sequence of the gene encoding the membrane protein of human coronavirus 229 E (1989) Archives of Virology, 107, pp. 323-328; Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E (1990) Journal of General Virology, 71, pp. 1065-1073; Repass, J.F., Makino, S., Importance of the positive-strand RNA secondary structure of a murine coronavirus defective interfering RNA internal replication signal in positive-strand RNA synthesis (1998) Journal of Virology, 72, pp. 7926-7933; Ruggli, N., Rice, C.M., Functional cDNA clones of the Flaviviridae: Strategies and applications (1999) Advances in Virus Research, 53, pp. 183-207; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Advances in Experimental Medicine and Biology, 440, pp. 215-219; Siddell, S.G., Snijder, E.J., Coronaviruses, toroviruses and arteriviruses (1998) Topley & Wilson's Microbiology and Microbial Infections, pp. 463-484. , 9th edn, Edited by B.W.J. Mahy & L. Collier. London: Arnold; Smith, G.L., Moss, B., Infectious poxvirus vectors have capacity for at least 25 000 base pairs of foreign DNA (1983) Gene, 25, pp. 21-28; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., van der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO Journal, 2, pp. 1839-1844; Stalcup, R.P., Baric, R.S., Leibowitz, J.L., Genetic complementation among three panels of mouse hepatitis virus gene 1 mutants (1998) Virology, 241, pp. 112-121; Thiel, V., Rashtchian, A., Herold, J., Schuster, D.M., Guan, N., Siddell, S.G., Effective amplification of 20-kb DNA by reverse transcription PCR (1997) Analytical Biochemistry, 252, pp. 62-70; van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proceedings of the National Academy of Sciences, USA, 96, pp. 12056-12061; Williams, G.D., Chang, R.Y., Brian, D.A., A phylogenetically conserved hairpin-type 3′ untranslated region pseudoknot functions in coronavirus RNA replication (1999) Journal of Virology, 73, pp. 8349-8355; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) Journal of Virology, 74, pp. 10600-10611; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) Journal of General Virology, 81, pp. 853-879","Siddell, S.G.; Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; email: siddell@vim.uni-wuerzburg.de",,"Society for General Microbiology",00221317,,JGVIA,"11369870","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034969913
"Ismail M.M., Cho K.O., Hasoksuz M., Saif L.J., Saif Y.M.","36793864500;57193116476;6603236044;7102226747;35563198200;","Antigenic and genomic relatedness of turkey-origin coronaviruses, bovine coronaviruses, and infectious bronchitis virus of chickens",2001,"Avian Diseases","45","4",,"978","984",,12,"10.2307/1592877","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035544241&doi=10.2307%2f1592877&partnerID=40&md5=578f48bafd8a2bbf923e0ccbd8004e1f","Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States","Ismail, M.M., Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Cho, K.O., Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Hasoksuz, M., Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Saif, Y.M., Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States","In earlier studies in our laboratory, we found that bovine coronavirus (BCV) was pathogenic for 1-day-old turkey poults. This finding prompted us to study the antigenic and genomic relatedness of turkey origin coronaviruses (TOCVs) to BCV. A one-step reverse transcription (RT) - polymerase chain reaction (PCR) targeting a 730-base pair fragment of the nucleocapsid (N) gene of BCV and a nested PCR targeting a 407-base pair fragment of the N gene were used in an attempt to detect TOCV from North Carolina, Indiana, and a prototype turkey coronavirus (TCV) obtained from the American Type Culture Collection. Both the one-step RT-PCR and the nested PCR amplified cell culture - passaged isolates of calf diarrhea strains of BCV but none of the 15 tested TOCVs or transmissible gastroenteritis coronavirus of swine. TOCVs also did not cross-react in a BCV antigen-capture (AC) enzyme-linked immunosorbent assay (ELISA) system with monoclonal antibodies (MAbs) against N, spike glycoprotein, and hemagglutinin esterase glycoprotein proteins of BCV as coating antibodies. The same TOCVs could be detected with primers designed from the genome of infectious bronchitis virus (IBV) of chickens. These primers amplified a 1082-base pair region spanning portions of the membrane glycoprotein (M) and N protein genes of IBV and TCV. The TOCVs also cross-reacted in an AC-ELISA with MAbs against the M and subunit 2 of spike glycoprotein of IBV.","Bluecomb; Bovine coronavirus; Infectious bronchitis virus; Poult enteritis and mortality syndrome; Turkey coronavirus","Animalia; Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; DNA viruses; Gallus gallus; Meleagris gallopavo; Sus scrofa; Transmissible gastroenteritis virus; Turkey coronavirus; monoclonal antibody; nucleocapsid protein; virus antigen; virus DNA; animal; animal disease; article; Avian infectious bronchitis virus; cattle; chick embryo; chicken; classification; Coronavirus; cross reaction; enzyme linked immunosorbent assay; gene amplification; genetics; germfree animal; immunology; nucleotide sequence; reverse transcription polymerase chain reaction; turkey (bird); virus gene; Animals; Antibodies, Monoclonal; Antigens, Viral; Base Sequence; Cattle; Chick Embryo; Chickens; Coronavirus, Bovine; Coronavirus, Turkey; Cross Reactions; DNA, Viral; Enzyme-Linked Immunosorbent Assay; Gene Amplification; Genes, Viral; Infectious bronchitis virus; Nucleocapsid Proteins; Reverse Transcriptase Polymerase Chain Reaction; Specific Pathogen-Free Organisms; Turkeys","Andreasen, J.R., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis., 35, pp. 216-220; Breslin, J.J., Smith, L.G., Fuller, F.G., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 4, pp. 22-29; Cho, K.-O., Hasoksuz, M., Nielson, P.R., Chang, K.O., Lathrop, S., Saif, L.J., Cross-protection studies between respiratory and calf diarrhea or winter dysentery coronavirus strains in calves and RT-PCR and nested PCR for their detection (2001) Arch. Virol., , In press; Chomczynski, P., Sacchi, N., Single step method of RNA isolation by acid guanidinium thiocyanate-phenol chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Dea, S., Verbeek, A.J., Tijssen, P., Transmissible enteritis of turkeys: Experimental inoculation studies with tissue-culture-adapted turkey and bovine coronaviruses (1991) Avian Dis., 35, pp. 767-777; Guy, J., Barnes, H.J., Smith, L.J., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis and mortality syndrome - Affected turkeys (1997) Avian Dis., 41, pp. 583-590; Guy, S.J., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses: A review (2000) Avian Pathol., 29, pp. 207-212; Hasoksuz, M.H., Lathrop, S.L., Gadfield, K.L., Saif, L.J., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am. J. Vet. Res., 60, pp. 1227-1233; Ismail, M.M., Cho, K.-O., Ward, L.A., Saif, L.J., Saif, Y.M., Experimental bovine coronavirus in turkey poults and young chickens (2001) Avian Dis., 45, pp. 157-163; Karaca, K., Naqi, S., Gelb Jr., J., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Dis., 36, pp. 903-915; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990) Viral diarrhea of man and animals, pp. 185-236. , L. J. Saif and K. W. Theil, eds. CRC Press, Inc., Boca Raton, FL; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J. Vet. Diagn. Invest., 8, pp. 99-105; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol., 140, pp. 1303-1311; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666; Xu, L., Harbour, D., McCrae, M.A., The application of polymerase chain reaction to the detection of rotaviruses in feces (1990) J. Virol. Methods, 27, pp. 29-38; Yu, M., Tang, Y., Guo, M., Zhang, Q., Saif, Y.M., Characterization of a small round virus associated with the poult enteritis and mortality syndrome (2000) Avian Dis., 44, pp. 600-610","Saif, Y.M.; Food Animal Health Research Program, Ohio Agricultural Res./Devt. Ctr., Ohio State University, Wooster, OH 44691, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11785902","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0035544241
"Ismail M.M., Cho K.O., Ward L.A., Saif L.J., Saif Y.M.","36793864500;57193116476;7201849705;7102226747;35563198200;","Experimental bovine coronavirus in turkey poults and young chickens",2001,"Avian Diseases","45","1",,"157","163",,31,"10.2307/1593023","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035067471&doi=10.2307%2f1593023&partnerID=40&md5=18e484b935479b58baa231c4dd307965","Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States","Ismail, M.M., Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Cho, K.O., Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Ward, L.A., Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States; Saif, Y.M., Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States","The DB2 calf strain of bovine coronavirus (BCV) was used to inoculate 1-day-old specific-pathogen-free (SPF) turkey poults in three trials. In all trials, the birds developed clinical signs of enteritis at 48-72 hr postinoculation. Birds euthanatized at 3, 5, and 7 days postinoculation (DPI) had flaccid, pale intestines with watery contents, and the ceca were markedly enlarged with frothy contents. Coronavirus particles were detected by immune electron microscopy with BCV antibodies from the intestinal contents of birds killed at 3, 5, 7, and 12 DPI. Body weights of inoculated poults killed at 3, 5, and 7 DPI were significantly reduced as compared with controls. Hemagglutinating antibodies were detected in sera of convalescent birds at 12 DPI. However, experimental inoculation of 1-day-old SPF chicks in two trials with the same virus resulted in no clinical signs or macroscopic or microscopic lesions. No coronaviruses were detected from intestinal contents, and there were no significant differences in body weights of inoculated and noninoculated control chicks.","Bluecomb; Bovine coronavirus; Chickens; Diarrhea; Enteritis; Poult enteritis and mortality syndrome; Turkey coronavirus","Animalia; Aves; Bovinae; Bovine coronavirus; Coronavirus; Gallus gallus; Meleagris gallopavo; Turkey coronavirus","Akashi, H., Inaba, Y., Miurai, Y., Sato, K., Tokuhisa, S., Asagi, M., Havashi, Y., Propagation of the Kakegawa strain of bovine coronavirus in suckling mice, rats and hamsters (1981) Arch. Virol., 67, pp. 367-370; Dea, S., Garzon, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (bluecomb) coronaviruses in a continuous human rectal adenocarcinoma cell line (1989) Am. J. Vet. Res., 50, pp. 1310-1318; Dea, S., Tijssen, P., Viral agents associated with outbreaks of diarrhea in turkey flocks in Quebec (1988) Can. J. Vet. Res., 52, pp. 53-57; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine coronaviruses (1990) J. Virol., 64, pp. 3112-3118; Dea, S., Verbeek, A., Tijssen, P., Transmissible enteritis of turkeys: Experimental inoculation studies with tissue-culture-adapted turkey and bovine coronaviruses (1991) Avian Dis., 35, pp. 767-777; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) Am. J. Vet. Res., 35, pp. 1549-1552; Goodwin, M.A., Latimer, K.S., Nersessian, B.N., Fletcher, O.J., Quantitation of intestinal D-xylose absorption in normal and reovirus-inoculated turkeys (1984) Avian Dis., 28, pp. 959-967; Guy, J., Barnes, H.J., Smith, L.J., Breslin, J., Antigenic characterization ora turkey coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Guy, J.S., Virus infections of the gastrointestinal tract of poultry (1998) Poult. Sci., 77, pp. 1166-1175; Hayhow, C.S., Saif, Y.M., Experimental infection of specific-pathogen-free turkey poults with single and combined enterovirus and group A rotavirus (1993) Avian Dis., 37, pp. 546-557; Heckert, R.A., Saif, L.J., Myers, G.W., Development of protein A-gold immunoelectron microscopy for detection of bovine coronavirus in calves: Comparison with ELISA and direct immunofluorescence of nasal epithelial cells (1989) Vet. Microbiol., 19, pp. 217-231; McNulty, M.S., Rotavirus infections (1997) Diseases of poultry, 10th ed., pp. 692-701. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, LA; McNulty, M.S., Allan, G.M., Stuart, J.C., Rotavirus infection in avian species (1978) Vet. Rec., 103, pp. 319-320; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a coronavirus like agent (1973) Vet. Pathol., 10, pp. 45-64; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of poultry, 10th ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, LA; Reynolds, D.L., Saif, Y.M., Astrovirus: A cause of an enteric disease in turkey poults (1986) Avian Dis., 30, pp. 728-735; Reynolds, D.L., Saif, Y.M., Theil, K.W., Enteric viral infections of turkey poults: Incidence of infection (1987) Avian Dis., 31, pp. 272-276; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990), pp. 185-236. , Viral diarrhea of man and animals. L. J. Saif and K. W. Theil, eds. CRC Press, Inc., Boca Raton, FL; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am. J. Vet. Res., 47, pp. 1426-1432; Saif, L.J., Saif, Y.M., Theil, K.W., Enteric viruses of diarrheic turkey poults (1985) Avian Dis., 29, pp. 798-811; Saif, Y.M., Saif, L.J., Hofacre, C.L., Hayhow, C., Swayne, D.E., Dearth, R.N., A small round virus associated with enteritis in turkey poults (1990) Avian Dis., 34, pp. 762-764; Snedecor, G.W., Cochran, W.G., One way classifications; analysis of variance (1980) Statistical methods, 7th ed., pp. 215-237. , Iowa State University Press, Ames, LA; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666","Saif, Y.M.; Food Animal Health Research Program, Ohio Agricult. Res. and Devt. Ctr., Ohio State University, Wooster, OH 44691, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11332477","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0035067471
"Dessau R.B., Lisby G., Frederiksen J.L.","6603866036;6603928311;7102315536;","Coronaviruses in brain tissue from patients with multiple sclerosis",2001,"Acta Neuropathologica","101","6",,"601","604",,13,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034926146&partnerID=40&md5=7e0bca485f51c3b2de31368168b750b9","Dept. of Clinical Microbiology 75K2, Herlev University Hospital, 2730 Herlev, Denmark","Dessau, R.B., Dept. of Clinical Microbiology 75K2, Herlev University Hospital, 2730 Herlev, Denmark; Lisby, G., Dept. of Clinical Microbiology 75K2, Herlev University Hospital, 2730 Herlev, Denmark; Frederiksen, J.L., Dept. of Clinical Microbiology 75K2, Herlev University Hospital, 2730 Herlev, Denmark","Brain tissue from 25 patients with clinically definite multiple sclerosis (MS) and as controls brain tissue from 36 patients without neurological disease was tested for the presence of human coronaviral RNA. Four PCR assays with primers specific for N-protein of human coronavirus strain 229E and three PCR assays with primers specific for the nucleocapsid protein of human corona-virus strain OC43 were performed. Sporadic positive PCR assays were observed in both patients and controls in some of the PCR assays. However, these results were not reproducible and there was no difference in the proportion of positive signals from the MS patients compared to controls. Evidence for a chronic infection with the human coronaviruses strain 229E or OC43 in brain tissue from patients with MS or controls has not been found in this study.","Brain; Coronavirus; Multiple sclerosis; Polymerase chain reaction","guanine nucleotide binding protein; nucleocapsid protein; virus RNA; adult; aged; article; brain tissue; clinical article; controlled study; Coronavirus; human; human tissue; multiple sclerosis; neurologic disease; nucleotide sequence; polymerase chain reaction; priority journal; reproducibility; signal transduction; virus infection; Adult; Aged; Aged, 80 and over; Brain; Coronavirus; DNA Primers; Female; Humans; Male; Middle Aged; Multiple Sclerosis; Myelin Basic Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral","Arbour, N., Bonavia, A., Yong, V.W., Newcombe, J., Dessau, R.B., Talbot, P.J., Human coronaviruses and multiple sclerosis: Detection by RT-PCR in human brains and infection of primary cultures of neural cells (1996), Abstracts of the Xth International Congress of Virology, Jerusalem; Armitage, P., Berry, G., Further analysis of qualitative data (1987) Statistical Methods in Medical Research, pp. 371-407. , Blackwell, Oxford; Barthold, S.W., Smith, A.L., Viremic dissemination of mouse hepatitis virus-JHM following intranasal inoculation of mice (1992) Arch Virol, 122, pp. 35-44; Burks, J.S., DeVald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Cabirac, G.F., Soike, K.F., Zhang, J.Y., Hoel, K., Butunoi, C., Cai, G.Y., Johnson, S., Murray, R.S., Entry of coronavirus into primate CNS following peripheral infection (1994) Microbiol Pathog, 16, pp. 349-357; Dessau, R.B., Coronaviruses in patients with multiple sclerosis (1997), PhD thesis, Faculty of Health Sciences, University of Copenhagen, Copenhagen; Dessau, R.B., Lisby, G., Frederiksen, J.L., Coronaviruses in spinal fluid of patients with acute monosymptomatic optic neuritis (1999) Acta Neurol Scand, 100, pp. 88-91; Dickersin, K., Min, Y.I., NIH clinical trials and publication bias (1993) Online J Curr Clin Trials Doc, , No 50; Fazakerley, J.K., Buchmeier, M.J., Pathogenesis of virus-induced demyelination (1993) Adv Virus Res, 42, pp. 249-324; Johnson, S.A., Morgan, D.G., Finch, C.E., Extensive postmortem stability of RNA from rat and human brain (1993) J Neurosci Res, 16, pp. 267-280; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res, 12, pp. 1-9; Kurtzke, J.F., Epidemiologic evidence for multiple sclerosis as an infection (1993) Clin Microbiol Rev, 6, pp. 382-427; Kwok, S., Higuchi, R., Avoiding false positives with PCR (1989) Nat Med, 339, pp. 237-238; Leonard, S., Logel, J., Luthman, D., Casanova, M., Kirch, D., Freedman, R., Biological stability of mRNA isolated from human postmortem brain collections (1993) Biol Psychiatry, 33, pp. 456-466; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann Neurol, 31, pp. 525-533; Murray, R.S., Cai, G.Y., Hoel, K., Johnson, S., Cabirac, G.F., Coronaviruses and multiple sclerosis (1993) Adv Exp Med Biol, 342, pp. 353-357; Myint, S.H., Human coronavirus infections (1995) The Coronaviridae., pp. 389-401. , Siddell SG (ed) Plenum Press, New York; Noguchi, I., Arai, H., Iizuka, R., A study on postmortem stability of vasopressin messenger RNA in rat brain compared with those in total RNA and ribosomal RNA (1991) J Neural Transm, 83, pp. 171-178; Perlman, S., Jacobsen, G., Moore, S., Regional localization of virus in the central nervous system of mice persistently infected with murine coronavirus JHM (1988) Virology, 166, pp. 328-338; Perlman, S., Jacobsen, G., Afifi, A., Spread of a neurotropic murine coronavirus into the CNS via the trigeminal and olfactory nerves (1989) Virology, 170, pp. 556-560; Perrett, C.W., Marchbanks, R.M., Whatley, S.A., Characterisation of messenger RNA extracted post-mortem from the brains of schizophrenic, depressed and control subjects (1988) J Neurol Neurosurg Psychiatry, 51, pp. 325-331; Sambrook, J., Fritsch, E.F., Maniatis, T., (1990) Molecular cloning. A laboratory manual., pp. 7.19-7.21. , Cold Spring Harbor Laboratory Press, New York; Schreiber, J., Kamahora, T., Lai, M.M.C., Sequence analysis of the nucleocapsid protein gene of human coronavirus 229E (1989) Virology, 169, pp. 142-151; Southern, E.M., Detection of specific sequences among DNA fragments separated by gel electrophoresis (1975) J Mol Biol, 98, p. 503; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Streicher, R., Stoffel, W., The organization of the human myelin basic protein gene - Comparison with the mouse gene (1989) Biol Chem Hoppe-Seyler, 370, pp. 503-510; Wege, H., Immunopathological aspects of coronavirus infections (1995) Springer Semin Immunopathol, 17, pp. 133-148",,,,00016322,,,"11515789","English","Acta Neuropathol.",Article,"Final",,Scopus,2-s2.0-0034926146
"Koljesar G., Yoo D.","6505798787;7103242554;","Targeted RNA recombination of the membrane and nucleocapsid protein genes between mouse hepatitis virus and bovine coronavirus.",2001,"Journal of veterinary science (Suwon-si, Korea)","2","3",,"149","157",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035748649&partnerID=40&md5=d2b7ce31fac89936a2359307c3ff8f75","Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Canada","Koljesar, G., Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Canada; Yoo, D., Department of Pathology, Ontario Veterinary College, University of Guelph, Guelph, Canada","The targeted RNA recombination was attempted to substitute the membrane (M) protein gene and part of the nucleocapsid (N) protein gene of mouse hepatitis virus with the corresponding sequences from bovine coronavirus. Using a defective interfering (DI) RNA-like cDNA construct derived from pMH54, 690 nucleotides representing the entire M gene and the 5' most 915 nucleotides of the N gene of the mouse hepatitis virus Albany 4 mutant were attempted to be replaced. Upon infection of cells with Albany 4 followed by transfection with synthetic RNA transcribed from the DI-like cDNA construct, recombinant mouse hepatitis viruses as the large plaque forming phenotype were isolated by plaque assays at the non-permissive temperature of 391 degrees C. By RT-PCR and sequencing, those large plaque phenotypes were confirmed to have contained the thermostable phenotype marker derived from the transfected RNA, demonstrating that recombination occurred between the Albany 4 genomic RNA and the in vitro RNA transcripts. Further analysis of the recombinant viruses indicated that there combination had taken place within the region of 222 nucleotides between positions 916 and 1,137 of the N gene. This is the region immediately downstream of the replacement sequence and the start of the temperature resistant phenotype marker. The results suggest that the M and part of the N genes of bovine coronavirus may not be able to complement the function of those of mouse hepatitis virus. This study redirects our current approach of utilizing the MHV targeted RNA recombination as a means to study bovine coronavirus genetics towards the construction of an infectious cDNA clone.",,"complementary DNA; matrix protein; nucleocapsid protein; virus RNA; amino acid sequence; animal; animal disease; article; cattle; cell culture; chemistry; Coronavirus; gene targeting; gene vector; genetic transfection; genetics; isolation and purification; methodology; molecular genetics; mouse; Murine hepatitis coronavirus; nucleotide sequence; phenotype; reverse transcription polymerase chain reaction; sequence homology; virus culture; Amino Acid Sequence; Animals; Base Sequence; Cattle; Cells, Cultured; Coronavirus, Bovine; DNA, Complementary; Gene Targeting; Genetic Vectors; Mice; Molecular Sequence Data; Murine hepatitis virus; Nucleocapsid Proteins; Phenotype; Plaque Assay; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sequence Homology, Amino Acid; Transfection; Viral Matrix Proteins",,"Koljesar, G.email: gkoljesar@hemosol.com",,,1229845X,,,"12441693","English","J. Vet. Sci.",Article,"Final",,Scopus,2-s2.0-0035748649
"Breslin J.J., Smith L.G., Guy J.S.","7004753945;37109180900;7202723649;","Baculovirus expression of Turkey coronavirus nucleocapsid protein",2001,"Avian Diseases","45","1",,"136","143",,14,"10.2307/1593020","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035066915&doi=10.2307%2f1593020&partnerID=40&md5=3bf2456e07c2e57ebaccff10f634ecaf","Department of Microbiology, North Carolina State University, Raleigh, NC 27606, United States","Breslin, J.J., Department of Microbiology, North Carolina State University, Raleigh, NC 27606, United States; Smith, L.G., Department of Microbiology, North Carolina State University, Raleigh, NC 27606, United States; Guy, J.S., Department of Microbiology, North Carolina State University, Raleigh, NC 27606, United States","The nucleocapsid (N) gene of turkey coronavirus (TCV) was amplified by reverse transcriptase-polymerase chain reaction, cloned, and expressed in the baculovirus expression system. A recombinant baculovirus containing the TCV N gene (rBTCV/N) was identified by polymerase chain reaction and expression of TCV N protein as determined by western immunoblot analysis. Two TCV-specific proteins, 52 and 43 kDa, were expressed by rBTCV/N; one of these proteins, p52, was comparable in size to native TCV N protein. Baculovirus-expressed N proteins were used as antigen in an indirect enzyme-linked immunosorbent assay (ELISA) for detection of TCV-specific antibodies. The ELISA detected antibodies specific for TCV and infectious bronchitis virus, a closely related avian coronavirus, but did not detect antibodies specific for other avian viruses (avian influenza, avian reovirus, avian paramyxovirus 3, avian adenovirus 1, or Newcastle disease virus). These findings indicate that baculovirus-expressed TCV N protein is a suitable source of antigen for ELISA-based detection of TCV-specific antibodies in turkeys.","Baculovirus; Enzyme-linked immunosorbent assay; Turkey coronavirus","antibody detection; Aviadenovirus; avian influenza virus; avian paramyxovirus; Avian reovirus; enzyme linked immunosorbent assay; infectious bronchitis virus; Newcastle disease paramyxovirus; nucleocapsid protein; polymerase chain reaction; protein expression; reverse transcription polymerase chain reaction; turkey coronavirus; virus antibody; virus expression; virus gene; Aves; Aviadenovirus; Avian adenovirus; Avian infectious bronchitis virus; Avian influenza virus; Avian orthoreovirus; Avian paramyxovirus 3; Coronavirus; Influenza virus; Newcastle disease virus; Paramyxoviridae; Reovirus sp.; Turkey coronavirus; unidentified baculovirus","Ahmad, S., Bassiri, M., Banerjee, A.K., Yilma, T., Immunological characterization of the VSV nucleocapsid (N) protein expressed by recombinant baculovirus (1993) Virology, 192, pp. 207-216; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of poultry, 10th ed., pp. 1025-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Carpenter, A.B., Enzyme-linked immunoassays (1992) Manual of clinical laboratory immunology, 4th ed., pp. 2-9. , N. E. Rose, E. C. de Macario, J. L. Fahey, H. Friedman, and G. M. Penn, eds. American Society for Microbiology, Washington, DC; Cavanagh, D., Structural polypeptides of coronavirus IBV (1981) J. Gen. Virol., 53, pp. 93-103; Cheley, S., Anderson, R., Cellular synthesis and modification of murine hepatitis virus polypeptides (1981) J. Gen. Virol., 54, pp. 301-311; Errington, W., Steward, M., Emmerson, P.T., A diagnostic immunoassay for Newcastle disease virus based on the nucleocapsid protein expressed by a recombinant baculovirus (1995) J. Virol. Methods, 55, pp. 357-365; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis from pheasants (1996) Vet. Rec., 138, pp. 208-209; Guy, J.S., New methods for diagnosis of turkey coronavirus infections (1998) Proc. 49th North Central Avian Disease Conference and Symposium on Enteric and Emerging Diseases, pp. 8-10. , Indianapolis, IN; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hummel, K.B., Erman, D.D., Heath, J., Bellini, W.J., Baculovirus expression of the nucleocapsid protein gene of measles virus and utility of the recombinant protein in diagnostic enzyme immunoassays (1992) J. Clin. Microbiol., 30, pp. 2874-2880; Ignjatovic, J., Galli, L., Structural proteins of avian infectious bronchitis virus: Role in immunity and protection (1993) Adv. Exp. Med. Biol., 342, pp. 449-453; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , S. G. Siddell, ed. Plenum Press, New York; Mountcastle, W.E., Compans, R.W., Caliguiri, L.W., Choppin, P.W., Nucleocapsid protein subunits of simian virus 5, Newcastle disease virus, and Sendai virus (1970) J. Virol., 6, pp. 677-684; Mountcastle, W.E., Compans, R.W., Lackland, H., Choppin, P.W., Proteolytic cleavage of subunits of the nucleocapsid of the paramyxovirus simian virus 5 (1974) J. Virol., 14, pp. 1253-1261; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of poultry, 10th ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; O'Reilly, D.R., Miller, L.K., Luckow, V.A., (1992) Baculovirus expression vectors: a laboratory manual, , W. H. Freeman and Company, New York; Patel, B.L., Pomeroy, B.S., Gonder, E., Cronkite, C.E., Indirect fluorescent antibody test for the diagnosis of coronaviral enteritis of turkeys (bluecomb) (1976) Am. J. Vet. Res., 37, pp. 1111-1112; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning, a laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Senne, D.A., Virus propagation in embryonating eggs (1989) A laboratory manual for the isolation and identification of avian pathogens, 3rd ed., pp. 176-181. , H. G. Purchase, L. H. Arp, C. H. Domermuth, and J. E. Pearson, eds. American Association of Avian Pathologists, Kennett Square, PA; Siddell, S.G., The Coronaviridae an introduction (1995) Coronaviridae, pp. 1-9. , S. G. Siddell, ed. Plenum Press, New York; Spackman, D., Cameron, I.D.R., Isolation of infectious bronchitis virus from pheasants (1983) Vet. Rec., 113, pp. 354-355; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Stern, D.F., Burgess, L., Sefton, B.F., Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus (1982) J. Virol., 42, pp. 208-219; Stern, D.F., Sefton, B.M., Coronavirus proteins: Biogenesis of avian infectious bronchitis virus virion proteins (1982) J. Virol., 44, pp. 794-803; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200","Guy, J.S.; Department of Microbiology, North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11332474","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0035066915
"Hiscox J.A., Wurm T., Wilson L., Britton P., Cavanagh D., Brooks G.","7004565877;6602454962;56227719300;57203302770;26642890500;7202058172;","The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus",2001,"Journal of Virology","75","1",,"506","512",,118,"10.1128/JVI.75.1.506-512.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034751088&doi=10.1128%2fJVI.75.1.506-512.2001&partnerID=40&md5=da8e44eb96a3a116e2eae9a84b652692","Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom","Hiscox, J.A., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Wurm, T., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Wilson, L., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Britton, P., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Cavanagh, D., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Brooks, G., Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom","The coronavirus nucleoprotein (N) has been reported to be involved in various aspects of virus replication. We examined by confocal microscopy the subcellular localization of the avian infectious bronchitis virus N protein both in the absence and in the context of an infected cell and found that N protein localizes both to the cytoplasmic and nucleolar compartments.",,"virus nucleoprotein; animal cell; article; Avian infectious bronchitis virus; cellular distribution; confocal microscopy; cytoplasm; nonhuman; nucleolus; nucleotide sequence; priority journal; protein localization; virus cell interaction; Amino Acid Sequence; Animals; Cell Nucleolus; Cercopithecus aethiops; Cytoplasm; Infectious bronchitis virus; Microscopy, Confocal; Molecular Sequence Data; Nucleocapsid Proteins; Vero Cells","Alberts, B., Bray, D., Levis, J., Raff, M., Roberts, K., Watson, J.D., Molecular biology of the cell (1994), pp. 381-382. , 3rd ed. Garland Publishing, New York, N.Y; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. Virol., 62, pp. 4280-4287; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequence of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Carmo-Fonseca, M., Mendes-Soares, L., Campos, I., To be or not to be in the nucleolus (2000) Nat. Cell Biol., 2, pp. E107-E112; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Chang, R.-Y., Brian, D.A., cis Requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Compton, J.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., In vitro replication of mouse hepatitis virus strain A59 (1987) J. Virol., 61, pp. 1814-1820; Davies, H.A., Dourmashkin, R.R., MacNaughton, R., Ribonucleoprotein of avian infectious bronchitis virus (1981) J. Gen. Virol., 53, pp. 67-74; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol., 67, pp. 923-932; Hiscox, J.A., Ball, L.A., Cotranslational disassembly of flock house virus in a cell-free system (1997) J. Virol., 71, pp. 7974-7977; Hiscox, J.A., Cavanagh, D., Britton, P., Quantification of individual subgenomic mRNA species during replication of the coronavirus transmissible gastroenteritis virus (1995) Virus Res., 36, pp. 119-130; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Keck, J.G., Hague, B.G., Brian, D.A., Lai, M.M.C., Temporal regulation of bovine coronavirus RNA synthesis (1988) Virus Res., 9, pp. 343-356; Kozak, M., An analysis of vertebrate mRNA sequences: Intimations of translational control (1991) J. Cell Biol., 115, pp. 887-903; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lapps, W., Hague, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein gene (1987) Virology, 157, pp. 47-57; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995), pp. 141-163. , S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Arch. Virol., 125, pp. 141-160; Mockett, A.P.A., Envelope proteins of avian infectious bronchitis virus: Purification and biological properties (1985) J. Virol. Methods, 12, pp. 271-278; Molenkamp, R., Van Tol, H., Rozier, B.C.D., Van der Meer, Y., Spaan, W.J.M., Snijder, E.J., The arterivirus replicase is the only viral protein required for genome replication and subgenomic mRNA transcription (2000) J. Gen. Virol., 81, pp. 2491-2496; Nelson, G.W., Stohlman, S.A., Localization of the RNA-binding domain of mouse hepatitis virus nucleocapsid protein (1993) J. Gen. Virol., 74, pp. 1975-1979; Nelson, G.W., Stohlman, S.A., Tahara, S.M., High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA (2000) J. Gen. Virol., 81, pp. 181-188; Parker, M.M., Masters, P.S., Sequence comparison of the N genes of 5 strains of the coronavirus mouse hepatitis virus suggests a 3 domain-structure for the nucleocapsid protein (1990) Virology, 179, pp. 463-468; Pedersen, K.W., Van der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) J. Virol., 73, pp. 2016-2026; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Rowland, R.R., Kerwin, R., Kuckleburg, C., Sperlich, A., Benfield, D.A., The localization of porcine reproductive and respiratory syndrome virus nucleocapsid protein to the nucleolus of infected cells and identification of a potential nucleolar localization signal sequence (1999) Virus Res., 64, pp. 1-12; Sapats, S.I., Ashton, F., Wright, P.J., Ignjatovic, J., Novel variation in the N protein of avian infectious bronchitis virus (1996) Virology, 226, pp. 412-417; Sethna, P.B., Brian, D.A., Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes (1997) J. Virol., 71, pp. 7744-7749; Shi, S.T., Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Oh, J.W., Lai, M.M.C., Colocalization and membrane association of murine hepatitis virus gene 1 products and de nova-synthesized viral RNA in infected cells (1999) J. Virol., 73, pp. 5957-5969; Siddell, S., Wege, H., Barthel, A., Ter Meulen, V., Intracellular protein synthesis and the in vitro translation of coronavirus JHM mRNA (1981) Adv. Exp. Med. Biol., 142, pp. 193-207; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translational regulation: Leader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Ulmanen, I., Soderlund, H., Kaarianen, L., Semliki Forest virus capsid protein associates with 60S ribosomal subunit in infected cells (1976) J. Virol., 20, pp. 203-210; Van der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Locker, J.K., Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73, pp. 7641-7657; Wengler, G., Wengler, G., Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection (1984) Virology, 134, pp. 435-442; Wengler, G., Wurkner, D., Wengler, G., Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores (1992) Virology, 191, pp. 880-888; Wilhelmsen, K.C., Leibowitz, J.L., Bond, C.W., Robb, J.A., The replication of murine coronaviruses in enucleated cells (1981) Virology, 110, pp. 225-230; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other viruses (1992) Virus Res., 25, pp. 213-222; Wilson, T.M.A., Cotranslational disassembly of tobacco mosaic virus in vitro (1984) Virology, 137, pp. 155-265; Zhou, M.L., Willlams, A.K., Chung, S.I., Wang, L., Collisson, E.W., Infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3' terminus of the genome (1996) Virology, 217, pp. 191-199","Hiscox, J.A.; Sch. of Anim./Microbial Sciences, University of Reading, Whiteknights, P.O. Box 228, Reading RG6 6AJ, United Kingdom; email: j.a.hiscox@reading.ac.uk",,,0022538X,,JOVIA,"11119619","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034751088
"Reschová S., Pokorova D., Nevoránková Z., Franz J.","56617433600;56632403800;6603471221;7102171889;","Monoclonal antibodies to bovine coronavirus and their use in enzymoimmunoanalysis and immunochromatography",2001,"Veterinarni Medicina","46","5",,"125","131",,4,"10.17221/7869-VETMED","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347608566&doi=10.17221%2f7869-VETMED&partnerID=40&md5=f250f08ff67899a5c03af15cd016e3df","Veterinary Research Institute, Brno, Czech Republic","Reschová, S., Veterinary Research Institute, Brno, Czech Republic; Pokorova, D., Veterinary Research Institute, Brno, Czech Republic; Nevoránková, Z., Veterinary Research Institute, Brno, Czech Republic; Franz, J., Veterinary Research Institute, Brno, Czech Republic","Two monoclonal antibodies (MAb) to the outer structural protein E2 (spike peplomeric protein) and two MAb to the inner capsid protein N of bovine coronavirus (BCV) were prepared and identified by Western blotting to be used for increasing the specificity and sensitivity of BCV detection. The MAb were checked by the haemagglutination inhibition test and immunoperoxidase tests and no cross reactivity with rotavirus was demonstrated by the immunoperoxidase test and ELISA. A mixture of all the four MAb at predetermined optimum concentrations was first used in sandwich ELISA and then, in combination with an anti-coronavirus polyclonal antibody, for the development of a simple and rapid immunochromatographic test (ICT). The results of which can be read visually within 10 min. The inclusion of MAb into ELISA and ICT allows the detection of both intact and incomplete BCV virions. ELISA and ICT were used in the examination of a set of 74 faecal samples collected from calves suffering from diarrhoea. ELISA, used as the golden standard verified by electron microscopy, detected BCV in 15 samples (20.3%) and ICT in 16 samples. Three of the ICT-positive samples were negative by ELISA. On the other hand, two of the 58 ICT-negative samples were positive by ELISA, Sensitivity and specificity of ICT were 94.9% and 86.7%, respectively. © 2007 Veterinarni Medicina.","Bovine coronavirus (BCV); Bovine rotavirus; ELISA; Immunochromatographic test (ICT)",,"Babiuk, L.A., (1985) Rotavirus and coronavirus infection in animals, pp. 80-120. , Prog. Vet. Microbiol. Immun., /; Bhaskar, S., Singh, S., Sharma, M., A single-step Immu-nochromatographic test for detection of Entamoeba histolytica antigen in stool samples (1996) J. Immunol. Meth, 196, pp. 193-198; Bonzom, P., Latex et diagnostic (1996) Le Technoscope De Biofutur, 161, pp. 2-11; Brenner, S., Home, E.W., A negative staining method for high resolution electronmicroscopy of viruses (1959) Biochem. Biophys. Acta, 34, pp. 103-110; Clark, M.A., Bovine coronavirus (1993) Brit. Vet. J, 149, pp. 51-70; Crouch, C.F., Raybould, T.J.G., Acres, S.D., Monoclonal antibody capture enzyme-linked immunosorbent assay for detection of bovine enteric coronavirus (1984) J. Clin. Microbiol, 19, pp. 388-393; Czerny, C.P., Eichhorn, W., Characterization of monoclonal and polyclonal antibodies to bovine coronavirus: establishment of an effecient ELISA for antigen detection in feces (1989) Vet. Microbiol, 20, pp. 111-122; Dar, V.S., Ghosh, S., Broor, S., Rapid detection of rotavirus by using colloidal gold particles labeled with monoclonal antibody (1994) J. Virol. Meth, 47, pp. 51-58; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Sahara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J. Gen. Virol, 68, pp. 2863-2877; Fair, A.G., Nakane, P.K., Immunohistochemistry with enzyme labelled antibodies: a brief review (1981) J. Immunol. Meth, 47, pp. 129-144; Galfre, G., Milstein, C., Preparation of monoclonal antibodies (1981) Strategies and procedures. Meth. Enzymol, 73, pp. 3-46; Gupta, R., Talwar, G.P., Gupta, S.K., Rapid antibody capture assay for detection of group-A streptoccoci using monoclonal antibody and colloidal gold-monospecific polyvalent antibody conjugate (1992) J. Immunoassay, 13, pp. 441-455; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparsion of bovine coronavirus (BCV) antigens: monoclonal antibodies to the spike glycoprotein distinquish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Klingenberg, K., Esfandiari, J., Evaluation of a one-step test for rapid, in practise detection of rotavirus in farm animals (1996) Vet. Rec, 138, pp. 393-395; Millane, G., Michaud, L., Dea, S., Biological and molecular differtiation between coronaviruses associated with neonatal calf diarrhoea and winter dysentery in adult cattle (1995) Adv. Exp. Med. Biol, 380, pp. 29-33; Reschova, S., Franz, J., Stepanek, J., Rozkosna, A., Im-munochromatographic detection of bovine rotavirus using egg yolk antibodies (2000) Vet. Med.-Czech, 45, pp. 33-37; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec, 119, pp. 34-39; Rodak, L., Babiuk, L.A., Acres, S.D., Detection by radioimmunoassay and enzyme-linked immunosorbent assay of coronavirus antibodies in bovine serum and lacteal secretions (1982) J. Clin. Microbiol, 16, pp. 30-34; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: an enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Sato, K., Ichiyama, S., Iinuma, Y., Nada, T., Shimokata, K., Na-kashima, N., Evaluation of immunochromatographic assay systems for rapid detection of hepatitis B surface antigen and antibody Dainascreen HBsAg and Dainascreen Ausab (1996) J. Clin. Microbiol, 34, pp. 1420-1422; Schoenthaler, S.L., Kapil, S., Development and applications of bovine coronavirus antigen detection enzyme-linked immunosorbent assay (1999) Clin. Diagn. Lab. Immunol, 6, pp. 130-132; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J. Vet. Diagn. Invest, 8, pp. 99-105; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354; Tsunemitsu, H., Saif, L.J., Antigenic and biological com-parsions of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol, 740, pp. 1303-1311; Vautherot, J.F., Laporte, J., Utilization of monoclonal antibodies for antigenic characterization of coronaviruses (1983) Ann. Rech. Vet, 14, pp. 144-437","Reschová, S.; Veterinary Research Institute, Hudcova 70, Czech Republic; email: reschova@vri.cz",,"Czech Academy of Agricultural Sciences",03758427,,,,"English","Vet. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0347608566
"Cho K.-O., Hoet A.E., Loerch S.C., Wittum T.E., Saif L.J.","57193116476;6602855175;7004696614;7004009529;7102226747;","Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle",2001,"American Journal of Veterinary Research","62","9",,"1436","1441",,46,"10.2460/ajvr.2001.62.1436","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035460118&doi=10.2460%2fajvr.2001.62.1436&partnerID=40&md5=105b249bd07e25dcce973093cb5d66e9","Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Department of Animal Science, Ohio State University, Wooster, OH 44691, United States; Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States","Cho, K.-O., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Hoet, A.E., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States; Loerch, S.C., Department of Animal Science, Ohio State University, Wooster, OH 44691, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 43210, United States; Saif, L.J., Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States","Objective - To assess the relationship between shedding of bovine coronavirus (BCV) via the respiratory tract and enteric routes and the association with weight gain in feedlot cattle. Animals - 56 crossbred steers. Procedures - Paired fecal samples and nasal swab specimens were obtained and were tested for BCV, using antigen-capture ELISA. Paired serum samples obtained were tested for antibodies to BCV, using antibody-detection ELISA. Information was collected on weight gain, clinical signs, and treatments for enteric and respiratory tract disease during the study period. Results - Number of samples positive for bovine respiratory coronavirus (BRCV) or bovine enteric coro navirus (BECV) was 37/224 (17%) and 48/223 (22%), respectively. Some cattle (25/46, 45%) shed BECV and BRCV. There were 25/29 (86%) cattle positive for BECV that shed BRCV, but only 1/27 (4%) cattle negative to BECV shed BRCV. Twenty-seven of 48 (56%) paired nasal swab specimens and fecal samples positive for BECV were positive for BRCV. In contrast, only 10/175 (6%) paired nasal swab specimens and fecal samples negative for BECV were positive for BRCV. Only shedding of BECV was associated with significantly reduced weight gain. Seroconversion to BCV during the 21 days after arrival was detected in 95% of the cattle tested. Conclusions and Clinical Implications - Feedlot cattle infected with BCV after transport shed BCV from the respiratory tract and in the feces. Fecal shedding of BCV was associated with significantly reduced weight gain. Developing appropriate control measures for BCV infections could help reduce the decreased weight gain observed among infected feedlot cattle.",,"Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; virus antibody; virus antigen; animal; animal disease; article; blood; body weight; cattle; cattle disease; Coronavirus; enteritis; feces; growth, development and aging; male; multivariate analysis; nose cavity; pathology; respiratory tract disease; statistical model; virology; virus infection; virus shedding; Animals; Antibodies, Viral; Antigens, Viral; Body Weight; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Enteritis; Feces; Logistic Models; Male; Multivariate Analysis; Nasal Cavity; Respiratory Tract Diseases; Virus Shedding","Saif, L.J., Heckert, R., Enteropathogenic coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-1152. , Saif LJ, Theil KW, eds. Boca Raton, Fla: CRC Press; Bridger, J.C., Woode, G.N., Meyling, A., Isolation of corona viruses from neonatal calf diarrhea in Great Britain and Denmark (1978) Vet Microbiol, 3, pp. 101-113; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1479) Am J Vet Res, 34, pp. 145-150; Sharpee, R.L., Mebus, C.A., Bass, E.R., Characterization of a calf diarrhea coronavirus (1976) Am J Vet Res, 37, pp. 1031-1041; Stair, E.L., Rhodes, M.B., White, R.G., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am J Vet Res, 33, pp. 1147-1156; Benfield, D.A., Saif, L.J., Cell culture propagation of a coro navirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Horner, G.W., Hunter, R., Kirbrid, C.A., A coronavirus-like agent present in feces of cows with diarrhea (1975) N Z Vet J, 23, p. 98; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery in cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Takahashi, E., Inaba, Y., Sato, K., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet Microbiol, 5, pp. 151-154; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am J Vet Res, 40, pp. 1476-1478; McNulty, M.S., Bryson, D.G., Allan, G.M., Coronavirus infection of the bovine respiratory tract (1984) Vet Microbiol, 9, pp. 425-434; Mebus, C.A., Stair, E.L., Rhodes, M.B., Pathology of neonatal calf diarrhea induced by a corona-like agent (1973) Vet Pathol, 10, pp. 45-64; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, E.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Brodersen, B.W., Kelling, C.L., Effect of concurrent experimentally induced bovine respiratory syncytial virus and bovine viral diarrhea virus infection on respiratory tract and enteric diseases in calves (1998) Am J Vet Res, pp. 591423-591430; Bryson, D.G., McFerran, J.B., Ball, H.J., Observations on outbreaks of respiratory disease in housed calves. Epidemiological, clinical and microbiological findings (1978) Vet Rec, 103, pp. 485-489; Martin, S.W., Analysis and causal interpretation of biologic data. A seroepidemiologic study of respiratory disease (1985) Vet Med, 57, pp. 46-54. , Fourth International Symposium on Veterinary Epidemiology and Economics; Hasoksuz, M.H., Lathrop, S.E., Gadfield, K.E., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Antibody titers against bovine coronavirus and shedding of the virus via the respiratory tract in feedlot cattle (2000) Am J Vet Res, 61, pp. 1057-1061; Silva, M.R., O'Reilly, K.L., Lin, X., Sensitivity comparison for detection of respiratory bovine coronaviruses in nasal samples from feedlot cattle by ELISA and isolation with the G clone of HRT-18 cells (1999) J Vet Diagn Invest, 11, pp. 15-19; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swabs samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1454; Lathrop, S.L., Wittum, T.E., Brock, K.V., Association between infection of the respiratory tract attributable to bovine coronavirus and health and growth performance of cattle in feedlots (2000) Am J Vet Res, 61, pp. 1062-1066; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal anti-bodies for the detection of bovine coronavirus (1995) J Vet Diagn Invest, 8, pp. 99-105; Smith, D.R., Fedorka-Cray, P.J., Mohan, R., Epidemiology of winter dysentery in dairy cattle: Assessment of herd-level causative agents and risk factors (1998) Am J Vet Res, 59, pp. 994-1001; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Fukutomi, T., Tsunemitsu, H., Akashi, H., Detection of bovine coronaviruses from adult cows with epizootic diarrhea and their antigenic and biological diversities (1999) Arch Viirol, 144, pp. 997-1006; Zhang, X., Herbst, W., Kousoulas, K.G., Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 134, pp. 421-426; Martin, S.W., Nagy, E., Shewen, P.E., The association of tilers to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261; Thomson, R.G., Pathology and pathogenesis of the common disease of the respiratory tract of cattle (1974) Can Vet J, 15, pp. 249-251; Dyer, R.M., The bovine respiratory disease complex: Infectious agents (1981) Compend Contin Educ Pract Vet, 3, pp. S374-S382; Straub, O.C., Viral respiratory infections of cattle (1995) Bovine Pract, 29, pp. 66-70; Crouch, C.F., Ohmann, H.B., Watts, T.C., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinical normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Tsunemitsu, H., Smith, D.R., Saif, L.J., Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coro navirus in feces by RT-PCR (1999) Arch Virol, 144, pp. 167-175","Saif, L.J.; Food Animal Health Research Program, Dept. of Vet. Preventive Medicine, Ohio State University, Wooster, OH 44691, United States",,"American Veterinary Medical Association",00029645,,AJVRA,"11560274","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0035460118
"Pratelli A., Martella V., Elia G., Decaro N., Aliberti A., Buonavoglia D., Tempesta M., Buonavoglia C.","7004884960;7003300496;7005135633;6701636107;6507113796;7004335810;7005599031;7005623145;","Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV)",2001,"Molecular and Cellular Probes","15","4",,"229","233",,25,"10.1006/mcpr.2001.0364","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034924337&doi=10.1006%2fmcpr.2001.0364&partnerID=40&md5=7443bed0a96ba08727a5b6f6b3e3e521","Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Institute of Infectious Diseases, Faculty of Veterinary Medicine, Messina, 98123, Italy","Pratelli, A., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Martella, V., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Elia, G., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Decaro, N., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Aliberti, A., Institute of Infectious Diseases, Faculty of Veterinary Medicine, Messina, 98123, Italy; Buonavoglia, D., Institute of Infectious Diseases, Faculty of Veterinary Medicine, Messina, 98123, Italy; Tempesta, M., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Buonavoglia, C., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy","A nucleotide variability in the sequence of the gene encoding for the transmembrane protein M of canine coronavirus (CCV) is described. A total of 177 faecal samples from pups with enteritis were analysed by a PCR and n-PCR specific for CCV. Four samples, collected from a dog presenting a long-duration shedding of CCV, and a sample from another diarrhoeic dog, were found positive by PCR but negative by n-PCR. Sequence analysis of the samples revealed silent nucleotide substitutions in the binding site of the internal primer used for the n-PCR. Moreover, the nucleotide substitutions occurring over the whole fragment of the five samples analysed were similar. © 2001 Academic Press.","Canine coronavirus; M protein; Variation","membrane protein; virus protein; article; binding site; Coronavirus; dog; enteritis; gene sequence; genetic variability; nonhuman; nucleic acid base substitution; nucleotide sequence; polymerase chain reaction; priority journal; sequence analysis; virus shedding; Canine coronavirus; Canis familiaris; Coronavirus","Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, B.S., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhoea (1974) Proceedings of the 78th Meeting of the US Animal Health Association, pp. 359-366; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) Journal of General Virology, 73, pp. 2849-2862; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., BuilIdo, M.J., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus with the S protein of feline and porcine coronaviruses (1994) Journal of General Virology, 75, pp. 1789-1794; Carmichael, L.E., Binn, L.N., New enteric viruses in the dog (1981) Advances in Veterinary Science and Comparative Medicine, 25, pp. 1-37; Cartwright, S., Lucas, M., Vomiting and diarrhoea in dogs (1972) Veterinary Record, 91, pp. 571-572; Vandenberghe, J., Ducatelle, R., Debouck, P., Hoorens, J., Coronavirus infection in a litter of pups (1980) Veterinary Quarterly, 2, pp. 136-141; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.C., Gaskell, C.J., Canine coronavirus infection in dog following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) American Journal of Veterinary Research, 37, pp. 247-256; Takeuchi, A., Binn, L.N., Jervis, H.R., Keenan, K.P., Hildebrandt, P.K., Valas, R.B., Electron microscope study of experimental enteric infections in neonatal dogs with a canine coronavirus (1976) Laboratory Investigation, 34, pp. 539-549; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR assay for the detection of canine coronavirus (1999) Journal of Virological Methods, 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using n-PCR (2000) Journal of Virological Methods, 84, pp. 91-94; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice (1994) Nucleic Acids Research, 22, pp. 4673-4680; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies tp murine hepatitis virus-4 (strain JHM) define the viral glicoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Risco, C., Anton, I.M., Sune, C., Pedregosa, A.M., Martin-Alonso, J.M., Parra, F., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) Journal of Virology, 68, pp. 5269-5277; Kathryn, V.H., Coronaviridae and their replication (1991) Fundamental Virology, pp. 471-486. , (B. N. Fields, D. M. Knipe, eds.). New York: Raven Press Ltd; Gunn-Moore, D.A., Gunn-Moore, F.J., Gruffydd-Jones, T.J., Harbour, D.A., Detection of FCoV quasispecies using denaturing gradient gel electrophoresis (1999) Veterinary Microbiology, 69, pp. 127-130; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinok, M.C., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Rottier, P.J.M., The molecular dynamics of feline coronaviruses (1999) Veterinary Microbiology, 69, pp. 117-125; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Research, 61, pp. 145-152","Pratelli, A.; Department of Health, Faculty of Veterinary Medicine, University of Bari, Strada per Casamassima Km 3, 70010 Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,"Academic Press",08908508,,MCPRE,"11513558","English","Mol. Cell. Probes",Article,"Final",Open Access,Scopus,2-s2.0-0034924337
"Jenkinson C.P., Hanson R., Cray K., Wiedrich C., Knowler W.C., Bogardus C., Baier L.","7006094881;7401746098;6506716431;6507629590;57202552357;7102903658;57213918913;","Cross-protection studies between respiratory and calf diarrhea and winter dysentery coronavirus strains in calves and RT-PCR and nested PCR for their detection",2001,"Archives of Virology","146","12",,"2401","2419",,71,"10.1007/s007050170011","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035559553&doi=10.1007%2fs007050170011&partnerID=40&md5=4e05677b594393fd2f385bb8417841dc","Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States","Jenkinson, C.P., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Hanson, R., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Cray, K., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Wiedrich, C., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Knowler, W.C., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Bogardus, C., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States; Baier, L., Phoenix Epidemiology and Clinical Research Branch, National Institute of Digestive Diabetes and Kidney Diseases, National Institutes of Health, Phoenix, AR, United States","A 1-step RT-PCR assay, targeting a 730 bp fragment of the nucleo-capsid (N) gene of bovine coronavirus (BCV), and a nested PCR assay, targeting a 407 bp fragment of the N gene, were developed to detect BCV in nasal swab and fecal samples of calves experimentally exposed to BCV. Both 1-step RT-PCR and nested PCR recognized cell culture passaged isolates of 10 bovine respiratory coronavirus (BRCV), 5 calf diarrhea (CD) and 8 winter dysentery (WD) strains of BCV, but not transmissible gastroenteritis coronavirus or bovine rotavirus. The sensitivity of the 1-step RT-PCR and nested PCR was compared to that of an antigen-capture ELISA. The lowest detection limit of the 1-step RT-PCR and nested PCR as determined by using tenfold serial dilutions of the BRCV 255 and 440 strains in BCV negative nasal swab suspensions from preexposure gnotobiotic calves was 2 × 104 and 2 × 102 TCID50/0.1 ml for each strain, respectively. The lowest detection limit of the antigen-capture ELISA as determined by using the same serially diluted samples was 1 × 106 TCID50/0.1 ml for each strain. Therefore, the 1-step RT-PCR and nested PCR assays were 50 and 5000 times, respectively more sensitive than the antigen-capture ELISA to detect BRCV in nasal swab suspensions. To investigate in vivo cross-protection between the BRCV and CD or WD strains of BCV and to detect nasal and fecal shedding of BCV using the 1-step RT-PCR, nested PCR and antigen-capture ELISA, 6 colostrum-deprived and two gnotobiotic calves were inoculated with a BRCV, a CD or a WD strain of BCV and then challenged 3-4 weeks later with either BRCV, CD or WD strains of BCV. All calves developed diarrhea after inoculation and BCV antigen (ELISA) or RNA (RT-PCR) was detected in the diarrheic fecal samples or the corresponding nasal swab samples. In addition, low amounts of BCV were also detected only by nested PCR in the fecal and nasal swab samples before and after diarrhea. No respiratory clinical signs were observed during the entire experimental period, but elevated rectal temperatures were detected during diarrhea in the BCV-inoculated calves. All calves recovered from infection with the BRCV, CD, or WD strains of BCV were protected from BCV-associated diarrhea after challenge exposure with either a heterologous or homologous strain of BCV. However, all calves challenged with heterologous BCV strains showed subclinical BCV infection evident by detection of nasal and fecal shedding of BCV RNA detected only by nested PCR. Such results confirm field and experimental data documenting reinfection of the respiratory and enteric tracts of cattle, suggesting that, in closed herds, respiratory or enteric tract reinfections may constitute a source of BCV transmissible to cows (WD) or neonatal or feedlot calves. In addition, the present 1-step RT-PCR and nested PCR assays were highly sensitive to detect BCV in nasal swab and fecal specimens. Therefore, these assays should be useful to diagnose BCV infections in calves and adult cows.",,"Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Cross Reactions; Diarrhea; Dysentery; Enzyme-Linked Immunosorbent Assay; Feces; Nose; Nucleocapsid; Polymerase Chain Reaction; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction; Sensitivity and Specificity; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Bovine rotavirus; Bovine viral diarrhea virus 1; Coronavirus; DNA viruses; Rotavirus","Chomczynski, P., Sacchi, N., Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal Biochem, 162, pp. 156-159; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Compton, S.R., Rogers, D.B., Holmes, K.V., Fertsch, D., Remenick, J., McGowan, J.J., In vitro replication of mouse hepatitis virus strain A59 (1987) J Virol, 61, pp. 1814-1820; Crouch, C.F., Ohmann, H.B., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Cruciere, C., Laporte, J., Sequence and analysis of bovine enteric coronavirus (F15) genome. 1. Sequence of the gene coding for the nucleocapsid protein; analysis of the predicted protein (1988) Am Inst Pasteur Virol, 139, pp. 123-138; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Sem Virol, 8, pp. 33-47; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Saif, L.J., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am J Vet Res, 57, pp. 48-53; Fukutomi, T., Tsunemitsu, H., Akashi, H., Detection of bovine coronaviruses from adult cows with epizootic diarrhea and their antigenic and biological diversities (1999) Arch Virol, 144, pp. 997-1006; Hasoksuz, M., Lathrop, S.L., Gadfield, K.L., Saif, L.J., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Heckert, R.A., Saif, L.J., Myers, G., Agnes, A.G., Epidemiologic factors and isotype-specific antibody responses in serum and mucosal secretions of dairy calves with bovine coronavirus respiratory tract and enteric tract infections (1991) Am J Vet Res, 52, pp. 845-851; Husain, M., Seth, P., Broor, S., Detection of group A rotavirus by reverse transcriptase and polymerase chain reaction in feces from children with acute gastroenteritis (1995) Arch Virol, 140, pp. 1225-1233; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Saif, L.J., Bovine coronavirus respiratory shedding and antibody titers in feedlot cattle (2000) Am J Vet Res; Lathrop, S.L., Wittum, T.E., Brock, K.V., Saif, L.J., The association between bovine coronavirus respiratory tract infection and health and growth performance of feedlot cattle (2000) Am J Vet Res; Lucchelli, A., Lance, S.E., Bartlett, P.B., Miller, G.Y., Saif, L.J., Prevalence of bovine group A rotavirus shedding among dairy calves in Ohio (1992) Am J Vet Res, 53, pp. 169-174; Martin, S.W., Analysis and causal interpretation of biologic data. A seroepidemi-ologic study of respiratory disease. Fourth International Symposium on Veterinary Epidemiology and Economics (1985) Vet Med, 57, pp. 46-54; Martin, S.W., Bonnett, B., Clinical epidemiology (1987) Can Vet J, 28, pp. 318-325; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Development of nasal, fecal and serum isotype-specific antibodies in calves challenged with bovine coronavirus or rotavirus (1987) Vet Immunol Immunopathol, 17, pp. 425-439; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter dysentery cows: An enigma resolved? (1990) Cornell Vet, 80, pp. 303-311; Saif, L.J., Redman, D.R., Moorhead, P.D., Theil, K.W., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Silva, M.R., O'Reilly, K.L., Lin, X., Stine, L., Storz, J., Sensitivity comparison for detection of respiratory bovine coronaviruses in nasal samples from feedlot cattle by ELISA and isolation with the G clone of HRT-18 cells (1999) J Vet Diagn Invest, 11, pp. 15-19; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Spaan, W.D., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-29522; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Tsunemitsu, H., Yonemichi, H., Hirai, T., Kudo, T., Onoe, S., Mori, K., Shimizu, M., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Tsunemitsu, H., Smith, D.R., Saif, L.J., Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coronavirus in feces by RT-PCR (1999) Arch Virol, 144, pp. 167-175; Watanabe, H., Gust, I.D., Holmes, I.H., Human rotavirus and its antibody: Their coexistence in feces of infants (1978) J Clin Microbiol, 7, pp. 405-409; Wilde, J., Eiden, J., Yolken, R., Removal of inhibitory substances from human fecal specimens for detection of group A rotaviruses by reverse transcriptase and polymerase chain reaction (1990) J Clin Microbiol, 28, pp. 1300-1307; Xu, L., Harbour, D., McCrae, M.A., The application of polymerase chain reaction to the detection of rotaviruses in feces (1990) J Virol Methods, 27, pp. 29-38; Zhang, X., Herbst, W., Kousoulas, K.G., Storz, J., Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 134, pp. 421-426",,,,03048608,,,"11811688","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035559553
"Zarnke R.L., Evermann J., Ver Hoef J.M., McNay M.E., Boertje R.D., Gardner C.L., Adams L.G., Dale B.W., Burch J.","7004222371;7005408825;6701631330;7003898040;6603330492;7202389151;7202283144;7201512014;7201814528;","Serologic survey for canine coronavirus in wolves from Alaska",2001,"Journal of Wildlife Diseases","37","4",,"740","745",,18,"10.7589/0090-3558-37.4.740","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035491944&doi=10.7589%2f0090-3558-37.4.740&partnerID=40&md5=63d60bc68c8b621fcd04bdf758e63101","Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Dept. of Vet. Clinical Sciences, College of Veterinary Medicine, Washington State University, Pullman, WA 99164-6610, United States; Alaska Department of Fish and Game, P.O. Box 355, Tok, AK 99780-0355, United States; U.S. Geological Survey, Alaska Biological Science Center, 1011 East Tudor Road, Anchorage, AK 99503, United States; Alaska Department of Fish and Game, 333 Raspberry Road, Anchorage, AK 99518-1599, United States; National Park Service, 201 First Avenue, Fairbanks, AK 99701, United States","Zarnke, R.L., Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Evermann, J., Dept. of Vet. Clinical Sciences, College of Veterinary Medicine, Washington State University, Pullman, WA 99164-6610, United States; Ver Hoef, J.M., Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; McNay, M.E., Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Boertje, R.D., Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Gardner, C.L., Alaska Department of Fish and Game, P.O. Box 355, Tok, AK 99780-0355, United States; Adams, L.G., U.S. Geological Survey, Alaska Biological Science Center, 1011 East Tudor Road, Anchorage, AK 99503, United States; Dale, B.W., Alaska Department of Fish and Game, 333 Raspberry Road, Anchorage, AK 99518-1599, United States; Burch, J., National Park Service, 201 First Avenue, Fairbanks, AK 99701, United States","Wolves (Canis lupus) were captured in three areas of Interior Alaska (USA). Four hundred twenty-five sera were tested for evidence of exposure to canine coronavirus by means of an indirect fluorescent antibody procedure. Serum antibody prevalence averaged 70% (167/ 240) during the spring collection period and 25% (46/185) during the autumn collection period. Prevalence was 0% (0/42) in the autumn pup cohort (age 4-5 mo), and 60% (58/97) in the spring pup cohort (age 9-10 mo). Prevalence was lowest in the Eastern Interior study area. A statistical model indicates that prevalence increased slightly each year in all three study areas. These results indicate that transmission occurs primarily during the winter months, antibody decay is quite rapid, and reexposure during the summer is rare.","Canine coronavirus; Canis lupus; Serology; Survey; Wolf","Canidae; Canine coronavirus; Canis; Canis familiaris; Canis lupus; Coronavirus; virus antibody; animal; animal disease; article; blood; cohort analysis; Coronavirus; epidemiology; female; fluorescent antibody technique; immunology; male; season; United States; virus infection; wolf; Alaska; Animal; Antibodies, Viral; Cohort Studies; Coronavirus Infections; Coronavirus, Canine; Female; Fluorescent Antibody Technique, Indirect; Male; Seasons; Seroepidemiologic Studies; Support, U.S. Gov't, Non-P.H.S.; Wolves","Appel, M., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Veterinary Medicine, 83, pp. 360-366; Ballard, W.B., Stephenson, R.O., Spraker, T.H., (1981) Nelchina Basin Wolf Studies, , Alaska Department of Fish and Game. Federal Aid in Wildlife Restoration. Final Report. Grants W-17-8, W-17-9, W-17-10, and W-17-11. 201 pp; Carbyn, L.N., Incidence of disease and its potential role in the population dynamics of wolves in Riding Mountain National park, Manitoba (1982) Wolves of the World, pp. 106-116. , F. H. Harrington and P. C. Paquet (eds.). Noyes Publishing, Park Ridge, New Jersey; Carmichael, L.E., Binn, L.N., New enteric viruses in the dog (1981) Advances in Veterinary Science and Comparative Medicine, 25, pp. 1-37; Davidson, W.R., Appel, M.J., Doster, G.L., Baker, O.E., Brown, J.F., Diseases and parasites of red foxes, gray foxes, and coyotes from commercial sources selling to fox-chasing enclosures (1992) Journal of Wildlife Diseases, 28, pp. 581-589; Evermann, J.F., Benfield, D.A., Coronaviral infections (2000) Infectious Diseases of Wild Animals, , E. S. Williams and I. K. Barker, (eds.). Iowa State University Press, Ames, Iowa, In Press; Foreyt, W., Maag-Miller, L., Leathers, C.W., McKeirnan, A.J., Leamaster, B., Acute hemorrhagic enteritis associated with canine coronavirus and parvovirus infections in a captive coyote population (1980) Journal of the American Veterinary Medical Association, 177, pp. 784-786; Mckeirnan, A.J., Eugster, A.K., Solzano, R.F., Collins, J.K., Black, J.W., Kim, J.S., Update on canine coronavirus infections and interactions with other enteric pathogens of the dog (1989) Companion Animal Practice, 19, pp. 6-12; Foreyt, W.J., Evermann, J.F., Serologic survey of canine coronavirus in wild coyotes in the western United States, 1972-1982 (1985) Journal of Wildlife Diseases, 21, pp. 428-430; Garcelon, D.K., Wayne, R.K., Gonzales, B.J., A serologic survey of the island fox (Urocyon littoralis) on the Channel Islands, California (1992) Journal of Wildlife Diseases, 28, pp. 223-229; Green, J.S., Bruss, M.L., Evermann, J.F., Bergstrom, P.K., Serologic response of captive coyotes (Canis latrans say) to canine parvovirus and accompanying profiles of canine coronavirus titers (1984) Journal of Wildlife Diseases, 20, pp. 6-11; Herreweigh, A.A., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and Canine coronavirus (1998) Journal of Virology, 72, pp. 4508-4514; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Virology, Third Edition, pp. 1075-1093. , B. N. Fields, D. M. Knipe, and P. M. Howley (eds.). Lippincott-Raven Publishers, Philadelphia, Pennsylvania; Holzman, S., Conroy, M.J., Davidson, W.R., Diseases, parasites and survival of coyotes in south-central Georgia (1992) Journal of Wildlife Diseases, 28, pp. 572-580; Mccullagh, P., Nelder, J.A., (1989) Generalized Linear Models. 2nd Edition, , Chapman and Hall, London, UK, 511 pp; Mech, L.D., (1970) The Wolf: The Ecology and Behavior of an Endangered Species, , The Natural History Press, Garden City, New York, 384 pp; Adams, L.G., Meier, T.J., Burch, J.W., (1998) The Wolves of Denali, , University of Minnesota Press, Minneapolis, Minnesota, 227 pp; Neiland, K.A., Rangiferine brucellosis in Alaskan canids (1970) Journal of Wildlife Diseases, 6, pp. 136-139; Peterson, R.O., Woolington, J.D., Bailey, T.N., Wolves of the Kenai Peninsula. Alaska (1984) Wildlife Monographs, 88. , 52 pp; Thomas, N.J., Thurber, J.M., Vucetich, J.A., Waite, T.A., Population limitation and wolves of Isle Royale (1998) Journal of Mammalogy, 79, pp. 828-841; Stephenson, R.O., James, D., Wolf movement and food habits in northwest Alaska (1982) Wolves of the World, pp. 26-112. , F. H. Harrington and P. C. Paquet (eds.). Noyes Publ., Park Ridge, New Jersey; Ritter, D.G., Nielsen, C.A., Serologic survey for canine distemper and infectious canine hepatitis in wolves in Alaska (1982) Journal of Wildlife Diseases, 18, pp. 419-424; Stott, J.L., Coronaviridae (1999) Veterinary Microbiology, pp. 418-429. , D. M. Hirsh and Y. C. Zee (eds.). Blackwell Science, Malden, Massachusetts; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Gaskell, C.J., Canine coronavirus infection in the dog following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18; Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Veterinary Record, 132, pp. 7-11; Tsunetitsu, H., El-Kanawati, R., Smith, D.R., Reed, H.H., Saif, L.J., Isolation of coronavirus antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) Journal of Clinical Microbiology, 33, pp. 3264-3269; Zarnke, R.L., Ballard, W.B., Serologic survey for selected microbial pathogens of wolves in Alaska, 1975-1982 (1987) Journal of Wildlife Diseases, 23, pp. 77-85","Zarnke, R.L.; Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; email: randy_zarnke@fishgame.state.ak.us",,"Wildlife Disease Association, Inc.",00903558,,,"11763737","English","J. Wildl. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0035491944
"Sigurardóttir Ó.G., Kolbjornsen O., Lutz H.","7801581519;16156988000;57202819852;","Orchitis in a cat associated with coronavirus infection",2001,"Journal of Comparative Pathology","124","2-3",,"219","222",,14,"10.1053/jcpa.2000.0443","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034942290&doi=10.1053%2fjcpa.2000.0443&partnerID=40&md5=dfb8fb19bc9418b55669932d3f2920d7","Section of Pathology, National Veterinary Institute, Dep. 0033, P.O. Box 8156, Oslo, Norway; Clinical Laboratory, Department of Internal Veterinary Medicine, Winterhurestr. 260, 8057 Zurich, Switzerland","Sigurardóttir, Ó.G., Section of Pathology, National Veterinary Institute, Dep. 0033, P.O. Box 8156, Oslo, Norway; Kolbjornsen, O., Section of Pathology, National Veterinary Institute, Dep. 0033, P.O. Box 8156, Oslo, Norway; Lutz, H., Clinical Laboratory, Department of Internal Veterinary Medicine, Winterhurestr. 260, 8057 Zurich, Switzerland","A case of severe, pyogranulomatous and necrotizing orchitis in a cat, which later succumbed to systemic feline infectious peritonitis (FIP), is described. The 3.5-year-old cat, positive for feline immunodeficiency virus infection, presented with a left testicular enlargement. A few months after castration the animal was humanely destroyed due to declining health. Post-mortem examination revealed inflammatory lesions in abdominal organs and in the brain compatible with FIP. Infection was confirmed with a reverse transcriptase-polymerase chain reaction test and by immunohistochemical demonstration of coronavirus antigen in the affected tissues, including the left testicle. FIP is usually as systemic disease. However, lesions and presenting clinical signs in a single organ system such as the brain are not uncommon. The results of this case study indicate that orchitis, although rare, should be on the list of lesions of FIP. © 2001 Harcourt Publishers Ltd.",,"virus antigen; abdominal organ rupture; article; autopsy; bacterial peritonitis; brain injury; castration; cat; cat disease; Coronavirus; Feline immunodeficiency virus; immunohistochemistry; male; nonhuman; orchitis; reverse transcription polymerase chain reaction; systemic disease; testis; testis size; virus infection","Davidson, M.G., Rottman, J.B., English, R.V., Lappin, M.R., Tompkins, M.B., Feline immunodeficiency virus predisposes cats to acute generalized toxoplasmosis (1993) American Journal of Pathology, 143, pp. 1486-1497; Foley, J.E., Lapointe, J.M., Koblik, P., Poland, A., Pedersen, N.C., Diagnostic features of clinical neurologic feline infectious peritonitis (1998) Journal of Veterinary Internal Medicine, 12, pp. 415-423; Foster, R.A., Caswell, J.L., Rinkardt, N., Chronic fibrinous and necrotic orchitis in a cat (1996) Canadian Veterinary Journal, 37, pp. 681-682; Gut, M., Leutenegger, C., Huder, J., Pedersen, N., Lutz, H., One-tube fluorogenic reverse transcription-polymerase chain reaction for the quantitation of feline coronavirus (1999) Journal of Virological Methods, 77, pp. 37-46; Holash, J.A., Harik, S.I., Perry, G., Stewart, P.A., Barrier properties of testis microvessels (1993) Proceedings of the National Academy of Sciences of the United States of America, 90, pp. 11069-11073; Kipar, A., Bellmann, S., Kremendahl, J., Köhler, K., Reinacher, M., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Veterinary Immunology and Immunopathology, 65, pp. 243-257; Ladds, P.W., The male genital system (1993) Pathology of Domestic Animals, 4th Edit, , K. V. F. Jubb, P. C. Kennedy and N. Palmer, Eds, Academic Press, New York; Mukasa, A., Hiromatsu, K., Matsuzaki, G., O'Brien, R., Born, W., Nomoto, K., Bacterial infection of the testis leading to autoaggressive immunity triggers apparently opposed response of αβ and γδ T cells (1995) Journal of Immunology, 155, pp. 2047-2056; Paltrinieri, S., Cammarata, M.P., Cammarata, G., Comazzi, S., Some aspects of humoral and cellular immunity in naturally occurring feline infectious peritonitis (1998) Veterinary Immunology and Immunopathology, 65, pp. 205-220; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Practice, 23, pp. 7-20; Tammer, R., Evensen, O., Lutz, H., Reinacher, M., Immunohistological demonstration of feline infectious peritonitis virus antigen in paraffin-embedded tissues using feline ascites or murine monoclonal antibodies (1995) Veterinary Immunology and Immunopathology, 49, pp. 177-182",,,,00219975,,,"11222021","English","J. Comp. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0034942290
"Chouljenko V.N., Lin X.Q., Storz J., Kousoulas K.G., Gorbalenya A.E.","6603655227;36768282000;7006694594;7003476092;7005626044;","Comparison of genomic and predicted amino acid sequences of respiratory and enteric bovine coronaviruses isolated from the same animal with fatal shipping pneumonia",2001,"Journal of General Virology","82","12",,"2927","2933",,52,"10.1099/0022-1317-82-12-2927","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035192831&doi=10.1099%2f0022-1317-82-12-2927&partnerID=40&md5=1d69ad2b6b400c860d5f76fd7e4d9640","Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Chouljenko, V.N., Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Lin, X.Q., Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Storz, J., Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Kousoulas, K.G., Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Gorbalenya, A.E., Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","The complete genome sequences are reported here of two field isolates of bovine coronavirus (BCoV), which were isolated from respiratory and intestinal samples of the same animal experiencing fatal pneumonia during a bovine shipping fever epizootic. Both genomes contained 31028 nucleotides and included 13 open reading frames (ORFs) flanked by 5′- and 3′-untranslated regions (UTRs). ORF1a and ORF1b encode replicative polyproteins pp1a and pp1ab, respectively, that contain all of the putative functional domains documented previously for the closest relative, mouse hepatitis virus. The genomes of the BCoV isolates differed in 107 positions, scattered throughout the genome except the 5′-UTR. Differences in 25 positions were non-synonymous and were located in all proteins except pp1b. Six replicase mutations were identified within or immediately downstream of the predicted largest pp1a-derived protein, p195/ p210. Single amino acid changes within p195/ p210 as well as within the S glycoprotein might contribute to the different phenotypes of the BCoV isolates.",,"amino acid; nucleotide; polyprotein; virus protein; 3' untranslated region; 5' untranslated region; amino acid sequence; article; cattle disease; comparative study; controlled study; Coronavirus; gene mutation; gene sequence; intestine; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; open reading frame; phenotype; pneumonia; prediction; priority journal; protein domain; respiratory system; sample; virus genome; virus isolation; zoonosis; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; DNA viruses; Murinae; Murine hepatitis virus; RNA viruses","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceedings of the National Academy of Sciences, USA, 97, pp. 5516-5521; Ballesteros, M.L., Sanchez, C.M., Martin-Caballero, J., Enjuanes, L., Molecular bases of tropism in the PUR46 cluster of transmissible gastroenteritis coronaviruses (1995) Advances in Experimental Medicine and Biology, 380, pp. 557-562; 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Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) Journal of Virology, 71, pp. 3285-3287; Kubo, H., Takase-Yoden, S., Taguchi, F., Neutralization and fusion inhibition activities of monoclonal antibodies specific for the S1 subunit of the spike protein of neurovirulent murine coronavirus JHMV c1-2 variant (1993) Journal of General Virology, 74, pp. 1421-1425; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lim, K.P., Ng, L.F., Liu, D.X., Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products (2000) Journal of Virology, 74, pp. 1674-1685; 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Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Schuler, G.D., Altschul, S.F., Lipman, D.J., A workbench for multiple alignment construction and analysis (1991) Proteins, 9, pp. 180-190; Shi, S.T., Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Oh, J.W., Lai, M.M., Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells (1999) Journal of Virology, 73, pp. 5957-5969; Siddell, S., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Edited by S. G. Siddell. New York: Plenum Press; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J., Comparison of the genome organization of toro- and coronaviruses: Evidence for two nonhomologous RNA recombination events during Berne virus evolution (1991) Virology, 180, pp. 448-452; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2952; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Research, 60, pp. 181-189; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) Journal of the American Veterinary Medical Association, 208, pp. 1452-1455; Storz, J., Lin, X., Purdy, C.W., Chouljenko, V.N., Kousoulas, K.G., Enright, F.M., Gilmore, W.C., Loan, R.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans′ criteria for causation (2000) Journal of Clinical Microbiology, 38, pp. 3291-3298; Storz, J., Purdy, C.W., Lin, X., Burrell, M., Truax, R.E., Briggs, R.E., Frank, G.H., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) Journal of the American Veterinary Medical Association, 216, pp. 1599-1604; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) Journal of Virology, 64, pp. 3042-3050; Swofford, D.L., PAUP*: Phylogenetic analysis using parsimony (*and other methods) (2000), version 4. Sunderland, MA : Sinauer Associates; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTALwindows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Research, 25, pp. 4876-4882; Tijms, M.A., Van Dinten, L.C., Gorbalenya, A.E., Snijder, E.J., A zinc finger-containing papain-like protease couples sub-genomic mRNA synthesis to genome translation in a positive-stranded RNA virus (2001) Proceedings of the National Academy of Sciences, USA, 98, pp. 1889-1894; Van der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J., Locker, J.K., Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) Journal of Virology, 73, pp. 7641-7657; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Current Topics in Microbiology and Immunology, 99, pp. 165-200; Yoo, D.W., Parker, M.D., Babiuk, L.A., The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells (1991) Virology, 180, pp. 395-399; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) Journal of General Virology, 81, pp. 853-879; Ziebuhr, J., Thiel, V., Gorbalenya, A.E., The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond (2001) Journal of Biological Chemistry, 276, pp. 33220-33232","Kousoulas, K.G.; Dept. of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; email: vtgusk@lsu.edu",,"Society for General Microbiology",00221317,,JGVIA,"11714968","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035192831
"Dalton K., Casais R., Shaw K., Stirrups K., Evans S., Britton P., Brown T.D.K., Cavanagh D.","7006042187;6602185676;7202206256;57210222541;7402709581;57203302770;56248391000;26642890500;","cis-acting sequences required for coronavirus infectious bronchitis virus defective-RNA replication and packaging",2001,"Journal of Virology","75","1",,"125","133",,43,"10.1128/JVI.75.1.125-133.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034751118&doi=10.1128%2fJVI.75.1.125-133.2001&partnerID=40&md5=fc067eb1914ed6815cb752abc4997d94","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","Dalton, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Casais, R., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Shaw, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Stirrups, K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Evans, S., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Brown, T.D.K., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","The parts of the RNA genome of infectious bronchitis virus (IBV) required for replication and packaging of the RNA were investigated using deletion mutagenesis of a defective RNA (D-RNA) CD-61 (6.1 kb) containing a chloramphenicol acetyltransferase reporter gene. A D-RNA with the first 544, but not as few as 338, nucleotides (nt) of the 5' terminus was replicated; the 5' untranslated region (UTR) comprises 528 nt. Region I of the 3' UTR, adjacent to the nucleocapsid protein gene, comprised 212 nt and could be removed without impairment of replication or packaging of D-RNAs. A D-RNA with the final 338 nt, including the 293 nt in the highly conserved region II of the 3' UTR, was replicated. Thus, the 5'-terminal 544 nt and 3'-terminal 338 nt contained the necessary signals for RNA replication. Phylogenetic analysis of 19 strains of IBV and 3 strains of turkey coronavirus predicted a conserved stem-loop structure at the 5' end of region II of the 3' UTR. Removal of the predicted stem-loop structure abolished replication of the D-RNAs. D-RNAs in which replicase gene 1b-derived sequences had been removed or replaced with all the downstream genes were replicated well but were rescued poorly, suggesting inefficient packaging. However, no specific part of the 1b gene was required for efficient packaging.",,"cis acting element; nucleocapsid protein; animal cell; article; Coronavirus; deletion mutant; DNA packaging; nonhuman; nucleotide sequence; phylogeny; priority journal; RNA replication; virus genome; virus infection; virus morphology; virus nucleocapsid; virus replication; 3' Untranslated Regions; Animals; Cercopithecus aethiops; Defective Viruses; Infectious bronchitis virus; RNA, Viral; Vero Cells; Viral Structural Proteins; Virus Assembly","Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3' untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Brian, D.A., Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Role of subgenomic minus-strand RNA in coronavirus replication (1994) Arch. Virol., 9 (SUPPL.), pp. 173-180; Cavanagh, D., Brian, D.A., Brinton, M.A., Enjuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Chang, R.Y., Brian, D.A., cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Cologna, R., Hogue, B.G., Identification of a bovine coronavirus packaging signal (2000) J. Virol., 74, pp. 580-583; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses - A review (2000) Avian Pathol., 29, pp. 207-212; Hsue, B., Masters, P.S., A bulged stem-loop structure in the 3'untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J. Virol., 71, pp. 7567-7578; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Mendez, A., Plana-Duran, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Kim, Y.-N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Kim, Y.N., Makino, S., Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal (1995) J. Virol., 69, pp. 4963-4971; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lin, Y.J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Lin, Y.J., Liao, C.L., Lai, M.M., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. 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Virol., 64, pp. 6045-6053; Matzura, O., Wennborg, A., RNAdraw: An integrated program for RNA secondary structure calculation and analysis under 32-bit Microsoft Windows (1996) CABIOS, 12, pp. 247-249; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Repass, J.F., Makino, S., Importance of the positive-strand RNA secondary structure of a murine coronavirus defective interfering RNA internal replication signal in positive-strand RNA synthesis (1998) J. 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Virol., 81, pp. 791-801; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., Cloning and sequencing of genes encoding structural proteins of avian infectious bronchitis virus (1988) Virology, 165, pp. 589-595; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J.M., A domain at the 3' end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Van der Most, R.G., Luytjes, W., Rutjes, S., Spaan, W.J.M., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J. Virol., 69, pp. 3744-3751; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Analysis of a hypervariable region in the 3' non-coding end of the infectious bronchitis virus genome (1993) Virus Res., 28, pp. 19-27; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other coronaviruses (1992) Virus Res., 25, pp. 213-222; Williams, G.D., Chang, R.Y., Brian, D.A., A phylogenetically conserved hairpin-type 3' untranslated region pseudoknot functions in coronavirus RNA replication (1999) J. Virol., 73, pp. 8349-8355","Cavanagh, D.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; email: dave.cavanagh@bbsrc.ac.uk",,,0022538X,,JOVIA,"11119581","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034751118
"Naylor M.J., Monckton R.P., Lehrbach P.R., Deane E.M.","7103407832;6603011612;6603728862;7006255983;","Canine coronavirus in Australian dogs",2001,"Australian Veterinary Journal","79","2",,"116","119",,29,"10.1111/j.1751-0813.2001.tb10718.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035258988&doi=10.1111%2fj.1751-0813.2001.tb10718.x&partnerID=40&md5=49981a2cba646f0c6d77cfcfc1962494","School of Science, University of Western Sydney, Kingswood, NSW 2747, Australia; Fort Dodge Australia Pty Limited, 1 Maitland Place, Baulkham Hills, NSW 2153, Australia","Naylor, M.J., School of Science, University of Western Sydney, Kingswood, NSW 2747, Australia; Monckton, R.P., Fort Dodge Australia Pty Limited, 1 Maitland Place, Baulkham Hills, NSW 2153, Australia; Lehrbach, P.R., Fort Dodge Australia Pty Limited, 1 Maitland Place, Baulkham Hills, NSW 2153, Australia; Deane, E.M., School of Science, University of Western Sydney, Kingswood, NSW 2747, Australia","Objective: To estimate the frequency of serum antibodies (IgG and IgM) to canine coronavirus (CCV) in the Australian dog population and evaluate the role of CCV as a causative agent of gastroenteritis. Design: A serological survey of antibodies to CCV among different dog populations. Procedure: The development and characterisation of an indirect ELISA for the detection of antibodies (IgG and IgM) to CCV was undertaken. Sera collected from both diarrhoeal and non-diarrhoeal dogs from various populations throughout Australia were tested for these antibodies to CCV. Results: Serum samples (1396) collected from 1984 to 1998 were tested for the presence of IgG antibodies to CCV. Samples were divided into two categories on the basis of the number of dogs housed together. The groups were either an open population containing dogs housed as groups of three or less, or kennel populations. Sera from 15.8% of the open population and 40.8% of kennelled dogs were positive for CCV antibodies. The prevalence of antibodies varied from zero to 76% in kennelled dogs. About 23% of 128 dogs positive for IgG antibodies to CCV were also positive for IgM antibodies to CCV, indicating recent CCV infection. Of those dogs that were presented with clinical signs of gastroenteritis such as diarrhoea and vomiting(n = 29), 85% were positive in the IgM ELISA and 85.7% in the IgG ELISA for antibodies to CCV. In comparison, for those dogs presented without any history of gastroenteritis only 15% were positive for IgM and 30% positive for IgG. Conclusion: Serological evidence indicates that infection with CCV in dogs is widespread throughout the Australian mainland. The prevalence of antibodies varies greatly among different populations, with an average of 40.8% positive in kennelled populations and 15.8% in the open population.","Canine coronavirus; Dogs; ELISA; Gastroenteritis; Serological survey","Canine coronavirus; Canis familiaris; Coronavirus; immunoglobulin G; immunoglobulin M; virus antibody; animal; animal disease; animal housing; article; Australia; blood; Coronavirus; dog; dog disease; enzyme linked immunosorbent assay; female; gastroenteritis; immunology; isolation and purification; male; prevalence; virology; virus infection; Animals; Antibodies, Viral; Australia; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Enzyme-Linked Immunosorbent Assay; Female; Gastroenteritis; Housing, Animal; Immunoglobulin G; Immunoglobulin M; Male; Prevalence","Binn, L.N., Lazar, E.C., Keenan, K.P., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proceedings of the 78th Annual Meeting of the us Animal Health Assoc, pp. 359-366. , Roanoke, Va; Kennan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71:Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) Am J Vet Res, 37, pp. 247-256; Binn, L.N., Alford, J.P., Marchwicki, R.H., Studies of respiratory disease in random source laboratory dogs: Viral infections in unconditioned dogs (1979) Lab Anim Sci, 29, pp. 48-52; McNulty, M.S., Curran, W.L., McFerran, J.B., Collins, D.S., Viruses and diarrhoea in dogs (1980) Vet Rec, 106, pp. 350-351; Greene, C.E., (1990) Infectious Disease in the Dog and Cat, pp. 281-283. , Saunders, Philadelphia; Schnagl, R.D., Holmes, I.H., Coronavirus-like particles in stools from dogs, from some country areas of Australia (1978) Vet Rec, 102, pp. 528-529; Marshall, J.A., Healey, D.S., Studdert, M.J., Viruses and virus-like particles in the faeces of dogs with and without diarrhoea (1984) Aust Vet J, 61, pp. 33-38; Finlaison, D.S., Faecal viruses of dogs - An electron microscope study (1995) Vet Microbiol, 46, pp. 295-305; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro-neutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jap J Vet Sci, 49, pp. 563-565; Tuchiya, K., Horimoto, T., Azetaka, M., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet Microbiol, 26, pp. 41-51; Rimmelzwaan, G.F., Giroen, J., Egberink, H., The use of an enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in the Netherlands (1991) Vet Microbiol, 26, pp. 25-40; Osterhaus, A.D.M.E., Drost, G.A., Wirahadiredja, R.M.S., Van Den Ingh, T.S.G.A.M., Canine viral enteritis: Prevalence of parvo-, corona-, and rotavirus infections in dogs in the Netherlands (1980) Vet Quart, 2, pp. 181-190; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Vet Rec, 132, pp. 7-11; Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet Med, 83, pp. 360-366; Brunner, C.J., Swango, L.J., Canine parvoviral infection: Effects on the immune system and factors that predispose to severe disease (1985) Compend Cont Educ Pract Vet, 7, pp. 979-989; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res Vet Sci, 51, pp. 11-18","Lehrbach, P.R.; Fort Dodge Australia Pty Limited, 1 Maitland Place, Baulkham Hills, NSW 2153, Australia",,"Australian Veterinary Association",00050423,,,"11256282","English","Austr. Vet. J.",Article,"Final",Open Access,Scopus,2-s2.0-0035258988
"Loa C.C., Lin T.L., Wu C.C., Bryan T., Thacker H.L., Hooper T., Schrader D.","6602648721;7404860140;7501664098;7005517787;7007150767;7005121335;7007179253;","Humoral and cellular immune responses in Turkey poults infected with Turkey coronavirus",2001,"Poultry Science","80","10",,"1416","1424",,18,"10.1093/ps/80.10.1416","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035487119&doi=10.1093%2fps%2f80.10.1416&partnerID=40&md5=3bc1f9e6e797838bde69259813258da0","Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Loa, C.C., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Lin, T.L., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T., Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Thacker, H.L., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","The objective of the present study was to elucidate the kinetics of humoral and cellular immune responses of turkey poults infected with turkey coronavirus (TCV). Turkey poults were orally inoculated with TCV at 10 d of age, and the immune responses were analyzed at 1, 3, 7, 14, 21, 28, 42, and 63 d postinfection (PI) in three different experiments. Total Ig to TCV was initially detected at 7 and 14 d PI in Experiments 1 and 3. In addition, Ig gradually increased from 7 to 21 d PI and remained at 80 immunofluroescent antibody assay (IFA) titers or more thereafter. Lymphocyte proliferation responses of spleen cells to concanavalin A were higher in TCV-infected turkeys than in noninfected control turkeys with significant differences (P &lt; 0.05) being noted at 14 and 63 d PI in Experiment 2 and at 3 and 28 d PI in Experiment 3. Strong IFA staining response to TCV antigen was observed in intestines of turkeys at 1. 3, and 7 d PI, and the response declined from 14 to 28 d PI in Experiment 3. In Experiment 3, the IgG isotype antibody response to TCV was markedly increased after 21 d PI and remained high until 63 d PI. The IgM isotype antibody response to TCV was 1.40 and 0.91 at 7 and 14 d PI, respectively. The IgA isotype antibody response to TCV was very low as detected at 7 (0.13), 14 (0.20), and 21 (0.17) d PI. Turkeys infected with TCV had significantly higher (P &lt; 0.05) antibody response to sheep erythrocytes than noninfected controls at 7d PI. Virus-specific lymphocyte proliferation response of spleen cells was significantly stimulated (P &lt; 0.05) at 63 d PI in Experiment 3. The proportion of the CD4+ subpopulation of T lymphocytes was significantly increased (P &lt; 0.05) at 1, 7, and 21 d PI in Experiment 3. The results indicate that humoral and cellular immunities to TCV are elicited in turkeys following infection with TCV.","Cellular; Humoral; Immune response; Turkey coronavirus; Turkey poult enteritis","concanavalin A; immunoglobulin; virus antibody; animal; animal disease; article; biosynthesis; bird disease; cellular immunity; Coronavirus; cytology; erythrocyte; female; fluorescent antibody technique; immunology; intestine; lymphocyte; lymphocyte activation; male; spleen; time; turkey (bird); virology; Animals; Antibodies, Viral; Concanavalin A; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Erythrocytes; Female; Fluorescent Antibody Technique, Indirect; Immunity, Cellular; Immunoglobulins; Intestines; Lymphocyte Activation; Lymphocytes; Male; Spleen; Time Factors; Turkeys","Barta, O., Barta, V., Domermuth, C.H., Pierson, F.W., Optimum conditions for the turkey lymphocyte transformation test (1992) Avian Dis., 36, pp. 386-394; Brim, T.A., VanCott, J.L., Lunney, J.K., Saif, L.J., Cellular immune responses of pigs after primary inoculation with porcine respiratory coronavirus or transmissible gastroenteritis virus and challenge with transmissible gastroenteritis virus (1995) Vet. Immunol. Immunopathol., 48, pp. 35-54; Dea, S., Garzon, S., Identification of coronaviruses by the use of indirect protein A-gold immunoelectron microscopy (1991) J. Vet. Diagn. Invest., 3, pp. 297-305; Dea, S., MarsoLais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1985) Avian Dis., 30, pp. 319-326; Dhinakar Raj, G., Jones, R.C., Infectious bronchitis virus: Immunopathogenesis of infection in the chicken (1997) Avian Pathol., 26, pp. 677-706; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Saif, L.J., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am. J. Vet. Res., 57, pp. 48-53; Heggen, C.L., Qureshi, M.A., Edens, F.W., Barnes, H.J., Havenstein, G.B., Alterations in the lymphocytic and mononuclear phagocytic systems of turkey poults associated with exposure to poult enteritis and mortality syndrome (1998) Avian Dis., 42, pp. 711-720; Lessard, M., Hutchings, D.L., Spencer, J.L., Cell-mediated and humoral immune responses in chickens infected with Salmonella typhimurium (1995) Avian Dis., 39, pp. 230-238; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Dis., 44, pp. 498-506; Nagaraja, K.V., Pomeroy, B.S., Secretory antibodies against turkey coronaviral enteritis (1978) Am. J. Vet. Res., 39, pp. 1463-1465; Nagaraja, K.V., Pomeroy, B.S., Cell-mediated immunity against turkey coronaviral enteritis (bluecomb) (1980) Am. J. Vet. Res., 41, pp. 915-917; Nagaraja, K.V., Pomeroy, B.S., Immunofluorescent studies on localization of secretory immunoglobulins in the intestines of turkeys recovered from turkey coronaviral enteritis (1980) Am. J. Vet. Res., 41, pp. 1283-1284; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry. 10th Ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, ed. Iowa State University Press, Ames, IA; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 1265-1267; Patel, B.L., Pomeroy, B.S., Gonder, E., Cronkite, C.E., Indirect fluorescent antibody test for the diagnosis of coronaviral enteritis of turkeys (bluecomb) (1976) Am. J. Vet. Res., 37, pp. 1111-1112; Reed, L.J., Muench, H., A simple method for estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Sharma, J.M., Belzer, S.W., Blastogenic response of whole blood cells of turkeys to a T-cell mitogen (1992) Dev. Comp. Immunol., 16, pp. 77-84; Slifka, M.K., Antia, R., Whitmire, J.K., Ahmed, R., Humoral immunity due to long-lived plasma cells (1998) Immunity, 8, pp. 363-372; Suresh, M., Sharma, J.M., Belzer, S.W., Studies on lymphocyte subpopulations and the effect of age on immune competence in turkeys (1993) Dev. Comp. Immunol., 17, pp. 525-535; Tizard, I., (1996) Veterinary Immunology: An Introduction. 5th Ed., , Saunders, New York, NY; Van Nerom, A., Ducatelle, R., Haesebrouck, F., Arnouts, S., Goddeeris, B., Davison, T.F., Kaspers, B., Monoclonal and polyclonal antibodies to chicken immunoglobulin isotypes specifically detect turkey immunoglobulin isotypes (1997) Vet. Immunol. Immunopathol., 57, pp. 305-314","Lin, T.L.; Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,"Poultry Science Association",00325791,,,"11599699","English","Poult. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0035487119
"Haring J., Perlman S.","7101956116;7102708317;","Mouse hepatitis virus",2001,"Current Opinion in Microbiology","4","4",,"462","466",,51,"10.1016/S1369-5274(00)00236-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034900010&doi=10.1016%2fS1369-5274%2800%2900236-8&partnerID=40&md5=a3eb0ca2d8e21c1bfa6d1b4073fad074","Departments of Microbiology and Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Haring, J., Departments of Microbiology and Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; Perlman, S., Departments of Microbiology and Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Inoculation of mice with most neurotropic strains of the coronavirus mouse hepatitis virus results in an immune response-mediated demyelinating disease that serves as an excellent animal model for the human disease multiple sclerosis. Recent work has shown that either virus-specific CD4+ or CD8+ T cells are able to mediate demyelination and also that the antibody response is crucial for clearing infectious virus. Another exciting advance is the development of recombinant coronaviruses, which, for the first time, will allow genetic manipulation of the entire viral genome.",,"animal experiment; animal model; cellular immunity; central nervous system infection; disease model; mouse; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; pathogenesis; review; viral genetics; virus cell interaction; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Stohlman, S.A., Bergmann, C.C., Perlman, S., Mouse hepatitis virus (1998) Persistent Viral Infections, pp. 537-557. , Edited by Ahmed R, Chen I. 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Altman, J., Moss, P., Goulder, P., Barouch, D., McHeyzer-Williams, M., Bell, J., McMichael, A., Davis, M., Phenotypic analysis of antigen-specific T lymphocytes (1996) Science, 274, pp. 94-96; Bergmann, C.C., Altman, J.D., Hinton, D., Stohlman, S.A., Inverted immunodominance and impaired cytolytic function of CD8+ T cells during viral persistence in the central nervous system (1999) J Immunol, 163, pp. 3379-3387; Pewe, L., Heard, S.B., Bergmann, C.C., Dailey, M.O., Perlman, S., Selection of CTL escape mutants in mice infected with a neurotropic coronavirus: Quantitative estimate of TCR diversity in the infected CNS (1999) J Immunol, 163, pp. 6106-6113; Haring, J.S., Pewe, L., Perlman, S., High magnitude, virus-specific CD4+ T cell response in the central nervous system of coronavirus-infected mice (2001) J Virol, 75, pp. 3043-3047; Zajac, A.J., Blattman, J.N., Murali-Krishna, K., Sourdive, D., Suresh, M., Altman, J.D., Ahmed, R., Viral immune evasion due to persistence of activated T cells without effector function (1998) J Exp Med, 188, pp. 2205-2213; Parra, B., Hinton, D., Marten, N., Bergmann, C., Lin, M.T., Yang, C.S., Stohlman, S.A., IFN-γ is required for viral clearance from central nervous system oligodendroglia (1999) J Immunol, 162, pp. 1641-1647; Marten, N.W., Stohlman, S.A., Atkinson, R.D., Hinton, D.R., Fleming, J.O., Bergmann, C.C., Contributions of CD8+ T cells and viral spread to demyelinating disease (2000) J Immunol, 164, pp. 4080-4088; Hawke, S., Stevenson, P.G., Freeman, S., Bangham, C.R., Long-term persistence of activated cytotoxic T lymphocytes after viral infection of the central nervous system (1998) J Exp Med, 187, pp. 1575-1582; Pewe, L., Wu, G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Stohlman, S.A., Bergmann, C.C., Lin, M.T., Cua, D.J., Hinton, D.R., CTL effector function within the central nervous system requires CD4+ T cells (1998) J Immunol, 160, pp. 2896-2904; Lane, T.E., Liu, M.T., Chen, B.P., Asensio, V.C., Samawi, R.M., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., A central role for CD4+ T cells and RANTES in virus-induced central nervous system inflammation and demyelination (2000) J Virol, 74, pp. 1415-1424; 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Stohlman, S.A., Hinton, D.R., Cua, D., Dimacali, E., Sensintaffar, J., Hofman, F.M., Tahara, S.M., Yao, Q., Tumor necrosis factor expression during mouse hepatitis virus-induced demyelinating encephalomyelitis (1995) J Virol, 69, pp. 5898-5903; Lane, T.E., Asensio, V., Yu, N., Paoletti, A.D., Campbell, I., Buchmeier, M.J., Dynamic regulation of α and β-chemokine expression in the central nervous system during mouse hepatitis virus-induced demyelinating disease (1998) J Immunol, 160, pp. 970-978; Liu, M.T., Chen, B.P., Oertel, P., Buchmeier, M.J., Armstrong, D., Hamilton, T.A., Lane, T.E., The T cell chemoattractant IFN-inducible protein 10 is essential in host defense against viral-induced neurologic disease (2000) J Immunol, 165, pp. 2327-2330; Liu, M.T., Armstrong, D., Hamilton, T.A., Lane, T.E., Expression of Mig (Monokine induced by interferon-gamma) is important in T lymphocyte recruitment and host defense following viral infection of the central nervous system (2001) J Immunol, 166, pp. 1790-1795; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv Virus Res, 53, pp. 245-264; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J Virol, 74, pp. 1393-1406; Williams, R.K., Jiang, G., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc Natl Acad Sci USA, 88, pp. 5533-5536; Chen, D., Asanaka, M., Yokomori, K., Wang, F., Hwang, S., Li, H., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc Natl Acad Sci USA, 92, pp. 12095-12099; Krueger, D.K., Kelly, S.M., Lewicki, D.N., Ruffolo, R., Gallagher, T.M., Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion (2001) J Virol, 75, pp. 2792-2802; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Das Sarma, J., Fu, L., Tsai, J.C., Weiss, S.R., Lavi, E., Demyelination determinants map to the spike glycoprotein gene of coronavirus mouse hepatitis virus (2000) J Virol, 74, pp. 9206-9213; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J Virol, 73, pp. 7607-7618; Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc Natl Acad Sci USA, 97, pp. 5516-5521; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J Virol, 74, pp. 10600-10611; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J Gen Virol, 82, pp. 1273-1281; Dandekar, A., Wu, G., Pewe, L.L., Perlman, S., Axonal damage is T cell mediated and occurs concomitantly with demyelination in mice infected with a neurotropic cornavirus (2001) J Virol, 75, pp. 6115-6120","Haring, J.; Department of Microbiology, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: jodie-haring@uiowa.edu",,"Elsevier Ltd",13695274,,COMIF,"11495812","English","Curr. Opin. Microbiol.",Review,"Final",,Scopus,2-s2.0-0034900010
"Anzai T., Fukunaga Y., Matsumura T., Imagawa H., Oikawa M.-A.","7102794220;7102147580;7402226666;8149749600;35458407700;","Serological examination for viral infection among young racehorses transported by vehicle over a long distance",2001,"Journal of Equine Science","12","4",,"135","137",,5,"10.1294/jes.12.135","https://www.scopus.com/inward/record.uri?eid=2-s2.0-31044432269&doi=10.1294%2fjes.12.135&partnerID=40&md5=5cbb6332880aaeceda042f4bafef2d53","Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; Equine Research Institute, Japan Racing Association, 321-4 Tokami-cho, Utsunomiya-Shi, Tochigi 320-0856, Japan","Anzai, T., Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; Fukunaga, Y., Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; Matsumura, T., Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; Imagawa, H., Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; Oikawa, M.-A., Equine Research Institute, Japan Racing Association, 321-4 Tokami-cho, Utsunomiya-Shi, Tochigi 320-0856, Japan","The influence of long distance transport on various viral infections was investigated serologically by examining 29 young racehorses for infection by respiratory agents including equine herpesvirus, equine adenovirus and equine rhinovirus, as well as coronavirus which has been suggested to be an etiological agent of diarrhea and febrile disease in horses. Serological evidence of infections by these viruses was not shown in any of the 18 febrile horses. However 4 of 11 nonfebrile horses which were loaded on the same vehicle as two horses which were seropositive for coronavirus, seroconverted after transportation.","Coronavirus; Racehorse; Shipping fever",,"Guy, J.S., Breslin, J.J., Breuhaus, B., Vivrette, S., Smith, L.G., Characterization of a coronavirus isolated from a diarrheic foal (2000) J. Clin. Microbiol., 38, pp. 4523-4526; Hayakawa, Y., Komae, H., Ide, H., Nakagawa, H., Yoshida, Y., Kamada, M., Kataoka, Y., Nakazawa, M., An occurrence of equine transport pneumonia caused by mixed infection with Pasterella caballi, Streptococcus suis and Streptococcus zooepidemicus (1993) J. Vet. Med. Sci., 55, pp. 455-456; Hoffman, A.M., Veil, L., Prescott, J.F., Incidence of lower respiratory disorders in large weanling farms: A review (1999) Proc. 8th Int. Conf. Equine Inf. Dis., pp. 95-98; Imagawa, H., Fukunaga, Y., Kamada, M., Detection of neutralizing antibody against calf diarrheal coronavirus in horse serum (1990) Bull. Equine Res. Inst., 27, pp. 25-30; Kamada, M., Akivama, Y., A survey on precipitating antibody against adenovirus in light horses of Japan (1977) Exp. Rep. Equine Hlth Lab., 14, pp. 29-37; Kamada, M., Akiyama, Y., Sato, K., Rodera, S., Isolation of adenovirus from adult Thoroughbred horses (1977) Jpn. J. Vet. Sci., 39, pp. 661-664; Kumanomido, T., Akiyama, Y., Serological survey of equine rhinovirus serotype 1 among light horses in Japan (1979) Exp. Rep. Equine Hlth Lab., 16, pp. 15-22; Matsumura, T., Sugiura, T., Imagawa, H., Fukunaga, Y., Kamada, M., Epizootiological aspects of type 1 and type 4 equine herpesvirus infections among horse populations (1992) J. Vet. Med. Sci., 54, pp. 207-211; Oikawa, M., Karnada, M., Yoshikawa, Y., Yoshikawa, T., Pathology of equine pneumonia associated with transport and isolation of Streptococcus equi subsp. zooepidemirus (1994) J. Comp. Path., 111, pp. 205-212; Sugiura, T., Matsumura, T., Fukunaga, Y., Isolation and identification of viruses from racehorses with pyrexia (1989) Bull Equine Res. Inst., 26, pp. 53-59; Sugiura, T., Matsumura, T., Fukunaga, Y., Hirasawa, K., Sero-epizootiological study of racehorses with pyrexia in the training centers of the Japan Racing Association (1987) Jpn J. Vet. Sci., 49, pp. 1087-1096; Wood, J.L.N., Newton, J.R., Chanter, N., Mumford, J.A., Townsent, H.G.G., Lakhani, R.H., Gower, S.M., Windsor, G.D., A longitudinal epidemiological study of respiratory disease in racehorses: Disease definition, prevalence and incidence (1999) Pror. 8th Int. Conf. Equine Inf. Dis., pp. 64-70","Anzai, T.; Epizootic Research Station, Equine Research Institute, Japan Racing Association, 1400-4 Shiba, Kokubunji-machi, Shimotsuga-gun, Tochigi 329-0412, Japan; email: anzai@epizoo.equinst.go.jp",,"Japanese Society of Equine Science",13403516,,,,"English","J. Equine Sci.",Article,"Final",Open Access,Scopus,2-s2.0-31044432269
"Savary K.C.M., Sellon R.K., Law J.M.","6602255708;7003800375;8273676100;","Chylous abdominal effusion in a cat with feline infectious peritonitis",2001,"Journal of the American Animal Hospital Association","37","1",,"35","40",,9,"10.5326/15473317-37-1-35","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035218681&doi=10.5326%2f15473317-37-1-35&partnerID=40&md5=c6b0097c5ec1b72658586599dc79c836","Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Dept. Microbiol., Pathol., P., College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Dept. of Vet. Clinical Sciences, Washington State University, Pullman, WA 99164-7060, United States","Savary, K.C.M., Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Sellon, R.K., Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States, Dept. of Vet. Clinical Sciences, Washington State University, Pullman, WA 99164-7060, United States; Law, J.M., Dept. Microbiol., Pathol., P., College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States","A 10-year-old cat was diagnosed with chyloperitoneum based on the effusion characteristics. Feline coronavirus serology was positive. The owner declined further evaluation and elected euthanasia. Necropsy revealed vasculitis with multifocal areas of necrosis and lymphocytic-plasmacytic inflammation in multiple solid organs, most likely due to feline infectious peritonitis (FIP). Immunohistochemistry was negative for FIP antigen. Notwithstanding, the final diagnosis of FIP was based on the characteristic histopathological lesions. Underlying causes of chyloperitoneum in cats and humans are discussed, and possible pathogenesis of the chyloperitoneum in association with a vasculitis such as FIP is discussed.",,"Coronavirus; Felidae; Feline coronavirus; Felis catus; animal; animal disease; article; ascites fluid; case report; cat; cat disease; chylous ascites; differential diagnosis; male; pathology; Animals; Ascitic Fluid; Cat Diseases; Cats; Chylous Ascites; Diagnosis, Differential; Feline Infectious Peritonitis; Male","Fossum, T.W., Forrester, S.D., Swenson, C.L., Chylothorax in cats: 37 cases (1969-1989) (1991) J Am Vet Med Assoc, 198, pp. 672-678; Gores, B.R., Berg, J., Carpenter, J.L., Ullman, S.L., Chylous ascites in cats: Nine cases (1978-1993) (1994) J Am Vet Med Assoc, 205, pp. 1161-1164; Myers, N.C., Engler, S.J., Jakowski, R.M., Chylothorax and chylous ascites in a dog with mediastinal lymphangiosarcoma (1996) J Am Anim Hosp Assoc, 32, pp. 263-269; Fossum, T.W., Hay, W.H., Boothe, H.W., Zack, P.M., Sherding, R.G., Miller, M.W., Chylous ascites in three dogs (1992) J Am Vet Med Assoc, 200, pp. 70-76; Robinson, W.F., Maxie, M.G., The cardiovascular system (1993) Pathology of Domestic Animals. 4th Ed., 3, pp. 51-53. , Jubb KVF, Kennedy PC, Palmer N, eds. San Diego: Academic Press; Michel, P., Pagliano, G., Le chyloperitoine aigu (1992) Journal de Chirurgie, 129, pp. 544-549; Hawkins, E.C., Clinical manifestations of pleural cavity and mediastinal disease (1998) Essentials of Small Animal Internal Medicine. 2nd Ed., pp. 313-318. , Nelson RW, Couto CG, eds. St Louis: Mosby; Fossum, T.W., Feline chylothorax (1993) Comp Cont Ed Sm Anim Pract, 15, pp. 549-564; Meadows, R.L., Mac Williams, P.S., Chylous effusions revisited (1994) Vet Clin Pathol, 23, pp. 54-62; Fossum, T.W., Jacobs, R.M., Birchard, S.J., Evaluation of cholesterol and triglyceride concentrations in differentiating chylous and non-chylous pleural effusion in dogs and cats (1986) J Am Vet Med Assoc, 188, pp. 49-51; Waddle, J.R., Gigers, U., Lipoprotein electrophoresis differentiation of chylous and non-chylous pleural effusions in dogs and cats and its correlation with pleural effusion triglyceride concentration (1990) Vet Clin Pathol, 19, pp. 80-85; McReynolds, C., Macy, D., Feline infectious peritonitis. Part I. Etiology and diagnosis (1997) Comp Cont Ed Sm Anim Pract, 19, pp. 1007-1016; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., An appraisal of the value of laboratory tests in the diagnosis of feline infectious peritoni-tis (1994) J Am Anim Hosp Assoc, 30, pp. 345-350; Nix, J.T., Albert, M., Dugas, J.E., Wendt, D.L., Chylothorax and chylous ascites: A study of 302 selected cases (1957) Am J Gastroenterol, 28, pp. 40-55; Browse, N.L., Wilson, N.M., Russo, F., Al-Hassan, H., Allen, D.R., Aetiology and treatment of chylous ascites (1992) Br J Surg, 79, pp. 1145-1150; Tsuchiya, M., Okazaki, I., Maruyama, K., Asakura, H., Morita, A., Chylous ascites formation and a review of 84 cases (1973) Angiology, 24, pp. 576-584; Abadoglu, O., Osma, E., Ucan, E.S., Behçet's disease with pulmonary involvement, superior vena cava syndrome, chyloptysis and chylous ascites (1996) Respir Med, 90, pp. 429-431; McReynolds, C., Macy, D., Feline infectious peritonitis. Part II. Treatment and prevention (1997) Comp Cont Ed Sm Anim Pract, 19, pp. 1111-1117; Harvey, C.J., Lopez, J.W., Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) J Am Vet Med Assoc, 209, pp. 1117-1120","Savary, K.C.M.; Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States",,"American Animal Hospital Association",05872871,,JAAHB,"11204475","English","J. Am. Anim. Hosp. Assoc.",Article,"Final",,Scopus,2-s2.0-0035218681
"Spagnolo J.F., Hogue B.G.","6508353146;7003393593;","Requirement of the poly(A) tail in coronavirus genome replication",2001,"Advances in Experimental Medicine and Biology","494",,,"467","474",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703841&partnerID=40&md5=89811bad8fcb5117ac98ba41707877b5","Department of Molecular Virology, Baylor College of Medicine, Houston, TX, United States","Spagnolo, J.F., Department of Molecular Virology, Baylor College of Medicine, Houston, TX, United States; Hogue, B.G., Department of Molecular Virology, Baylor College of Medicine, Houston, TX, United States",[No abstract available],,"3' untranslated region; 5' untranslated region; conference paper; Coronavirus; molecular interaction; nonhuman; priority journal; RNA analysis; sequence analysis; virus genome; virus replication; 3' Untranslated Regions; Animals; Cattle; Cell Line; Coronavirus, Bovine; Defective Viruses; Genome, Viral; Mice; Murine hepatitis virus; Poly(A)-Binding Proteins; RNA, Messenger; RNA-Binding Proteins; Virus Replication; Coronavirus","Chang, R.Y., Brian, D.A., cis Requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J Virol, 70, pp. 2201-2207; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J Virol, 68, pp. 8223-8231; Cui, T., Sankar, S., Porter, A.G., Binding of encephalomyocarditis virus RNA polymerase to the 3′-noncoding region of the viral RNA is specific and requires the 3′-poly(A) tail (1993) J Biol Chem, 268, pp. 26093-26098; De, R.J., Groot, Van, R.G., der Most, Spaan, W.J., The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations (1992) J Virol, 66, pp. 5898-5905; Hill, K.R., Hajjou, M., Hu, J.Y., Raju, R., RNA-RNA recombination in Sindbis virus: Roles of the 3′ conserved motif, poly(A) tail, and nonviral sequences of template RNAs in polymerase recognition and template switching (1997) J Virol, 71, pp. 2693-2704; Hofmann, M.A., Brian, D.A., The 5′ end of coronavirus minus-strand RNAs contains a short poly(U) tract (1991) J Virol, 65, pp. 6331-6333; Kim, Y.N., Jeong, Y.S., Makino, S., Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication (1993) Virology, 197, pp. 53-63; Lai, M.M., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: Mrna structure and genetic localization of the sequence divergence from hepatotropic strain MHV-3 (1981) J Virol, 39, pp. 823-834; Lin, Y.J., Lai, M.M., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J Virol, 67, pp. 6110-6118; Lin, Y.J., Liao, C.L., Lai, M.M., Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J Virol, 68, pp. 8131-8140; Sarnow, P., Role of 3′-end sequences in infectivity of poliovirus transcripts made in vitro (1989) J Virol, 63, pp. 467-470; Spagnolo, J.F., Hogue, B.G., Host protein interactions with the 3′ end of bovine coronavirus RNA and the requirement of the Poly(A) tail for coronavirus defective genome replication (2000) J Virol, 74, pp. 5053-5065; Spector, D.H., Baltimore, D., Requirement of 3′-terminal poly(adenylic acid) for the infectivity of poliovirus RNA (1974) Proc Natl Acad Sci U S A, 71, pp. 2983-2987; Van, R.G., der Most, Luytjes, W., Rutjes, S., Spaan, W.J., Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus (1995) J Virol, 69, pp. 3744-3751","Spagnolo, J.F.; Department of Molecular Virology, Baylor College of Medicine, Houston, TX, United States",,,00652598,,,"11774509","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035703841
"Matsuyama S., Watanabe R., Taguchi F.","7201442043;7202994471;7103209890;","Neurovirulence for mice of soluble receptor-resistant mutants of murine coronavirus JHMV",2001,"Advances in Experimental Medicine and Biology","494",,,"145","148",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703704&partnerID=40&md5=01c11e6829d30a7977087e0389ff651d","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Institute of Life Science, Soka University, 1-236 Tangi Hachiohji, Tokyo 192-8577, Japan","Matsuyama, S., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Watanabe, R., Institute of Life Science, Soka University, 1-236 Tangi Hachiohji, Tokyo 192-8577, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",[No abstract available],,"amino acid; receptor; spike protein; unclassified drug; virus protein; animal experiment; animal model; animal tissue; apoptosis; brain; central nervous system infection; conference paper; controlled study; histopathology; LD 50; male; mouse; Murine hepatitis coronavirus; neuropathology; nonhuman; priority journal; spinal cord; strain difference; survival; syncytium; virogenesis; virus mutant; virus pathogenesis; virus replication; virus strain; virus virulence; Animals; Brain; Central Nervous System Diseases; Coronavirus Infections; Glycoproteins; Membrane Glycoproteins; Mice; Mice, Inbred ICR; Murine hepatitis virus; Mutation; Spinal Cord; Viral Envelope Proteins; Virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) J. Virol., 71, pp. 9024-9031; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization or a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; Taguchi, F., Yamada, A., Fujiwara, K., Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: Enhanced antiviral activity of macrophages (1980) Infect. Immun., 29, pp. 42-49","Matsuyama, S.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",,,00652598,,,"11774459","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035703704
"Liu M.T., Chen B.P., Oertel P., Buchmeier M.J., Hamilton T.A., Armstrong D.A., Lane T.E.","56174294500;57198480594;6603655445;7006201704;35419190300;57196856509;24722465300;","The CXC chemokines IP-10 and Mig are essential in host defense following infection with a neurotropic coronavirus",2001,"Advances in Experimental Medicine and Biology","494",,,"323","327",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701625&partnerID=40&md5=38d9e465d09778dbdbb70d785fa6b0bb","Department of Molecular Biology and Biochemistry, University of California at Irvine, California, United States; The Scripps Research Institute, La Jolla, CA, United States; Department of Immunology, The Lerner Research Institute, Cleveland, OH, United States","Liu, M.T., Department of Molecular Biology and Biochemistry, University of California at Irvine, California, United States; Chen, B.P., Department of Molecular Biology and Biochemistry, University of California at Irvine, California, United States; Oertel, P., Department of Molecular Biology and Biochemistry, University of California at Irvine, California, United States; Buchmeier, M.J., The Scripps Research Institute, La Jolla, CA, United States; Hamilton, T.A., Department of Immunology, The Lerner Research Institute, Cleveland, OH, United States; Armstrong, D.A., Department of Immunology, The Lerner Research Institute, Cleveland, OH, United States; Lane, T.E., Department of Molecular Biology and Biochemistry, University of California at Irvine, California, United States",[No abstract available],,"alpha chemokine; gamma interferon; gamma interferon inducible protein 10; animal experiment; animal model; central nervous system infection; conference paper; controlled study; disease activity; host resistance; lymphocyte function; mortality; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; T lymphocyte; virus infection; virus load; Animals; Chemokines, CXC; Coronavirus Infections; Encephalomyelitis; Intercellular Signaling Peptides and Proteins; Mice; Murine hepatitis virus; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Asensio, V.C., Campbell, I.L., Chemokine gene expression in the brains of mice with lymphocytic choriomeningitis (1997) J. Virol., 71, pp. 7832-7840; Biddison, W.E., Cruikshank, W.W., Center, D.M., Pelfrey, C.M., Taub, D.D., Turner, R.V., CD8+ myelin peptide-specific T cells can chemoattract CD4+ myelin peptide specific T cells: Importance of IFN-inducible protein 10 (1998) J. Immunol., 160, pp. 444-448; Buchmeier, M.J., Lane, T.E., Viral-induced neurodegenerative disease (1999) Curr. Op. Micro., 2, pp. 398-402; Cheret, A., Le Grand, R., Caufour, P., Neildez, O., Matheux, F., Theodoro, F., Boussin, F., Dormont, D., Chemoattractant factors (IP-10, MIP-1 alpha, IL-16) mRNA expression in mononuclear cells from diferent tissues during acute SIVmac251 infection of macaques (1997) J. Med. Primatol., 26, pp. 19-26; Farber, J.M., Mig and IP-10: CXC chemokines that target lymphocytes (1997) J. Leukoc. Biol., 61, pp. 246-257; Hoffman, L.M., Fife, B.T., Begolka, W.S., Miller, S.D., Karpus, W.J., Central nervous system chemokine expression during Theiler's virus-induced demyelinating disease (1999) J. Neurovirol., 5, pp. 635-642; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Kolb, S.A., Sporer, B., Lahrtz, F., Koedel, U., Pfister, H.W., Fontana, A., Identification of a T cell chemotactic factor in the cerebral spinal fluid of HIV-infected individuals as interferon gamma inducible protein 10 (1999) J. Immunol., 163, pp. 5686-5692; Lane, T.E., Paoletti, A.D., Buchmeier, M.J., Disassociation between the in vitro and in vivo effects of nitric oxide on a neurotropic murine coronavirus (1997) J. Virol., 71, pp. 2202-2210; Lane, T.E., Asensio, V.C., Yu, N., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., Dynamic regulation of alpha and beta chemokine expression in the central nervous system during mouse hepatitis virus-induced demyelinating disease (1998) J. Immunol., 160, pp. 970-978; Lane, T.E., Liu, M.T., Chen, B.P., Asensio, V.C., Samawi, R.M., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., A central role for CD4+ T cells and RANTES in virus-induced central nervous system inflammation and demyelination (2000) J. Virol., 74, pp. 1415-1424; Loetsher, M., Gerber, B., Loetscher, P., Jones, S.A., Piali, L., Lewis, I.C., Baggiolini, M., Moser, B., Chemokine receptor specific for IP-10 and Mig: Structure, function and expression in activated T-lymphocytes (1996) J. Exp. Med., 184, pp. 963-969; Luster, A.D., Chemokines - Chemotactic cytokines that mediate inflammation (1998) N. Engl. J. Med., 338, pp. 436-445; Parra, B., Hinton, D.R., Marten, N.W., Bergmann, C.C., Lin, M.T., Yang, C.S., Stohlman, S.A., IFN-gamma is required for viral clearance from central nervous system oligodendroglia (1999) J. Immunol., 162, pp. 1641-1647; Piali, L., Weber, C., LaRosa, G., Mackay, C.R., Springer, T.A., Clark-Lewis, I., Moser, B., The chemokine receptor CXCR3 mediates rapid and shear-resistant adhesion-induction of effector T lymphocytes by the chemokines IP-10 and Mig (1998) Eur. J. Immunol., 28, pp. 961-972; Theil, D.J., Tsunoda, I., Libbey, J.E., Derfuss, T.J., Fujinami, R.S., Alterations in cytokine but not chemokine mRNA expression during three distinct Theiler's virus infections (2000) J. Neuroimmunol., 104, pp. 22-30","Liu, M.T.; Department of Molecular Biology, University of California, Irvine, CA, United States",,,00652598,,,"11774487","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035701625
"Boucher A., Denis F., Duquette P., Talbot P.J.","57197051778;35414314000;7005094902;7102670281;","Generation from multiple sclerosis patients of long-term t-cell clones that are activated by both human coronavirus and myelin antigens",2001,"Advances in Experimental Medicine and Biology","494",,,"355","362",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699616&partnerID=40&md5=f22edc4d52674fe311246fd941d6edec","Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada; Notre-Dame Hospital, Montreal, QC, H2L 4K, Canada","Boucher, A., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada; Denis, F., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada; Duquette, P., Notre-Dame Hospital, Montreal, QC, H2L 4K, Canada; Talbot, P.J., Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada",[No abstract available],,"myelin; central nervous system infection; conference paper; controlled study; Coronavirus; cross reaction; disease activity; human; human tissue; molecular mimicry; multiple sclerosis; nonhuman; pathogenesis; priority journal; serotype; T lymphocyte activation; virus infection; Cell Line; Clone Cells; Coronavirus 229E, Human; Cross Reactions; Humans; Lymphocyte Activation; Multiple Sclerosis; Myelin Basic Proteins; T-Lymphocytes; Coronavirus","Arbour, N., Ekandé, S., Côté, G., Lachance, C., Chagnon, F., Tardieu, M., Cashman, N.R., Talbot, P.J., Persistent infection of human oligodendrocytic and neuroglial cell lines by human coronavirus 229E (1999) J. Virol., 73, pp. 3326-3337; Arbour, N., Côté, G., Lachance, C., Tardieu, M., Cashman, N.R., Talbot, P.J., Acute and persistent infection of human neural cell lines by human coronavirus OC43 (1999) J. Virol., 73, pp. 3338-3350; Arbour, N., Day, R., Newcombe, J., Talbot, P.J., Neuroinvasion by human respiratory coronaviruses (2000) J. Virol., , in press; Bonavia, A., Arbour, N., Yong, V.W., Talbot, P.J., Infection of primary cultures of human neural cells by human coronaviruses 229E and OC43 (1997) J. Virol., 71, pp. 800-806; Burks, J.S., DeVald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Challoner, P.B., Smith, K.T., Parker, J.D., Macleod, D.L., Coulter, S.N., Rose, T.M., Schultz, E.R., Burmer, G.C., Plaque-associated expression of human herpesvirus 6 in multiple sclerosis (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 7440-7444; Collins, A.R., Sorensen, O., Regulation of viral persistence in human glioblastoma and rhabdomyosarcoma cells infected with coronavirus OC43 (1986) Microb. Pathog., 6, pp. 573-582; Ebers, G.C., Sadovnick, A.D., The role of genetic factors in multiple sclerosis susceptibility (1993) J. Neuroimmunol., 54, pp. 1-17; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol., 5, pp. 9-14; Murray, R.S., Brown, B., Brian, D., Cabirac, G.F., Detection of coronavirus RNA and antigen in multiple sclerosis brain (1992) Ann. Neurol., 31, pp. 525-533; Oldstone, M.B.A., Molecular mimicry and autoimmune disease (1987) Cell, 50, pp. 819-820; Sadovnick, A.D., Armstrong, H., Rice, G.P., Bulman, D., Hashimoto, L., Paty, D.W., Warren, S., Murray, T.J., A population-based study of multiple sclerosis in twins: Update (1993) Ann. Neurol., 33, pp. 281-285; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Talbot, P.J., Paquette, J.-S., Ciurli, C., Antel, J.P., Ouellet, F., Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis (1996) Ann. Neurol., 39, pp. 233-240; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 5930, pp. 150-153; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis (1973) Arch. Neurol., 5, pp. 298-303; Wekerle, H., Kojima, K., Lannes-Vieira, J., Lassmann, H., Linington, C., Animal models (1994) Ann. Neurol., 36, pp. S47-S53; Wucherpfennig, K.W., Strominger, J.L., Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein (1995) Cell, 80, pp. 695-705; Zhao, Z.S., Granucci, F., Yeh, L., Schaffer, P.A., Cantor, H., Molecular mimicry by herpes simplex virus-type 1: Autoimmune disease after viral infection (1998) Science, 279, pp. 1344-1347","Boucher, A.; Human Health Research Center, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC H7V 1B7, Canada",,,00652598,,,"11774492","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035699616
"Gélinas A.-M., Sasseville A.-J., Dea S.","6602090251;6603215910;7006056287;","Identification of specific variations within the HE, S1, and ORF4 genes of bovine coronaviruses associated with enteric and respiratory diseases in dairy cattle",2001,"Advances in Experimental Medicine and Biology","494",,,"63","67",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699365&partnerID=40&md5=e730465dfd3790273dbc434825bda45f","Centre de Recherche en Microbiologie et Biotechnologie, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada","Gélinas, A.-M., Centre de Recherche en Microbiologie et Biotechnologie, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada; Sasseville, A.-J., Centre de Recherche en Microbiologie et Biotechnologie, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada; Dea, S., Centre de Recherche en Microbiologie et Biotechnologie, INRS-Institut Armand-Frappier, Université du Québec, Laval, QC, H7V 1B7, Canada",[No abstract available],,"cattle; conference paper; Coronavirus; dairy industry; enteritis; gene isolation; genetic variability; he gene; nonhuman; orf4 gene; priority journal; respiratory tract disease; s1 gene; virus gene; Animals; Capsid Proteins; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Dairying; Diarrhea; Hemagglutinins, Viral; Open Reading Frames; Respiratory Tract Infections; Sequence Analysis, DNA; Variation (Genetics); Viral Fusion Proteins; Viral Proteins; Virulence; Bos taurus; Bovinae; Coronavirus","Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction (1987) Ann Biochem, 162, pp. 156-159; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus genes, 17, pp. 33-42; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation in cell cultures (1980) Am J Vet Res, 41, pp. 30-38; Dea, S., Michaud, L., Milane, G., Comparison of bovine coronavirus isolates associated with neonatal calf diarrhoea and winter dysentery in adult dairy cattle in Québec (1995) J Gen Virol, 76, pp. 1263-1270; Dea, S., Tijssen, P., Antigenic and polypeptide structure of turkey enteric coronaviruses as defined by monoclonal antibodies (1989) J Gen Virol, 70, pp. 1725-1741; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Milane, G., Kourtesis, A.B., Dea, S., Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates (1997) J Clin Microbiol, 35, pp. 33-40; Mounir, S., Talbot, P.J., Human coronavirus OC43 RNA lacks two open reading framed located downstream of the S gene of bovine coronavirus (1993) Virology, 192, pp. 355-360; Parker, M.D., Yoo, D., Babiuk, L.A., Expression and secretion of the bovine coronavirus hemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses (1990) J Virol, 64, pp. 1625-1629; Reynolds, D.J., Debney, T.J., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Spaan, W.D., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Storz, J., Stine, L., Liem, A., Coronavirus isolation from nasal swabs samples in cattle with signs of respiratory tract disease after shipping (1996) JAVMA, 208, pp. 1452-1454; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: Detailed antigenic analysis of S1, S2 and HE (1992) J Gen Virol, 73, pp. 1725-1737","Gélinas, A.-M.; Ctr. de Rech. Microbiol./Biotechnol., INRS-Institut Armand-Frappier, Université du Québec, Laval, QC H7V 1B7, Canada",,,00652598,,,"11774537","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035699365
"Kanjanahaluethai A., Baker S.C.","6603130302;7403307881;","Processing of the replicase of murine coronavirus: Papain-like proteinase 2 (PLP2) acts to generate p150 and p44",2001,"Advances in Experimental Medicine and Biology","494",,,"267","273",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699347&partnerID=40&md5=5fb42936dc8ffbcbeab707e2096a85e7","Department of Microbiology and Immunology, Loyala University of Chicago, Stritch School of Medicine, Maywood, IL, United States","Kanjanahaluethai, A., Department of Microbiology and Immunology, Loyala University of Chicago, Stritch School of Medicine, Maywood, IL, United States; Baker, S.C., Department of Microbiology and Immunology, Loyala University of Chicago, Stritch School of Medicine, Maywood, IL, United States",[No abstract available],,"papain like proteinase 2; protein orf1a; protein p 150; protein p44; proteinase; RNA directed RNA polymerase; unclassified drug; virus protein; conference paper; controlled study; enzyme activity; enzyme assay; HeLa cell; human; human cell; molecular model; Murine hepatitis coronavirus; nonhuman; priority journal; protein degradation; protein domain; protein processing; protein synthesis; Animals; Hela Cells; Humans; Mice; Murine hepatitis virus; Papain; Plasmids; Protein Precursors; RNA Replicase; Transfection; Viral Proteins; Coronavirus; Murinae; Murine hepatitis virus","Denison, M.R., Hughes, S.A., Weiss, S.R., Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59 (1995) Virology, 207, pp. 316-320; Denison, M.R., Zoltick, P.W., Hughes, S.A., Giangreco, B., Olson, A.L., Perlman, S., Leibowitz, L.L., Weiss, S.R., Intracellular processing of the N-terminal ORF1a proteins of the coronavirus MHV-A59 requires multiple proteolytic events (1992) Virology, 189, pp. 274-284; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Gosert, R., Kanjanahaluethai, A., Egger, D., Bienz, K., Baker, S.C., Comparison of replicase localization in different types of mouse hepatitis virus (MHV)-infected cells (2000) The Nidoviruses, , (E. Lavi, ed.), Plenum Press, New York (in press); Kanjanahaluethai, A., Baker, S.C., Identification of mouse hepatitis virus papain-like proteinase 2 activity (2000) J. Virol., , in press; Lemm, J.A., Rumenapf, T., Strauss, E.G., Strauss, J.H., Rice, C.M., Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus- and plus-strand RNA synthesis (1994) EMBO J., 13, pp. 2925-2934; Lim, K.P., Ng, L.F.P., Liu, D.X., Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame 1a of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products (2000) J. Virol., 74, pp. 1674-1685; Lu, Y., Sims, A.C., Denison, M.R., Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro (1998) J. Virol., 72, pp. 2265-2271; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Skirako, Y., Strauss, J.H., Regulation of Sindbis virus RNA replication: Uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis (1994) J. Virol., 68, pp. 1874-1885; Snijder, E.J., Meulenberg, J.J.M., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Van der Meer, Y., Van Tol, H., Locker, J.K., Snijder, E.J., ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex (1998) J. Virol., 72, pp. 6689-6698","Kanjanahaluethai, A.; Department of Microbiology, Loyala University of Chicago, Stritch School of Medicine, Maywood, IL, United States",,,00652598,,,"11774480","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035699347
"Lavi E., Weiss S.R., Hingley S.T.","7006986911;57203567044;6701491322;","The Nidoviruses (Coronaviruses and Arteriviruses): Preface",2001,"Advances in Experimental Medicine and Biology","494",,,"v","vii",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699195&partnerID=40&md5=2432e7621a5a91d7b7a19f687ce7e99d",,"Lavi, E.; Weiss, S.R.; Hingley, S.T.",[No abstract available],,"Arterivirus; conference paper; Coronavirus; gene structure; international cooperation; molecular evolution; nidovirus; nomenclature; nonhuman; priority journal; standard; taxonomy; virus; virus morphology; Arterivirus; Coronavirus",,,,"Kluwer Academic/Plenum Publishers",00652598,,AEMBA,,"English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699195
"Baker S.C., Kanjanahaluethai A., Sherer N.M., Axtell D.D., Schiller J.J.","7403307881;6603130302;6506598817;6507072617;56354099200;","Exploiting DNA immunization to generate polyclonal antisera to coronavirus replicase proteins",2001,"Advances in Experimental Medicine and Biology","494",,,"283","289",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699164&partnerID=40&md5=0d8b936bd5048b56d8cd33085e387983","Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States","Baker, S.C., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States; Kanjanahaluethai, A., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States; Sherer, N.M., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States; Axtell, D.D., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States; Schiller, J.J., Department of Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States",[No abstract available],,"cytotoxic T lymphocyte antigen 4; DNA vaccine; plasmid DNA; polyclonal antibody; RNA directed RNA polymerase; animal experiment; antibody blood level; antibody response; conference paper; controlled study; DNA synthesis; gene gun; immunization; immunostimulation; Murine hepatitis coronavirus; nonhuman; priority journal; rabbit; treatment outcome; Animals; Antibodies, Viral; Antigens, Viral; Cell Line; Hela Cells; Humans; Immunization; Murine hepatitis virus; Plasmids; Rabbits; RNA Replicase; Vaccines, DNA; Viral Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Oryctolagus cuniculus","Akbari, O., Panjwani, N., Garcia, S., Tascon, R., Lowrie, D., Stockinger, B., DNA vaccination: Transfection and activation of dendritic cells as key events for immunity (1999) J. Exp. Med., 189, pp. 169-177; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Boyle, J.S., Brady, J.L., Lew, A.M., Enhanced responses to a DNA vaccine encoding a fusion antigen that is directed to sites of immune induction (1998) Nature, 392, pp. 408-411; Boyle, J.S., Silva, A., Brady, J.L., Lew, A.M., DNA immunization: Induction of higher avidity antibody and effect of route on T cell cytotoxicity (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 14626-14631; Donnelly, J.J., Ulmer, J.B., Shiver, J.W., Liu, M.A., DNA vaccines (1997) Annu. Rev. Immunol., 15, pp. 617-648; Isono, T., Seto, A., Cloning and sequencing of the rabbit gene encoding T-cell costimulatory molecules (1995) Immunogenetics, 42, pp. 217-220; Kanjanahaluethai, A., Baker, S.C., Identification of activity of mouse hepatitis virus papain-like proteinase 2 (2000) J. Virol., , in press; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., Monica, N.L., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Letvin, N.L., Montefiori, D.C., Yasutomi, Y., Perry, H.C., Davies, M.E., Lekutis, C., Alroy, M., Shiver, J.W., Potent, protective anti-HIV immune responses generated by bimodal HIV envelope DNA plus protein vaccination (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9378-9383; Linsley, P.S., Brady, W., Urnes, M., Grosmaire, L.S., Damle, N.K., Ledbetter, J.A., CTLA-4 is a second receptor for the B cell activation antigen B7 (1991) J. Exp. Med., 174, pp. 561-569; Richmond, J.F.L., Lu, S., Santoro, J.C., Weng, J., Hu, S.L., Montefiori, D.C., Robinson, H.L., Studies of the neutralizing activity and avidity of anti-human immunodeficiency virus type 1 env antibody elicited by DNA priming and protein boosting (1998) J. Virol., 72, pp. 9092-9100; Robinson, H.L., Torres, C.A.T., DNA vaccines (1997) Semin. Immunol., 9, pp. 271-283; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Sundaram, P., Xiao, W., Brandsma, J.L., Particle-mediated delivery of recombinant expression vectors to rabbit skin induces high-titered polyclonal antisera (and circumvents purification of a protein immunogen) (1996) Nucl. Acids Res., 24, pp. 1375-1377; Takashima, A., Morita, A., Dendritic cells in genetic immunization (1999) J. Leukoc. Biol., 66, pp. 350-356; Torres, C.A.T., Iwasaki, A., Barber, B.H., Robinson, H.L., Differential dependence on target site tissue for gene gun and intramuscular DNA immunizations (1997) J. Immunol., 158, pp. 4529-4532; Wells, D.J., Improved gene transfer by direct plasmid injection associated with regeneration in mouse skeletal muscle (1993) FEBS, 332, pp. 179-182","Baker, S.C.; Department of Microbiology, Loyola University of Chicago, Stritch School of Medicine, Maywood, IL, United States",,,00652598,,,"11774482","English","Adv. Exp. Med. Biol.",Article,"Final",,Scopus,2-s2.0-0035699164
"Foley J.E., Leutenegger C.","7402872921;7006706489;","A review of coronavirus infection in the central nervous system of cats and mice",2001,"Journal of Veterinary Internal Medicine","15","5",,"438","444",,19,"10.1111/j.1939-1676.2001.tb01572.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035461670&doi=10.1111%2fj.1939-1676.2001.tb01572.x&partnerID=40&md5=01bf25318be43f88b0e2c5592c66e067","School of Veterinary Medicine, Center for Companion Animal Health, University of California, Davis, CA, United States; Dept. of Medicine and Epidemiology, University of California, Davis, CA, United States; School of Veterinary Medicine, Dept. of Medicine and Epidemiology, Davis, CA 95616, United States","Foley, J.E., School of Veterinary Medicine, Center for Companion Animal Health, University of California, Davis, CA, United States, Dept. of Medicine and Epidemiology, University of California, Davis, CA, United States, School of Veterinary Medicine, Dept. of Medicine and Epidemiology, Davis, CA 95616, United States; Leutenegger, C., Dept. of Medicine and Epidemiology, University of California, Davis, CA, United States","Feline infectious peritonitis (FIP) is a common cause of death in cats. Management of this disease has been hampered by difficulties identifying the infection and determining the immunological status of affected cats and by high variability in the clinical, pathological, and immunological characteristics of affected cats. Neurological FIP, which is much more homogeneous than systemic effusive or noneffusive FIP, appears to be a good model for establishing the basic features of FIP immunopathogenesis. Very little information is available about the immunopathogenesis of neurologic FIP, and it is reasonable to use research from the well-characterized mouse hepatitis virus (MHV) immune-mediated encephalitis system, as a template for FIP investigation, and to contrast findings from the MHV model with those of FIP. It is expected that the immunopathogenic mechanisms will have important similarities. Such comparative research may lead to better understanding of FIP immunopathogenesis and rational prospects for management of this frustrating disease. Copyright © 2001 by the American College of Veterinary Internal Medicine.","Cats; Feline infectious peritonitis; Mouse hepatitis virus; Neurological disease","animal; animal disease; cat; cat disease; Coronavirus; disease model; encephalitis; mouse; Murine hepatitis coronavirus; review; rodent disease; virology; virus infection; Animals; Cat Diseases; Cats; Coronavirus Infections; Coronavirus, Feline; Disease Models, Animal; Encephalitis; Feline Infectious Peritonitis; Mice; Murine hepatitis virus; Rodent Diseases","Foley, J., Pedersen, N., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Pract, 24, pp. 14-22; Poland, A.M., Vennema, H., Foley, J.E., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J Clin Microbiol, 34, pp. 3180-3184; Vennema, H., Poland, A., Hawkins, K.F., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract, 23, pp. 40-46; Vennema, H., Poland, A., Foley, J., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Herrewegh, A.A., Smeenk, I., Horzinek, M.C., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J Virol, 72, pp. 4508-4514; Herrewegh, A.A., Vennema, H., Horzinek, M.C., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Vennema, H., Heijnen, L., Rottier, P.J., A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal (1992) J Virol, 66, pp. 4951-4956; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J Virol, 56, pp. 904-911; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J Virol, 59, pp. 463-471","Foley, J.E.; School of Veterinary Medicine, Dept. of Medicine and Epidemiology, Davis, CA 95616, United States; email: jefoley@ucdavis.edu",,"American College of Veterinary Internal Medicine",08916640,,,"11596730","English","J. Vet. Intern. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0035461670
"Woods R.D.","7401706916;","Efficacy of a transmissible gastroenteritis coronavirus with an altered ORF-3 gene",2001,"Canadian Journal of Veterinary Research","65","1",,"28","32",,25,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035230089&partnerID=40&md5=9a10e0b306c12ad822e549f9df8d0330","Virus Prion Dis. Livestock Res. U., National Animal Disease Center, Agricultural Research Service, P.O. Box 70, Ames, IA 50010, United States","Woods, R.D., Virus Prion Dis. Livestock Res. U., National Animal Disease Center, Agricultural Research Service, P.O. Box 70, Ames, IA 50010, United States","Serial passage of virulent transmissible gastroenteritis virus through cell culture reduced its virulence in 3-day-old piglets. Intramuscular inoculation of pregnant gilts with 2 doses of this modified-live virus elicited a level of lactogenic immunity that protected their nursing piglets against a lethal dose of challenge virus. Sequence analysis of a 637-bp fragment of the spike gene containing most of the aminopeptidase receptor and the 4 major antigenic sites from the original and the serially passed viruses were nearly identical. Gel analysis revealed that the fragment from the ORF-3 gene of virulent virus was smaller than the corresponding fragment from the serially passed virus. Sequence analysis of the fragment from the passed virus revealed that the sequence between nt 5310 and nt 5434 was replaced by a 636-bp fragment from the polymerase 1A gene. This replacement resulted in the loss of the CTAAACTT leader RNA-binding site and ATG start codon for the ORF-3A gene but it did not affect the ORF-3B gene.",,"primer DNA; virus antibody; virus vaccine; animal; animal disease; article; biosynthesis; blood; evaluation; female; genetics; immunology; milk; molecular genetics; molecular weight; newborn; nucleotide sequence; passive immunization; pathogenicity; pregnancy; reverse transcription polymerase chain reaction; standard; suckling; swine; swine disease; Transmissible gastroenteritis virus; virulence; virus culture; Animals; Animals, Newborn; Animals, Suckling; Antibodies, Viral; Base Sequence; DNA Primers; Female; Gastroenteritis, Transmissible, of Swine; Immunity, Maternally-Acquired; Milk; Molecular Sequence Data; Molecular Weight; Pregnancy; Reverse Transcriptase Polymerase Chain Reaction; Serial Passage; Swine; Transmissible gastroenteritis virus; Viral Vaccines; Virulence","Siddell, S.G., Anderson, R., Cavanagh, D., Coronaviridae (1983) Intervirology, 20, pp. 181-189; Pedersen, N.C., Ward, J., Mengeling, W.L., Antigenic relationship of the feline infections peritonitis virus to coronaviruses of other species (1978) Arch Virol, 58, pp. 45-53; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1999) Diseases of Swine. 8th Ed., pp. 362-386. , Leman AD, Straw BE, Mengeling WL, D'Allaire S, Taylor DJ, eds. Ames, Iowa: Iowa State University Press; Moon, H.W., Kemeny, L.J., Lambert, G., Stark, S.L., Booth, G.D., Age-dependent resistance to transmissible gastroenteritis of swine. III. Effects of epithelial cell kinetics on coronavirus production and on atrophy of intestinal villi (1975) Vet Pathol, 12, pp. 434-445; Bay, W.W., Doyle, L.P., Hutchings, L.M., Some properties of the causative agent of transmissible gastroenteritis in swine (1953) Am J Vet Res, 13, pp. 318-321; Bohl, E.H., Guta, R.K., Olquin, M.V., Saif, L.J., Antibody responses in serum, colostrum, and milk of swine after infection or vaccination with transmissible gastroenteritis virus (1975) Infect Immun, 6, pp. 289-301; Saif, L.J., Vancott, J.L., Brim, T.A., Immunity to transmissible gastroenteritis virus and porcine respiratory coronavirus infections in swine (1994) Vet Immunol Immunopathol, 43, pp. 89-97; Bohl, E.H., Kumagai, T., The use of cell cultures for the study of TGE virus of swine (1965) Proc US Livestock Sanit Assoc, 69, pp. 343-350; Frederick, G.T., Bohl, E.H., Local and systemic cell-mediated immunity against transmissible gastroenteritis an intestinal viral infection of swine (1976) J Immunol, 116, pp. 1001-1004; Tamoglia, T.W., Present status of products available for use against transmissible gastroenteritis (1972) J Am Vet Med Assoc, 160, pp. 554-558; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet Microbiol, 18, pp. 197-208; Woods, R.D., Development of PCR-based techniques to identify porcine transmissible gastroenteritis coronavirus isolates (1997) Can J Vet Res, 61, pp. 167-172; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Lande, H., Complete sequence (20 kilontbases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Kwon, H.M., Saif, L.J., Jackwood, D.J., Field isolates of transmissible gastroenteritis virus differ at the molecular level from the Miller and Purdue virulent and attenuated strains and from porcine respiratory coronaviruses (1998) J Vet Med Sci, 60, pp. 589-597; McGoldrick, A., Lowings, J.P., Paton, D.J., Characterization of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a (1999) Arch Virol, 144, pp. 763-770; Vaughan, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J Virol, 69, pp. 3176-3184","Woods, R.D.; Virus Prion Dis. Livestock Res. U., National Animal Disease Center, Agricultural Research Service, P.O. Box 70, Ames, IA 50010, United States; email: rwoods@nadc.ars.usda.gov",,,08309000,,CJVRE,"11227191","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0035230089
"Sizun J., Gagneur A., Legrand C., Baron M.R.","35605340000;6508170069;57197352492;18833250600;","Respiratory coronavirus infections in children [3]",2001,"Pediatric Infectious Disease Journal","20","5",,"555","",,8,"10.1097/00006454-200105000-00026","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035024218&doi=10.1097%2f00006454-200105000-00026&partnerID=40&md5=a9edd2173fc693024fd3ccbc580306fe","Department of Pediatrics, University Hospital, Brest, France; Department of Microbiology, University Hospital, Brest, France; Public Health Department, University Hospital, Brest, France","Sizun, J., Department of Pediatrics, University Hospital, Brest, France, Department of Microbiology, University Hospital, Brest, France, Public Health Department, University Hospital, Brest, France; Gagneur, A., Department of Pediatrics, University Hospital, Brest, France, Department of Microbiology, University Hospital, Brest, France, Public Health Department, University Hospital, Brest, France; Legrand, C., Department of Pediatrics, University Hospital, Brest, France, Department of Microbiology, University Hospital, Brest, France, Public Health Department, University Hospital, Brest, France; Baron, M.R., Department of Pediatrics, University Hospital, Brest, France, Department of Microbiology, University Hospital, Brest, France, Public Health Department, University Hospital, Brest, France",[No abstract available],"Coronavirus","child; childhood disease; Coronavirus; hospital infection; human; letter; mixed infection; priority journal; respiratory tract infection","Nokso-Koivisto, J., Pikäranta, A., Blomqvist, S., Kilpi, T., Respiratory coronavirus infections in children younger than two years of age (2000) Pediatr Infect Dis J, 19, pp. 164-166; Waner, J.L., Mixed viral infections: Detection and management (1994) Clin Microbiol Rev, 7, pp. 143-151; Mortimer, E.A., Fox, J.P., Epidemiology of infectious diseases (1992), pp. 67-91. , Feigin RD, Cherry JD, eds. Textbook of pediatric infectious diseases. Philadelphia: Saunders; Falsey, A.R., McCann, R.M., Hall, W.J., The ""common cold"" in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J Am Geriatr Soc, 45, pp. 706-711; Vabret, A., Brouard, J., Petitjean, J., Eugene-Ruellan, G., Freymuth, F., Infections à coronavirus humans: Importance et diagnostic (1998) Presse Med, 27, pp. 1813-1817; Sizun, J., Soupre, D., Legrand, M.C., Neonatal nosocomial respiratory infection with coronavirus (1995) Acta Paediatr, 84, pp. 617-620; Sizun, J., Gagneur, A., Legrand, M.C., Prospective evaluation of community-acquired and nosocomial viral respiratory tract infections in a NPICU (1999) Pediatr Res, 45, pp. 174A","Sizun, J.; Department of Pediatrics, University Hospital, Brest, France",,"Lippincott Williams and Wilkins",08913668,,PIDJE,"11368126","English","Pediatr. Infect. Dis. J.",Letter,"Final",Open Access,Scopus,2-s2.0-0035024218
"Hirano N., Haga S., Sada Y., Tohyama K.","7101604276;35430103200;16465089300;7102822159;","Susceptibility of rats of different ages to inoculation with swine haemagglutinating encephalomyelitis virus (a coronavirus) by various routes",2001,"Journal of Comparative Pathology","125","1",,"8","14",,8,"10.1053/jcpa.2001.0471","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034946159&doi=10.1053%2fjcpa.2001.0471&partnerID=40&md5=2200258b6878d246dd389ed01771d811","Department of Veterinary Microbiology, Iwate University, Morioka 020-8550, Japan; The Center for Electron Microscope and Bio-Imaging Research, Department of Neuroanatomy, Iwate University, Morioka 020-8550, Japan; Laboratory for Neural Architecture, Brain Science Institute, RIKEN, Wako 351-0198, Japan","Hirano, N., Department of Veterinary Microbiology, Iwate University, Morioka 020-8550, Japan; Haga, S., Department of Veterinary Microbiology, Iwate University, Morioka 020-8550, Japan; Sada, Y., Department of Veterinary Microbiology, Iwate University, Morioka 020-8550, Japan; Tohyama, K., The Center for Electron Microscope and Bio-Imaging Research, Department of Neuroanatomy, Iwate University, Morioka 020-8550, Japan, Laboratory for Neural Architecture, Brain Science Institute, RIKEN, Wako 351-0198, Japan","Haemagglutinating encephalomyelitis virus, strain 67N, was used to inoculate 1-, 2-, 4- and 8-week-old rats by the intracerebral (i.c.), intranasal (i.n.), intraperitoneal (i.p.), subcutaneous (s.c.), intravenous (i.v.) and oral routes with graded doses. The routes of infection, in descending order of efficacy, were: i.c., i.n., s.c., i.p., i.v. and oral. Rats aged 1 and 2 weeks were generally similar in terms of mortality and mean time to death, regardless of inoculation route, except for the oral route, which had little effect. In comparison with the 1- and 2-week-old rats, the 4-week-old rats were less susceptible to the virus by all routes. Eight-week-old rats inoculated by the i.c., i.n. or s.c. routes died, but all those inoculated by other routes survived. To follow the spread of virus in the central nervous system, 4-week-old rats inoculated by the i.c. route were examined. The virus was first detected in the brain on day 1 and in the spinal cord on day 2. The viral titres in both tissues reached a plateau of 107 plaque-forming units (PFU)/0.2 g by day 4, at which time clinical signs had developed. By immunohistochemical analysis, virus-specific antigen was found first in the pyramidal cells of the hippocampus and cerebral cortex, and later in the large-sized neurons of the pons and spinal cord. Still later (day 4) immunolabelling was found in Purkinje cells of the cerebellum, but not in the ependymal cells, choroid plexus or other glial cells. © Harcourt Publishers Ltd.",,"virus antigen; age; animal cell; animal experiment; animal tissue; antibody labeling; article; brain cortex; central nervous system; choroid plexus; comparative study; controlled study; Coronavirus; encephalomyelitis; ependyma cell; experimental infection; female; glia cell; hippocampus; immunohistochemistry; infection sensitivity; inoculation; male; mortality; nerve cell; nonhuman; pons; Purkinje cell; pyramidal nerve cell; rat; spinal cord; swine disease; virus concentration; virus detection; virus hemagglutination; virus replication; virus strain","Alexander, T.J.L., Viral encephalomyelitis of swine in Ontario. Experimental and natural transmission (1962) American Journal of Veterinary Research, 32, pp. 756-762; Alexander, J.T.L., Saunders, C.N., Vomiting and wasting disease of piglets (1969) Veterinary Record, 84, p. 178; Andries, K., Pensaert, M., Virus isolation and immunofluorescence in different organs of pigs infected with hemagglutinating encephalomyelitis virus (1980) American Journal of Veterinary Research, 41, pp. 215-218; Andries, K., Pensaert, M., Immunofluorescence studies on the pathogenesis of hemagglutinating encephalomyelitis virus after oronasal inoculation (1980) American Journal of Veterinary Research, 41, pp. 1372-1378; Andries, K., Pensaert, M., Callebaut, P., Pathogenicity of hemagglutinating encephalomyelitis (vomiting and wasting disease) virus of pigs using different routes of inoculation (1978) Zentralblatt für Veterinärmedizin, Reihe B, 25, pp. 461-468; Appel, M., Greig, A.S., Corner, A.H., Encephalomyelitis of swine caused by a haemagglutinating virus. IV. Transmission routes (1965) Research in Veterinary Science, 6, pp. 482-489; Cartwright, S.F., Lucas, M., Cavil, J.P., Gush, A.F., Blandford, T.B., Vomiting and wasting disease of piglets (1969) Veterinary Record, 84, pp. 175-176; Greig, A.S., Girard, A., Encephalomyelitis of swine caused by haemagglutinating virus. II. Virological studies (1963) Research in Veterinary Science, 4, pp. 511-517; Greig, A.S., Johnson, C.N., Bouillant, A.M.P., Encephalomyelitis of swine caused by a haemagglutinating virus. VI. Morphology of the virus (1971) Research in Veterinary Science, 12, pp. 305-307; Hirai, K., Chang, C., Shimakura, S., A serological survey on hemagglutinating encephalomyelitis virus infection in pigs in Japan (1974) Japanese Journal of Veterinary Science, 36, pp. 375-382; Hirano, N., Haga, S., Fujiwara, K., The route of transmission of hemagglutinating encephalomyelitis virus (HEV) 67N strain in 4-week-old rats (1994) Advances in Experimental Medicine and Biology, 342, pp. 333-338; Hirano, N., Nomura, T., Tawara, K., Ono, K., Iwasaki, Y., Neuronal spread of swine hemagglutinating encephalomyelitis virus (HEV) 67N strain in 4-week-old rats (1995) Advances in Experimental Medicine and Biology, 380, pp. 117-119; Hirano, N., Ono, K., Takasawa, T., Murakami, T., Haga, S., Replication and plaque formation of swine hemagglutinating encephalomyelitis virus (67N) in swine cell line, SK-K culture (1990) Journal of Virological Methods, 27, pp. 91-100; Hirano, N., Takenaka, S., Fujiwara, K., Pathogenicity of mouse hepatitis virus for mice depending upon host age and route of infection (1975) Japanese Journal of Experimental Medicine, 45, pp. 285-292; Hirano, N., Tohyama, K., Taira, H., Spread of swine hemagglutinating encephalomyelitis virus from peripheral nerve to the CNS (1998) Advances in Experimental Medicine and Biology, 440, pp. 601-607; Kaye, H.S., Yarbrouch, W.B., Reed, C.J., Harrison, A.K., Antigenic relationship between human coronavirus strain OC43 and hemagglutinating encephalomyelitis virus strain 67N of swine; Antibody responses in human and animal sera (1977) Journal of Infectious Diseases, 135, pp. 201-209; Kershaw, G.F., Vomiting and wasting disease of piglets (1969) Veterinary Record, 84, pp. 178-179; Mengeling, W.L., Bloothe, A.D., Richite, A.E., Characteristics of a coronavirus (strain 67N) of pigs (1972) American Journal of Veterinary Research, 33, pp. 297-308; Mengeling, W.L., Cutlip, R.C., Pathogenicity of field isolants of hemagglutinating encephalomyelitis virus for neonatal pigs (1976) Journal of the American Veterinary Medical Association, 128, pp. 236-239; Mitchell, D., Encephalomyelitis of swine caused by a haemagglutinating virus. I. Case histories (1963) Research in Veterinary Science, 4, pp. 306-310; Narita, M., Kawanura, H., Haritani, M., Kobayashi, M., Demonstration of viral antigen and immunoglobulin (IgG and IgM) in brain tissue of pigs experimentally infected with haemagglutinating encephalomyelitis virus (1989) Journal of Comparative Pathology, 100, pp. 119-128; Phillip, J.H.I., Cartwright, S.F., Scott, A.C., The size and morphology of TGE and vomiting and wasting disease viruses of pigs (1971) Veterinary Record, 88, pp. 311-312; Roe, C.K., Alexander, T.J.L., A disease of nursing pigs previously unreported in Ontario (1958) Canadian Journal of Comparative Medicine, 22, pp. 305-307; Siddell, S.G., Anderson, R., Cavanagh, D., Fujiwara, K., Klenk, H.D., Macnaughton, M.R., Pensaert, M., Van Der Zeijist, B.A.M., Coronaviridae (1983) Intervirology, 20, pp. 181-189; Yagami, K., Hirai, K., Hirano, N., Pathogenesis of haemagglutinating encephalomyelitis virus (HEV) in mice experimentally infected by different routes (1986) Journal of Comparative Pathology, 96, pp. 645-657","Hirano, N.; Department of Veterinary Microbiology, Iwate University, Morioka 020-8550, Japan",,,00219975,,,"11437511","English","J. Comp. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0034946159
"Delmage D.A., Kelly D.F.","6602597455;7403137149;","Auricular chondritis in a cat",2001,"Journal of Small Animal Practice","42","10",,"499","501",,8,"10.1111/j.1748-5827.2001.tb02457.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035487586&doi=10.1111%2fj.1748-5827.2001.tb02457.x&partnerID=40&md5=ffabb4bede51e15e349e736c8a2a0aed","24 Mere Road, Blackpool, Lancashire FY3 9AT, United Kingdom; Department of Veterinary Pathology, University of Liverpool, Liverpool L69 3BX, United Kingdom","Delmage, D.A., 24 Mere Road, Blackpool, Lancashire FY3 9AT, United Kingdom; Kelly, D.F., Department of Veterinary Pathology, University of Liverpool, Liverpool L69 3BX, United Kingdom","A four-year-old male neutered domestic shorthaired cat developed bilateral thickening of the pinnae, with slight curling, intense erythema and pain. No ear canal disease was present. The cat was negative for feline immunodeficiency virus, feline leukaemia virus and feline coronavirus. Biopsy of the ear lesion revealed auricular chondritis. In humans, histologically similar lesions may involve the pinnae, nose, trachea, joints, eyes and heart, and the disease is termed relapsing polychondritis. The cat reported had a history of corneal damage, resulting in corneal vascularisation and opacity, eyelid distortion, necessitating an entropion operation, and radiological evidence of mild cardiac enlargement. The ear disease responded rapidly to treatment with prednisolone and, apart from slight thickening and curling of the pinnae, the cat remained normal and pain-free. After two years, the prednisolone was withdrawn, and there was no recurrence of the condition in a follow-up period of 14 months.",,"animal; animal disease; article; case report; cat; cat disease; differential diagnosis; ear tumor; male; pathology; relapsing polychondritis; Animals; Cat Diseases; Cats; Diagnosis, Differential; Ear Neoplasms; Male; Polychondritis, Relapsing","Bunge, M.M., Foil, C.S., Taylor, H.W., Glaze, M.B., Relapsing polychondritis in a cat (1992) Journal the American Animal Hospital Association, 28, pp. 203-206; Ebringer, R., Rook, G., Swana, G.T., Autoantibodies to cartilage and type II collagen in relapsing polychondritis and other rheumatic diseases (1981) Annals of Rheumatic Disease, 40, pp. 473-479; Foidart, J.M., Abe, S., Martin, G.R., Zizic, T.M., Barnett, E.V., Lawley, T.J., Katz, S.I., Antibodies to type II collagen in relapsing polychondritis (1978) New England Journal of Medicine, 299, pp. 1203-1207; Gauguere, E., Declercq, J., Plasma cell chondritis (1999) A Practical Guide to Feline Dermatology, pp. 7.6-7.7. , Eds E. Guaguere and P. Prelaud. Veterinary Times/ Veterinary Business Development, Peterborough; Gauguere, E., Prelaud, P., Mialot, M., Pierson, G., Polychondrite auriculaire atrophiante: A propos d'un cas chez un chat (1992) Practique Medicale et Chirurgicale de l'Animal de Compagnie, 27, pp. 557-562; Joyce, J.A., Day, M.J., Immunopathogenesis of canine aural haematoma (1997) Journal of Small Animal Practice, 38, pp. 152-158; Mckee, P.H., Relapsing polychondritis (1996) Pathology of the Skin, 2nd Edn., pp. 8.27-8.28. , Mosby-Wolfe, London; Mcewen, B.S., Barsoum, N.J., Auricular chondritis in Wistar rats (1990) Laboratory Animals, 24, pp. 280-283; Meyer, O., Cyna, J., Dryll, A., Relapsing polychondritis - Pathogenic role of anti-native collagen type II antibodies: A case report (1981) Journal of Rheumatology, 8, pp. 820-824; Michet, C.J., Mckenna, C.H., Luthra, H.S., O'Fallon, W.M., Relapsing polychondritis: Survival and predictive role of early disease manifestations (1986) Annals of Internal Medicine, 104, pp. 74-78; Pearson, T., Floppy pinnae in Siamese cats (1998) Veterinary Record, 143, p. 456; Rest, J.R., Floppy pinnae in Siamese cats (1998) Veterinary Record, 143, p. 568; Scott, D.W., Feline dermatology 1983-1985 - 'The secret sits' (1987) Journal of the American Animal Hospital Association, 23, pp. 255-274; White, J.W., Relapsing polychondritis (1985) Southern Medical Journal, 78, pp. 448-451","Delmage, D.A.24 Mere Road, Blackpool, Lancashire FY3 9AT, United Kingdom",,"British Veterinary Association",00224510,,JAPRA,"11688526","English","J. Small Anim. Pract.",Article,"Final",,Scopus,2-s2.0-0035487586
"Paltrinieri S., Grieco V., Comazzi S., Cammarata Parodi M.","7003879241;6701439634;6701819007;6506781296;","Laboratory profiles in cats with different pathological and immunohistochemical findings due to feline infectious peritonitis (FIP)",2001,"Journal of Feline Medicine and Surgery","3","3",,"149","159",,31,"10.1053/jfms.2001.0126","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035174286&doi=10.1053%2fjfms.2001.0126&partnerID=40&md5=2a92dce053ffc4c48ef9ba95bf94a09b","Dipartimento Di Patologia Animale, Igiene E Sanità Pubblica Veterinaria, Via Celoria 10, 20133, Milano, Italy","Paltrinieri, S., Dipartimento Di Patologia Animale, Igiene E Sanità Pubblica Veterinaria, Via Celoria 10, 20133, Milano, Italy; Grieco, V., Dipartimento Di Patologia Animale, Igiene E Sanità Pubblica Veterinaria, Via Celoria 10, 20133, Milano, Italy; Comazzi, S., Dipartimento Di Patologia Animale, Igiene E Sanità Pubblica Veterinaria, Via Celoria 10, 20133, Milano, Italy; Cammarata Parodi, M., Dipartimento Di Patologia Animale, Igiene E Sanità Pubblica Veterinaria, Via Celoria 10, 20133, Milano, Italy","Blood was collected from 55 cats with feline infectious peritonitis (FIP) and from 50 control cats in order to define whether differences in pathological findings and in distribution of feline coronaviruses (FCoV) can be associated with changes in haemograms, serum protein electrophoresis, and antibody titres. Compared to controls, the whole group of FIP-affected cats had blood changes consistent with FIP. Based on the pathological findings or on the immunohistochemical distribution of viral antigen, FIP-affected cats were divided in the following groups: subacute against acute lesions; low against strong intensity of positivity; intracellular against extracellular positivities; positive against negative lymph nodes. Lymphopenia was more evident in cats with acute forms, strong intensity of positivity, extracellular antigen and negative lymph nodes. Cats with positive lymph nodes had the most evident changes in the protein estimations. These results suggest that differences in pathological findings might depend on different reactive patterns to the FCoVs. © 2001 European Society of Feline Medicine.",,"protein; virus antigen; animal; animal disease; animal tissue; antibody titer; article; blood; blood sampling; case control study; cat; cat disease; controlled study; Coronavirus; disease classification; feline coronavirus; female; hospitalization; immunohistochemistry; immunology; laboratory test; lymphocytopenia; male; nonhuman; pathology; peritonitis; protein blood level; protein electrophoresis; virology; Felidae; Felis catus","Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., The risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) American Journal of Veterinary Research, 56, pp. 429-434; Barlough, J.E., Stoddart, C.A., Feline Infectious Peritonitis (1990) Veterinary Reports, 1, pp. 13-17; Cammarata Parodi, M., Cammarata, G., Paltrinieri, S., Ape, F., Using direct immunofluorescence to detect coronaviruses in peritoneal and pleural effusion (1993) Journal of Small Animal Practice, 34, pp. 609-613; Cattoretti, G., Pileri, S., Parravicini, C., Becker, M.H.G., Poggi, S., Bifulco, C., Key, G., Rilke, F., Antigen unmasking on formalin-fixed, paraffin-embedded tissue sections (1993) Journal of Pathology, 171, pp. 83-98; Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebreed cats (1996) Feline Practice, 24, pp. 14-22; Gunn-Moore, D.A., Caney, S.M.A., Gruffyd-Jones, T.J., Helps, C.R., Harbour, D.A., Antibody and cytokine responses in kittens during the development of feline infectious peritonitis (FIP) (1998) Veterinary Immunology and Immunopathology, 65, pp. 221-242; Haagmans, B.L., Egbernik, H.F., Horzinek, M.C., Apoptosis and T-cell depletion during feline infectious peritonitis (1996) Journal of Virology, 70, pp. 8977-8983; Hayashi, T., Goto, N., Takahashi, R., Fujiwara, K., Systemic vascular lesions in feline infectious peritonitis (1977) Japanese Journal of Veterinary Science, 39, pp. 365-377; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egbernik, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissue and body fluids of naturally infected cats by reverse transcriptase PCR (1995) Journal of Clincal Microbiology, 33, pp. 684-689; Herrewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egbernik, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Hodatsu, T., Yamada, H., Ishizuka, Y., Koyama, H., Enhancement and neutralization of feline inectious peritonitis infection in feline macrophages by neutralizing monoclonal antibodies recognizing different epitopes (1993) Microbiology and Immunology, 37, pp. 499-504; Hodatsu, T., Tokunaga, J., Koyama, H., The role of IgG subclass of mouse monoclonal antibodies in antibody-dependent enhancement of feline infectious peritonitis virus infection of feline macrophages (1994) Archives of Virology, 139, pp. 273-285; Hsu, S.M., Raine, L., Farger, H., Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures (1981) Journal of Histochemistry and Cytochemistry, 29, pp. 577-580; Jacobse-Geels, H.E.L., Daha, M.R., Horzinek, M.C., Antibody, immune complexes, and complement activity fluctuations in kittens with experimentally induced feline infectious peritonitis (1982) American Journal of Veterinary Research, 43, pp. 666-670; Jain, N.C., (1993) Essential of veterinary hematology, , (1st edn.). Lea & Febiger, Philadelphia; Kaneko, J.J., Harvey, J.W., Bruss, M.L., Blood analyte reference values in small and some laboratory animals (1997) Clinical Biochemistry of Domestic Animals, pp. 895-899. , (5th edn.). Kaneko JJ, Harvey JM, Bruss ML (eds). Academic Press, San Diego; Kipar, A., Bellmann, S., Kremendhal, J., Reinacher, M., Antibody production in situ in cats with feline infectious peritonitis (1997) Proceedings of the 15th meeting of the European Society of Veterinary Pathology, p. 94; Kipar, A., Bellmann, S., Kremendhal, J., Kohler, K., Reinacher, M., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Veterinary Immunology and Immunopathology, 65, pp. 243-257; Kipar, A., Bellmann, S., Gunn-Moore, D.A., Leucert, W., Kohler, K., Menger, S., Reinacher, M., Histopathological alterations of lymphatic tissues in cats without feline infectious peritonitis after long term exposure to FIP virus (1999) Veterinary Microbiology, 69, pp. 131-137; Kristensen, F., Barsanti, J., Analysis of serum proteins in clinically normal pet and colony cats, using agarose electrophoresis (1977) American Journal of Veterinary Research, 38, pp. 399-402; Paltrinieri, S., Parodi Cammarata, M., Cammarata, G., Mambretti, M., Type IV hypersensitivity in the pathogenesis of FIPV induced lesions (1998) Journal of Veterinary Medicine B, 45, pp. 151-159; Paltrinieri, S., Cammarata Parodi, M., Cammarata, G., Comazzi, S., Some aspects of humoral and cellular immunity in spontaneously occuring feline infectious peritonitis (1998) Veterinary Immunology and Immunopathology, 65, pp. 205-220; Pasquinelli, F., Tecniche ematologiche (1984) Diagnostica e tecniche di laboratorio, 2, pp. 835-854. , (1st edn.). Pasquinelli F (ed). Rosini editrice s.r.l., Firenze; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) American Journal of Veterinary Research, 37, pp. 1449-1453; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Advances in Experimental Medicine and Biology, 218, pp. 529-550; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Practice, 23, pp. 7-20; Pedersen, N.C., The history and interpretation of feline coronavirus serology (1995) Feline Practice, 23, pp. 46-51; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) Journal of Clinical Microbiology, 34, pp. 3180-3184; Richards, J.R., Problems in the interpretation of feline coronavirus serology (specificity vs. sensitivity of test procedures) (1995) Feline Practice, 23, pp. 52-55; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., Feline infectious peritonitis: A review of clinicopathological changes in 65 cases, and a critical assessment of their diagnostic value (1991) Veterinary Record, 129, pp. 209-212; Steinman, R.M., The dendritic cell system and its role in immunogenicity (1991) Annual Review of Immunology, 9, pp. 271-296; Stoddart, M.E., Whicher, J.T., Harbour, D.A., Cats inoculated with feline infectious peritonitis virus exhibit a biphasic acute phase plasma protein response (1988) Veterinary Record, 123, pp. 621-624; Tammer, R., Evensen, O., Lutz, H., Reinacher, M., Immunological demonstration of feline infectious peritonitis virus antigen in paraffin-embedded tissues using feline ascites or murine monoclonal antibodies (1995) Veterinary Immunology and Immunopathology, 49, pp. 177-182; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs: What they tell us about relationship between feline coronaviruses and their evolution (1995) Feline Practice, 23, pp. 40-44; Walter, J., Dohse, K., Rudolph, R., Eine modification der ABC-methode (avidin-biotin-peroxidase-complex) für den nachweis von viralen antigenen bei der infektion der katze durch ein coronavirus (FIP) und der infektion des hundes durch das parvovirus-typ 2 (1989) Journal of Veterinary Medicine B, 36, pp. 321-332; Ward, J.M., Gribble, D.H., Dungworth, D.L., Feline infectious peritonitis: Experimental evidence for its multiphasic nature (1974) American Journal of Veterinary Research, 35, pp. 1271-1275; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Pathologic changes and immunofluorescence (1981) American Journal of Veterinary Research, 42, pp. 2036-2048",,,,1098612X,,,"11876632","English","J. Feline Med. Surg.",Article,"Final",,Scopus,2-s2.0-0035174286
"Pritchard G.","7101687286;","Milk antibody testing in cattle",2001,"In Practice","23","9",,"542","549",,30,"10.1136/inpract.23.9.542","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034769884&doi=10.1136%2finpract.23.9.542&partnerID=40&md5=9eeb44fa4473d36db7f917f6d92260f9",,"Pritchard, G.","Milk antibody testing has played a significant role in cattle disease control and eradication programmes in many countries, particularly in mainland Europe and Scandinavia, since the mid-1980s. In Britain, bulk milk antibody testing is an integral part of the statutory control programmes for brucellosis and enzootic bovine leukosis. It is also used by veterinary diagnostic laboratories, and within formal cattle health schemes, for measuring bovine viral diarrhoea virus (BVDV), infectious bovine rhinotracheitis virus (IBRV)/bovine herpesvirus 1 and Leptospira hardjo infections. A bulk tank antibody test for Mycobacterium avium subspecies paratuberculosis (Johne's disease) was used for a recent prevalence study in Denmark, but proved unreliable. Milk antibody testing has, however, been successfully developed for several other important cattle infections including salmonella, respiratory syncytial virus and coronavirus. In 1997, the VLA introduced bulk milk antibody testing for BVDV, IBRV and L hardjo in its Regional Laboratories. This article discusses the use of these tests, with particular emphasis on practical and cost-effective approaches.",,"antibody; immunoglobulin G; antibody detection; antibody specificity; article; cattle; cattle disease; cohort analysis; controlled study; cost effectiveness analysis; enzyme linked immunosorbent assay; immunoassay; infection; infection control; Infectious bovine rhinotracheitis virus; laboratory test; leptospirosis; milk; monitoring; nonhuman; optical density; preservation; sampling; seroconversion; Bos taurus; Bovinae; Bovine herpesvirus 1; Bovine rhinotracheitis virus; Bovine viral diarrhea virus 1; Coronavirus; Herpesviridae; herpesvirus 1; Leptospira; Leptospira interrogans serovar Hardjo; Mycobacterium; Mycobacterium avium; Respiratory syncytial virus; Salmonella; Syncytial virus","Bercovich, Z., Taaijke, R., Bokhout, B.A., Evaluation of an ELISA for the diagnosis of experimentally induced and naturally occurring Leptospira hardjo infections in cattle (1990) Veterinary Microbiology, 21, pp. 255-262; Paton, D.J., Christiansen, K.H., Alenius, S., Cranwell, M.P., Pritchard, G.C., Drew, T.W., Prevalence of antibodies to bovine virus diarrhoea virus and other viruses in bulk tank milk in England and Wales (1998) Veterinary Record, 142, pp. 385-391; Pritchard, G.C., Kirkwood, G., Sayers, A.R., Detecting antibodies to infectious bovine rhinotracheitis and bovine virus diarrhoea virus infections using milk samples from individual cows (2001) Veterinary Record, , (In press); Tizard, I.R., Immunity in the fetus and newborn (2000) Veterinary Immunology - An Introduction, pp. 210-221. , Philadelphia, W.B. Saunders; Woodward, M.J., Swallow, C., Kitching, A., Dalley, C., Sayers, A.R., Leptospira hardjo serodiagnosis: A comparison of MAT, ELISA and Immunocomb (1997) Veterinary Record, 141, pp. 603-604",,,"BMJ Publishing Group",0263841X,,IPRCD,,"English","In Practice",Article,"Final",,Scopus,2-s2.0-0034769884
"Aurisicchio L., Bujard H., Hillen W., Cortese R., Ciliberto G., La Monica N., Palombo F.","6602678522;7005379703;7102025822;7006727126;55368402800;7003288203;7003602570;","Regulated and prolonged expression of mIFNα in immunocompetent mice mediated by a helper-dependent adenovirus vector",2001,"Gene Therapy","8","24",,"1817","1825",,33,"10.1038/sj.gt.3301596","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035709608&doi=10.1038%2fsj.gt.3301596&partnerID=40&md5=f9ebdd5ccc0e46ce8698072fde0fd32b","IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy; Zentrum fur Molekulare Biologie der Universitat Heidelberg (ZMBH), Heidelberg, Germany; Institut fur Mikrobiologie, Universitat Erlangen, Erlangen, Germany","Aurisicchio, L., IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy; Bujard, H., Zentrum fur Molekulare Biologie der Universitat Heidelberg (ZMBH), Heidelberg, Germany; Hillen, W., Institut fur Mikrobiologie, Universitat Erlangen, Erlangen, Germany; Cortese, R., IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy; Ciliberto, G., IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy; La Monica, N., IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy; Palombo, F., IRBM P Angeletti, Via Pontina Km 30 600, 00040 Pomezia Rome, Italy","A major goal in gene therapy is to develop efficient gene transfer protocols that allow tissue-specific, long-term and tightly regulated expression of the desired transgene. This objective is becoming more attainable through the co-evolution of gene transfer vectors and regulation systems. The ideal vector should efficiently transduce non-dividing cells with minimal toxicity, thus endowing the system with persistent transgene expression. The helper-dependent adenovirus vectors meet these requirements, as demonstrated in various studies in the literature. The most promising regulation system is the tet-on system, which has low basal transcriptional activity and high inducibility. To explore the regulated transgene expression in the context of a helper-dependent vector, we constructed the HD-TET-IFN vector, containing the mIFNα gene under the control of the tetracycline inducible transactivator rtTA2s-S2. Mice injected with HD-TET-IFN showed high levels of serum mIFNα only upon transcriptional activation. The transgene expression was reinducible to the same high level up to 3 months p.i., and the amount of expressed cytokine could be regulated by dosing doxycycline. Transcriptional activation of mIFNα induced by doxycycline resulted in prolonged survival and reduced liver damage in HD-TET-IFN-injected mice challenged with a lethal dose of coronavirus. Activation of antiviral genes mediated by doxycycline-dependent mIFNα expression was also observed at low HD-TET-IFN doses. The possibility of controlling gene expression by the combination of HD vectors and the latest tet-on transactivator also holds promise for studying gene function in other animal models. © 2001 Nature Publishing Group All rights reserved.","Antivirals; Gene regulation; Helper-dependent adenovirus vector; Tetracycline","adenovirus vector; alpha interferon; antigestagen; cytokine; doxycycline; mifepristone; rapamycin; recombinant alpha interferon; recombinant beta interferon; tetracycline; transactivator protein; acute hepatitis; animal cell; animal experiment; animal model; antiviral activity; article; blood level; controlled study; Coronavirus; expression vector; gene activation; gene construct; gene control; gene expression regulation; gene function; immunocompetence; interferon production; lethal dose; liver injury; liver protection; mouse; nonhuman; priority journal; provocation test; survival time; transactivation; transgene; viral gene delivery system; viral gene therapy; virus hepatitis; Adenoviridae; Alanine Transaminase; Animals; Anti-Bacterial Agents; Carcinoma, Hepatocellular; Cell Line; Doxycycline; Enzyme-Linked Immunosorbent Assay; Female; Gene Expression; Gene Expression Regulation; Gene Therapy; Genetic Vectors; Hepatitis, Viral, Animal; Humans; Interferon-alpha; Liver; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Models, Animal; RNA, Messenger; Trans-Activators; Transgenes; Adenoviridae; Animalia; Coronavirus; DNA viruses; vectors","Russell, W.C., Update on adenovirus and its vectors (2000) J. Gen. Virol., 81, pp. 2573-2604; Lusky, M., In vitro and in vivo biology of recombinant adenovirus vectors with E1, E1/E2A, or E1/E4 deleted (1998) J. Virol., 72, pp. 2022-2032; Schiedner, G., Genomic DNA transfer with a high-capacity adenovirus vector results in improved in vivo gene expression and decreased toxicity (1998) Nat. Genet., 18, pp. 180-183. , (published erratum appears in Nat Genet 1998; 18: 298); Thomas, C.E., Peripheral infection with adenovirus causes unexpected long-term brain inflammation in animals injected intracranially with first-generation, but not with high-capacity, adenovirus vectors: Toward realistic therapy for chronic diseases (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 7482-7487; Maione, D., Prolonged expression and effective readministration of erythropoietin delivered with a fully deleted adenoviral vector (2000) Hum. Gene. Ther., 11, pp. 859-868; Parks, R.J., A helper-dependent adenovirus vector system: Removal of helper virus by Cre-mediated excision of the viral packaging signal (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 13565-13570; Kochanek, S., High-capacity adenoviral vectors for gene transfer and somatic gene therapy (1999) Hum. Gene. Ther., 10, pp. 2451-2459; Corti, O., Long-term doxycycline-controlled expression of human tyrosine hydroxylase after direct adenovirus-mediated gene transfer to a rat model of Parkinson’s disease (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12120-12125; Burcin, M.M., Adenovirus-mediated regulable target gene expression in vivo (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 355-360; Baron, U., Bujard, H., Tet repressor-based system for regulated gene expression in eukaryotic cells: Principles and advances (2000) Meth. Enzymol., 327, pp. 401-421; Gossen, M., Bujard, H., Tight control of gene expression in mammalian cells by tetracycline-responsive promoters (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 5547-5551; Gossen, M., Transcriptional activation by tetracyclines in mammalian cells (1995) Science, 268, pp. 1766-1769; Kafri, T., Van Praag, H., Gage, F.H., Verma, I.M., Lentiviral vectors: Regulated gene expression (2000) Mol. Ther., 1, pp. 516-521; Pitzer, C., In vivo manipulation of interleukin-2 expression by a retroviral tetracycline (tet)-regulated system (1999) Cancer Gene. Ther., 6, pp. 139-146; Rizzuto, G., Efficient and regulated erythropoietin production by naked DNA injection and muscle electroporation (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 6417-6422; Urlinger, S., Exploring the sequence space for tetracycline-dependent transcriptional activators: Novel mutations yield expanded range and sensitivity (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 7963-7968; Eto, T., Takahashi, H., Enhanced inhibition of hepatitis B virus production by asialoglycoprotein receptor-directed interferon (1999) Nat. Med., 5, pp. 577-581; Aurisicchio, L., Liver-specific alpha 2 interferon gene expression results in protection from induced hepatitis (2000) J. Virol., 74, pp. 4816-4823; Protzer, U., Interferon gene transfer by a hepatitis B virus vector efficiently suppresses wild-type virus infection (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 10818-10823; Carlow, D.A., Teh, S.J., Teh, H.S., Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases (1998) J. Immunol., 161, pp. 2348-2355; Sandig, V., Optimization of the helper-dependent adenovirus system for production and potency in vivo (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 1002-1007; Kistner, A., Doxycycline-mediated quantitative and tissue-specific control of gene expression in transgenic mice (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 10933-10938; Kato, Y., Effect of exogenous mouse interferon on murine fulminant hepatitis induced by mouse hepatitis virus type 2 (1986) Dig. Dis. Sci., 31, pp. 177-180; Minagawa, H., Takenaka, A., Mohri, S., Mori, R., Protective effect of recombinant murine interferon beta against mouse hepatitis virus infection (1987) Antiviral. Res., 8, pp. 85-95; Schowalter, D.B., Implication of interfering antibody formation and apoptosis as two different mechanisms leading to variable duration of adenovirus-mediated transgene expression in immune-competent mice (1999) J. Virol, 73, pp. 4755-4766; Hitt, M.M., Addison, C.L., Grahm, F.L., Human adenovirus vectors for gene transfer into mammalian cells (1997) Adv. Pharmacol., 40, pp. 137-206; Rivera, V.M., Long-term regulated expression of growth hormone in mice after intramuscular gene transfer (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 8657-8662; Hasan, M.T., Long-term, non-invasive imaging of regulated gene expression in living mice (2001) Genesis, 29, pp. 116-122; Pastore, L., Use of a liver-specific promoter reduces immune response to the transgene in adenoviral vectors (1999) Hum. Gene. Ther., 10, pp. 1773-1781; Morral, N., Administration of helper-dependent adenoviral vectors and sequential delivery of different vector serotype for long-term liver-directed gene transfer in baboons (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12816-12821",,,,09697128,,,"11821934","English","Gene Ther.",Article,"Final",Open Access,Scopus,2-s2.0-0035709608
"Granzow H., Weiland F., Fichtner D., Schütze H., Karger A., Mundt E., Dresenkamp B., Martin P., Mettenleiter T.C.","7004101171;7005516269;7004184131;7003432999;7005618464;7004238027;6507728200;57213855529;7006059985;","Identification and ultrastructural characterization of a novel virus from fish",2001,"Journal of General Virology","82","12",,"2849","2859",,17,"10.1099/0022-1317-82-12-2849","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035192829&doi=10.1099%2f0022-1317-82-12-2849&partnerID=40&md5=0b50c079104da00221b66a216773d8dd","Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany","Granzow, H., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Weiland, F., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Fichtner, D., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Schütze, H., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Karger, A., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Mundt, E., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Dresenkamp, B., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Martin, P., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; Mettenleiter, T.C., Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany","During routine investigations on fish, a virus (isolate DF 24/00) with novel morphological features and hitherto undescribed morphogenesis was isolated from a white bream (Blicca bjoerkna L.; Teleostei, order Cypriniformes). Cell-free virions consist of a rod-shaped nucleocapsid (120-150 × 19-22 nm) similar to that seen in baculoviruses. The virion has a bacilliform shape (170-200 × 75-88 nm) reminiscent of rhabdoviruses with an envelope containing coronavirus-like spikes (20-25 nm). DF 24/00 replicated well in various fish cell lines. Inhibitor studies with 5-iodo-2′-deoxyuridine indicated that the viral genome consists of RNA and chloroform sensitivity correlated with ultrastructural demonstration of enveloped virions. The buoyant density of the virus determined in sucrose was 1.17-1.19 g/ml. Preliminary biochemical characterization revealed the presence of six antigenic glycoproteins, three of which contain sugars with concanavalin-A specificity. Ultrastructurally, morphogenesis of virus progeny was detected only in the cytoplasm. Nucleocapsids were observed to bud through membranes of the endoplasmic reticulum and/or Golgi apparatus into dilated vesicles. Egress of mature virions occurs primarily by exocytosis and, only very rarely, by budding directly at the plasma membrane. Morphologically similar viruses had previously been isolated from grass carp (Ctenopharyngodon idella), blue crab (Callinectis sapidus), European shore crab (Carcinus maenas) and shrimp (Penaeus monodon). To date, none of them has been classified. In summary, the first characterization of a new virus that might represent a member of a novel virus family that has morphological features resembling those found in rhabdo-, corona- and baculoviruses is presented.",,"broxuridine; chloroform; concanavalin A; sucrose; sugar; virus glycoprotein; virus RNA; article; Baculovirus; carp; cell line; cell membrane; cell vacuole; controlled study; Coronavirus; crab; cytoplasm; density; endoplasmic reticulum; exocytosis; fish; Golgi complex; nonhuman; priority journal; progeny; Rhabdovirus; RNA virus; shrimp; ultrastructure; virion; virus classification; virus envelope; virus genome; virus isolation; virus morphogenesis; virus nucleocapsid; virus replication; Blicca bjoerkna; Blicca bjoerkna; Callinectes sapidus; Callinectis sapidus; Carcinus maenas; Carcinus maenas; Coronavirus; Ctenopharyngodon idella; Ctenopharyngodon idella; Cypriniformes; Cyprinus carpio; Decapoda (Crustacea); Grapsidae; Hyperoglyphe porosa; Monodon; Penaeus monodon; Penaeus monodon; Rhabdoviridae; RNA viruses; Teleostei; unidentified baculovirus","Ahne, W., Kurstak, E., Viruses of fishes (1989) Viruses of Lower Vertebrates, pp. 141-452. , Vienna & New York: Springer-Verlag; Ahne, W., Jiang, Y., Thomsen, I., A new virus isolated from cultured grass carp Ctenopharyngodon idella (1987) Diseases of Aquatic Organisms, 3, pp. 181-185; Anderson, I.G., Prior, H.C., Baculovirus infections in the mud crab, Scylla serrata, and a freshwater crayfish, Cherax quadricarinatus, from Australia (1992) Journal of Invertebrate Pathology, 60, pp. 265-273; Anon, A., (1992), p. 19. , Commission Decision 92/532/EEG of 19 November 1992 laying down the sampling plans and diagnostic methods for the detection and confirmation of certain fish diseases. OJ No L 337, 21 November 1992, p 18 as last 96/240/EC of 5 February 1996. OJ No L 79, 29 March 1996; Asagi, M., Ogawa, T., Minetoma, T., Sato, K., Inaba, Y., Detection of transmissible gastroenteritis virus in feces from pigs by reversed passive hemagglutination (1986) American Journal of Veterinary Research, 47, pp. 2161-2164; Blissard, G.W., Rohrmann, G.F., Baculovirus diversity and molecular biology (1990) Annual Review of Entomology, 35, pp. 127-155; Boonyaratpalin, S., Supamattaya, K., Kasornchandra, J., Direkbusaracom, S., Aekpanithanpong, U., Chantanahookin, C., Non-occluded baculo-like virus the causative agent of yellow-head disease in the black tiger shrimp Penaeus monodon (1993) Fish Pathology, 28, pp. 103-109; Chantanachookin, C., Boonyaratpalin, S., Kasornchandra, J., Direkbusarakom, S., Ekpanithanpong, U., Supamataya, K., Sriurairatana, S., Flegel, T.W., Histology and ultrastructure reveal a new granulosis-like virus in Penaeus monodon affected by yellow-head disease (1993) Diseases of Aquatic Organisms, 17, pp. 145-157; Chassard-Bouchaud, C., Hubert, M., Bonami, J.R., Particules d'allure viral associées a l'organe du crabe, Carcinus maenas (Crustaceae, Decapode) (1976) Comptes Rendus des Seances de l'Académie des Sciences Paris, 282, pp. 1565-1567; Darlington, R.W., Trafford, R., Wolf, K., Fish rhabdoviruses: Morphology and ultrastructure of North American salmonid isolates (1972) Archiv für die gesamte Virusforschung, 39, pp. 257-264; Deuter, A., Enzmann, P.J., Comparative biochemical and serological studies on two fish pathogenic rhabdoviruses (VHSV and SVCV) (1986) Journal of Veterinary Medicine B, 33, pp. 36-46; Dresenkamp, B., Untersuchungen zur oralen immunisierbarkeit gegen die frühjahrsvirämie der karpfen (SVC) (1992), Dissertation, Humboldt-Universität Berlin, Germany; Dubois-Dalcq, M., Holmes, K.V., Rentier, B., Assembly of Enveloped RNA Viruses (1984), Vienna & New York: Springer-Verlag; Edgerton, B., Paasonen, P., Henttonen, P., Owens, L., Description of a bacilliform virus from the freshwater crayfish Astacus astacus (1996) Journal of Invertebrate Pathology, 68, pp. 187-190; Falk, K., Namork, E., Rimstad, E., Mjaaland, S., Dannevig, B., Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.) (1997) Journal of Virology, 71, pp. 9016-9023; Fraser, M.J., Ultrastructural observations of virion maturation in Autographa californica nuclear polyhedrosis virus-infected Spodoptera frugiperda cell cultures (1986) Journal of Ultrastructure Research, 95, pp. 189-195; Fryer, J.L., Lannan, C.N., Three decades of fish cell culture: A current listing of cell lines derived from fishes (1994) Journal of Tissue Culture Methods, 16, pp. 87-94; Granzow, H., Weiland, F., Fichtner, D., Enzmann, P.J., Studies of the ultrastructure and morphogenesis of fish pathogenic viruses grown in cell culture (1997) Journal of Fish Diseases, 20, pp. 1-10; Groff, J.M., McDowell, T., Friedman, C.S., Hedrick, R.P., Detection of a non-occluded baculovirus in the freshwater crayfish Cherax quadricarinatus in North America (1993) Journal of Aquatic Animal Health, 5, pp. 275-279; Hedrick, R.P., McDowell, T.S., Friedman, C.S., Baculoviruses found in two species of crayfish from California (1995) Aquaculture, , Abstract 135; Hetrick, F.M., Hedrick, R.P., New viruses described in finfish from 1988-1992 (1993) Annual Review of Fish Diseases, 3, pp. 7-27; Hovland, T., Nylund, A., Watanabe, K., Endresen, C., Observation of infectious salmon anaemia virus in Atlantic salmon, Salmo salar L (1994) Journal of Fish Diseases, 17, pp. 291-296; Jackson, A.O., Francki, R.I., Zuidema, D., Biology, structure and replication of plant rhabdoviruses (1987) In Rhabdoviruses, pp. 427-508. , Edited by R. R. Wagner. New York: Plenum; Johnson, P.T., Lightner, D.V., Rod-shaped nuclear viruses of crustaceans: Gut-infecting species (1988) Diseases of Aquatic Organisms, 5, pp. 123-141; Koren, C., Nylund, A., Morphology and morphogenesis of infectious salmon anemia virus replicating in the endothelium of Atlantic salmon Salmo salar (1997) Diseases of Aquatic Organisms, 29, pp. 99-109; McKinnon, E.A., Henderson, J.F., Stoltz, D.B., Faulkner, P., Morphogenesis of nuclear polyhedrosis virus under conditions of prolonged passage in vitro (1974) Journal of Ultrastructure Research, 49, pp. 419-435; Mari, J., Bonami, J.-R., Poulos, B., Lightner, D., Preliminary characterization and partial cloning of the genome of a baculovirus from Penaeus monodon (PmSNPV = MBV) (1993) Diseases of Aquatic Organisms, 16, pp. 207-215; Nadala E.C.B., Jr., Tapay, L.M., Loh, P.C., Yellow-head virus: A rhabdovirus-like pathogen of penaeid shrimp (1997) Diseases of Aquatic Organisms, 31, pp. 141-146; Nylund, A., Hovland, T., Watanabe, K., Endresen, C., Presence of infectious salmon anaemia virus (ISAV) in tissues of Atlantic salmon, Salmon salar L., collected during three separate outbreaks of the disease (1995) Journal of Fish Diseases, 18, pp. 135-145; Pilcher, K.S., Fryer, J.L., The viral diseases of fish: A review through 1978 (1980) CRC Critical Reviews in Microbiology, 7, pp. 10-11; Pilcher, K.S., Fryer, J.L., The viral diseases of fish: A review through 1978 (1980) CRC Critical Reviews in Microbiology, 8, p. 351; Reynolds, E.S., The use of lead citrate at high pH as an electron opaque stain in electron microscopy (1963) Journal of Cell Biology, 17, pp. 208-212; Rohrmann, G.F., Baculovirus structural proteins (1992) Journal of General Virology, 73, pp. 749-761; Spann, K.M., Vickers, J.E., Lester, R.G.J., Lymphoid organ virus of Penaeus monodon from Australia (1995) Diseases of Aquatic Organisms, 23, pp. 127-134; Spann, K.M., Cowley, J.A., Walker, P.J., Lester, R.G.J., A yellow-head-like virus from Penaeus monodon cultured in Australia (1997) Diseases of Aquatic Organisms, 31, pp. 169-179; Towbin, H., Staehelin, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proceedings of the National Academy of Sciences, USA, 76, pp. 4350-4354; Van Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., Carstens, E.B., Estes, M.K., Lemon, S.M., Maniloff, J., Wickner, R.B., (2000), Virus Taxonomy. Seventh Report of the International Committee on Taxonomy of Viruses. San Diego: Academic Press; Wolf, K., Viral diseases of fish and their relation to public health (1981) CRC Handbook Series in Zoonoses: Section B Viral Zoonoses, pp. 403-437. , Boca Raton, FL: CRC Press; Wolf, K., (1988) Fish Viruses and Fish Viral Diseases, , Ithaca, NY: Cornell University Press; Wongteerasupaya, C., Sriurairatane, S., Vickers, J.E., Akrajamorn, A., Boonsaeng, V., Panyim, S., Tassanakajon, A., Flegel, T.W., Yellow-head virus of Penaeus monodon is an RNA virus (1995) Diseases of Aquatic Organisms, 22, pp. 45-50; Yudin, A.I., Clark W.H., Jr., Two virus-like particles found in the ecdysial gland of the blue crab, Callinectes sapidus (1978) Journal of Invertebrate Pathology, 32, pp. 219-221; Yudin, A.I., Clark W.H., Jr., A description of rhabdovirus-like particles in the mandibular gland of the blue crab, Callinectes sapidus (1979) Journal of Invertebrate Pathology, 33, pp. 133-147","Granzow, H.; Institutes of Infectology, Friedrich-Loeffler-Institutes, Fed. Res. Ctr. for Virus Dis. Anim., Boddenblick 5 A, D-17498 Insel Riems, Germany; email: harald.granzow@rie.bfav.de",,"Society for General Microbiology",00221317,,JGVIA,"11714959","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035192829
"Youngentob S.L., Schwob J.E., Saha S., Manglapus G., Jubelt B.","7003819686;7006729004;18936957800;8110511300;7004094825;","Functional consequences following infection of the olfactory system by intranasal infusion of the olfactory bulb line variant (OBLV) of mouse hepatitis strain JHM",2001,"Chemical Senses","26","8",,"953","963",,12,"10.1093/chemse/26.8.953","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034771762&doi=10.1093%2fchemse%2f26.8.953&partnerID=40&md5=23a45bfa9edc104376f98f49391abc57","Department of Neuroscience and Physiology, SUNY Upstate Medical University, Syracuse, NY 13210, United States; Clinical Olfactory Research Center, SUNY Upstate Medical University, Syracuse, NY 13210, United States; Department of Neuroscience and Physiology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, United States; Department of Anatomy and Cellular Biology, Tufts University School of Medicine, MA 02111, United States; Department of Neurology, SUNY Upstate Medical University, Syracuse, NY 13210, United States","Youngentob, S.L., Department of Neuroscience and Physiology, SUNY Upstate Medical University, Syracuse, NY 13210, United States, Clinical Olfactory Research Center, SUNY Upstate Medical University, Syracuse, NY 13210, United States, Department of Neuroscience and Physiology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, United States; Schwob, J.E., Department of Anatomy and Cellular Biology, Tufts University School of Medicine, MA 02111, United States; Saha, S., Clinical Olfactory Research Center, SUNY Upstate Medical University, Syracuse, NY 13210, United States, Department of Neurology, SUNY Upstate Medical University, Syracuse, NY 13210, United States; Manglapus, G., Department of Neuroscience and Physiology, SUNY Upstate Medical University, Syracuse, NY 13210, United States, Clinical Olfactory Research Center, SUNY Upstate Medical University, Syracuse, NY 13210, United States; Jubelt, B., Clinical Olfactory Research Center, SUNY Upstate Medical University, Syracuse, NY 13210, United States, Department of Neurology, SUNY Upstate Medical University, Syracuse, NY 13210, United States","The present study assessed the functional consequences of viral infection with a neurotropic coronavirus, designated MHV OBLV, that specifically targets central olfactory structures. Using standard operant techniques and a 'go, no-go' successive discrimination paradigm, six BALB/c mice were trained to discriminate between the presentation of an air or odor stimulus (three mice for each of the odorants propanol and propyl acetate). Two additional BALB/c mice were trained to discriminate between the presentation of air and the presentation of either vanillin or propionic acid. Following criterion performance, each mouse received an additional 2000 trials of overtraining. At completion of overtraining one mouse from the propanol and propyl acetate groups were allocated as untreated. The remaining six mice were inoculated with 300 μl of the OBLV stock per nostril for a total of 1.5 × 106 p.f.u. in 600 μl. Following a 1 month rest, untreated and inoculated animals were again tested on their respective air versus odor discrimination task. Untreated animals immediately performed at criterion levels. In contrast, inoculated animals varied in their capacity to discriminate between air and odorant. Five of the six inoculated mice showed massive disruption of the olfactory bulb, including death of mitral cells; the other was more modestly affected. In addition, the density of innervation of the olfactory mucosa by substance P-containing trigeminal fibers is also affected by inoculation. Those mice that remained anosmic to the training odorants had the most severe reduction in mitral cell number and substance P fiber density among the inoculated animals.",,"propanol; propionic acid; substance P; valeric acid; vanillin; air; animal behavior; animal cell; animal experiment; animal model; animal tissue; anosmia; article; cell count; cell death; controlled study; density; inoculation; male; mitral cell; mouse; mouse strain; Murine hepatitis coronavirus; nonhuman; olfactory bulb; olfactory discrimination; olfactory epithelium; olfactory system; priority journal; rest; sensory nerve; stimulus response; training; trigeminal nerve; virus infection; virus strain; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Barthold, S.W., Olfactory neural pathway in mouse hepatitis virus nasoencephalitis (1988) Acta Neuropathol., 76, pp. 502-506; Burd, G.D., Morphological study of the effects of intranasal zinc sulfate irrigation on the mouse olfactory epithelium and olfactory bulb (1993) Microsc. Res. Technol., 24, pp. 195-213; Doty, R.L., Intranasal trigeminal detection of chemical vapors by humans (1975) Physiol. Behav., 14, pp. 855-859; Doty, R.L., Brugger, W.E., Jurs, P.C., Orndorff, M.A., Snyder, P.J., Lowery, L.D., Intranasal trigeminal stimulation from odorous volatiles: Psychometric responses from anosmic and normal humans (1978) Physiol. Behav., 20, pp. 175-185; Evans, A.S., Kaslow, R.A., (1997) Viral Infections of Humans: Epidemiology and Control, , 4th edn. Plenum Publishing, New York, NY; Finger, T.E., St Jeor, V.L., Kinnamon, J.C., Silver, W.L., Ultrastructure of substance P and CGRP-immunoreactive nerve fibers in the nasal epithelium of rodents (1990) J. Comp. Neurol., 294, pp. 293-305; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Harding, J.W., Getchell, T.V., Margolis, F.L., Denervation of the primary olfactory pathway in mice. V. Long-term effect of intranasal ZnSO4 irrigation on behavior, biochemistry and morphology (1978) Brain Res., 140, pp. 271-285; Hastings, L., Sensory neurotoxicology: Use of the olfactory system in the assessment of toxicity (1990) Neurotoxicol. Teratol., 12, pp. 455-459; Hastings, L., Miller, M.L., Minnema, D.J., Evans, J., Radike, M., Effects of methyl bromide on the rat olfactory system (1991) Chem. Senses, 16, pp. 43-55; Henton, W.W., Smith, J.C., Tucker, D., Odor discrimination in pigeons (1966) Science, 153, pp. 1138-1139; Henton, W.W., Smith, J.C., Tucker, D., Odor discrimination in pigeons following section of the olfactory nerves (1969) Comp. Physiol. Psychol., 69, pp. 317-323; Hornung, D.E., Kurtz, D.B., Youngentob, S.L., Can anosmic patients separate trigeminal and non-trigeminal stimulants? (1994) Proceedings of the 11th International Symposium of Olfaction and Taste, p. 635. , Springer-Verlag, Kurihara, K., Sukuki, N. and Ogawa H. (eds), Tokyo; Hurtt, M.E., Thomas, D.A., Working, P.K., Monticello, T.M., Morgan, K.T., Degeneration and regeneration of the olfactory epithelium following inhalation exposure to methyl bromide: Pathology, cell kinetics, and olfactory function (1988) Toxicol. Appl. Pharmacol., 94, pp. 311-328; Kurtz, D., White, T.L., Hornung, D.E., Belknap, E., What a tangled web we weave: Discriminating between malingering and anosmia (1999) Chem. Senses, 24, pp. 697-700; Larson, H.E., Reed, S.E., Tyrrell, D.A., Isolation of rhinoviruses and coronaviruses from 38 colds in adults (1980) J. Med. 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Neurol., 359, pp. 15-37; Schwob, J.E., Saha, S., Youngentob, S.L., Jubelt, B., Intranasal inoculation with the olfactory bulb line variant of mouse hepatitis virus causes extensive destruction of the olfactory bulb and accelerated turnover of neurons in the olfactory epithelium of mice (2001) Chem. Senses, p. 26. , (accompanying paper TF8-99); Silver, W.L., Moulton, D.G., Chemosensitivity of the rat nasal trugeminal receptors (1982) Physiol. Behav., 28, pp. 927-931; Slotnick, B., Olfactory stimulus control in the rat (1984) Chem. Senses, 9, pp. 157-165; Slotnick, B.M., Gutman, L.A., Evaluation of intranasal zinc sulfate treatment on olfactory discrimination in rats (1977) J. Comp. Physiol. 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Laryngol., 99, pp. 205-210; Yamagishi, M., Fujiwara, M., Nakamura, H., Olfactory mucosal findings and clinical course in patients with olfactory disorders following upper respiratory viral infection (1994) Rhinology, 32, pp. 113-118; Youngentob, S.L., Margolis, F.L., OMP gene deletion causes an elevation in behavioral threshold sensitivity (1999) NeuroReport, 10, pp. 15-19; Youngentob, S.L., Markert, L.M., Mozell, M.M., Hornung, D.E., A method for establishing a five odorant identification confusion matrix in rats (1990) Physiol. Behav., 47, pp. 1053-1059; Youngentob, S.L., Hornung, D.E., Mozell, M.M., Determination of carbon dioxide detection thresholds in trained rats (1991) Physiol. Behav., 49, pp. 21-26; Youngentob, S.L., Markert, L.M., Hill, T.W., Matyas, E.P., Mozell, M.M., Odorant identification in rats: An update (1991) Physiol. Behav., 49, pp. 1293-1296; Youngentob, S.L., Schwob, J.E., Sheehe, P.R., Youngentob, L.M., Odorant threshold following methyl bromide-induced lesions of the olfactory epithelium (1997) Physiol. Behav., 62, pp. 1241-1252","Youngentob, S.L.; Department of Neuroscience/Physiol., SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, United States; email: youngens@mail.upstate.edu",,"Oxford University Press",0379864X,,CHSED,"11595672","English","Chem. Senses",Article,"Final",Open Access,Scopus,2-s2.0-0034771762
"Jackwood M.W., Hilt D.A., Callison S.A., Lee C.-W., Plaza H., Wade E.","7003643324;7004853799;6602562897;24075183200;6507033233;7006005773;","Spike glycoprotein cleavage recognition site analysis of infectious bronchitis virus",2001,"Avian Diseases","45","2",,"366","372",,72,"10.2307/1592976","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034965458&doi=10.2307%2f1592976&partnerID=40&md5=285b006ffc91dfed0145b3781e0a729a","Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States","Jackwood, M.W., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States; Hilt, D.A., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States; Callison, S.A., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States; Lee, C.-W., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States; Plaza, H., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States; Wade, E., Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States","The spike glycoprotein of infectious bronchitis virus (IBV), a coronavirus, is translated as a precursor protein (S0), then cleaved into two subunits (S1 and S2) by host cell serine proteases. In this study, we compared the cleavage recognition site of 55 IBV isolates to determine if the cleavage recognition site sequence, which consists of five basic amino acid residues, correlates with host cell range, serotype, geographic origin, and pathogenicity as it does in orthomyxoviruses and paramyxoviruses. The most common cleavage recognition site observed (33 of 55 viruses) was Arg-Arg-Ser-Arg-Arg, representing at least 11 different serotypes. Thus, cleavage recognition site does not appear to correlate with serotype. We also determined that cleavage recognition site sequence does not correlate with pathogenicity because attenuated and pathogenic isolates (different passages of the same virus) contain identical cleavage recognition site sequences. In addition, nephropathogenic strains had the same cleavage recognition site sequence as many nonnephropathogenic isolates. Cleavage recognition site sequence does correlate with viruses in different geographic regions, which may be an important characteristic to examine in epidemiologic studies. An IBV monoclonal antibody neutralization-resistant mutant (NR 18) had an unusual substitution of Ile for Arg at the fourth position, giving the sequence Arg-Arg-Ser-Ile-Arg, which likely prevents cleavage and, thus, destroys the conformationally dependent monoclonal antibody binding epitope. Six residues on the amino-terminal side of the cleavage recognition site are conserved in 31% of the isolates and consist of only one or two basic amino acids. Thus, the number of basic residues around the cleavage recognition site does not appear to correlate with increased cleavability, host cell range, and increased virulence as it does with envelope glycoproteins in orthomyxoviruses and paramyxoviruses.","Cleavage recognition site; Infectious bronchitis virus; Spike glycoprotein gene","amino acid substitution; cleavage recognition site; epidemiology; epitope; genetic correlation; genetic strain; infectious bronchitis virus; molecular recognition; monoclonal antibody; neutralizing antibody; protein conformation; protein precursor; protein subunit; serotype; virus antibody; virus glycoprotein; virus mutation; Avian infectious bronchitis virus; Coronavirus","Callison, S.A., Jackwood, M.W., Hilt, D.A., Infectious bronchitis virus S2 gene sequence variability may affect S1 subunit specific antibody binding (1999) Virus Genes, 19, pp. 1-8; Cavanagh, D., The coronarvirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , S. G. Siddell, ed. Plenum Press, New York; Cavanagh, D., Davis, P.J., Pappin, D.J.C., Binns, M.M., Boursnell, M.E.G., Brown, T.D.K., Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41 (1986) Virus Res., 4, pp. 133-143; Gelb J., Jr., Jackwood, M.W., Infectious bronchitis (1997) Isolation and identification of avian pathogens, 4th ed., , The American Association of Avian Pathologists, Kennett Square, PA; Glickman, R.L., Syddall, R.J., Iorio, R.M., Sheehan, J.P., Bratt, M.A., Quantitative basic residue requirements in the cleavage-activation site of the fusion glycoprotein as a determinant of virulence for Newcastle disease virus (1988) J. Virol., 62, pp. 354-356; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Holmes, K.V., Coronaviridae and their replication (1990) Virology, 2nd ed., pp. 841-856. , B. N. Fields and D. M. Knipe, eds. Raven Press, Ltd., New York; Jackwood, M.W., Yousef, N.M.H., Hilt, D.A., Further development and use of a molecular serotype identification test for infectious bronchitis virus (1997) Avian Dis., 41, pp. 105-110; King, D.J., Cavanagh, D., Infectious bronchitis (1991) Diseases of poultry, 9th ed., pp. 471-484. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoder, Jr. Iowa State University Press, Ames, IA; Moore, K.M., Jackwood, M.W., Hilt, D.A., Brown, T.P., Identification of amino acids involved in a serotype and neutralization specific epitope within the S1 subunit of avian infectious bronchitis virus (1997) Arch. Virol., 142, pp. 2249-2256; Voet, D., Voet, J.G., (1990) Biochemistry, pp. 373-382. , John Wiley and Sons, Inc., New York; Webster, R.G., Kawaoka, Y., Bean W.J., Jr., Molecular changes in A/chicken/pennsylvania/83 (H5N2) influenza virus associated with acquisition of virulence (1986) Virology, 149, pp. 165-173","Jackwood, M.W.; Department of Avian Medicine, Poultry Diagnostic and Res. Center, University of Georgia, Athens, GA 30602-4875, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11417816","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0034965458
"Carver D.K., Vaillancourt J., Stringham M., Guy J.S., Barn H.J.","7006941312;7004505622;6507274068;7202723649;6504209914;","Mortality patterns associated with poult enteritis mortality syndrome (PEMS) and coronaviral enteritis in turkey flocks raised in PEMS-affected regions",2001,"Avian Diseases","45","4",,"985","991",,7,"10.2307/1592878","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035544240&doi=10.2307%2f1592878&partnerID=40&md5=f6d3a112e525f0e24c10662ab85a08f9","Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States","Carver, D.K., Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States; Vaillancourt, J., Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States; Stringham, M., Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States; Guy, J.S., Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States; Barn, H.J., Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States","Poult enteritis mortality syndrome (PEMS) is an economically devastating disease. To date, many questions about the syndrome remain unanswered, including its cause, transmission of causative agent(s), and control methods. Turkey coronavirus (TCV) infection has been associated with some outbreaks of PEMS, with areas having a higher prevalence of TCV infection also experiencing an increased incidence of PEMS. This study was designed to establish mortality patterns for flocks experiencing excess mortality and TCV infection in PEMS-affected regions and to delineate the possible role of TCV in PEMS-affected flocks. Fifty-four commercial turkey flocks on farms in areas with and without a history of TCV infection were monitored for weekly mortality and for antibodies to TCV. Flocks were chosen on the basis of placement dates and were monitored from day of placement until processing. All flocks were tested for TCV by an indirect fluorescent antibody assay. PEMS status was determined with the use of the clinical definition of mortality greater than 2% during any 3-wk period from 2 wk of age through the end of brooding due to unknown cause. Of the 54 flocks, 24 remained healthy, 23 experienced PEMS, and 7 tested positive for TCV but did not experience PEMS. Ten flocks experienced PEMS and tested positive for TCV, whereas 13 flocks experienced PEMS and did not test positive for TCV. Four health status groups were evident: healthy, PEMS positive, TCV positive, and PEMS + TCV positive. Distinct mortality patterns were seen for each of the four health status groups. Whereas TCV was associated with PEMS in 43% of PEMS cases, 13 cases (57%) of PEMS did not involve TCV. Additionally, 7 out of 17 cases of TCV (41%) did not experience excess mortality (PEMS) at any time during brooding of the flock. The results of this study indicate that TCV can be associated with PEMS but is neither necessary nor sufficient to cause PEMS.","Avian; Coronavirus; Disease; Enteric; Mortality; Poult enteritis mortality syndrome; Turkey","Aves; Coronavirus; Galliformes; Meleagris gallopavo; Turkey coronavirus; virus antibody; animal; animal disease; article; bird disease; blood; Coronavirus; fluorescent antibody technique; immunology; longitudinal study; mortality; prospective study; syndrome; turkey (bird); United States; virus infection; Animals; Antibodies, Viral; Coronavirus; Coronavirus Infections; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Fluorescent Antibody Technique, Indirect; Longitudinal Studies; North Carolina; Poultry Diseases; Prospective Studies; Syndrome; Turkeys","Barnes, H.J., Guy, J.S., Spiking mortality of turkeys (SMT) and related disorders: An update (1995) Proc. 19th Annual North Carolina Turkey Industry Days Conference, pp. 16-21. , North Carolina State University, Raleigh, NC; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of poultry, 10th ed., pp. 1025-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Brown, T.P., Howell, D.R., Garcia, A.P., Villegas, P., Histological lesions of spiking mortality of turkeys (SMT): Comparison of lesions induced by SMT organ suspension and cell culture (1996) J. Am. Vet. Med. Assoc., 209, p. 373; Edens, F.W., Parkhurst, C.R., Qureshi, M.A., Casas, I.A., Havenstein, G.B., Atypical Escherichia coli strains and their association with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 952-960; Edens, F.W., Qureshi, R.A., Parkhurst, C.R., Qureshi, M.A., Havenstein, G.B., Casas, I.A., Characterization of two Escherichia coli strains associated with poult enteritis and mortality syndrome (PEMS) (1997) Poult. Sci., 76, pp. 1665-1673; Guy, J.S., New methods for diagnosis of turkey coronavirus infections (1998) Proc. 49th North Central Avian Disease Conference and Symposium on Enteric and Emerging Diseases, pp. 8-10. , Indianapolis, IN; Guy, J.S., Virus infections of the gastrointestinal tract of poultry (1998) Poult. Sci., 77, pp. 1166-1175; Guy, J.S., Smith, L.G., Breslin, J.J., Vaillancourt, J.P., Barnes, H.J., High mortality and growth depression experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus (2000) Avian Dis., 44, pp. 105-113; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Dis., 44, pp. 498-506; Patel, B.L., Pomeroy, B.S., Gonder, E., Cronkite, C.E., Indirect fluorescent antibody test for diagnosis of coronaviral enteritis of turkeys (blue-comb) (1976) Am. J. Vet. Res., 37, pp. 1111-1112; Qureshi, M.A., Yu, M., Saif, Y.M., A novel ""small round virus"" inducing poult enteritis and mortality syndrome and associated immune alterations (2000) Avian Dis., 44, pp. 275-283; Schultz-Cherry, S., Kapczynski, D.R., Simmons, V.M., Koci, M.D., Brown, C., Barnes, H.J., Identifying agent(s) associated with poult enteritis mortality syndrome: Importance of the thymus (2000) Avian Dis., 44, pp. 256-265; Yu, M., Dearth, R.N., Qureshi, M.A., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome (1998) Proc. 79th Annual Conference of Research Workers in Animal Diseases, p. 42. , Chicago, IL; Yu, M., Ismail, M.M., Qureshi, M.A., Dearth, R.N., Barnes, H.J., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome: The role of a small round virus and a turkey coronavirus (2000) Avian Dis., 44, pp. 297-304","Carver, D.K.; Department of Poultry Science, Coll. of Agriculture and Life Sci., North Carolina State University, Raleigh, NC 27695, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"11785903","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0035544240
"Gallagher T.M., Buchmeier M.J.","7202310503;7006201704;","Coronavirus spike proteins in viral entry and pathogenesis",2001,"Virology","279","2",,"371","374",,278,"10.1006/viro.2000.0757","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035864294&doi=10.1006%2fviro.2000.0757&partnerID=40&md5=e3ef6ea79ede16316803ecea14f1dd7f","Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States","Gallagher, T.M., Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Buchmeier, M.J., Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States",[No abstract available],,"virus protein; vitronectin; Coronavirus; Murine hepatitis coronavirus; nonhuman; priority journal; protein interaction; short survey; virus pathogenesis; virus transmission; virus virulence; Coronavirus; Murinae; Murine hepatitis virus","Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. Virol., 71, pp. 1946-1955; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basole, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type 4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J. Virol., 71, pp. 3129-3137; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Godfraind, C., Havaux, N., Hormes, K.V., Couteleir, J.P., Role of virus receptor-bearing endothelial cells of the blood-brain barrier in preventing the spread of mouse hepatitis virus-A59 into the central nervous system (1997) J. Neurovirol., 3, pp. 428-434; Holmes, K.V., Dveksler, G.S., Specificity of coronavirus/receptor interactions (1994) Cell Receptors for Animal Viruses, pp. 403-443. , E. Wimmer, Ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Krueger, D.K., Kelly, S.M., Lewicki, D.N., Ruffolo, R., Gallagher, T.M., Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion (2000) J. Virol., , submitted for publication; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Kuo, L., Godeke, G.-J., Raamsman, M.J.B., Masters, P.S., Rottier, P.J.M., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Luo, Z., Weiss, S.R., Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein (1998) Virology, 244, pp. 483-494; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T cell mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol., 68, pp. 5483-5495; Perlman, S., Lane, T.E., Buchmeier, M.J., (2000) Coronaviruses: Hepatitis Peritonitis and Central Nervous System Disease, pp. 331-348. , (M. W. Cunningham and R. S. Fujinami, Eds.), Chap. 21. Lippincott-Williams and Wilkins, Philadelphia; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV-4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Rao, P.V., Kumari, S., Gallagher, T.M., Identification of a contiguous 6-residue determinant in the MHV receptor that controls the level of virion binding to cells (1997) Virology, 229, pp. 336-348; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) J. Virol., 71, pp. 9024-9031; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Singh, M., Berger, B., Kim, P.S., LearnCoil-VMF: Computational evidence for coiled-coil-like motifs in many viral membrane fusion proteins (1999) J. Mol. Biol., 290, pp. 1031-1041; Skehel, J.J., Wiley, D.C., Coiled coils in both intracellular vesicle and viral membrane fusion (1998) Cell, 95, pp. 871-874; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Wang, F.I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749","Buchmeier, M.J.; Division of Virology, Department of Neuropharmacology, Scripps Research Institute, San Diego, CA 92037, United States",,"Academic Press Inc.",00426822,,VIRLA,"11162792","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0035864294
"Krempl C., Herrler G.","6602462665;7006339246;","Sialic acid binding activity of transmissible gastroenteritis coronavirus affects sedimentation behavior of virions and solubilized glycoproteins",2001,"Journal of Virology","75","2",,"844","849",,22,"10.1128/JVI.75.2.844-849.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035163804&doi=10.1128%2fJVI.75.2.844-849.2001&partnerID=40&md5=253d2f52662cf4a1afbb1d8001fe2920","Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany","Krempl, C., Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany; Herrler, G., Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany","The sedimentation behavior of transmissible gastroenteritis coronavirus (TGEV) was analyzed. Upon sucrose gradient centrifugation, the major virus band was found at a density of 1.20 to 1.22 g/cm3. This high density was observed only when TGEV with a functional sialic acid binding activity was analyzed. Mutants of TGEV that lacked sialic acid binding activity due to a point mutation in the sialic acid binding site of the S protein were mainly recovered at a lower-density position on the sucrose gradient (1.18 to 1.19 g/cm3). Neuraminidase treatment of purified virions resulted in a shift of the sedimentation value from the higher to the lower density. These results suggest that binding of sialoglycoproteins to the virion surface is responsible for the sedimentation behavior of TGEV. When purified virions were treated with octylglucoside to solubilize viral glycoproteins, ultracentrifugation resulted in sedimentation of the S protein of TGEV. However, when neuraminidase-treated virions or mutants with a defective sialic acid binding activity were analyzed, the S protein remained in the supernatant rather than in the pellet fraction. These results indicate that the interaction of the surface protein S with sialoglycoconjugates is maintained after solubilization of this viral glycoprotein by detergent treatment.",,"octyl glucoside; sialic acid; sialidase; unclassified drug; virus glycoprotein; virus protein; virus protein s; animal cell; article; Enterovirus; nonhuman; point mutation; priority journal; swine; testis cell; ultracentrifugation; virion; Animals; Centrifugation, Density Gradient; Glucosides; Microscopy, Electron; N-Acetylneuraminic Acid; Neuraminidase; Solubility; Swine; Transmissible gastroenteritis virus; Viral Proteins; Virion","Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J. Gen. Virol., 76, pp. 2235-2241; Cavanagh, D., Brian, D.A., Brinton, M.A., Enjuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Revision of the taxonomy of the coronavirus, torovirus and arterivirus genera (1994) Arch. Virol., 135, pp. 227-237; Correa, I., Jimenez, G., Sune, C., Bullido, M.J., Enjuanes, L., Antigenic structure of the E2 glycoprotein from transmissible gastroenteritis coronavirus (1988) Virus Res., 10, pp. 77-93; Cox, E., Pensaert, M.B., Callebaut, P., Van Deun, K., Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis (1990) Vet. Microbiol., 23, pp. 237-243; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, O., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Hughes, M.T., Matrosovich, M., Rodgers, M.E., McGregor, M., Kawaoka, Y., Influenza A viruses lacking sialidase activity can undergo multiple cycles of replication in cell culture, eggs, or mice (2000) J. Virol., 74, pp. 5206-5212; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J. Virol., 71, pp. 3285-3287; Krempl, C., Ballesteros, M.L., Zimmer, G., Enjuanes, L., Klenk, H.-D., Herrler, G., Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants (2000) J. Gen. Virol., 81, pp. 489-496; Liu, C., Eichelberger, M.C., Compans, R.W., Air, G.M., Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding (1995) J. Virol., 69, pp. 1099-1106; Noda, M., Koide, F., Asagi, M., Inaba, Y., Physicochemical properties of transmissible gastroenteritis virus hemagglutinin (1988) Arch. Virol., 99, pp. 163-172; Noda, M., Yamashita, H., Koide, F., Kadoi, K., Omori, T., Asagi, M., Inaba, Y., Hemagglutination with transmissible gastroenteritis virus (1987) Arch. Virol., 96, pp. 109-115; Palese, P., Compans, R.W., Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action (1976) J. Gen. Virol., 33, pp. 159-163; Pensaert, M., Callebaut, P., Cox, E., Enteric coronaviruses of animals (1993), pp. 627-696. , A. Z. Kapikian (ed.), Viral infections of the gastrointestinal tract. Marcel Dekker, New York, N.Y; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71, pp. 2599-2607; Sánchez, C.M., Gebauer, F., Suné, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Schultze, B., Gross, H.-J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) J. Virol., 70, pp. 5634-5637; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293","Herrler, G.; Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany; email: herrler@viro.tiho-hannover.de",,,0022538X,,JOVIA,"11134297","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035163804
"Steininger C., Aberle S.W., Popow-Kraupp T.","6603944509;35607513000;7003520037;","Early detection of acute rhinovirus infections by a rapid reverse transcription-PCR assay",2001,"Journal of Clinical Microbiology","39","1",,"129","133",,52,"10.1128/JCM.39.1.129-133.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035175160&doi=10.1128%2fJCM.39.1.129-133.2001&partnerID=40&md5=b2a4b5e241a4f3cbe8d9b9415b9007c6","Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria","Steininger, C., Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria; Aberle, S.W., Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria; Popow-Kraupp, T., Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria","The development of a rhinovirus (RV)-RNA-specific reverse transcription (RT)-PCR assay is complicated by the close homology between the RV and enterovirus (EV) genomes in the highly conserved 5′-noncoding region, which is chosen for primer design in most RT-PCR assays. We have developed a sensitive, rapid, and RV-specific nested RT-PCR assay and have used it to test nasopharyngeal aspirates from 556 patients presenting with acute respiratory tract infections. RV RNA was detected by nested RT-PCR not only in all of 52 samples that were RV positive by virus isolation methods but also in 124 of 367 samples that were negative by virus isolation methods and enzyme-linked immunosorbent assay (ELISA). In addition, in 23 of 137 samples that were positive for a different respiratory virus by virus isolation and/or ELISA, RV RNA was detected by RT-PCR. EVs, adenoviruses, respiratory syncytial viruses, coronaviruses, and influenza and parainfluenza viruses, including clinical isolates as well as stock viruses, were not amplified in our RV-specific RT-PCR assay, indicating that this assay was highly specific. The processing time was less than 2 days for the RT-PCR, as opposed to up to 2 weeks for virus isolation. These results indicate that nested RT-PCR is more sensitive than conventional methods for the detection of RV in patients experiencing acute respiratory tract infections and represents the only reliable tool for the early laboratory diagnosis of RV infections. This is especially important in light of new opportunities for therapy currently being developed.",,"virus RNA; adolescent; adult; aged; article; aspiration; child; controlled study; Coronavirus; diagnostic accuracy; diagnostic value; early diagnosis; Enterovirus; enzyme linked immunosorbent assay; gene amplification; genome; human; infant; Influenza virus; major clinical study; newborn; Parainfluenza virus; priority journal; Respiratory syncytial pneumovirus; reverse transcription polymerase chain reaction; Rhinovirus; sequence homology; virus detection; virus infection; virus isolation; Adolescent; Adult; Aged; Aged, 80 and over; Child; Child, Preschool; Enzyme-Linked Immunosorbent Assay; Humans; Infant; Infant, Newborn; Middle Aged; Nasopharynx; Picornaviridae Infections; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction; Rhinovirus; RNA, Viral; Sensitivity and Specificity; Coronavirus; Enterovirus; Influenza virus; Respiratory syncytial virus; Rhinovirus; RNA viruses; Syncytial virus","Andeweg, A.C., Bestebroer, T.M., Huybreghs, M., Kimman, T.G., De Jong, J.C., Improved detection of rhinoviruses in clinical samples by using a newly developed nested reverse transcription-PCR assay (1999) J. Clin. Microbiol., 37, pp. 524-530; Arola, M., Ziegler, T., Ruuskanen, O., Mertsola, J., Näntö-Salonen, K., Halonen, P., Rhinovirus in acute otitis media (1988) J. Pediatr., 113, pp. 693-695; Berman, S., McIntosh, K., Selective primary health care: Strategies for control of disease in the developing world. XXI. Acute respiratory infections (1985) Rev. Infect. Dis., 7, pp. 674-691; Blomqvist, S., Skyttä, A., Roivainen, M., Hovi, T., Rapid detection of human rhinoviruses in nasopharyngeal aspirates by a microwell reverse transcription-PCR-hybridization assay (1999) J. Clin. Microbiol., 37, pp. 2813-2816; Couch, R.B., Rhinoviruses (1996), pp. 713-734. , B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, T. P. Monath, J. L. Meinick, and B. Roizman (ed.), Fields' virology. Lippincott-Raven, Philadelphia, Pa; Gern, J.E., Busse, W.W., Association of rhinovirus infections with asthma (1999) Clin. Microbiol. Rev., 12, pp. 9-18; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypiä, T., Hurskainen, P., Pallansch, M., Detection of enteroviruses and rhinoviruses in clinical specimens by PCR and liquid-phase hybridization (1995) J. Clin. Microbiol., 33, pp. 648-653; Hueston, W.J., Mainous, A.G., Ornstein, S., Pan, Q., Jenkins, R., Antibiotics for upper respiratory tract infections: Follow-up utilization and antibiotic use (1999) Arch. Fam. Med., 8, pp. 426-430; Ireland, D.C., Kent, J., Nicholson, K.G., Improved detection of rhinoviruses in nasal and throat swabs by seminested RT-PCR (1993) J. Med. Virol., 40, pp. 96-101; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Campbell, M.J., Josephs, L.K., Cunningham, A., Holgate, S.T., The relationship between upper respiratory infections and hospital admissions for asthma: A time-trend analysis (1996) Am. J. Respir. Crit. Care Med., 154, pp. 654-660; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Lambden, P.R., Holgate, S.T., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J. Clin. Microbiol., 31, pp. 111-117; Kämmerer, U., Kunkel, B., Korn, K., Nested PCR for specific detection and rapid identification of human picornaviruses (1994) J. Clin. Microbiol., 32, pp. 285-291; Kellner, G., Popow-Kraupp, T., Kundi, M., Binder, C., Wallner, H., Kunz, C., Contribution of rhinoviruses to respiratory viral infections in childhood: A prospective study in a mainly hospitalized infant population (1988) J. Med. Virol., 25, pp. 455-469; Kellner, G., Popow-Kraupp, T., Popow, C., Kundi, M., Kunz, C., Surveillance of viral respiratory tract infections over a one year period in mainly hospitalized Austrian infants and children by a rapid enzyme-linked immunosorbent assay diagnosis (1990) Wien. Klin. Wochenschr., 102, pp. 100-106; Mainous, A.G., Hueston, W.J., Love, M.M., Antibiotics for colds in children: Who are the high prescribers? (1998) Arch. Pediatr. Adolesc. Med., 152, pp. 349-352; Melnick, J.L., Enteroviruses: Polioviruses, coxsackieviruses, echoviruses, and newer enteroviruses (1996), pp. 655-712. , B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, T. P. Monath, J. L. Meinick, and B. Roizman (ed.), Fields' virology. Lippincott-Raven, Philadelphia, Pa; Monto, A.S., Studies of the community and family: Acute respiratory illness and infection (1994) Epidemiol. Rev., 16, pp. 351-373; Monto, A.S., Bryan, E.R., Ohmit, S., Rhinovirus infections in Tecumseh, Michigan: Frequency of illness and number of serotypes (1987) J. Infect. Dis., 156, pp. 43-49; Monto, A.S., Bryan, E.R., Rhodes, L.M., The Tecumseh study of respiratory illness. VII. Further observations on the occurrence of respiratory syncytial virus and Mycoplasma pneumoniae infections (1974) Am. J. Epidemiol., 100, pp. 458-468; Monto, A.S., Cavallaro, J.J., The Tecumseh study of respiratory illness. IV. Prevalence of rhinovirus serotypes 1966-1969 (1972) Am. J. Epidemiol., 96, pp. 352-360; Olive, D.M., Al-Mufti, S., Al-Mulla, W., Khan, M.A., Pasca, A., Stanway, G., Al-Nakib, W., Detection and differentiation of picornaviruses in clinical samples following genomic amplification (1990) J. Gen. Virol., 71, pp. 2141-2147; Pitkäranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR (1997) J. Clin. Microbiol., 35, pp. 1791-1793; Santti, J., Hyypiä, T., Halonen, P., Comparison of PCR primer pairs in the detection of human rhinoviruses in nasopharyngeal aspirates (1997) J. Virol. Methods, 66, pp. 139-147; Sarkkinen, H.K., Halonen, P.E., Arstila, P.P., Salmi, A.A., Detection of respiratory syncytial, parainfluenza type 2, and adenovirus antigens by radioimmunoassay and enzyme immunoassay on nasopharyngeal specimens from children with acute respiratory disease (1981) J. Clin. Microbiol., 13, pp. 258-265; Stott, E.J., Tyrrell, D.A., Some improved techniques for the study of rhinoviruses using HeLa cells (1968) Arch. Gesamte Virusforsch., 23, pp. 236-244; Wang, Q.M., Protease inhibitors as potential antiviral agents for the treatment of picornaviral infections (1999) Prog. Drug. Res., 52, pp. 197-219; Yun, B.Y., Kim, M.R., Park, J.Y., Choi, E.H., Lee, H.J., Yun, C.K., Viral etiology and epidemiology of acute lower respiratory tract infections in Korean children (1995) Pediatr. Infect. Dis. J., 14, pp. 1054-1059","Popow-Kraupp, T.; Institute of Virology, University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria; email: theresia.popow@univie.ac.at",,,00951137,,JCMID,"11136760","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0035175160
"Van Elden L.J.R., Nijhuis M., Schipper P., Schuurman R., Van Loon A.M.","6602259994;6701777688;7004066843;56898703600;35476145800;","Simultaneous detection of influenza viruses A and B using real-time quantitative PCR",2001,"Journal of Clinical Microbiology","39","1",,"196","200",,326,"10.1128/JCM.39.1.196-200.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035166438&doi=10.1128%2fJCM.39.1.196-200.2001&partnerID=40&md5=3b36673e5e04dc32247088ea30a5ac54","Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands","Van Elden, L.J.R., Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands; Nijhuis, M., Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands; Schipper, P., Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands; Schuurman, R., Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands; Van Loon, A.M., Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands","Since influenza viruses can cause severe illness, timely diagnosis is important for an adequate intervention. The available rapid detection methods either lack sensitivity or require complex laboratory manipulation. This study describes a rapid, sensitive detection method that can be easily applied to routine diagnosis. This method simultaneously detects influenza viruses A and B in specimens of patients with respiratory infections using a TaqMan-based real-time PCR assay. Primers and probes were selected from highly conserved regions of the matrix protein gene of influenza virus A and the hemagglutinin gene segment of influenza virus B. The applicability of this multiplex PCR was evaluated with 27 influenza virus A and 9 influenza virus B reference strains and isolates. In addition, the specificity of the assay was assessed using eight reference strains of other respiratory viruses (parainfluenza viruses 1 to 3, respiratory syncytial virus Long strain, rhinoviruses 1A and 14, and coronaviruses OC43 and 229E) and 30 combined nose and throat swabs from asymptomatic subjects. Electron microscopy-counted stocks of influenza viruses A and B were used to develop a quantitative PCR format. Thirteen copies of viral RIgA were detected for influenza virus A, and 11 copies were detected for influenza virus B, equaling 0.02 and 0.006 50% tissue culture infective doses, respectively. The diagnostic efficacy of the multiplex TaqMan-based PCR was determined by testing 98 clinical samples. This real-time PCR technique was found to be more sensitive than the combination of conventional viral culturing and shell vial culturing.",,"article; assay; controlled study; diagnostic accuracy; diagnostic value; disease severity; DNA probe; early diagnosis; electron microscopy; human; influenza; Influenza virus A; Influenza virus B; intermethod comparison; polymerase chain reaction; priority journal; respiratory tract infection; throat culture; virus culture; virus detection; virus isolation; Follow-Up Studies; Humans; Influenza A virus; Influenza B virus; Influenza, Human; Polymerase Chain Reaction; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sensitivity and Specificity; Taq Polymerase; Virus Cultivation; human influenza virus; Influenza virus; Influenzavirus A; Influenzavirus B; Respiratory syncytial virus; Rhinovirus; RNA viruses; Syncytial virus","Atmar, R.L., Baxter, B.D., Dominguez, E.A., Taber, L.H., Comparison of reverse transcription-PCR with tissue culture and other rapid diagnostic assays for detection of type A influenza virus (1996) J. Clin. Microbiol., 34, pp. 2604-2606; Boom, R., Sol, C.J., Salimans, M.M., Jansen, C.L., Wertheim-Van Dillen, P.M., Van der Noorda, J., Rapid and simple method for purification of nucleic acids (1990) J. Clin. Microbiol., 28, pp. 495-503; Claas, E.C., Van Milaan, A.J., Sprenger, M.J., Ruiten-Stuiver, M., Arron, G.I., Rothbarth, P.H., Masurel, N., Prospective application of reverse transcriptase polymerase chain reaction for diagnosing influenza infections in respiratory samples from a children's hospital (1993) J. Clin. Microbiol., 31, pp. 2218-2221; Doller, G., Schuy, W., Tjhen, K.Y., Stekeler, B., Gerth, H.J., Direct detection of influenza virus antigen in nasopharyngeal specimens by direct enzyme immunoassay in comparison with quantitating virus shedding (1992) J. Clin. Microbiol., 30, pp. 866-869; Ellis, J.S., Fleming, D.M., Zambon, M.C., Multiplex reverse transcription-PCR for surveillance of influenza A and B viruses in England and Wales in 1995 and 1996 (1997) J. Clin. Microbiol., 35, pp. 2076-2082; Hayden, F.G., Atmar, R.L., Schilling, M., Johnson, C., Poretz, D., Paar, D., Huson, L., Mills, R.G., Use of the selective oral neuraminidase inhibitor oseltamivir to prevent influenza (1999) N. Engl. J. Med., 341, pp. 1336-1343; Hayden, F.G., Osterhaus, A.D.M.E., Treanor, J.J., Fleming, D.M., Aoki, F.Y., Nicholson, K.G., Bohnen, A.M., Wightman, K., Efficacy and safety of the neuraminidase inhibitor zanamivir in the treatment of influenzavirus infections (1997) N. Engl. J. Med., 337, pp. 874-880; Hayden, F.G., Treanor, J.J., Fritz, R.S., Lobo, M., Betts, R.F., Miller, M., Kinnersley, N., Straus, S.E., Use of the oral neuraminidase inhibitor oseltamivir in experimental human influenza: Randomized controlled trials for prevention and treatment (1999) JAMA, 282, pp. 1240-1246; Heid, C.A., Stevens, J., Livak, K.J., Williams, P.M., Real time quantitative PCR (1996) Genome Res., 6, pp. 986-994; Kato, T., Mizokami, M., Mukaide, M., Orito, E., Ohno, T., Nakano, T., Tanaka, Y., Kojiro, M., Development of a TT virus DNA quantification system using real-time detection PCR (2000) J. Clin. Microbiol., 38, pp. 94-98; Kok, J., Mickan, L., Burrell, C.J., Routine diagnosis of seven respiratory viruses and Mycoplasma pneumoniae by enzyme immunoassay (1994) J. Virol. Methods, 50, pp. 87-100; Randomised trial of efficacy and safety of inhaled zanamavir in treatment of influenza A and B virus infections (1998) Lancet, 352, pp. 1877-1881; Nijhuis, M., Boucher, C.A., Schuurman, R., Sensitive procedure for the amplification of HIV-1 RNA using a combined reverse-transcription and amplification reaction (1995) BioTechniques, 19, pp. 178-180. , 182; Pongers-Willemse, M.J., Verhagen, O.J., Tibbe, G.J., Wijkhuijs, A.J., De Haas, V., Roovers, E., Van Der Schoot, C.E., Van Dongen, J.J., Realtime quantitative PCR for the detection of minimal residual disease in acute lymphoblastic leukemia using junctional region specific TaqMan probes (1998) Leukemia, 12, pp. 2006-2014; Schmid, M.L., Kudesia, G., Wake, S., Read, R.C., Prospective comparative study of culture specimens and methods in diagnosing influenza in adults (1998) Br. Med. J., 316, p. 275; Schweiger, B., Zadow, I., Heckler, R., Timm, H., Pauli, G., Application of a fluorogenic PCR assay for typing and subtyping of influenza viruses in respiratory samples (2000) J. Clin. Microbiol., 38, pp. 1552-1558; Vet, J.A., Majithia, A.R., Marras, S.A., Tyagi, S., Dube, S., Poiesz, B.J., Kramer, F.R., Multiplex detection of four pathogenic retroviruses using molecular beacons (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 6394-6399; Wiselka, M., Influenza: Diagnosis, management, and prophylaxis (1994) Br. Med. J., 308, pp. 1341-1345; Wright, K.E., Wilson, G.A., Novosad, D., Dimock, C., Tan, D., Weber, J.M., Typing and subtyping of influenza viruses in clinical samples by PCR (1995) J. Clin. Microbiol., 33, pp. 1180-1184; Ziegler, T., Hall, H., Sanchez-Fauquier, A., Gamble, W., Cos, N., Type and subtype specific detection of influenza viruses in clinical specimens by rapid culture assay (1995) J. Clin. Microbiol., 33, pp. 318-322","Van Elden, L.J.R.; Eijkman-Winkler Inst. Microbiol., Department of Virology, University Medical Center Utrecht, P.O. Box 85500, 3508 GA Utrecht, Netherlands; email: l.vanelden@digd.azu.nl",,,00951137,,JCMID,"11136770","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0035166438
"Reddy G.S., Srinivasan V.A.","7402668386;57203072398;","Development of canine coronavirus vaccine",2001,"Indian Veterinary Journal","78","2",,"98","100",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-24044495302&partnerID=40&md5=19f0ffae931c03f675a382d08b76bea6","Indian Immunologicals Limited, Hyderabad - 500 019, India","Reddy, G.S., Indian Immunologicals Limited, Hyderabad - 500 019, India; Srinivasan, V.A., Indian Immunologicals Limited, Hyderabad - 500 019, India","Two formulations of canine coronavirus (CCV) vaccines were prepared from local CCV isolate. The efficacy of the vaccine was tested in dogs and guinea pigs. The guinea pigs vaccinated with inactivated coronavirus vaccine 1 (ICCV I) and ICCV II showed serological response of log10 2.56 SN50 and log10 3.22 SN50 respectively on 28th day post vaccination (dpv) against the 0 day titre of log10 &lt;0.30 SN50. The seronegative dogs vaccinated with ICCV I and ICCV II elicited mean antibody response of log10 2.68 SN50 and log10 3.14 SN50 respectively. The two formulations of inactivated CCV vaccine were safe and efficacious.",,,"Appel, M.J., (1987) Virus Infections of Carnivores, p. 115. , Ed by Max J. Appel. Elsevier Science Publishers, Amsterdam, The Netherlands; Appel, M.J.G., (1999) Adv. Vet. Med., 41, p. 309; Appel, M.J.G., Meunier, P., Pollock, R., Greisen, H., Carmicheal, L., Glickman, L., (1980) Canine Pract., 7, p. 22; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.G., Marchiwicki, R.H., Strano, A.J., (1975) Proceedings of 78th Annual Meeting of US Animal Health Association, p. 359; (1998) British Pharmacopoeia (Veterinary), , HMSO. London; Fairchild, G.A., Cohen, D., (1969) Am. J. Vet. Res., 30, p. 923; Fulker, R., Wasmoen, T., Atchison, R., Chu, H.J., Acree, W., (1995) Current Concepts in Molecular Biology and Pathogenesis, p. 229. , Ed. by Tabot, P.J., Levy, G.A., New York, USA; Ganesan, P.I., Ramdass, P., Gunaseelan, L., Thanappa Pillai, M., Raghavan, N., (1990) Indian Vet. J., 67, p. 1088; Karber, (1931) Archives Experimental Pathologic and Pharmakologie, 162, p. 480; Martin, M.L., (1985) Compend. Cont. Educ. Pract. Vet., 7, p. 1013","Srinivasan, V.A.; Indian Immunologicals Limited, Hyderabad - 500 019, India",,,00196479,,,,"English","Indian Vet. J.",Article,"Final",,Scopus,2-s2.0-24044495302
"Escors D., Ortego J., Laude H., Enjuanes L.","6507259181;35254237800;7006652624;7006565392;","The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability",2001,"Journal of Virology","75","3",,"1312","1324",,82,"10.1128/JVI.75.3.1312-1324.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035157384&doi=10.1128%2fJVI.75.3.1312-1324.2001&partnerID=40&md5=081bb0fafc83ce957b3bb4e88266e1cc","Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Escors, D., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Ortego, J., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Laude, H., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The architecture of transmissible gastroenteritis coronavirus includes three different structural levels, the envelope, an internal core, and the nucleocapsid that is released when the core is disrupted. Starting from purified virions, core structures have been reproducibly isolated as independent entities. The cores were stabilized at basic pH and by the presence of divalent cations, with Mg2+ ions more effectively contributing to core stability. Core structures showed high resistance to different concentrations of detergents, reducing agents, and urea and low concentrations of monovalent ions (&lt;200 Mm). Cores were composed of the nucleoprotein, RNA, and the C domain of the membrane (M) protein. At high salt concentrations (200 to 300 Mm), the M protein was no longer associated with the nucleocapsid, which resulted in destruction of the core structure. A specific ionic interaction between the M protein carboxy terminus and the nucleocapsid was demonstrated using three complementary approaches: (i) a binding assay performed between a collection of M protein amino acid substitution or deletion mutants and purified nucleocapsids that led to the identification of a 16-amino-acid (aa) domain (aa 237 to 252) as being responsible for binding the M protein to the nucleocapsid; (ii) the specific inhibition of this binding by monoclonal antibodies (MAbs) binding to a carboxy-terminal M protein domain close to the indicated peptide but not by MAbs specific for the M protein amino terminus; and (iii) a 26-residue peptide, including the predicted sequence (aa 237 to 252), which specifically inhibited the binding. Direct binding of the M protein to the nucleoprotein was predicted, since degradation of the exposed RNA by RNase treatment did not affect the binding. It is proposed that the M protein is embedded within the virus membrane and that the C region, exposed to the interior face of the virion in a population of these molecules, interacts with the nucleocapsid to which it is anchored, forming tile core. Only the C region of the M protein is part of the core.",,"amino acid; detergent; M protein; magnesium; nucleoprotein; ribonuclease; RNA; urea; animal cell; article; carboxy terminal sequence; Coronavirus; nonhuman; priority journal; protein binding; swine; virion; virus core; virus nucleocapsid; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Epitope Mapping; Molecular Sequence Data; Nucleocapsid; Swine; Transmissible gastroenteritis virus; Viral Matrix Proteins; Virus Assembly","Almazan, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. 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Virol., 23, pp. 717-724; Bremer, A., Häner, M., Aebi, U., Negative staining (1998), 3, pp. 277-284. , J. E. Celis (ed.), Cell biology. A laboratory handbook, 2nd ed. Academic Press, San Diego, Calif; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995), pp. 165-176. , S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y; Charley, B., Laude, H., Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of transmembrane glycoprotein E1 (1988) J. Virol., 62, pp. 8-10; Cheng, R.H., Kuhn, R.J., Olson, N.H., Rossmann, M.G., Choi, H., Smith, T.J., Baker, T.S., Nucleocapsid and glycoprotein organization in an enveloped virus (1995) Cell, 80, pp. 621-630; Correa, I., Gebauer, F., Bullido, M.J., Suñé, C., Baay, M.F.D., Zwaagstra, K.A., Posthumus, W.P.A., Enjuanes, L., Localization of antigenic sites of the E2 glycoprotein of transmissible gastroenteritis coronavirus (1990) J. Gen. Virol., 71, pp. 271-279; Cosson, P., Direct interaction between the envelope and matrix proteins of HIV-1 (1996) EMBO J., 15, pp. 5783-5788; De Haan, C.A.M., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J.M., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; De Haan, C.A.M., Smeets, M., Vernooij, F., Vennema, H., Rottier, P.J.M., Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein (1999) J. Virol., 73, pp. 7441-7452; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000), pp. 835-849. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M. Lemon, M. A. Mayo, D. J. McGeoch, C. R. Pringle, and R. B. Wickner (ed.), Virus taxonomy. Academic Press, New York, N.Y; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Gajardo, R., Vende, P., Poncet, D., Cohen, J., Two proline residues are essential in the calcium-binding activity of rotavirus VP7 outer capsid protein (1997) J. Virol., 71, pp. 2211-2216; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Helenius, A., Kartenbeck, J., The effects of octylglucoside on the Semliki forest virus membrane. Evidence for a spike-protein-nucleocapsid interaction (1980) Eur. J. 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Microbiol., 18, pp. 197-208; Woods, R.D., Wesley, R.D., Kapke, P.A., Complement-dependent neutralization of transmissible gastroenteritis virus by monoclonal antibodies (1987) Adv. Exp. Med. Biol., 218, pp. 493-500; Ye, Z., Liu, T., Offringa, D.P., McInnis, J., Levandowski, R.A., Association of influenza virus matrix protein with ribonucleoproteins (1999) J. Virol., 73, pp. 7467-7473","Enjuanes, L.; Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,0022538X,,JOVIA,"11152504","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035157384
"Navas S., Seo S.-H., Chua M.M., Sarma J.D., Lavi E., Hingley S.T., Weiss S.R.","7003695377;7202469910;7006092803;55662977700;7006986911;6701491322;57203567044;","Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis",2001,"Journal of Virology","75","5",,"2452","2457",,57,"10.1128/JVI.75.5.2452-2457.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035127581&doi=10.1128%2fJVI.75.5.2452-2457.2001&partnerID=40&md5=a668b58eb33cc740d348bee30172b9c2","Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Navas, S., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Seo, S.-H., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Chua, M.M., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Sarma, J.D., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Lavi, E., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Hingley, S.T., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Recombinant mouse hepatitis viruses (MHV) differing only in the spike gene, containing A59, MHV-4, and MHV-2 spike genes in the background of the A59 genome, were compared for their ability to replicate in the liver and induce hepatitis in weanling C57BL/6 mice infected with 500 PFU of each virus by intrahepatic injection. Penn98-1, expressing the MHV-2 spike gene, replicated to high titer in the liver, similar to MHV-2, and induced severe hepatitis with extensive hepatocellular necrosis. SA59R13, expressing the A59 spike gene, replicated to a somewhat lower titer and induced moderate to severe hepatitis with zonal necrosis, similar to MHV-A59. S4R21, expressing the MHV-4 spike gene, replicated to a minimal extent and induced few if any pathological changes, similar to MHV-4. Thus, the extent of replication and the degree of hepatitis in the liver induced by these recombinant viruses were determined largely by the spike protein.",,"gene product; protein spike; unclassified drug; virus protein; animal experiment; animal model; animal tissue; article; controlled study; Coronavirus; gene expression; hepatitis; liver; liver necrosis; mouse; nonhuman; priority journal; virus recombinant; virus replication; virus strain; Animals; Coronavirus Infections; Hepatitis, Viral, Animal; Immunohistochemistry; Liver; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Recombination, Genetic; Viral Envelope Proteins; Virus Replication","Ando, K., Moriyama, T., Guidotti, L.G., Wirth, S., Schreiber, R.D., Schlicht, H.J., Huang, S.N., Chisari, F.V., Mechanisms of class I restricted immunopathology: A transgenic mouse model of fulminant hepatitis (1993) J. Exp. 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Biol., 380, pp. 577-582; Hingley, S.T., Lepare-Goffart, I., Weiss, S.R., The spike protein of routine coronavirus mouse hepatitis virus strain A59 is not cleaved in primary glial cells and primary hepatocytes (1998) J. Virol., 72, pp. 1606-1609; Hirano, N., Murakami, T., Taguchi, F., Fujiwara, K., Matumoto, M., Comparison of mouse hepatitis virus strains for pathogenicity in weanling mice infected by various routes (1981) Arch. Virol., 70, pp. 69-73; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Joseph, J., Kim, R., Siebert, K., Lublin, F.D., Offenbach, C., Knobler, R.L., Organ specific endothelial cell heterogeneity influences differential replication and cytopathogenicity of MHV-3 and MHV-4: Implications in viral tropism (1995) Adv. Exp. Med. Biol., 380, pp. 43-50; Knobler, R.L., Haspel, M.V., Oldstone, M.B., Mouse hepatitis virus type 4 (JHM strains), induced fatal central nervous system disease. I. 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Virol., 69, pp. 87-98; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Requirement of proteolytic cleavage of the murine coronavirus MHV-2 spike protein for fusion activity (1998) Adv. Exp. Med. Biol., 440, pp. 89-93; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"11160748","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035127581
"Shen X., Masters P.S.","36867025200;7006234572;","Evaluation of the role of heterogeneous nuclear ribonucleoprotein A1 as a host factor in murine coronavirus discontinuous transcription and genome replication",2001,"Proceedings of the National Academy of Sciences of the United States of America","98","5",,"2717","2722",,38,"10.1073/pnas.031424298","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035957016&doi=10.1073%2fpnas.031424298&partnerID=40&md5=dabd828ffcae9f3e98ccbff662804d25","Wadsworth Center for Laboratories and Research, Department of Biomedical Sciences, State University of New York, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States","Shen, X., Wadsworth Center for Laboratories and Research, Department of Biomedical Sciences, State University of New York, Albany, NY 12201, United States; Masters, P.S., Wadsworth Center for Laboratories and Research, Department of Biomedical Sciences, State University of New York, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States","Viruses with RNA genomes often capture and redirect host cell components to assist in mechanisms particular to RNA-dependent RNA synthesis. The nidoviruses are an order of positive-stranded RNA viruses, comprising coronaviruses and arteriviruses, that employ a unique strategy of discontinuous transcription, producing a series of subgenomic mRNAs linking a 5′ leader to distal portions of the genome. For the prototype coronavirus mouse hepatitis virus (MHV), heterogeneous nuclear ribonucleoprotein (hnRNP) A1 has been shown to be able to bind in vitro to the negative strand of the intergenic sequence, a cis-acting element found in the leader RNA and preceding each downstream ORF in the genome, hnRNP A1 thus has been proposed as a host factor in MHV transcription. To test this hypothesis genetically, we initially constructed MHV mutants with a very high-affinity hnRNP A1 binding site inserted in place of, or adjacent to, an intergenic sequence in the MHV genome. This inserted hnRNP A1 binding site was not able to functionally replace, or enhance transcription from, the intergenic sequence. This finding led us to test more directly the role of hnRNP A1 by analysis of MHV replication and RNA synthesis in a murine cell line that does not express this protein. The cellular absence of hnRNP A1 had no detectable effect on the production of infectious virus, the synthesis of genomic RNA, or the quantity or quality of subgenomic mRNAs. These results strongly suggest that hnRNP A1 is not a required host factor for MHV discontinuous transcription or genome replication.",,"cis acting element; heterogeneous nuclear ribonucleoprotein; animal cell; article; binding site; controlled study; gene sequence; Murine hepatitis coronavirus; nonhuman; priority journal; protein binding; virus genome; virus replication; virus transcription; Animals; Base Sequence; Coronavirus; DNA Primers; Heterogeneous-Nuclear Ribonucleoprotein Group A-B; Heterogeneous-Nuclear Ribonucleoproteins; Mice; Mutagenesis, Site-Directed; Ribonucleoproteins; Transcription, Genetic; Tumor Cells, Cultured; Virus Replication; Animalia; Coronavirus; DNA viruses; Murinae; Murine hepatitis virus; RNA viruses","Lai, M.M.C., (1998) Virology, 244, pp. 1-12; Strauss, J.H., Strauss, E.G., (1999) Science, 283, pp. 802-804; Das, T., Mathur, M., Gupta, A.K., Janssen, G.M.C., Banerjee, A.K., (1998) Proc. Natl. Acad. Sci. 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USA, 97, pp. 5516-5521; Bai, Y., Lee, D., Yu, T., Chasin, L.A., (1999) Nucleic Acids Res., 27, pp. 1126-1134; Zhang, X., Li, H.-P., Xue, W., Lai, M.M.C., (1999) Virology, 264, pp. 115-124; Zhang, X., Wang, Y., (1999) Virology, 265, pp. 96-109; Molenkamp, R., Van Tol, H., Rozier, B.C.D., Van der Meer, Y., Spaan, W.J.M., Snijder, E.J., (2000) J. Gen. Virol., 81, pp. 2491-2496; Shi, S.T., Huang, P., Li, H.-P., Lai, M.M.C., (2000) EMBO J., 19, pp. 4701-4711; Lin, Y.-J., Liao, C.-L., Lai, M.M.C., (1994) J. Virol., 68, pp. 8131-8140","Masters, P.S.; David Axelrod Institute, Wadsworth Center, New York State Department of Health, New Scotland Avenue, Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,00278424,,PNASA,"11226306","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0035957016
"Krueger D.K., Kelly S.M., Lewicki D.N., Ruffolo R., Gallagher T.M.","7103338021;57198994758;7006093173;57196538674;7202310503;","Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion",2001,"Journal of Virology","75","6",,"2792","2802",,62,"10.1128/JVI.75.6.2792-2802.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035129841&doi=10.1128%2fJVI.75.6.2792-2802.2001&partnerID=40&md5=26c79cd19778ea9a517796e154292849","Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States","Krueger, D.K., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States; Kelly, S.M., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States; Lewicki, D.N., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States; Ruffolo, R., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States; Gallagher, T.M., Dept. of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States","The prototype JHM strain of murine hepatitis virus (MHV) is an enveloped, RNA-containing coronavirus that has been selected in vivo for extreme neurovirulence. This virus encodes spike (S) glycoproteins that are extraordinarily effective mediators of intercellular membrane fusion, unique in their ability to initiate fusion even without prior interaction with the primary MHW receptor, a murine carcinoembryonic antigen-related cell adhesion molecule (CEACAM). In considering the possible role of this hyperactive membrane fusion activity in neurovirulence, we discovered that the growth of JHM in tissue culture selected for variants that had lost murine CEACAM-independent fusion activity. Among the collection of variants, mutations were identified in regions encoding both the receptor-binding (S1) and fusion-inducing (S2) subunits of the spike protein. Each mutation was separately introduced into cDNA encoding the prototype JHM spike, and the set of cDNAs was expressed using vaccinia virus vectors. The variant spikes were similar to that of JHM in their assembly into oligomers, their proteolysis into S1 and S2 cleavage products, their transport to cell surfaces, and their affinity for a soluble form of murine CEACAM. However, these tissue culture-adapted spikes were significantly stabilized as S1-S2 heteromers, and their entirely CEACAM-dependent fusion activity was delayed or reduced relative to prototype JHM spikes. The mutations that we have identified therefore point to regions of the S protein that specifically regulate the membrane fusion reaction. We suggest that cultured cells, unlike certain in vivo environments, select for S proteins with delayed, CEACAM-dependent fusion activities that may increase the likelihood of virus internalization prior to the irreversible uncoating process.",,"carcinoembryonic antigen; cell adhesion molecule; complementary DNA; protein subunit; spike glycoprotein; unclassified drug; virus glycoprotein; virus protein; virus vector; article; controlled study; human; human cell; internalization; membrane fusion; Murine hepatitis coronavirus; priority journal; protein degradation; Vaccinia virus; virogenesis; virus cell interaction; virus virulence; Animals; Antigens, CD; Carcinoembryonic Antigen; Cell Adhesion Molecules; Cell Line; Coronavirus Infections; Gene Expression Regulation, Viral; Giant Cells; Glycoproteins; Humans; Membrane Fusion; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutation; Receptors, Virus; Variation (Genetics); Viral Envelope Proteins","Alkhatib, G., Broder, C.C., Berger, E.A., Cell-type-specific fusion cofactors determine human immunodeficiency virus type 1 tropism for T-cell lines versus primary macrophages (1996) J. 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"Haring J.S., Pewe L.L., Perlman S.","7101956116;6603143496;7102708317;","High-magnitude, virus-specific CD4 T-cell response in the central nervous system of coronavirus-infected mice",2001,"Journal of Virology","75","6",,"3043","3047",,37,"10.1128/JVI.75.6.3043-3047.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035124174&doi=10.1128%2fJVI.75.6.3043-3047.2001&partnerID=40&md5=d3bbb97c1285caff8cc91aca87a580c4","Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Haring, J.S., Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; Pewe, L.L., Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","The neurotropic JHM strain of mouse hepatitis virus (MHV) causes acute encephalitis and chronic demyelinating encephalomyelitis in rodents. Previous results indicated that CD8 T cells infiltrating the central nervous system (CNS) were largely antigen specific in both diseases. Herein we show that by 7 days postinoculation, nearly 30% of the CD4 T cells in the acutely infected CNS were MHV specific by using intracellular gamma interferon (IFN-γ) staining assays. In mice with chronic demyelination, 10 to 15% of the CD4 T cells secreted IFN-γ in response to MHV-specific peptides. Thus, these results show that infection of the CNS is characterized by a large influx of CD4 T cells specific for MHV and that these cells remain functional, as measured by cytokine secretion, in mice with chronic demyelination.",,"CD4 antigen; CD8 antigen; gamma interferon; T lymphocyte receptor; animal experiment; animal model; animal tissue; article; cell specificity; cellular immunity; central nervous system infection; chronicity; controlled study; Coronavirus; cytokine release; demyelination; immunohistochemistry; lymphocytic infiltration; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; T lymphocyte subpopulation; virus encephalitis; Animals; CD4-Positive T-Lymphocytes; Central Nervous System Viral Diseases; Coronavirus Infections; Mice; Murine hepatitis virus; Receptors, Antigen, T-Cell, alpha-beta","Bergmann, C.C., Altman, J.D., Hinton, D., Stohlman, S.A., Inverted immunodominance and impaired cytolytic function of CD8+ T cells during viral persistence in the central nervous system (1999) J. 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Immunol., 163, pp. 6106-6113; Stohlman, S.A., Bergmann, C.C., Lin, M.T., Cua, D.J., Hinton, D.R., CTL effector function within the central nervous system requires CD4+ T cells (1998) J. Immunol., 160, pp. 2896-2904; Stohlman, S.A., Bergmann, C.C., Perlman, S., Mouse hepatitis virus (1998) Persistent viral infections, pp. 537-557. , R. Ahmed and I. Chen (ed.). John Wiley & Sons, Ltd., New York, N.Y; Topham, D.J., Doherty, P.C., Longitudinal analysis of the acute Sendai virus-specific CD4+ T cell response and memory (1998) J. Immunol., 161, pp. 4530-4535; Varga, S., Welsh, R., Detection of a high frequency, of virus-specific CD4+ T cells during acute infection with lymphocytic choriomeningitis virus (1998) J. Immunol., 161, pp. 3215-3218; Varga, S.M., Welsh, R.M., High frequency, of virus-specific interleukin-2-producing CD4+ T cells and Th1 predominance during lymphocytic choriomeningitis virus infection (2000) J. Virol., 74, pp. 4429-4432; Varga, S.M., Welsh, R.M., Stability of virus-specific CD4+ T cell frequencies from acute infection into long term memory (1998) J. Immunol., 161, pp. 367-374; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol., 28, pp. 298-303; Whitmire, J.K., Asano, M.S., Murali-Krishna, K., Suresh, M., Ahmed, R., Long-term CD4 Th1 and Th2 memory following acute lymphocytic choriomeningitis virus infection (1998) J. Virol., 72, pp. 8281-8288; Wu, G., Dandekar, A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286; Wu, G.F., Perlman, S., Macrophage infiltration, but not apoptosis, is correlated with immune-mediated demyelination following murine infection with a neurotropic coronavirus (1999) J. Virol., 73, pp. 8771-8780; Xue, S., Perlman, S., Antigen specificity of CD4 T cell response in the central nervous system of mice infected with mouse hepatitis virus (1997) Virology, 238, pp. 68-78; Xue, S., Sun, N., Van Rooijen, N., Perlman, S., Depletion of blood-borne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus (1999) J. Virol., 73, pp. 6327-6334","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"11222733","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035124174
"Maeda J., Repass J.F., Maeda A., Makino S.","23135329700;57186535600;7201779383;7403067550;","Membrane topology of coronavirus E protein",2001,"Virology","281","2",,"163","169",,47,"10.1006/viro.2001.0818","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035866660&doi=10.1006%2fviro.2001.0818&partnerID=40&md5=4543d8f405f5aeacdb829e44ed846565","Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, United States","Maeda, J., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, United States; Repass, J.F., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, United States; Maeda, A., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, United States; Makino, S., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, United States","Coronavirus small envelope protein E has two known biological functions: it plays a pivotal role in virus envelope formation, and the murine coronavirus E protein induces apoptosis in E protein-expressing cultured cells. The E protein is an integral membrane protein. Its C-terminal region extends cytoplasmically in the infected cell and in the virion toward the interior. The N-terminal two-thirds of the E protein is hydrophobic and lies buried within the membrane, but its orientation in the lipid membrane is not known. Immunofluorescent analyses of cells expressing biologically active murine coronavirus E protein with a hydrophilic short epitope tag at the N-terminus showed that the epitope tag was exposed cytoplasmically. Immunoprecipitation analyses of the purified microsomal membrane vesicles that contain the same tagged E protein revealed the N-terminal epitope tag outside the microsomal membrane vesicles. These analyses demonstrated that the epitope tag at the N-terminus of the E protein was exposed cytoplasmically. Our data were consistent with an E protein topology model, in which the N-terminal two-thirds of the transmembrane domain spans the lipid bilayer twice, exposing the C-terminal region to the cytoplasm or virion interior. © 2001 Academic Press.",,"epitope; virus envelope protein; amino terminal sequence; article; carboxy terminal sequence; Coronavirus; hydrophobicity; immunofluorescence; immunoprecipitation; membrane structure; microsome membrane; nonhuman; priority journal; protein structure; Coronavirus; Murinae; Murine hepatitis virus","An, S., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Bos, E.C., Luytjes, W., Van der Meulen, H.V., Koerten, H.K., Spaan, W.J., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Corse, E., Machamer, C.E., Infectious bronchitis virus E protein is targeted to the Golgi complex and directs release of virus-like particles (2000) J. Virol., 74, pp. 4319-4326; David-Ferreira, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) J. Cell Biol., 24, pp. 57-78; De Haan, C.A., Roestenberg, P., De Wit, M., De Vries, A.A., Nilsson, T., Vennema, H., Rottier, P.J., Structural requirements for O-glycosylation of the mouse hepatitis virus membrane protein (1998) J. Biol. Chem., 273, pp. 29905-29914; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirm a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Godet, M., L'Haridon, R., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3c protein with the virion envelope (1991) Virology, 185, pp. 911-917; Maeda, J., Maeda, A., Makino, S., Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells (1999) Virology, 263, pp. 265-272; Narayanan, K., Maeda, A., Maeda, J., Makino, S., Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells (2000) J. Virol., 74, pp. 8127-8134; Plutner, H., Davidson, H.W., Saraste, J., Balch, W.E., Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: Role of the P58 containing compartment (1992) J. Cell Biol., 119, pp. 1097-1116; Raamsman, M.J., Locker, J.K., De Hooge, A., De Vries, A.A., Griffiths, G., Vennema, H., Rottier, P.J., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Rottier, P., Brandenburg, D., Armstrong, J., Van der Zeijst, B., Warren, G., Assembly in vitro of a spanning membrane protein of the endoplasmic reticulum: The E1 glycoprotein of coronavirus mouse hepatitis virus A59 (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 1421-1425; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Tung, F.Y., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J, 15, pp. 2020-2028; Yokomori, K., La Monica, N., Makino, S., Shieh, C.K., Lai, M.M., Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus (1989) Virology, 173, pp. 683-691; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Makino, S.; Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555, United States; email: shmakino@utmb.edu",,"Academic Press Inc.",00426822,,VIRLA,"11277690","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0035866660
"Naylor M.J., Harrison G.A., Monckton R.P., McOrist S., Lehrbach P.R., Deane E.M.","7103407832;35560324800;6603011612;57213024418;6603728862;7006255983;","Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterization of a new Australian isolate",2001,"Journal of Clinical Microbiology","39","3",,"1036","1041",,29,"10.1128/JCM.39.3.1036-1041.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035094478&doi=10.1128%2fJCM.39.3.1036-1041.2001&partnerID=40&md5=d9bd545b3721ed046517d3bd19caa40f","Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia","Naylor, M.J., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; Harrison, G.A., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; Monckton, R.P., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; McOrist, S., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; Lehrbach, P.R., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; Deane, E.M., Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia","A nested PCR (nPCR) assay for the detection of canine coronavirus (CCV) in fecal samples is described. The target sequence for the assay was a 514-bp fragment within the spike (S) glycoprotein gene. The sensitivity of the assay is extremely high, detecting as little as 25 50% tissue culture infective doses per g of unprocessed feces. A clinical trial using dogs challenged orally with CCV SA4 and CCV NVSL was used to compare viral isolation and the nPCR assay as detection techniques over a 2-week period of infection. Virus isolation detected CCV shedding from day 4 to 9 postchallenge, while the nPCR assay detected CCV shedding from day 4 to 13 postchallenge. Cloning and sequencing of the nPCR assay product enabled investigation of the evolutionary relationships between strains within the S gene. The simple and rapid procedure described here makes this assay an ideal alternative technique to electron microscopy and viral isolation in cell culture for detection of CCV shedding in feces. The described assay also provides a method of identifying new strains of CCV without the complicated and time-consuming practice of raising antibodies to individual strains. This is illustrated by the identification, for the first time, of an Australian isolate of CCV (UWSMN-1).",,"glycoprotein; amino acid sequence; animal cell; animal experiment; animal model; article; Australia; controlled study; Coronavirus; feces; gene amplification; molecular cloning; nonhuman; nucleotide sequence; phylogeny; polymerase chain reaction; priority journal; sequence analysis; virus characterization; virus isolation; virus shedding; Amino Acid Sequence; Animals; Australia; Base Sequence; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Feces; Gastroenteritis; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Polymerase Chain Reaction; Sequence Analysis, DNA; Viral Envelope Proteins; Animalia; Canine coronavirus; Canis familiaris; Coronavirus; RNA viruses","Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet. Med. Small Anim. Clin., 83, pp. 360-366; Binn, L.N., Lazar, E., Keenan, K.P., Huxsoll, D., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1975) Proc. Annu. Meet. U. S. Anim. Health Assoc., 78, pp. 359-366; Carmichael, L.E., Infectious canine enteritis caused by corona-like virus: Current status and request for information (1978) Baker Inst. Lab. Report., 9. , Series 2; Crandell, R.A., Fabricant, C.G., Nelson Rees, W.A., Development, characterisation, and viral susceptibility of a feline (Felis catus) renal cell line (CRFK) (1973) In Vitro, 9, pp. 176-185; DeGroot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , S. G. Siddell (ed.), Plenum Press, New York, N.Y; Finlaison, D.S., Faceal viruses of dogs - An electron microscope study (1995) Vet. Microbiol., 46, pp. 295-305; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol., 35, pp. 673-675; Gaskell, R.M., Gaskell, C.J., Dennis, D.E., Wooldbridge, M.J.A., Efficacy of an inactivated feline calicivirus (FCV) vaccine against challenge with United Kingdom strains and its interaction with the FCV carrier state (1982) Res. Vet. Sci., 32, pp. 23-26; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains and 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Jiang, X., Wang, J., Graham, D.Y., Estes, M.K., Detection of Norwalk virus in stool by polymerase chain reaction (1992) J. Clin. Microbiol., 30, pp. 2529-2534; Kokubu, T., Taharaguchi, S., Katayama, S., Hatano, M., Takahashi, T., Iwamoto, K., Masubuchi, K., Inaba, Y., Nucleotide sequence of the spike protein of canine coronavirus strain 5821 (1998) J. Jpn. Vet. Med. Assoc., 51, pp. 251-255; Lai, M.M.C., Baric, R.C., Makino, S., Keck, J.G., Engbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronavirus (1985) J. Virol., 56, pp. 449-456; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronavirus (1986) J. Virol., 57, pp. 729-739; Marshall, J.A., Healy, D.S., Studdert, M.J., Scott, P.C., Kennett, M.L., Ward, B.K., Gust, I.D., Viruses and virus-like particles in the faeces of dogs with and without diarrhoea (1984) Aust. Vet. J., 61, pp. 33-38; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro-neutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Naylor, M.J., Monckton, R.P., Lehrbach, P.R., Deane, E.M., Canine coronavirus in Austalian dogs (2001) Aust. Vet. J., 79, pp. 27-30; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) J. Virol. Methods, 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested PCR (2000) J. Virol. Methods, 84, pp. 91-94; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H.A., UytdeHaag, F.G.C.M., Osterhaus, A.D.M.E., The use of enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in The Netherlands (1991) Vet. Microbiol., 26, pp. 25-40; Saif, L.J., Coronavirus immunogens (1993) Vet. Microbiol., 37, pp. 285-297; Schnagl, R.D., Holmes, I.H., Coronavirus-like particles in stools from dogs, from some country areas of Australia (1978) Vet. Rec., 102, pp. 528-529; Schunck, B., Kraft, W., Truyen, U., A simple touch-down polymerase chain reaction for the detection of canine parvovirus and feline panleukopenia virus in feces (1995) J. Virol. Methods, 55, pp. 427-433; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Prevalence of antibodies to four major canine viral disease in dogs in a Liverpool hospital population (1991) J. Small Anim. Pract., 32, pp. 175-179; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Vet. Rec., 132, pp. 7-11; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Tuchiya, K., Horimoto, T., Azetaka, M., Takahashi, E., Konishi, S., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet. Microbiol., 26, pp. 41-51; Uwatoka, K., Sunairi, M., Nakajima, M., Yamaura, K., Rapid method utilizing the polymerase chain reaction for detection of canine parvovirus in feces of diarrheic dogs (1995) Vet. Microbiol., 43, pp. 315-323; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Res., 61, pp. 145-152; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Naylor, M.J.; Cancer Research Program, Garvan Inst. of Medical Research, St. Vincent's Hospital, Sydney, NSW 2010, Australia; email: m.naylor@garvan.unsw.edu.au",,,00951137,,JCMID,"11230424","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0035094478
"Yoo D., Deregt D.","7103242554;7004513974;","A single amino acid change within antigenic domain II of the spike protein of bovine coronavirus confers resistance to virus neutralization",2001,"Clinical and Diagnostic Laboratory Immunology","8","2",,"297","302",,44,"10.1128/CDLI.8.2.297-302.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035099329&doi=10.1128%2fCDLI.8.2.297-302.2001&partnerID=40&md5=d094e81fa90c448ea3022755238b1cae","Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","Yoo, D., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Deregt, D., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","The spike glycoprotein is a major neutralizing antigen of bovine coronavirus (BCV). Conformational neutralizing epitopes of group A and group B monoclonal antibodies (MAbs) have previously been mapped to two domains at amino acids 351 to 403 (domain I) and amino acids 517 to 621 (domain II). To further map antigenic sites, neutralization escape mutants of BCV were selected with a group A MAb which has both in vitro and in vivo virus-neutralizing ability. The escape mutants were demonstrated to be neutralization resistant to the selecting group A Mab and remained sensitive to neutralization by a group B MAb. In radioimmunoprecipitation assays, the spike proteins of neutralization escape mutants were shown to have lost their reactivities with the selecting group A MAb. Sequence analysis of the spike protein genes of the escape mutants identified a single nucleotide substitution of C to T at position 1583, resulting in the change of alanine to valine at amino acid position 528 (A528V). The mutation occurs in domain II and in a location which corresponds to the hypervariable region of the spike protein of the coronavirus mouse hepatitis virus. Experimental introduction of the A528V mutation into the wild-type spike protein resulted in the loss of MAb binding of the mutant protein, confirming that the single point mutation was responsible for the escape of BCV from immunological selective pressure.",,"amino acid; epitope; monoclonal antibody; mutant protein; neutralizing antibody; spike protein; unclassified drug; amino acid substitution; article; cattle; Coronavirus; gene mutation; genetic resistance; nonhuman; nucleotide sequence; priority journal; protein domain; radioimmunoprecipitation; sequence analysis; virus mutant; virus neutralization; Amino Acid Sequence; Amino Acid Substitution; Animals; Antibodies, Monoclonal; Cattle; Cell Line; Epitopes; Hela Cells; Humans; Kidney; Membrane Glycoproteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Neutralization Tests; Protein Structure, Tertiary; Viral Envelope Proteins","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Cavanagh, D., Davis, P.J., Coronavirus IBV: Removal of spike glycoprotein S1 by urea abolishes infectivity and hemagglutination but not attachment to cells (1986) J. Gen. Virol., 67, pp. 1443-1448; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5kb) of respiratory coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Mono clonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Dayhoff, M., Schwartz, R.M., Orcutt, B.C., A model of evolutionary change in proteins (1978) Atlas of protein sequence and structure, 5 (SUPPL. 3), pp. 345-352. , M. Dayhoff (ed.). National Biomedical Research Foundation, Silver Spring. Md; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation and cultivation in continuous cell lines (1980) Am. J. Vet. Res., 41, pp. 30-38; Deregt, D., Gilford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Parker, M.D., Cox, G.J., Babiuk, L.A., Mapping of neutralizing epitopes to fragments of bovine coronavirus E2 protein by proteolysis of antigen-antibody complexes (1989) J. Gen. Virol., 70, pp. 647-658; Deregt, D., Masri, S.A., Cho, H.J., Bielefeldt-Ohmann, H., Monoclonal antibodies to the p80/125 and gp53 proteins of bovine viral diarrhea virus: Their potential use as diagnostic reagents (1990) Can. J. Vet. Res., 54, pp. 343-348; Espinasse, J., Viso, M., Laval, A., Savey, M., Le Layec, C., Blot, J.P., L'Haridon, R., Cohen, J., Winter dysentery: A coronavirus-like agent in the faeces of beef and dairy cattle with diarrhoea (1982) Vet. Rec., 110, p. 385; Furest, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Hasoksuz, M., Lathrop, S.L., Gadfield, K.L., Saif, L.J., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am. J. Vet. Res., 60, pp. 1227-1233; Hogue, B.G., King, B., Brian, D.A., Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59 (1984) J. 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Virol., 71, pp. 9024-9031; Saif, L.D., Redman, R.J., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet. Rec., 123, pp. 300-301; Schultz, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Stair, E.L., Rhodes, M.B., White, R.G., Mebus, C.A., Neonatal calf diarrhea: Purification and electron microscopy of a coronavirus-like agent (1972) Am. J. Vet. Res., 33, pp. 1147-1156; St. Cyr-Coats, K.S., Storz, J., Hussain, K.A., Schnorr, K.L., Structural proteins of bovine coronavirus strain L9: Effects of the host cell and trypsin treatment (1988) Arch. Virol., 103, pp. 35-45; Storz, J., Kaluza, G., Niemann, H., Rott, R., On enteropathogenic bovine coronavirus (1981) Adv. Exp. Med. 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Virol., 65, pp. 3369-3373; Yoo, D., Parker, M.D., Song, J., Cox, G.J., Deregt, D., Babiuk, L.A., Structural analysis of the conformational domains involved in neutralization of bovine coronavirus using deletion mutants of the spike glycoprotein S1 subunit expressed by recombinant baculoviruses (1991) Virology, 183, pp. 91-98; Yoo, D., Parker, M.D., Babiuk, L.A., Analysis of the S spike (peplomer) glycoprotein of bovine coronavirus synthesized in insect cells (1990) Virology, 179, pp. 121-128; Yoo, D., Parker, M.D., Babiuk, L.A., The S2 subunit glycoprotein of bovine coronavirus mediates membrane fusion in insect cells (1991) Virology, 180, pp. 395-399; Yoo, D., Pei, Y., Christie, N., Cooper, M., Primary structure of the sialodacryoadenitis virus genome: Sequence of the structural-protein region and its application for differential diagnosis (2000) Clin. Diagn. Lab. Immunol., 7, pp. 568-573; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Yoo, D.; Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; email: dyoo@uoguelph.ca",,,1071412X,,CDIME,"11238212","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0035099329
"Lin X., O'Reilly K.L., Burrell M.L., Storz J.","36768282000;7103313844;7006801008;7006694594;","Infectivity-neutralizing and hemagglutinin-inhibiting antibody responses to respiratory coronavirus infections of cattle in pathogenesis of shipping fever pneumonia",2001,"Clinical and Diagnostic Laboratory Immunology","8","2",,"357","362",,16,"10.1128/CDLI.8.2.357-362.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035102717&doi=10.1128%2fCDLI.8.2.357-362.2001&partnerID=40&md5=cfad40c291e37d54dfcc37128b9386d9","Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States","Lin, X., Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States; O'Reilly, K.L., Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States; Burrell, M.L., Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States; Storz, J., Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States","Respiratory bovine coronaviruses (RBCV) emerged as an infectious agent most frequently isolated from respiratory tract samples of cattle with acute respiratory tract diseases. Infectivity-neutralizing (IN) and hemagglutinin-inhibiting (HAI) antibodies induced by RBCV infections were monitored in sequential serum samples collected from cattle during a naturally evolving and experimentally monitored epizootic of shipping fever pneumonia (SFP). Cattle nasally shedding RBCV at the beginning of the epizootic started with low levels of serum IN and HAI antibodies. An increase in serum IN antibody after day 7 led to reduction of virus shedding in nasal secretions by the majority of the cattle between days 7 and 14. A substantial rise in the serum HAI antibody was observed during the initial phase among the sick but not the clinically normal cattle which were infected with RBCV. The RBCV isolation-positive cattle that developed fatal SFP had minimal serum IN and HAI antibodies during the course of disease development. Cattle that remained negative in RBCV isolation tests entered this epizootic with high levels of serum IN and HAI antibodies, which dramatically increased during the next two weeks. Protection against SFP was apparently associated with significantly higher levels of serum IN antibodies at the beginning of the epizootic. The RBCV-neutralizing activity is associated with serum immunoglobulin G (IgG), particularly the IgG2 subclass, while RBCV-specific HAI antibody is related to both serum IgG and IgM fractions.",,"hemagglutination inhibiting antibody; immunoglobulin G1; immunoglobulin G2; immunoglobulin M; infectivity neutralizing antibody; neutralizing antibody; unclassified drug; antibody titer; article; cattle disease; Coronavirus; epizootiology; humoral immunity; nonhuman; nose secretion; priority journal; respiratory tract infection; virus infection; virus infectivity; virus shedding; Animals; Antibodies, Viral; Cattle; Coronavirus Infections; Coronavirus, Bovine; Hemagglutination Tests; Immunoglobulin G; Immunoglobulin M; Neutralization Tests; Pneumonia, Viral","Chouljenko, V.N., Kousoulas, K.G., Lin, X.Q., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 149, pp. 51-70; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J. Virol., 66, pp. 6690-6705; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Heckert, R.A., Saif, L.J., Hoblet, K.H., Agnes, A.G., A longitudinal study of bovine coronavirus enteric and respiratory infections in dairy calves in two herds in Ohio (1990) Vet. Microbiol., 22, pp. 187-201; Heckert, R.A., Saif, L.J., Mengel, J.P., Myers, G.W., Isotype-specific antibody responses to bovine coronavirus structural proteins in serum, feces, and mucosal secretions from experimentally challenged colostrum-deprived calves (1991) Am. J. Vet. Res., 52, pp. 692-699; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Jacobse-Geels, H., Daha, M.R., Horzinek, M., Antibody, immune complex, and complement activity fluctuations in kittens with experimentally induced feline infectious peritonitis (1982) Am. J. Vet. Res., 43, pp. 666-670; Lai, M.M.C., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; LeJan, C., Asso, J., The local and systemic immune response of calves following experimental infection with 1BR virus (1980), pp. 677-692. , J. E. Butler (ed.). The ruminant immune system. Plenum Press, New York, N.Y; Lin, X.Q., Chouljenko, V.N., Kousoulas, K.G., Storz, J., Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses (2000) J. Med. Microbiol., 49, pp. 1119-1127; Lin, X.Q., O'Reilly, K.L., Storz, J., Purdy, C.W., Loan, R.W., Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis (2000) Arch. Virol., 145, pp. 2335-2349; Mebus, C.A., Reovirus and coronavirus infections (1980) Bovine medicine and surgery, pp. 127-138. , H. E. Amstutz (ed.). American Veterinary Publications, Inc., Santa Barbara, Calif; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a corona-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Olsen, C.W., Corapi, W.V., Jacobson, R.H., Simkins, R.A., Saif, L.J., Scott, F.W., Identification of antigenic sites mediating antibody-dependent enhancement of feline infectious peritonitis virus infectivity (1993) J. Gen. Virol., 74, pp. 745-749; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Parker, M.D., Yoo, D., Babiuk, L.A., Expression and secretion of bovine coronavirus hemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses (1990) J. Virol., 64, pp. 1625-1629; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet. Rec., 123, pp. 300-301; Schmidt, O.W., Kenny, G.E., Polypeptides and functions of antigens from human coronaviruses 229E and OC43 (1982) Infect. Immun., 32, pp. 1000-1006; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetyl-neuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J. Gen. Virol., 74, pp. 901-906; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., Isolated HE-protein from haemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Storz, J., Lin, X.Q., Purdy, C.W., Chouljenko, V.N., Kousoulas, K.G., Enright, F.M., Gilmore, W.C., Loan, R.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans criteria for causation (2000) J. Clin. Microbiol., 38, pp. 3291-3298; Storz, J., Purdy, C.W., Lin, X.Q., Burrell, M., Truax, R.E., Briggs, R.E., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp from cattle involved in two natural outbreaks of shipping fever (2000) J. Am. Vet. Med. Assoc., 216, pp. 1599-1604; Storz, J., Respiratory disease of cattle associated with coronavirus infections (1999) Current veterinary therapy: food animal practice 4, pp. 291-293. , J. L. Howard and R. A. Smith (ed.). The W. B. Saunders Co., Philadelphia, Pa; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J. Am. Vet. Med. Assoc., 208, pp. 1452-1455; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch. Virol., 125, pp. 193-204; Storz, J., Herrler, G., Snodgrass, D.R., Hussain, K.A., Zhang, X.M., Clark, M.A., Rott, R., Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine coronavirus (1991) J. Gen. Virol., 72, pp. 2817-2820; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med. Microbiol. Immun., 169, pp. 169-178; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect. Immun., 31, pp. 1214-1222; Storz, J., Rott, R., Über die verbreitung der coronavirusinfektion bei rindern in ausgewählten gebieten Deutschlands: Antikörpernachweis durch mikroimmundiffusion und neutralisation (1980) Dtsch. Tierärztl. Wochenschr., 87, pp. 252-254; Yates, W.D.G., A review of infectious bovine rhinotracheitis, shipping fever pneumonia and viral-bacterial synergism in respiratory disease of cattle (1982) Can. J. Comp. Med., 46, pp. 225-263; Zhang, X.M., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and function comparison between virulent and avirulent strains (1991) Virology, 185, pp. 847-852","Storz, J.; Dept. Vet. Microbiol. and Parasitol., LA State Univ. Sch. of Vet. Medicine, Baton Rouge, LA 70803, United States; email: JStorz@vetmed.lsu.edu",,,1071412X,,CDIME,"11238222","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0035102717
"Cavanagh D.","26642890500;","A nomenclature for avian coronavirus isolates and the question of species status",2001,"Avian Pathology","30","2",,"109","115",,58,"10.1080/03079450120044506","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035304891&doi=10.1080%2f03079450120044506&partnerID=40&md5=89797fb63405ca5fdf3f666fcfba2200","Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Currently, there is no agreed naming system for isolates of infectious bronchitis virus (IBV), whose host is the domestic fowl (Gallus gallus domesticus). A uniform, informative system for naming IBV isolates would be very helpful. Furthermore, the desirability of a single naming system has become more important with the recent discoveries that coronaviruses with genome organizations and gene sequences very similar to those of IBV have been isolated from turkeys (Meleagris gallopavo) and pheasants (Phasianus colchicus). To date, no genetic features have been found that are unique to turkey isolates and to pheasant isolates that would permit unequivocal differentiation from IBVs. Should the avian coronaviruses from turkeys, pheasants and other birds each be considered as distinct coronavirus species? Or should avian coronaviruses that have gene sequences similar to those of IBV be treated as host-range variants of IBV or, more objectively, as host-range variants of a species that might be called avian coronavirus (ACoV)? Clearly, the topic of avian coronavirus species differentiation requires debate. For the moment, a naming system for avian coronavirus isolates is overdue. Increasingly, papers will include data of coronaviruses isolated from more than one species of bird. It is desirable to have a nomenclature for avian coronaviruses that indicates the host species of origin. Furthermore, it would be helpful if the name of an isolate included the country/region of origin, an isolate number and the year of isolation. The names of avian paramyxovirus (APMV) and avian influenza virus (AIV) isolates have long since contained this information; I suggest that we adopt a similar convention for isolates of avian coronaviruses. For example, the D274 isolate of IBV could be named chicken/Netherlands/D274/78. Representatives of avian coronaviruses from turkey and pheasant would include turkey/United States(Nc)/NC95/95 and pheasant/UK/750/83. Two upper case letters would be used to denote country of isolation, whereas one upper and one lower case letter would be used to indicate state or province, e.g. Nc, North Carolina. The full-length names could be abbreviated, when desired, similar to the convention used for AIV isolates, e.g. chNL78, tyUS(Nc)95 and phUK83. If the serotype of an isolate has been clearly established, this might be included in the name at end, like the serotype designation of AIVs, e.g. chicken/China/NRZ/91 (Mass.) for the Chinese isolate of the Massachusetts serotype. This suggested naming system for isolates is essentially neutral with regard to whether viruses from different bird species should be considered as different coronavirus species or simply as variants of just one avian coronavirus species. In my opinion an informative nomenclature for avian coronavirus isolates is required now, to improve communication, and need not be delayed until a decision on the definition of coronavirus species has been made.",,"avian coronavirus; avian influenza virus; avian paramyxovirus; gene sequence; genetic strain; genome organization; infectious bronchitis virus; Netherlands; serotype; species difference; United Kingdom; United States","Adams, N.R., Hofstad, M.S., Isolation of transmissible gastroenteritis agent of turkeys in avian embryos (1971) Avian Diseases, 15, pp. 426-433; Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathology, 25, pp. 817-836; Albassam, M.A., Winterfield, R.W., Thacker, H.L., Comparison of the nephropathogenicity of four strains of infectious bronchitis virus (1986) Avian Diseases, 30, pp. 468-476; Alexander, D.J., Newcastle disease and other avian Paramyxoviridae infections (1997) Diseases of Poultry 10th Edn, pp. 541-569. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds.), Ames: Iowa State University Press; Banks, J., Speidel, B.C., Harris, P.A., Alexander, D.J., Phylogenetic analysis of influenza A viruses of H9 haemagglutinin subtype (2000) Avian Pathlogy, 29, pp. 353-359; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome ('spiking mortality') of turkeys (1997) Diseases of Poultry 10th Edn, pp. 1025-1031. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds.), Ames: Iowa State University Press; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Brown, T.P., Howell, D.R., Garcia, A.P., Adult cattle as inapparent carriers of spiking mortality of turkeys (1996) Proceedings of the 133rd Annual Meeting of the American Veterinary Medical Association, pp. 118-121. , Louisville, KY, USA; Capua, I., Cough, R.E., Mancini, M., Casaccia, C., Weiss, C., A 'novel' infectious bronchitis strain infecting broiler chickens in italy (1994) Journal of Veterinary Medicine Series B, 41, pp. 83-89; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Co-circulation of four types of infectious bronchitis virus (793/B, 624/I, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 587-592; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of Poultry 10th Edn, pp. 511-526. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds.), Ames: Iowa State University Press; Cavanagh, D., Brian, D.A., Brinton, M.A., Enjuanes, L., Holmes, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Coronaviridae (1995) Virus Taxonomy, Sixth Report of the International Committee on Taxonomy of Viruses, pp. 407-411. , F.A. Murphy, C.M. Fauquet, D.H.L. Bishop, S.A. Ghabrial, A.W. Jarvis, G.P. Martelli, M.A. Mayo & M.D. Summers (Eds.), Wien: Spinger-Verlag; Cavanagh, D., Mawditt, K., Britton, P., Naylor, C.J., Longitudinal field studies of infectious bronchitis virus and avian pneumovirus in broilers using type-specific polymerase chain reactions (1999) Avian Pathology, 28, pp. 593-605; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., A coronavirus from turkey in Britain that is genetically close to infectious bronchitis virus of chickens (2001) Avian Pathology, 30. , in press; Cavanagh, D., Mawditt, K., Welchman, D., Britton, P., Gough, R.E., (2001) Coronaviruses from Pheasants (Phasianus Colchicus) that are Genetically Close to Infectious Bronchitis Virus of Chickens, , Submitted for publication; Cowen, B.S., Hitchner, S.B., PH stability studies with avian infectious bronchitis virus (Coronavirus) (1975) Journal of Virology, 15, pp. 430-432; Cumming, R.B., Infectious avian nephrosis (uraemia) in Australia (1963) Australian Veterinary Journal, 39, pp. 145-147; Darbyshire, J.H., Cook, J.K.A., Peters, R.W., Comparative growth kinetic studies on avian infectious bronchitis virus in different systems (1975) Journal of Comparative Pathology, 85, pp. 623-630; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) Journal of Virology, 64, pp. 3112-3118; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) American Journal of Veterinary Research, 35, pp. 1549-1552; De Wit, J.J., Detection of infectious bronchitis virus (2000) Avian Pathology, 29, pp. 71-93; Dhinaker Raj, G., Jones, R.C., Infectious bronchitis virus: Immunopathogenesis of infection in the chicken (1997) Avian Pathology, 26, pp. 677-706; Easterday, B.C., Hinshaw, V.S., Halvorson, D.A., Influenza (1997) Diseases of Poultry 10th Edn, pp. 583-605. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds), Ames: Iowa State University Press; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, Seventh Report of the International Committee on Taxonomy of Viruses, pp. 835-849. , M.H.V. Van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle & R.B. Wickner (Eds.), New York: Academic Press; Gelb J., Jr., Keeler C.L., Jr., Nix, W.A., Rosenberger, J.K., Cloud, S.S., Antigenic and S-1 genomic characterization of the Delaware variant serotype of infectious bronchitis virus (1997) Avian Diseases, 41, pp. 661-669; Gohm, D.S., Thür, B., Hofmann, M.A., Detection of Newcastle disease virus in organs and faeces of experimentally infected chickens using RT-PCR (2000) Avian Pathology, 29, pp. 143-152; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis virus from pheasants (1996) Veterinary Record, 138, pp. 208-209; Guy, J.S., Barnes, J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis-and mortality syndrome-affected turkeys (1997) Avian Diseases, 47, pp. 583-590; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses (2000) Avian Pathology, 29, pp. 206-212; Heckert, R.A., McIsacc, M., Chan, M., Zhou, E.-M., Experimental infection of emus (Dromaiius novaehollandiae) with avian influenza viruses of varying virulence: Clinical signs, virus shedding and serology (1999) Avian Pathology, 28, pp. 13-16; Ismail, M.M., Cho, K.O., Ward, L.A., Saif, L.J., Saif, Y.M., Experimental bovine coronavirus in turkey poults and young chickens (2001) Avian Diseases, 45. , in press; Jones, R.C., Ambali, A.G., Re-excretion of an enterotropic infectious bronchitis virus by hens at point of lay after experimental infection at day old (1987) The Veterinary Record, 120, pp. 617-620; Keeler C.L., Jr., Reed, K.L., Nix, W.A., Gelb J., Jr., Serotype identification of avian infectious bronchitis virus by RT-PCR of the peplomer (S-1) gene (1998) Avian Diseases, 42, pp. 275-284; Kwon, H.M., Jackwood, M.W., Gelb J., Jr., Differentiation of infectious bronchitis virus serotypes using polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Diseases, 37, pp. 194-202; Lambrechts, C., Pensaert, M., Ducatelle, R., Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus (1993) Avian Pathology, 22, pp. 577-590; Lister, S.A., Beer, J.V., Gough, R.E., Holmes, R.G., Jones, J.M.W., Orton, R.G., Outbreaks of nephritis in pheasants (Phasianus colchicus) with a possible coronavirus aetiology (1985) Veterinary Record, 117, pp. 612-613; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Diseases, 44, pp. 498-506; Meulemans, G., Carlier, M.C., Gonze, M., Petit, P., Vandenbroeck, M., Incidence, characterization, and prophylaxis of nephropathogenic avian infectious bronchitis viruses (1987) Veterinary Record, 120, pp. 205-206; Pennycott, T.W., Causes of mortality and culling in adult pheasants (2000) Veterinary Record, 146, pp. 273-278; Pensaert, M., Lambrechts, C., Vaccination of chickens against a Belgian nephropathogenic strain of infectious bronchitis virus B1648 using attenuated homologous and heterologous strains (1994) Avian Pathology, 23, pp. 631-641; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from eleven coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Research, 60, pp. 181-189; Song, C.-S., Lee, Y.-J., Kim, J.-H., Sung, H.-W., Lee, C.-W., Izumiya, Y., Miyazawa, T., Mikami, T., Epidemiological classification of infectious bronchitis virus isolated in Korea between 1986 and 1997 (1998) Avian Pathology, 27, pp. 409-416; Van Regenmortel, M.H.V., Introduction to the species concept in virus taxonomy (2000) Virus Taxonomy, Seventh Report of the International Committee on Taxonomy of Viruses, pp. 835-849. , M.H.V. Van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle & R.B. Wickner (Eds.), New York: Academic Press; Van Regenmortel, M.H.V., Bishop, D.H.L., Fauquet, C.M., Mayo, M.A., Maniloff, J., Calisher, C.H., Guidelines to the demarcation of virus species (1997) Archives of Virology, 142, pp. 1505-1518; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) Journal of General Virology, 72, pp. 1659-1666; Verbeek, A., Dea, S., Tijssen, P., Genomic relationship between turkey and bovine enteric coronaviruses identified by hybridization with BCV or TCOV specific cDNA probes (1991) Archives of Virology, 121, pp. 199-211; Weisman, Y., Aronovici, A., Malkinson, M., Prevalence of IBV antibodies in turkey breeding flocks in Israel (1987) The Veterinary Record, 120, p. 494; Wu, Q., Yang, Q.W., Fu, C., Zhao, X.Y., Ignjatovich, J., (1998) Avian Pathology, 27, pp. 578-585","Cavanagh, D.; Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; email: dave.cavanagh@bbsrc.ac.uk",,,03079457,,AVPAD,,"English","Avian Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0035304891
"Freymuth F., Vabret A., Gouarin S., Petitjean J., Campet M.","7103410207;7003959575;56107903900;7006379234;6506923168;","Epidemiology of respiratory virus infections [Epidémiologie des infections virales respiratoires]",2001,"Allergie et Immunologie","33","2",,"66","69",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035076102&partnerID=40&md5=90b02adb94fe1d149222d86487d05b2a","Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France","Freymuth, F., Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France; Vabret, A., Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France; Gouarin, S., Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France; Petitjean, J., Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France; Campet, M., Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France","Respiratory viral infections are very common in young children. They sometimes occur as primary infections (and sometimes re-infections) by influenza and parainfluenza virus, respiratory syncytial virus (VRS), adenovirus, rhinovirus and coronavirus. The clinical pictures are very varied and without strict clinico-virological correlation. In adults the role of the site (frail lung, aged persons) and the type of virus play an important part. Many viral infections develop in an epidemiological way (influenza, VRS bronchiolitis, rhinovirus infections...) and several epidemics by different viruses overlap from September-October to March-April making it very difficult to decide the precise cause. Epidemics are followed thanks to networks of medical practitioners (GROG, SENTINELLE...) and by data from hospitalised patients, but precise identification of epidemic viruses is only possible and validated by virological analysis of samples taken from patients.","Adenovirus; Coronavirus; Epidemiology; Influenza virus; Respiratory syncytial virus; Rhinovirus","Adenovirus; clinical feature; conference paper; Coronavirus; epidemic; human; Influenza virus; Parainfluenza virus; Respiratory syncytial pneumovirus; respiratory tract infection; Rhinovirus; virus infection; Adenoviridae Infections; Adenoviruses, Human; Adolescent; Adult; Aerosols; Age Factors; Child; Child, Preschool; Coronavirus Infections; Disease Outbreaks; Disease Susceptibility; Humans; Infant; Influenza, Human; Population Surveillance; Respiratory Syncytial Virus Infections; Respiratory Tract Infections; Seasons; Virus Diseases","Agius, G., Dindinaud, G., Biggar, R.-J., Peyre, R., Vaillant, V., Ranger, S., An epidemic of respiratory syncytial virus in elderly peaple: Clinical and serological findings (1990) J. Med. Virol., 30, pp. 117-127; Brouard, J., Ribet, J., Petitjean, J., Freymuth, F., Duhamel, J.-F., Infections ò virus influenza A chez l'enfant. Spectre clinique et comparoison ovec l'otteinte par le virus respiratoire syncytial durant l'hiver 1989-1990 (1992) Arch. Fr. Pediotr., 49, pp. 693-697; Chomel, J.-J., Pardon, D., Thouvenot, D., Allord, J.-P., Aymard, M., Comparison between three rapid methods for direct diagnosis of influenza and the conventional isolation procedure (1991) Biologicals, 19, pp. 287-292; Duverlie, G., Houbart, L., Visse, B., Chomel, J.-J., Manuguerra, J.-C., Honnoun, C., Orfila, J., A nylon membrane enzyme immunoassay for rapid diagnosis of influenza A infection (1992) J. Virol. Methods, 40, pp. 77-84; Falsey, A., Respiratory syncycial virus infection in older persons (1998) Vaccine, 16, pp. 1775-1778; Freymuth, F., Rapid diagnosis of respiratory syncytial virus infection in children (1980) Lancet, 11, pp. 539-540; Freymuth, E., Quibriac, M., Petitjean, J., Doon, F., Amiel, M.-L., Les virus responsables d'infection respirtoire en pediotrie. Bilon de 3480 ospirations nasales réolisées chez l'enfant en une période de six ans (1987) Ann. Pediotr., 34, pp. 493-501; Freymuth, F., Eugene, G.-A., Valbret, A., Petitjean, J., Gennetay, E., Brouard, J., Duhomel, J.-F., Guillois, B., Detection of respiratory syncytial virus by reverse transcription-PCR and hybridization with o DNA enzyme immunoossay (1995) J. Clin. Microbiol., 33, pp. 3352-3355. , 1996; Erratum J. Clin. Microbiol. 34: 1601; Freymuth, F., Vobret, A., Galateau-Salle, F., Ferey, Eugene, G., Petitjean, J., Gennetoy, E., Guillois, B., Detection of respiratory syncytial virus, parainfluenza virus 3, adenovirus and rhinovirus sequences in respiratory tract of infants by polymerase chain reaction and hybridization (1997) Clin. Diagn. Virol., 8, pp. 31-40; Freymuth, F., Vobret, A., Galoteau, F., Brouard, J., Eugene, G., Petitjean, J., Gennetoy, E., Étiologie et diagnostic des bronchopneumopathies virales (1998) Ann. Biol. Clin., 56, pp. 29-40; Freymuth, F., Vobret, A., Brouard, J., Duhamel, J.-F., Guillois, B., Eugene, G., Petitjean, J., Proust, C., Epidémiologie de l'infection virole et osthme (1998) Rev. Fr. Allergol., 38, pp. 319-325; Freymuth, F., Vabret, A., Brouard, J., Toutain, F., Verdon, R., Petijean, J., Gouarin, S., Guillois, B., Detection of viral Chlamydio pneumonioe, Mycoplasma pneumoniae infections in exacerbations of asthma in children (1999) J. Clin. Virol, 13, pp. 131-139; Freymuth, F., Vabret, A., Petitjean, J., Gouarin, S., Gueudin, M., Campet, M., Diagnostic de deux principales viroses respiratoires épidémiques: La grippe et les infections à virus respiratoire syncytial. Place de la virologie moléculaire Med. Mal. Infect., , sous presse; Gardner, R.-S., McQuillin, J., Application of immunofluorescent antibody technique in the rapid diagnosis of respiratory syncytial virus infection (1968) Br. Med. J., 2, pp. 340-341; Lina, B., Valette, M., Foray, S., Luciani, J., Stagnara, J., See, D.-M., Aymard, M., Surveillance of community-acquired viral infections due ta respiratory viruses in Rhones-Alpes (France) during winter 1994 to 1995 (1996) J. Clin. Microbiol., 34, pp. 3007-3011; Pothier, P., Denoyel, G.-A., Ghim, S., Prudhomme de St Maur, G., Freymuth, F., Use of monaclonal antibodies for rapid detection of influenza virus in nasapharyngeal secretions (1986) Eur. J. Clin. Microbiol., 5, pp. 336-339","Freymuth, F.; Virologie Humaine/Moleculaire Lab., Hôpital Universitaire, Avenue Georges Clemenceau, 14033 Caen, France",,,03979148,,ALGIB,"11339056","French","Allerg. Immunol.",Conference Paper,"Final",,Scopus,2-s2.0-0035076102
"Wieler L.H., Ilieff A., Herbst W., Bauer C., Vieler E., Bauerfeind R., Failing K., Klös H., Wengert D., Baljer G., Zahner H.","7003828429;6504257147;16161781000;7402387375;6603650281;7004142234;7006178405;22944349800;6506062225;7005088999;7007182664;","Prevalence of enteropathogens in suckling and weaned piglets with diarrhoea in Southern Germany",2001,"Journal of Veterinary Medicine, Series B","48","2",,"151","159",,89,"10.1046/j.1439-0450.2001.00431.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035052338&doi=10.1046%2fj.1439-0450.2001.00431.x&partnerID=40&md5=2cf72ec398853c1049a8bbb18d59c3e6","Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany; Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany; Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany; Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany; Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, Berlin, Germany","Wieler, L.H., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, Berlin, Germany; Ilieff, A., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Herbst, W., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Bauer, C., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Vieler, E., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Bauerfeind, R., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Failing, K., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Klös, H., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Wengert, D., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Baljer, G., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany; Zahner, H., Institut für Parasitologie, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Hygiene und Infektionskrankheiten der Tiere, Justus-Liebig-Universität Giessen, D-35392 Giessen, Germany, Institut für Mikrobiologie und Tierseuchen, Freien Universität Berlin, D-10115 Berlin, Germany, Arbeitsgruppe Biomathematik und Datenverarbeitung des Fachbereichs Veterinärmedizin, Justus-Liebig-Universität Giessen, Giessen, Germany, Staatliches Tierärztliches Untersuchungsamt Heidelberg, D-69115 Heidelberg, Germany","Faecal samples from suckling (n = 205) and weaned piglets (n = 82) with diarrhoea from 24 farms in Southern Germany were examined for shedding of important metazoic parasitic, viral and bacterial pathogens using culture, microscopic and electronmicroscopic methods. Escherichia coli isolates were tested further for the enterotoxin genes est-Ia and elt-I by colony blot hybridization. Isospora suis was diagnosed in 26.9 % and Cryptoporidium parvum in 1.4 % of the piglets investigated. The proportion of coronavirus-positive animals was 13.4 % and 4 % were positive for rotavirus. It was found that 17.6 % of the animals were infected with enterotoxigenic E. coli (ETEC; 10.1% ETEC-ST-Ia and 8.6 % ETEC-LT-I, respectively). The occurrence of the pathogens was significantly associated with the age of the animals examined (P < 0.001). Isopora suis was predominantly isolated from suckling piglets (in the second and third week of life), while in weaned piglets (fourth week of life) rotavirus and ETEC were most prevalent. On 22 of the 24 piglet production farms examined at least one of the investigated pathogens was detected. Coronavirus was diagnosed in 66.7 %, I. suis in 62.5 %, rotavirus in 20.8 % and C. parvum in 8.3 % of the farms, These results underline the fact that despite the hygienic, technical and immune preventive efforts during the last years, enteropathogens are still common in German piglet production units.",,"age; Coronavirus; enteropathogen; Escherichia coli enterotoxin; feces analysis; feces; Germany; pathogenesis; piglet; prevalence; Rotavirus; virus infection; Animals; Animals, Suckling; Coronavirus; Cryptosporidium; Diarrhea; DNA Primers; Escherichia coli; Feces; Female; Germany; Isospora; Male; Polymerase Chain Reaction; Prevalence; Rotavirus; Swine; Swine Diseases; Weaning; Animalia; Bacteria (microorganisms); Coronavirus; Cryptosporidium parvum; Escherichia coli; Isopora; Isospora suis; Rotavirus","Baljer, G., Eichhorn, W., Göbel, G., Wolf, M., Bachmann, P.A., Vorkommen und verbreitung wichtiger durchfallerreger bei neugeborenen kälbern in süddeutschland im zeitraum 1984-86 (1987) Tierärztl. Umschau, 42, pp. 56-63; Bergeland, M.E., Henry, S.C., Infectious diarrhoeas of young pigs (1982) Vet. Clin. North Am, Large Anim. Practice, 4, pp. 389-399; Biehl, L.G., Hoefling, D.C., Diagnosis, treatment and prevention of diarrhoea in 7-14 day old pigs (1986) J. Am. Vet. Med, Assoc., 188, pp. 1144-1146; Biermann, U., Herbst, W., Krauss, H., Schliesser, T., Elektronenmikroskopische nachweisrate enteraler viren bei durchfallkrankheiten von hund, katze, kalb, schwein und fohlen im jahre 1988 (1989) Berl. Münch. Tierärztl. Wochenschr., 102, pp. 412-414; Biermann, U., Schmitt, H., Krauss, H., Elektronenmikroskopische virusdiagnostik bei hund, kalb, schwein und fohlen im jahre 1989 (1989) Berl. Münch. Tierärztl. Wochenschr., 104, pp. 117-119; Dixon, W.J., (1993) BMDP Statistical Software Manual, 1-2. , University of California Press, Berkeley, Los Angeles; Driesen, S.J., Carland, P.G., Fahy, V.A., Studies on preweaning diarrhoea (1993) Austr. Vet. J., 70, pp. 259-262; Evans, M.G., Waxler, G.L., Newman, J.P., Prevalence of K88, K99 and 987P pill of Escherichia coli in neonatal pigs with enteric coli-bacillosis (1986) Am. J. Vet. Res., 47, pp. 2431-2434; Eyskers, M., Boerdam, G.A., Hollanders, W., Verheijden, J.H., The prevalence of Isospora suis and Strongyloides ransomi in suckling piglets in The Netherlands (1994) Vet. Q., 16, pp. 203-205; Fitzgerald, G.R., Barker, T., Welter, M.W., Welter, C.J., Diarrhoea in young pigs: Comparing the incidence of the five most common infectious agents (1988) Vet. Med., 83, pp. 80-86; Guscetti, F., (1991) Untersuchungen zum Erregerspektrum und zur Morphologie des Darmes bei 1 bis 4 Wochen alten Saugferkeln mit Durchfall, , Thesis, University of Zürich, Zürich; Heine, J., Eine einfache nachweismethode für kryptosporidien im kot (1982) Zentralblatt Vet. Med. B, 29, pp. 324-327; Henriksen, S.A., Christensen, J.P.B., Coccidiosis in piglets in Denmark. 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Tierheilk., 120, pp. 513-525; Krauss, H., Arens, M., Die elektronenmikroskopische untersuchung von kot- und organmaterial als diagnostischer schnellnachweis bei der parvovirusinfektion der hunde (1981) Prakt. Tierarzt, 62, pp. 38-41; Lathe, P., Hirth, M., DeWilde, N., Harford, J.P., Lecocq, S.A., Cell-free synthesis of enterotoxin of E. coli from a cloned gene (1980) Nature, 284, pp. 473-474; Lindsay, D.S., Current, W.L., Ernst, J.V., Stuart, B.P., Stewart, B., Prevalence of oocysts of Isospora suis and Eimeria species from sows on farms with and without a history of neonatal coccidiosis (1984) J. Am. Vet. Med. Ass., 185, pp. 419-421; Meyer, C., Joachim, A., Daugschies, A., Occurrence of Isospora suis in larger piglet production units and on specialized piglet rearing farms (1999) Vet. Parasitol., 83, pp. 277-284; Moon, H.W., Schneider, R.A., Moseley, S.L., Comparative prevalence of four enterotoxin genes among Escherichia coli isolated from swine (1986) Am. J. Vet. Res., 47, pp. 210-212; Morin, M., Turgeon, D., Jolette, J., Robinson, Y., Phaneuf, J.B., Saufageau, R., Beauregard, M., Lariviere, S., Neonatal diarrhoea of pigs in Quebec: Infectious causes of significant outbreaks (1983) Can. J. Comp. Med., 47, pp. 11-17; Morris, R.G., Jordan, H.E., Luce, W.G., Coburn, C.T., Maxwell, C.V., Prevalence of gastrointestinal parasitism in Oklahoma swine (1984) Am. J. Vet. Res., 45, pp. 2421-2423; Moseley, S.L., Hardy, J.W., Huq, M.I., Echeverria, P., Falkow, S., Isolation and nucleotide sequence determination of a gene encoding for a heat stable entcrotoxin of Escherichia coli (1983) Infect. Immun., 39, pp. 1167-1174; Muss, C., Hasslinger, M.A., Epidemiologische untersuchungen zur wurmbürde in ferkelerzeuger- und mastbetrieben schwabens (1989) Dtsch. Tierärztl. Wochenschr., 96, pp. 45-84; Nagy, B., Casey, T.A., Moon, H.W., Phenotype and genotype of Escherichia coli isolated from pigs with postweaning diarrhea in Hungary (1990) J. Clin. Microbiol., 28, pp. 651-653; Nakazawa, M., Sugimoto, C., Isayama, Y., Kashiwazaki, M., Virulence factors in Escherichia roll isolated from piglets with neonatal and post-weaning diarrhea in Japan (1987) Vet. Microbiol., 13, pp. 291-300; Nilsson, O., Isospora suis in pigs with postweaning diarrhoea (1988) Vet. Rec., 122, p. 310; Nilsson, O., Martinsson, K., Persson, E., Epidemiology of porcine neonatal steatorrhoea in Sweden: Prevalence and clinical significance of coccidial and rotaviral infections (1984) Nord Vet. Med., 36, pp. 103-110; Ojeniyi, B., Ahrens, P., Jorsal, S.E., Meyling, A., Detection of enterotoxigenic Escherichia coli from pigs with diarrhea using colony hybridization and S labelled probe (1992) Proceedings of the 12th International Pig Veterinary Society Congress, p. 246. , The Hague. Pig Veterinary Society; Otten, A., Takla, M., Daugschies, A., Rommel, M., The epizootiology and pathogenic significance of infections with Isospora suis in ten piglet production operations in Nordrhein-Westfalen (1996) Berl. Münch. Tierärztl. Wochenschr., 109, pp. 220-223; Pritchard, G.C., Transmissible gastroenteritis in endemically infected breeding herds of pigs in East Anglia (1987) Vet. Rec., 120, pp. 226-230; Roberts, L., Walker, E.J., Field study of coccidial and rotaviral diarrhoea in unweaned piglets (1982) Vet. Rec., 110, pp. 11-13; Roepstorff, A., Jorsal, S.E., Relationship of the prevalence of swine helminths to management practises and anthelminthic treatment in Danish sow herds (1989) Vet. Parasitol., 36, pp. 245-257; Rommel, M., Eckert, J., Kutzer, E., Untersuchungsmethoden (1992) Veterinärmedizinische Parasitologie, 4th edn., pp. 46-69. , Eckert, J., E. Kutzer, M. Rommel, H.-J. Bürger, and W. Körting (eds), Paray, Berlin; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning, 2nd edn., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York; Sanford, S.E., Enteric cryptosporidial infection in pigs. 184 Cases (1981-85) (1987) J. Am. Vet. Med. Assoc., 190, pp. 695-698; Stuart, B.P., Gosser, H.S., Allen, C.B., Bedell, D.M., Coccidiosis in swine: Dose and age response to Isospora suis (1982) Can. J. Comp. Med., 46, pp. 317-320; Svensmark, B., Nielsen, K., Dalsgaard, K., Willeberg, P., Epidemiological studies of piglet diarrhea in intensively managed Danish sow herds. 3. Rotavirus infection (1989) Acta Vet. Scand., 30, pp. 63-70; Trotti, G.C., Pampiglione, S., Visconti, S., Crytospotidium species and Isospora suis in pigs in Italy (1987) Parasitology, 26, pp. 299-304; Tubbs, R.C., A review of porcine neonatal Coccidiosis (1986) Mod. Vet. Pract., 67, pp. 899-903; Villacorta, I., Ares-Mazas, E., Lorenzo, M.J., Cryptosporidium parvum in cattle, sheep and pigs in Galicia (1991) Vet. Parasitol., 38, pp. 249-252; Wilson, R.A., Francis, D.H., Fimbriae and enterotoxins associated with Escherichia coli serogroups isolated from pigs with colibacillosis (1986) Am. J, Vet. Res., 47, pp. 213-217; Wray, C., McLaren, I.M., Carroll, P.J., Escherichia coli isolated from farm animals in England and Wales between 1986 and 1991 (1993) Vet. Rec., 133, pp. 439-442","Wieler, L.H.; Institut für Mikrobiologie, Tierseuchen der Freien-Univ. Berlin, D-10115 Berlin, Germany",,,09311793,,JVMBE,"11315526","English","J. Vet. Med. Ser. B",Article,"Final",,Scopus,2-s2.0-0035052338
"Schwegmann C., Zimmer G., Yoshino T., Enss M.-L., Herrler G.","15744497500;7102982629;36846580000;6701700558;7006339246;","Comparison of the sialic acid binding activity of transmissible gastroenteritis coronavirus and E. coli K99",2001,"Virus Research","75","1",,"69","73",,8,"10.1016/S0168-1702(01)00228-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035050638&doi=10.1016%2fS0168-1702%2801%2900228-3&partnerID=40&md5=f7a09d2e372f729e5900d5265ad54207","Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Department of Chemistry, International Christian University, 3-10-2 Osawa, Mitaka, Tokyo 181-8585, Japan; Zentrales Tierlabor, Medizinische Hochschule Hannover, 30623 Hannover, Germany","Schwegmann, C., Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Zimmer, G., Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Yoshino, T., Department of Chemistry, International Christian University, 3-10-2 Osawa, Mitaka, Tokyo 181-8585, Japan; Enss, M.-L., Zentrales Tierlabor, Medizinische Hochschule Hannover, 30623 Hannover, Germany; Herrler, G., Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany","Transmissible gastroenteritis coronavirus (TGEV) and Escherichia coli K99 are both enteropathogenic for pigs with infections being most severe in neonate animals. For both microorganisms, a sialic acid binding activity has been shown to be an essential pathogenicity factor. Here we demonstrate with haemagglutination and haemagglutination-inhibition assays that TGEV and E. coli K99 differ in their sialic acid binding activities with respect to the type and amount of sialic acid residues required on the erythrocytes surface as well as with respect to the type of sialoglycoconjugate preferentially recognized. Intestinal mucins from piglets (12-14 days old) and adult animals were shown to inhibit TGEV to the same extent. From our results we conclude that E. coli K99 and TGEV interact with different sialoglycoconjugates to establish an intestinal infection. The implications for the enteropathogenicity of TGEV are discussed. © 2001 Elsevier Science B.V.","E. coli K99; Glycolipids; Mucins; Sialic acid; TGEV","mucin; salicylic acid; sialoglycoprotein; animal cell; article; cell surface; conjugate; controlled study; Coronavirus; enteropathy; erythrocyte; Escherichia coli; gastroenteritis; hemagglutination; nonhuman; pathogenicity; priority journal; swine; virus inhibition; virus transmission; Age Factors; Animals; Animals, Newborn; Cattle; Chickens; Erythrocytes; Escherichia coli; Hemagglutination Inhibition Tests; Hemagglutination Tests; Horses; Mucins; N-Acetylneuraminic Acid; Neuraminidase; Swine; Transmissible gastroenteritis virus; Animalia; Coronavirus; Escherichia coli; Transmissible gastroenteritis virus","Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Enss, M.-L., Schmidt-Wittig, U., Müller, H., Mai, U.E.H., Coenen, M., Hedrich, H.J., Response of germfree rat colonic mucous cells to peroral endotoxin application (1996) Eur. J. Cell Biol., 71, pp. 99-104; Gaastra, W., De Graaf, F.K., Host-specific fimbrial adhesins of non-invasive enterotoxigenic Escherichia coli strains (1982) Microbiol. Rev., 46, pp. 129-161; Hakomori, S., Saito, T., Isolation and characterization of a glycosphingolipid having a new sialic acid (1969) Biochemistry, 8, pp. 5082-5088; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J. Virol., 71, pp. 3285-3287; Krempl, C., Ballesteros, M.L., Zimmer, G., Enjuanes, L., Klenk, H.-D., Herrler, G., Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants (2000) J. Gen. Virol., 81, pp. 489-496; Mouricout, M., Petit, J.M., Carias, J.R., Julien, R., Glycoprotein glycans that inhibit adhesion of Escherichia coli mediated by K99 fimbriae: Treatment of experimental colibacillosis (1990) Infection and Immunity, 58, pp. 98-106; Noda, M., Yamashita, H., Koide, F., Kadoi, K., Omori, T., Asagi, M., Inaba, Y., Hemagglutination with transmissible gastroenteritis virus (1987) Arch. Virol., 96, pp. 109-115; Noda, M., Koide, F., Asagi, M., Inaba, Y., Physicochemical properties of transmissible gastroenteritis virus hemagglutinin (1988) Arch. Virol., 99, pp. 163-172; Ono, E., Abe, K., Nakazawa, M., Naiki, M., Ganglioside epitope recognized by K99 fimbriae from enterotoxigenic Escherichia coli (1989) Infect. Immun., 57, pp. 907-911; Pensaert, M., Callebaut, P., Cox, E., Enteric coronaviruses of animals (1993) Viral Infections of the Gastrointestinal Tract, pp. 627-696. , Kapikian, A.Z. (Ed.), Marcel Dekker, New York; Reuter, G., Stoll, S., Kamerling, J.P., Vliegenthart, J.F.G., Schauer, R., Sialic acids on erythrocytes and in blood plasma of mammals (1988) Proceedings of the Japanese-German Symposium on Sialic Acids, pp. 88-89. , Sialic Acids 1988: Schauer, R., Yamakawa, T. (Eds,), Kieler Verlag Wissenschaft und Bildung, Kiel, Germany; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) J. Virol., 70, pp. 5634-5637; Seignole, D., Mouricout, M., Duval-Iflah, Y., Quintard, B., Julien, R., Adhesion of K99 fimbriated Escherichia coli to pig intestinal epithelium: Correlation of adhesive and non-adhesive phenotypes with the sialoglycolipid content (1991) J. Gen. Microbiol., 137, pp. 1591-1601; Teneberg, S., Willemsen, P., De Graaf, F.K., Karlsson, K.A., Receptor-active glycolipids of epithelial cells of the small intestine of young and adult pigs in relation to susceptibility to infection with Escherichia coli K99 (1990) FEBS Lett., 263, pp. 10-14; Teneberg, S., Willemsen, P.T., De Graaf, F.K., Stenhagen, G., Pimlott, W., Jovall, P.A., Angstrom, J., Karlsson, K.A., Characterization of gangliosides of epithelial cells of calf small intestine, with special reference to receptor-active sequences for enteropathogenic Escherichia coli K99 (1994) J. Biochem. (Tokyo), 116, pp. 560-574","Herrler, G.; Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; email: herrler@viro.tiho-hannover.de",,,01681702,,VIRED,"11311429","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0035050638
"Mochizuki M., Hashimoto M., Ishida T.","7403050664;7404557915;7403962144;","Recent Epidemiological Status of Canine Viral Enteric Infections and Giardia Infection in Japan",2001,"Journal of Veterinary Medical Science","63","5",,"573","575",,34,"10.1292/jvms.63.573","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035348340&doi=10.1292%2fjvms.63.573&partnerID=40&md5=0c7b1e91b5df805a433ee47c0828a21d","Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan; Akasaka Animal Hospital, 4-1-29 Akasaka, Minato-ku, Tokyo 107-0052, Japan","Mochizuki, M., Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan; Hashimoto, M., Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan; Ishida, T., Akasaka Animal Hospital, 4-1-29 Akasaka, Minato-ku, Tokyo 107-0052, Japan","Epidemiology of canine enteric infections was studied. Rectal swabs collected from 95 dogs presented at animal hospitals during a period from January to June of 2000 were examined for enteric pathogens, including viruses and Giardia lamblia (G. lamblia). Most frequently detected in both diarrheal and normal feces were canine coronavirus (55.4%) and G. lamblia (48.2%). Canine parvovirus type 2 (CPV-2) was specifically associated with diarrheal cases and CPV-2b was the predominant antigenic type. Although canine rotavirus, canine adenovirus, and canine distemper virus were also detected in a small number of diarrheal cases, no evidence for calicivirus infection was obtained.","Canine coronavirus; Canine parvovirus; Giardia lamblia","Adenoviridae; Animalia; Caliciviridae; Canine adenovirus; Canine coronavirus; Canine distemper virus; Canine parvovirus; Canine parvovirus 2; Canine rotavirus; Canis familiaris; Coronavirus; distemper virus; Giardia; Giardia intestinalis; Parvovirus; Rotavirus; animal; animal disease; article; Coronavirus; diarrhea; dog; dog disease; feces; Giardia lamblia; giardiasis; isolation and purification; Japan; parasitology; Parvovirus; virology; virus infection; Animals; Coronavirus; Coronavirus Infections; Diarrhea; Dog Diseases; Dogs; Feces; Giardia lamblia; Giardiasis; Japan; Parvoviridae Infections; Parvovirus; Virus Diseases","Addiss, D.G., (1991) J. Clin. Microbiol., 29, pp. 1137-1142; Appel, M., (1987) Virus Infections of Carnivores, pp. 115-122. , (Appel, M. J. ed.), Elsevier Science Publishers B.V., Amsterdam; Arasima, Y., Kumasaka, K., Kawano, K., Asano, T., Hokari, S., Murasugi, E., Iwasita, E., Matsuo, K., (1992) J. Jpn. Assoc. Infec. Dis., 66, pp. 1062-1066; Asano, T., Hokari, N., Murasugi, E., Arasima, Y., Kubo, N., Kawano, K., (1991) J. Jpn. Assoc. Infec. Dis., 65, pp. 157-161; Bandai, C., Ishiguro, S., Masuya, N., Hohdatsu, T., Mochizuki, M., (1999) J. Vet. Med. Sci., 61, pp. 731-736; Barr, S.C., Bowman, D.D., (1994) Compendium Contin. Educ. Pract. Vet., 16, pp. 603-611; Hashimoto, M., Roerink, F., Tohya, Y., Mochizuki, M., (1999) J. Vet. Med. Sci., 61, pp. 603-608; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., (1995) J. Clin. Microbiol., 33, pp. 684-689; Ikeda, Y., Mochizuki, M., Naito, R., Nakamura, K., Miyazawa, T., Mikami, T., Takahashi, E., (2000) Virology, 278, pp. 13-19; Iwatsuki, K., Miyashita, N., Yoshida, E., Gemma, T., Shin, Y.-S., Mori, T., Hirayama, N., Mikami, T., (1997) J. Gen. Virol., 78, pp. 373-380; Leib, M.S., Zajac, A.M., (1999) Vet. Med., 94, pp. 793-802; Mochizuki, M., (1996) J. Jpn. Vet. Med. Assoc., 49, pp. 293-300. , in Japanese; Mochizuki, M., Hashimoto, M., Hagiwara, S., Yoshida, Y., Ishiguro, S., (1999) J. Clin. Microbiol., 37, pp. 2936-2942; Mochizuki, M., Hida, S., Hsuan, S.W., Sato, H., (1984) Jpn. J. Vet. Sci., 46, pp. 841-844; Mochizuki, M., Hsuan, S.-W., (1984) Jpn. J. Vet. Sci., 46, pp. 905-908; Mochizuki, M., Konishi, S., Ajiki, M., Akaboshi, T., (1989) Jpn. J. Vet. Sci., 51, pp. 264-272; Mochizuki, M., Nakagomi, T., Nakagomi, O., (1997) Clin. Microbiol., 35, pp. 1272-1275; Mochizuki, M., Nakagomi, O., Shibata, S., (1992) Arch. Virol., 122, pp. 373-381; Mochizuki, M., San Gabriel, M.C., Nakatani, H., Yoshida, M., (1993) Res. Vet. Sci., 55, pp. 60-63; Parrish, C.R., (1994) Encyclopedia of Virology, pp. 1061-1067. , (Webster, R. G. and Granoff, A. eds.), Academic Press, London; Sugano, H., Fukase, T., Chinone, S., Itagaki, H., (1989) J. Jpn. Vet. Med. Assoc., 42, pp. 68-71; Yasoshima, A., Fujinami, F., Doi, K., Kojima, A., Takada, H., Okaniwa, A., (1983) Jpn. J. Vet. Sci., 45, pp. 217-225; Zajac, A., (1992) Compendium Contin. Educ. Pract. Vet., 14, pp. 604-611","Mochizuki, M.; Laboratory of Clinical Microbiology, Kyoritsu Shoji Corporation, 1-12-4 Kudankita, Chiyoda-ku, Tokyo 102-0073, Japan",,,09167250,,,"11411507","English","J. Vet. Med. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0035348340
"Lim K.P., Liu D.X.","7403175857;8972667300;","The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins",2001,"Journal of Biological Chemistry","276","20",,"17515","17523",,72,"10.1074/jbc.M009731200","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035907388&doi=10.1074%2fjbc.M009731200&partnerID=40&md5=60ce836e5cb03d91e17967375a95c971",,"Lim, K.P.; Liu, D.X.","One missing link in the coronavirus assembly is the physical interaction between two crucial structural proteins, the membrane (M) and envelope (E) proteins. In this study, we demonstrate that the coronavirus infectious bronchitis virus E can physically interact, via a putative peripheral domain, with M. Deletion of this domain resulted in a drastic reduction in the incorporation of M into virus-like particles. Immunofluorescent staining of cells coexpressing M and E supports that E interacts with M and relocates M to the same subcellular compartments that E resides in. E was retained in the pre-Golgi membranes, prior to being translocated to the Golgi apparatus and the secretory vesicles; M was observed to exhibit similar localization and translocation profiles as E when coexpressed with E. Deletion studies identified the C-terminal 6-residue RDKLYS as the endoplasmic reticulum retention signal of E, and site-directed mutagenesis of the -4 lysine residue to glutamine resulted in the accumulation of E in the Golgi apparatus. The third domain of E that plays a crucial role in virus budding is a putative transmembrane domain present at the N-terminal region, because deletion of the domain resulted in a free distribution of the mutant protein and in dysfunctional viral assembly.",,"Biochemistry; Cell membranes; Fluorescence; Immunology; Mutagenesis; Viruses; Golgi apparatus; Proteins; complementary DNA; membrane protein; virus envelope protein; virus protein; virus RNA; cycloheximide; membrane protein; animal cell; article; Avian infectious bronchitis virus; cellular distribution; Coronavirus; gene overexpression; Golgi complex; nonhuman; plasmid; polyacrylamide gel electrophoresis; polymerase chain reaction; priority journal; protein localization; protein protein interaction; radioimmunoprecipitation; site directed mutagenesis; Vero cell; virus assembly; virus envelope; virus particle; amino acid sequence; amino acid substitution; animal; cell strain COS1; Cercopithecus; chemistry; endoplasmic reticulum; gene deletion; genetics; glycosylation; Golgi complex; metabolism; molecular genetics; physiology; virion; virology; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; RNA viruses; Amino Acid Sequence; Amino Acid Substitution; Animals; Cercopithecus aethiops; COS Cells; Cycloheximide; Endoplasmic Reticulum; Gene Products, env; Glycosylation; Golgi Apparatus; Infectious bronchitis virus; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Sequence Deletion; Vero Cells; Virion","Brautigam, S., Snezhkov, E., Bishop, D.H., (1993) Virology, 192, pp. 512-524; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J., Rottier, P.J.M., (1996) EMBO J., 15, pp. 2020-2028; Li, T.C., Yamakawa, Y., Suzuki, K., Tatsumi, M., Razak, M.A., Uchida, T., Takeda, N., Miyamura, T., (1997) J. Virol., 71, pp. 7207-7213; White, L.J., Hardy, M.E., Estes, M.K., (1997) J. Virol., 71, pp. 8066-8072; Baumert, T.F., Ito, S., Wong, D.T., Liang, T.J., (1998) J. Virol., 72, pp. 3827-3836; Jiang, B., Barniak, V., Smith, R.P., Sharma, R., Corsaro, B., Hu, B., Madore, H.P., (1998) Biotechnol. Bioeng., 60, pp. 369-374; Garbutt, M., Chan, H., Hobman, T.C., (1999) Virology, 261, pp. 340-346; Neumann, G., Watanabe, T., Kawaoka, Y., (2000) J. Virol., 74, pp. 547-551; Haglund, K., Forman, J., Krausslich, H., Rose, J.K., (2000) Virology, 268, pp. 112-121; Holmes, K.V., Doller, E.W., Sturman, L.S., (1981) Virology, 115, pp. 334-344; Hogue, B.G., Brian, D.A., (1986) Virus Res., 5, pp. 131-144; Delmas, B., Laude, H., (1990) J. Virol., 64, pp. 5367-5375; Locker, J.K., Rose, J.K., Horzinek, M.C., Rottier, P.J.M., (1992) J. Biol. Chem., 267, pp. 21911-21918; Liu, D.X., Inglis, S.C., (1991) Virology, 185, pp. 911-917; Corse, E., Machamer, C.E., (2000) J. Virol., 74, pp. 4319-4326; Dea, S., Tijssen, P., (1988) Arch. Virol., 99, pp. 173-186; Risco, C., Muntion, M., Enjuanes, L., Carrascosa, J.L., (1998) J. Virol., 72, pp. 4022-4031; Salanueva, I.J., Carrascosa, J.L., Risco, C., (1999) J. Virol., 73, pp. 7952-7964; Tooze, J., Tooze, S.A., Warren, G., (1984) Eur. J. Cell Biol., 33, pp. 281-293; Chen, B.Y., Itakura, C., (1996) Avian Pathol., 25, pp. 675-690; Maeda, J., Maeda, A., Makino, S., (1999) Virology, 263, pp. 265-272; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., (2000) J. Virol., 74, pp. 2333-2342; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., (1998) J. Virol., 72, pp. 7885-7894; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., (1998) J. Virol., 72, pp. 8636-8643; Smith, A.R., Boursnell, M.E.G., Binns, M.M., Brown, T.D.K., Inglis, S.C., (1990) J. Gen. Virol., 71, pp. 3-11; Liu, D.X., Shen, S., Xu, H.Y., Wang, S.F., (1998) Virology, 246, pp. 288-297; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., (1986) Proc. Natl. Acad. Sci. U. S. A., 83, pp. 8122-8126; Laemmli, U.K., (1970) Nature, 227, pp. 680-685; Ng, L.F.P., Liu, D.X., (2000) Virology, 272, pp. 27-39; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., (1991) Virology, 184, pp. 531-544; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., (1994) J. Virol., 68, pp. 5772-5780; Machamer, C.E., Mentone, S.A., Rose, J.K., Farquhar, M.G., (1990) Proc. Natl. Acad. Sci. U. S. A., 87, pp. 6944-6948; Nakai, K., Kanehisa, M., (1992) Genomics, 14, pp. 897-911; Hofmann, K., Stoffel, W., (1993) Biol. Chem. Hoppe-Seyler, 347, p. 166; De Haan, C.A.M., Vennema, H., Rottier, P.J.M., (2000) J. Virol., 74, pp. 4967-4978; De Haan, C.A.M., Smeets, M., Vernooij, F., Vennema, H., Rottier, P.J.M., (1999) J. Virol., 73, pp. 7441-7452; Nguyen, V.-P., Hogue, B., (1997) J. Virol., 71, pp. 9278-9284; Narayanan, K., Maeda, A., Maeda, J., Makino, S., (2000) J. Virol., 74, pp. 8127-8134; Budzilowicz, C.J., Weiss, S.R., (1987) Virology, 157, pp. 509-515; Alonso-Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., (1984) Virus Res., 2, pp. 153-167; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M., Geuze, H.J., Rottier, P.J.M., (1994) J. Virol., 68, pp. 6523-6534; De Haan, C.A., Kuo, L., Masters, P., Vennema, H., Rottier, P.J.M., (1998) J. Virol., 72, pp. 6838-6850; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., (1996) J. Virol., 70, pp. 4773-4777; Nilsson, T., Jackson, M., Peterson, P.A., (1989) Cell, 58, pp. 707-718; Lee, C.-W., Jackwood, M.W., (2000) Avian Dis., 44, pp. 650-654; Sutou, S., Sato, S., Okabe, T., Nakai, M., Sasaki, N., (1988) Virology, 165, pp. 589-595; Teasdale, R.D., Jackson, M.R., (1996) Annu. Rev. Cell Dev. Biol., 12, pp. 27-54; Mounir, S., Talbot, P.J., (1993) Virology, 192, pp. 355-360; Almanzan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 5516-5521",,,,00219258,,JBCHA,"11278557","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0035907388
"Rossen J.W.A., Kouame J., Goedheer A.J.W., Vennema H., Rottier P.J.M.","7005977394;6601977837;8968488900;7003697291;7006145490;","Feline and canine coronaviruses are released from the basolateral side of polarized epithelial LLC-PK1 cells expressing the recombinant feline aminopeptidase-N cDNa",2001,"Archives of Virology","146","4",,"791","799",,16,"10.1007/s007050170147","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035012184&doi=10.1007%2fs007050170147&partnerID=40&md5=cc4628c2d7a94ce0c92b14f62aa5d0f9","Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Pediat. Gastroenterol. and Nutrition, Erasmus University Medical Center, Rotterdam, Netherlands; Pediat. Gastroenterol. and Nutrition, Erasmus Univ. Med. Center Rotterdam, Dr. Molewaterplein 50, 3015 GE Rotterdam, Netherlands","Rossen, J.W.A., Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands, Pediat. Gastroenterol. and Nutrition, Erasmus University Medical Center, Rotterdam, Netherlands, Pediat. Gastroenterol. and Nutrition, Erasmus Univ. Med. Center Rotterdam, Dr. Molewaterplein 50, 3015 GE Rotterdam, Netherlands; Kouame, J., Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Goedheer, A.J.W., Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Vennema, H., Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Rottier, P.J.M., Department of Infectious Diseases, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands","In this study feline (FECV and FIPV) and canine (CCoV) coronavirus entry into and release from polarized porcine epithelial LLC-PK1 cells, stably expressing the recombinant feline aminopeptidase-N cDNA, were investigated. Virus entry appeared to occur preferentially through the apical membrane, similar to the entry of the related porcine coronavirus transmissible gastroenteritis virus (TGEV) into these cells. However, whereas TGEV is released apically, feline and canine coronaviruses were found to be released from the basolateral side of the epithelial cells. These observations indicate that local infections as caused by TGEV, FECV and CCoV do not strictly correlate with apical release, as suggested by earlier work.",,"complementary DNA; Coronavirus; enzyme release; epithelium cell; feline coronavirus; microsomal aminopeptidase; recombinant enzyme; swine; transmissible gastroenteritis virus; Aminopeptidases; Animals; Cats; Cell Polarity; Coronavirus; Coronavirus, Canine; DNA, Complementary; Epithelial Cells; LLC-PK1 Cells; Recombinant Proteins; Swine; Transfection; Canine coronavirus; Coronavirus; Felidae; Feline coronavirus; Feline infectious peritonitis virus; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Cerneus, D.P., Strous, G.J., Van der Ende, A., Bidirectional transcytosis determines the steady state distribution of the transferrin receptor at opposite plasma membrane domains of BeWo cells (1993) J Cell Biol, 122, pp. 1223-1230; Hohdatsu, T., Izumiya, Y., Yokoyama, Y., Kida, K., Koyama, H., Differences in virus receptor for type I and type II feline infectious peritonitis virus (1998) Arch Virol, 143, pp. 839-850; Horzinek, M.C., Lutz, H., Pedersen, N.C., Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses (1982) Infect Immun, 37, pp. 1148-1155; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Levis, R., Cardellichio, C.B., Scanga, C.A., Compton, S.R., Holmes, K.V., Multiple receptor-dependent steps determine the species specificity of HCV-229E infection (1995) Adv Exp Med Biol, 380, pp. 337-343; Lin, X., O'Reilly, K., Storz, J., Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny (1997) Am J Vet Res, 58, pp. 1120-1124; Rossen, J.W.A., Bekker, C.P.J., Voorhout, W.F., Strous, G.J.A.M., Van der Ende, A., Rottier, P.J.M., Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells (1994) J Virol, 68, pp. 7966-7973; Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Van der Ende, A., Strous, G.J.A.M., Rottier, P.J.M., MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally (1995) Virology, 210, pp. 54-66; Rossen, J.W.A., Bekker, C.P., Strous, G.J., Horzinek, M.C., Dveksler, G.S., Holmes, K.V., Rottier, P.J., A murine and a porcine coronavirus are released from opposite surfaces of the same epithelial cells (1996) Virology, 224, pp. 345-351; Rossen, J.W., Strous, G.J., Horzinek, M.C., Rottier, P.J., Mouse hepatitis virus strain A59 is released from opposite sides of different epithelial cell types (1997) J Gen Virol, 78, pp. 61-69; Rossen, J.W., De Beer, R., Godeke, G.J., Raamsman, M.J., Horzinek, M.C., Vennema, H., Rottier, P.J., The viral spike protein is not involved in the polarized sorting of coronaviruses in epithelial cells (1998) J Virol, 72, pp. 497-503; Schultze, B., Zimmer, G., Herrler, G., Virus entry into a polarized epithelial cell line (MDCK): Similarities and dissimilarities between influenza C virus and bovine coronavirus (1996) J Gen Virol, 77, pp. 2507-2514; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J Virol, 70, pp. 8669-8674; Vennema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J.M., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409; Wessels, H.P., Hansen, G.H., Fuhrer, C., Look, A.T., Sjostrom, H., Noren, O., Spiess, M., Aminopeptidase N is directly sorted to the apical domain in MDCK cells (1990) J Cell Biol, 111, pp. 2923-2930; Yeaman, C., Grindstaff, K.K., Nelson, W.J., New perspectives on mechanisms involved in generating epithelial cell polarity (1999) Physiol Rev, 79, pp. 73-98; Zegers, M.M.P., Hoekstra, D., Mechanisms and functional features of polarized membrane traffic in epithelial and hepatic cells (1998) Biochem J, 336, pp. 257-269","Rossen, J.W.A.; Pediat. Gastroenterol. and Nutrition, Erasmus Univ. Med. Center Rotterdam, Dr. Molewaterplein 50, 3015 GE Rotterdam, Netherlands; email: rossen@kgk.fgg.eur.nl",,,03048608,,ARVID,"11402864","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035012184
"Addie D.D., Jarrett O.","7003910352;7006845693;","Use of a reverse-transcriptase polymerase chain reaction for monitoring the shedding of feline coronavirus by healthy cats",2001,"Veterinary Record","148","21",,"649","653",,64,"10.1136/vr.148.21.649","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035954225&doi=10.1136%2fvr.148.21.649&partnerID=40&md5=31fda4e9e0cc1509dd60f761ccea1ee7","Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom","Addie, D.D., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom; Jarrett, O., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom","The pattern of shedding of feline coronavirus (FCov) was established in 155 naturally infected pet cats from 29 households over periods of up to five years. Viral RNA was detected in faeces by reverse-transcriptase PCR (RT-PCR), and plasma antiviral antibodies by immunofluorescence. The cats rarely shed FCov in their saliva. Three patterns of FCov shedding were observed. Eighteen of the cats shed virus continuously, so were persistent, and possibly lifelong, carriers; none of them developed feline infectious peritonitis. Fifty-six cats ceased shedding virus, although they were susceptible to reinfection, and 44 shed intermittently or were being continuously reinfected. Four of the cats were resistant to infection. Seventy-three per cent of the virus shedding episodes lasted up to three months and 95 per cent up to nine months. There was a correlation between shedding and antibody titre but the cats could remain seropositive for some time after they had ceased shedding virus. One-off testing for FCoV by RT-PCR is inappropriate. Identification of long-term carriers requires that a positive result be obtained by RT-PCR on faecal samples for at least eight consecutive months. A cat should be shown to be negative over five months, or to have become seronegative, to ensure that it has ceased shedding virus.",,"virus antibody; virus RNA; animal; animal disease; article; blood; cat; cat disease; Coronavirus; feces; fluorescent antibody technique; genetics; heterozygote; immunology; isolation and purification; pathophysiology; reverse transcription polymerase chain reaction; time; virology; virus infection; virus shedding; Animals; Antibodies, Viral; Carrier State; Cat Diseases; Cats; Coronavirus Infections; Coronavirus, Feline; Feces; Fluorescent Antibody Technique, Indirect; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Time Factors; Virus Shedding","Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infection in kittens (1992) Veterinary Record, 130, pp. 133-137; Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., The risk of feline infectious peritonitis in cats naturally infected with feline coronavirus (1995) American Journal of Veterinary Research, 56, pp. 429-434; Duthie, S., Eckersall, P.D., Addie, D.D., Lawrence, C.E., Jarrett, O., Value of α1-acid glycoprotein in the diagnosis of feline infectious peritonitis (1997) Veterinary Record, 141, pp. 299-303; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) Journal of the American Veterinary Medical Association, 210, pp. 1307-1312; Gonon, V., Eloit, M., Monteil, M., Evolution de la prevalence de l'infection a coronavirus felin dans deux effectifs adoptant des conduites d'élevage differentes (1995) Recueil de Medecine Veterinaire, 171, pp. 33-38; Harpold, L.M., Legendre, A.M., Kennedy, M.A., Plummer, P.J., Milesaps, K., Rohrbach, B., Fecal shedding of feline coronavirus in adult cats and kittens in an Abyssinian cattery (1999) Journal of the American Veterinary Medical Association, 215, pp. 948-951; Hegyi, A., Kolb, A.F., Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N (1998) Journal of General Virology, 79, pp. 1387-1391; Herrewegh, A.A.P.M., De Grout, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissue, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) Journal of Clinical Microbiology, 35, pp. 684-689; Herrewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Kolb, A.F., Hegyi, A., Maile, J., Heister, A., Hagemann, M., Siddell, S.G., Molecular analysis of the coronavirus-receptor function of aminopeptidase N (1998) Advances in Experimental Medicine and Biology, 440, pp. 61-67; Lutz, H., Fehr, D., Rohrer, C., Suter, P.F., Current knowledge on FIP from a European perspective; current concepts of the disease, current and future research (1995) Proceedings of the AAFP Symposium on Feline Infectious Diseases, pp. 22-27. , Washington DC; Michael, N.L., Nelson, J.A., Kewalramani, V.N., Chang, G., O'Brien, S.J., Mascola, J.R., Volsky, B., O'Brien, T.R., Exclusive and persistent use of the entry coreceptor CXCR4 by human immunodeficiency virus type 1 from a subject homozygous for CCR5 delta32 (1998) Journal of Virology, 72, pp. 6040-6047; Stoddart, M.E., Gaskell, R.M., Harbour, D.A., Gaskell, C.J., Virus shedding and immune responses in cats inoculated with cell culture-adapted feline infectious peritonitis virus (1988) Veterinary Microbiology, 16, pp. 145-158; Tresnan, D.B., Holmes, K.V., Feline aminopeptidase N is a receptor for all group I coronaviruses (1998) Advances in Experimental Medicine and Biology, 440, pp. 69-75; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) Journal of Virology, 70, pp. 9669-9674","Addie, D.D.; Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom",,"British Veterinary Association",00424900,,VETRA,"11400984","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0035954225
"Akin A., Lin T.L., Wu C.C., Bryan T.A., Hooper T., Schrader D.","7006727744;7404860140;7501664098;7005517787;7005121335;7007179253;","Nucleocapsid protein gene sequence analysis reveals close genomic relationship between Turkey coronavirus and avian infectious bronchitis virus",2001,"Acta Virologica","45","1",,"31","38",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035025756&partnerID=40&md5=827949f3c3b87303bdfe20b138d64d11","Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States","Akin, A., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Lin, T.L., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T.A., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States","Antibodies to infectious bronchitis virus (IBV) cross-react with turkey coronavirus (TCV) in immunofluorescence assay (IFA) indicating that IBV and TCV may share an amino acid sequence similarity. To determine its extent, the gene encoding the nucleocapsid (N) protein of TCV was amplified by reverse transcription-PCR (RT-PCR) from RNA purified from intestines of embryos of turkeys infected with various TCV isolates and from allantoic fluid of chicken embryos infected with IBV M41 strain, the obtained N genes were cloned, sequenced and compared with known sequences of N genes of five IBV strains. The primers for amplification were designed from the genome of IBV. PCR products were obtained only from two of eight TCV isolates tested. It was found that the two TCV isolates were identical with five IBV strains by 90.1-94.1% at the N gene level. It was also observed that the N gene of eight TCV isolates originating from various regions of the USA could not be amplified by the primers designed from the N gene of bovine coronavirus (BCV).","Infectious bronchitis virus; Nucleocapsid protein gene, genomic similarity; Turkey coronavirus","cross reacting antibody; nucleocapsid protein; virus antibody; amino acid sequence; article; Avian infectious bronchitis virus; chick embryo; Coronavirus; cross reaction; gene library; genome; nonhuman; reverse transcription polymerase chain reaction; RNA purification; sequence analysis; sequence homology; strain difference; virus characterization; virus nucleocapsid; Amino Acid Sequence; Animals; Antibodies, Viral; Base Sequence; Chick Embryo; Cloning, Molecular; Coronavirus, Turkey; Cross Reactions; DNA, Viral; Genes, Viral; Genome, Viral; Infectious bronchitis virus; Molecular Sequence Data; Nucleocapsid Proteins; Phylogeny; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Turkeys",,"Lin, T.L.; Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,,0001723X,,AVIRA,"11394575","English","Acta Virol.",Article,"Final",,Scopus,2-s2.0-0035025756
"Bost A.G., Prentice E., Denison M.R.","6506678262;7003706540;7101971810;","Mouse hepatitis virus replicase protein complexes are translocated to sites of M protein accumulation in the ERGIC at late times of infection",2001,"Virology","285","1",,"21","29",,52,"10.1006/viro.2001.0932","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035918981&doi=10.1006%2fviro.2001.0932&partnerID=40&md5=867524e8eb3b15d1042a6f2bf1c5031e","Department of Microbiology and Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232, United States","Bost, A.G., Department of Microbiology and Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232, United States; Prentice, E., Department of Microbiology and Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232, United States; Denison, M.R., Department of Microbiology and Immunology, Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University, Nashville, TN 37232, United States","The coronavirus mouse hepatitis virus (MHV) directs the synthesis of viral RNA on discrete membranous complexes that are distributed throughout the cell cytoplasm. These putative replication complexes are composed of intimately associated but biochemically distinct membrane populations, each of which contains proteins processed from the replicase (gene 1) polyprotein. Specifically, one membrane population contains the gene 1 proteins p65 and p1a-22, while the other contains the gene 1 proteins p28 and helicase, as well as the structural nucleocapsid (N) protein and newly synthesized viral RNA. In this study, immunofluorescence confocal microscopy was used to define the relationship of the membrane populations comprising the putative replication complexes at different times of infection in MHV-A59-infected delayed brain tumor cells. At 5.5 h postinfection (p.i.) the membranes containing N and helicase colocalized with the membranes containing p1a-22/p65 at foci distinct from sites of M accumulation. By 8 to 12 h p.i., however, the membranes containing helicase and N had a predominantly perinuclear distribution and colocalized with M. In contrast, the p1a-22/p65-containing membranes retained a peripheral, punctate distribution at all times of infection and did not colocalize with M. By late times of infection, helicase, N, and M each also colocalized with ERGIC p53, a specific marker for the endoplasmic reticulum-Golgi-intermediate compartment. These data demonstrated that the putative replication complexes separated into component membranes that relocalized during the course of infection. These results suggest that the membrane populations within the MHV replication complex serve distinct functions both in RNA synthesis and in delivery of replication products to sites of virus assembly. © 2001 Academic Press.",,"nucleocapsid protein; RNA directed RNA polymerase; virus protein; virus RNA; animal cell; article; brain cell; confocal microscopy; controlled study; Coronavirus; gene translocation; hepatitis virus; nonhuman; priority journal; protein localization; RNA synthesis; tumor cell culture; virus assembly; virus infection; Coronavirus; Murine hepatitis virus","Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Bi, W., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., Intracellular localization of polypeptides encoded in mouse hepatitis virus open reading frame 1A (1995) Adv. Exp. Med. 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Biol., 440, pp. 121-127; Denison, M.R., Spaan, W.J., Van der Meer, Y., Gibson, C.A., Sims, A.C., Prentice, E., Lu, X.T., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) J. Virol., 73 (8), pp. 6862-6871; Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes (1988) J. Cell Biol., 107 (6), pp. 2075-2086; Hauri, H., Kappeler, F., Andersson, H., Appenzeller, C., ERGIC-53 and traffic in the secretory pathway (2000) J. Cell Sci., 113, pp. 587-596; Heusipp, G., Grotzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78 (PART 11), pp. 2789-2794; Hirano, N., Fujiwara, K., Matumoto, M., Mouse hepatitis virus (MHV-2): Plaque assay and propagation in mouse cell line DBT cells (1976) Jpn. J. Microbiol., 20 (3), pp. 219-225; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X.T., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor e64dd (1995) Virology, 208, pp. 1-8; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68 (10), pp. 6523-6534; Krijnse-Locker, J., Ericsson, M., Rottier, P.J., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J. Cell Biol., 124 (1-2), pp. 55-70; Leibowitz, J.L., DeVries, R.R., Haspel, M.V., Genetic analysis of murine hepatitis virus strain JHM (1982) J. Virol., 42, pp. 1080-1087; Lombardi, D., Soldati, T., Riederer, M.A., Goda, Y., Zerial, M., Pfeffer, S.R., Rab9 functions in transport between late endosomes and the trans Golgi network (1993) EMBO J., 12 (2), pp. 677-682; Lu, X.T., Sims, A.C., Denison, M.R., Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro (1998) J. Virol., 72 (3), pp. 2265-2271; Narayanan, K., Maeda, A., Maeda, J., Makino, S., Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells (2000) J. Virol., 74 (17), pp. 8127-8134; Nejmeddine, M., Trugnan, G., Sapin, C., Kohli, E., Svensson, L., Lopez, S., Cohen, J., Rotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells (2000) J. Virol., 74 (7), pp. 3313-3320; Perlman, S., Reese, D., Bolger, E., Chang, L.J., Stoltzfus, C.M., MHV nucleocapsid synthesis in the presence of cycloheximide and accumulation of negative strand MHV RNA (1987) Virus Res., 6, pp. 261-272; Rossanese, O.W., Soderholm, J., Bevis, B.J., Sears, I.B., O'Connor, J., Williamson, E.K., Glick, B.S., Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae (1999) J. Cell Biol., 145 (1), pp. 69-81; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis (1986) J. 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Virol., 73 (7), pp. 5957-5969; Sims, A.C., Ostermann, J., Denison, M.R., Mouse hepatitis virus replicase proteins associate with two distinct populations of intracellular membranes (2000) J. Virol., 74, pp. 5647-5654; Thyberg, J., Moskalewski, S., Role of microtubules in the organization of the Golgi complex (1999) Exp. Cell Res., 246, pp. 263-279; Van der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J., Locker, J.K., Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73 (9), pp. 7641-7657; Westaway, E.G., Mackenzie, J.M., Kenney, M.T., Jones, M.K., Khromykh, A.A., Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures (1997) J. Virol., 71 (9), pp. 6650-6661; White, J., Johannes, L., Mallard, F., Girod, A., Grill, S., Reinsch, S., Keller, R., Stelzer, E.H., Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells (1999) J. Cell Biol., 147 (4), pp. 743-760. , Published erratum appears in J. Cell Biol. 2000, 148(1); Ziebubr, J., Siddell, S.G., Processing of the human corona-virus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185","Denison, M.R.; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232-2581, United States; email: mark.denison@mcmail.vanderbilt.edu",,"Academic Press Inc.",00426822,,VIRLA,"11414802","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0035918981
"Gélinas A.-M., Boutin M., Sasseville A.M.-J., Dea S.","6602090251;7003272229;6603215910;7006056287;","Bovine coronaviruses associated with enteric and respiratory diseases in Canadian dairy cattle display different reactivities to anti-HE monoclonal antibodies and distinct amino acid changes in their HE, S and ns4.9 protein",2001,"Virus Research","76","1",,"43","57",,33,"10.1016/S0168-1702(01)00243-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343773064&doi=10.1016%2fS0168-1702%2801%2900243-X&partnerID=40&md5=2aa6b171a8eef400e64c2c2e35e68002","Centre de Microbiologie and Biotechnologie, INRS-Institut Armand Frappier, Université du Québec, 531 boulevard des Prairies, Laval, QC, H7V 1B7, Canada","Gélinas, A.-M., Centre de Microbiologie and Biotechnologie, INRS-Institut Armand Frappier, Université du Québec, 531 boulevard des Prairies, Laval, QC, H7V 1B7, Canada; Boutin, M., Centre de Microbiologie and Biotechnologie, INRS-Institut Armand Frappier, Université du Québec, 531 boulevard des Prairies, Laval, QC, H7V 1B7, Canada; Sasseville, A.M.-J., Centre de Microbiologie and Biotechnologie, INRS-Institut Armand Frappier, Université du Québec, 531 boulevard des Prairies, Laval, QC, H7V 1B7, Canada; Dea, S., Centre de Microbiologie and Biotechnologie, INRS-Institut Armand Frappier, Université du Québec, 531 boulevard des Prairies, Laval, QC, H7V 1B7, Canada","Bovine coronavirus isolates associated with recent outbreaks of respiratory disease in Ontario and Quebec dairy farms were compared to reference strains known to be responsible for neonatal calf diarrhea (NCD) or winter dysentery (WD) of adult cattle. In respect to their hemagglutinating properties and their higher RDE activities with rat erythrocytes, WDBCoV strains differed from NCDBCoV strains and respiratory bovine coronaviruses RBCoV strains. Serologically, three MAbs directed to the HE glycoprotein of the WDBCoV strain BCQ.2590 recognized two serogroups amongst NCDBCoV strains by hemagglutination inhibition, whereas only one of the MAbs failed to react toward three of the four RBCoV isolates tested. Sequencing analysis of the S (S1 portion), HE, ORF4 and ORF5 genes of BCoV isolates associated with different clinical syndromes indicated that neither insertions or deletions could explain their distinct tropism. For the HE glycoprotein, a total of 15 amino acids (aa) substitutions were identified by comparing field isolates to the prototype Mebus strain. Two specific proline substitutions were identified for virulent strains being located in the signal peptides (aa 5) and aa position 367; one specific aa change was revealed at position 66 for RBCoV field isolates. Analysis of the S1 portion of the S glycoprotein revealed a total of eight aa changes specific to enteropathogenic (EBCoV) strains and eight aa changes specific to RBCoV strains. For all BCoV isolates studied, the region located between the S and M genes (ORF4) apparently encodes for two non-structural (ns) proteins of 4.9 and 4.8 kDa. A specific non-sense mutation was identified for the nucleotide at position 88 of the putative 4.9 kDa protein gene of RBCoV isolates resulting in 29 rather that 43 aa residues. The ORF5, which encodes a 12.7 ns protein and the 9.5 kDa E protein, was highly conserved amongst the BCoV field isolates. © 2001 Elsevier Science B.V.","Antigenic and genomic variability; Bovine enteropathogenic and respiratory coronaviruses; Esterase; Hemagglutinin; Monoclonal antibodies; Structural proteins; Winter dysentery","amino acid; monoclonal antibody; proline; signal peptide; structural protein; virus glycoprotein; amino acid substitution; article; Canada; cattle disease; controlled study; Coronavirus; enzyme activity; erythrocyte; gene deletion; gene insertion; gene sequence; genetic code; genetic conservation; hemagglutination inhibition; nonhuman; nonsense mutation; nucleotide sequence; priority journal; strain difference; virus hemagglutination; virus isolation; virus reactivation; virus strain; virus virulence; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Canada; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Cross Reactions; Diarrhea; Dysentery; Hemagglutinins, Viral; Mice; Milk; Molecular Sequence Data; Mutation, Missense; Reverse Transcriptase Polymerase Chain Reaction; Viral Proteins; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7 and 9.5 kDa encoded between the spike and membrane protien genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; Allende, R., Lewis, T.L., Lu, Z., Rock, D.L., Kutish, G.F., Ali, A., Doster, A.R., Osario, F.A., North American and European porcine reproductive and respiratory syndrome viruses differ in non-structural protein coding regions (1999) J. 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"O'Connor A., Martin S.W., Nagy E., Menzies P., Harland R.","57028928200;7404840647;57203079361;6701578867;7103070905;","The relationship between the occurrence of undifferentiated bovine respiratory disease and titer changes to bovine coronavirus and bovine viral diarrhea virus in 3 Ontario feedlots",2001,"Canadian Journal of Veterinary Research","65","3",,"137","142",,42,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035408474&partnerID=40&md5=efb9c80aac54d4028be98183b4faa5da","Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Novartis Animal Health Inc., University of Guelph Research Park, Stone Road, Guelph, Ont. N1G 2W1, Canada; Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States","O'Connor, A., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Martin, S.W., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Nagy, E., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Menzies, P., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Harland, R., Novartis Animal Health Inc., University of Guelph Research Park, Stone Road, Guelph, Ont. N1G 2W1, Canada","Serological evidence of previous viral exposure (titer at arrival) and current viral exposure (titer increase) during a 28-day study period, was used to determine if bovine coronavirus (BCV) or bovine viral diarrhea virus (BVDV) was associated with the occurrence of undifferentiated bovine respiratory disease (UBRD) in feedlot calves. Neutralizing antibody titers to BCV and BVDV were determined for 852 animals from 3 Ontario feedlots. Calves at 2 of the 3 feedlots (n = 753) received a modified live 4-way viral vaccine containing BVDV. On arrival at the feedlots, 90% of animals were seropositive for BCV, while 39% of animals were seropositive for BVDV. This evidence of previous exposure to both viruses was associated with reduced subsequent UBRD risk. Evidence of exposure to BCV during the study period was common, as 50% of animals showed a 16-fold or greater titer increase; however, treatment for UBRD was not associated with titer change. Although the majority of animals were vaccinated for BVDV at arrival, within a feedlot, animals treated for UBRD had larger titer increases to BVDV than non-treated animals. Based on our findings we infer that BCV was not causally related to UBRD occurrence, however consistent with other literature, BVDV may be causally related to UBRD occurrence.",,"virus antibody; virus vaccine; animal; animal disease; article; blood; Bovine diarrhea virus; cattle; cattle disease; Coronavirus; epidemiology; female; immunology; longitudinal study; male; respiratory tract infection; virology; virus infection; virus load; Animals; Antibodies, Viral; Bovine Virus Diarrhea-Mucosal Disease; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea Viruses, Bovine Viral; Female; Longitudinal Studies; Male; Respiratory Tract Infections; Seroepidemiologic Studies; Viral Load; Viral Vaccines","Storz, J., Purdy, C., Lin, X.B.M., Isolation of respiratory bovine coronavirus, other cytocidal virus, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J Am Vet Med Assoc, 216, pp. 1599-1604; Carman, P.S., Hazlett, M.J., Bovine coronavirus infection in Ontario, 1990-1991 (1992) Can Vet J, 33, pp. 812-814; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1455; Martin, S.W., Nagy, E., Shewen, P.E., Harland, R.J., The association of titers to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261; Perino, L.J., Apley, M.D., Clinical trial design in feedlots (1998) Vet Clin North Am Food Anim Pract, 14, pp. 343-366; Shewen, P.E., Wilkie, B.N., Vaccination of calves with leukotoxin culture supernatant from Pasteurella haemolytica (1988) Can J Vet Res, 52, pp. 30-36; Martin, S.W., Harland, R.J., Bateman, K.G., Nagy, E., The association of titers to Haemophilus somnus, and other putative pathogens, with the occurrence of bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 262-267; Thrusfield, M., (1995) Veterinary Epidemiology, , Don Mills, Ontario: Blackwell Science Ltd; Maldonado, G., Greenland, S., Simulation study of confounder-selection strategies (1993) Am J Epidemiol, 138, pp. 923-936; Ganaba, R., Belanger, D., Dea, S., Bigras-Poulin, M., A seroepide-miological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from northwestern Quebec (1995) Can J Vet Res, 59, pp. 26-33; Crouch, C.F., Acres, S.D., Prevalence of rotavirus and coronavirus antigens in the feces of normal cows (1984) Can J Comp Med, 48, pp. 340-342; Martin, S.W., Bateman, K.G., Shewen, P.E., Rosendal, S., Bohac, J.E., The frequency, distribution and effects of antibodies, to 7 putative respiratory pathogens, on respiratory disease and weight gain in feedlot calves in Ontario (1989) Can J Vet Res, 53, pp. 355-362; Martin, S.W., Nagy, E., Armstrong, D., Rosendal, S., The associations of viral and myocplasmal antibody titers with respiratory disease and weight gain in feedlot calves (1999) Can Vet J, 40, pp. 560-567; Booker, C.W., Guichon, P.T., Jim, G.K., Schunicht, O.C., Harland, R.J., Morley, P.S., Seroepidemiology of undifferentiated fever in feedlot calves in western Canada (1999) Can Vet J, 40, pp. 40-48; Storz, J., XiaoQing, L., Purdy, C.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans criteria for causation (2000) J Clin Microbiol, 38, pp. 3291-3298; Taylor, L.F., Van Donkersgoed, J., Dubovi, E.J., The prevalence of bovine viral diarrhea virus infection in a population of feedlot calves in western Canada (1995) Can J Vet Res, 59, pp. 87-93; Kleinbaum, D.G., Kupper, L.L., Morganstern, H., (1982) Epidemiological Research, Principals and Quantitative Methods, , New York Von Nostrand Reinhold International Company Ltd; Greenland, S., The effect of misclassification in the presence of covariates (1980) Am J Epidemiol, 112, pp. 564-569; Marshall, J.R., Hastrup, J.L., Mismeasurement and resonance of strong confounders: Uncorrelated errors (1996) Am J Epidemiol, 143, pp. 1069-1078; Jacobson, R.H., Validation of serological assays for diagnosis of infectious diseases (1998) Rev Sci Tech Off Int Epiz, 17, pp. 469-486; Potgieter, L.N., Bovine respiratory tract disease caused by bovine viral diarrhea virus (1997) Vet Clin North Am Food Anim Pract, 13, pp. 471-481; Potgieter, L.N., Immunology of bovine viral diarrhea virus (1995) Vet Clin North Am Food Anim Pract, 11, pp. 501-520; Martin, S.W., Bohac, J.G., The association between serological titers in infectious bovine rhinotracheitis virus, bovine viral diarrhea virus, parainfluenza-3 virus, respiratory syncytial virus and treatment for respiratory disease in Ontario feedlot calves (1986) Can J Vet Res, 50, pp. 351-358","O'Connor, A.; Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; email: oconnor@iastate.edu",,,08309000,,CJVRE,"11480517","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0035408474
"O'Connor A., Martin S.W., Nagy E., Menzies P., Harland R.","57028928200;7404840647;57203079361;6701578867;7103070905;","The relationship between the occurrence of undifferentiated bovine respiratory disease and titer changes to Haemophilus somnus and Mannheimia haemolytica at 3 Ontario feedlots",2001,"Canadian Journal of Veterinary Research","65","3",,"143","150",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035408428&partnerID=40&md5=75915aa2f80c99b6944e0096a33ecbe6","Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Novartis Animal Health Inc., University of Guelph, Research Park, Stone Road, Guelph, Ont. N1G 2W1, Canada; Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States","O'Connor, A., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada, Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; Martin, S.W., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Nagy, E., Department of Pathobiology, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Menzies, P., Department of Population Medicine, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Harland, R., Novartis Animal Health Inc., University of Guelph, Research Park, Stone Road, Guelph, Ont. N1G 2W1, Canada","The association between exposure to Haemophilus somnus and Mannheimia haemolytica (formerly Pasteurella haemolytica) and the risk of undifferentiated bovine respiratory disease (UBRD) was investigated using serological evidence of exposure coupled with a factorial design vaccine field trial. Measures of previous exposure (titer at arrival) and current exposure (titer increase in the study period) to these agents were used. The vaccine field trial involved systematic allocation of animals into groups that received either a M. haemolytica vaccine, an H. somnus vaccine, a combined M. haemolytica and H. somnus vaccine, and an unvaccinated control group. Serum was collected from the 852 animals enrolled to determine titers to H. somnus, M. haemolytica, bovine coronavirus and bovine viral diarrhea virus. Vaccination with H. somnus in combination with M. haemolytica and with M. haemolytica alone reduced the risk of UBRD. The odds ratio for vaccination with H. somnus alone and UBRD risk suggested some sparing effect, but the 95% confidence limits included unity. There was no association between serological evidence of concurrent exposure to M. haemolytica and UBRD occurrence. There was an association between titer change to H. somnus and UBRD risk. However, the association changed with time of BRD treatment; animals diagnosed and treated for UBRD on or after day 10 showed little evidence of exposure to H. somnus, despite evidence of natural H. somnus exposure in the unvaccinated group. The association between titer change to H. somnus and UBRD occurrence seen in this study may be a consequence of prolonged exposure to antibiotics, rather than a causal association.",,"antiinfective agent; bacterial vaccine; bacterium antibody; animal; animal disease; article; bacterial infection; blood; cattle; cattle disease; epidemiology; female; Gram negative infection; Haemophilus; immunology; male; Mannheimia haemolytica; microbiology; respiratory tract infection; risk factor; Animals; Anti-Bacterial Agents; Antibodies, Bacterial; Bacterial Vaccines; Cattle; Cattle Diseases; Female; Haemophilus; Haemophilus Infections; Male; Mannheimia haemolytica; Pasteurella Infections; Respiratory Tract Infections; Risk Factors; Seroepidemiologic Studies","Martin, S.W., Harland, R.J., Bateman, K.G., Nagy, E., The association of titers to Haemophilus somnus, and other putative pathogens, with the occurrence of bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 262-267; Booker, C.W., Guichon, P.T., Jim, G.K., Schunicht, O.C., Harland, R.J., Morley, P.S., Seroepidemiology of undifferentiated fever in feedlot calves in western Canada (1999) Can Vet J, 40, pp. 40-48; Martin, S.W., Nagy, E., Shewen, P.E., Harland, R.J., The association of titers to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261; Thrusfield, M., (1995) Veterinary Epidemiology, , Don Mills, Ontario: Blackwell Science Ltd; Shewen, P.E., Wilkie, B.N., Vaccination of calves with leukotoxin culture supernatant from Pasteurella hemolytica (1988) Can J Vet Res, 52, pp. 30-36; Kleinbaum, D.G., Kupper, L.L., Morganstern, H., (1982) Epidemiological Research, Principals and Quantitative Methods, , New York: Von Nostrand Reinhold International Company; Martin, S.W., Bateman, K.G., Shewen, P.E., Rosendal, S., Bohac, J.E., The frequency, distribution and effects of antibodies, to seven putative respiratory pathogens, on respiratory disease and weight gain in feedlot calves in Ontario (1989) Can J Vet Res, 53, pp. 355-362; Shewen, P.E., Host response to infection with HAP: Implications for vaccine development (1995) Haemophilus, Actinobacillus and Pasteurella, , Donachie W, Lainson F, Hodgson JC, eds. New York: Plenum Press; Hodgins, D.C., Shewen, P.E., Vaccination of neonatal colostrumdeprived calves against Pasteurella haemolytica A1 (2000) Can J Vet Res, 64, pp. 3-8; Jacobson, R.H., Validation of serological assays for diagnosis of infectious diseases (1998) Rev Sci Tech Off Int Epiz, 17, pp. 469-486; Marshall, J.R., Hastrup, J.L., Mismeasurement and resonance of strong confounders: Uncorrelated errors (1996) Am J Epidemiol, 143, pp. 1069-1078; Greenland, S., The effect of misclassification in the presence of covariates (1980) Am J Epidemiol, 112, pp. 564-569; Martin, S.W., Nagy, E., Armstrong, D., Rosendal, S., The associations of viral and myocplasmal antibody titers with respiratory disease and weight gain in feedlot calves (1999) Can Vet J, 40, pp. 560-567","O'Connor, A.; Dept. Vet. Diagn. Prod. Anim. Med., Iowa State University, Ames, IA 50011-1250, United States; email: oconnor@iastate.edu",,,08309000,,CJVRE,"11480518","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0035408428
"Kipar A., Kremendahl J., Jackson M.L., Reinacher M.","7004576445;6507138764;7404069137;7003284148;","Comparative Examination of Cats with Feline Leukemia Virus-associated Enteritis and Other Relevant Forms of Feline Enteritis",2001,"Veterinary Pathology","38","4",,"359","371",,21,"10.1354/vp.38-4-359","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035403798&doi=10.1354%2fvp.38-4-359&partnerID=40&md5=d6347970064aa22fa142c91e8e3acfc7","Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Giessen, Germany; Veterinary Practice for Cats, Wuppertal-Cronenberg, Germany; Department of Veterinary Pathology, W. College of Veterinary Medicine, University of Saskatchewan, Saskatoon, Sask., Canada; Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Frankfurter Strasse 96, D-35392 Giessen, Germany","Kipar, A., Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Giessen, Germany, Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Frankfurter Strasse 96, D-35392 Giessen, Germany; Kremendahl, J., Veterinary Practice for Cats, Wuppertal-Cronenberg, Germany; Jackson, M.L., Department of Veterinary Pathology, W. College of Veterinary Medicine, University of Saskatchewan, Saskatoon, Sask., Canada; Reinacher, M., Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Giessen, Germany","Cats with feline leukemia virus (FeLV)-associated enteritis (FAE), enteritis of other known viral etiology (parvovirus [PV], enteric coronavirus [CoV]), and enteritis of unknown etiology with histologic features similar to those of FAE and PV enteritis (EUE) and FeLV-negative and FeLV-positive cats without enterocyte alterations were examined. Amount and types of infiltrating leukocytes in the jejunum and activity and cellular constituents of mesenteric lymph nodes, spleen, and bone marrow were determined. PV and CoV infections were confirmed by immunohistologic demonstration of PV and CoV antigen, ultrastructural demonstration of viral particles in the intestinal content, and in situ hybridization for PV genome. FeLV infection was detected by immunohistology for gp70, p27, and p15E. Latent FeLV infection was excluded by polymerase chain reaction methods for exogenous FeLV DNA. Enterocyte lesions involved the crypts in cats with PV enteritis, FAE, and EUE and the villous tips in cats with CoV enteritis. Inflammatory infiltration was generally dominated by mononuclear cells and was moderate in the unaltered intestine and in cats with PV enteritis and marked in cats with FAE, CoV enteritis, and EUE. In cats with EUE, myeloid/histiocyte antigen-positive macrophages were relatively numerous, suggesting recruitment of peripheral blood monocytes. Lymphoid tissues were depleted in cats with PV enteritis and with EUE but were normal or hyperplastic in cats with FAE. Bone marrow activity was decreased in cats with PV enteritis; in cats with FAE or EUE and in FeLV-positive cats without enterocyte alterations, activity was slightly increased. In cats with FAE and PV enteritis, a T-cell-dominated response prevailed. EUE showed some parallels to human inflammatory bowel disease, indicating a potential harmful effect of infiltrating macrophages on the intestinal epithelium.","Cats; Coronavirus; Enteritis; FeLV; Immunohistology; In situ hybridization; Inflammatory bowel disease; Leukocytes; Parvovirus; Polymerase chain reaction","virus DNA; animal; animal disease; article; bone marrow; cat; cat disease; chemistry; comparative study; Coronavirus; electron microscopy; enteritis; Feline leukemia virus; Feline panleukopenia virus; female; genetics; immunohistochemistry; in situ hybridization; isolation and purification; jejunum; lymph node; male; pathology; polymerase chain reaction; retrospective study; Retrovirus infection; spleen; ultrastructure; virology; virus infection; Animals; Bone Marrow; Cat Diseases; Cats; Coronavirus; Coronavirus Infections; DNA, Viral; Enteritis; Feline panleukopenia virus; Female; Immunohistochemistry; In Situ Hybridization; Jejunum; Leukemia Virus, Feline; Lymph Nodes; Male; Microscopy, Electron; Parvoviridae Infections; Polymerase Chain Reaction; Retrospective Studies; Retroviridae Infections; Spleen; Tumor Virus Infections","Arens, M., Krauss, H., Detection of parvovirus in dogs with acute gastroenteritis (1980) Berl Münch Tierärztl Wochenschr, 93, pp. 156-157; Barker, I.K., Van Dreumel, A.A., Palmer, N., The alimentary system (1993) Pathology of Domestic Animals, pp. 106-199. , ed. Jubb KVF, Kennedy PC, and Palmer N, 4th ed., Academic Press, San Diego, CA; Beebe, A.M., Dua, N., Faith, T.G., Moore, P.F., Pedersen, N.C., Dandekar, S., Primary stage of feline immunodeficiency virus infection: Viral dissemination and cellular targets (1994) J Virol, 68, pp. 3080-3091; Bjerke, K., Halstensen, T.S., Jahnsen, F., Pulford, K., Brandtzaeg, P., Distribution of macrophages and granulocytes expressing L1 protein (calprotectin) in human Peyer's patches compared with normal ileal lamina propria and mesenteric lymph nodes (1993) Gut, 34, pp. 1357-1363; Brandtzaeg, P., Gabrielsen, T.O., Dale, I., Miller, F., Steinbakk, M., Fagerhol, M.K., The leucocyte protein L1 (calprotectin): A putative nonspecific defence factor at epithelial surfaces (1995) Adv Exp Med Biol, 371 A, pp. 201-206; Breuer, W., Stahr, H., Majzoub, M., Hermanns, W., Bone marrow changes in infectious diseases and lymphohaemopoietic neoplasias in dogs and cats - A retrospective study (1998) J Comp Pathol, 119, pp. 57-66; Brown, P.J., Hopper, C.D., Harbour, D.A., Pathological features of lymphoid tissues in cats with natural feline immunodeficiercy virus infection (1991) J Comp Pathol, 104, pp. 345-355; Carlson, J.H., Scott, F.W., Duncan, J.R., Feline panleukopenia. 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Pathogenesis in germfree and specific pathogen-free cats (1977) Vet Patiol, 14, pp. 79-88; Casey, J.W., Roach, A., Mullins, J.J., Bauman Burck, K., Nicolson, M.O., Gardner, M.B., Davidson, N., The U3 portion of feline leukemia virus DNA identifies horizontally acquired proviruses in leukemic cats (1981) Proc Natl Acad Sci USA, 78, pp. 7778-7782; Coffman, R.L., Weissman, I.L., B220: A B cell-specific member of the T200 glycoprotein family (1981) Nature, 289, pp. 681-683; Dale, I., Fagerhol, M.K., Naesgard, I., Purification and partial characterization of highly immunogenic human leukocyte protein, the L1 antigen (1983) Eur J Biochem, 134, pp. 1-6; Domingo, M., Einig, C., Eigenbrodt, E., Reinacher, M., Immunohistological demonstration of pyruvate kinase isoenzyme type L in rat with monoclonal antibodies (1986) J Histochem Cytochem, 40, pp. 665-673; Donahue, P.R., Quackenbush, S.L., Gallo, M.V., DeNoronha, C.M.C., Overbaugh, J., Hoover, E.A., Mullins, J.I., Viral genetic determinants of T-cell killing and immunodeficiency disease induction by the feline leukemia virus FeLV-FAIDS (1991) J Virol, 65, pp. 4461-4469; Flavell, D.J., Jones, D.B., Wright, D.H., Identification of tissue histiocytes on paraffin sections by a new monoclonal antibody (1987) J Histochem Cytochem, 35, pp. 1217-1226; Harbour, D.A., Feline enteric viral infections (1998) Infectious Diseases of the Dog and Cat, pp. 69-71. , ed. 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Philadelphia, PA; Hardy W.D., Jr., Feline leukemia virus non-neoplastic diseases (1981) J Am Anim Hosp Assoc, 17, pp. 941-949; Hardy W.D., Jr., Immunopathology induced by feline leukemia virus (1982) Springer Semin Immunopathol, 5, pp. 75-106; Hart, J.R., Shaker, E., Patnaik, A.K., Garvey, M.S., Lymphocytic-plasmacytic enterocolitis in cats: 60 cases (1988-1990) (1994) J Am Anim Hosp Assoc, 30, pp. 505-514; Hoover, E.A., Mullins, J.I., Quackenbush, S.L., Gasper, P.W., Experimental transmission and pathogenesis of immunodeficiency syndrome in cats (1987) Blood, 70, pp. 1880-1882; Hoshino, Y., Scott, F.W., Coronavirus-like particles in the faeces of normal cats (1980) Arch Virol, 63, pp. 147-152; Jackson, M.L., Haines, D.M., Meric, S.M., Misra, V., Feline leukemia virus detection by immunohistochemistry and polymerase chain reaction in formalin-fixed, paraffin-embedded tumor tissue from cats with lymphosarcoma (1993) Can J Vet Res, 57, pp. 269-276; Jergens, A.E., Feline idiopathic inflammatory bowel disease (1992) Compend Cont Educ Small Anim Pract, 14, pp. 509-518; Kipar, A., Bellmann, S., Gunn-Moore, D.A., Leukert, W., Köhler, K., Menger, S., Reinacher, M., Histopathological alterations of lymphatic tissues in cats without feline infectious peritonitis after long-term exposure to FIP virus (1999) Vet Microbiol, 69, pp. 131-137; Kipar, A., Bellmann, S., Kremendahl, J., Köhler, K., Reinacher, M., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions of feline infectious peritonitis (1998) Vet Immunol Immunopathol, 65, pp. 243-257; Kipar, A., Kremendahl, J., Addie, D.D., Leukert, W., Grant, C.K., Reinacher, M., Fatal enteritis associated with coronavirus infection in cats (1998) J Comp Pathol, 119, pp. 1-14; Kipar, A., Kremendahl, J., Grant, C.K., Von Bothmer, I., Reinacher, M., Expression of viral proteins in feline leukemia virus-associated enteritis (2000) Vet Pathol, 37, pp. 129-136; Kovacevic, S., Kipar, A., Kremendahl, J., Teebken-Schuler, D., Grant, C.K., Reinacher, M., Immunohistochemical diagnosis of feline leukemia virus infection in formalin-fixed tissue (1997) Eur J Vet Pathol, 3, pp. 13-19; Langheinrich, K.A., Nielsen, S.W., Histopathology of feline panleukopenia: Report of 65 cases (1971) J Am Vet Med Assoc, 158, pp. 863-872; Larsen, S., Flagstad, A., Aalbaek, B., Experimental feline panleucopenia in the conventional cat (1976) Vet Pathol, 13, pp. 216-240; Luna, L.G., (1968) Manual of Histologic Staining Methods of the Armed Forces Institute of Pathology, 3rd Ed., , McGraw-Hill, New York, NY; Lutz, H., Castelli, I., Ehrensperger, F., Pospischil, A., Rosskopf, M., Siegl, G., Grob, M., Martinod, S., Panleukopenia-like syndrome of FeLV caused by co-infection with FeLV and feline panleukopenia virus (1995) Vet Immunol Immunopathol, 46, pp. 21-33; Mahida, Y.R., Wu, K.C., Jewell, D.P., Respiratory burst activity of intestinal macrophages in normal and inflammatory bowel disease (1989) Gut, 30, pp. 1362-1370; McClane, S.J., Rombeau, J.L., Cytokines and inflammatory bowel disease: A review (1999) J Parenter Enteral Nutr, 23, pp. S20-S24; Monteith, C.E., Chelack, B.J., Davis, W.C., Haines, D.M., Identification of monoclonal antibodies for immunohistochemical staining of feline B lymphocytes in frozen and formalin-fixed paraffin-embedded tissues (1996) Can J Vet Res, 60, pp. 193-198; Pallaske, G., Schmiedel, E., (1959) Pathologisch-Histologische Technik, p. 184. , Paul Parey Verlag; Papasouliotis, K., Gruffydd-Jones, T.J., Werrett, G., Brown, P.J., Hopper, C.D., Stokes, C.R., Harbour, D.A., Assessment of intestinal function in cats with chronic diarrhea after infection with feline immunodeficiency virus (1998) Am J Vet Res, 59, pp. 569-574; Papasouliotis, K., Sparkes, A.H., Werret, G., Egan, K., Gruffydd-Jones, E.A., Gruffydd-Jones, T.J., Assessment of the bacterial flora of the proximal part of the small intestine in healthy cats, and the effect of sample collection method (1998) Am J Vet Res, 59, pp. 48-51; Pedersen, N.C., Feline infectious peritonitis and feline enteric coronavirus infections. 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Med. Diss., Institut für Veterinär-Pathologie, Justus-Liebig-Universität, Giessen, Germany; Strombeck, D.R., Microflora of the gastrointestinal tract and its symbiotic relationship with the host (1996) Strombeck's Small Animal Gastroenterology, pp. 14-19. , ed. Guilford WG, Center SA. Strombeck DR, Williams DA, and Meyer DJ, 3rd ed., WB Saunders, Philadelphia, PA; Sturgess, C.P., Gruffydd-Jones, T.J., Stokes, C.R., Prevalence of leukocyte subsets within the feline colon: A CD8, IgG & IgA dominated environment (1998) Synopses Br Small Amim Vet Assoc Congr, 41; Waldvogel, A.S., Hassam, S., Stoerckle, N., Weilenmann, R., Tratschin, J.D., Siegl, G., Pospischil, A., Specific diagnosis of parvovirus enteritis in dogs and cats by in situ hybridization (1992) J Comp Pathol, 107, pp. 141-146; Yamasaki, K., Suematsu, H., Takahashi, T., Comparison of gastric and duodenal lesions in dogs with and without lymphocytic-plasmacytic enteritis (1996) J Am Vet Med Assoc, 209, pp. 95-97","Kipar, A.; Inst. F. Veterinär-Pathologie, Justus-Liebig-Univ. Giessen, Frankfurter Strasse 96, D-35392 Giessen, Germany; email: anja.kipar@vetmed.uni-giessen.de",,,03009858,,VTPHA,"11467470","English","Vet. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0035403798
"Dandekar A.A., Wu G.F., Pewe L., Perlman S.","7005818765;7404976255;6603143496;7102708317;","Axonal damage is T cell mediated and occurs concomitantly with demyelination in mice infected with a neurotropic coronavirus",2001,"Journal of Virology","75","13",,"6115","6120",,56,"10.1128/JVI.75.13.6115-6120.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034978123&doi=10.1128%2fJVI.75.13.6115-6120.2001&partnerID=40&md5=0d052b0d1817cebe1019d7df3a14c17b","Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States","Dandekar, A.A., Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States; Wu, G.F., Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States; Pewe, L., Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States","Mice infected with mouse hepatitis virus (MHV) strain JHM develop primary demyelination. Herein we show that axonal damage occurred in areas of demyelination and also in adjacent areas devoid of myelin damage. Immunodeficient MHV-infected RAG1-/- mice (mice defective in recombinase activating gene 1 expression) do not develop demyelination unless they receive splenocytes from a mouse previously immunized against MHV (G. F. Wu, A. Dandekar, L. Pewe, and S. Perlman, J. Immunol. 165:2278-2286, 2000). In the present study, we show that adoptive transfer oft cells was also required for the majority of the axonal injury observed in these animals. Both demyelination and axonal damage were apparent by 7 days posttransfer. Recent data suggest that axonal injury is a major factor in the long-term disability observed in patients with multiple sclerosis. Our data demonstrate that immune system-mediated damage to axons is also a common feature in mice with MHV-induced demyelination. Remarkably, there appeared to be a minimal, if any, interval of time between the appearance of demyelination and that of axonal injury.",,"recombinase; adoptive transfer; animal model; animal tissue; article; axonal injury; cellular immunity; demyelination; gene expression; mouse; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; priority journal; spleen cell; T lymphocyte; virus infection; Adoptive Transfer; Animals; Axons; Coronavirus Infections; Demyelinating Diseases; Homeodomain Proteins; Immunohistochemistry; Mice; Murine hepatitis virus; Neurofilament Proteins; Spinal Cord; T-Lymphocytes","Arnold, D.L., Magnetic resonance spectroscopy: Imaging axonal damage in MS (1999) J. Neuroimmunol., 98, pp. 2-6; Bailey, O., Pappenheimer, A.M., Cheever, F.S., Daniels, J.B., A marine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin (1949) J. Exp. 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Neurosci., 7, pp. 3474-3488; McGavern, D.B., Murray, P.D., Rivera-Quinones, C., Schmelzer, J.D., Low, P.A., Rodriguez, M., Axonal loss results in spinal cord atrophy, electrophysiological abnormalities and neurological deficits following demyelination in a chronic inflammatory model of multiple sclerosis (2000) Brain, 123, pp. 519-531; Noseworthy, J.H., Progress in determining the causes and treatment of multiple sclerosis (1999) Nature, 399, pp. A40-A47; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating encephalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog., 2, pp. 185-194; Raine, C.S., Cross, A.H., Axonal dystrophy as a consequence of long-term demyelination (1989) Lab. 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John Wiley & Sons, Ltd., New York, N.Y; Stohlman, S.A., Weiner, L.P., Chronic central nervous system demyelination in mice after JHM virus infection (1981) Neurology, 31, pp. 38-44; Storch, M., Lassmann, H., Pathology and pathogenesis of demyelinating diseases (1997) Curr. Opin. Neurol., 10, pp. 186-192; Sun, N., Grzyhicki, D., Castro, R., Murphy, S., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Trapp, B., Peterson, J., Ransohoff, R., Rudick, R., Monk, S., Bo, L., Axonal transection in the lesions of multiple sclerosis (1998) N. Engl. J. Med., 338, pp. 278-285; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Wu, G., Dandekar, A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286; Wu, G.F., Perlman, S., Macrophage infiltration, but not apoptosis, is correlated with immune-mediated demyelination following murine infection with a neurotropic coronavirus (1999) J. Virol., 73, pp. 8771-8780; Xue, S., Sun, N., Van Rooijen, N., Perlman, S., Depletion of blood-borne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus (1999) J. Virol., 73, pp. 6327-6334","Perlman, S.; Department of Pediatrics, 2042 Medical Laboratories, University of Iowa, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"11390613","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034978123
"Thiel V., Herold J., Schelle B., Siddell S.G.","35238592100;7006838690;6602866326;7005260816;","Viral replicase gene products suffice for coronavirus discontinuous transcription",2001,"Journal of Virology","75","14",,"6676","6681",,86,"10.1128/JVI.75.14.6676-6681.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034990084&doi=10.1128%2fJVI.75.14.6676-6681.2001&partnerID=40&md5=efd697488b428c1ba696b31a2def3548","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Thiel, V., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Herold, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Schelle, B., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Siddell, S.G., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","We have used vaccinia virus as a vector to clone a 22.5-kbp cDNA that represents the 5′ and 3′ ends of the human coronavirus 229E (HCoV 229E) genome, the HCoV 229E replicase gene, and a single reporter gene (coding for green fluorescent protein [GFP]) located downstream of a regulatory element for coronavirus mRNA transcription. When RNA transcribed from this cDNA was transfected into BHK-21 cells, a small percentage of cells displayed strong fluorescence. A region of the mRNA encoding GFP was amplified by PCR and shown to have the unique mRNA leader-body junction indicative of coronavirus-mediated transcription. These data show that the coronavirus replicase gene products suffice for discontinuous subgenomic mRNA transcription.",,"gene product; green fluorescent protein; RNA directed RNA polymerase; signal peptide; virus vector; article; Coronavirus; polymerase chain reaction; priority journal; protein processing; RNA transcription; virus genome; virus replication; virus transcription; Coronavirus; Coronavirus 229E, Human; Genetic Vectors; RNA Replicase; RNA, Messenger; RNA, Viral; Transcription, Genetic; Transfection; Vaccinia virus","Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic Sindbis virus RNA vectors for heterologous gene expression (1998) Proc. 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Virol., 8, pp. 33-47; Diez, J., Ishikawa, M., Kaido, M., Ahlquist, P., Identification and characterization of a host protein required for efficient template selection in viral RNA replication (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 3913-3918; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Herold, J., Andino, R., Poliovirus RNA replication requires genome circularization through a protein-protein bridge (2001) Mol. Cell, 7, pp. 581-591; Heusipp, G., Harms, U., Siddell, S.G., Ziebuhr, J., Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E (1997) J. Virol., 71, pp. 5631-5634; Hsue, B., Masters, P.S., Insertion of a new transcriptional unit into the genome of mouse hepatitis virus (1999) J. Virol., 73, pp. 6128-6135; Kim, K.H., Makino, S., Two murine coronavirus genes suffice for viral RNA synthesis (1995) J. Virol., 69, pp. 2313-2321; Kuo, L., Godeke, G.J., Raamsman, M.J.B., Masters, P.S., Rottier, P.J.M., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lohmann, V., Korner, F., Koch, J., Herian, U., Theilmann, L., Bartenschlager, R., Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line (1999) Science, 285, pp. 110-113; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. 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Biol., 440, pp. 215-219; Seybert, A., Hegyi, A., Siddell, S.G., Ziebuhr, J., The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity (2000) RNA, 6, pp. 1056-1068; Siddell, S.G., Snijder, E.J., Coronaviruses, toroviruses and arteriviruses (1998) Topley & Wilson's microbiology and microbial infections, 9th ed., pp. 463-484. , B. W. J. Mahy and L. Collier (ed.), Arnold, London, United Kingdom; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S.B., Van der Zeijst, A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Stohlman, S.A., Baric, R.S., Nelson, G.N., Soe, L.H., Welter, L.M., Deans, R.J., Specific interaction between coronavirus leader RNA and nucleocapsid protein (1988) J. Virol., 62, pp. 4288-4295; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Thiel, V., Rashtchian, A., Herold, J., Schuster, D.M., Guan, N., Siddell, S.G., Effective amplification of 20-kb DNA by reverse transcription PCR (1997) Anal. Biochem., 252, pp. 62-70; Tijms, M.A., Van Dinten, L.C., Gorbalenya, A.E., Snijder, E.J., A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 1889-1894; Van der Most, R.G., De Groot, R.J., Spaan, W.J., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Van Marle, G., Luytjes, W.R., Van der Most, G., Van der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879","Thiel, V.; Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; email: v.thiel@mail.uni-wuerzburg.de",,,0022538X,,JOVIA,"11413334","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034990084
"Liu C., Xu H.Y., Liu D.X.","55680711400;55703819800;8972667300;","Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus",2001,"Journal of Virology","75","14",,"6402","6409",,67,"10.1128/JVI.75.14.6402-6409.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034984605&doi=10.1128%2fJVI.75.14.6402-6409.2001&partnerID=40&md5=197301cd33e7b2a8262dfd162b0e2961","Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore 117406, Singapore","Liu, C., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore 117406, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore 117406, Singapore; Liu, D.X., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore 117406, Singapore","Avian coronavirus infectious bronchitis virus (IBV) is the causative agent of chicken infectious bronchitis, an acute, highly contagious viral respiratory disease. Replication of IBV in Vero cells causes extensive cytopathic effects (CPE), leading to destruction of the entire monolayer and the death of infected cells. In this study, we investigated the cell death processes during acute IBV infection and the underlying mechanisms. The results show that both necrosis and apoptosis may contribute to the death of infected cells in lytic IBV infection. Caspase-dependent apoptosis, as characterized by chromosomal condensation, DNA fragmentation, caspase-3 activation, and poly(ADP-ribose) polymerase degradation, was detected in IBV-infected Vero cells. Addition of the general caspase inhibitor z-VAD-FMK to the culture media showed inhibition of the hallmarks of apoptosis and increase of the release of virus to the culture media at 16 h postinfection. However, neither the necrotic process nor the productive replication of IBV in Vero cells was severely affected by the inhibition of apoptosis. Screening of 11 IBV-encoded proteins suggested that a 58-kDa mature cleavage product could induce apoptotic changes in cells transiently expressing the protein. This study adds one more example to the growing list of animal viruses that induce apoptosis during their replication cycles.",,"caspase; DNA fragment; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase; animal cell; apoptosis; article; Avian infectious bronchitis virus; chromosome condensation; controlled study; cytopathogenic effect; DNA transfection; enzyme activation; gene expression system; nonhuman; polyacrylamide gel electrophoresis; priority journal; Sindbis virus; Vero cell; virus replication; Western blotting; Amino Acid Chloromethyl Ketones; Animals; Apoptosis; Caspase 3; Caspases; Cercopithecus aethiops; Chromosomes; Cytopathogenic Effect, Viral; Eukaryotic Cells; Infectious bronchitis virus; Molecular Weight; Poly(ADP-ribose) Polymerases; Vero Cells; Viral Proteins","Agol, V.I., Belov, G.A., Bienz, K., Egger, D., Kolesnikova, M.S., Raikhlin, N.T., Romanova, L.I., Tolskaya, E.A., Two types of death of poliovirus-infected cell: Caspase involvement in the apoptosis but not cytopathic effect (1998) Virology, 252, pp. 343-353; An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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"Enjuanes L., Sola I., Almazan F., Ortego J., Izeta A., Gonzalez J.M., Alonso S., Sanchez J.M., Escors D., Calvo E., Riquelme C., Sanchez C.","7006565392;7003336781;6603712040;35254237800;6602523425;57201828108;57210695335;57212742351;6507259181;12801394500;7004010730;57193985365;","Coronavirus derived expression systems",2001,"Journal of Biotechnology","88","3",,"183","204",,33,"10.1016/S0168-1656(01)00281-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035850220&doi=10.1016%2fS0168-1656%2801%2900281-4&partnerID=40&md5=e64285fa5455270f795ad914ee66abdd","Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Enjuanes, L., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Almazan, F., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Ortego, J., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Gonzalez, J.M., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Alonso, S., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sanchez, J.M., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Escors, D., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Calvo, E., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Riquelme, C., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sanchez, C., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Both helper dependent expression systems, based on two components, and single genomes constructed by targeted recombination, or by using infectious cDNA clones, have been developed. The sequences that regulate transcription have been characterized mainly using helper dependent expression systems and it will now be possible to validate them using single genomes. The genome of coronaviruses has been engineered by modification of the infectious cDNA leading to an efficient (&gt; 20 μg ml-1) and stable (&gt; 20 passages) expression of the foreign gene. The possibility of engineering the tissue and species tropism to target expression to different organs and animal species, including humans, increases the potential of coronaviruses as vectors. 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"Pratelli A., Martella V., Elia G., Tempesta M., Guarda F., Capucchio M.T., Carmichael L.E., Buonavoglia C.","7004884960;7003300496;7005135633;7005599031;7004244347;6603584480;7101757988;7005623145;","Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus",2001,"Journal of Veterinary Medicine, Series B","48","5",,"385","392",,67,"10.1046/j.1439-0450.2001.00466.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034944483&doi=10.1046%2fj.1439-0450.2001.00466.x&partnerID=40&md5=7c6f2a01a38daf90834f05ace86738d9","Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy; Department of Animal Pathology, Faculty of Veterinary Medicine, Via Leonardo da Vinci 44, Torino, Italy; James A. Baker Institute for Animal Health, New York State College of Veterinary Medicine, Ithaca 14853, NY, United States; Department of Health and Animal Well-being, Faculty of Veterinary Medicine, University of Bari, Italy","Pratelli, A., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy, Department of Health and Animal Well-being, Faculty of Veterinary Medicine, University of Bari, Italy; Martella, V., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy; Elia, G., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy; Tempesta, M., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy; Guarda, F., Department of Animal Pathology, Faculty of Veterinary Medicine, Via Leonardo da Vinci 44, Torino, Italy; Capucchio, M.T., Department of Animal Pathology, Faculty of Veterinary Medicine, Via Leonardo da Vinci 44, Torino, Italy; Carmichael, L.E., James A. Baker Institute for Animal Health, New York State College of Veterinary Medicine, Ithaca 14853, NY, United States; Buonavoglia, C., Department of Health and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy","An outbreak of dual infection in dogs with canine adenovirus type 1 (CAV-1) and canine coronavirus (CCV) infection is reported in an animal shelter that comprised approximately 200 adults stray dogs and 30 puppies. Twenty puppies died 7-8 days after the onset of the clinical signs (severe enteritis, leucopoenia, respiratory distress and dehydration). Both CAV-1 and CCV were isolated from tissue or swab samples. Antibodies to CCV and, at high levels, to CAV-1 also were detected in several puppies. The principal histological findings were atrophy of small intestinal villi, lymphoid depletion, hepatitis and bronchopneumonia. The persistence of CCV in the faeces, observed by the polymerase chain reaction assay, was longer than previously reported. Results demonstrated the serious consequences which may occur with dual infections by CAV-1 and CCV in assembled groups of dogs that are housed in poorly managed kennels with inadequate vaccination programmes.",,"canine adenovirus; Coronavirus; day length; dog; environment; feces; intestine; kennel; mortality; persistence; polymerase chain reaction; vaccination; virus infection; Adenoviruses, Canine; Animals; Coronavirus Infections; Coronavirus, Canine; Disease Outbreaks; Dog Diseases; Dogs; Enteritis; Feces; Hepatitis, Infectious Canine; Italy; Polymerase Chain Reaction; Adenoviridae; Animalia; Canine adenovirus type 1; Canine coronavirus; Canis familiaris; Chicken anemia virus; Coronavirus; Human adenovirus type 1","Appel, M.J., Canine adenovirus type 1 (infectious canine hepatitis virus) (1987) Virus Infections of Vertebrates, Vol. I. Virus Infections of Carnivores, 1, pp. 29-43. , Horzinek, M. C. (series ed.), Elsevier Science Publishers, Amsterdam, The Netherlands; Appel, M.J., Canine coronavirus (1987) Virus Infections of Vertebrates, Vol. I. Virus Infections of Carnivores, 1, pp. 115-122. , Horzinek, M. C. (series ed.), Elsevier Science Publishers, Amsterdam, The Netherlands; Appel, M.J., Cooper, B.J., Greisen, H., Scott, F., Carmichael, L.E., Canine viral enteritis. I. Status report on corona- and parvo-like viral enteritides (1979) Cornell Vet., 69, pp. 123-133; Brunner, K.T., Scheitlin, M., Stunzi, H., Zum serologischen nachweis der hepatitis contagiosa canis (1951) Schweiz Arch. Tierheilk., 93, pp. 443-458; Buonavoglia, D., Ferrara, G., Marsilio, F., Cavalli, A., Voigt, V., Tipizzazione di uno stipite di adenovirus (1993) O.D.V., 10, pp. 39-41; Cabasso, V.J., Canine viruses. II. Infectious canine hepatitis and rabies control (1953) Southwest. Vet., 6, pp. 137-141; Evermann, J.F., Foreyt, W., Maag-Miller, L., Leathers, C.W., McKeirnan, A.J., LeaMaster, B., Acute hemorrhagic enteritis associated with canine coronavirus and parvovirus in a captive coyote population (1980) J. Am. Vet. Med. Assoc., 177, pp. 784-786; Green, C.E., Infectious canine hepatitis (1990) Infectious Diseases of the Dog, and Cat, pp. 242-251. , Green, C. E. (ed.), W. B. Saunders, Philadelphia, PA; Hammond, M.M., Timoney, P.J., An electron microscopic study of viruses associated with canine gastroenteritis (1983) Cornell Vet., 73, pp. 82-97; Hoskins, J.D., Canine coronaviral enteritis (1998) Infectious Diseases of the Dog, and Cat, pp. 45-47. , Green, C. E. (ed.), W. B. Saunders, Philadelphia, PA; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Kobayashi, Y., Ochiai, K., Itakura, C., Dual infection with canine distemper virus and infectious canine hepatitis virus (canine adenovirus type 1) in a dog (1993) J. Vet. Med. Sci., 55, pp. 699-701; Marshall, J.N., Healey, D.S., Studdert, M.J., Scott, P.C., Kennett, M.L., Ward, B.K., Gust, I.D., Viruses and virus-like particles in the faeces of dogs with and without diarrhoea (1984) Austral. Vet. J., 61, pp. 33-38; Martin, H.D., Zeidner, N.S., Concomitant cryptosporidia, coronavirus and parvovirus infection in a raccoon (Procyon, lotor) (1992) J. Wildl. Dis., 28, pp. 113-115; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR assay for the detection of canine coronavirus (1999) J. Virol. Meth., 80, pp. 11-15; Pratelli, A., Tempesta, M., Roperto, F.P., Sagazio, P., Carmichael, L.E., Buonavoglia, C., Fatal coronavirus infection in puppies following canine parvovirus 2b infection (1999) J. Vet. Diagn. Invest., 11, pp. 550-553; Rubarth, S., An acute virus disease with liver lesions in dogs (hepatitis contagiosa canis). A pathologico-anatomical and aetiologic investigation (1947) Acta Pathol. Microbiol. Scand. (Suppl. 69), 24, pp. 1-222; Sasaki, N., Nakai, M., Iwamoto, I., Konishi, S., Ikegami, T., Studies on infectious hepatitis of dogs. II. The distribution of the disease in Japan, and its immunization (1956) Jpn. J. Vet. Sci., 18, pp. 113-118; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Yasoshima, A., Fucinami, F., Doi, K., Dojima, A., Takada, H., Okaniwa, A., Case report on mixed infection of canine parvovirus and canine coronavirus. Electron microscopy and recovery of canine coronavirus (1983) Jpn. J. Vet. Sci., 45, pp. 217-225","Pratelli, A.; Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, Strada Casamassima km 3, 70010 Valenzano (Bari), Italy; email: a.pratelli@veterinaria.uniba.it",,,09311793,,JVMBE,"11471849","English","J. Vet. Med. Ser. B",Article,"Final",Open Access,Scopus,2-s2.0-0034944483
"Tråvén M., Näslund K., Linde N., Linde B., Silván A., Fossum C., Hedlund K.O., Larsson B.","6603563444;8306740800;15723867000;15723847600;6701783135;7003448639;7005104728;7202678840;","Experimental reproduction of winter dysentery in lactating cows using BCV - Comparison with BCV infection in milk-fed calves",2001,"Veterinary Microbiology","81","2",,"127","151",,51,"10.1016/S0378-1135(01)00337-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035954836&doi=10.1016%2fS0378-1135%2801%2900337-6&partnerID=40&md5=c260f7a89a86fa7aba258213f0c569e6","Department of Ruminant Medicine and Veterinary Epidemiology, Swedish University of Agricultural Sciences, Box 7019, S-750 07 Uppsala, Sweden; Section of Virology, National Veterinary Institute, Box 7073, S-750 07 Uppsala, Sweden; Medicago AB, Uppsala, Sweden; Department of Veterinary Microbiology, Section of Immunology, Swedish University of Agricultural Sciences, S-751 23 Uppsala, Sweden; Swedish Institute for Infectious Disease Control, S-171 82 Solna, Sweden","Tråvén, M., Department of Ruminant Medicine and Veterinary Epidemiology, Swedish University of Agricultural Sciences, Box 7019, S-750 07 Uppsala, Sweden; Näslund, K., Section of Virology, National Veterinary Institute, Box 7073, S-750 07 Uppsala, Sweden; Linde, N., Section of Virology, National Veterinary Institute, Box 7073, S-750 07 Uppsala, Sweden; Linde, B., Medicago AB, Uppsala, Sweden; Silván, A., Department of Ruminant Medicine and Veterinary Epidemiology, Swedish University of Agricultural Sciences, Box 7019, S-750 07 Uppsala, Sweden; Fossum, C., Department of Veterinary Microbiology, Section of Immunology, Swedish University of Agricultural Sciences, S-751 23 Uppsala, Sweden; Hedlund, K.O., Swedish Institute for Infectious Disease Control, S-171 82 Solna, Sweden; Larsson, B., Department of Ruminant Medicine and Veterinary Epidemiology, Swedish University of Agricultural Sciences, Box 7019, S-750 07 Uppsala, Sweden","Infection models were developed for adult cows and for young calves using the same strain of bovine coronavirus (BCV), which for the first time allows experimental reproduction of winter dysentery (WD) in seronegative lactating cows. The cattle were infected through direct contact with an experimentally inoculated calf. All experimental cattle shed faecal BCV with development of diarrhoea, being profusely watery with small amounts of blood in the most severely affected animals, including both cows and calves. The cows, in contrast to the calves, showed depressed general condition and appetite leading to a marked decrease in milk yield. Further age-associated differences were a shorter incubation period in the two youngest calves, but with milder fever and milder decrease in white blood cell counts. These findings shed light on the apparent epidemiological differences between WD and calf BCV diarrhoea suggesting that, (1) the same strains of BCV cause natural outbreaks of calf diarrhoea and WD, (2) seronegative cows are more severely affected by the infection than seronegative conventionally reared calves, and (3) unaffected general condition in diarrhoeic calves may lead to underestimation of the occurrence of calf diarrhoea in WD outbreaks. In response to infection, all cattle produced early interferon type 1 in serum and, except for one calf, in nasal secretions. A finding not previously reported is the detection of interferon type 1 responses in bovine milk. All cattle developed high IgM antibody responses and long-lasting IgA antibody responses both systemically and locally. The serum IgM antibody responses came earlier in most of the calves than in the cows. Prolonged IgM antibody responses were detected in serum and milk, while those in nasal secretions were much shorter. BCV-specific IgA was present in nasal secretions from all cattle throughout the 6 months follow-up. The IgA antibody response in serum was detected up to 17 months post-infection and the duration showed an age-related variation indicating a more prominent IgA memory in the adult cattle and in the older calves than in the younger ones. BCV-specific IgG was detected in all cattle during the experimental period of up to 22 months. In conclusion, WD was reproduced in seronegative lactating cows. The cows showed a more severe general diseases than seronegative calves infected concurrently. Very long-lasting IgA antibody responses were detected both systemically and locally. © 2001 Elsevier Science B.V.","Bovine coronavirus; Cattle-bacteria; Experimental infection; IgA; IgM; Interferon type 1; Winter dysentery","immunoglobulin A; immunoglobulin G; immunoglobulin M; interferon; age; animal experiment; animal model; antibody response; appetite disorder; article; blood; cattle; cattle disease; controlled study; Coronavirus; diarrhea; disease severity; disease transmission; dysentery; epidemic; feces; female; fever; follow up; incubation time; infection rate; inoculation; lactation; leukocyte count; male; nonhuman; nose secretion; virus infection; Age Factors; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Cytopathogenic Effect, Viral; Dysentery; Enzyme-Linked Immunosorbent Assay; Feces; Female; Immunoglobulin A; Immunoglobulin Isotypes; Interferon Type I; Lactation; Male; Milk; Nasal Mucosa; Seasons",,"Tråvén, M.; Department of Ruminant Medicine, Swedish Univ. of Agricultural Sci., Box 7019, S-750 07 Uppsala, Sweden; email: madelein.traven@idmed.slu.se",,,03781135,,VMICD,"11376958","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0035954836
"Crouch C.F., Oliver S., Francis M.J.","7006793407;55424287900;7201841723;","Serological, colostral and milk responses of cows vaccinated with a single dose of a combined vaccine against rotavirus, coronavirus and Escherichia coli F5 (K99)",2001,"Veterinary Record","149","4",,"105","108",,23,"10.1136/vr.149.4.105","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035963883&doi=10.1136%2fvr.149.4.105&partnerID=40&md5=f9ff7c756aa923e07deb931cfb7a2191","Schering-Plough Animal Health, Breakspear Road South, Harefield, Uxbridge UB9 6LS, United Kingdom","Crouch, C.F., Schering-Plough Animal Health, Breakspear Road South, Harefield, Uxbridge UB9 6LS, United Kingdom; Oliver, S., Schering-Plough Animal Health, Breakspear Road South, Harefield, Uxbridge UB9 6LS, United Kingdom; Francis, M.J., Schering-Plough Animal Health, Breakspear Road South, Harefield, Uxbridge UB9 6LS, United Kingdom","Twenty-five Ayrshire/Friesian cows were vaccinated once with a new combined vaccine against rotavirus, coronavirus and Escherichia coli F5 (K99) or given a saline placebo 31 days before the first expected calving date. Blood samples were taken from the cows at intervals from vaccination until seven days after calving and from their calves up to 28 days after birth, and colostrum and milk samples were collected from the cows at intervals for 28 days after calving. There was a significant increase in the mean specific antibody titre against all three antigens in the serum of the vaccinated animals (even in the presence of pre-existing antibody) which was accompanied by increased levels of protective antibodies to rotavirus, coronavirus and E coli F5 (K99) in their colostrum and milk for at least 28 days.",,"corona virus vaccine; Escherichia coli vaccine; rotavec corona; Rotavirus vaccine; unclassified drug; virus antibody; virus vaccine; animal experiment; animal model; antibody response; article; blood sampling; colostrum; controlled study; Coronavirus; cow; drug blood level; drug mechanism; drug metabolism; Escherichia coli; milk; nonhuman; Rotavirus; vaccination","Acres, S.D., Forman, A.J., Kapitany, R.A., Antigen extinction profile in pregnant cows using K99-containing whole-cell bacterin to induce passive protection against enterotoxigenic colibacillosis in calves (1982) American Journal of Veterinary Research, 14, pp. 569-575; Acres, S.D., Isaacson, R.E., Babiuk, L.A., Kapitany, R.A., Immunization of calves against enterotoxigenic colibacillosis by vaccinating dams with purified K99 antigen and whole cell bacterins (1979) Infection and Immunity, 25, pp. 121-126; Brussow, H., Walther, I., Fryder, V., Sidoti, J., Bruttin, A., Cross-neutralizing antibodies induced by single serotype vaccination of cows with rotavirus (1988) Journal of General Virology, 69, pp. 1647-1658; Butler, J.E., Synthesis and distribution of immunoglobulins (1973) Journal of the American Veterinary Medical Association, 163, pp. 795-798; Castrucci, G., Frigeri, F., Ferrari, M., Cilli, V., Caleffi, F., Aldrovandi, V., Nigrelli, A., The efficacy of colostrum from cows vaccinated with rotavirus in protecting calves to experimentally induced rotavirus infection (1984) Comparative Immunology, Microbiology and Infectious Disease, 7, pp. 11-18; Crouch, C.F., Vaccination against enteric rota and coronaviruses in cattle and pigs: Enhancement of lactogenic immunity (1985) Vaccine, 3, pp. 284-291; Crouch, C.F., Acres, S.D., Prevalence of rotavirus and coronavirus antigens in the feces of normal cows (1984) Canadian Journal of Comparative Medicine, 48, pp. 340-342; Dauvergne, M., Laporte, J., Reynaud, G., Soulebot, J.-P., Brun, A., Espinasse, J., Vaccination of dams with a combined rotavirus-coronavirus vaccine to protect newborn calves against diarrhea (1983) Proceedings of the 4th International Symposium on Neonatal Diarrhea, pp. 424-432. , VIDO, Sakatchewan, Canada; Green, K.Y., Taniguchi, K., Mackow, E.R., Kapikian, A.Z., Homotypic and heterotypic epitope-specific antibody responses in adult and infant rotavirus vaccinees: Implications for vaccine development (1990) Journal of Infectious Diseases, 161, pp. 667-679; Hess, R.G., Bachmann, P.A., Eichhorn, W., Frahm, K., Plank, P., Stimulierung der laktogenen immunitat des rindes gegunuber rotavirusinfektionen (1982) Fortschrift fur Veterinar Medizin, 35, pp. 103-108; Karkhanis, Y.D., Bhogal, B.S., A single-step isolation of K99 pili from B-44 strain of Escherichia coli (1986) Analytical Biochemistry, 155, pp. 51-55; Kohara, J., Hirai, T., Mori, K., Ishizaki, H., Tsunemitsu, H., Enhancement of passive immunity with maternal vaccine against newborn calf diarrhea (1997) Journal of Veterinary Medical Research, 59, pp. 1023-1025; Krogh, H.V., Infection with enterotoxigenic Escherichia coli in calves and protection of the calves by vaccination of the dams (1983) Annales des Recherches Veterinaires, 14, pp. 522-525; Moon, H.W., McClukin, A.W., Isaacson, R.E., Pohlenz, J., Skardtvedt, S.M., Gillette, K.G., Baetz, A.C., Pathogenic relationships of rotavirus, Escherichia coli and other agents in mixed infections of calves (1978) Journal of the American Veterinary Medical Association, 173, pp. 577-583; Mostl, K., Burkl, F., Incidence of diarrhoea and of rotavirus-and coronavirus-shedding in calves whose dams had been vaccinated with an experimental oil-adjuvanted vaccine containing bovine rotavirus and bovine coronavirus (1988) Journal of Veterinary Medicine, 35, pp. 186-196; Nagy, B., Vaccination of cows with a K99 extract to protect newborn calves against experimental enterotoxic colibacillosis (1980) Infection and Immunity, 27, pp. 21-24; Newby, T.J., Stokes, C.R., Bourne, F.J., Immunological activities of milk (1982) Veterinary Immunology and Immunopathology, 3, pp. 67-94; Runnels, P.L., Moon, H.W., Schneider, R.A., Development of resistance with host age to adhesion of K99+ Escherichia coli to isolated intestinal epithelial cells (1980) Infection and Immunity, 28, pp. 298-300; Saif, L.J., Smith, K.L., Landmeier, B.J., Bohl, E.H., Theil, K.W., Todhunter, D.A., Immune response of pregnant cows to bovine rotavirus immunization (1984) American Journal of Veterinary Research, 45, pp. 49-58; Snodgrass, D.R., Evaluation of a combined rotavirus and enterotoxigenic Escherichia coli vaccine in cattle (1986) Veterinary Record, 119, pp. 39-43; Snodgrass, D.R., Browning, G., Enteric vaccines for farm animals and horses (1993) Vaccines for Veterinary Applications, pp. 59-81. , Oxford, Butterworth-Heinemann; Snodgrass, D.R., Fahey, K.J., Wells, P.W., Campbell, I., Whitelaw, A., Passive immunity in calf rotavirus infections: Maternal vaccination increases and prolongs immunoglobulin G1 antibody secretion in milk (1980) Infection and Immunity, 28, pp. 344-349; Snodgrass, D.R., Nagy, L.K., Sherwood, D., Cambell, I., Passive immunity in calf diarrhea: Vaccination with K99 antigen of enterotoxigenic Escherichia coli and rotavirus (1982) Infection and Immunity, 37, pp. 586-591; Snodgrass, D.R., Ojeh, C.K., Campbell, I., Herring, A.J., Bovine rotavirus serotypes and their significance for immunization (1984) Journal of Clinical Microbiology, 20, pp. 342-346; Stepanek, J., Salajka, E., Zuffa, A., Mensik, J., Franz, J., New polyvalent vaccine against intestinal infections in newborn calves (1987) Veterinarni-medicina, 32, pp. 65-80; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Advances in Veterinary Science and Comparative Medicine, 29, pp. 103-206; Wieda, J., Bengelsdorff, H.-J., Bernhardt, D., Hungerer, K.D., Antibody levels in milk of vaccinated and unvaccinated cows against organisms of neonatal diarrhoea (1987) Journal of Veterinary Medicine, 34, pp. 495-503","Crouch, C.F.; Schering-Plough Animal Health, Breakspear Road South, Harefield, Uxbridge UB9 6LS, United Kingdom",,"British Veterinary Association",00424900,,VETRA,,"English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0035963883
"Kourtesis A.B., Gélinas A.-M., Dea S.","6507567386;6602090251;7006056287;","Genomic and antigenic variations of the HE glycoprotein of bovine coronaviruses associated with neonatal calf diarrhea and winter dysentery",2001,"Archives of Virology","146","6",,"1219","1230",,8,"10.1007/s007050170117","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034903365&doi=10.1007%2fs007050170117&partnerID=40&md5=4bff275b5dd745b16a477f6249dbfb3a","Centre of Microbiology and Biotechnology, INRS-Institut Armand Frappier, Université du Québec, Laval, Que., Canada","Kourtesis, A.B., Centre of Microbiology and Biotechnology, INRS-Institut Armand Frappier, Université du Québec, Laval, Que., Canada; Gélinas, A.-M., Centre of Microbiology and Biotechnology, INRS-Institut Armand Frappier, Université du Québec, Laval, Que., Canada; Dea, S., Centre of Microbiology and Biotechnology, INRS-Institut Armand Frappier, Université du Québec, Laval, Que., Canada","In this study, we attempted to define differences in the hemagglutinin-esterase (HE) glycoprotein between 11 bovine coronaviruses (BCV) recent (post-1991) and past (pre-1991) isolates from neonatal calf diarrhoea (NCD) and winter dysentery (WD) syndromes as a basis for strain differentiation related to the clinical source of the isolates. The five WD-associated BCV isolates studied could be distinguished from past NCD-isolates by their hemagglutinating (HA) properties at 4° and 37°C, their receptor-destroying enzyme (RDE) activities with rat erythrocytes and lack of reactivity of these NCD isolates to four HA inhibiting (HAI) monoclonal antibodies (MAbs) directed against the HE glycoprotein of the reference WD-associated BCQ.2590 Quebec strain. Although minor or no differences could be demonstrated by comparing biological properties of the HE of WD-isolates to those of recent NCD-isolates, past NCD isolates lacked reactivity with the WD HAI MAbs, whereas recent NCD isolates displayed two distinct reactivity patterns. Attempts to define sequence differences in the HE genes of the WD and NCD strains revealed high nucleotide (NT) identities with only scattered amino acid differences, seemingly unrelated to the clinical origin of the isolates or HAI MAb reactivities.",,"cattle; Coronavirus; enzyme activity; erythrocyte; gene sequence; genetic difference; genetic strain; hemagglutinin esterase; inositol; monoclonal antibody; neonatal calf diarrhea; temperature; virus enzyme; virus infection; virus protein; winter dysentery; Amino Acid Substitution; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigenic Variation; Base Sequence; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; DNA Primers; Dysentery; Genome, Viral; Hemagglutinins, Viral; Molecular Sequence Data; Species Specificity; Syndrome; Variation (Genetics); Viral Fusion Proteins; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus","Benfield, D.A., Saif, L.J., Cell culture propagation of a coronavirus isolated from cows with winter dysentery (1990) J Clin Microbiol, 28, pp. 1454-1457; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction (1987) Ann Biochem, 162, pp. 156-159; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 30genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Crouch, C.F., Bielefeldt, O.H., Watts, T.C., Babiuk, L.A., Chronic shedding of bovine enteric coronavirus antigen-antibody complexes by clinically normal cows (1985) J Gen Virol, 66, pp. 1489-1500; Dea, S., Roy, R.S., Begin, M.E., Bovine coronavirus isolation in continuous cell lines (1980) Am J Vet Res, 41, pp. 30-38; Dea, S., Garzon, S., Strykowski, H., Tijssen, P., Ultrastructure and protein A-gold immunolabelling of HRT-18 cells infected with turkey enteric coronavirus (1989) Vet Microbiol, 20, pp. 21-33; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J Virol, 64, pp. 3112-3118; Dea, S., Michaud, L., Milane, G., Comparison of bovine coronavirus isolates associated with neonatal calf diarrhoea and winter dysentery in adult dairy cattle in Québec (1995) J Gen Virol, 76, pp. 1263-1270; Deregt, D., Sabara, M., Babiuk, L.A., Structural proteins of bovine coronavirus and their intracellular processing (1987) J Gen Virol, 68, pp. 2863-287710; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; El-Ghorr, A.A., Snodgrass, D.R., Scott, F.M.M., Campbell, I., A serological comparison of bovine coronavirus strains (1989) Arch Virol, 104, pp. 241-248; Fukutomi, T., Tsunemitsu, H., Akashi, H., Detection of bovine coronaviruses from adult cows with epizootic diarrhea and their antigenic and biological diversities (1999) Arch Virol, 144, pp. 997-1006; Hogue, B.G., Brian, D.A., Structural proteins of human respiratory coronavirus OC43 (1986) Virus Res, 5, pp. 131-144; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike protein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; King, B., Poots, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Res, 2, pp. 53-59; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am J Vet Res, 34, pp. 145-150; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch Virol, 131, pp. 455-465; Milane, G., Kourtesis, A.B., Dea, S., Characterization of monoclonal antibodies to the hemagglutinin-esterase glycoprotein of a bovine coronavirus associated with winter dysentery and cross-reactivity to field isolates (1997) J Clin Microbiol, 35, pp. 33-40; Parker, M.D., Yoo, D., Babiuk, L.A., Expression and secretion of the bovine coronavirus hemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses (1990) J Virol, 64, pp. 1625-1629; Rogan, D., Dea, S., Percy, D., Culbert, R., Ability of winter dysentery isolates of bovine coronaviruses to induce bloody diarrhea in newborn calves (1996) 77th annual CRWAD meeting, , Nov. 11-13, Chicago (abstract no. 107); Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Sanger, N.S., Nicklen, S., Coulson, A.R., DNA sequencing with chain termination inhibitors (1977) Proc Natl Acad Sci USA, 74, pp. 5463-5467; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J Virol, 65, pp. 6232-6237; Spaan, W.D., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J Gen Virol, 69, pp. 2939-2952; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch Virol, 125, pp. 193-204; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swabs samples in cattle with signs of respiratory tract disease after shipping (1996) J Am Vet Med Assoc, 208, pp. 1452-1454; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine corona-viruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: Detailed antigenic analysis of S1, S2 and HE (1992) J Gen Virol, 73, pp. 1725-1737; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J Virol, 62, pp. 4686-4690; Zhang, X., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Zhang, X., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains (1991) Virology, 185, pp. 847-852","Dea, S.; INRS-Institut Armand-Frappier, Center of Microbiology/Biotechnology, 531 boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Serge.Dea@INRS-IAF.UQUEBEC.CA",,,03048608,,ARVID,"11504427","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034903365
"Gra̧dzki Z.","7004052971;","Application of cDNA probes for detecting and differentiating TGEV RNA [Zastosowanie sond cDNA do wykrywania i róznicowania RNA wirusa TGEV]",2001,"Medycyna Weterynaryjna","57","8",,"598","602",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035413514&partnerID=40&md5=3b385c8847627596a9eca366dfd1a21a","Kat. Epizootiologii I Klinika C., ul. Głȩboka 30, 20-612 Lublin, Poland; ul. Bursztynowa 15/109, 20-576 Lublin, Poland","Gra̧dzki, Z., Kat. Epizootiologii I Klinika C., ul. Głȩboka 30, 20-612 Lublin, Poland, ul. Bursztynowa 15/109, 20-576 Lublin, Poland","PCR-generated non-radioactive probes (Dig-85 and Dif-12) used in this study hybridised specifically to the RNA extracted from TGEV strains isolated in Europe and USA as well as the RNA from Polish field C-71 isolate. Neither of the used probes hybridised to the RNA from PEDV, CSV, group A porcine rotaviruses and nucleic acids extracted from non-infected cell cultures (ST and LLC PK1) and the faeces of healthy pigs. The diagnostic Dig-85 probe was also hybridised to the RNA extracted from reference PRCV strains. The Dif-12 probe hybridised exclusively to the RNA extracted from TGEV and enabled a differentiation of the enteric TGEV with its respiratory variant, PRCV. PCR-generated diagnostic probe labelled with digoxygenin was able to detect 3.5-7.0 ng of TGEV RNA. RT-PCR technology and appeared to be a fast and reliable method of synthesis in laboratory scales, probes for diagnostic and differentiation of coronavirus infections in swine.","cDNA probe; Diagnostic; TGEV/PRCV",,"Bae, J., Jackwood, D.J., Benfield, D.A., Saif, L.J., Wesley, R.D., Hill, H., Differentiation of transmissible gastroenteritis virus from porcine respiratory coronavirus and other antigenically related coronaviruses by using cDNA probes specific for the 5' region of the S glycoprotein gene (1991) J. Clin. Microbiol., 29, pp. 215-218; Benfield, D.A., Jackwood, D.J., Bae, I., Saif, L.J., Wesley, R.D., Detection of transmissible gastroenteritis virus using cDNA probes (1991) Arch. Virol., 116, pp. 91-106; Britton, P., Kottier, S., Chen, C.M., Pocock, D.H., Salmon, H., Aynaud, J.M., (1994) The Use of PCR Genome Mapping for the Characterisation of TGEV Strains. w: Coronaviruses: Molecular Biology and Virus-host Interactions, pp. 29-43. , red. H. Laude, J. F., Vautherot, Plenum Press, New York; Clavijo, A., Thorsen, J., Chemiluminescent detection of caprine arthritis ecephalitis virus with a PCR-generated single standed nonradiolabelled probe (1995) Vet. Microbiol., 43, pp. 295-305; Collomb, J., Finance, C., Alabouch, S., Laporte, J., Radioactive and enzymatic cloned cDNA probes for bovine enteric coronavirus detection by molecular hybridization (1992) Arch. Virol., 125, pp. 25-37; Cristallo, A., Biamonti, G., Battaglia, M., Cereda, P.M., cDNA probe for the human coronavirus OC43 also detects neonatal calf diarrhea coronavirus (NCDCV) Microbiologica 1996, 19, pp. 251-256; Gra̧dzki, Z., Winiarczyk, S., Koronawirus układu oddechowego (PRCV) i jego patogenność dla świń (1997) Medycyna Wet., 53, pp. 448-453; Gra̧dzki, Z., Winiarczyk, S., Metody biologii molekularnej w rozpoznawaniu wirusowego zapalenia żoła̧dka i jelit (TGE) świń (1997) Medycyna Wet., 53, pp. 197-201; Gra̧dzki, Z., Winiarczyk, S., Metody rozpoznawania wirusowego zapalenia żoła̧dka i jelit świń (1996) Medycyna Wet., 52, pp. 553-558; Gra̧dzki, Z., Winiarczyk, S., Przydatność wybranych metod ekstrakcji RNA do wykrywania wirusa TGE w hodowli komórkowej i kale świń metoda̧ RT-PCR Medycyna Wet., , Praca w druku; Gra̧dzki, Z., Winiarczyk, S., Zastosowanie metody RT-PCR do wykrywania i różnicowania wirusa TGEV Medycyna Wet., , Praca w druku; Gra̧zki, Z., (1998) Zastosowanie Metod Detekcji Kwasów Nukleinowych do Diagnostyki Oraz Różnicowania Zakażeń Koronawirusowych (TGEV I PRCV) U świń, , Praca hab., Wyd. AR Lublin; Guesdon, J.L., Immunoenzymatic techniques applied to the specific detection of nucleic acids (1992) J. Immun. Meth., 150, pp. 33-49; Jackwood, D.J., Kwon, H.M., Saif, L.J., Molecular differentiation of transmissible gastroenteritis virus and porcine respiratory coronavirus strains (1996) Adv. Exp. Med. Biol., 380, pp. 35-41; Jacobs, DeGrot, R., Van Der Zcijst, B.A., Horzonek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res., 8, pp. 363-371; Paton, D.J., Lowings, P., Discrimination between transmissible gastroenteritis isolates (1997) Arch. Virol., 142, pp. 1703-1711; Saif, L.J., Wesley, R.D., (1992) Transmissible Gastroenteritis. w: Diseases of Swine, pp. 362-386. , red. A. D. Leman, B. E. Strauss, W. L. Mengeling, S. D'Allaire, D. J. Taylor, 7th ed., Iowa State University Press, Ames. IA; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Maria, J.B., Gebauer, F., Enjuanez, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Shockley, L.J., Kapke, P.A., Lapps, W., Brian, D.A., Potgeiter, L.N., Woods, R., Diagnosis of porcine and bovine enteric coronavirus infections using cloned cDNA probes (1987) J. Clin. Microbiol., 25, pp. 1591-1596; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV), in formalin-fixed paraffinembedded tissues (1996) J. Virol. Methods, 56, pp. 149-160; Tenover, F.C., Diagnostic deoxyribonucleic acid probes for infectious diseases (1988) Clin. Microbiol. Rev., 1, pp. 82-101; Vaughn, E.M., Halbur, P.G., Paul, P.S., Use of non-radioactive cDNA probes to differentiate porcine respiratory coronavirus and transmissible gastroenteritis virus isolates (1996) J. Vet. Diagn. Invest., 8, pp. 241-244; Vaughn, E.M., Paul, P.S., Antigenic and biological diversity among transmissible gastroenteritis virus isolates of swine (1993) Vet. Microbiol., 36, pp. 333-347; Verbeek, A., Dea, S., Tijssen, P., Genomic relationship between turkey and bovine enteric coronaviruses identified by hybridization with BCV or TCV specific cDNA probes (1991) Arch. Virol., 121, pp. 199-211; Verbeek, A., Tijssen, P., Polymerase chain reaction for probe synthesis and for direct amplification in detection of bovine coronavirus (1990) J. Virol. Methods, 29, pp. 243-256; Verbeek, A., Tijssen, P., Biotinylated and radioactive cDNA probes in the detection by hybridization of bovine enteric coronavirus (1988) Moll. Cell. Probes, 2, pp. 209-223; Vieler, E., Schlapp, T., Andrers, C., Herbst, W., Genomic relationship of porcine hemagglutinating encephalomyelitis virus to bovine coronavirus and human coronavirus OC43 as studied by the use of bovine coronavirus S gene-specific probes (1995) Arch. Virol., 140, pp. 1215-1223; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus using a cDNA probe (1991) J. Vet. Diagn. Invest., 3, pp. 29-32; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, J.M., Nucleotide sequence and expression of the spike S gene of canine coronavirus and comparison wilh the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794; Winiarczyk, S., (1995) Zastosowanie Metod Biologii Molekularnej w Diagnostyce Zakażeń Rotawirusowych u świń, , Praca hab., Wyd. AR Lublin","Gra̧dzki, Z.ul. Bursztynowa 15/109, 20-576 Lublin, Poland",,,00258628,,,,"Polish","Med. Weter.",Article,"Final",,Scopus,2-s2.0-0035413514
"Bergmann C.C., Ramakrishna C., Kornacki M., Stohlman S.A.","35449739000;7004391978;57213684232;35502534500;","Impaired T cell immunity in B cell-deficient mice following viral central nervous system infection",2001,"Journal of Immunology","167","3",,"1575","1583",,58,"10.4049/jimmunol.167.3.1575","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035424120&doi=10.4049%2fjimmunol.167.3.1575&partnerID=40&md5=16795057c6655c42197aacde8da9ef6d","MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States","Bergmann, C.C., MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States; Ramakrishna, C., MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States; Kornacki, M., MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States; Stohlman, S.A., MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States","CD8+ T cells are required to control acute viral replication in the CNS following infection with neurotropic coronavirus. By contrast, studies in B cell-deficient (μMT) mice revealed Abs as key effectors in suppressing virus recrudescence. The apparent loss of initial T cell-mediated immune control in the absence of B cells was investigated by comparing T cell populations in CNS mononuclear cells from infected μMT and wild-type mice. Following viral recrudescence in μMT mice, total CD8+ T cell numbers were similar to those of wild-type mice that had cleared infectious virus; however, virus-specific T cells were reduced at least 3-fold by class I tetramer and IFN-γ ELISPOT analysis. Although overall T cell recruitment into the CNS of μMT mice was not impaired, discrepancies in frequencies of virus-specific CD8+ T cells were most severe during acute infection. Impaired ex vivo cytolytic activity of μMT CNS mononuclear cells, concomitant with reduced frequencies, implicated IFN-γ as the primary anti viral factor early in infection. Reduced virus-specific CD8+ T cell responses in the CNS coincided with poor peripheral expansion and diminished CD4+ T cell help. Thus, in addition to the lack of Ab, limited CD8+ and CD4+ T cell responses in μMT mice contribute to the ultimate loss of control of CNS infection. Using a model of virus infection restricted to the CNS, the results provide novel evidence for a role of B cells in regulating T cell expansion and differentiation into effector cells.",,"gamma interferon; animal cell; animal experiment; animal model; animal tissue; article; B lymphocyte; central nervous system infection; controlled study; cytolysis; cytotoxic T lymphocyte; effector cell; flow cytometry; lymphocyte differentiation; Lymphocytic choriomeningitis virus; male; mononuclear cell; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; T lymphocyte; T lymphocyte activation; virus infection; virus replication","Moskophidis, D., Lechner, F., Pircher, H., Zinkernagel, R.M., Virus persistence in acutely infected immunocompetent mice by exhaustion of antiviral cytotoxic effector T cells (1993) Nature, 362, p. 758; Gallimore, A., Glithero, A., Godkin, A., Tissot, A.C., Pluckthun, A., Elliott, T., Hengartner, H., Zinkernagel, R., Induction and exhaustion of lymphocytic choriomeningitis virus-specific cytotoxic T lymphocytes visualized using soluble tetrameric major histocompatibility complex class I-peptide complexes (1998) J. 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Wiley, New York; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol., 1, p. 9; Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, p. 337; Bergmann, C., Dimacali, E., Stohl, S., Wei, W., Lai, M.M.C., Tahara, S., Marten, N., Variability of persisting MHV RNA sequences comprising immune and replication relevant domains (1998) Virology, 244, p. 563; Lin, M.T., Stohlman, S.A., Hinton, D.R., Mouse hepatitis virus is cleared from the central nervous system of mice lacking perforin-mediated cytolysis (1997) J. Virol., 71, p. 383; Fleming, J.O., Trousdale, M., Zactarim, F.E., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with mAb (1986) J. 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Immunol., 3, p. 471; Matloubian, M., Conception, R.J., Ahmed, R., CD4+ T cells are required to sustain CD8+ cytotoxic T cell responses during chronic viral infection (1994) J. Virol., 68, p. 8056; Altfeld, M., Rosenberg, E.S., The role of CD4+ T helper cells in the cytotoxic T lymphocyte response to HIV-1 (2000) Curr. Opin. Immunol., 12, p. 375; Doherty, P.C., Topham, D.J., Tripp, R.A., Cardin, R.D., Brooks, J.W., Stevenson, P.G., Effector CD4 and CD8 T cell mechanisms in the control of respiratory infections (1997) Immunol. Rev., 159, p. 105; Roth, R., Mamula, M.J., Trafficking of adoptively transferred B lymphocytes in B-lymphocyte-deficient mice (1997) J. Exp. Biol., 200, p. 2057; Cserr, H.F., Knopf, P.M., Cervical lymphatics, the blood brain barrier, and the immunoreactivity of the brain (1997) Immunology of the Central Nervous System, p. 134. , R. W. Keane and W. F. Hickey, eds. Oxford Univ. Press, Oxford; Sedgwick, J.D., Hickey, W.F., Antigen presentation in the central nervous system (1997) Immunology of the Central Nervous System, p. 364. , R. W. Keane and W. F. Hickey, eds. Oxford Univ. Press, Oxford; Parra, B., Lin, M.T., Stohlman, S.A., Bergmann, C.C., Atkinson, R., Hinton, D.A., Fas-Fas ligand interactions do not contribute to the pathogenesis of mouse hepatitis virus in the central nervous system (2000) J. Virol., 74, p. 2447; Deshpande, S.P., Zheng, M., Daheshia, M., Rouse, B.T., Pathogenesis of herpes simplex virus-induced ocular immunoinflammatory lesions in B-cell-deficient mice (2000) J. Virol., 74, p. 3517; Linton, P.-J., Harbertson, J., Bradley, L.M., A critical role of B cells in the development of memory CD4 cells (2000) J. Immunol., 165, p. 5558; Hamano, Y., Hisashi, A., Saisho, H., Saito, T., Immune complex and Fc receptor-mediated augmentation of antigen presentation for in vivo Th cell responses (2000) J. Immunol., 164, p. 6113; Stevenson, P.G., Freeman, S., Bangham, C.R.M., Hawke, S., Virus dissemination through the brain parenchyma without immunologic control (1997) J. Immunol., 159, p. 1876; Mozdzanowska, K., Maiese, K., Gerhard, W., Th cell-deficient mice control influenza virus infection more effectively than Th- and B cell-deficient mice: Evidence for a Th-independent contribution by B cells to virus clearance (2000) J. Immunol., 164, p. 2635; Moulin, V., Andris, F., Thielemans, K., Maliszewski, C., Urbain, J., Moser, M., B lymphocytes regulate dendritic cell (DC) function in vivo: Increased interleukin 12 production by DCs from B cell-deficient mice results in T helper cell type I deviation (2000) J. Exp. Med., 192, p. 47","Bergmann, C.C.; MCH 142, 1333 San Pablo Street, Los Angeles, CA 90033, United States; email: cbergman@hsc.usc.edu",,"American Association of Immunologists",00221767,,JOIMA,"11466379","English","J. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0035424120
"Kennedy M., Boedeker N., Gibbs P., Kania S.","7402308045;57204371382;56220248800;24177256900;","Deletions in the 7a ORF of feline coronavirus associated with an epidemic of feline infectious peritonitis",2001,"Veterinary Microbiology","81","3",,"227","234",,61,"10.1016/S0378-1135(01)00354-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035828241&doi=10.1016%2fS0378-1135%2801%2900354-6&partnerID=40&md5=e91e6d45d767e2d054a7e2b706e93e4f","Department of Comparative Medicine, University of Tennessee, College of Veterinary Medicine, P.O. Box 1071, Knoxville, TN 37901-1071, United States","Kennedy, M., Department of Comparative Medicine, University of Tennessee, College of Veterinary Medicine, P.O. Box 1071, Knoxville, TN 37901-1071, United States; Boedeker, N., Department of Comparative Medicine, University of Tennessee, College of Veterinary Medicine, P.O. Box 1071, Knoxville, TN 37901-1071, United States; Gibbs, P., Department of Comparative Medicine, University of Tennessee, College of Veterinary Medicine, P.O. Box 1071, Knoxville, TN 37901-1071, United States; Kania, S., Department of Comparative Medicine, University of Tennessee, College of Veterinary Medicine, P.O. Box 1071, Knoxville, TN 37901-1071, United States","A population of Persian cats experienced an epidemic of feline infectious peritonitis (FIP) over 2 years. Twelve cases of FIP occurred in litters born during this period. Cats contracting FIP were all genetically related through the sire. Feline coronavirus (FCoV) genomic RNA was detected consistently in this study in biologic samples from adult cats, kittens suffering from FIP, and their siblings. Analysis of viral 7a/7b open reading frame (ORFs) were analyzed and revealed two distinct virus variants circulating in the population, one with an intact 7a ORF and one with two major deletions in the 7a ORF. The 7b ORFs were intact and similar among all virus isolates, although point mutations resulting in amino acid changes were present. The sire was determined to be infected with both variants, and was persistently virus-infected. We speculate the deletion variant arose from the non-deletion variant during viral replication in this population, possibly in the sire. © 2001 Elsevier Science B.V.","Coronavirus mutation; Feline coronavirus; Feline infectious peritonitis","RNA; amino acid sequence; animal experiment; animal model; article; cat disease; controlled study; Coronavirus; epidemic; gene deletion; genetic procedures; nonhuman; open reading frame; phylogeny; point mutation; sequence analysis; virus isolation; Amino Acid Sequence; Animals; Cats; Coronavirus, Feline; Disease Transmission, Vertical; Feline Infectious Peritonitis; Gene Deletion; Molecular Sequence Data; Open Reading Frames; Point Mutation; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; United States; Coronavirus; Felidae; Feline coronavirus; Felis catus","Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebred catteries (1996) Feline Pract., 24 (1), pp. 14-22; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronavirus: Comparative sequence analysis of the ORF 7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Horzinek, M.C., Herrewegh, A., De Groot, R.J., Perspectives on feline coronavirus evolution (1995) Feline Pract., 23, pp. 34-39; Hoskins, J.D., Coronavirus infection in cats (1993) Veterinary Clinics of North America: Small Animal Practice, pp. 1-16. , Hoskins, J.D., Loar, A.S. (Eds.). W.B. Saunders Company, Philadelphia, PA; Kennedy, M.A., Brenneman, K., Millsaps, K., Black, J., Potgieter, L.N.D., Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis (1998) J. Vet. Diag. Invest., 10, pp. 93-97; O'Brien, S.J., Roelke, M.E., Marker, L., Newman, A., Winkler, C.A., Meltzer, D., Colly, L., Wildt, D.E., Genetic basis for species vulnerability in the cheetah (1985) Science, 227, pp. 1428-1434; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-20; Poland, A.M., Vennema, H., Foley, J., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34 (12), pp. 3180-3184; Scott, F.W., Corapi, W.V., Olsen, C.W., Evaluation of the safety and efficacy of Primucell-FIP vaccine (1992) Feline Health Topics, 7, pp. 6-8; Vennema, H., Rossen, J.W.A., Wesseling, J., Horzinek, M.C., Rottier, P.J.M., Genomic organization and expression of the 3′-end of the canine and feline enteric coronaviruses (1992) Virology, 91, pp. 134-140; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Wolf, J., The impact of feline infectious peritonitis on catteries (1995) Feline Pract., 23, pp. 21-23",,,,03781135,,,"11390106","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0035828241
"Vabret A., Mouthon F., Mourez T., Gouarin S., Petitjean J., Freymuth F.","7003959575;15736098500;8553384500;56107903900;7006379234;7103410207;","Direct diagnosis of human respiratory coronaviruses 229E and OC43 by the polymerase chain reaction",2001,"Journal of Virological Methods","97","1-2",,"59","66",,61,"10.1016/S0166-0934(01)00343-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034904937&doi=10.1016%2fS0166-0934%2801%2900343-3&partnerID=40&md5=e47657b61f83ad9425b30d94b78ff3c1","Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France; ENS.45, Rue d'Ulm, 75 005 Paris, France","Vabret, A., Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France; Mouthon, F., ENS.45, Rue d'Ulm, 75 005 Paris, France; Mourez, T., Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France; Gouarin, S., Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France; Petitjean, J., Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France; Freymuth, F., Laboratory of Human and Molecular Virology, University Hopital, Av. Georges Clemenceau, 14 033 Caen, France","An RT-PCR-hybridization was developed that amplified genetic material from the M protein gene of HCoV-229E and HCoV-OC43. The analytic sensitivity of these original primers were compared with primers defined in the N gene and described previously. The results show that 0.05 TCID50 of HCoV-229E and 0.01 TCID50 of HCoV-OC43 can be detected by this molecular method using the original method. Detection of HCoV-229E and HCoV-OC43 in clinical specimens is possible using this method: 348 respiratory specimens (202 sputum and 146 nasal aspirates) were tested with this RT-PCR-hybridization and 12 human coronavirus are detected (3%). The method could provide a useful tool for demonstrating the role of human coronavirus in infections of the respiratory tract. © 2001 Elsevier Science B.V. All rights reserved.","Gene M; HcoV-229E; HcoV-OC43; Molecular method; Respiratory coronavirus","M protein; adult; article; aspiration; asthma; controlled study; Coronavirus; gene amplification; human; human cell; hybridization; major clinical study; nonhuman; priority journal; respiratory tract infection; reverse transcription polymerase chain reaction; sputum analysis; virus detection; virus diagnosis; virus strain; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus OC43, Human; DNA Primers; Humans; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sensitivity and Specificity; Viral Matrix Proteins; Coronavirus; human coronavirus","Cantaloube, J.F., Charrel, R.N., Attoui, H., Biagini, P., De Micco, P., De Lamballerie, X., Evaluation of four PCR sustems amplifying different genomic regions for molecular diagnosis of GB virus C infections (1997) J. Virol. Methods, 64, pp. 131-135; Freymuth, F., Quibriac, M., Petitjean, J., Daon, F., Amiel, M.L., Les virus responsables d'infections respiratoires en pédiatrie. Bilan de 3480 aspirations nasales réalisées chez l'enfant sur une période de six ans (1987) Ann. Pédiatr., 34, pp. 493-501; Freymuth, F., Eugène, G., Vabret, A., Petitjean, J., Gennetay, E., Brouard, J., Duhamel, J.F., Guillois, B., Detection of Respiratory Syncytial Virus by reverse transcription-PCR and hybridization with a DNA enzyme immunoassay (1995) J. Clin. Microbiol., 33 (12), pp. 3352-3355; Freymuth, F., Vabret, A., Brouard, J., Toutain, F., Verdon, R., Petitjean, J., Gouarin, S., Guillois, B., Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae in exacerberations of asthma in children (1999) J. Clin. Virol., 13, pp. 131-139; Garcia F., Jr., Garcia, F., Bernal, M.C., Leyva, A., Piedrola, G., Maroto, M.C., Evaluation of enzyme immunoassay for hepatitis B virus DNA based on anti-double-stranded DNA (1995) J. Clin. Microbiol., 33 (2), pp. 413-415; Ieven, M., Goossens, H., Relevance of nucleic acid amplification techniques for diagnosis of respiratory tract infections in the clinical laboratory (1997) Clin. Microbiol. Rev., 10 (2), pp. 242-256; Jouvenne, P., Richarson, C.D., Schreiber, S.S., Lai, M., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus 229E (1990) Virology., 169, pp. 142-151; Levy, R., Najioullah, F., Thouvenot, D., Bosshard, S., Aymard, M., Lina, B., Evaluation and comparison of PCR and hybridization methods for rapid detection of cytomegalovirus in clinical samples (1996) J. Virol. Methods, 62 (2), pp. 103-111; Myint, S.H., Human coronavirus: A brief review (1994) Medical Virol., 4, pp. 35-46; Myint, S.H., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol. Cell. Probes, 8, pp. 357-364; Nokso-Koivisto, J., Pitkäranta, A., Blomvist, S., Kilpi, T., Hovi, T., Respiratory coronavirus infections in children younger than two years of age (2000) Pediatr. Infect. Dis., 19 (2), pp. 164-166; Rottier, P.J.M., The coronavirus membrane glycoprotein (1995) The Coronaviridae, pp. 115-139. , Siddell, Ed Stuart G.(Ed.), Plenum Press, New York; Sizun, J., Arbour, N., Talbot, P.J., Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture (1998) J. Virol. Methods, 72 (2), pp. 145-152; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Stewart, J.N., Mounir, S., Talbot, P.J., Detection of coronaviruses by the polymerase chain reaction (1995) Diagnosis of Human Viruses by Polymerase Chain Reaction Technology, pp. 316-327. , Becker, Y., Daraï, G. (Eds.). Springer-Verlag, New York; Trigg, C.L., Nicholson, K.G., Wang, J.H., Bronchial inflammation and the common cold: A comparison of atopic and non-atopic individuals (1996) Clin. Exp. Allergy, 26, pp. 665-676; Vabret, A., Brouard, J., Petitjean, J., Eugène-Ruellan, G., Freymuth, F., Infections à coronavirus humains, importance et diagnostic (1998) La Presse Médicale, 27 (35), pp. 1813-1818; Van Der Most, R.G., Spaan, W.J.M., Coronavirus. Replication. Transcription, and RNA Recombinaison (1995) The Coronaviridae, pp. 11-33. , Siddell, Ed Stuart G. (Ed.). Plenum Press, New York","Vabret, A.; Lab. of Human/Molecular Virology, University Hopital, av. Georges Clemenceau, 14 033 Caen, France; email: vabret-a@chu-caen.fr",,,01660934,,JVMED,"11483217","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0034904937
"Mckean M.C., Leech M., Lambert P.C., Hewitt C., Myint S., Silverman M.","7004143832;7005703973;7402303348;7202923866;35479862600;7403299029;","A model of viral wheeze in nonasthmatic adults: Symptoms and physiology",2001,"European Respiratory Journal","18","1",,"23","32",,20,"10.1183/09031936.01.00073101","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034895229&doi=10.1183%2f09031936.01.00073101&partnerID=40&md5=406008b48c5421d8268d22343474a9e8","Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom","Mckean, M.C., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom; Leech, M., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom; Lambert, P.C., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom; Hewitt, C., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom; Myint, S., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom; Silverman, M., Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom","Episodic wheezing associated with viral infections of the upper respiratory tract (URT) is a common problem in young children but also occurs in adults. It is hypothesized that an experimental infection with human coronavirus (HCoV), the second most prevalent common cold virus, would cause lower respiratory tract (LRT) changes in adults with a history of viral wheeze. Twenty-four viral wheezers (15 atopic) and 19 controls (seven atopic) were inoculated with HCoV 229E and monitored for the development of symptoms, changes in airway physiology and provocative concentration of methacholine causing a 20% fall in forced expiratory volume in one second (FEV1) (PC20). At baseline, viral wheezers were similar to controls in PC20 (mean±SD log2PC20: 5.1±1.9 and 5.8±1.4 g·L-1, respectively) but had a lower FEV1 than controls (mean±SD 85.8±11.4 and 95.6±13.2% predicted, respectively p &lt; 0.05). Nineteen viral wheezers and 11 controls developed colds. Viral wheezers with colds reported significantly more URT symptoms than controls (median scores (interquartile range): 24 (10-37) and 6 (4-15), respectively p=0.014). Sixteen viral wheezers and no controls reported LRT symptoms (wheeze, chest tightness and shortness of breath). The viral wheezers with colds had small (3-4%) reductions in FEV1 and peak expiratory flow on days with LRT symptoms (days 3-6), but a progressive reduction in PC20 from baseline on days 2, 4 and 17 after inoculation (by 0.82, 1.35 and 1.82 doubling concentrations, respectively). The fall in PC20 affected both atopic and nonatopic subjects equally. There were no changes in FEV1 or PC20 in controls. An adult model of viral wheeze that is independent of atopy and therefore, of classical atopic asthma was established.","Paediatrics; Viral infection; Wheezing","methacholine; adult; airway; allergic asthma; anamnesis; article; asthma; atopy; clinical article; common cold; controlled study; Coronavirus; disease model; dyspnea; female; forced expiratory volume; human; hypothesis; inoculation; lower respiratory tract; male; patient monitoring; peak expiratory flow; physiology; priority journal; provocation; symptom; upper respiratory tract infection; virus infection; wheezing; Adult; Airway Resistance; Asthma; Bronchial Provocation Tests; Common Cold; Coronavirus Infections; Female; Humans; Intradermal Tests; Male; Respiratory Sounds; Respiratory Tract Infections; Rhinitis, Allergic, Perennial; Risk Factors","Silverman, M., Out of the mouths of babes and sucklings: Lessons from early childhood asthma (1993) Thorax, 48, p. 1200; Martinez, F.D., Wright, A.L., Taussig, L.M., Asthma and wheezing in the first six years of life (1995) N Engl J Med, 332, pp. 133-138; Godden, D.J.S., Ross, S., Abdalla, M., Outcome of wheeze in childhood. Symptoms and pulmonary function 25 years later (1994) Am J Respir Crit Care Med, 149, pp. 106-112; Mckean, M.C., Ducharme, F., Inhaled steroids for episodic viral wheeze in children (1999), Cochrane Library; Stevenson, E.C., Turner, G., Heaney, L.G., Bronchoalveolar lavage findings suggest two different forms of childhood asthma (1997) Clin Exp Allergy, 27, pp. 1027-1035; Lemanske R.F., Jr., Dick, E.C., Swenson, C.A., Vrtis, R.F., Busse, W.W., Rhinovirus upper respiratory infection increases airway hyperreactivity and late asthmatic reactions (1989) J Clin Invest, 83, pp. 1-10; Cheung, D.E., Dick, C., Timmers, M.C., de Klerk, E.P., Spaan, W.J., Sterk, P.J., Rhinovirus inhalation causes long-lasting excessive airway narrowing in response to methacholine in asthmatic subjects in vivo (1995) Am J Respir Crit Care Med, 152, pp. 1490-1496; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Eur Arch Otorhinolaryngol, 151, pp. S879-S886; Gern, J.E., Calhoun, W., Swenson, C., Shen, G., Busse, W.W., Rhinovirus infection preferentially increases lower airway responsiveness in allergic subjects (1997) Am J Respir Crit Care Med, 155, pp. 1872-1876; Grunberg, K., Smits, H.H., Timmers, M.C., Experimental rhinovirus 16 infection: Effects on cell differentials and soluble markers in sputum in asthmatic subjects (1997) Am J Respir Crit Care Med, 156, pp. 609-616; Isaacs, D., Flowers, D., Clarke, J.R., Valman, H.B., Macnaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch Dis Child, 58, pp. 500-503; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, M.A., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Inf Dis, 130, pp. 502-507; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) BMJ, 307, pp. 982-986; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Crapo, R.O., Hankinson, J.L., Irvin, C., Standardization of spirometry: 1994 Update (1995) Am J Respir Crit Care Med, 152, pp. 1107-1136; Jackson, G.G., Dowling, H.F., Speisman, I.G., Boand, A.V., Transmission of the common cold under controlled conditions. 1. The common cold as a clinical entity (1958) Arch Intern Med, 101, pp. 267-278; Myint, S., Siddell, S., Tyrrell, D., Detection of human coronavirus 229E in nasal washings using RNA: RNA hybridisation (1989) J Med Virol, 29, pp. 70-73; Gwaltney J.M., Jr., Hendley, O., Hayden, F.G., Updated recommendations for safety-testing of viral inocula used in volunteer experiments on rhinovirus colds (1992) Prog Med Virol, 39, pp. 256-263; Sterk, P.J., Fabbri, L.M., Quanjer, P.H., Airway responsiveness. Standardized challenge testing with pharmacological, physical and sensitizing stimuli in adults (1993) Eur Respir J, 6, pp. S53-S83; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Koren, H.S., Hatch, G.E., Graham, D.E., Nasal lavage as a tool in assessing acute inflammation in response to inhaled pollutants (1990) Toxicology, 60, pp. 15-25; Kraaijeveld, C.A., Reed, S.E., Macnaughton, M.R., Enzyme-linked immunosorbent assay for detection of antibody in volunteers experimentally infected with human coronavirus strain 229 E (1980) J Clin Microbiol, 12, pp. 493-497; Knudson, R.J., Slatin, R.C., Lebowitz, M.D., Burrows, B., The maximal expiratory flow-volume curve. 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Oxford, Blackwell Scientific; Trigg, C.J., Nicholson, K.G., Wang, J.H., A comparison of atopic and non-atopic individuals (1996) Clin Exper Allergy, 26, pp. 665-676; Folkerts, G., Busse, W.W., Nijkamp, F.P., Sorkness, R., Gem, J.E., Virus-induced airway hyperresponsiveness and asthma (1998) Am J Respir Crit Care Med, 157, pp. 1708-1720; Jacoby, D.B., Fryer, A.D., Interaction of viral infections with muscarinic receptors (1999) Clinical & Exper Allergy, 29, pp. S59-S64; Macek, V., Hogg, J.C., The persistence of respiratory viruses in asthma: The host response in viral bronchiolitis and asthma (1998) Eur Respir Rev, 8, pp. 1108-1110; Pizzichini, M.M.M., Pizzichini, E., Efthimiadis, A., Asthma and natural colds. Inflammatory indices in induced sputum: A feasibility study (1998) Am J Respir Crit Care Med, 158, pp. 1178-1184; Gern, J.E., Vrtis, R., Kelly, E.A., Dick, E.C., Busse, W.W., Rhinovirus produces nonspecific activation of lymphocytes through a monocyte-dependent mechanism (1996) J Immunol, 157, pp. 1605-1612; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161","Mckean, M.C.; Children's Asthma Centre, Department of Child Health, University of Leicester, Robert Kilpatrick Clin. Sci. Bldg., Leicester LE2 7LX, United Kingdom",,,09031936,,ERJOE,"11510797","English","Eur. Respir. J.",Article,"Final",Open Access,Scopus,2-s2.0-0034895229
"Ozdarendeli A., Ku S., Rochat S., Williams G.D., Senanayake S.D., Brian D.A.","6602775874;11438944700;6603226632;7406083594;7004008817;7006460232;","Downstream sequences influence the choice between a naturally occurring noncanonical and closely positioned upstream canonical heptameric fusion motif during bovine coronavirus subgenomic mRNA synthesis",2001,"Journal of Virology","75","16",,"7362","7374",,42,"10.1128/JVI.75.16.7362-7374.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034905254&doi=10.1128%2fJVI.75.16.7362-7374.2001&partnerID=40&md5=4623f69b86c33d4f4c5fd418df017e5d","Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Ozdarendeli, A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Ku, S., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Rochat, S., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Williams, G.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Senanayake, S.D., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Mechanisms leading to subgenomic mRNA (sgmRNA) synthesis in coronaviruses are poorly understood but are known to involve a heptameric signaling motif, originally called the intergenic sequence. The intergenic sequence is the presumed crossover region (fusion site) for RNA-dependent RNA polymerase (RdRp) during discontinuous transcription, a process leading to sgmRNAs that are both 5′ and 3′ coterminal. In the bovine coronavirus, the major fusion site for synthesis of mRNA 5 (GGUAGAC) does not conform to the canonical motif (UC[U,C]AAAC) at three positions (underlined), yet it lies just 14 nucleotides downstream from such a sequence (UCCAAAC). The infrequently used canonical sequence, by computer prediction, is buried within the stem of a stable hairpin (-17.2 kcal/mol). Here we document the existence of this stem by enzyme probing and examine its influence and that of neighboring sequences on the unusual choice of fusion sites by analyzing transcripts made in vivo from mutated defective interfering RNA constructs. We learned that (i) mutations that were predicted to unfold the stem-loop in various ways did not switch RdRp crossover to the upstream canonical site, (ii) a totally nonconforming downstream motif resulted in no measurable transcription from either site, (iii) the canonical upstream site does not function ectopically to lend competence to the downstream noncanonical site, and (iv) altering flanking sequences downstream of the downstream noncanonical motif in ways that diminish sequence similarity with the virus genome 5′ end caused a dramatic switch to the upstream canonical site. These results show that sequence elements downstream of the noncanonical site can dramatically influence the choice of fusion sites for synthesis of mRNA 5 and are interpreted as being most consistent with a mechanism of similarity-assisted RdRp strand switching during minus-strand synthesis.",,"RNA directed RNA polymerase; 5' untranslated region; article; Coronavirus; crossing over; DNA flanking region; gene fusion; gene mutation; gene switching; messenger RNA synthesis; nonhuman; nucleotide sequence; priority journal; RNA sequence; RNA transcription; sequence homology; virus genome; Animals; Base Sequence; Cattle; Coronavirus, Bovine; Genome, Viral; Molecular Sequence Data; Mutation; RNA, Messenger; RNA, Viral; Transcription, Genetic","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Sequence and expression analysis of potential nonstructural proteins of 4.9, 4.8, 12.7 and 9.5 kilodaltons encoded between the spike and membrane protein genes of the bovine coronavirus (1990) Virology, 177, pp. 488-495; An, S., Makino, S., Characterization of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency (1998) Virology, 243, pp. 198-207; Baric, R.S., Shieh, C.-K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. 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"Blau D.M., Turbide C., Tremblay M., Olson M., Ĺtourneau S., Michaliszyn E., Jothy S., Holmes K.V., Beauchemin N.","15729433700;6603461883;7202066888;8783067500;8783067600;6507917769;7005657762;7201657724;7005461095;","Targeted disruption of the Ceacam1 (MHVR) gene leads to reduced susceptibility of mice to mouse hepatitis virus infection",2001,"Journal of Virology","75","17",,"8173","8186",,31,"10.1128/JVI.75.17.8173-8186.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034878935&doi=10.1128%2fJVI.75.17.8173-8186.2001&partnerID=40&md5=417834b34d38801ed19d088f67666cbf","McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada","Blau, D.M., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Turbide, C., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Tremblay, M., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Olson, M., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Ĺtourneau, S., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Michaliszyn, E., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Jothy, S., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Holmes, K.V., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; Beauchemin, N., McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada","The CEACAM1 glycoproteins (formerly called biliary glycoproteins; BGP, C-CAM, CD66a, or MHVR) are members of the carcinoembryonic antigen family of cell adhesion molecules. In the mouse, splice variants of CEACAM1 have either two or four immunoglobulin (Ig) domains linked through a transmembrane domain to either a short or a long cytoplasmic tail. CEACAM1 has cell adhesion activity and acts as a signaling molecule, and long-tail isoforms inhibit the growth of colon and prostate tumor cells in rodents. CEACAM1 isoforms serve as receptors for several viral and bacterial pathogens, including the murine coronavirus mouse hepatitis virus (MHV) and Haemophilus influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis in humans. To elucidate the mechanisms responsible for the many biological activities of CEACAM1, we modified the expression of the mouse Ceacam1 gene in vivo. Manipulation of the Ceacam1 gene in mouse embryonic stem cells that contained the Ceacam1 allele yielded a partial knockout. We obtained one line of mice in which the insert in the Ceacam1a gene had sustained a recombination event. This resulted in the markedly reduced expression of the two CEACAM1a isoforms with four Ig domains, whereas the expression of the two isoforms with two Ig domains was doubled relative to that in wild-type BALB/c (+/+) mice. Homozygous (p/p) Ceacam1a-targeted mice (Ceacam1aΔ4D) had no gross tissue abnormalities and were viable and fertile; however, they were more resistant to MHV A59 infection and death than normal (+/+) mice. Following intranasal inoculation with MHV A59, p/p mice developed markedly fewer and smaller lesions in the liver than +/+ or heterozygous (+/p) mice. The titers of virus produced in the livers were 50- to 100-fold lower in p/p mice than in +/p or +/+ mice. p/p mice survived a dose 100-fold higher than the lethal dose of virus for +/+ mice. +/p mice were intermediate between +/+ and p/p mice in susceptibility to liver damage, virus growth in liver, and susceptibility to killing by MHV. Ceacam1a-targeted mice provide a new model to study the effects of modulation of receptor expression on susceptibility to MHV infection in vivo.",,"carcinoembryonic antigen; glycoprotein; immunoglobulin; isoprotein; animal cell; animal experiment; animal model; animal tissue; article; cell adhesion; female; gene disruption; gene expression; gene targeting; growth inhibition; infection sensitivity; knockout gene; lethal dose; liver injury; male; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein domain; protein family; tumor growth; virus hepatitis; Animals; Antigens, CD; Carcinoembryonic Antigen; Cell Adhesion Molecules; Disease Susceptibility; Gene Targeting; Genetic Engineering; Glycoproteins; Hepatitis, Viral, Animal; Kidney; Liver; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Mice, Knockout; Murine hepatitis virus; Receptors, Virus","Balfe, P., Churcher, Y., Penny, M., Easterbrook, P.J., Goodall, R.L., Galpin, S., Gotch, F., McKeating, J.A., Association between a defective CCR-5 gene and progression to disease in HIV infection (1998) AIDS Res. 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Harwood Academic Publishers, Amsterdam, The Netherlands","Beauchemin, N.; McGill Cancer Centre, McGill University, McIntyre Medical Sciences Building, 3655 Promenade Sir William Osler, Montreal, Que. H3G 1Y6, Canada; email: nicoleb@med.mcgill.ca",,,0022538X,,JOVIA,"11483763","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034878935
"Ziebuhr J., Thiel V., Gorbalenya A.E.","7003783935;35238592100;7005626044;","The Autocatalytic Release of a Putative RNA Virus Transcription Factor from Its Polyprotein Precursor Involves Two Paralogous Papain-like Proteases that Cleave the Same Peptide Bond",2001,"Journal of Biological Chemistry","276","35",,"33220","33232",,97,"10.1074/jbc.M104097200","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035980126&doi=10.1074%2fjbc.M104097200&partnerID=40&md5=cb18a8811f4a246a0dc0436cca89428f","Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Advanced Biomedical Computing Center, Sci. Applic. Intl. Corporation, NCI-F. Cancer Res./Devmt. Ctr., 430 Miller Dr., Frederick, MD 21702-1201, United States","Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Thiel, V., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Gorbalenya, A.E., Advanced Biomedical Computing Center, Sci. Applic. Intl. Corporation, NCI-F. Cancer Res./Devmt. Ctr., 430 Miller Dr., Frederick, MD 21702-1201, United States","The largest replicative protein of coronaviruses is known as p195 in the avian infectious bronchitis virus (IBV) and p210 (p240) in the mouse hepatitis virus. It is autocatalytically released from the precursors pp1a and pp1ab by one zinc finger-containing papain-like protease (PLpro) in IBV and by two paralogous PLpros, PL1pro and PL2pro, in mouse hepatitis virus. The PLpro-containing proteins have been recently implicated in the control of coronavirus subgenomic mRNA synthesis (transcription). By using comparative sequence analysis, we now show that the respective proteins of all sequenced coronaviruses are flanked by two conserved PLpro cleavage sites and share a complex (multi)domain organization with PL1pro being inactivated in IBV. Based upon these predictions, the processing of the human coronavirus 229E p195/p210 N terminus was studied in detail. First, an 87-kDa protein (p87), which is derived from a pp1a/pp1ab region immediately upstream of p195/p210, was identified in human coronavirus 229E-infected cells. Second, in vitro synthesized proteins representing different parts of pp1a were autocatalytically processed at the predicted site. Surprisingly, both PL1pro and PL2pro cleaved between p87 and p195/p210. The PL1pro-mediated cleavage was slow and significantly suppressed by a non-proteolytic activity of PL2pro. In contrast, PL2pro, whose proteolytic activity and specificity were established in this study, cleaved the same site efficiently in the presence of the upstream domains. Third, a correlation was observed between the overlapping substrate specificities and the parallel evolution of PL1pro and PL2pro. Collectively, our results imply that the p195/p210 autoprocessing mechanisms may be conserved among coronaviruses to an extent not appreciated previously, with PL2pro playing a major role. A large subset of coronaviruses may employ two proteases to cleave the same site(s) and thus regulate the expression of the viral genome in a unique way.",,"Chemical bonds; Diseases; Enzymes; RNA; Synthesis (chemical); Viruses; Autoprocessing mechanisms; Biochemistry; papain; polyprotein; protein precursor; proteinase; transcription factor; zinc finger protein; messenger RNA; papain; primer DNA; recombinant protein; virus protein; virus RNA; amino terminal sequence; article; Avian infectious bronchitis virus; chemical bond; controlled study; Coronavirus; DNA flanking region; enzyme mechanism; enzyme specificity; gene expression regulation; gene inactivation; genetic conservation; human; human cell; messenger RNA synthesis; Murine hepatitis coronavirus; nonhuman; priority journal; protein degradation; protein processing; protein synthesis; RNA virus; sequence analysis; virus genome; amino acid sequence; animal; catalysis; cattle; cell line; chemistry; Coronavirus; fibroblast; genetics; metabolism; molecular genetics; mouse; nucleotide sequence; open reading frame; phylogeny; polymerase chain reaction; probability; RNA virus; sequence alignment; sequence homology; Aves; Avian infectious bronchitis virus; Coronavirus; Human coronavirus 229E; Murinae; Murine hepatitis virus; RNA viruses; Amino Acid Sequence; Animals; Base Sequence; Catalysis; Cattle; Cell Line; Conserved Sequence; Coronavirus; Coronavirus 229E, Human; Coronavirus, Bovine; DNA Primers; Endopeptidases; Fibroblasts; Humans; Infectious bronchitis virus; Markov Chains; Mice; Molecular Sequence Data; Murine hepatitis virus; Open Reading Frames; Papain; Phylogeny; Polymerase Chain Reaction; Protein Processing, Post-Translational; Recombinant Proteins; RNA Viruses; RNA, Messenger; RNA, Viral; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factors; Viral Proteins","Kräusslich, H.G., Wimmer, E., (1988) Annu. 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G., ed), Plenum Press, New York; Ryan, M.D., Flint, M., (1997) J. Gen. Virol., 78, pp. 699-723; Bi, W., Piñón, J.D., Hughes, S., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., (1998) J. Neurovirol., 4, pp. 594-605; Gorbalenya, A.E., Koonin, E.V., (1993) Sov. Sci. Rev. Sect. D Physicochem. Biol., 11, pp. 1-84; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., (1994) Virology, 198, pp. 736-740","Ziebuhr, J.; Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; email: ziebuhr@vim.uni-wuerzburg.de",,,00219258,,JBCHA,"11431476","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0035980126
"Banerjee S., Repass J.F., Makino S.","55851941933;57186535600;7403067550;","Enhanced accumulation of coronavirus defective interfering RNA from expressed negative-strand transcripts by coexpressed positive-strand RNA transcripts",2001,"Virology","287","2",,"286","300",,1,"10.1006/viro.2001.1047","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035450961&doi=10.1006%2fviro.2001.1047&partnerID=40&md5=65855cbc608298f3fd39cc3dab31699e","Department of Microbiology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States; Department of Microbiology and Immunology, University of Texas, Medical Branch at Galveston, Galveston, TX 77555-1019, United States","Banerjee, S., Department of Microbiology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States, Department of Microbiology and Immunology, University of Texas, Medical Branch at Galveston, Galveston, TX 77555-1019, United States; Repass, J.F., Department of Microbiology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States, Department of Microbiology and Immunology, University of Texas, Medical Branch at Galveston, Galveston, TX 77555-1019, United States; Makino, S., Department of Microbiology, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, United States, Department of Microbiology and Immunology, University of Texas, Medical Branch at Galveston, Galveston, TX 77555-1019, United States","Expression of negative-strand murine coronavirus mouse hepatitis virus (MHV) defective interfering (DI) RNA transcripts in MHV-infected cells results in the accumulation of positive-strand DI RNAs (M. Joo et al., 1996, J. Virol. 70, 5769-5776). However, the expressed negative-strand DI RNA transcripts are poor templates for positive-strand DI RNA synthesis. The present study demonstrated that DI RNA accumulation from the expressed negative-strand DI RNA transcripts in MHV-infected cells was enhanced by the coexpression of complementary RNA transcripts that correspond to the 5′ region of positive-strand DI RNA. The positive-strand RNA transcripts corresponding to the 5′ end-most 0.7-2.0 kb DI RNA had a similar enhancement effect. The coexpressed positive-strand RNA transcripts lacking the leader sequence or those containing only the leader sequence failed to demonstrate this enhancement effect, demonstrating that the presence of the leader sequence in the coexpressed positive-strand RNA transcripts was necessary, but not sufficient, for the enhancement of DI RNA accumulation from the coexpressed negative-strand DI RNA transcripts. Negative-strand DI RNA transcripts that were coexpressed with the partial-length positive-strand RNA transcripts were no more stable than those expressed alone, suggesting that a higher stability of the expressed negative-strand RNA transcripts was an unlikely reason for the higher DI RNA accumulation in cells coexpressing two complementary DI RNA transcripts. Sequence analyses unexpectedly demonstrated that the leader sequence of the majority of accumulated DI RNAs switched to helper virus derived leader sequence, suggesting that enhancement of DI RNA accumulation was mediated by the efficient utilization of helper virus derived leader sequence for DI RNA synthesis. Furthermore, our data suggested that this leader switching, a type of homologous RNA-RNA recombination, occurred during positive-strand DI RNA synthesis and that MHV positive-strand RNA synthesis mechanism may have a preference toward recognizing double-stranded RNA structures over single-stranded negative-strand RNA to produce positive-strand DI RNAs. © 2001 Academic Press.","Coronaviruses; Defective-interfering RNA; Double-stranded RNAs; Leader sequence; Leader switching; Mouse hepatitis virus; Negative-strand RNA; RNA expression; RNA recombination; RNA replication","complementary RNA; double stranded RNA; signal peptide; virus RNA; article; controlled study; Coronavirus; defective virus; gene expression; genetic analysis; helper virus; Murine hepatitis coronavirus; nonhuman; priority journal; RNA recombination; RNA replication; RNA stability; RNA synthesis; sequence analysis; viral genetics; Coronavirus; Murinae; Murine hepatitis virus","An, S., Maeda, A., Makino, S., Coronavirus transcription early in infection (1998) J. 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USA, 86 (14), pp. 5626-5630; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2 (10), pp. 1839-1844; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Cavanagh, D., Britton, P., Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81 (PART 3), pp. 791-801; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65 (6), pp. 3219-3226; Van der Most, R.G., De Groot, R.J., Spaan, W.J., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68 (6), pp. 3656-3666; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96 (21), pp. 12056-12061; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71 (1), pp. 824-827","Makino, S.; Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,"Academic Press Inc.",00426822,,VIRLA,"11531407","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0035450961
"Watt S.M., Teixeira A.M., Zhou G.-Q., Doyonnas R., Zhang Y., Grunert F., Blumberg R.S., Kuroki M., Skubitz K.M., Bates P.A.","7102659490;56559328400;23394245100;6602247912;57196210650;7003755998;7102990864;56531509500;7006006597;56463571400;","Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: Structural analysis of the binding site",2001,"Blood","98","5",,"1469","1479",,80,"10.1182/blood.V98.5.1469","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035469860&doi=10.1182%2fblood.V98.5.1469&partnerID=40&md5=8068406a43c4e0d6e74bf6dbb9b5ae5f","Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom; Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal; GENOVAC AG, Freiburg, Germany; Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States; First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan; University of Minnesota, Medical School, Minneapolis, MN, United States; Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Stem Cell Laboratory, National Blood Service, John Radcliffe Hospital, Headington, Oxford, OX3 9DS, United Kingdom","Watt, S.M., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom, Stem Cell Laboratory, National Blood Service, John Radcliffe Hospital, Headington, Oxford, OX3 9DS, United Kingdom; Teixeira, A.M., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Zhou, G.-Q., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Doyonnas, R., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Zhang, Y., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Grunert, F., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Blumberg, R.S., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Kuroki, M., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Skubitz, K.M., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom; Bates, P.A., Nuffield Department of Clinical and Laboratory Sciences, MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford, United Kingdom, Faculdade de Ciencias do Desporto e Educacao Fisica, Universidade de Coimbra, Coimbra, Portugal, GENOVAC AG, Freiburg, Germany, Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States, First Department of Biochemistry, School of Medicine, Fukuoka University, Fukuoka, Japan, University of Minnesota, Medical School, Minneapolis, MN, United States, Biomolecular Modelling Laboratory, Imperial Cancer Research Fund, London, United Kingdom","CEACAM1 on leukocytic, endothelial, and epithelial cells functions in homophilic adhesion, tumor suppression, regulating cell adhesion and proliferation, and in heterophilic adhesion as a receptor for E-selectin and Neisseria meningiditis, Neisseria gonorrhoeae, Haemophilus influenzae, and murine coronaviruses. The 8 transmembrane isoforms of human CEACAM1 possess an extracellular N-terminal IgV domain, followed by variable numbers of IgC2 domains. To establish which key amino acids contribute specifically to CEACAM1 homophilic adhesion, exposed amino acids in the N-terminal domain of a soluble form of CEACAM1 were subjected to mutagenesis. Analyses of mutant proteins with conformationally dependent antibodies indicated that most mutations did not substantially affect the structural integrity of CEACAM1. Nevertheless, decreased adhesion was observed for the single mutants V39A or D40A (single-letter amino acid codes) in the CC′ loop and for the triple mutants located in the GFCC′C″ face of the N-terminal domain. Interestingly, whereas single mutations in R64 or D82 that are predicted to form a salt bridge between the base of the D and F β strands close to the critical V39 and D40 residues also abolish adhesion, an amino acid swap (R64D and D82R), which maintains the salt bridge was without significant effect. These studies indicate that the CC′ loop plays a crucial role in the homophilic adhesion of CEACAM1. They further predict that specific hydrophobic amino acid residues on the nonglycosylated GFCC′C″ face of CEACAM1 N-terminal domain are not only involved in heterophilic interactions with Opa proteins and H influenzae, but are also critical for protein-protein interactions between 2 CEACAM1 molecules on opposing cells. © 2001 by The American Society of Hematology.",,"amino acid; carcinoembryonic antigen; carcinoembryonic antigen related cell adhesion molecule 1; gene product; mutant protein; unclassified drug; amino acid sequence; amino terminal sequence; animal cell; article; binding site; cancer inhibition; cell proliferation; controlled study; Coronavirus; epithelium cell; female; gene control; gene mutation; Haemophilus influenzae; hydrophobicity; immunoglobulin variable region; leukocyte; mouse; multigene family; mutagenesis; mutational analysis; Neisseria gonorrhoeae; Neisseria meningitidis; nonhuman; priority journal; protein analysis; protein binding; protein conformation; protein domain; protein localization; protein protein interaction; rat; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antigens, CD; Antigens, Differentiation; Binding Sites; Carcinoembryonic Antigen; Cell Adhesion; Cell Adhesion Molecules; CHO Cells; Cricetinae; Cricetulus; Epitopes; Humans; Models, Molecular; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Organ Specificity; Protein Conformation; Protein Isoforms; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship","Obrink, B., CEA adhesion molecules: Multifunctional proteins with signal-regulatory properties (1997) Curr Opin Cell Biol, 9, pp. 616-626; Beauchemin, N., Draber, P., Dveksler, G., Redefined nomenclature for members of the carcinoembryonic antigen family (1999) Exp Cell Res, 252, pp. 243-249; Watt, S.M., Sala-Newby, G., Hoang, T., CD66 identifies a neutrophil-specific epitope within the hematopoietic system that is expressed by members of the carcinoembryonic antigen family of adhesion molecules (1991) Blood, 78, pp. 63-74; 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"Penzes Z., González J.M., Calvo E., Izeta A., Smerdou C., Méndez A., Sánchez C.M., Sola I., Almazán F., Enjuanes L.","55761804900;57201828108;12801394500;6602523425;6602856664;36823007700;57193985365;7003336781;6603712040;7006565392;","Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the purdue virus cluster",2001,"Virus Genes","23","1",,"105","118",,63,"10.1023/A:1011147832586","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034871574&doi=10.1023%2fA%3a1011147832586&partnerID=40&md5=702be27e98d72625cdc547238c74a9c0","Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain","Penzes, Z., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; González, J.M., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Calvo, E., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Izeta, A., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Smerdou, C., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Méndez, A., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Sánchez, C.M., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Sola, I., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Almazán, F., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain","The complete sequence (28580 nt) of the PUR46-MAD clone of the Purdue cluster of transmissible gastroenteritis coronavirus (TGEV) has been determined and compared with members of this cluster and other coronaviruses. The computing distances among their S gene sequences resulted in the grouping of these coronaviruses into four clusters, one of them exclusively formed by the Purdue viruses. Three new potential sequence motifs with homology to the α-subunit of the polymerase-associated nucleocapsid phosphoprotein of rinderpest virus, the Bowman-Birk type of proteinase inhibitors, and the metallothionein superfamily of cysteine rich chelating proteins have been identified. Comparison of the TGEV polymerase sequence with that of other RNA viruses revealed high sequence homology with the A-E domains of the palm subdomain of nucleic acid polymerases.","Coronavirus; Genome; RNA virus; Sequence; TGEV","cysteine proteinase; metallothionein; phosphoprotein; proteinase inhibitor; RNA polymerase; virus RNA; animal tissue; article; Cattle plague virus; Coronavirus; gene cluster; gene sequence; molecular cloning; nonhuman; nucleotide sequence; priority journal; sequence homology; swine disease; virus nucleocapsid; virus strain; Amino Acid Sequence; Animals; Evolution, Molecular; Genome, Viral; Molecular Sequence Data; Open Reading Frames; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Swine; Transmissible gastroenteritis virus","Almazan, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., (2000) Proc Natl Acad Sci USA, 97, pp. 5516-5521; Ballesteros, M.L., Sánchez, C.M., Enjuanes, L., (1997) Virology, 227, pp. 378-388; Baric, R.S., Yount, B., (2000) J Virol, 74, pp. 4039-4046; Bernard, S., Laude, H., (1995) J Gen Virol, 76, pp. 2235-2241; Bohl, E.H., Cross, R.F., (1971) Ann NY Acad Sci, 176, pp. 150-161; Bohl, E.H., Gupta, P., Olquin, F., Saif, L.J., (1972) Infect Immun, 6, pp. 289-301; Bohl, E.H., Kumagai, T., (1965) Proceedings United States Livestock Sanitary Association, 69, pp. 343-350; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., (1987) J Gen Virol, 68, pp. 57-77; Brian, D.A., Dennis, D.E., Guy, J.S., (1980) J Virol, 34, pp. 410-415; Britton, P., Mawditt, K.L., Page, K.W., (1991) Virus Res, 21, pp. 181-198; Chen, C.-M., Cavanagh, D., Britton, P., (1995) Vir Res, 38, pp. 83-89; Domingo, E., Holland, J.J., (1994) The Evolutionary Biology of Viruses-Mutation Rates and Rapid Evolution of RNA Viruses, , Raven Press, New York; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., (1995) Virology, 206, pp. 817-822; Eleouet, J.F., Slee, E.A., Saurini, F., Castagne, N., Poncet, D., Garrido, C., Solary, E., Martin, S.J., (2000) J Virol, 74, pp. 3975-3983; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., (2000) Virus Taxonomy. 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Yoo, D., Pei, Y., (2001) Nidovirus: Coronavirus and Arterivirus-Full-Length Genomic Sequence of Bovine Coronavirus, , Kluwer Academic/Plenum Publishers, New York; Yount, B., Curtis, K.M., Baric, R.S., (2000) J Virol, 74, pp. 10600-10611","Enjuanes, L.; Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,09208569,,VIGEE,"11556396","English","Virus Genes",Article,"Final",Open Access,Scopus,2-s2.0-0034871574
"Glass W.G., Liu M.T., Kuziel W.A., Lane T.E.","7004536096;56174294500;7006422901;24722465300;","Reduced macrophage infiltration and demyelination in mice lacking the chemokine receptor CCR5 following infection with a neurotropic coronavirus",2001,"Virology","288","1",,"8","17",,92,"10.1006/viro.2001.1050","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035885037&doi=10.1006%2fviro.2001.1050&partnerID=40&md5=b76ab0e24c76731c040cf4b33413e696","Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States; Section of Molecular Genetics and Microbiology, Institute for Cellular and Molecular Biology, University of Texas, Austin, TX 78712, United States; Reeve-Irvine Research Center, University of California, Irvine, CA 92697-3900, United States","Glass, W.G., Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States; Liu, M.T., Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States; Kuziel, W.A., Section of Molecular Genetics and Microbiology, Institute for Cellular and Molecular Biology, University of Texas, Austin, TX 78712, United States; Lane, T.E., Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, United States, Reeve-Irvine Research Center, University of California, Irvine, CA 92697-3900, United States","Studies were performed to investigate the contributions of the CC chemokine receptor CCR5 in host defense and disease development following intracranial infection with mouse hepatitis virus (MHV). T cell recruitment was impaired in MHV-infected CCR5-/- mice at day 7 postinfection (pi), which correlated with increased (P ≤ 0.03) titers within the brain. However, by day 12 pi, T cell infiltration into the CNS of infected CCR5-/- and CCR5+/+ mice was similar and both strains exhibited comparable viral titers, indicating that CCR5 expression is not essential for host defense. Following MHV infection of CCR5+/+ mice, greater than 50% of cells expressing CCR5 antigen were activated macrophage/microglia (determined by F4/80 antigen expression). In addition, infected CCR5-/- mice exhibited reduced (P ≤ 0.02) macrophage (CD45highF4/80+) infiltration, which correlated with a significant reduction (P ≤ 0.001) in the severity of demyelination compared to CCR5+/+ mice. These data indicate that CCR5 contributes to MHV-induced demyelination by allowing macrophages to traffic into the CNS. © 2001 Academic Press.","Chemokine; Chemokine receptor; Demyelination; Macrophage; Multiple sclerosis; Neuroimmunology","chemokine; chemokine receptor CCR5; cytokine; adolescent; animal cell; animal model; animal tissue; antigen expression; article; brain infection; controlled study; demyelination; gene expression; host resistance; lymphocytic infiltration; macrophage; macrophage activation; microglia; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; T lymphocyte; virus infection; Coronavirus; Murine hepatitis virus","Andres, R.E., Beck, R.L., Mizoguchi, A., Bhan, A.K., Dawson, T., Kuziel, W.A., Maeda, N., Reinecker, H., Mice with a selective deletion of the CC chemokine receptors 5 or 2 are protected from dextran sodium sulfate-mediated colitus: Lack of CC chemokine receptor 5 expression results in a NK1.1+ lymphocyte associated Th2-type immune response in the intestine (2000) J. 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Immunol., 160, pp. 4018-4025; Zlotnik, A., Yoshie, O., Chemokines: A new classification system and their role in immunity (2000) Immunity, 12, pp. 121-127","Lane, T.E.; Department of Molecular Biology, Biological Sciences II, University of California, Irvine, CA 92697-3900, United States; email: tlane@uci.edu",,"Academic Press Inc.",00426822,,VIRLA,"11543653","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0035885037
"Van Benten I.J., KleinJan A., Neijens H.J., Osterhaus A.D.M.E., Fokkens W.J.","6602761888;6603838293;7005377066;55533604400;35355799700;","Prolonged nasal eosinophilia in allergic patients after common cold",2001,"Allergy: European Journal of Allergy and Clinical Immunology","56","10",,"949","956",,25,"10.1034/j.1398-9995.2001.00212.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034841076&doi=10.1034%2fj.1398-9995.2001.00212.x&partnerID=40&md5=9d2efceffc8f74da5d2d0a44b005092e","Department of Otorhinolaryngology, Erasmus Medical Centre, Rotterdam, Netherlands; Department of Paediatrics, Erasmus Medical Centre, Rotterdam, Netherlands; Institute for Virology, Erasmus Medical Centre, Rotterdam, Netherlands; Department of Otorhinolaryngology, Erasmus University Rotterdam, Dr Molewaterplein 50, 3015 GD Rotterdam, Netherlands","Van Benten, I.J., Department of Otorhinolaryngology, Erasmus Medical Centre, Rotterdam, Netherlands, Department of Otorhinolaryngology, Erasmus University Rotterdam, Dr Molewaterplein 50, 3015 GD Rotterdam, Netherlands; KleinJan, A., Department of Otorhinolaryngology, Erasmus Medical Centre, Rotterdam, Netherlands; Neijens, H.J., Department of Paediatrics, Erasmus Medical Centre, Rotterdam, Netherlands; Osterhaus, A.D.M.E., Institute for Virology, Erasmus Medical Centre, Rotterdam, Netherlands; Fokkens, W.J., Department of Otorhinolaryngology, Erasmus Medical Centre, Rotterdam, Netherlands","Background: Viral respiratory tract infections may cause both harmless common colds and severe asthma exacerbations; the differences in disease expression probably depend on the allergic status of the patient, To determine whether altered immunologic mechanisms underlie these differences, we investigated nasal inflammation during naturally acquired common cold. Methods: In a group of 16 patients (eight allergic), nasal brush samples were taken, and nasal symptoms were recorded during common cold, 2 weeks later (convalescence), and at baseline (≥ 4 weeks without nasal symptoms). Nasal brush cells were stained immunohistochemically for Langerhans cells, T cells, monocytes, neutrophils, B cells, macrophages, natural killer (NK) cells, mast cells, eosinophils, eotaxin, and RANTES, Results: Four rhinovirus, four coronavirus, three RSV, one Mycoplasma pneumoniae, and one influenza A/enterovirus double infection were confirmed, Increased numbers of T cells, monocytes, macrophages, NK cells, eosinophils, and RANTES- and eotaxin-positive cells, but not neutrophils, were observed during common cold in allergic and nonallergic patients, and increased numbers of mast cells in allergic patients. Compared to nonallergic patients, in allergic patients eosinophil influx persisted into convalescence. Conclusions: Prolonged nasal eosinophil influx was observed in allergic patients after common cold. What immunologic factors can induce prolonged eosinophil influx and whether this may increase the risk of subsequent allergen-induced hypersensitivity reactions must be studied further.","Adults; Allergy; Cell markers; Chemokines; Common cold; Immunohistochemistry; Inflammation; Respiratory infection; Virus infection","cell marker; chemokine; eotaxin; RANTES; adult; allergy; article; clinical article; common cold; controlled study; Coronavirus; disease exacerbation; disease severity; eosinophilia; female; human; hypersensitivity; immunohistochemistry; inflammation; Langerhans cell; macrophage; male; mast cell; Mycoplasma pneumoniae; natural killer cell; neutrophil; nose disease; priority journal; Respiratory syncytial pneumovirus; respiratory tract infection; Rhinovirus; virus infection; Adult; Antibodies, Monoclonal; Asthma; Chemokines, CC; Common Cold; Cytokines; Eosinophilia; Humans; Immunohistochemistry; RANTES; Time Factors","Gern, J.E., Calhoun, W., Swenson, C., Shen, G., Busse, W.W., Rhinovirus infection preferentially increases lower airway responsiveness in allergic subjects (1997) Am J Respir Crit Care Med, 155, pp. 1872-1876; Grunberg, K., Smits, H.H., Timmers, M.C., Experimental rhinovirus 16 infection. Effects on cell differentials and soluble markers in sputum in asthmatic subjects (1997) Am J Respir Crit Care Med, 156 (2 PART 1), pp. 609-616; Grunberg, K., Timmers, M.C., Smits, H.H., Effect of experimental rhinovirus 16 colds on airway hyperresponsiveness to histamine and interleukin-8 in nasal lavage in asthmatic subjects in vivo (1997) Clin Exp Allergy, 27, pp. 36-45; Hinriksdottir, I., Melen, I., Allergic rhinitis and upper respiratory tract infections (1994) Acta Otolaryngol Suppl, 515, pp. 30-32; Doyle, W.J., Skoner, D.P., Fireman, P., Rhinovirus 39 infection in allergic and nonallergic subjects (1992) J Allergy Clin Immunol, 89, pp. 968-978; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310 (6989), pp. 1225-1229; Makela, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Levandowski, R.A., Weaver, C.W., Jackson, G.G., Nasal-secretion leukocyte populations determined by flow cytometry during acute rhinovirus infection (1988) J Med Virol, 25, pp. 423-432; Pizzichini, M.M., Pizzichini, E., Efthimiadis, A., Asthma and natural colds. Inflammatory indices in induced sputum: A feasibility study (1998) Am J Respir Crit Care Med, 158, pp. 1178-1184; Winther, B., Farr, B., Turner, R.B., Hendley, J.O., Gwaltney J.M., Jr., Mygind, N., Histopathologic examination and enumeration of polymorphonuclear leukocytes in the nasal mucosa during experimental rhinovirus colds (1984) Acta Otolaryngol Suppl (Stockh), 413, pp. 19-24; Trigg, C.J., Nicholson, K.G., Wang, J.H., Bronchial inflammation and the common cold: A comparison of atopic and nonatopic individuals (1996) Clin Exp Allergy, 26, pp. 665-676; Thomas, L.H., Fraenkel, D.J., Bardin, P.G., Johnston, S.L., Holgate, S.T., Warner, J.A., Leukocyte responses to experimental infection with human rhinovirus (1994) J Allergy Clin Immunol, 94 (6 PART 2), pp. 1255-1262; Roseler, S., Holtappels, G., Wagenmann, M., Bachert, C., Elevated levels of interleukins IL-1 beta, IL-6 and IL-8 in naturally acquired viral rhinitis (1995) Eur Arch Otorhinolaryngol Suppl, 1, pp. S61-S63; Fleming, H.E., Little, F.F., Schnurr, D., Rhinovirus-16 colds in healthy and in asthmatic subjects: Similar changes in upper and lower airways (1999) Am J Respir Crit Care Med, 160, pp. 100-108; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Am J Respir Crit Care Med, 151 (3 PART 1), pp. 879-886; Godthelp, T., Holm, A.F., Fokkens, W.J., Dynamics of nasal eosinophils in response to a nonnatural allergen challenge in patients with allergic rhinitis and control subjects: A biopsy and brush study (1996) J Allergy Clin Immunol, 97, pp. 800-811; Andeweg, A.C., Bestebroer, T.M., Huybreghs, M., Kimman, T.G., De Jong, J.C., Improved detection of rhinoviruses in clinical samples by using a newly developed nested reverse transcription-PCR assay (1999) J Clin Microbiol, 37, pp. 524-530; Arruda, E., Pitkaranta, A., Witek T.J., Jr., Doyle, C.A., Hayden, F.G., Frequency and natural history of rhinovirus infections in adults during autumn (1997) J Clin Microbiol, 35, pp. 2864-2868; Calhoun, W.J., Dick, E.C., Schwartz, L.B., Busse, W.W., A common cold virus, rhinovirus 16, potentiates airway inflammation after segmental antigen bronchoprovocation in allergic subjects (1994) J Clin Invest, 94, pp. 2200-2208; Fokkens, W.J., Godthelp, T., Holm, A.F., Klein-Jan, A., Local corticosteroid treatment: The effect on cells and cytokines in nasal allergic inflammation (1998) Am J Rhinol, 12, pp. 21-26; Igarashi, Y., Skoner, D.P., Doyle, W.J., White, M.V., Fireman, P., Kaliner, M.A., Analysis of nasal secretions during experimental rhinovirus upper respiratory infections (1993) J Allergy Clin Immunol, 92, pp. 722-731; Yawalkar, N., Uguccioni, M., Scharer, J., Enhanced expression of eotaxin and CCR3 in atopic dermatitis (1999) J Invest Dermatol, 113, pp. 43-48; Ying, S., Robinson, D.S., Meng, Q., Enhanced expression of eotaxin and CCR3 mRNA and protein in atopic asthma. Association with airway hyperresponsiveness and predominant co-localization of eotaxin mRNA to bronchial epithelial and endothelial cells (1997) Eur J Immunol, 27, pp. 3507-3516; Vignola, A.M., Campbell, A.M., Chanez, P., HLA-DR and ICAM-I expression on bronchial epithelial cells in asthma and chronic bronchitis (1993) Am Rev Respir Dis, 148, pp. 689-694; Ciprandi, G., Pronzato, C., Ricca, V., Bagnasco, M., Canonica, G.W., Evidence of intercellular adhesion molecule-1 expression on nasal epithelial cells in acute rhinoconjunctivitis caused by pollen exposure (1994) J Allergy Clin Immunol, 94, pp. 738-746; Bentley, A.M., Durham, S.R., Robinson, D.S., Expression of endothelial and leukocyte adhesion molecules interacellular adhesion molecule-1, E-selectin, and vascular cell adhesion molecule-1 in the bronchial mucosa in steady-state and allergen-induced asthma (1993) J Allergy Clin Immunol, 92, pp. 857-868; Simon, H., Alam, R., Regulation of eosinophil apoptosis: Transduction of survival and death signals (1999) Int Arch Allergy Immunol, 118, pp. 7-14","Van Benten, I.J.; Department of Otorhinolaryngology, Erasmus University Rotterdam, Dr Molewaterplein 50, 3015 GD Rotterdam, Netherlands",,,01054538,,LLRGD,"11576073","English","Allergy Eur. J. Allergy Clin. Immunol.",Article,"Final",,Scopus,2-s2.0-0034841076
"Wurm T., Chen H., Hodgson T., Britton P., Brooks G., Hiscox J.A.","6602454962;57209632300;7102167875;57203302770;7202058172;7004565877;","Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division",2001,"Journal of Virology","75","19",,"9345","9356",,117,"10.1128/JVI.75.19.9345-9356.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034849496&doi=10.1128%2fJVI.75.19.9345-9356.2001&partnerID=40&md5=96579f76ad30151e3eb4f439fc752ee9","Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom","Wurm, T., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Chen, H., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Hodgson, T., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Britton, P., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Brooks, G., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Hiscox, J.A., Sch. of Anim. and Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom","The subcellular localization of transmissible gastroenteritis virus (TGEV) and mouse hepatitis virus (MHV) (group I and group II coronaviruses, respectively) nucleoproteins (N proteins) were examined by confocal microscopy. The proteins were shown to localize either to the cytoplasm alone or to the cytoplasm and a structure in the nucleus. This feature was confirmed to be the nucleolus by using specific antibodies to nucleolin, a major component of the nucleolus, and by confocal microscopy to image sections through a cell expressing N protein. These findings are consistent with our previous report for infectious bronchitis virus (group III coronavirus) (J. A. Hiscox et al., J. Virol. 75:506-512, 2001), indicating that nucleolar localization of the N protein is a common feature of the coronavirus family and is possibly of functional significance. Nucleolar localization signals were identified in the domain III region of the N protein from all three coronavirus groups, and this suggested that transport of N protein to the nucleus might be an active process. In addition, our results suggest that the N protein might function to disrupt cell division. Thus, we observed that approximately 30% of cells transfected with the N protein appeared to be undergoing cell division. The most likely explanation for this is that the N protein induced a cell cycle delay or arrest, most likely in the G2/M phase. In a fraction of transfected cells expressing coronavirus N proteins, we observed multinucleate cells and dividing cells with nucleoli (which are only present during interphase). These findings are consistent with the possible inhibition of cytokinesis in these cells.",,"guanine nucleotide binding protein; nucleolin; nucleoprotein; virus protein; animal cell; article; cell cycle G2 phase; cell division; cellular distribution; controlled study; Coronavirus; cytokinesis; genetic transfection; mammal cell; Murine hepatitis coronavirus; nonhuman; nucleolus; priority journal; protein localization; protein transport; sequence analysis; virus replication; Animals; Cell Line; Cell Nucleolus; Coronavirus; Fluorescent Antibody Technique, Indirect; Immunity, Natural; Mice; Nucleocapsid; Nucleocapsid Proteins; Virus Replication","Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K., Watson, J.D., (1994) Molecular biology of the cell, 3rd ed., pp. 381-382. , Garland Publishing, New York, N.Y; Albo, C., Valencia, A., Portela, A., Identification of an RNA binding region within the N-terminal third of the influenza virus nucleoprotein (1995) J. 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"Narayanan K., Makino S.","7101933409;7403067550;","Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging",2001,"Journal of Virology","75","19",,"9059","9067",,61,"10.1128/JVI.75.19.9059-9067.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034854123&doi=10.1128%2fJVI.75.19.9059-9067.2001&partnerID=40&md5=ca880d82d79c64b857ee650d2f854574","Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Narayanan, K., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Makino, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Murine coronavirus mouse hepatitis virus (MHV) produces a genome-length mRNA, mRNA 1, and six or seven species of subgenomic mRNAs in infected cells. Among these mRNAs, only mRNA 1 is efficiently packaged into MHV particles. MHV N protein binds to all MHV mRNAs, whereas envelope M protein interacts only with mRNA 1. This M protein-mRNA 1 interaction most probably determines the selective packaging of mRNA 1 into MHV particles. A short cis-acting MHV RNA packaging signal is necessary and sufficient for packaging RNA into MHV particles. The present study tested the possibility that the selective M protein-mRNA 1 interaction is due to the packaging signal in mRNA 1. Regardless of the presence or absence of the packaging signal, N protein bound to MHV defective interfering RNAs and intracellularly expressed non-MHV RNA transcripts to form ribonucleoprotein complexes; M protein, however, interacted selectively with RNAs containing the packaging signal. Moreover, only the RNA that interacted selectively with M protein was efficiently packaged into MHV particles. Thus, it was the packaging signal that mediated the selective interaction between M protein and viral RNA to drive the specific packaging of RNA into virus particles. This is the first example for any RNA virus in which a viral envelope protein and a known viral RNA packaging signal have been shown to determine the specificity and selectivity of RNA packaging into virions.",,"cis acting element; protein; virus envelope protein; virus RNA; agar gel electrophoresis; article; genetic transfection; immunoprecipitation; Murine hepatitis coronavirus; nonhuman; Northern blotting; plasmid; priority journal; RNA processing; RNA transcription; virus particle; virus purification; Animals; Mice; Murine hepatitis virus; Nucleic Acid Conformation; Protein Binding; RNA, Viral; Signal Transduction; Viral Matrix Proteins; Virus Assembly","Adam, M.A., Miller, A.D., Identification of a signal in a murine retrovirus that is sufficient for packaging of nonretroviral RNA into virions (1988) J. 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"Xu H.Y., Lim K.P., Shen S., Liu D.X.","55703819800;7403175857;7403431806;8972667300;","Further identification and characterization of novel intermediate and mature cleavage products released from the ORF 1b region of the avian coronavirus infectious bronchitis virus 1a/1b polyprotein",2001,"Virology","288","2",,"212","222",,18,"10.1006/viro.2001.1098","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035975638&doi=10.1006%2fviro.2001.1098&partnerID=40&md5=9363ad298af2df92293a9a0c9d196724","Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore","Xu, H.Y., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore; Lim, K.P., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore; Shen, S., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, 1 Research Link, National University of Singapore, Singapore, 117604, Singapore","The coronavirus 3C-like proteinase is one of the viral proteinases responsible for processing of the 1a and 1a/1b polyproteins to multiple mature products. In cells infected with avian coronavirus infectious bronchitis virus (IBV), three proteins of 100, 39, and 35 kDa, respectively, were previously identified as mature cleavage products released from the lb region of the 1a/1b polyprotein by the 3C-like proteinase. In this report, we show the identification of two more cleavage products of 68 and 58 kDa released from the same region of the polyprotein. In addition, two stable intermediate cleavage products with molecular masses of 160 and 132 kDa, respectively, were identified in IBV-infected cells. The 160-kDa protein was shown to be an intermediate cleavage product covering the 100- and 68-kDa proteins, and the 132-kDa protein to be an intermediate cleavage product covering the 58-, 39-, and 35-kDa proteins. Immunofluorescent staining of IBV-infected cells and cells expressing individual cleavage products showed that the 100-, 68-, and 58-kDa proteins were associated with the membranes of the endoplasmic reticulum, and the 39- and 35-kDa proteins displayed diffuse distribution patterns. © 2001 Academic Press.",,"polyprotein; proteinase; animal cell; article; Avian infectious bronchitis virus; controlled study; endoplasmic reticulum; immunofluorescence test; molecular weight; nonhuman; open reading frame; priority journal; protein analysis; protein degradation; protein localization; protein processing; protein stability","Alonso-Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., Replication and morphogenesis of avian coronavirus in Vero cells and their inhibition by monensin (1984) Virus Res., 1, pp. 153-167; Arregui, C.O., Balsamo, J., Lilien, J., Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B (1998) J. 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"Vinores S.A., Wang Y., Vinores M.A., Derevjanik N.L., Shi A., Klein D.A., Detrick B., Hooks J.J.","56977286700;56802808200;6602941008;6602277121;57201751428;56076645400;7003911483;7006661655;","Blood-retinal barrier breakdown in experimental coronavirus retinopathy: Association with viral antigen, inflammation, and VEGF in sensitive and resistant strains",2001,"Journal of Neuroimmunology","119","2",,"175","182",,15,"10.1016/S0165-5728(01)00374-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035479023&doi=10.1016%2fS0165-5728%2801%2900374-5&partnerID=40&md5=fbdb3459c037add19f0f8e315bdbcc42","825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States; Department of Pathology, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States","Vinores, S.A., 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Wang, Y., Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States; Vinores, M.A., 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Derevjanik, N.L., 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Shi, A., 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Klein, D.A., 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Detrick, B., Department of Pathology, Johns Hopkins University School of Medicine, 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; Hooks, J.J., Immunology and Virology Section, Laboratory of Immunology, National Institutes of Health, Bethesda, MD, United States","Intraocular coronavirus inoculation results in a biphasic retinal disease in susceptible mice (BALB/c) characterized by an acute inflammatory response, followed by retinal degeneration associated with autoimmune reactivity. Resistant mice (CD-1), when similarly inoculated, only develop the early phase of the disease. Blood-retinal barrier (BRB) breakdown occurs in the early phase in both strains, coincident with the onset of inflammation. As the inflammation subsides, the extent of retinal vascular leakage is decreased, indicating that BRB breakdown in experimental coronavirus retinopathy (ECOR) is primarily due to inflammation rather than to retinal cell destruction. Vascular endothelial growth factor (VEGF) is upregulated only in susceptible mice during the secondary (retinal degeneration) phase. © 2001 Elsevier Science B.V. All rights reserved.","Blood-retinal barrier; Coronavirus; Retinopathy; Vascular endothelial growth factor","vasculotropin; virus antigen; animal tissue; article; blood retina barrier; cell destruction; controlled study; immunoreactivity; inflammation; inoculation; male; nonhuman; priority journal; rat; regulatory mechanism; retina cell; retina degeneration; retina disease; retinopathy; virus infection; virus resistance; virus strain; Animals; Antigens, Viral; Blood-Retinal Barrier; Cells, Cultured; Coronavirus Infections; Endothelial Growth Factors; Immunity, Natural; Immunohistochemistry; Leukocytes; Lymphokines; Male; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Receptor Protein-Tyrosine Kinases; Receptors, Growth Factor; Receptors, Vascular Endothelial Growth Factor; Retina; Retinitis; Serum Albumin; Species Specificity; Vascular Endothelial Growth Factor A; Vascular Endothelial Growth Factors","Agresti, A., (1990) Categorical Data Analysis, pp. 100-102. , Wiley, New York; Ault, K.A., Springer, T.A., Cross-reaction of a rat-anti-mouse phagocyte-specific monoclonal antibody (anti-Mac-1) with human monocytes and natural killer cells (1981) J. 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Ophthalmol. Visual Sci., 41, pp. 132-137; Vinores, S.A., Assessment of blood-retinal barrier integrity (1995) Histol. Histopathol., 10, pp. 141-154; Vinores, S.A., Gadegbeku, C., Campochiaro, P.A., Green, W.R., Immunohistochemical localization of blood-retinal barrier breakdown in human diabetics (1989) Am. J. Pathol., 134, pp. 231-235; Vinores, S.A., McGehee, R., Lee, A., Gadegbeku, C., Campochiaro, P.A., Ultrastructural localization of blood-retinal barrier sites in diabetic and galactosemic rats (1990) J. Histochem. Cytochem., 38, pp. 1341-1352; Vinores, S.A., Campochiaro, P.A., Lee, A., McGehee, R., Gadegbeku, C., Green, W.R., Localization of blood-retinal barrier breakdown in human pathologic specimens by immunohistochemical staining for albumin (1990) Lab. 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Visual Sci., 38, pp. S696; Vinores, S.A., Youssri, A.I., Luna, J.D., Chen, Y.-S., Bhargave, S., Vinores, M.A., Schoenfeld, C.-L., Campochiaro, P.A., Upregulation of vascular endothelial growth factor in ischemic and non-ischemic human and experimental retinal disease (1997) Histol. Histopathol., 12, pp. 99-109; Vinores, S.A., Chan, C.-C., Vinores, M.A., Mateson, D.M., Chen, Y.-S., Klein, D.A., Shi, A., Campochiaro, P.A., Increased vascular endothelial growth factor (VEGF) and transforming growth factor β (TGFβ) in experimental autoimmune uveoretinitis: Upregulation of VEGF without neovascularization (1998) J. Neuroimmunol., 89, pp. 43-50; Vinores, S.A., Derevjanik, N.L., Mahlow, J., Berkowitz, B.A., Wilson, C.A., Electron microscopic evidence for the mechanism of blood-retinal barrier breakdown in diabetic rabbits: Comparison with magnetic resonance imaging (1998) Pathol., Res. Pract., 194, pp. 497-505; Wang, Y., Detrick, B., Hooks, J.J., Coronavirus (JHM) replication within the retina: Analysis of cell tropism in mouse retinal cell cultures (1993) Virology, 193, pp. 124-137; Wang, Y., Burnier, M., Detrick, B., Hooks, J.J., Genetic predisposition to coronavirus-induced retinal disease (1996) Invest. Ophthalmol. Visual Sci., 37, pp. 250-254; Wang, Y., Detrick, B., Zhang, J., Yu, Z.-U., Chesky, L., Hooks, J.J., The role of apoptosis within the retina of coronavirus infected mice (2000) Invest. Ophthalmol. Visual Sci., 41, pp. 3011-3018; Whittum, J.A., McCulley, J.P., Niederkorn, J.Y., Streilein, J.W., Ocular disease induced in mice by anterior chamber inoculation of herpes simplex virus (1984) Invest. Ophthalmol. Visual Sci., 25, pp. 1065-1073","Vinores, S.A.; 825 Maumenee Building, Wilmer Ophthalmologic Institute, Johns Hopkins Univ. School of Med., 600 N. Wolfe Street, Baltimore, MD 21287-9289, United States; email: svinores@jhmi.edu",,,01655728,,JNRID,"11585619","English","J. Neuroimmunol.",Article,"Final",Open Access,Scopus,2-s2.0-0035479023
"Heil-Franke G., Haas L., Horzinek M.C., Müller E., Liessmann K.","7801429509;56248656100;7102624836;55532871600;6508146953;","The importance of the polymerase chain reaction (PCR) for the diagnosis of feline infectious peritonitis (FIP) [Die Bedeutung der Polymerase-Kettenreaktion (PCR) für die Diagnostik der Felinen Infektiösen Peritonitis (FIP)]",2001,"Kleintierpraxis","46","10",,"629","634",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035618910&partnerID=40&md5=1dbe4366c88f407d781adde75568ec7f","Am Schloßberg 22, 97688 Bad Kissingen, Germany; Laboklin, Labor f. Klinische Diagnostik GMBH, Prinzregentenstr. 3, D-97688 Bad Kissingen, Germany; Institut für Virologie, Tierarztl. Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany; Utrecht University, Veterinary Faculty, Yalelaan 1, Androclusgebouw, 3508 TD Utrecht, Netherlands","Heil-Franke, G., Am Schloßberg 22, 97688 Bad Kissingen, Germany; Haas, L., Institut für Virologie, Tierarztl. Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany; Horzinek, M.C., Utrecht University, Veterinary Faculty, Yalelaan 1, Androclusgebouw, 3508 TD Utrecht, Netherlands; Müller, E., Laboklin, Labor f. Klinische Diagnostik GMBH, Prinzregentenstr. 3, D-97688 Bad Kissingen, Germany; Liessmann, K., Laboklin, Labor f. Klinische Diagnostik GMBH, Prinzregentenstr. 3, D-97688 Bad Kissingen, Germany","The aim of this study was to investigate whether the application of RT-PCR to detect genomic RNA of feline coronavirus would improve the diagnosis of FIP. Therefore, plasma, ascites and blood of 95 clinically healthy cats and of 93 cats with clinical signs of FIP were analysed. In addition, antibody titers to feline coronaviruses, the total protein content and albumin values in serum as well as percentages of globulin fractions were determined. Cats suspected of FIP showed significantly more frequently coronavirus RNA (53 %), antibody titers of ≥ 400 (81.7 %) as well as higher total protein values (51.7 %) and decreased albumin/globulin ratios. However, 26% of the healthy animals were PCR-positive and 45.7% showed increased antibody titers. Therefore the final diagnosis of FIP should not rely on a mere positive RT-PCR result. Beside supporting other diagnostic methods, PCR assays are valuable tools for the management of catteries. They can monitor the success of early weaning programmes and control a corona-virus-free status.",,,"Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; Addie, D.D., Jarrett, O., Feline coronavirus antibodies in cats (1992) Vet. 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Assoc., 30, pp. 111-118; Knotek, Z., Toman, M., Faldyna, M., Clinical and immunological characteristics of cats affected by feline infectious peritonitis (2000) Acta Vet Brno, 69, pp. 55-60; Liessmann, K., (2000) Nachweis Feliner Coronavirus-RNA im Blut von Klinisch Gesunden Sowie an Feliner Infektiöser Peritonitis Erkrankten Katzen, , Diss. Hannover; Paltrinieri, S., Cammarata, M.P., Cammarata, G., Comazzi, S., Some aspects of humoral and cellular immunity in naturally occurring feline infectious peritonitis (1998) Vet. Immunol. and Immunopath., 65, pp. 205-220; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Pedersen, N.C., Coronavirus diseases (coronavirus enteritis, feline infectious peritonitis) (1987) Diseases of the Cat, Medicine and Surgery, pp. 193-214. , J. HOLZWORTH (Hrsg.): W. B. Saunders Co, Philadelphia, S; Richter, M., Schinkinger, M.F., Mostl, K., Detection of feline coronavirus type II infections in blood of cats using a reverse transcriptase polymerase chain reaction (RT-PCR) (1996) Wien. Tierärzt. Monatsschr., 83, pp. 263-268; Rohrer, C., (1992) Die Diagnostik der Felinen Infektiösen Peritonitis (FIP): Eine Retrospektive Studie, , Diss. Zürich; Scott, F.W., FIP antibody test-interpretation and recommendations (1979) J. Am. Vet. Med. Assoc., 175, pp. 1164-1168; Se, A., Feline infectious peritonitis (2000) Vet. Clin. North Am. Anim. Pract., 30, p. 987; Tasker, S., Gunn-Moore, D., Differential diagnosis of ascites in cats (2000) Pract., 22, pp. 472-479","Heil-Franke, G.Am Schloßberg 22, 97688 Bad Kissingen, Germany",,,00232076,,,,"German","Kleintierpraxis",Article,"Final",,Scopus,2-s2.0-0035618910
"Wentworth D.E., Holmes K.V.","57203154014;7201657724;","Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): Influence of N-linked glycosylation",2001,"Journal of Virology","75","20",,"9741","9752",,55,"10.1128/JVI.75.20.9741-9752.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034811621&doi=10.1128%2fJVI.75.20.9741-9752.2001&partnerID=40&md5=1f4d5afa08b65dadf8da86fad9ad30f9","Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Wentworth, D.E., Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Holmes, K.V., Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Aminopeptidase N (APN), a 150-kDa metalloprotease also called CD13, serves as a receptor for serologically related coronaviruses of humans (human coronavirus 229E [HCoV-229E]), pigs, and cats. These virus-receptor interactions can be highly species specific; for example, the human coronavirus can use human APN (hAPN) but not porcine APN (pAPN) as its cellular receptor, and porcine coronaviruses can use pAPN but not hAPN. Substitution of pAPN amino acids 283 to 290 into hAPN for the corresponding amino acids 288 to 295 introduced an N-glycosylation sequon at amino acids 291 to 293 that blocked HCoV-229E receptor activity of hAPN. Substitution of two amino acids that inserted an N-glycosylation site at amino acid 291 also resulted in a mutant hAPN that lacked receptor activity because it failed to bind HCoV-229E. Single amino acid revertants that removed this sequon at amino acids 291 to 293 but had one or five pAPN amino acid substitution(s) in this region all regained HCoV-229E binding and receptor activities. To determine if other N-linked glycosylation differences between hAPN, feline APN (fAPN), and pAPN account for receptor specificity of pig and cat coronaviruses, a mutant hAPN protein that, like fAPN and pAPN, lacked a glycosylation sequon at 818 to 820 was studied. This sequon is within the region that determines receptor activity for porcine and feline coronaviruses. Mutant hAPN lacking the sequon at amino acids 818 to 820 maintained HCoV-229E receptor activity but did not gain receptor activity for porcine or feline coronaviruses. Thus, certain differences in glycosylation between coronavirus receptors from different species are critical determinants in the species specificity of infection.",,"microsomal aminopeptidase; virus receptor; amino acid substitution; article; cat; Coronavirus; gene insertion; glycosylation; human; human cell; nonhuman; nucleotide sequence; priority journal; receptor binding; swine; virus mutant; Amino Acid Sequence; Amino Acid Substitution; Animals; Antigens, CD13; Binding Sites; Cell Line; Coronavirus; Coronavirus 229E, Human; Coronavirus Infections; Coronavirus, Feline; Glycosylation; Humans; Membrane Glycoproteins; Molecular Sequence Data; Receptors, Virus; Sequence Alignment; Species Specificity; Structure-Activity Relationship; Transfection; Transmissible gastroenteritis virus; Virulence","Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res., 25, pp. 3389-3402; Ashmun, R.A., Holmes, K.V., Shapiro, L.H., Favaloro, E.J., Razak, K., De Crom, R.P.G., Howard, C.J., Look, A.T., M3 CD13 (aminopeptidase N) cluster workshop report. 1. 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Virol., 69, pp. 2271-2278; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Wentworth, D.E.; Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; email: Dave.Wentworth@UCHSC.edu",,,0022538X,,JOVIA,"11559807","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0034811621
"Chen B.P., Kuziel W.A., Lane T.E.","57198480594;7006422901;24722465300;","Lack of CCR2 results in increased mortality and impaired leukocyte activation and trafficking following infection of the central nervous system with a neurotropic coronavirus",2001,"Journal of Immunology","167","8",,"4585","4592",,75,"10.4049/jimmunol.167.8.4585","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035887925&doi=10.4049%2fjimmunol.167.8.4585&partnerID=40&md5=cc5dc9361745e09abd40e794a602198f","Department of Molecular Biology, University of California, 3205 Biological Sciences II, Irvine, CA 92697-3900, United States","Chen, B.P., Department of Molecular Biology, University of California, 3205 Biological Sciences II, Irvine, CA 92697-3900, United States; Kuziel, W.A., Department of Molecular Biology, University of California, 3205 Biological Sciences II, Irvine, CA 92697-3900, United States; Lane, T.E., Department of Molecular Biology, University of California, 3205 Biological Sciences II, Irvine, CA 92697-3900, United States","In the present study, we evaluated the role of CCR2 in a model of viral-induced neurologic disease. An orchestrated expression of chemokines, including the CCR2 ligands monocyte chemoattractant protein-1/CCL2 and monocyte chemoattractant protein-3/CCL7, occurs within the CNS following infection with mouse hepatitis virus (MHV). Infection of mice lacking CCR2 (CCR2-/-) with MHV resulted in increased mortality and enhanced viral recovery from the brain that correlated with reduced (p ≤ 0.04) T cell and macrophage/microglial (determined by F4/80 Ag expression, p ≤ 0.004) infiltration into the CNS. Moreover, MHV-infected CCR2-/- mice displayed a significant decrease in Th1-associated factors IFN-γ (p ≤ 0.001) and RANTES/CCL5 (p ≤ 0.002) within the CNS as compared with CCR2+/+ mice. Further, peripheral CD4+ and CD8+ T cells from immunized CCR2-/- mice displayed a marked reduction in IFN-γ production in response to viral Ag and did not migrate into the CNS of MHV-infected recombination-activating gene (RAG)1-/- mice following adoptive transfer. In addition, macrophage/microglial infiltration into the CNS of RAG1-/- mice receiving CCR2-/- splenocytes was reduced (p ≤ 0.05), which correlated with a reduction in the severity of demyelination (p ≤ 0.001) as compared with RAG1-/- mice receiving splenocytes from CCR2+/+ mice. Collectively, these results indicate an important role for CCR2 in host defense and disease by regulating leukocyte activation and trafficking.",,"CD4 antigen; CD8 antigen; chemokine receptor CCR2; gamma interferon; monocyte chemotactic protein 1; RANTES; adoptive transfer; animal cell; animal experiment; animal model; animal tissue; antigen expression; article; brain infection; cell infiltration; controlled study; Coronavirus; cytokine production; demyelination; disease severity; genetic recombination; histopathology; immune response; interferon production; leukocyte activation; ligand binding; macrophage activation; microglia; mortality; mouse; Murine hepatitis coronavirus; neurologic disease; nonhuman; priority journal; spleen cell; T lymphocyte activation; Th1 cell","Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. 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Immunol., 163, p. 4642; Andjelkovic, A.V., Pachter, J.S., Characterization of binding sites for chemokines MCP-1 and MIP-1α on human brain microvessels (2000) J. Neurochem., 75, p. 1898; Fife, B.T., Huffnagle, G.B., Kuziel, W.A., Karpus, W.J., CC chemokine receptor 2 is critical for induction of experimental autoimmune encephalomyelitis (2000) J. Exp. Med., 192, p. 899; Siebert, H., Sachse, A., Kuziel, W.A., Maeda, N., Bruck, W., The chemokine receptor CCR2 is involved in macrophage recruitment to the injured peripheral nervous system (2000) J. Neuroimmunol., 110, p. 177; Glass, W.G., Liu, M.T., Kuziel, W.A., Lane, T.E., Reduced macrophage infiltration and demyelination in mice lacking the chemokine receptor CCR5 following infection with a neurotropic coronavirus (2001) Virology, 288, p. 8","Lane, T.E.; Department of Molecular Biology, University of California, 3205 Biological Sciences II, Irvine, CA 92697-3900, United States; email: tlane@uci.edu",,"American Association of Immunologists",00221767,,JOIMA,"11591787","English","J. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0035887925
"Kocherhans R., Bridgen A., Ackermann M., Tobler K.","6506004042;6603799081;7102624625;6701508835;","Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence",2001,"Virus Genes","23","2",,"137","144",,164,"10.1023/A:1011831902219","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034749116&doi=10.1023%2fA%3a1011831902219&partnerID=40&md5=86eefde8ea2cbe343e0edfe58e95c4d5","Virologisches Institut, Veterinär-Medizinischen Fakultät, Universität Zürich, Winterthurerstrasse 266A, CH-8057 Zürich, Switzerland; Division of Virology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G11 5JR, United Kingdom","Kocherhans, R., Virologisches Institut, Veterinär-Medizinischen Fakultät, Universität Zürich, Winterthurerstrasse 266A, CH-8057 Zürich, Switzerland; Bridgen, A., Division of Virology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G11 5JR, United Kingdom; Ackermann, M., Virologisches Institut, Veterinär-Medizinischen Fakultät, Universität Zürich, Winterthurerstrasse 266A, CH-8057 Zürich, Switzerland; Tobler, K., Virologisches Institut, Veterinär-Medizinischen Fakultät, Universität Zürich, Winterthurerstrasse 266A, CH-8057 Zürich, Switzerland","The sequence of the replicase gene of porcine epidemic diarrhoea virus (PEDV) has been determined. This completes the sequence of the entire genome of strain CV777, which was found to be 28,033 nucleotides (nt) in length (excluding the poly A-tail). A cloning strategy, which involves primers based on conserved regions in the predicted ORF1 products from other coronaviruses whose genome sequence has been determined, was used to amplify the equivalent, but as yet unknown, sequence of PEDV. Primary sequences derived from these products were used to design additional primers resulting in the amplification and sequencing of the entire ORF1 of PEDV. Analysis of the nucleotide sequences revealed a small open reading frame (ORF) located near the 5′ end (no 99-137), and two large, slightly overlapping ORFs, ORF1a (nt 297-12650) and ORF1b (nt 12605-20641). The ORF1a and ORF1b sequences overlapped at a potential ribosomal frame shift site. The amino acid sequence analysis suggested the presence of several functional motifs within the putative ORF1 protein. By analogy to other coronavirus replicase gene products, three protease and one growth factor-like motif were seen in ORF1a, and one polymerase domain, one metal ion-binding domain, and one helicase motif could be assigned within ORF1b. Comparative amino acid sequence alignments revealed that PEDV is most closely related to human coronavirus (HCoV)-229E and transmissible gastroenteritis virus (TGEV) and less related to murine hepatitis virus (MHV) and infectious bronchitis virus (IBV). These results thus confirm and extend the findings from sequence analysis of the structural genes of PEDV.","Coronavirus; ORF1; Porcine epidemic diarrhoea virus; Replicase gene","amino acid; growth factor; helicase; metal ion; nucleotide; polyadenylic acid; proteinase; RNA directed RNA polymerase; RNA polymerase; amino acid sequence; article; Avian infectious bronchitis virus; binding site; Coronavirus; frameshift mutation; gene amplification; gene sequence; genetic analysis; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; open reading frame; phylogeny; porcine epidemic diarrhea virus; priority journal; sequence analysis; viral genetics; virus strain; Amino Acid Sequence; Base Sequence; Cloning, Molecular; Coronavirus; Genome, Viral; Molecular Sequence Data; Open Reading Frames; Phylogeny; Sequence Homology, Amino Acid","Pensaert, M.B., Debouck, P., (1978) Arch Virol, 58, pp. 243-247; Hofmann, M., Wyler, R., (1988) J Clin Microbiol, 26, pp. 2235-2239; Pensaert, M.B., (1989) Porcine Epidemic Diarrhea Virus Virus Infections of Porcines, pp. 167-176. , Elsevier; Egberink, H.F., Ederveen, J., Callebaut, P., Horzinek, M.C., (1988) Am J Vet Res, 49, pp. 1320-1324; Utiger, A., Tobler, K., Bridgen, A., Ackermann, M., (1995) Virus Genes, 10, pp. 137-148; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J Gen Virol, 81 (4), pp. 853-879; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., (1994) Virology, 198, pp. 466-476; Bridgen, A., Duarte, M., Tobler, K., Laude, H., Ackermann, M., (1993) J Gen Virol, 74, pp. 1795-1804; Bridgen, A., Kocherhans, R., Tobler, K., Carvajal, A., Ackermann, M., (1998) Adv Exp Med Biol, 440, pp. 781-786; Herold, J., Raabe, T., Siddell, S., (1993) Arch Virol Suppl, 7, pp. 63-74; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., (1995) Adv Exp Med Biol, 380, pp. 459-461; Lee, H.-J., Shieh, C.-K., Gorbalenaya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdazhadzhyan, A., Lai, M.M., (1991) Virology, 180, pp. 567-582; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., (1994) Virology, 198, pp. 736-740; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J., (1990) Nucleic Acids Res, 18, pp. 1825-1832; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., (1987) J Gen Virol, 68, pp. 57-77; Tobler, K., Ackermann, M., (1995) Adv Exp Med Biol, 380, pp. 541-542; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., (1993) Virology, 195, pp. 680-691; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J., Weiss, S.R., (1989) Virology, 171, pp. 141-148; Soe, L.H., Shieh, C.K., Baker, S.C., Chang, M.F., Lai, M.M., (1987) J Virol, 61, pp. 3968-3976; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., (1995) Virology, 206, pp. 817-822; Cavanagh, D., (1995) Arch Virol, 142, pp. 629-633; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Brown, V.C., Blok, T.D., Inglis, S.C., (1987) EMBO J, 6, pp. 3779-3785; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., (1997) Seminars in Virology, 8, pp. 33-47; Brierley, I., Digard, P., Inglis, S.C., (1989) Cell, 57, pp. 537-547; Herold, J., Siddell, S.G., (1993) Nucleic Acids Res, 21, pp. 5838-5842; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., (1989) Nucleic Acids Res, 17, pp. 4847-4861; Duarte, M., Laude, H., (1989) J Gen Virol, 75, pp. 1195-1200; Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., (2000) Proc Natl Acad Sci USA, 97, pp. 5516-5521; Yount, B., Curtis, K.M., Baric, R.S., (2000) J Virol, 74, pp. 10600-10611; Thiel, V., Casais, T., Cavanagh, D., Britton, P., (2000) A reverse genetic system for coronaviruses, , European Congress of Virology, Glasgow","Tobler, K.; Virol. Inst. Vet.-Medizin. Fak., Universität Zürich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland; email: kurtt@vetvir.unizh.ch",,,09208569,,VIGEE,"11724265","English","Virus Genes",Article,"Final",Open Access,Scopus,2-s2.0-0034749116
"Das Sarma J., Fu L., Hingley S.T., Lai M.M.C., Lavi E.","6602813975;7401812822;6701491322;7401808497;7006986911;","Sequence analysis of the S gene of recombinant MHV-2/A59 coronaviruses reveals three candidate mutations associated with demyelination and hepatitis",2001,"Journal of NeuroVirology","7","5",,"432","436",,15,"10.1080/135502801753170282","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034755810&doi=10.1080%2f135502801753170282&partnerID=40&md5=ce15f763d8e2676ce1e1aebc986abe60","University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States","Das Sarma, J., University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States; Fu, L., University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States; Hingley, S.T., University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States; Lai, M.M.C., University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States; Lavi, E., University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States","Coronaviruses, mouse hepatitis virus (MHV) strains, exhibit various degrees of neurotropism and hepatotropism following intracerebral (IC) infection of 4-week-old C57Bl/6 mice. Whereas MHV-A59 produces acute meningitis, encephalitis, hepatitis, and chronic demyelination, a closely related strain, MHV-2, produces only acute meningitis and hepatitis. We previously reported that the spike glycoprotein gene of MHV contains determinants of demyelination and hepatitis. To further investigate the site of demyelination and hepatitis determinants within the S gene, we sequenced the S gene of several nondemyelinating recombinant viruses. We found that three encephalitis-positive, demyelination-negative, hepatitis-negative recombinant viruses have an MHV-A59-derived S gene, which contains three identical point mutations (I375M, L652I, and T1087N). One or more of the sites of these mutations in the MHV-A59 genome are likely to contribute to demyelination and hepatitis.","Coronavirus; Demyelination; Hepatitis; Mouse hepatitis virus (MHN); Multiple sclerosis (MS); Nidoviruses","virus glycoprotein; acute disease; animal experiment; animal model; animal tissue; article; brain infection; chronic disease; controlled study; demyelination; encephalitis; gene sequence; hepatitis; liver; meningitis; mouse; Murine hepatitis coronavirus; neurotropism; nonhuman; point mutation; priority journal; sequence analysis; virus gene; virus genome; virus recombinant; virus recombination; virus strain; Amino Acid Substitution; Animals; Brain; Cardiovirus Infections; Demyelinating Diseases; Encephalitis, Viral; Genes, Viral; Hepatitis, Viral, Animal; Liver; Male; Membrane Glycoproteins; Meningitis, Viral; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Point Mutation; Recombination, Genetic; Sequence Analysis, RNA; Species Specificity; Spinal Cord; Viral Envelope Proteins; Viral Structural Proteins; Virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch Virol, 142, pp. 629-633; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site specific alteration of murine hepatitis virus type 4 peplomer glycoprotein S results in reduced neurovirulence (1986) J Virol, 59, pp. 463-471; Das Sarma, J., Fu, L., Hingley, S.T., Lavi, E., Mouse hepatitis virus type-2 infection in mice: An experimental model system of acute meningitis and hepatitis (2001) Exp Mol Pathol, 71, pp. 1-12; Das Sarma, J., Fu, L., Tsai, J.C., Weiss, S.R., Lavi, E., Demyelination determinants map to the spike glycoprotein gene of coronavirus mouse hepatitis virus (2000) J Virol, 74, pp. 9206-9213; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., Monoclonal antibodies to the matrix (E1) glycoprotein of mouse hepatitis virus protect mice from encephalitis (1989) Virology, 168, pp. 162-167; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J Virol, 65, pp. 1916-1928; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Hirano, N., Fujiwara, K., Hino, S., Matumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch Ges Virusfors, 44, pp. 298-302; Hirano, N., Murakami, T., Taguchi, F., Fujiwara, K., Matumoto, M., Comparison of mouse hepatitis virus strains for pathogenicity in weanling mice infected by various routes (1981) Arch Virol, 70, pp. 69-73; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J NeuroVirol, 2, pp. 361-376; Keck, J.G., Soe, L.H., Makino, S., Stohlman, S.A., Lai, M.M.C., RNA recombination of murine coronavirus: Recombination between fusion-positive mouse hepatitis virus A59 and fusion-negative mouse hepatitis virus 2 (1988) J Virol, 62, pp. 1989-1998; Knobler, R.L., Haspel, M.V., Oldstone, M.B.A., Mouse hepatitis virus type 4 (JHM strain)-induced fatal central nervous system disease, part 1 (genetic control and the murine neurone as the susceptible site for disease) (1981) J Exp Med, 153, pp. 832-843; Knobler, R.L., Tunison, L.A., Lampert, P.W., Oldstone, M.B.A., Selected mutants of mouse hepatitis virus type 4 (JHM strain) induce different CNS diseases. Pathobiology of disease induced by wild type and mutants ts8 and ts15 in BALB/c and SJL/J mice (1982) Am J Pathol, 109, pp. 157-168; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of interferon by the coronavirus transmissible gastroenteritis virus (1992) J Virol, 66, pp. 743-749; Lavi, E., Fishman, S.P., Highkin, M.K., Weiss, S.R., Limbic encephalitis following inhalation of murine coronavirus MHV-A59 (1988) Lab Invest, 58, pp. 31-36; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., The organ tropism of mouse hepatitis virus A59 is dependent on dose and route of inoculation (1986) Lab Anim Sci, 36, pp. 130-135; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Haluskey, J.A., Masters, P.S., Targeted recombination between MHV-2 and MHV-A59 to study neurotropic determinants of MHV (1998) Adv Exp Med Biol, 440, pp. 543-547; Lavi, E., Kuo, L., Haluskey, J.A., Masters, P.S., The pathogenesis of MHV nucleocapsid gene chimeric viruses (1998) Adv Exp Med Biol, 440, pp. 537-541; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab Invest, 62, pp. 570-578; Lavi, E., Schwartz, T., Jin, Y.P., Fu, L., Nidovirus infections: Experimental model systems of human neurologic diseases (1999) J Neuropathol Exp Neurol, 58, pp. 1197-1206; Lavi, E., Weiss, S.R., Coronaviruses (1989) Clinical and Molecular Aspects of Neurotropic Viral Infections, pp. 101-139. , Gilden DH, Lipton HL (eds). Kluwer Academic Publishers: Boston, Massachusetts; Leparc-Goffart, I., Hingley, S.T., Chua, M.-M., Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis phenotypes of murine coronavirus MHV-A59 are associated with a Q159L amino acid substitution in the receptor binding domain of the spike protein (1997) Virology, 239, pp. 1-10; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J Virol, 72, pp. 9628-9636; Navas, S., Seo, S., Chua, M.M., Das Sarma, J., Lavi, E., Hingley, S.T., Weiss, S.R., The spike protein of murine coronavirus determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J Virol, 75, pp. 2452-2457; Perlman, S., Jacobsen, G., Olson, A.L., Afifi, A., Identification of the spinal cord as a major site of persistence during chronic infection with a murine coronavirus (1990) Virology, 175, pp. 418-426; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV-4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Reed, L., Muench, H., A simple method of estimating fifty percent end points (1938) Am J Hyg, 27, pp. 493-497; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Adv Virol Immunol, 99, pp. 165-200; Wege, H., Stephenson, J.R., Koga, M., Wege, H., Ter Meulen, V., Genetic variation of neurotropic and non-neurotropic murine coronaviruses (1981) J Gen Virol, 54, pp. 67-74; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch Neurol, 28, pp. 298-303; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the siganal sequence of the S protein (1997) Virology, 227, pp. 215-219; Yokomori, K., Banner, L.R., Lai, M.C., Heteroginity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657","Lavi, E.; University of Pennsylvania, School of Medicine, Division of Neuropathology, 422 Curie Blvd., Philadelphia, PA 19104-6100, United States; email: lavi@mail.med.upenn.edu",,,13550284,,JNVIF,"11582515","English","J. Neurovirol.",Article,"Final",Open Access,Scopus,2-s2.0-0034755810
"Phillips J.J., Chua M.M., Seo S.-H., Weiss S.R.","7404582468;7006092803;7202469910;57203567044;","Multiple regions of the murine coronavirus spike glycoprotein influence neurovirulence",2001,"Journal of NeuroVirology","7","5",,"421","431",,28,"10.1080/135502801753170273","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034767475&doi=10.1080%2f135502801753170273&partnerID=40&md5=f7a37c146d124c48248c98468a0a7364","Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Phillips, J.J., Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Chua, M.M., Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Seo, S.-H., Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","The spike (S) glycoprotein of mouse hepatitis virus (MHV) is a major determinant of neurovirulence. Using targeted recombination we previously demonstrated that the S gene of the highly neurovirulent MHV-4 conferred a dramatic increase in neurovirulence to the mildly neurovirulent MHV-A59. To identify the genetic determinants of neurovirulence within the MHV-4 spike, we generated isogenic recombinant viruses containing various MHV-4/MHV-A59 chimeric spike genes, and studied their phenotypes in vivo. The MHV-4/MHV-A59 chimeric spike genes consisted of either reciprocal exchanges between the S1 and S2 spike subunits, or smaller exchanges specifically in the hypervariable region (HVR) of S1. The chimeric spike gene containing recombinants all exhibited efficient replication in vitro, yet many were severely attenuated for virulence in vivo. Furthermore, these attenuated recombinants exhibited decreased titers of infectious virus in the brain relative to the parental recombinant viruses containing the full-length MHV-4 or MHV-A59 spike genes. This is the first report that compares the neurovirulence and pathogenesis of isogenic viruses with defined alterations in the MHV spike protein. From these studies, it appears that the interactions of multiple regions of the MHV spike, including the HVR, act in concert to allow for efficient infection of and virulence in the murine central nervous system.","Encephalitis; Mouse hepatitis virus; Neurovirulence; Recombinant coronaviruses","protein subunit; virus glycoprotein; animal cell; article; brain; central nervous system infection; chimera; controlled study; genetic recombination; in vitro study; in vivo study; Murine hepatitis coronavirus; nonhuman; pathogenesis; phenotype; priority journal; virus attenuation; virus gene; virus load; virus recombinant; virus replication; virus virulence; Animals; Cats; Cell Line; Lethal Dose 50; Male; Membrane Fusion; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Plaque Assay; Protein Subunits; Recombinant Fusion Proteins; Recombination, Genetic; RNA, Viral; Specific Pathogen-Free Organisms; Viral Envelope Proteins; Virulence; Virus Replication; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus strain 4","Banner, L.R., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Beauchemin, N., Draber, P., Dveksler, G., Gold, P., Gray-Owen, S., Grunert, F., Hammarstrom, S., Zimmermann, W., Redefined nomenclature for members of the carcinoembryonic antigen family (1999) Exp Cell Res, 252, pp. 243-249; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response (1996) J Gen Virol, 77, pp. 315-325; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Castro, R.F., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J Virol, 69, pp. 8127-8131; Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion (1982) Virology, 119, pp. 358-371; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J Virol, 59, pp. 463-471; DeGroot, R.J., Luytjes, W., Horzinek, M.C., Van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike proteins of coronaviruses (1987) J Mol Biol, 196, pp. 963-966; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hampster cell lines confers susceptibility to MHV (1991) J Virol, 65, pp. 6881-6891; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J Virol, 71, pp. 5148-5160; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J Virol, 58, pp. 869-875; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J Virol, 56, pp. 912-920; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J Virol, 71, pp. 3129-3137; Gallagher, T.M., Buchmeier, M.J., Perlman, S., Cell receptor-independent infection by a neurotropic murine coronavirus (1992) Virology, 191, pp. 517-522; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J Virol, 65, pp. 1916-1928; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the aminoterminal half of the spike glycoprotein (1990) J Virol, 64, pp. 731-741; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J Virol, 67, pp. 4504-4512; Grosse, B., Siddell, S.G., Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody (1994) Virology, 202, pp. 814-824; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the murine coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J Virol, 66, pp. 1841-1848; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J Virol, 68, pp. 5404-5410; Kuo, L., Godeke, G.-J., Raamsman, M.J.B., Masters, P.S., Rottier, P.J.M., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J Virol, 74, pp. 1393-1406; Lavi, E., Fishman, P.S., Highkin, M.K., Weiss, S.R., Limbic encephalitis after inhalation of a murine coronavirus (1988) Lab Investig, 58, pp. 31-36; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., The organ tropism of mouse hepatitis virus strain A59 is dependent on dose and route of inoculation (1986) Lab Anim Sci, 36, pp. 130-135; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J Virol, 72, pp. 9628-9636; Luytjes, W., Sturman, L.S., Bredenbeck, P.J., Charite, J., Van der Zeijst, B.A.M., Horzinek, M.C., Spaan, W.J.M., Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site (1987) Virology, 161, pp. 479-487; Maniatis, T., Fritsch, E.F., Sambrook, J., Molecular cloning, a laboratory manual (1982), Cold Spring Harbor Laboratory: Cold Spring Harbor, New York; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J Virol, 68, pp. 328-337; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Pewe, L., Wu, G.F., Barnett, E.M., Castro, R.F., Perlman, S., Cytotoxic T cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Pritchard, A.E., Jensen, K., Lipton, H.I., Assembly of Theiler's virus recombinants used in mapping determinants of neurovirulence (1993) J Virol, 67, pp. 3901-3907; Ramig, R.F., Isolation and genetic characterization of temperature sensitive mutants of simian rotavirus SA11 (1982) Virology, 120, pp. 93-135; Rao, P.V., Gallagher, T.M., Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections (1998) J Virol, 72, pp. 3278-3288; Reed, L.J., Muench, H., A simple method of estimating fifty per cent points (1938) Am J Hygeine, 27, pp. 493-497; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resisitant mutants (1997) J Virol, 71, pp. 9024-9031; Smith, A.L., Barthold, S.W., Methods in viral pathogenesis (1997) Viral Pathogenesis, pp. 483-506. , Nathanson N (ed). Lippincott-Raven: Philadelphia, Pennsylvania; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion (1990) J Virol, 64, pp. 3042-3050; Taguchi, F., Fleming, J.O., Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein (1989) Virology, 169, pp. 233-235; Tsai, C.-W., Chang, S.C., Chang, M.-F., A 12-amino acid stretch in the hypervariable region of the spike protein S1 subunit is critical for cell fusion activity of mouse hepatitis virus (1999) J Biol Chem, 274, pp. 26085-26090; Wang, F.-I., Fleming, J.O., Lai, M.M.C., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; Wege, H., Winter, J., Meyermann, R., The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis (1988) J Gen Virol, 69, pp. 87-98; Weismiller, D.G., Sturman, L.S., Buchmeier, M.J., Fleming, J.O., Holmes, K.V., Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions (1990) J Virol, 64, pp. 3051-3055; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc Natl Acad Sci USA, 88, pp. 5533-5536; Zhang, L., Senkowski, A., Shim, B., Roos, R.P., Chimeric cDNA studies of Theiler's murine encephalomyelitis virus neurovirulence (1993) J Virol, 67, pp. 4404-4408","Weiss, S.R.; Department of Microbiology, Univ. Pennsylvania School Medicine, 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: Weisssr@mail.med.upenn.edu",,,13550284,,JNVIF,"11582514","English","J. Neurovirol.",Article,"Final",Open Access,Scopus,2-s2.0-0034767475
"Cavanagh D., Mawditt K., Sharma M., Drury S.E., Ainsworth H.L., Britton P., Gough R.E.","26642890500;6603252273;57198780789;7005260071;6602543396;57203302770;7102835761;","Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens",2001,"Avian Pathology","30","4",,"355","368",,73,"10.1080/03079450120066368","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035172844&doi=10.1080%2f03079450120066368&partnerID=40&md5=b4ea2c905925db3f56d8aa10731d5907","Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom","Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Mawditt, K., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Sharma, M., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Drury, S.E., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Ainsworth, H.L., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Britton, P., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom; Gough, R.E., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom","Intestinal contents of 13-day-old turkey poults in Great Britain were analysed as the birds showed stunting, unevenness and lameness, with 4% mortality. At post mortem examination, the main gross features were fluid caecal and intestinal contents. Histological examination of tissues was largely unremarkable, apart from some sections that showed crypt dilation and flattened epithelia. Negative contrast electron microscopy of caecal contents revealed virus particles, which in size and morphology had the appearance of a coronavirus. RNA was extracted (turkey/UK/412/00) and used in a number of reverse transcription-polymerase chain reactions (RT-PCRs) with the oligonucleotides based on sequences derived from avian infectious bronchitis virus (IBV), a coronavirus of domestic fowl. The RT-PCRs confirmed that turkey/UK/412/00 was a coronavirus and, moreover, showed that it had the same partial gene order (S-E-M-5-N-3′ untranslated region) as IBV. This gene order is unlike that of any known mammalian coronavirus, which does not have a gene analogous to the gene 5 of IBV. The gene 5 of the turkey virus had two open reading frames, 5a and 5b, as in IBV and the coronaviruses isolated from turkeys in North America. The turkey/UK/412/00 also resembled IBV, but not mammalian coronaviruses, in having three open reading frames in the gene encoding E protein (gene 3). The percentage differences between the nucleotide sequences of genes 3 and 5 and the 3′ untranslated region of turkey/UK/412/00 when compared with those of IBVs were similar to the differences observed when different strains of IBV were compared with each other. No sequences unique to the turkey isolates were identified. These results demonstrate, for the first time, that a coronavirus was associated with disease in turkeys outside of North America and that it is a Group 3 coronavirus, like IBV.",,"age; chicken; Coronavirus; electron microscopy; gene sequence; genetic relationship; genetic similarity; histology; infectious bronchitis virus; morphology; mortality; open reading frame; reverse transcription polymerase chain reaction; turkey; United Kingdom; virus detection; virus gene; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; DNA viruses; Galliformes; Gallus gallus; Mammalia; Meleagris gallopavo","Adams, N.R., Hofstad, M.S., Isolation of transmissible gastroenteritis agent of turkeys in avian embryos (1971) Avian Diseases, 15, pp. 426-433; Adams, N.R., Hofstad, M.S., Observations on staining and antibiotic sensitivity of the transmissible enteritis agent of turkeys (1972) American Journal of Veterinary Research, 33, pp. 995-999; Adams, N.R., Hofstad, M.S., Transmissible enteritis infection in germfree and monocontaminated turkey poults (1972) American Journal of Veterinary Research, 33, pp. 1001-1005; Adams, N.R., Ball, R.A., Hofstad, M.S., Intestinal lesions in transmissible enteritis of turkeys (1970) Avian Diseases, 14, pp. 392-399; Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathology, 25, pp. 817-836; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome ('spiking mortality') of turkeys (1997) Diseases of Poultry 10th edn., pp. 1025-1031. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds). Ames, IA: Iowa State University Press; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Brown, T.P., Howell, D.R., Garcia, A.P., Adult cattle as inapparent carriers of spiking mortality of turkeys (1996) Proceedings of the 133rd Annual Meeting of the American Veterinary Medical Association, pp. 118-121. , Louisville, KY, USA; Brown, T.P., Garcia, A.P., Kelley, L., Spiking mortality of turkey poults: 1. Experimental reproduction in isolation facilities (1997) Avian Diseases, 41, pp. 604-609; Boursnell, M.E.B., Binns, M., Brown, T.D.K., Sequencing of the coronavirus IBV genomic RNA: Three open reading frames in the 5′ 'unique' region of mRNA D (1985) Journal of General Virology, 66, pp. 2253-2258; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Co-circulation of four types of infectious bronchitis virus (793/B, 624/I, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 587-592; Cavanagh, D., Commentary. A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathology, 30, pp. 109-115; Cavanagh, D., Davis, P.J., Evolution of avian coronavirus IBV: Sequence of the matrix glycoprotein gene and intergenic region of several serotypes (1988) Journal of General Virology, 69, pp. 621-629; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of Poultry. 10th edn, pp. 511-526. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoda (Eds). Ames, IA: Iowa State University Press; Cavanagh, D., Mawditt, K., Britton, P., Naylor, C.J., Longitudinal field studies of infectious bronchitis virus and avian pneumovirus in broilers using type-specific polymerase chain reactions (1999) Avian Pathology, 28, pp. 593-605; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analytical Biochemistry, 162, pp. 156-159; Dalton, K., Casais, R., Shaw, K., Stirrups, K., Evafis, S., Britton, P., Brown, T.D.K., Cavanagh, D., Identification of the cis-acting sequences required for coronavirus infectious bronchitis virus defective RNA replication and rescue (2001) Journal of Virology, 75, pp. 125-133; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) Journal of Virology, 64, pp. 3112-3118; De Wit, J.J., Detection of infectious bronchitis virus (2000) Avian Pathology, 29, pp. 71-93; Dhinaker Raj, G., Jones, R.C., Infectious bronchitis virus: Immunopathogenesis of infection in the chicken (1997) Avian Pathology, 26, pp. 677-706; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, Seventh Report of the International Committee on Taxonomy of Viruses, pp. 835-849. , M.H.V. 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New York: Academic Press; Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis complex/spiking mortality (1995) Avian Pathology, 24, pp. 497-505; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses (2000) Avian Pathology, 29, pp. 206-212; Guy, J.S., Barnes, J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Diseases, 41, pp. 583-590; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J.J., Experimental infection of specific-pathogen-free chickens with turkey coronavirus (1999) Proceedings of the 48th Western Poultry Disease Conference, pp. 91-92; Guy, J.S., Smith, L.G., Breslin, J.J., Vaillancourt, J.P., Barnes, H.J., High mortality and growth depression experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus (2000) Avian Diseases, 44, pp. 105-113; Hofstad, M.S., Adams, N., Frey, M.L., Studies on a filterable agent associated with infectious enteritis (bluecomb) of turkeys (1969) Avian Diseases, 13, pp. 386-393; Ismail, M.M., Cho, K.O., Ward, L.A., Saif, L.J., Saif, Y.M., Experimental bovine coronavirus in turkey poults and young chickens (2001) Avian Diseases, 45, pp. 157-163; Koci, M.D., Seal, B.S., Schultz-Cherry, S., Molecular characterisation of an avian astrovirus (2000) Journal of Virology, 74, pp. 6173-6177; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Lambrechts, C., Pensaert, M., Ducatelle, R., Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus (1993) Avian Pathology, 22, pp. 577-590; Larsen, C.T., The etiology of bluecomb disease of turkeys (1979) Dissertation Abstracts International, 40 B, pp. 625-626; Li, J., Cook, J.K.A., Brown, T.D.K., Shaw, K., Cavanagh, D., Detection of turkey rhinotracheitis virus in turkeys using the polymerase chain reaction (1993) Avian Pathology, 22, pp. 771-783; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Diseases, 44, pp. 498-506; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Archives of Virology, 131, pp. 455-465; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry 10th edn, pp. 686-692. , B.W. 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"Holmes K.V.","7201657724;","Enteric infections with coronaviruses and toroviruses",2001,"Novartis Foundation Symposium","238",,,"258","275",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035222881&partnerID=40&md5=3ff7a6f7d863ca17d34c093c960ef983","Department of Microbiology, B-175, Univ. of Colorado Hlth. Sci. Ctr., 4200 East 9th Avenue, Denver, CO 20862, United States","Holmes, K.V., Department of Microbiology, B-175, Univ. of Colorado Hlth. Sci. Ctr., 4200 East 9th Avenue, Denver, CO 20862, United States","Many enteric viruses are difficult or impossible to propagate in tissue culture. Coronaviruses and toroviruses are large, enveloped, plus-strand RNA viruses in the order Nidovirales that cause enteric disease in young pigs, cows, dogs, mice, cats and horses. Two different serogroups of mammalian coronaviruses cause frequent respiratory infections in humans, and coronaviruses and toroviruses have been implicated in human diarrhoeal disease by immunoelectron microscopy. However, there is as yet no consensus about the importance of these enveloped viruses in human diarrhoea, and little is known about their genetic variability. The large spike (S) glycoprotein is an important determinant of species specificity, tissue tropism and virulence of coronavirus infection. To infect enterocytes, both S glycoproteins and the viral envelope must resist degradation by proteases, low and high pH, and bile salts. One specific site on the S glycoprotein of bovine coronavirus must be cleaved by an intracellular protease or trypsin to activate viral infectivity and cell fusion. S glycoprotein binds to specific receptors on the apical membranes of enterocytes, and can undergo a temperature-dependent, receptor-mediated conformational change that leads to fusion of the viral envelope with host membranes to initiate infection. Analysing spike-receptor interactions may lead to new ways to propagate these enteric viruses as well as new strategies for development of novel antiviral drugs.",,"glycoprotein; virus envelope protein; virus receptor; article; chemistry; Coronavirus; enteropathy; human; metabolism; structure activity relation; Torovirus; virology; virus infection; Coronavirus; Coronavirus Infections; Glycoproteins; Humans; Intestinal Diseases; Receptors, Virus; Structure-Activity Relationship; Torovirus; Torovirus Infections; Viral Envelope Proteins","Baker, K.A., Dutch, R.E., Lamb, R.A., Jardetzky, T.S., Structural basis for paramyxovirus-mediated membrane fusion (1999) Mol Cell, 3, pp. 309-319; Battaglia, M., Passarani, N., Di Matteo, A., Gerna, G., Human enteric coronaviruses: Further characterization and immunoblotting of viral proteins (1987) J Infect Dis, 155, pp. 140-143; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; 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Duckmanton, L.M., Luan, B., Devenish, J., Tellier, R., Petric, M., Characterization of torovirus from human fecal specimens (1997) Virology, 239, pp. 158-168; Duckmanton, L.M., Tellier, R., Liu, P., Petrie, M., Bovine torovirus: Sequencing of the structural genes and expression of the nucleocapsid protein of Breda virus (1998) Virus Res, 58, pp. 83-96; Duckmanton, L.M., Tellier, R., Richardson, C., Petric, M., The novel hemagglutinin-esterase genes of human torovirus and Breda virus (1999) Virus Res, 64, pp. 137-149; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J Virol, 65, pp. 6881-6891; Godfraind, C., Langreth, S.G., Cardellichio, C.B., Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus (1995) Lab Invest, 73, pp. 615-627; Hegyi, A., Kolb, A.F., Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N (1998) J Gen Virol, 79, pp. 1387-1391; Hernandez, L.D., Hoffman, L.R., Wolfsberg, T.G., White, J.M., Virus-cell and cell-cell fusion (1996) Annu Rev Cell Dev Biol, 12, pp. 627-661; Hingley, S.T., Leparc-Goffart, I., Weiss, S.R., The spike protein of murine coronavirus mouse hepatitis virus strain A59 is not cleaved in primary glial cells and primary hepatocytes (1998) J Virol, 72, pp. 1606-1609; Holmes, K.V., Dveksler, G.S., Specificity of coronavirus-receptor interactions (1994) Cellular Receptors for Animal Viruses, pp. 403-443. , Wimmer E (ed) Cold Spring Harbor Press, Cold Spring Harbor, NY; Holmes, K.V., Frana, M.F., Robbins, S.G., Sturman, L.S., Coronavirus maturation (1984) Adv Exp Med Biol, 173, pp. 37-52; Jamieson, F.B., Wang, E.E., Bain, C., Good, J., Duckmanton, L., Petric, M., Human torovirus: A new nosocomial gastrointestinal pathogen (1998) J Infect Dis, 178, pp. 1263-1269; Koopmans, M., Horzinek, M.C., Toroviruses of animals and humans: A review (1994) Adv Virus Res, 43, pp. 233-273; Koopmans, M., Petric, M., Glass, R.I., Monroe, S.S., Enzyme-linked immunosorbent assay reactivity of torovirus-like particles in fecal specimens from humans with diarrhea (1993) J Clin Microbiol, 31, pp. 2738-2744; Koopmans, M.P., Goosen, E.S., Lima, A.A., Association of torovirus with acute and persistent diarrhea in children (1997) Pediatr Infect Dis J, 16, pp. 504-507; Krishnan, T., Naik, T.N., Electronmicroscopic evidence of torovirus like particles in children with diarrhoea (1997) Indian J Med Res, 105, pp. 108-110; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Lai, M.M.C., Holmes, K.V., Coronaviridae and their replication (2000) Fields' Virology, 4th Edition, , Knipe DM, Howley PM, Griffin D et al (eds) Lippincott-Raven, New York, in press; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Rossen, J.W., Strous, G.J., Horzinek, M.C., Rottier, P.J., Mouse hepatitis virus strain A59 is released from opposite sides of different epithelial cell types (1997) J Gen Virol, 78, pp. 61-69; Salanueva, I.J., Carrascosa, J.L., Risco, C., Structural maturation of the transmissible gastroenteritis coronavirus (1999) J Virol, 73, pp. 7952-7964; Schultze, B., Herrler, G., Recognition of N-acetyl-9-O-acetylneuraminic acid by bovine coronavirus and hemagglutinating encephalomyelitis virus (1993) Adv Exp Med Biol, 342, pp. 299-304; Siddell, S.G., Snijder, E.J., Coronaviruses, toroviruses and arteriviruses (1998) Topley and Wilson's Microbiology and Microbial Infections, pp. 463-484. , Mahy BWJ, Collier L (eds) Edward Arnold, London; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect Immun, 31, pp. 1214-1222; Suzuki, H., Taguchi, F., Analysis of the receptor-binding site of murine coronavirus spike protein (1996) J Virol, 70, pp. 2632-2636; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J Virol, 70, pp. 8669-8674; Tsunemitsu, H., Smith, D.R., Saif, L.J., Experimental inoculation of adult dairy cows with bovine coronavirus and detection of coronavirus in feces by RT-PCR (1999) Arch Virol, 144, pp. 167-175; Van Genderen, I.L., Godeke, G.J., Rottier, P.J., Van Meer, G., The phospholipid composition of enveloped viruses depends on the intracellular membrane through which they bud (1995) Biochem Soc Trans, 23, pp. 523-526; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) J Virol, 62, pp. 4686-4690; Weiss, M., Steck, F., Horzinek, M.C., Purification and partial characterization of a new enveloped RNA virus (Berne virus) (1983) J Gen Virol, 64, pp. 1849-1858; Weissenhorn, W., Dessen, A., Calder, L.J., Harrison, S.C., Skehel, J.J., Wiley, D.C., Structural basis for membrane fusion by enveloped viruses (1999) Mol Membr Biol, 16, pp. 3-9; Wessels, H.P., Hansen, G.H., Fuhrer, C., Aminopeptidase N is directly sorted to the apical domain in MDCK cells (1990) J Cell Biol, 111, pp. 2923-2930; Yeager, C.L., Ashmun, R.A., Williams, R.K., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Zelus, B.D., Wessner, D.R., Williams, R.K., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J Virol, 72, pp. 7237-7244; Zhang, X.M., Herbst, W., Kousoulas, K.G., Storz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J Med Virol, 44, pp. 152-161","Holmes, K.V.; Department of Microbiology, B-175, Univ. of Colorado Hlth. Sci. Ctr., 4200 East 9th Avenue, Denver, CO 20862, United States",,,,,,"11444030","English","Novartia Found. Symp.",Article,"Final",,Scopus,2-s2.0-0035222881
"Chilvers M.A., McKean M., Rutman A., Myint B.S., Silverman M., O'Callaghan C.","6604010600;7004143832;7004395293;57191936421;7403299029;35599642600;","The effects of coronavirus on human nasal ciliated respiratory epithelium",2001,"European Respiratory Journal","18","6",,"965","970",,69,"10.1183/09031936.01.00093001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035694436&doi=10.1183%2f09031936.01.00093001&partnerID=40&md5=c6e2583209034e00e24933565f664e81","Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom","Chilvers, M.A., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom; McKean, M., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom; Rutman, A., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom; Myint, B.S., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom; Silverman, M., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom; O'Callaghan, C., Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom","Human coronavirus (HCoV) accounts for 15-30% of common colds, but only one case report has described the effect of a coronavirus infection, that was asymptomatic, on human respiratory epithelium. The authors examined the effects of infection with HCoV on ciliary structure and function in healthy volunteers infected by intranasal inoculation with HCoV 229E. A further four volunteers were sham infected with ultraviolet-inactivated virus. Immediately before inoculation (day 0) and 3 days later (day 3), ciliated epithelium was obtained by brushing the inferior nasal turbinate. Ciliary beat frequency was determined and beat pattern analysed for evidence of dyskinesia (0=normal, 3=severely dyskinetic) using digital high-speed video photography. Ciliary ultrastructure was examined by transmission electron microscopy. Symptom diaries were kept for the duration of the study. All subjects inoculated with HCoV, including the three who did not develop symptoms of an upper respiratory tract infection, had disruption of their respiratory epithelium on day 3. Although there was no difference in the mean ciliary ciliary beat frequency between day 0 (11.3 Hz (95% confidence interval (CI): 8.6-14.0) and day 3 (9.4 Hz (95% CI 7.2-11.6)), there was a significant increase (p<0.05) in the ciliary dyskinesia score between day 0 (0.2 (95% CI 0-0.5)) and day 3 (1.1 (95% CI 0.05-1.7). In sham-infected subjects, no differences in epithelial integrity, or ciliary structure and function were found between day 0 and day 3. Inoculation of healthy volunteers with human coronavirus caused disruption of the ciliated epithelium and ciliary dyskinesia. This is likely to impair mucociliary clearance. Damage to the respiratory epithelium, due to human coronavirus infection, may occur without overt clinical symptoms.","Cilia; Ciliary beat frequency; Coronavirus; Respiratory epithelium; Ultrastructure; Viral infection","adult; article; ciliary motility; common cold; confidence interval; controlled study; Coronavirus; dyskinesia; female; frequency analysis; human; human cell; human experiment; male; mucociliary clearance; normal human; priority journal; scoring system; symptomatology; transmission electron microscopy; ultrastructure; ultraviolet radiation; upper respiratory tract infection; videorecording; volunteer; writing; Adult; Cilia; Coronaviridae Infections; Female; Humans; Male; Nasal Cavity; Respiratory Mucosa","Rautiainen, M., Nuutinen, J., Kiukaanniemi, H., Collan, Y., Ultrastructural changes in human nasal cilia caused by the common cold and recovery of ciliated epithelium (1992) Ann. Otol. Rhinol. Laryngol., 101, pp. 982-987; Wilson, R., Alton, E., Rutman, A., Upper respiratory tract viral infection and mucociliary clearance (1987) Eur. J. Respir. Dis., 70, pp. 272-279; Carson, J.L., Collier, A.M., Hu, S.S., Acquired ciliary defects in nasal epithelium of children with acute viral upper respiratory infections (1985) N. Engl. J. Med., 312, pp. 463-468; Sakakura, Y., Changes of mucociliary function during colds (1983) Eur. J. Respir. Dis., 128 (SUPPL.), pp. 348-354; Pedersen, M., Sakakura, Y., Winther, B., Brofeldt, S., Mygind, N., Nasal mucociliary transport, number of ciliated cells, and beating pattern in naturally acquired common colds (1983) Eur. J. Respir. Dis., 128 (SUPPL.), pp. 355-364; Sakakura, Y., Sasaki, Y., Hornick, R.B., Mucociliary function during experimentally induced rhinovirus infection in man (1973) Ann. Otolaryngol., 82, pp. 203-211; Bende, M., Barrow, I., Heptonstall, J., Changes in human nasal mucosa during experimental coronavirus common colds (1989) Acta. Otolaryngol., 107, pp. 262-269; Monto, A.S., Coronaviruses (1982) Viral Infections of Humans, pp. 151-165. , Evans AS, ed. New York, Plenium Book Company; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common-cold virus in organ cultures (1965) BMJ, 1, pp. 1467-1470; Afzelius, B.A., Ultrastructure of human nasal epithelium during an episode of coronavirus infection (1994) Virchows Archive, 424, pp. 295-300; Macnaughton, M.R., Madge, M.H., Reed, S.E., Two antigenic groups of human coronaviruses detected by using enzyme-linked immunosorbent assay (1981) Infect. Immun., 33, pp. 734-737; Myint, S., Siddell, S., Tyrrell, D., Detection of human coronavirus 229E in nasal washing using RNA: RNA hybridization (1989) J. Med. Virol., 29, pp. 70-73; Gwaltney J.M., Jr., Hendley, O., Hayden, F.G., Updated recommendations for safety-testing of viral inocula used in volunteer experiments on rhinovirus colds (1992) Prog. Med. Virol., 39, pp. 256-263; Johnston, S.L., Papi, A., Bates, P.J., Mastronarde, J.G., Monick, M.M., Hunninghake, G.W., Low grade rhinovirus infection induces a prolonged release of IL-8 in pulmonary epithelium (1998) J. Immunol., 160, pp. 6172-6181; Jackson, G.G., Dowling, H.F., Speisman, I.G., Boand, A.V., Transmission of the common cold under controlled conditions. 1. The common cold as a clinical entity (1958) Arch Intern Med, 101, pp. 267-278; Mckean, M.C., Leech, M., Lambert, P.L., Hewitt, C., Myint, S., Silverman, M., A model of viral wheeze in non-asthmatic adults: Symptoms and physiology (2001) Eur. Respir. J., 18, pp. 23-32; Rutland, J., Cole, P.J., Non-invasive sampling of nasal cilia for measurement of beat frequency and study of ultrastructure (1980) Lancet, 2, pp. 564-565; Tsang, K.W.T., Rutman, A., Tanaka, E., Interaction of Pseudomonas aeruginosa with human respiratory mucosa in vitro (1994) Eur. Respir. J., 7, pp. 1746-1753; Rayner, F.J., Rutman, A., Dewar, A., Greenstone, M.A., Cole, P.J., Wilson, R., Ciliary disorientation alone as a cause of primary ciliary dyskinesia (1996) Am. J. Respir. Crit. Care. Med., 153, pp. 1123-1129; Chilvers, M.A., O'Callaghan, C., Analysis of ciliary beat pattern and beat frequency using digital high speed imaging: Comparison with the photomultiplier and photodiode methods (2000) Thorax, 55, pp. 314-317; Hoorn, B., Tyrrell, D.A., Effects of some viruses on ciliated cells (1966) Am. Rev. Respir. Dis., 93 (SUPPL.), pp. 156-161; Tristram, D.A., Hicks W., Jr., Hard, R., Respiratory syncytial virus and human bronchial epithelium (1998) Arch. Otolaryngol. Head Neck Surg., 124, pp. 777-783; Giorgi, P.L., Oggiano, N., Braga, P.C., Cilia in children with recurrent upper respiratory tract infections: Ultrastructural observations (1992) Pediat. Pulmonol., 14, pp. 201-205; Winther, B., Brofeldt, S., Christensen, B., Mygind, N., Light and scanning electron microscopy of nasal biopsy material from patients with naturally acquired common colds (1984) Acta. Otolaryngol., 97, pp. 309-318; Becker, W.B., McIntosh, K., Dees, J.H., Chanock, R.M., Morphogenesis of avian infectious bronchitis virus and a related human virus (strain 229E) (1967) J. Virol., 1, pp. 1019-1027; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Chanock, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc. Natl. Acad. Sci. USA, 57, pp. 933-940; Evermann, J.F., Heeney, J.L., McKeirnan, A.J., O'Brien, S.J., Comparative features of a coronavirus isolated from a cheetah with feline infectious peritonitis (1989) Virus Res., 13, pp. 15-27; Collinson, J., Nicholson, K.G., Cancio, E., Effects of upper respiratory tract infections in patients with cystic fibrosis (1996) Thorax, 51, pp. 1115-1122","O'Callaghan, C.; Childrens Asthma Center, Dept. of Child Health, University of Leicester, P.O. Box 65, Leicester LE2 7LX, United Kingdom",,,09031936,,ERJOE,"11829103","English","Eur. Respir. J.",Article,"Final",Open Access,Scopus,2-s2.0-0035694436
"Prentice E., Denison M.R.","7003706540;7101971810;","The cell biology of coronavirus infection",2001,"Advances in Experimental Medicine and Biology","494",,,"609","614",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701383&partnerID=40&md5=b2e3bf25f36922d42d785b3c264ed596","Department of Microbiology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States","Prentice, E., Department of Microbiology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States; Denison, M.R., Department of Microbiology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States","The ability to obtain entire volume data on infected cells will allow us to define much more accurately the interactions of viral proteins with host cell structures such as ER, Golgi, and cytoskeletal elements. In addition, the demonstrated ability to express viral proteins fused to fluorescent markers in in live cells will allow us to follow specific proteins or complexes during the course of infection and to determine if exogenously expressed proteins are able to target to sites of active viral replication. This in turn will allow new approaches to the study of viral and cellular protein-protein interactions, as methods to study the biology and pathogenesis of MHV infection at a cellular level. Finally, the approaches described here will allow us to define protein complementation of defective viruses at a cellular level, rather than being dependent on population measurements of RNA, protein, or progeny virus. By combining these approaches with available biochemical and molecular biological approaches and the emerging reverse genetic and recombinant genetic approaches, rapid progess in understanding the details of coronavirus-cell interactions should be possible.",,"virus RNA; conference paper; confocal microscopy; controlled study; Coronavirus; cytology; cytoskeleton; endoplasmic reticulum; Golgi complex; image processing; Murine hepatitis coronavirus; nonhuman; priority journal; three dimensional imaging; virion; virus cell interaction; virus infection; Animals; Cell Line; Fluorescent Antibody Technique; Mice; Microscopy, Confocal; Murine hepatitis virus; Viral Proteins; Viral Structural Proteins; Coronavirus; Murinae; Murine hepatitis virus","Bi, W., Pinon, J.D., Hughes, S., Bonilla, P.J., Holmes, K.V., Weiss, S.R., Leibowitz, J.L., Localization of mouse hepatitis virus open reading frame la derived proteins (1998) J. Neurovirology, 4, pp. 594-605; Bost, A.G., Carnahan, R.H., Lu, X.-T., Denison, M.R., Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly (2000) J. Virol., 74, pp. 3379-3387; Denison, M.R., Spaan, J.M., Van der Meer, Y., Gibson, C.A., Sims, A.C., Prentice, E., Lu, X.T., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) J. Virol., 73, pp. 6862-6871; Holmes, K.V., Lai, M.M.C., Coronaviridae: The viruses and their replication (1996) Virology, 1, pp. 1075-1093. , (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.) 2 vols. Lippincott-Raven Publishers, Philadelphia; Shi, S.T., Schiller, J.J., Kanjanahaluethai, A., Baker, S., Oh, J., Lai, M.M.C., Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells (1999) J. Virol., 73, pp. 5957-5969; Sims, A.C., Ostermann, J., Denison, M.R., Mouse hepatitis virus replicase proteins associate with two distinct populations of intracellular membranes (2000) J. Virol., 74, pp. 5647-5654; Van der Meer, Y., Snijder, E.J., Dobbe, J.C., Schleich, S., Denison, M.R., Spaan, W.J.M., Krinjnse Locker, J., The localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication (1999) J. Virol., 73, pp. 7641-7657","Prentice, E.; Department of Microbiology, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States",,,00652598,,AEMBA,"11774533","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701383
"Soma T., Hara M., Ishii H., Yamamoto S.","7103108050;7403348767;55226825200;55475455200;","Antibody Testing Against Canine Coronavirus by Immunoperoxidase Plaque Staining",2001,"Veterinary Research Communications","25","4",,"327","336",,3,"10.1023/A:1010634810315","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035347923&doi=10.1023%2fA%3a1010634810315&partnerID=40&md5=07e50ec9ec1f7a02da12de8326a77fa6","Veterinary Diagnostic Laboratory, Marupi Lifetech Co., Ltd., Ikeda, Osaka, Japan; Department of Microbiology, School of Veterinary Medicine, Azabu University, Sagamihara, Kanagawa, Japan; Sukagawa Animal Hospital, Sukagawa, Fukushima, Japan; Department of Immunology, Coll. of Environ. and Health Science, Azabu University, Sagamihara, Kanagawa, Japan; Veterinary Diagnostic Laboratory, Marupi Lifetech Co., Ltd., 103 Fushiocho, Ikeda, Osaka 563-0011, Japan","Soma, T., Veterinary Diagnostic Laboratory, Marupi Lifetech Co., Ltd., Ikeda, Osaka, Japan, Veterinary Diagnostic Laboratory, Marupi Lifetech Co., Ltd., 103 Fushiocho, Ikeda, Osaka 563-0011, Japan; Hara, M., Department of Microbiology, School of Veterinary Medicine, Azabu University, Sagamihara, Kanagawa, Japan; Ishii, H., Sukagawa Animal Hospital, Sukagawa, Fukushima, Japan; Yamamoto, S., Department of Immunology, Coll. of Environ. and Health Science, Azabu University, Sagamihara, Kanagawa, Japan","The application of the immunoperoxidase (IP) plaque staining procedure (IP test) to the diagnosis of canine coronavirus (CCV) infection was investigated. The IP test did not react with sera from either 15 specific pathogen-free (SPF) dogs or 7 SPF dogs immunized with a multivalent vaccine, including canine parvovirus type 2, canine distemper virus, canine adenovirus type 2, and canine parainfluenza virus. To compare the IP test with the neutralizing test (NT), sera from 240 healthy dogs and from 3 experimentally CCV-infected dogs were examined. All 60 sera positive for NT antibody were positive for IP antibody, and all 180 sera negative for NT antibody were negative for IP antibody in the healthy dogs. The IP titres showed similar changes with time after CCV inoculation to those of the NT titres in the experimentally infected dogs. These findings indicate that the IP test specifically detected anti-CCV antibodies. When the IP test and NT were compared in dogs with diarrhoeic signs. 2.1% of 48 sera and 20.3% of 74 sera, which were all negative for NT antibody, were positive for IP antibody in the dogs of under one year of age and at least one year of age, respectively. The difference between the IP and NT titres (log10 [reciprocal of IP titre] - log10 [reciprocal of NT titre]) for the diarrhoeic dogs of under one year of age (2.350±0.931) was significantly larger than that for the healthy dogs (0.982±0.447) (p &lt; 0.0001), the NT titre being negative or very low, despite a high IP titre in many diarrhoeic dogs. Hence, the IP test is more able to detect anti-CCV antibodies, especially in dogs showing clinical signs. The IP-positivity rate was significantly higher in the diarrhoeic dogs of under one year of age (48.7%) than in the healthy dogs (25.0%) (χ2 = 19.844, p&lt;0.0001), suggesting that CCV may contribute to diarrhoea in many juvenile dogs.","Antibody; Canine coronavirus; Diagnosis; Diarrhoea; Dog; Immunoperoxidase plaque staining; Neutralizing test; Serology","Adenoviridae; Canine adenovirus type 2; Canine coronavirus; Canine distemper virus; Canine parainfluenza virus; Canine parvovirus 2; Canis familiaris; Coronavirus; distemper virus; Human adenovirus type 2; Parvovirus; virus antibody; animal; animal disease; article; blood; comparative study; Coronavirus; dog; dog disease; enzyme immunoassay; germfree animal; isolation and purification; sensitivity and specificity; serodiagnosis; virology; virus infection; Animals; Antibodies, Viral; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Immunoenzyme Techniques; Neutralization Tests; Sensitivity and Specificity; Specific Pathogen-Free Organisms","Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Veterinary Medicine, 83, pp. 360-366; Appel, M.J.G., Cooper, B.J., Greisen, H., Scott, F., Carmichael, L.E., Canine viral enteritis. I. Status report on corona- And parvo-like viral enteritides (1979) Cornell Veterinarian, 69, pp. 123-133; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, R.S., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proceedings of the 78th Meeting of the us Animal Health Association, pp. 359-366; Bland, J.M., Altman, D.G., Statistical methods for assessing agreement between two methods of clinical measurement (1986) The Lancet, 1, pp. 307-310; Garwes, D.J., Reynolds, D.J., The polypeptide structure of canine coronavirus and its relationship to porcine transmissible gastroenteritis virus (1981) Journal of General Virology, 52, pp. 153-157; Hara, M., Fukuyama, M., Ikeda, T., Kiuchi, A., Tabuchi, K., Antibody response in puppies infected with canine coronavirus (1993) Journal of Japanese Veterinary Medical Association, 46, pp. 861-865. , in Japanese with English summary; Kai, K., Yukimune, M., Murata, T., Uzuka, Y., Kanoe, M., Matsumoto, H., Humoral immune responses of cats to feline infectious peritonitis virus infection (1992) Journal of Veterinary Medical Science, 54, pp. 501-507; Kokubu, T., Taharaguchi, S., Hatano, M., Takahashi, T., Iwamoto, K., Masubuchi, K., Yamanaka, M., Inaba, Y., Pathogenicity of canine coronavirus for puppies (1998) Journal of Japanese Veterinary Medical Association, 51, pp. 193-196. , in Japanese with English summary; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro-neutralization test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Japanese Journal of Veterinary Science, 49, pp. 563-565; Palmer-Densmore, M.L., Johnson, A.F., Sabara, M.I.J., Development and evaluation of an ELISA to measure antibody responses to both the nucleocapsid and spike proteins of canine coronavirus (1998) Journal of Immunoassay, 19, pp. 1-22; Pan, I.C., Huang, T.S., Hess, W.R., New method of antibody detection by indirect immunoper-oxidase plaque staining for serodiagnosis of African swine fever (1982) Journal of Clinical Microbiology, 16, pp. 650-655; Reed, L.J., Muench, H., A simple method of estimating fifty percent end points (1938) American Journal of Hygiene, 27, pp. 493-497; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H., UytdeHaag, F.G., Osterhaus, A.D., The use of enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in the Netherlands (1991) Veterinary Microbiology, 26, pp. 25-40; Sato, K., Tanaka, Y., Kurogi, H., Tokuhisa, S., Numba, K., Inaba, Y., Matumoto, M., Detection of antibody to pseudorabies virus in swine sera by indirect immunoperoxidase plaque staining (1988) Journal of Clinical Microbiology, 26, pp. 79-81; Schnagl, R.D., Holmes, I.H., Coronavirus-like particles in stools from dogs from some country areas of Australia (1978) Veterinary Record, 102, pp. 528-529; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Veterinary Microbiology, 42, pp. 255-259; Towbin, H., Staehelin, T., Gordan, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proceedings of the National Academy of Sciences of the USA, 76, pp. 4350-4354; Tuchiya, K., Horimoto, T., Azetaka, M., Takahashi, E., Konishi, S., Enzyme-linked immunosor-bent assay for the detection of canine coronavirus and its antibody in dogs (1991) Veterinary Microbiology, 26, pp. 41-51; Yasoshima, A., Fujinami, F., Doi, K., Kojima, A., Takada, H., Okaniwa, A., A case report on mixed infection of canine parvovirus. Electron microscopy and recovery of canine coronavirus (1983) Japanese Journal of Veterinary Science, 45, pp. 217-225","Soma, T.; Veterinary Diagnostic Laboratory, Marupi Lifetech Co., Ltd., 103 Fushiocho, Ikeda, Osaka 563-0011, Japan",,,01657380,,VRCOD,"11432433","English","Vet. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-0035347923
"Cavanagh D.","26642890500;","Innovation and discovery: The application of nucleic acid-based technology to avian virus detection and characterization",2001,"Avian Pathology","30","6",,"581","598",,30,"10.1080/03079450120092071","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035666130&doi=10.1080%2f03079450120092071&partnerID=40&md5=74ca399f20f8950d9dc1acfb6be3b6cf","Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom","Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury RG20 7NN, United Kingdom","Polymerase chain reaction (PCR)-based approaches to the detection, differentiation and characterization of avian pathogens continue to be developed and refined. The PCRs, or reverse transcriptase-PCRs, may be general, designed to detect all or most variants of a pathogen, or to be serotype, genotype or pathotype specific. Progress is being made with respect to making nucleic acid approaches more suitable for use in diagnostic laboratories. Robotic workstations are now available for extraction of nucleic acid from many samples in a short time, for routine diagnosis. Following general PCR, the DNA products are commonly analyzed by restriction endonuclease mapping (restriction fragment length polymorphism), using a small number of restriction endonucleases, based on a large body of sequence data. Increasingly, however, nucleotide sequencing is being used to analyze the DNA product, in part due to the expanding use of non-radioactive sequencing methods that are safe and enable high throughout. In this review, I highlight some recent developments with many avian viruses: Newcastle disease virus; circoviruses in canary and pigeon; infectious bursal disease virus (Gumboro disease virus); avian adenoviruses, including Angara disease/infectious hydropericardium virus, haemorrhagic enteritis virus of turkeys, and egg drop syndrome virus; avian herpesviruses, including infectious laryngotracheitis virus, duck plague virus, psittacine herpesvirus (Pacheco's parrot disease virus), Marek's disease virus and herpesvirus of turkeys; avian leukosis virus (associated with lymphoid leukosis or myeloid leukosis, and egg transmission); avian pneumoviruses (turkey rhinotracheitis virus); avian coronaviruses, including infectious bronchitis virus, turkey coronavirus and pheasant coronavirus; astrovirus, in the context of poult enteritis and mortality syndrome, and avian nephritis virus; and avian encephalomyelitis virus, a picornavirus related to hepatitis A virus.",,"Anas sp.; Animalia; Astroviridae; Aves; Aviadenovirus; avian adenovirus; Avian encephalomyelitis virus; Avian infectious bronchitis virus; Avian leukosis virus; Avian nephritis virus; Avian pneumovirus; Circoviridae; Columba; Coronavirus; DNA viruses; Duck adenovirus 1; Gallid herpesvirus 1; Gallid herpesvirus 2; Hepatitis A virus; Herpesviridae; herpetovirus; Infectious bursal disease virus; leukosis virus; Meleagrid herpesvirus 1; Newcastle disease virus; Pheasant coronavirus; Picornaviridae; Pneumovirus; Psittacidae; Psittaciformes; Turkey adenovirus 3; Turkey coronavirus; Turkey rhinotracheitis virus","Abe, T., Nakamura, K., Tojo, H., Shibahara, T., Yamaguchi, S., Yuasa, N., Histology, immunchemistry and ultrastructure of hydropericardium syndrome in adult broiler breeders and broiler chicks (1998) Avian Diseases, 42, pp. 606-612; Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathology, 25, pp. 817-836; Adzhar, A., Gough, R.E., Haydon, D., Shaw, K., Britton, P., Cavanagh, D., Molecular analysis of the 793/B serotype of infectious bronchitis virus in Great Britain (1997) Avian Pathology, 26, pp. 625-640; Aldous, E.W., Alexander, D.J., Technical review: Detection and differentiation of Newcastle disease virus (avian paramyxovirus type 1) (2001) Avian Pathology, 30, pp. 117-130; Aldous, E.W., Collins, M.S., McGoldrick, A., Alexander, D.J., Rapid pathotyping of Newcastle disease virus (NDV) using fluorogenic probes in a PCR assay (2001) Veterinary Microbiology, 80, pp. 201-213; Arshad, S.S., Smith, L.M., Howes, K., Russell, P.H., Venugopal, K., Payne, L.N., Tropism of subgroup J avian leukosis virus as detected by in situ hybridisation (1999) Avian Pathology, 28, pp. 163-169; Bacon, L.D., Detection of endogenous avian leukosis virus envelope in chicken plasma using R2 antiserum (2000) Avian Pathology, 29, pp. 153-164; Bai, J., Payne, L.N., Skinner, M.A., HPRS-103 (exogenous avian leukosis virus subgroup J) has an env gene related to those of endogenous elements EAV-0 and E51 and has an E element found previously only in sarcoma viruses (1995) Journal of Virology, 69, pp. 779-784; Ballagi-Pordány, A., Wehmann, E., Herczeg, J., Belák, S., Lomniczi, B., Identification and grouping of Newcastle disease virus strains by restriction site analysis of a region from the F gene (1996) Archives of Virology, 141, pp. 243-261; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry 10th edn, pp. 1025-1031. , B.W. 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Ames, IA: Iowa State Univeristy Press; Bäyon-Auboyer, M.H., Jestin, V., Toquin, D., Cherbonnel, M., Eterradossi, N., Comparison of F, G and N based RT PCR protocols with conventional virological procedures for the detection and typing of turkey rhinotracheitis virus (1999) Archives of Virology, 144, pp. 1091-1109; Bäyon-Auboyer, M.H., Jestin, V., Toquin, D., Cherbonnel, M., Eterradossi, N., Nucleotide sequences of the F, L and G protein genes of two non-A/non-B avian pneumoviruses (APV) reveal a novel APV subgroup (2000) Journal of General Virology, 81, pp. 2723-2733; Blackall, P.J., Miflin, J.K., Identification and typing of Pasteurella multocida: A review (2000) Avian Pathology, 29, pp. 271-287; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Bumstead, N., Sillibourne, J., Rennie, M., Ross, N., Davison, F., Quantification of Marek's disease virus in chicken lymphocytes using the polymerase chain reaction with fluorescence detection (1997) Journal of Virological Method, 65, pp. 75-81; Burgess, S.C., Davison, T.F., A quantitative duplex PCR technique for measuring amounts of cell-associated Marek's disease virus: Differences in two populations of lymphoma cells (1999) Journal of Virological Methods, 82, pp. 27-37; Capua, I., Marangon, S., The avian influenza epidemic in Italy, 1999-2000: A review (2000) Avian Pathology, 29, pp. 289-294; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Co-circulation of four types of infectious bronchitis virus (793/B, 624/I, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 587-592; Cattoli, G., Manvell, R.J., Tisato, E., Banks, J., Capua, I., Characterisation of Newcastle diseae viruses isolated in Italy in 2000 (2001) Avian Pathology, 30, pp. 465-469; Cavanagh, D., Commentary. 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"Eiros Bouza J.Ma., Bachiller Luque Ma.R., Ortiz de Lejarazu R.","7003505874;6603221623;7003417829;","Emergent riboviruses implicated in gastroenteritis [Ribovirus emergentes implicados en las gastroenteritis]",2001,"Anales Espanoles de Pediatria","54","2",,"136","144",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035744893&partnerID=40&md5=c27c6f18c267b61899dadd5d6555e44c","Depto. de Microbiología, 6.a pl. Facultad de Medicina, Avda. Ramón y Cajal, 7, 47005 Valladolid, Spain","Eiros Bouza, J.Ma., Depto. de Microbiología, 6.a pl. Facultad de Medicina, Avda. Ramón y Cajal, 7, 47005 Valladolid, Spain; Bachiller Luque, Ma.R., Depto. de Microbiología, 6.a pl. Facultad de Medicina, Avda. Ramón y Cajal, 7, 47005 Valladolid, Spain; Ortiz de Lejarazu, R., Depto. de Microbiología, 6.a pl. Facultad de Medicina, Avda. Ramón y Cajal, 7, 47005 Valladolid, Spain","Viral agents are one of the main causes of acute diarrhea, particularly in infants and young children. Astrovirus, coronavirus, torovirus, and picobirnavirus are increasingly being identified as causative agents of gastroenteritis. Astroviruses have been detected in the stools of between 1.2% and 20% of children with diarrhea requiring medical care in a variety of geographical areas. Outbreaks have been described in schools, day care settings and pediatric wards. Children younger than 3 years old are the most frequently affected. In temperate climates incidence is greater in winter whereas in tropical areas infection occurs throughout the year. Transmission is mainly through the fecal-oral route. At least seven serotypes of human astroviruses have been recognized and serotype 1 is more common than the other serotypes. Astroviruses are often shed in stools during long periods and can be detected by electron microscopy. An enzyme-immunoassay technique that detects the astrovirus group antigen has been widely used in epidemiological studies. Nucleic acid hybridization and polymerase chain reaction-based techniques have also been used. Enteric coronaviruses have most frequently been associated with gastrointestinal disease in neonates and children younger than 12 years old. The role of toroviruses and picobirnaviruses as causative agents of gastroenteritis is still emerging. Further epidemiological studies to determine the frequency of these viruses in the community and to identify their mechanisms of transmission are needed, as are further studies to elucidate the pathophysiology of diseases due to these agents.","Astrovirus; Coronavirus; Gastroenteritis; Picobirnavirus; Torovirus","acute diarrhea; antigen detection; Astrovirus; Coronavirus; electron microscopy; enzyme immunoassay; epidemic; feces analysis; gastroenteritis; human; pathophysiology; Picobirnavirus; review; ribovirus; Torovirus; virus; Acute Disease; Age Factors; Astroviridae; Astroviridae Infections; Child; Child, Preschool; Coronaviridae; Coronaviridae Infections; Diarrhea, Infantile; Feces; Gastroenteritis; Humans; Infant; Infant, Newborn; Microscopy, Electron; Picobirnavirus; Polymerase Chain Reaction; RNA Virus Infections; Torovirus; Torovirus Infections","Blacklow, N.R., Greenberg, H.B., Viral gastroenteritis (1991) N Engl J Med, 325, pp. 252-264; Sherman, P.M., Petric, M., Cohen, M.B., Infectious gastroenterocolitides in children: An update on emerging pathogens (1996) Pediatr Clin North Am, 43, pp. 391-407; Framm, S.R., Soave, R., Agents of diarrhea (1997) Med Clin North Am, 81, pp. 427-447; Treanor, J.J., Dolin, R., Astrovirus, Toroviruses and Picobirnaviruses (2000) Principles and practice of infectious diseases, 5.a ed., 2, pp. 1956-1958. , Mandell GL, Bennett JE, Dolin R, eds. Mandell, Douglas and Bennett's. 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Epidemiologic, clinical, and laboratory observations (1985) Am J Dis Child, 139, pp. 928-934; Marshall, J.A., Birch, C.J., Williamson, H.G., Bowden, D.K., Boveington, C.M., Kuberski, T., Coronavirus-like particles and other agents in the faeces of children in Efate, Vanuatu (1982) J Trop Med Hyg, 85, pp. 213-215; Luby, J.P., Clinton, R., Kurtz, S., Adaptation of human enteric coronavirus to growth in cell lines (1999) J Clin Virol, 12, pp. 43-51; De Haan, C.A., Vennema, H., Rottier, P.J., Coronavirus envelope assembly in sensitive to changes in the terminal regions of the viral M protein (1998) Adv Exp Med Biol, 440, pp. 367-375; Cristallo, A., Biamonti, G., Battaglia, M., Cereda, P.M., DNA probe for the human coronavirus OC43 also detects neonatal calf diarrhea coronavirus (NCDCV) (1996) New Microbiol, 19, pp. 251-256; McGoldrick, A., Lowings, J.P., Paton, D.J., Characterisation of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a (1999) Arch Virol, 144, pp. 763-770; Cavanagh, D., Horzinek, M.C., Genus Torovirus assigned to the Coronaviridae (1993) Arch Virol, 128, pp. 395-396; Horzinek, M.C., Molecular evolution of corona-and toroviruses (1999) Adv Exp Med Biol, 473, pp. 61-72; Beards, G.M., Hall, C., Green, J., Flewett, T.H., Lamouliatte, F., Du Pasquier, P., An enveloped virus in stools of children and adults with gastroenteritis that resembles the Breda virus of calves (1984) Lancet, 1, pp. 1050-1052; Koopmans, M., Herrewegh, A., Horzinek, M.C., Diagnosis of torovirus infection (1991) Lancet, 337, p. 859; Koopmans, M., Petric, M., Glass, R., Monroe, S.S., Enzyme-linked immunosorbent assay reactivity of torovirus-like particles in fecal specimens from humans wuth diarrhea (1993) J Clin Microbiol, 31, pp. 2738-2744; Krishnan, T., Naik, T.N., Electronmicroscopic evidence of totovirus like particles in children with diarrhoea (1997) Indian J Med Res, 105, pp. 108-110; Jamieson, F.B., Wang, E.E., Bain, C., Good, J., Duckmanton, L., Petric, M., Human torovirus: A new nosocomial gastrointestinal pathogen (1998) J Infect Dis, 178, pp. 1263-1269; Duckmanton, L., Luan, B., Devenish, J., Tellier, R., Petric, M., Characterizarion of torovirus from human fecal specimens (1997) Virology, 239, pp. 158-168; Koopmans, M.P., Goosen, E.S., Lima, A.A., McAuliffe, I.T., Nataro, J.P., Barrett, L.J., Association of torovirus with acute and persistent diarrhea in children (1997) Pediatr Infect Dis J, 16, pp. 504-507; Snijder, E.J., Horzinek, M.C., Toroviruses: Replication, evolution and comparison with other members of the coronavirus-like superfamily (1993) J Gen Virol, 74, pp. 2305-2316; Pereira, H.G., Fialho, A.M., Flewett, T.H., Teixeira, J.M., Andrade, Z.P., Novel viruses in human faeces (1988) Lancet, 2, pp. 103-104; Chandra, R., Picobirnavirus, a novel group of undescribed viruses of mammals and birds: A minireview (1997) Acta Virol, 41, pp. 59-62; Grohmann, G.S., Glass, R.I., Pereira, H.G., Monroe, S.S., Hightower, A.W., Weber, R., Enteric viruses and diarrhea in HIV-infected patients (1993) N Engl J Med, 329, pp. 14-20. , Enteric oportunistic Infectoins Working Group; Giordano, M.O., Martinez, L.C., Rinaldi, D., Espul, C., Martinez, N., Isa, M.B., Diarrhea and enteric emerging viruses in HIV-infected patients (1999) AIDS Res Hum Retroviruses, 15, pp. 1427-1432; Gonzalez, G.G., Pujol, F.H., Liprandi, F., Deibis, L., Ludert, J.E., Prevalence of enteric viruses in human immunodeficiency virus seropositive patients in Venezuela (1998) J Med Virol, 55, pp. 288-292; Gallimore, C.I., Appleton, H., Lewis, D., Green, J., Brown, D.W., Detection and characterization of bisegmented double-stranded RNA viruses (picobirnaviruses in human faecal specimens) (1995) J Med Virol, 45, pp. 135-140; Cascio, A., Bosco, M., Vizzi, E., Giammanco, A., Ferraro, D., Arista, S., Identification of picobirnavirus from faeces of Italian children suffering from acute diarrhea (1996) Eur J Epidemiol, 12, pp. 545-547","Eiros Bouza, J.Ma.; Depto. de Microbiología, 6.a pl. Facultad de Medicina, Avda. Ramón y Cajal, 7, 47005 Valladolid, Spain; email: eiros@med.uva.es",,,03024342,,AEPDC,"11181210","Spanish","An. Esp. Pediatr.",Review,"Final",,Scopus,2-s2.0-0035744893
"Collins A.R.","24439435400;","Induction of apoptosis in MRC-5, diploid human fetal lung cells after infection with human coronavirus OC43",2001,"Advances in Experimental Medicine and Biology","494",,,"677","682",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035704372&partnerID=40&md5=48453367ee84f2516af1d708392d0131","Department of Microbiology, State University of New York, Buffalo, NY 14214, United States","Collins, A.R., Department of Microbiology, State University of New York, Buffalo, NY 14214, United States",[No abstract available],,"cell death; ciliated epithelium; conference paper; Coronavirus; diploidy; epithelium cell; fetus lung; human; human cell; lung alveolus cell; multiple sclerosis; pathogenesis; priority journal; tissue culture; upper respiratory tract infection; virus induction; virus infection; Apoptosis; Cell Line; Coronavirus OC43, Human; Cytopathogenic Effect, Viral; DNA Fragmentation; Humans; Lung; Coronavirus","An, S., Chen, C.-J., Xin, Y., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Arbour, N., Côté, G., Lachance, C., Tardieu, M., Cashman, N.R., Talbot, P.J., Acute and persistent infection of human neural cell lines by human coronavirus OC43 (1999) J. Virol., 73, pp. 3338-3350; Bonati, A., Albertini, R., Garau, D., Pinelli, S., Lunghi, P., Almici, C., Carlo-Stella, C., Dall'aglio, P., BCL2 oncogene protein expression in human hematopoietic precursors during fetal life (1996) Exp. Hematol., 24, pp. 459-465; Collins, A.R., Sorensen, O., Regulation of viral persistence in human glioblastoma and rhabdomyosarcoma cells infected with coronavirus OC43 (1986) Microbial Path., 1, pp. 573-583; Cristallo, A., Gambaro, F., Biamonte, G., Ferrante, P., Battaglia, M., Cereda, P.M., Human coronavirus polyadenylated RNA sequences in cerebrospinal fluid from multiple sclerosis patients (1997) New Microb., 20, pp. 105-114; Eleouet, J., Chilmonczyk, S., Besnardeau, L., Laude, H., Transmissible gastroenteritis coronavirus induces programmed cell death in infected cells through a caspase-dependent pathway (1998) J. Virol., 66, pp. 4918-4924; Fischer, F., Stegen, C.R., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Hruskova, J., Heinz, F., Svandova, E., Pennigerova, S., Antibodies to human coronaviruses 229e and OC43 in the population of C.R. (1990) Arch. Virol., 34, pp. 346-352; Jan, J., Griffin, D.E., Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication (1999) J. Virol., 73, pp. 10296-10302; Jendrach, M., Theil, V., Siddell, S., Characterization of an internal ribosome entry site within mRNA5 of murine hepatitis virus (1999) Arch. Virol., 144, pp. 921-933; Makela, M.J., Puhakka, T., Ruuskanen, O., Leinonen, L.M., Saikku, P., Kimpimaki, M., Blomqvist, S., Arstila, P., Viruses and bacteria in the etiology of the common cold (1998) J. Clin. Microbiol., 36, pp. 539-542; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virol., 191, pp. 502-505; Varsano, S., Frolkis, I., Ophir, D., Expression and distribution of cell-membrane complement regulatory glycoproteins along the human respiratory tract (1995) Am. J. Respir. Crit. Care Med., 152, pp. 1087-1093","Collins, A.R.; Department of Microbiology, State University of New York, Buffalo, NY 14214, United States",,,00652598,,AEMBA,"11774544","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035704372
"Narayanan K., Makino S.","7101933409;7403067550;","Characterization of nucleocapsid-M protein interaction in murine coronavirus",2001,"Advances in Experimental Medicine and Biology","494",,,"577","582",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035704307&partnerID=40&md5=c953e6850a586c39dc3121ead62b1d3f","Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas, Austin, TX 78712, United States","Narayanan, K., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas, Austin, TX 78712, United States; Makino, S., Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas, Austin, TX 78712, United States",[No abstract available],,"bromelain; nucleocapsid protein; triton x 114; virus RNA; animal cell; conference paper; controlled study; Coronavirus; mouse; nonhuman; priority journal; protein protein interaction; protein RNA binding; virion; virus assembly; virus envelope; virus nucleocapsid; virus particle; Animals; Bromelains; Cell Line; Genome, Viral; Mice; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; RNA, Viral; Viral Matrix Proteins; Virion; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Baric, R.S., Fu, K., Schaad, M.C., Stohlman, S.A., Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups (1990) Virology, 177, pp. 646-656; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterisation of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte. Virusforch., 44, pp. 298-302; Kim, K.H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J. Virol., 71, pp. 3922-3931; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Eugene, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Macnaughton, M.R., Davies, H.A., Nermut, M.V., Ribonucleoprotein-like structures from coronavirus particles (1978) J. Gen. Virol., 39, pp. 545-549; Makino, S., Taguchi, F., Hayami, M., Fujiwara, K., Characterisation of small plaque mutants of mouse hepatitis virus, JHM strain (1983) Microbiol. Immunol., 27, pp. 445-454; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Narayanan, K., Maeda, A., Maeda, J., Makino, S., Characterisation of the coronavirus M protein and nucleocapsid interaction in infected cells, , In press; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation ofcoronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462","Narayanan, K.; Department of Microbiology, Inst. for Cell. and Molec. Biology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"11774528","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035704307
"Matsuyama S., Taguchi F.","7201442043;7103209890;","Inefficient infection of soluble receptor-resistant mutants of murine coronavirus in cells expressing MHVR2 receptor",2001,"Advances in Experimental Medicine and Biology","494",,,"233","236",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703993&partnerID=40&md5=3490177ef95f1cb50e84cfd4ec0185a7","National Institute of Neuroscience, NCNP 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Matsuyama, S., National Institute of Neuroscience, NCNP 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Taguchi, F., National Institute of Neuroscience, NCNP 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",[No abstract available],,"mouse hepatitis virus receptor 1; mouse hepatitis virus receptor 2; unclassified drug; virus receptor; vitronectin; animal cell; animal model; cell fusion; conference paper; controlled study; cytopathogenic effect; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; strain difference; syncytium; virus adsorption; virus infection; virus mutant; virus pathogenesis; virus strain; Animals; Cell Line; Glycoproteins; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutation; Viral Envelope Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. U.S.A., 83, pp. 8122-8126; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) J. Virol., 71, pp. 9024-9031; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Charactetization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435","Matsuyama, S.; National Institute of Neuroscience, NCNP 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",,,00652598,,AEMBA,"11774474","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703993
"Chen C.-J., An S., Makino S.","56288577100;55107136200;7403067550;","Induction of apoptosis in murine coronavirus-infected 17C1-1 cells",2001,"Advances in Experimental Medicine and Biology","494",,,"615","620",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703968&partnerID=40&md5=ff0ba9cd56854bf4d959dcb7ddc5eba1","Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Chen, C.-J., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; An, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Makino, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States",[No abstract available],,"caspase; DNA fragment; hoe 33342; animal cell; apoptosis; conference paper; controlled study; Coronavirus; DNA cleavage; mouse; Murine hepatitis coronavirus; nick end labeling; nonhuman; priority journal; transmissible gastroenteritis virus; virus infection; Animals; Apoptosis; Caspases; Cell Line; Mice; Murine hepatitis virus; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Transmissible gastroenteritis virus","Belyavskyi, M., Belyavskaya, E., Levy, G.A., Leibowitz, J.L., Coronavirus MHV-3-induced apoptosis in macrophages (1998) Virology, 250, pp. 41-49; Cohen, G.M., Caspases: The executioners of apoptosis (1997) Biochem. J., 326, pp. 1-16; Eleouet, J.-F., Chilmonczyk, S., Besnardeau, L., Laude, H., Transmissible gastroenteritis coronavirus induces programmed cell death in infected cells through a caspase-dependent pathway (1998) J. Virol., 72, pp. 4918-4924; Hinshaw, V.S., Olsen, C.W., Dybdahl-Sissoko, N., Evans, D., Apoptosis: A mechanism of cell killing by influenza A and B viruses (1994) J. Virol., 68, pp. 3667-3673; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Fesamte Virusforch., 44, pp. 298-302; Jacobson, M.D., Weil, M., Raff, M.C., Programmed cell death in animal development (1997) Cell, 88, pp. 347-354; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462","Chen, C.-J.; Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States",,,00652598,,AEMBA,"11774534","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703968
"Taguchi F., Shimazaki Y.K.","7103209890;36944983600;","Involvement in fusion activity of an epitope in the S2 subunit of murine coronavirus spike protein",2001,"Advances in Experimental Medicine and Biology","494",,,"213","218",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703922&partnerID=40&md5=32c98ff2216cdc794c9311c82527e181","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Shimazaki, Y.K., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",[No abstract available],,"epitope; protein subunit; spike glycoprotein; unclassified drug; virus fusion protein; amino acid sequence; amino acid substitution; animal cell; cell fusion; cell line; conference paper; hydrophobicity; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; receptor binding; sequence analysis; virus cell interaction; virus mutant; virus mutation; virus pathogenesis; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Viral; Cell Line; Epitopes; Membrane Fusion; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Mutation; Neutralization Tests; Receptors, Virus; Viral Envelope Proteins; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Collins, A.R., Knobler, R.L., Powell, H., Buchmeier, M.M.J., Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion (1982) Virology, 119, pp. 358-371; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. U.S.A., 83, pp. 8122-8126; Koolen, J.J.M., Borst, M.A., Horzinek, J.M.C., Spaan, W.J.M., Immunogenic peptide comprising a mouse hepatitis virus A59 B-cell epitope and an influenza virus T-cell epitope protects against lethal infection (1990) J. Virol., 64, pp. 6270-6273; Kubo, H., Takase, S.Y., Taguchi, F., Neutralization and fusion inhibition activities of monoclonal antibodies specific for the S1 subunit of the spike protein of neurovirulent murine coronavirus JHMV c1-2 variant (1993) J. Gen. Virol., 74, pp. 1421-1425; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Luo, Z., Weiss, S.R., Roles in cell-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein (1998) Virology, 244, pp. 483-494; Luytjes, W., Geerts, D., Posthumus, W., Meloen, R., Spaan, W.J.M., Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses (1989) J. Virol., 63, pp. 1408-1412; Schmidt, I., Skinner, M., Siddell, S., Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM (1987) J. Gen. Virol., 68, pp. 47-56; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant c1-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., Fleming, J.O., Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein (1989) Virology, 169, pp. 233-235; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant c1-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan",,,00652598,,AEMBA,"11774471","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703922
"Seybert A., Ziebuhr J.","7004923617;7003783935;","Guanosine triphosphatase activity of the human coronavirus helicase",2001,"Advances in Experimental Medicine and Biology","494",,,"255","260",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703706&partnerID=40&md5=950b6dc37e904ccdbf3abe3ec6dd7646","Institute of Virology, University of Würzburg, 97078 Würzburg, Germany","Seybert, A., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology, University of Würzburg, 97078 Würzburg, Germany",[No abstract available],,"adenosine triphosphatase; adenosine triphosphate; guanosine triphosphatase; guanosine triphosphate; helicase; polyuridylic acid; Baculovirus; concentration response; conference paper; Coronavirus; DNA denaturation; enzyme activity; enzyme assay; nonhuman; priority journal; protein expression; Acid Anhydride Hydrolases; Animals; Baculoviridae; Base Sequence; Cells, Cultured; Coronavirus 229E, Human; Guanosine Triphosphate; Humans; Insects; Molecular Sequence Data; Nucleoside-Triphosphatase; Recombination, Genetic; RNA Helicases; Coronavirus; unidentified baculovirus","Gorbalenya, A.E., Koonin, E.V., Viral proteins containing the purine NTP-binding sequence pattern (1989) Nucleic Acids Res., 17, pp. 8413-8440; Gorbalenya, A.E., Koonin, E.V., Comparative analysis of the amino acid sequences of the key enzymes of the replication and expression of positive-strand RNA viruses. Validity of the approach and functional and evolutionary implications (1993) Sov. Sci. Rev. D. Physicochem. Biol., 11, pp. 1-84; Gorbalenya, A.E., Koonin, E.V., Helicases: Amino acid sequence comparisons and structure-function relationships (1993) Curr. Opin. Struct. Biol., 3, pp. 419-429; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination (1988) FEBS Lett., 235, pp. 16-24; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes (1989) Nucleic Acids Res., 17, pp. 4713-4730; Kadaré, G., Haenni, A.L., Virus-encoded RNA helicases (1997) J. Virol., 71, pp. 2583-2590; Koonin, E.V., Dolja, V.V., Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences (1993) Crit. Rev. Biochem. Mol. Biol., 28, pp. 375-430; Lohman, T.M., Bjornson, K.P., Mechanisms of helicase-catalyzed DNA unwinding (1996) Annu. Rev. Biochem., 65, pp. 169-214; Schmid, S.R., Linder, P., D-E-A-D protein family of putative RNA helicases (1992) Mol. Microbiol., 6, pp. 283-291; Seybert, A., Hegyi, A., Siddell, S.G., Ziebuhr, J., The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity (2000) RNA, 6. , in press; Soultanas, P., Dillingham, M.S., Velankar, S.S., Wigley, D.B., DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase (1999) J. Mol. Biol., 290, pp. 137-148; Walker, J.E., Saraste, M., Runswick, M.J., Gay, N.J., Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold (1982) EMBO J., 1, pp. 945-951; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879","Seybert, A.; Institute of Virology, University of Würzburg, 97078 Würzburg, Germany",,,00652598,,AEMBA,"11774478","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703706
"Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Enjuanes L.","6603712040;57201828108;55761804900;6602523425;12801394500;7006565392;","A strategy for the generation of an infectious transmissible gastroenteritis coronavirus from cloned cDNA",2001,"Advances in Experimental Medicine and Biology","494",,,"261","266",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703639&partnerID=40&md5=6976372e515906d0965f57354ae6140a","Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Almazan, F., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Gonzalez, J.M., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Penzes, Z., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Calvo, E., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",[No abstract available],,"complementary DNA; animal cell; animal experiment; animal model; animal tissue; conference paper; controlled study; Coronavirus; gastroenteritis; genetic engineering; molecular cloning; newborn; nonhuman; priority journal; swine; technique; virus infectivity; virus isolation; virus pathogenesis; virus replication; Animals; Cells, Cultured; Cloning, Molecular; DNA, Complementary; Gastroenteritis, Transmissible, of Swine; Genetic Engineering; Swine; Transfection; Transmissible gastroenteritis virus; Virulence; Animalia; Coronavirus; Sus scrofa","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 5516-5521; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1996) J. Virol., 73, pp. 1535-1545; Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J. Virol., 66, pp. 1841-1848; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv. Virus Res., 53, pp. 245-264; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebaguer, F., Callebaut, P., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Wang, K., Boysen, C., Shizuya, H., Simon, M.I., Hood, L., Complete nucleotide sequence of two generations of a bacterial artificial chromosome cloning vector (1997) Biotechniques, 23, pp. 992-994","Almazan, F.; Centro Nacional de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"11774479","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703639
"Scwegmann C., Zimmer G., Herrler G.","6507172656;7102982629;7006339246;","Are intestinal mucins involved in the pathogenicity of transmissible gastroenteritis coronavirus?",2001,"Advances in Experimental Medicine and Biology","494",,,"219","223",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703528&partnerID=40&md5=fd1f434ae3d5213239c062a5bd3e572a","Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany","Scwegmann, C., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Zimmer, G., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Herrler, G., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany",[No abstract available],,"mucin; sialic acid; animal tissue; binding affinity; conference paper; Coronavirus; diarrhea; high performance liquid chromatography; nonhuman; priority journal; swine disease; virus envelope; virus pathogenesis; virus virulence; Animals; Gastroenteritis, Transmissible, of Swine; Intestine, Small; Mucins; N-Acetylneuraminic Acid; Swine; Transmissible gastroenteritis virus; Animalia; Coronavirus; Sus scrofa","Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Enss, M.-L., Schmidt-Wittig, U., Müller, H., Mai, U.E.H., Coenen, M., Hedrich, H.J., Response of germfree rat colonic mucous cells to peroral endotoxin application (1996) European Journal of Cell Biology, 71, pp. 99-104; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) Journal of Virology, 71, pp. 3285-3287; Krempl, C., Ballesteros, M.L., Zimmer, G., Enjuanes, L., Klenk, H.-D., Herrler, G., Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants (2000) Jounal of General Virology, 81, pp. 489-496; Pensaert, M., Callebaut, P., Cox, E., Enteric coronaviruses of animals (1993) Viral Infections of the Gastrointestinal Tract, pp. 627-696. , Edited by A.Z. Kapikian. New York, Marcel Dekker; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) Journal of General Virology, 73, pp. 901-906; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) Journal of Virology, 70, pp. 5634-5637","Scwegmann, C.; Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany",,,00652598,,AEMBA,"11774472","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703528
"Shen S., Ding X.L.","7403431806;8972667300;","Characterization of temperature-sensitive (ts) mutants of coronavirus infectious bronchitis virus (IBV)",2001,"Advances in Experimental Medicine and Biology","494",,,"557","562",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035703272&partnerID=40&md5=7a429c02ac38aec03055036ddc19ab4d","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Linke, Singapore 117604, Singapore","Shen, S., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Linke, Singapore 117604, Singapore; Ding, X.L., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Linke, Singapore 117604, Singapore",[No abstract available],,"arginine; glutamine; isoleucine; leucine; membrane protein; methionine; nucleoprotein; spike protein; structural protein; threonine; unclassified drug; virus envelope protein; virus protein; virus RNA; animal cell; Avian infectious bronchitis virus; conference paper; controlled study; nonhuman; Northern blotting; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; RNA sequence; RNA synthesis; temperature sensitive mutant; Vero cell; virus mutant; Animals; Cercopithecus aethiops; Infectious bronchitis virus; Mutation; Plaque Assay; RNA, Viral; Sequence Analysis, DNA; Temperature; Vero Cells; Viral Structural Proteins; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus","Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68 (PART 1), pp. 57-77; Lai, M.M.C., Cavanagh, D., The Molecular Biology of Coronaviruses (1998) Advances in Virus Research, 48, pp. 1-99; Liu, D.X., Shen, S., Xu, H.Y., Wang, S.F., Proteolytic mapping of the coronavirus infectious virus 1b polyprotein: Evidence for the presence of four cleavage sites of the 3C-like proteinase and identification of two novel cleavage products (1998) Virology, 246, pp. 288-297; Luytjes, W., Gerritsma, H., Bos, E., Spaan, W., Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein (1997) J. Virol., 71 (2), pp. 949-955; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Shen, S., Burke, B., Desselberger, U., Rearrangement of the VP6 gene of a group A rotavirus in combination with a point mutation affecting trimer stability (1994) J. Virol., 68, pp. 1682-1688; Shen, S., McKee, T.A., Wang, Z.D., Desselberger, U., Liu, D.X., Sequence analysis and in vitro expression of genes 6 and 11 of an ovine group B rotavirus isolate, KB63: Evidence for a non-defective, C-terminally truncated NSP1 and a phosphorylated NSP5 (1999) J. Gen. Viral., 80, pp. 2077-2085; Shen, S., Liu, D.X., Determination of the complete nucleotide sequence of a vaccine strain of porcine reproductive and respiratory syndrome virus and identification of the NSP2 gene with an unique insertion (2000) Arch. Virol., 145, pp. 871-883","Shen, S.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Linke, Singapore 117604, Singapore",,,00652598,,AEMBA,"11774524","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035703272
"Enjuanes L., Sola I., Almazan F., Izeta A., Gonzalez J.M., Alonso S.","7006565392;7003336781;6603712040;6602523425;57201828108;57210695335;","Coronavirus derived expression systems",2001,"Advances in Experimental Medicine and Biology","494",,,"309","321",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701789&partnerID=40&md5=0b7e19d215ad944a14e849b1513d33c7","Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Enjuanes, L., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Almazan, F., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Gonzalez, J.M., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Alonso, S., Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",[No abstract available],,"virus messenger RNA; virus vector; base pairing; conference paper; Coronavirus; gene expression; gene expression system; gene frequency; gene insertion sequence; helper virus; molecular cloning; nonhuman; priority journal; transcription regulation; virus genome; virus infectivity; virus recombination; Animals; Base Sequence; Coronavirus; Gene Expression; Genetic Vectors; Humans; Molecular Sequence Data; Proteins; Coronavirus; insertion sequences; RNA viruses; unidentified insertion sequence","Afanasiev, B.N., Ward, T.W., Beaty, B.J., Carlson, J.O., Transduction of Aedes aegypti mosquitoes with vectors derived from Aedes densovirus (1999) Virology, 257, pp. 62-72; Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic Sindbis virus RNA vectors for heterologous gene expression (1998) Proc. 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Virol., 71, pp. 5148-5160; Fisher, J., Goff, S.P., Mutational analysis of stem-loops in the RNA packaging signal of the Moloney murine leukemia virus (1998) Virology, 244, pp. 133-145; Izeta, A., Sánchez, C.M., Smerdou, C., Méndez, A., Alonso, S., Balasch, M., Plana-Durán, J., Enjuanes, L., The spike protein of transmissible gastroenteritis coronavirus controls the tropism of pseudorecombinant virions engineered using synthetic minigenomes (1998) Adv. Exp. Med. Biol., 440, pp. 207-214; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Jeong, Y.S., Repass, J.F., Kim, Y.-N., Hwang, S.-M., Makino, S., Coronavirus transcription mediated by sequences flanking the transcription consensus sequence (1996) Virology, 217, pp. 311-322; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Krishnan, R., Chang, R.Y., Brian, D.A., Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the downstream-most initiation site (1996) Virology, 218, pp. 400-405; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Semin. 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Virol., 73, pp. 772-777; Li, H.-P., Zhang, X., Duncan, R., Comai, L., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9544-9549; Liao, C.L., Zhang, X., Lai, M.M.C., Coronavirus defective-interfering RNA as an expression vector: The generation of a pseudorecombinant mouse hepatitis virus expressing hemagglutinin-esterase (1995) Virology, 208, pp. 319-327; Liljeström, P., Garoff, H., A new generation of animal cell expression vectors based on the Semliki Forest virus replicon (1991) Biotechnology, 9, pp. 1356-1361; Lin, Y.J., Lai, M.M.C., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. Virol., 67, pp. 6110-6118; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus messenger RNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv. Virus Res., 53, pp. 245-264; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Molenkamp, R., Rozier, B.C.D., Greve, S., Spaan, W.J.M., Snijder, E.J., Isolation and characterization of an arterivirus defective interfering RNA genome (2000) J. Virol., 74, pp. 3156-3165; Parks, R.J., Graham, F.L., A helper-dependent system for adenovirus vector production helps define a lower limit for efficient DNA packaging (1997) J. Virol., 71, pp. 3293-3298; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durfin, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. 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Virol., 68, pp. 3656-3666; Van der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S. G. Siddell, Ed. Plenum Press, New York; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Nat. Acad. Sc. USA, 96, pp. 12056-12061; Van Marle, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J.M., Regulation of Coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M.C., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.-L., Lai, M.M.C., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Enjuanes, L.; Centro National de Biotecnologia, Department of Molecular Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"11774485","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701789
"Gonzalez J.M., Almazan F., Penzes Z., Calvo E., Enjuanes L.","57201828108;6603712040;55761804900;12801394500;7006565392;","Cloning of a transmissible gastroenteritis coronavirus full-length cDNA",2001,"Advances in Experimental Medicine and Biology","494",,,"533","536",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701637&partnerID=40&md5=bd45e98c2ed119a2bb273147efae60fd","Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Gonzalez, J.M., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Almazan, F., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Penzes, Z., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Calvo, E., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",[No abstract available],,"complementary DNA; conference paper; controlled study; Coronavirus; disease association; gastroenteritis; gene function; gene replication; genetic transcription; genome; molecular cloning; nonhuman; plasmid; priority journal; promoter region; sequence analysis; virus replication; virus transcription; Animals; Chromosomes, Artificial, Bacterial; Cloning, Molecular; DNA, Complementary; Genome, Viral; Swine; Transmissible gastroenteritis virus; Virus Assembly; Coronavirus","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; González, J.M., Almazán, F., Pénzes, Z., Calvo, E., Enjuanes, L., (2000) Construction of a stable transmissible gastroenteritis coronavirus full-length cDNA, , Submitted; Izeta, A., Smerdou, C., Alonso, S., Pénzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618","Gonzalez, J.M.; Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain",,,00652598,,AEMBA,"11774519","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701637
"Gallagher T.M.","7202310503;","Murine coronavirus spike glycoprotein: Receptor binding and membrane fusion activities",2001,"Advances in Experimental Medicine and Biology","494",,,"183","192",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701623&partnerID=40&md5=1f23d6a323735d3f133d76f9e4dbb74a","Department of Microbiology, Loyola University Medical Center, Maywood, IL 60153, United States","Gallagher, T.M., Department of Microbiology, Loyola University Medical Center, Maywood, IL 60153, United States",[No abstract available],,"spike glycoprotein; unclassified drug; virus glycoprotein; binding site; cell fusion; cell surface; conference paper; conformational transition; intracellular transport; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein assembly; protein conformation; protein protein interaction; protein transport; virus cell interaction; virus pathogenesis; virus transmission; virus virulence; Animals; Antigens, CD; Cell Adhesion Molecules; Genetic Vectors; Glycoproteins; Hela Cells; Humans; Membrane Fusion; Membrane Glycoproteins; Mice; Protein Binding; Vaccinia; Viral Envelope Proteins; Coronavirus; Murinae; Murine hepatitis virus","Alkhatib, G., Broder, C.C., Berger, E.A., Cell-type specific fusion cofactors determine human immunodeficiency virus type 1 tropism for T-cell lines versus primary macrophages (1996) J. Virol., 70, pp. 5487-5494; Beauchemin, N., Draber, P., Dveksler, G., Gold, P., Gray-Owen, S., Grunert, F., Hammarstrom, S., Thomas, P., Redefined nomenclature for members of the carcinoembryonic antigen family (1999) Exptal. Cell Research, 252, pp. 243-249; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-115. , (S. G. Siddell, ed.), Plenum Press, New York and London; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin: Isolation and biological properties of the virus (1949) J. Exp. Med., 90, pp. 181-194; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Fazakerley, J.K., Parker, S.E., Bloom, F., Buchmeier, M.J., The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system (1992) Virology, 187, pp. 178-188; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M.C., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Fuerst, T.R., Earl, P.L., Moss, B., Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes (1987) Mol. Cell. Biol., 7, pp. 2538-2544; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein (1990) J. Virol., 64, pp. 731-741; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J. Virol., 71, pp. 3129-3137; Krueger, D.K., Kelly, S.M., Lewicki, D.N., Ruffolo, R., Gallagher, T.M., The unique receptor-independent membrane fusion activity of MHV strain JHM is eliminated by mutations in disparate regions of the spike gene (2000) J. Virol., , Submitted; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus A59: Q159 is a determinant of hepatotropism (1998) J. Virol., 72, pp. 9628-9636; Nussbaum, O., Broder, C.C., Berger, E.A., Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation (1994) J. Virol., 68, pp. 5411-5422; Opstelten, D.-J.E., Raamsman, M.J.B., Wolfs, K., Horzinek, M.C., Rottier, P.J.M., Envelope glycoprotein interactions in coronavirus assembly (1995) J. Cell Biol., 131, pp. 339-349; Rao, P.V., Gallagher, T.M., Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections (1998) J. Virol., 72, pp. 3278-3288; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Vennema, H., Rottier, P.J.M., Heijnen, L., Godeke, G.J., Horzinek, M.C., Spaan, W.J.M., Biosynthesis and function of the coronavirus spike protein (1990) Adv. Expt. Med. Biol., 276, pp. 9-19","Gallagher, T.M.; Department of Microbiology, Loyola University Medical Center, Maywood, IL 60153, United States",,,00652598,,AEMBA,"11774466","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701623
"Navas S., Seo S.-H., Ming M.C., Das Sarma J., Hingley S.T., Lavi E., Weiss S.R.","7003695377;7202469910;36884051000;6602813975;6701491322;7006986911;57203567044;","Role of the spike protein in murine coronavirus induced hepatitis: An in vivo study using targeted RNA recombination",2001,"Advances in Experimental Medicine and Biology","494",,,"139","144",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701596&partnerID=40&md5=cc917e396afd9da566e0106525203c1a","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States","Navas, S., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Seo, S.-H., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Ming, M.C., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Das Sarma, J., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Hingley, S.T., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Lavi, E., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States",[No abstract available],,"spike protein; unclassified drug; virus protein; virus RNA; animal experiment; animal model; animal tissue; conference paper; controlled study; histopathology; immunohistochemistry; in vivo study; liver injury; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; RNA recombination; strain difference; virus hepatitis; virus mutant; virus pathogenesis; virus replication; virus strain; virus virulence; Animals; Coronavirus Infections; Hepatitis, Viral, Animal; Liver; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Recombination, Genetic; RNA, Viral; Viral Envelope Proteins; Virulence; Animalia; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Buchmeier, M.J., Lane, T.E., Viral-induced neurodegenerative disease (1999) Curr Opinion Microbiol, 2, pp. 398-402; Das Sarma, J., Fu, L., Tsai, J., Weiss, S.R., Lavi, E., Demyelination determinants map to the spike gene of coronavirus mouse hepatitis virus J Virol, 74, pp. 9206-9213; Ding, J.W., Ning, Q., Liu, M.F., Lai, A., Leibowitz, J., Peltekian, K.M., Cole, E.H., Levy, G.A., Fulminant hepatic failure in murine hepatitis virus strain 3 infection: Tissue-specific expression of a novel fgl2 prothrombinase (1997) J Virol, 71, pp. 9223-9230; Fleming, J.O., Trousdale, M.D., El-Zaatari, F.A.K., Stohlmam, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1989) J Virol, 58, pp. 869-875; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J Virol, 67, pp. 4504-4512; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., MHV-A59 fusion mutants are attenuated and display altered hepatotropism (1994) Virology, 200, pp. 1-10; Hingley, S.T., Gombold, J.L., Lavi, E., Weiss, S.R., Hepatitis mutants of mouse hepatitis virus strain A59 (1995) Adv Exp Med Biol, 380, pp. 577-582; Koetzner, C.A., Parker, M.M., Richard, C.S., Sturman, S., Masters, P.S., Repair and mutagenesis of the genome of a deletion mutant of the murine coronavirus mouse hepatitis virus by targeted RNA recombination (1992) J Virol, 66, pp. 1841-1848; Kuo, I., Godeke, G.J., Raamsman, J.B., Masters, P.S., Rottier, P., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J Virol, 74, pp. 1393-1406; Leparc-Goffart, I., Hingley, S.T., Chua Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associatted with a Q159L amino acid substitution in the spike protein (1997) Virology, 239, pp. 1-10; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J Virol, 72, pp. 9628-9636; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Advances Virus Research, 53, pp. 245-264; Perlman, S., Pathogenesis of coronavirus-induced infections. Review of pathological and immunological aspects (1998) Coronaviruses and Arteriviruses, , L. Enjuanes, S.G. Sidell and W. Spaan, ed. Plenum Press, New York; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterization of spike deletion variants during persistent infection (1997) J Virol, 71, pp. 2959-2969; Smith, A.L., Barthold, S.W., Methods in viral pathogenesis (1997) Viral pathogenesis, , N. Nathanson (ed.). Lippincott-Raven, Philadelphia","Navas, S.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States",,,00652598,,AEMBA,"11774458","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701596
"Yoo D., Pei Y.","7103242554;7202306693;","Full-length genomic sequence of bovine coronavirus (31kb): Completion of the open reading frame 1a/1b sequences",2001,"Advances in Experimental Medicine and Biology","494",,,"73","76",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701584&partnerID=40&md5=f09e3fc9b64fe4604828c5794d4ab4ea","Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","Yoo, D., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; Pei, Y., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada",[No abstract available],,"animal disease; cattle; conference paper; Coronavirus; diarrhea; gene sequence; hybridization; molecular cloning; nonhuman; nucleotide sequence; open reading frame; priority journal; reverse transcription polymerase chain reaction; sequence homology; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus, Bovine; DNA, Complementary; Ecthyma, Contagious; Genome, Viral; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; Sequence Analysis, DNA; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana Duran, J., Enjuanes, L., (2000) Proc. Natl. Acad. Sci. U.S.A., 97, pp. 5516-5521; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., (1994) Virology, 198, pp. 736-740; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., (1987) J. Gen. Virol, 68, pp. 57-77; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J., (1990) Nucl. Acids Res., 18, pp. 1825-1832; Herold, J., Raabe, T., Schelle Prinz, B., Siddell, S.G., (1993) Virology, 195, pp. 680-691; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhardzhyan, A., Lai, M.M.C., (1991) Virology, 180, pp. 567-582; Storz, J., Stine, L., Liem, A., Anderson, G.A., (1996) J. Am. Vet. Med. Assoc., 208, pp. 1452-1455","Yoo, D.; Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada; email: dyoo@uoguelph.ca",,,00652598,,AEMBA,"11774548","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701584
"Lim K.P., Xu H.Y., Liu D.X.","7403175857;55703819800;8972667300;","Physical interaction between the membrane (M) and envelope (E) proteins of the coronavirus avian infectious bronchitis virus (IBV)",2001,"Advances in Experimental Medicine and Biology","494",,,"595","602",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701481&partnerID=40&md5=3e2063d28ef84564008a496a97eb257b","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Lim, K.P., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore",[No abstract available],,"membrane protein; nucleocapsid protein; virus envelope protein; animal cell; Avian infectious bronchitis virus; cell strain COS7; conference paper; confocal microscopy; controlled study; immunofluorescence microscopy; nonhuman; polyacrylamide gel electrophoresis; polymerase chain reaction; priority journal; protein domain; protein protein interaction; radioimmunoprecipitation; virus particle; Animals; Cercopithecus aethiops; COS Cells; Gene Deletion; Infectious bronchitis virus; Plasmids; Polymerase Chain Reaction; Viral Envelope Proteins; Viral Matrix Proteins; Virion; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus","Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Chen, B.Y., Itakura, C., Cytopathology of chick renal epithelial cells experimentally infected with avian infectious bronchitis virus (1996) Avian Pathology, 25, pp. 675-690; Corse, E., Machamer, C.E., Infectious bronchitis virus E protein is targeted to the golgi complex and directs release of virus-like particles (2000) J. Virol., 74, pp. 4319-4326; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Furest, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesis bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad Sci. USA, 83, pp. 8122-8127; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M., Geuze, H.J., Rottier, P.J.M., Coronavirus accumulates beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Liu, D.X., Cavanagh, P.G., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3c protein with the virion envelope (1991) Virology, 185, pp. 911-917; Machamer, C.E., Mentone, S.A., Rose, J.K., Farquhar, M.G., The El glycoprotein of an avian coronavirus is targeted to the cis golgi complex (1990) Proc. Natl. Acad Sci. USA, 87 (18), pp. 6944-6948; Maeda, J., Maeda, A., Makino, S., Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells (1999) Virology, 263, pp. 265-272; Ng, L.F.P., Liu, D.X., Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site (2000) Virology, 272. , In press; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M., Opstelten, D.-J., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (2000) EMBO J., 15, pp. 2020-2028","Lim, K.P.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore",,,00652598,,AEMBA,"11774531","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701481
"Escors D., Ortego J., Enjuanes L.","6507259181;35254237800;7006565392;","The membrane M protein of the transmissible gastroenteritis coronavirus binds to the internal core through the carboxy-terminus",2001,"Advances in Experimental Medicine and Biology","494",,,"589","593",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701480&partnerID=40&md5=73bbb7205c750095b82e5c0fdd47ee32","Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain","Escors, D., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain; Ortego, J., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain; Enjuanes, L., Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain",[No abstract available],,"M protein; membrane protein; virus protein; carboxy terminal sequence; conference paper; controlled study; Coronavirus; in vitro study; nonhuman; priority journal; protein protein interaction; transmissible gastroenteritis virus; virion; virus core; virus nucleocapsid; Animals; Genome, Viral; Nucleocapsid; Transmissible gastroenteritis virus; Viral Core Proteins; Viral Matrix Proteins; Virion; Coronavirus; Transmissible gastroenteritis virus","Almazán, F., González, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana, J., Enjuanes, L., Engenearing the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) PNAS., 97, pp. 5516-5521; Escors, D., Ortego, J., Enjuanes, L., (2000) The membrane M protein carboxy-terminus interacts with transmissible gastroenteritis coronavirus core and is essential for core stability, , Submitted for publication; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Risco, C., Antón, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Risco, C., Antón, I.M., Suñé, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of the transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface fo the virion (1995) J. Virol., 69, pp. 5269-5277; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462","Escors, D.; Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autónoma, 28049 Madrid, Spain",,,00652598,,AEMBA,"11774530","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701480
"Wentworth D.E., Holmes K.V.","57203154014;7201657724;","Addition of a single glycosylation site to hAPN blocks human coronavirus-229E receptor activity",2001,"Advances in Experimental Medicine and Biology","494",,,"199","204",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701332&partnerID=40&md5=2e6e187ee9ca3f69b7ca43bce69933a3","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States","Wentworth, D.E., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States",[No abstract available],,"microsomal aminopeptidase; mutant protein; amino acid sequence; cell strain BHK; conference paper; Coronavirus; human; human cell; nonhuman; priority journal; protein glycosylation; reaction analysis; receptor blocking; receptor intrinsic activity; sequence analysis; serotype; signal transduction; virus cell interaction; virus strain; Amino Acid Substitution; Aminopeptidases; Animals; Cats; Cell Line; Coronavirus 229E, Human; Glycosylation; Humans; Receptors, Virus; Coronavirus; Human coronavirus 229E","Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) Journal of Virology, 68, pp. 5216-5224; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Advances in Experimental Medicine & Biology, 342, pp. 293-298; Hegyi, A., Kolb, A.F., Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N (1998) Journal of General Virology, 79, pp. 1387-1391; Kenny, A.J., Maroux, S., Topology of microvillar membrance hydrolases of kidney and intestine (1982) Physiological Reviews, 62, pp. 91-128. , 153 refs; Kolb, A.F., Hegyi, A., Siddell, S.G., Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N (1997) Journal of General Virology, 78, pp. 2795-2802; Lachance, C., Arbour, N., Cashman, N.R., Talbot, P.J., Involvement of aminopeptidase N (CD13) in infection of human neural cells by human coronavirus 229E (1998) Journal of Virology, 72, pp. 6511-6519; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) Journal of Clinical Investigation, 83, pp. 1299-1307; Noren, O., Sjostrom, H., Olsen, J., (1997) Cell-Surface Peptidases in Health and Disease, pp. 175-191. , (Kenney, A.J. and Boustead, C.M., Eds.) BIOS Scientific Publishers, Oxford; Riemann, D., Kehlen, A., Langner, J., CD13 - Not just a marker in leukemia typing (1999) Immunology Today, 20, pp. 83-88; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup 1 (1996) Journal of Virology, 70, pp. 8669-8674; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Wentworth, D.E.; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States",,,00652598,,AEMBA,"11774469","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701332
"Blau D.M., Holmes K.V.","15729433700;7201657724;","Human coronavirus HCoV-229E enters susceptible cells via the endocytic pathway",2001,"Advances in Experimental Medicine and Biology","494",,,"193","198",,16,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035701331&partnerID=40&md5=5b43c4e61fd6f272e84e80255a846a05","Univ. of Colorado Hlth. Sci. Center, Department of Microbiology, 4200 E 9th Avenue, Denver, CO 80262, United States","Blau, D.M., Univ. of Colorado Hlth. Sci. Center, Department of Microbiology, 4200 E 9th Avenue, Denver, CO 80262, United States; Holmes, K.V., Univ. of Colorado Hlth. Sci. Center, Department of Microbiology, 4200 E 9th Avenue, Denver, CO 80262, United States",[No abstract available],,"bafilomycin; chloroquine; nocodazole; apical membrane; basement membrane; cell strain CACO 2; conference paper; controlled study; Coronavirus; endocytosis; endosome; human; human cell; lung alveolus epithelium; nonhuman; priority journal; upper respiratory tract infection; virion; virus cell interaction; virus envelope; virus pathogenesis; virus strain; Caco-2 Cells; Cell Line; Coronavirus 229E, Human; Endocytosis; Epithelial Cells; Humans; Lung; Coronavirus","Hansen, G.H., Delmas, B., Besnardeau, L., Vogel, L.K., Laude, H., Sjostrom, H., Noren, O., The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment (1998) J. Virol., 72, pp. 527-534; Hernandez, L.D., Hoffman, L.R., Wolfsberg, T.G., White, J.M., Virus-cell and cell-cell fusion (1996) Annu. Rev. Cell Dev. Biol., 12, pp. 627-661; Gruenberg, J., Howell, K.E., Membrane traffic in endocytosis: Insights from cell-free assays (1989) Annu. Rev. Cell Biol., 5, pp. 453-481; Kooi, C., Cervin, M., Anderson, R., Differentiation of acid-pH-dependent and -nondependent entry pathways for mouse hepatitis virus (1991) Virology, 180, pp. 108-119; Lachance, C., Arbour, N., Cashman, N.R., Talbot, P.J., Involvement of aminopeptidase N (CD13) in infection of human neural cells by human coronavirus 229E (1998) J. Virol., 72, pp. 6511-6519; Lamarre, A., Talbot, P.J., Effect of pH and temperature on the infectivity of human coronavirus 229E (1989) Can. J. Microbiol., 35, pp. 972-974; Laude, H., Gelfi, J., Aynaud, J.M., In vitro properties of low- and high- passage strains of gastroenteritis coronavirus of swine (1981) Am. J. Vet. Res., 42, pp. 447-449; LeBivic, A., Quaroni, A., Nichols, B., Rodriguez-Boulan, E., Biogenic pathways of plasma membrane proteins in Caco-2, a human intestinal epithelial cell line (1990) J. Cell Biol., 111, pp. 1351-1361; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) J. Clin. Invest., 83, pp. 1299-1307; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37° C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Tooze, J., Tooze, S.A., Fuller, S.D., Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells (1987) J. Cell Biol., 105, pp. 1215-1226; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac-cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Wang, G., Deering, C., Macke, M., Shao, J., Burns, R., Blau, D.M., Holmes, K.V., McCray Jr., P.B., Human coronavirus 229E infects polarized airway epithelia from the apical surface (2000) J. Virol., , Submitted; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Blau, D.M.; Univ. of Colorado Hlth. Sci. Center, Department of Microbiology, 4200 E 9th Avenue, Denver, CO 80262, United States",,,00652598,,AEMBA,"11774468","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035701331
"Ng L.F.P., Xu H.Y., Liu D.X.","7201477950;55703819800;8972667300;","Further identification and characterization of products processed from the coronavirus avian infectious bronchitis virus (IBV) 1a polyprotein by the 3C-like proteinase",2001,"Advances in Experimental Medicine and Biology","494",,,"291","298",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699445&partnerID=40&md5=589e5831c1591aba10d0f70710438582","Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore","Ng, L.F.P., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Xu, H.Y., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore; Liu, D.X., Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore",[No abstract available],,"3c like proteinase; protein orf1a; proteinase; unclassified drug; virus protein; animal cell; Avian infectious bronchitis virus; cell strain COS7; cellular distribution; conference paper; controlled study; nonhuman; priority journal; protein analysis; protein degradation; protein domain; protein localization; protein processing; Vero cell; virus infection; Animals; Cercopithecus aethiops; COS Cells; Cysteine Endopeptidases; Infectious bronchitis virus; Vero Cells; Viral Proteins; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus","Bost, A.G., Carnahan, R., Lu, X.T., Denison, M.R., Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly (2000) J. Virol., 74, pp. 3379-3387; Lim, K.P., Ng, L.F.P., Liu, D.X., Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by ORF1a of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products (2000) J. Virol., 74, pp. 1674-1685; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF1a products (1994) J. Virol., 68, pp. 5772-5780; Liu, D.X., Xu, H.Y., Brown, T.D.K., Proteolytic processing of the coronavirus infectious bronchitis virus 1a polyprotein: Identification of a 10-kilodalton polypeptide and determination of its cleavage sites (1997) J. Virol., 71, pp. 1814-1820; Liu, D.X., Shen, S., Xu, H.Y., Wang, S.F., Proteolytic mapping of the coronavirus infectious bronchitis virus 1b polyprotein: Evidence for the presence of four cleavage sites of the 3C-like proteinase and identification of two novel cleavage products (1998) Virology, 246, pp. 288-297; Ng, L.F.P., Liu, D.X., Identification of a 24-kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites (1998) Virology, 243, pp. 388-395; Ng, L.F.P., Liu, D.X., Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site (2000) Virology, 272. , in press; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185","Ng, L.F.P.; Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, Singapore 117604, Singapore",,,00652598,,AEMBA,"11774483","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699445
"Chouljenko V.N., Foster T.P., Lin X., Storz J., Kousoulas K.G.","6603655227;57212401085;36768282000;7006694594;7003476092;","Elucidation of the genomic nucleotide sequence of bovine coronavirus and analysis of cryptic leader mRNA fusion sites",2001,"Advances in Experimental Medicine and Biology","494",,,"49","55",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699443&partnerID=40&md5=dff78fb83f5a4f4b8b699173592bf3a9","Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States","Chouljenko, V.N., Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Foster, T.P., Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Lin, X., Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Storz, J., Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States; Kousoulas, K.G., Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",[No abstract available],,"messenger RNA; signal peptide; cattle; computer prediction; conference paper; Coronavirus; gene fusion; gene sequence; molecular cloning; nonhuman; nucleotide sequence; priority journal; protein secondary structure; RNA virus; virus morphology; 5' Untranslated Regions; Animals; Base Sequence; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Genome, Viral; Intestines; Lung; Molecular Sequence Data; RNA, Messenger; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; RNA viruses","Chouljenko, V.N., Kousoulas, K.G., (2000) Cryptic leader-mRNA fusion sites within the bovine coronavirus S and 12.7 kDa coding sequences, , Submitted; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1977) J. Virol., 71, pp. 5148-5160; Storz, J., Purdy, C.W., Lin, X., Burrell, M., Truax, R.E., Briggs, R.E., Frank, G.H., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp from cattle involved in two natural outbreaks of shipping fever J. Am. Vet. Med. Assoc., 216, pp. 1601-1606; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swap samples in cattle with signs of respiratory tract disease after shipping (1996) J. Am. Vet. Med. Assoc., 208, pp. 1452-1455; Zhang, X.M., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S-Genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404; Matzura, O., Wennborg, A., RNAdraw: An integrated program for RNA secondary structure calculation and analysis under 32-bit microsoft windows (1996) Comp. Applic. Bioscie. (CABIOS), 12, pp. 247-249","Chouljenko, V.N.; Dept. of Veterinary Microbiology, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, United States",,,00652598,,AEMBA,"11774512","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699443
"Zhang X., Lyle C., Wang Y., Zeng L.","55715175900;57197984463;7601495525;55106640600;","Role of hnRNP A1 in coronavirus RNA synthesis",2001,"Advances in Experimental Medicine and Biology","494",,,"437","446",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699351&partnerID=40&md5=79970fe396fa88e6a0d12f534bc0d60a","Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States","Zhang, X., Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Lyle, C., Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Wang, Y., Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Zeng, L., Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States",[No abstract available],,"heterogeneous nuclear ribonucleoprotein; mutant protein; small nuclear RNA; virus protein; virus RNA; animal cell; conference paper; controlled study; Coronavirus; Human immunodeficiency virus; in vitro study; mouse; Murine hepatitis coronavirus; nonhuman; open reading frame; plasmid; priority journal; regulatory mechanism; RNA synthesis; sequence analysis; site directed mutagenesis; Animals; Astrocytoma; DNA, Complementary; Heterogeneous-Nuclear Ribonucleoprotein Group A-B; Heterogeneous-Nuclear Ribonucleoproteins; Mice; Murine hepatitis virus; Mutation; Plasmids; Recombination, Genetic; Ribonucleoproteins; RNA, Viral; Transfection; Tumor Cells, Cultured; Vaccinia virus; Virus Replication; Animalia; Coronavirus; Human immunodeficiency virus; Murinae; Murine hepatitis virus; RNA viruses","Black, A.C., Luo, J., Chun, S., Baker, A., Faser, J.K., Rosenblatt, J.D., Specific binding of polypyrimidine tract binding protein and hnRNP A1 to HIV-1 CRS elements (1996) Virus Genes, 12, pp. 275-285; Black, A.C., Luo, J., Watanabe, C., Chun, S., Baker, A., Faser, J.K., Morgan, J.P., Rosenblatt, J.D., Polypyrimidine tract-binding protein and heterogeneous nuclear ribonucleoprotein A1 bind to human T-cell leukemia virus type 2 RNA regulatory elements (1995) J. Virol., 69, pp. 6852-6858; Buvoli, M., Biamonti, G., Tsoulfas, P., Bassi, M.T., Ghetti, A., Riva, S., Morandi, C., cDNA cloning of human hnRNP protein A1 reveals the existence of multiple mRNA isoforms (1988) Nucl. Acids Res., 16, pp. 3751-3770; Buvoli, M., Cobianchi, F., Riva, S., Interaction of hnRNP A1 with snRNPs and pre-mRNAs: Evidence for a possible role of A1 RNA annealing activity in the first steps of spliceosome assembly (1992) Nucl. Acids Res., 20, pp. 5017-5025; Caputi, M., Mayeda, A., Krainer, A.R., Zahler, A.M., HnRNPA/B proteins are required for inhibition of HIV-1 pre-mRNA splicing (1999) EMBO J., 18, pp. 4060-4067; Cartegni, L., Maconi, M., Morandi, E., Cobianchi, F., Riva, S., Biamonti, G., hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins (1996) J. Mol. Biol., 259, pp. 337-348; Dreyfuss, G., Matunis, M.J., Pinol-Roma, S., Burd, C.G., hnRNP proteins and the biogenesis of mRNA (1993) Annu. Rev. Biochem., 62, pp. 289-321; Furuya, T., Lai, M.M.C., Three different cellular proteins bind to the complementary sites on the 5′-end positive- and 3′-end negative-strands of mouse hepatitis virus RNA (1993) J. Virol., 67, pp. 7215-7222; Hirano, N., Fujiwara, K., Hino, S., Matsumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Li, H.P., Zhang, X.M., Duncan, R., Comai, L., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 9544-9549; Li, H.P., Huang, P., Park, S., Lai, M.M.C., Polypyrimidine tract-binding protein binds to the leader RNA of mouse hepatitis virus and serves as a regulator of viral transcription (1999) J. Virol., 73, pp. 772-777; Liao, C.L., Lai, M.M.C., Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription (1994) J. Virol., 68, pp. 4727-4737; Makino, S., Lai, M.M.C., Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro (1989) Virology, 169, pp. 227-232; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3′-end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69, pp. 2016-2023; Zhang, X.M., Liao, C.L., Lai, M.M.C., Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription both in trans and in cis (1994) J. Virol., 68, pp. 4738-4746; Zhang, X.M., Lai, M.M.C., Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of murine hepatitis virus RNAs: Correlation with the amounts of subgenomic mRNA transcribed (1995) J. Virol., 69, pp. 1637-1644; Zhang, X.M., Li, H.P., Xue, W., Lai, M.M.C., Formation of a ribonucleoprotein complex of mouse hepatitis virus involving heterogeneous nuclear ribonucleoprotein A1 and transcription-regulatory elements of viral RNA (1999) Virology, 264, pp. 115-124","Zhang, X.; Department of Microbiology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States",,,00652598,,AEMBA,"11774505","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699351
"Banerjee S., An S., Makino S.","55851941932;55107136200;7403067550;","Specific cleavage of 28S ribosomal RNA in murine coronavirus-infected cells",2001,"Advances in Experimental Medicine and Biology","494",,,"621","626",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699201&partnerID=40&md5=5ce680c7973df6ed1f30ef36b2011f36","Department of Microbiology, Inst. of Cell. and Molecular Biology, University of Texas, Austin, TX 78712, United States","Banerjee, S., Department of Microbiology, Inst. of Cell. and Molecular Biology, University of Texas, Austin, TX 78712, United States; An, S., Department of Microbiology, Inst. of Cell. and Molecular Biology, University of Texas, Austin, TX 78712, United States; Makino, S., Department of Microbiology, Inst. of Cell. and Molecular Biology, University of Texas, Austin, TX 78712, United States",[No abstract available],,"ribosome RNA; RNA 28S; RNA polymerase; animal cell; apoptosis; conference paper; Coronavirus; mouse; nonhuman; open reading frame; priority journal; protein binding; protein synthesis inhibition; RNA cleavage; strain difference; virus envelope; virus genome; virus infection; virus particle; virus strain; Animals; Cell Line; Mice; Murine hepatitis virus; RNA, Ribosomal, 28S; Virus Replication; Animalia; Coronavirus; Murinae; Murine hepatitis virus","An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.-S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Epression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Hilton, A., Mizzen, L., Macintyre, G., Cheley, S., Anderson, R., Translational control in murine hepatitis virus infection (1986) J. Gen. Virol., 67, pp. 923-932; Kim, K.-H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J. Virol., 71, pp. 3922-3931; Kyuwa, S., Cohen, M., Nelson, G.W., Tahara, S.M., Stohlman, S.A., Modulation of cellular macromolecular synthesis by coronavirus: Implications for pathogenesis (1994) J. Virol., 68, pp. 6815-6819; Lai, M.M.C., Brayton, P.R., Armen, R.C., Patton, C.D., Pugh, C., Stohlman, S.A., Mouse hepatitis virus A59: mRNA structure and genetic localisation of the sequence divergence from hepatotropic strain MHV-3 (1981) J. Virol., 39, pp. 823-834; Lee, H.-J., Shieh, C.-K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Sawicki, S.G., Sawicki, D.L., Coronavirus minus-strand RNA synthesis and effect of cyclohexamide on coronavirus RNA synthesis (1986) J. Virol., 57, pp. 328-334; Siddell, S., Wege, H., Barthel, A., Ter Meulen, V., Coronavirus JHM: Intracellular protein synthesis (1981) J. Gen. Virol., 53, pp. 145-155; Tahara, S.M., Dietlin, T.A., Bergmann, C.C., Nelson, G.W., Kyuwa, S., Anthony, R.P., Stohlman, S.A., Coronavirus translation regulation: Lader affects mRNA efficiency (1994) Virology, 202, pp. 621-630; Tahara, S.M., Dietlin, T.A., Nelson, G.W., Stohlman, S.A., Manno, D.J., Mouse hepatitis virus nucleocapsid protein as a translational effector of viral mRNAs (1998) Adv. Exp. Med. Biol., 440, pp. 313-318","Banerjee, S.; Department of Microbiology, Inst. of Cell. and Molecular Biology, University of Texas, Austin, TX 78712, United States",,,00652598,,AEMBA,"11774535","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699201
"Sola I., Alonso S., Sanchez C., Sanchez-Morgado J.M., Enjuanes L.","7003336781;57210695335;57193985365;6602349176;7006565392;","Expression of transcriptional units using transmissible gastroenteritis coronavirus derived minigenomes and full-length cDNA clones",2001,"Advances in Experimental Medicine and Biology","494",,,"447","451",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035699198&partnerID=40&md5=df6798c1e34a128fa9755666b35abcfd","Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain","Sola, I., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain; Alonso, S., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain; Sanchez, C., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain; Sanchez-Morgado, J.M., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain",[No abstract available],,"complementary DNA; virus vector; amino acid sequence; conference paper; Coronavirus; gene expression system; molecular cloning; nonhuman; priority journal; protein secondary structure; RNA structure; sequence analysis; transcription regulation; Transmissible gastroenteritis virus; virus genome; virus recombination; Animals; Cloning, Molecular; DNA, Complementary; Genetic Vectors; Genome, Viral; Humans; Regulatory Sequences, Nucleic Acid; Swine; Transcription, Genetic; Transmissible gastroenteritis virus; Coronavirus; Transmissible gastroenteritis virus","Almazan, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Alonso, S., Izeta, A., Sola, I., Enjuanes, L., (2000) Transcription regulatory sequences in transmissible gastroenteritis coronavirus, , Submitted; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteritis coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Sola, I., Alonso, S., Plana-Durán, J., Enjuanes, L., Heterologous gene expression with a single genome derived from transmissible gastroenteritis coronavirus (2000) J. Virol., , Submitted for publication","Sola, I.; Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, 28049 Madrid, Spain",,,00652598,,AEMBA,"11774506","English","Adv. Exp. Med. Biol.",Conference Paper,"Final",,Scopus,2-s2.0-0035699198
[No author name available],[No author id available],"Proceedings of the VIII International Symposium on Nidoviruses (Coronaviruses and Arteriviruses). May 20-25, 2000. Lake Harmony, Pennsylvania, USA.",2001,"Advances in Experimental Medicine and Biology","494",,,"1","728",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035553304&partnerID=40&md5=88b32a665abda2ef35f15b35c1bddd8a",,"",[No abstract available],,"animal; Arterivirus; conference paper; Coronavirus; human; virus infection; Animals; Arterivirus; Arterivirus Infections; Coronavirus; Coronavirus Infections; Humans",,,,,00652598,,,"12120585","English","Adv Exp Med Biol",Conference Paper,"Final",,Scopus,2-s2.0-0035553304
"Ferenc B., Vilmos P., Károly V., László P., Ferenc F.","6602166136;7003472044;7005765931;7004477363;35616337400;","Canine corona and rotavirus enteritis. Literature review [A kutyák corona- és rotavirus okozta bélgyulladása: Irodalmi áttekintés]",2001,"Magyar Allatorvosok Lapja","123","4",,"209","212",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346451645&partnerID=40&md5=8f25118bc0af17591738249b50008637","SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary; Orszagos Allat-egeszsegugyi Intezet, Tábornok u. 2, H-1149 Budapest, Hungary","Ferenc, B., SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary; Vilmos, P., Orszagos Allat-egeszsegugyi Intezet, Tábornok u. 2, H-1149 Budapest, Hungary; Károly, V., SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary; László, P., SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary; Ferenc, F., SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary","The latest literature data concerning canine corona and rotavirus enteritis are summarised. Canine coronavirus was first isolated from feces of military dogs In 1971. CCV is fairly widespread throughout the canine population with up to 80% of adult dogs having serologic evidence of exposure. Dogs are infected via fecal-oral route. CCV is highly contagious and spreads rapidly through groups of susceptible dogs. Neonatal pups are more severely affected than those of weaning age and adult dogs. Inapparent infection often occures. The incubation period for CCV following oral infection ranges from 1-4 days. CCV attacks the mature epithelial cells on the tip of intestinal villi resulting In villous atrophy and fusion. Dogs can have CCV and canine parvovirus simultaneously, CCV infection makes CPV infection more severe. Infected dogs usually have mild to moderate diarrhea, which is very malodorous, orange in color, and sometimes contains blood. Morbidity and mortality are low. The detection of CCV In fresh feces can be done by EM, ELISA and PCR. Serum ELISA test for CCV antibody has also been developed. Treatment is only supportive, and aims primarily at the correction of dehydration secondary to diarrhea. Broad-spectrum antimicrobial agents can be given to treat secondary bacterial infections. The principles of therapy are the same as in the case of parvoenteritis. Inactivated and MLV vaccines are available for protection against CCV infection. CCV is a major factor in enhancing CPV pathogenicity, vaccinating dogs against CCV would be important not only to protect them from CCV infection but from dual infection as well. Canine rotavirus enteritis was first described in 1980. CRV is widespread throughout the canine population, most adult dogs have serologic evidence of exposure. Clinical disease has been reported primarily in puppies less than 6 weeks of age. Most natural infections are apparently either subclinical or cause only mild diarrhea, anorexia and lethargy. Diagnosis is based on an increase in serum rotavirus antibody titers in paired samples, or by identification of the virus through EM or by an ELISA system on the feces. Supportive care is the only treatment necessary. No vaccine is currently available against canine rotavirus.",,,"Appel, M., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet. Med., 83, pp. 360-366; Binn, L.N., Lazar, E.C., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc. 78th Ann. Meeting, pp. 356-366. , U.S. Anim. Health Assoc; Bíró, F., Pálfi, V., Vörös, K., Papp, L., Újabb tapasztalatok a kutyák parvovirus okozta bélgyulladásának járványtanában, klinikumában és diagnosztikájában (1999) Magy. Állatorv. Lapja, 121, pp. 248-252; Bíró, F., Vörös, K., Papp, L., Felkai, F., Újabb tapasztalatok a kutyák parvovirus okozta bélgyulladásának gyógykezelésében (1999) Magy. Állatorv. Lapja, 121, pp. 725-732; England, J.J., Poston, R.P., Electron microscopic identification and subsequent isolation of a rotavirus from a dog with fatal neonatal diarrhea (1980) Am. J. Vet. Res., 41, pp. 782-783; Fulton, R.W., Johnson, C.A., Isolation of a rotavirus from a newborn dog with diarrhea (1981) Am. J. Vet. Res., 42, pp. 841-843; Greene, C., Immunoprophylaxis and immunotherapy (1998) Infectious Diseases of the Dog and Cat, pp. 717-750. , GREENE, C.: W.B. Saunders Co. Philadelphia; Ham, C., Maes, R., An RT-PCR assay to detect canine coronavirus and porcine transmissible gastroenteritis infections (1996) Proc. Am. Assoc. Vet. Lab. Diagnoses, , Little Rock, AR; Hamond, M.M., Timoney, P.J., An electron microscopic study of viruses associated with canine gastroenteritis (1983) Cornell Vet., 73, pp. 82-97; Hoskins, J.D., Canine viral enteritis (1998) Infectious Diseases of the Dog and Cat, pp. 40-49. , GREENE, C.: W.B. Saunders Co. Philadelphia; Johnson, C.A., Snider, T.G., Gross and light microscopic lesions in neonatal gnotobiotic dogs inoculated with a canine rotavirus (1983) Am. J. Vet. Res., 44, pp. 1687-1693; Jubb, K.V.F., Kennedy, P.C., Palmer, N., (1985) Pathology of Domestic Animals (3. Ed.), 2, pp. 120-122. , Academic Press, Inc. London; Keenan, K.P., Helen, R.J., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical, and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Mcnulty, M.S., Allan, G.M., Antibody to rotavirus in dogs and cats (1978) Vet. Rec., 102, pp. 534-535; Rimmelzwaan, G.F., Groen, J., The use of enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in the Netherlands (1991) Vet. Microbiol., 26, pp. 25-40; Tennant, B.J., Gaskell, R.M., Studies on the epizootiology of canine coronavirus (1993) Vet. Rec., 132, pp. 7-11; Tuboly, S., (1998) Állatorvosi Járványtan I. Mezogazda Kiadó, , Budapest; Tuchiya, K., Horimoto, T., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet. Microbiol., 26, pp. 41-51; Tzipori, S., Makin, T., Propagation of human rotavirus in young dogs (1978) Vet. Microbiol., 3, pp. 55-63","Ferenc, B.; SZIE-ÁOTK, Belgyogyaszati Tanszek es Klinika, István u. 2, H-1078 Budapest, Hungary",,,0025004X,,,,"Hungarian","Magyar Allatorv. Lapja",Review,"Final",,Scopus,2-s2.0-0346451645
"Casais R., Thiel V., Siddell S.G., Cavanagh D., Britton P.","6602185676;35238592100;7005260816;26642890500;57203302770;","Reverse genetics system for the avian coronavirus infectious bronchitis virus",2001,"Journal of Virology","75","24",,"12359","12369",,163,"10.1128/JVI.75.24.12359-12369.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035194291&doi=10.1128%2fJVI.75.24.12359-12369.2001&partnerID=40&md5=51913fe1f75d6d273c891ed83f9fa5ca","Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","Casais, R., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Thiel, V., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Siddell, S.G., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","Major advances in the study of the molecular biology of RNA viruses have resulted from the ability to generate and manipulate full-length genomic cDNAs of the viral genomes with the subsequent synthesis of infectious RNA for the generation of recombinant viruses. Coronaviruses have the largest RNA virus genomes and, together with genetic instability of some cDNA sequences in Escherichia coli, this has hampered the generation of a reverse-genetics system for this group of viruses. In this report, we describe the assembly of a full-length cDNA from the positive-sense genomic RNA of the avian coronavirus, infectious bronchitis virus (IBV), an important poultry pathogen. The IBV genomic cDNA was assembled immediately downstream of a T7 RNA polymerase promoter by in vitro ligation and cloned directly into the vaccinia virus genome. Infectious IBV RNA was generated in situ after the transfection of restricted recombinant vaccinia virus DNA into primary chick kidney cells previously infected with a recombinant fowlpox virus expressing T7 RNA polymerase. Recombinant IBV, containing two marker mutations, was recovered from the transfected cells. These results describe a reverse-genetics system for studying the molecular biology of IBV and establish a paradigm for generating genetically defined vaccines for IBV.",,"complementary DNA; RNA polymerase; animal cell; article; Avian infectious bronchitis virus; chicken; controlled study; DNA sequence; embryo; Escherichia coli; Fowlpox virus; gene mutation; genetic stability; nonhuman; nucleotide sequence; priority journal; promoter region; RNA synthesis; Vaccinia virus; viral genetics; virus assembly; virus genome; virus recombinant; Animals; Chick Embryo; Cloning, Molecular; DNA, Complementary; Infectious bronchitis virus; RNA, Viral; Vaccinia virus; Virus Assembly","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Alonso Caplen, F.V., Matsuoka, Y., Wilcox, G.E., Compans, R.W., Replication and morphogenesis of avian coronavirus in Vero cells and their inhibition by monensin (1984) Virus Res., 1, pp. 153-167; Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1987) Current protocols in molecular biology, , John Wiley & Sons, Inc., New York, N.Y; Baric, R.S., Stohlman, S.A., Lai, M.M.C., Characterization of replicative intermediate RNA of mouse hepatitis virus: Presence of leader RNA sequences on nascent chains (1983) J. Virol., 48, pp. 633-640; Bonfield, J.K., Smith, K.F., Staden, R., A new DNA sequence assembly program (1995) Nucleic Acids Res., 23, pp. 4992-4999; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Britton, P., Green, P., Kottier, S., Mawditt, K.L., Pénzes, Z., Cavanagh, D., Skinner, M.A., Expression of bacteriophage T7 RNA polymerase in avian and mammalian cells by a recombinant fowlpox virus (1996) J. Gen. Virol., 77, pp. 963-967; Cavanagh, D., A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathol., 30, pp. 109-115; Cavanagh, D., Davis, P.J., Pappin, D.J.C., Binns, M.M., Boursnell, M.E.G., Brown, T.D.K., Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41 (1986) Virus Res., 4, pp. 133-143; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of poultry, 10th ed., pp. 511-526. , B. W. Calnek, H. J. Barnes, C. W. Beard, W. M. Reid, and H. W. Yoda (ed.). Iowa State University Press, Ames, Iowa; Dalton, K., Casais, R., Shaw, K., Stirrups, K., Evans, S., Britton, P., Brown, T.D., Cavanagh, D., cis-Acting sequences required for coronavirus infectious bronchitis virus defective-RNA replication and packaging (2001) J. Virol., 75, pp. 125-133; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organisation of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Evans, S., Cavanagh, D., Britton, P., Utilizing fowlpox virus recombinants to generate defective RNAs of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81, pp. 2855-2865; Hiscox, J.A., Wurm, T., Wilson, L., Britton, P., Cavanagh, D., Brooks, G., The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus (2001) J. Virol., 75, pp. 506-512; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lambrechts, C., Pensaert, M., Ducatelle, R., Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus (1993) Avian Pathol., 22, pp. 577-590; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D.K., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J. Virol., 68, pp. 5772-5780; Mackett, M., Smith, G.L., Moss, B., The construction and characterisation of vaccinia virus recombinants expressing foreign genes (1985) DNA cloning: A practical approach, vol. 2, 2, pp. 191-211. , D. M Glover (ed.). IRL Press, Oxford, England; Mayr, A., Malicki, K., Attenuation of virulent fowlpox virus in tissue culture and characteristics of the attenuated strain (1966) Zentbl. Veterinarmedzin., 13, pp. 1-13; Merchlinsky, M., Moss, B., Introduction of foreign DNA into the vaccinia virus genome by in vitro ligation: Recombination-independent selectable cloning vectors (1992) Virology, 190, pp. 522-526; Mockett, A.P.A., Envelope proteins of avian infectious bronchitis virus: Purification and biological properties (1985) J. Virol. Methods, 12, pp. 271-278; Molenkamp, R., Van Tol, H., Rozier, B.C., Van Der Meer, Y., Spaan, W.J., Snijder, E.J., The arterivirus replicase is the only viral protein required for genome replication and subgenomic mRNA transcription (2000) J. Gen. Virol., 81, pp. 2491-2496; Pénzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D.K., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Pénzes, Z., Wroe, C., Brown, T.D., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Polo, S., Ketner, G., Levis, R., Falgout, B., Infectious RNA transcripts from full-length dengue virus type 2 cDNA clones made in yeast (1997) J. Virol., 71, pp. 5366-5374; Racaniello, V.R., Baltimore, D., Cloned poliovirus complementary DNA is infectious in mammalian cells (1981) Science, 214, pp. 916-919; Rice, C.M., Grakoui, A., Galler, R., Chambers, T.J., Transcription of infectious yellow lever RNA from full-length cDNA templates produced by in vitro ligation (1989) New Biol., 1, pp. 285-296; Ruggli, N., Tratschin, J.D., Mittelholzer, C., Hofmann, M.A., Nucleotide sequence of classical swine fever virus strain Alfort/187 and transcription of infectious RNA from stably cloned full-length cDNA (1996) J. Virol., 70, pp. 3478-3487; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning: A laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory, New York, N.Y; Satyanarayana, T., Bar-Joseph, M., Mawassi, M., Albiach-Marti, M.R., Ayllon, M.A., Gowda, S., Hilf, M.E., Dawson, W.O., Amplification of Citrus tristeza virus from a cDNA clone and infection of citrus trees (2001) Virology, 280, pp. 87-96; Satyanarayana, T., Gowda, S., Boyko, V.P., Albiach-Marti, M.R., Mawassi, M., Navas-Castillo, J., Karasev, A.V., Dawson, W.O., An engineered closterovirus RNA replicon and analysis of heterologous terminal sequences for replication (1999) Proc. Natl. Acad. Sri. USA, 96, pp. 7433-7438; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-219; Siddell, S.G., The Coronaviridae (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.). Plenum Publishing, Inc., New York, N.Y; Spaan, W.J.H., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A.M., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO. J., 2, pp. 1839-1844; Stern, D.F., Kennedy, S.I.T., Coronavirus multiplication strategy. I. Identification and characterization of virus-specific RNA (1980) J. Virol., 34, pp. 665-674; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Casais, R., Cavanagh, D., Britton, P., Expression of reporter genes from the defective RNA CD-61 of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81, pp. 1687-1698; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Cavanagh, D., Britton, P., Leader switching occurs during the rescue of defective RNAs by heterologous strains of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81, pp. 791-801; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Viral replicase gene products suffice for coronavirus discontinuous transcription (2001) J. Virol., 75, pp. 6676-6681; Tibbles, K.W., Cavanagh, D., Brown, T.D., Activity of a purified His-tagged 3C-like proteinase from the coronavirus infectious bronchitis virus (1999) Virus Res., 60, pp. 137-145; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Wang, K., Boysen, C., Shizuya, H., Simon, M.I., Hood, L., Complete nucleotide sequence of two generations of a bacterial artificial chromosome cloning vector (1997) BioTechniques, 23, pp. 992-994; Yamshchikov, V., Mishin, V., Cominelli, F., A new strategy in design of (+)RNA virus infectious clones enabling their stable propagation in E. coli (2001) Virology, 281, pp. 272-280; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; email: paul.britton@bbsrc.ac.uk",,,0022538X,,JOVIA,"11711626","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035194291
"Escors D., Camafeita E., Ortego J., Laude H., Enjuanes L.","6507259181;6602578497;35254237800;7006652624;7006565392;","Organization of two transmissible gastroenteritis coronavirus membrane protein topologies within the virion and core",2001,"Journal of Virology","75","24",,"12228","12240",,46,"10.1128/JVI.75.24.12228-12240.2001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035202436&doi=10.1128%2fJVI.75.24.12228-12240.2001&partnerID=40&md5=42dbc4f5f856e8e7d6dc4990dafc5f1d","Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Escors, D., Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Camafeita, E., Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Ortego, J., Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Laude, H., Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The difference in membrane (M) protein compositions between the transmissible gastroenteritis coronavirus (TGEV) virion and the core has been studied. The TGEV M protein adopts two topologies in the virus envelope, a Nexo-Cendo topology (with the amino terminus exposed to the virus surface and the carboxy terminus inside the virus particle) and a Nexo-Cexo topology (with both the amino and carboxy termini exposed to the virion surface). The existence of a population of M molecules adopting a Nexo-Cexo topology in the virion envelope was demonstrated by (i) immunopurification of 35S-labeled TGEV virions using monoclonal antibodies (MAbs) specific for the M protein carboxy terminus (this immunopurification was inhibited only by deletion mutant M proteins that maintained an intact carboxy terminus), (ii) direct binding of M-specific MAbs to the virus surface, and (iii) mass spectrometry analysis of peptides released from trypsin-treated virions. Two-thirds of the total number of M protein molecules found in the virion were associated with the cores, and one-third was lost during core purification. MAbs specific for the M protein carboxy terminus were bound to native virions through the M protein in a Nexo-Cexo conformation, and these molecules were removed when the virus envelope was disrupted with NP-40 during virus core purification. All of the M protein was susceptible to N-glycosidase F treatment of the native virions, which indicates that all the M protein molecules are exposed to the virus surface. Cores purified from glycosidase-treated virions included M protein molecules that completely or partially lost the carbohydrate moiety, which strongly suggests that the M protein found in the cores was also exposed in the virus envelope and was not present exclusively in the virus interior. A TGEV virion structure integrating all the data is proposed. According to this working model, the TGEV virion consists of an internal core, made of the nucleocapsid and the carboxy terminus of the M protein, and the envelope, containing the spike (S) protein, the envelope (E) protein, and the M protein in two conformations. The two-thirds of the molecules that are in a Nexo-Cendo conformation (with their carboxy termini embedded within the virus core) interact with the internal core, and the remaining third of the molecules, whose carboxy termini are in a Nexo-Cexo conformation, are lost during virus core purification.",,"carbohydrate; envelope protein; glycosidase; membrane protein; monoclonal antibody; spike protein; sulfur 35; trypsin; unclassified drug; virus protein; amino terminal sequence; animal cell; antigen binding; article; carboxy terminal sequence; controlled study; Coronavirus; deletion mutant; mass spectrometry; nonhuman; priority journal; protein conformation; protein degradation; protein localization; protein purification; virion; virus core; virus envelope; virus nucleocapsid; virus particle; Amino Acid Sequence; Animals; Glycoside Hydrolases; Male; Molecular Sequence Data; Swine; Transmissible gastroenteritis virus; Viral Matrix Proteins; Virion","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. 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Virol., 71, pp. 271-279; Delmas, B., Gelfi, J.R., L'Haridon, Vogel, L.K., Norén, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus taxonomy. Classification and nomenclature of viruses, pp. 835-849. , M. H. V. Van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M. Lemon, D. J. McGeoch, J. Maniloff, M. A. Mayo, C. R. Pringle, and R. B. Wickner (ed.). Academic Press, New York, N.Y; Escors, D., Ortego, J., Laude, H., Enjuanes, L., The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability (2001) J. 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Virol., 71, pp. 1107-1114; Houthaeve, T., Gausepohl, H., Mann, M., Ashman, K., Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins (1995) FEBS Lett., 376, pp. 91-94; Jiménez, G., Correa, I., Melgosa, M.P., Bullido, M.J., Enjuanes, L., Critical epitopes in transmissible gastroenteritis virus neutralization (1986) J. Virol., 60, pp. 131-139; Laude, H., Chapsal, J.M., Gelfi, J., Labiau, S., Grosclaude, J., Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins (1986) J. Gen. Virol., 67, pp. 119-130; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 743-749; Laude, H., Vanreeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Vet. Res., 24, pp. 125-150; Martín-Andrés, A., Luna-Castillo, J.D., (1994) Bioestadistica para las ciencias de la salud, 4th ed., , Ediciones Norma, S.A., Madrid, Spain; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Med. Vet. Sci., 30, pp. 190-198; Motulsky, H., (1995) Intuitive biostatistics, pp. 225-229. , Oxford University Press, New York, N.Y; Narayanan, K., Maeda, A., Maeda, J., Makino, S., Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells (2000) J. Virol., 74, pp. 8127-8134; Nishiyama, K., Suzuki, T., Tokuda, H., Inversion of the membrane topology of secG coupled with secA-dependent preprotein translocation (1996) Cell, 85, pp. 71-81; Penzes, Z., González, J.M., Calvo, E., Izeta, A., Smerdou, C., Mendez, A., Sánchez, C.M., Enjuanes, L., Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the Purdue virus cluster (2001) Virus Genes, 23, pp. 105-118; Poisson, F., Severac, A., Hourioux, C., Goudeau, A., Roingeard, P., Both pre-S1 and S domains of hepatitis B virus envelope proteins interact with the core particle (1997) Virology, 228, pp. 115-120; Prange, R., Streeck, R.E., Novel transmembrane topology of the hepatitis B virus envelope proteins (1995) EMBO J., 14, pp. 247-256; Raamsman, M.J.B., Locker, J.K., de Hooge, A., de Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Risco, C., Antón, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J. Virol., 70, pp. 4773-4777; Risco, C., Antón, I.M., Suñé, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Schevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels (1996) Anal. 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Academic Press, San Diego, Calif","Enjuanes, L.; Department of Molecular Biology, Centro Nacional de Biotechnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam",,,0022538X,,JOVIA,"11711614","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0035202436
"De Haan C.A.M., De Wit M., Kuo L., Montalto C., Masters P.S., Weiss S.R., Rottier P.J.M.","7003682643;7102191667;7101601942;57215272490;7006234572;57203567044;7006145490;","O-Glycosylation of the mouse hepatitis coronavirus membrane protein",2001,"Virus Research","82","1-2",,"77","81",,12,"10.1016/S0168-1702(01)00390-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037196588&doi=10.1016%2fS0168-1702%2801%2900390-2&partnerID=40&md5=b1e0f64d79da12f20d69029c6039ebb8","Department of Infectious Diseases and Immunology, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States","De Haan, C.A.M., Department of Infectious Diseases and Immunology, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Wit, M., Department of Infectious Diseases and Immunology, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Kuo, L., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Montalto, C., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Masters, P.S., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Weiss, S.R., Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Rottier, P.J.M., Department of Infectious Diseases and Immunology, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands",[No abstract available],,"alanine; alpha interferon; amino acid derivative; carbohydrate derivative; envelope protein; galactose; genomic RNA; hydroxyl group; M protein; membrane protein; methionine; mutant protein; n acetylgalactosamine; oligosaccharide; polypeptide; proline; serine; sialic acid; threonine; transferase; virus receptor; virus RNA; vitronectin; amino acid sequence; amino acid substitution; amino terminal sequence; Avian infectious bronchitis virus; binding site; carbohydrate analysis; carboxy terminal sequence; electrophoretic mobility; enzyme analysis; enzyme substrate; genotype phenotype correlation; glycosylation; Golgi complex; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; protein function; protein induction; protein localization; protein motif; receptor binding; short survey; virion; virogenesis; virus assembly; virus cell interaction; virus envelope; virus infection; virus mutation; virus nucleocapsid; virus recombinant; virus titration; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses","Clausen, H., Bennet, E.P., A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation (1996) Glycobiology, 6, pp. 635-646; De Haan, C.A.M., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J.M., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; Krijnse Locker, J., Griffiths, G., Horzinek, M.C., Rottier, P.J.M., O-glycosylation of the coronavirus M protein. Differential localization of the sialyltransferases in N- and O-linked glycosylation (1992) J. Biol. Chem., 267, pp. 14094-14101; Laude, H., Gelfi, J., Lavenant, L., Charley, B., Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus (1992) J. Virol., 66, pp. 743-749; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , Siddell, S.G. (Ed.). Plenum Press, New York; Röttger, S., White, J., Wandall, H., Olivo, J.C., Stark, A., Bennet, E., Whitehouse, C., Nilsson, T., Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus (1998) J. Cell Sci., 111, pp. 45-60","De Haan, C.A.M.; Faculty of Veterinary Medicine, Institute of Biomembranes, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: x.haan@vet.uu.nl",,"Elsevier",01681702,,VIRED,"11887793","English","Virus Res.",Review,"Final",Open Access,Scopus,2-s2.0-0037196588
"Parreño V., Costantini V., Cheetham S., Blanco Viera J., Saif L.J., Fernández F., Leoni L., Schudel A.","6603502038;7003793474;16051966200;6506108986;7102226747;57197112469;14063534200;7003338811;","First isolation of rotavirus associated with neonatal diarrhoea in guanacos (Lama guanicoe) in the Argentinean Patagonia region",2001,"Journal of Veterinary Medicine, Series B","48","9",,"713","720",,26,"10.1046/j.1439-0450.2001.00486.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035205952&doi=10.1046%2fj.1439-0450.2001.00486.x&partnerID=40&md5=88197af1621d4268509e5ec57007320b","Instituto de Virología/Patobiología, CICV y A, INTA, Wooster, OH, Argentina; Castelar Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Universidad de Buenos Aires, Argentina; CONICET, Argentina; Food Animal Health Research Program, Ohio Agricultural Research and Development Center, Ohio State University, Wooster, OH, United States; Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Chorroarin 280, (1427) Capital Federal, Argentina; Instituto de Virología, Centro de Investigaciones en Ciencias Veterinarias y Agronomicas (CICV y A), Universidad de Buenos Aires, Argentina","Parreño, V., Instituto de Virología/Patobiología, CICV y A, INTA, Wooster, OH, Argentina; Costantini, V., Instituto de Virología/Patobiología, CICV y A, INTA, Wooster, OH, Argentina; Cheetham, S., Castelar Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Universidad de Buenos Aires, Argentina; Blanco Viera, J., Instituto de Virología/Patobiología, CICV y A, INTA, Wooster, OH, Argentina; Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Research and Development Center, Ohio State University, Wooster, OH, United States; Fernández, F., Instituto de Virología/Patobiología, CICV y A, INTA, Wooster, OH, Argentina; Leoni, L., Castelar Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Universidad de Buenos Aires, Argentina; Schudel, A., Castelar Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Universidad de Buenos Aires, Argentina, CONICET, Argentina, Instituto de Investigaciones en Ciencias Veterinarias, Facultad de Ciencias Veterinarias, Chorroarin 280, (1427) Capital Federal, Argentina, Instituto de Virología, Centro de Investigaciones en Ciencias Veterinarias y Agronomicas (CICV y A), Universidad de Buenos Aires, Argentina","Group A rotavirus (RV) and coronavirus (CV) are common viral pathogens associated with neonatal diarrhoea in numerous animal species. The purpose of this work was to investigate the presence of these viral agents in two farm populations of captured guanacos (Lama guanicoe) in the Argentinean Patagonia region, that developed severe diarrhoea outbreaks. Stool and serum samples were analysed for RV and bovine CV antigen and antibody by enzyme-linked immunosorbent assay. Rotavirus was detected in faeces from two new-born guanacos with acute diarrhoea, one in each farm. After electrophoretic analysis, each isolated strain, showed a distinctive long dsRNA electropherotype characteristic of group A rotaviruses (4:2:3:2). In addition, 95% (38 of 40) of the sampled animals were positive for RV antibodies, suggesting a high prevalence of RV infection in the populations tested. No evidence of CV circulation by antigen or antibody analysis was observed. To our knowledge, this is the first report of the detection and isolation of RV associated with neonatal diarrhoea in Lama guanicoe.",,"virus antibody; animal; animal disease; Argentina; article; Artiodactyla; blood; diarrhea; feces; immunology; isolation and purification; newborn; Rotavirus; ultrastructure; virology; virus infection; Animals; Animals, Newborn; Antibodies, Viral; Argentina; Camelids, New World; Diarrhea; Feces; Rotavirus; Rotavirus Infections","Adams, R., Garry, F., Llama neonatology (1994) Vet Clin. North Am., Food Anim. Pract., 10, pp. 201-208; Barrandeguy, M.E., Cornaglia, E.M., Gottschalk, M., Fitjman, N., Pasini, M.I., Gomez Yafal, A., Parraud, J., Schudel, A.A., Rotavirus, enterotoxigenic Escherichia coli and other agents in the feces of dairy calves with and without diarrhoea (1988) Rev. Lat. Am. Microbiol., 30, pp. 239-245; Bellinzoni, C., Blackhall, J., Terzolo, H.R., Moreira, A.R., Auza, N., Mattion, N., Micheo, G.I., Scodeller, E., Mycrobiology of diarrhoea in young beef and dairy calves in Argentina (1990) Revista Argentina Microbiol., 22, pp. 130-137; Bellinzoni, C., Blackhall, J., Mattion, N., Estes, M., Snodgrass, D., La Torre, J., Scodeller, E., Serological characterization of bovine rotaviruses isolated from dairy and beef herds in Argentina (1989) J. Clin. Microbiol., 27, pp. 2619-2623; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 149, pp. 51-70; Cornaglia, E.M., Barrandeguy, M., Fijtman, N., Schudel, A., Enzyme-linked immuno-sorbent assay, immunofluorescence test and electrophoretic analysis of rotaviral RNA in the diagnosis and characterization of the bovine rotavirus (1989) Rev. Lat. Am. Microbiol., 31, pp. 59-62; Costantini, V., Parreño, V., Combessies, G., Bardón, J.C., Leunda, M., Saif, L., Fernández, F., Diagnostic and antigenic characterization of group A bovinc rotavirus in Argentina (1999) Proceedings of the 80th Annual Meeting of the CRWAD, pp. 1994-1998. , Ellis, R. P. (ed), November, Chicago, IL, USA, (Poster 56P). Iowa State University Press, Ames; Drew, M.L., Fowler, M.E., Comparison of methods for measuring serum immunoglobulin concentrations in neonatal llamas (1995) JAVMA, 206, pp. 1374-1380; Hoshino, Y., Wyatt, R.G., Greenberg, H., Kalica, A., Flores, J., Kapikian, A., Isolation, propagation and characterization of a second equine rotavirus serotype (1983) Infect. Immun., 41, pp. 1031-1037; Kapikian, A.Z., Chanock, R.M., Rotaviruses (1996) Fields Virology 3rd edn., pp. 1657-1708. , Fields, B., N. Knipe, D. M. Howley, et al. (eds), Chapter 55, Lippincott-Raven Publishers, Philadelphia, PA; Karesh, W.B., Uhart, M.M., Dierenfeld, E.S., Breselton, W.E., Torres, A., House, C., Puche, H., Cook, R.A., Health evaluation of free-ranging guanaco (Lama guanicoe) (1998) J. Zoo Wild Med., 29, pp. 134-141; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Mattion, N., Bellinzoni, R.C., Blackhall, J.O., La Torre, J., Scodeller, E.A., Antigenic characterization of swine rotavirus in Argentina (1989) J. Clin. Microbiol., 27, pp. 795-798; Mattson, D.E., Update of llama medicine, viral diseases (1994) Vet. Clin. North Am.: Food Anim. Pract., 10, pp. 345-351; Murphy, P.J., Obstetrics, neonatal care and congenital conditions (1989) Vet. Clin. North Am., Food Anim. Pract., 5, pp. 183-202; Panighi, M., (1990) Coronavirus detección de anticuerpos en bovinos de la Republica Argentina, , MS Thesis. 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B., 46, pp. 157-161; Rivera, H., Madewell, B.R., Ameghino, E., Serologic survey of viral antibodies in the Peruvian alpaca (Lama pacos) (1987) Am. J. Vet. Res., 48, pp. 189-191; Saif, L.J., Bohl, E.H., Kohler, E.M., Hughes, J., Immune electron microscopy of tge virus and rotavirus (reovirus-like agent) of swine (1977) Am. J. Vet. Res., 38, pp. 13-20; Saif, L.J., A review of evidence implicating bovine coronavirus in the etiology of winter disentery in cows: An enigma resolved? (1990) Cornell Vet., 80, pp. 303-311; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning. A Laboratory Manual, 2nd edn., , Cold Spring Harbor Laboratory Press, New York, USA; Smith, D.R., Tsunemitsu, H., Heckert, R., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J. Vet. Invest., 8, pp. 99-105","Schudel, A.; Inst. de Invest. en Ciencias Veter., Facultad de Ciencias Veterinarias, Universidad de Buenos Aires, Buenos Aires, Argentina; email: incoalex@mail.retina.ar",,,09311793,,JVMBE,"11765807","English","J. Vet. Med. Ser. B",Article,"Final",,Scopus,2-s2.0-0035205952
"Hegyi A., Ziebuhr J.","6603368848;7003783935;","Conservation of substrate specificities among coronavirus main proteases",2002,"Journal of General Virology","83","3",,"595","599",,80,"10.1099/0022-1317-83-3-595","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036187709&doi=10.1099%2f0022-1317-83-3-595&partnerID=40&md5=f212921114fb922ecaca23b2aa2609c8","Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","Hegyi, A., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","The key enzyme in coronavirus replicase polyprotein processing is the coronavirus main protease, 3CLpro. The substrate specificities of five coronavirus main proteases, including the prototypic enzymes from the coronavirus groups I, II and III, were characterized. Recombinant main proteases of human coronavirus (HCoV), transmissible gastroenteritis virus (TGEV), feline infectious peritonitis virus, avian infectious bronchitis virus and mouse hepatitis virus (MHV) were tested in peptide-based trans-cleavage assays. The determination of relative rate constants for a set of corresponding HCoV, TGEV and MHV 3CLpro cleavage sites revealed a conserved ranking of these sites. Furthermore, a synthetic peptide representing the N-terminal HCoV 3CLpro cleavage site was shown to be effectively hydrolysed by noncognate main proteases. The data show that the differential cleavage kinetics of sites within pp1a/pp1ab are a conserved feature of coronavirus main proteases and lead us to predict similar processing kinetics for the replicase polyproteins of all coronaviruses.",,"nucleotidyltransferase; peptide; polyprotein; proteinase; recombinant enzyme; synthetic peptide; virus enzyme; amino terminal sequence; article; assay; Avian infectious bronchitis virus; controlled study; Coronavirus; enzyme degradation; enzyme kinetics; enzyme specificity; hydrolysis; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; priority journal; protein processing; virus strain; Aves; Avian infectious bronchitis virus; Coronavirus; Felidae; Feline infectious peritonitis virus; Murinae; Murine hepatitis virus; RNA viruses; Transmissible gastroenteritis virus","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceedings of the National Academy of Sciences, USA, 97, pp. 5516-5521; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) Journal of Virology, 63, pp. 3693-3699; Bazan, J.F., Fletterick, R.J., Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications (1988) Proceedings of the National Academy of Sciences, USA, 85, pp. 7872-7876; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) Journal of Virology, 71, pp. 900-909; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO Journal, 6, pp. 3779-3785; Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., A reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) Journal of Virology, 75, pp. 12359-12369; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Archives of Virology, 142, pp. 629-633; den Boon, J.A., Snijder, E.J., Chirnside, E.D., de Vries, A.A., Horzinek, M.C., Spaan, W.J., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) Journal of Virology, 65, pp. 2910-2920; Denison, M.R., Spaan, W.J., van der Meer, Y., Gibson, C.A., Sims, A.C., Prentice, E., Lu, X.T., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) Journal of Virology, 73, pp. 6862-6871; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Gorbalenya, A.E., Donchenko, A.P., Blinov, V.M., Koonin, E.V., Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. 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Papain (1967) Biochemical and Biophysical Research Communications, 27, pp. 157-162; Seybert, A., Ziebuhr, J., Siddell, S.G., Expression and characterization of a recombinant murine coronavirus 3C-like proteinase (1997) Journal of General Virology, 78, pp. 71-75; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., van der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO Journal, 2, pp. 1839-1844; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) Journal of General Virology, 82, pp. 1273-1281; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Viral replicase gene products suffice for coronavirus discontinuous transcription (2001) Journal of Virology, 75, pp. 6676-6681; Tibbles, K.W., Brierley, I., Cavanagh, D., Brown, T.D., Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus (1996) Journal of Virology, 70, pp. 1923-1930; van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proceedings of the National Academy of Sciences, USA, 96, pp. 12056-12061; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) Journal of Virology, 73, pp. 177-185; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) Journal of Virology, 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) Journal of Virology, 71, pp. 3992-3997; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) Journal of General Virology, 81, pp. 853-879; Ziebuhr, J., Thiel, V., Gorbalenya, A.E., The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond (2001) Journal of Biological Chemistry, 276, pp. 33220-33232","Ziebuhr, J.; Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; email: ziebuhr@vim.uni-wuerzburg.de",,"Society for General Microbiology",00221317,,JGVIA,"11842254","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036187709
"Wurzer W.J., Obojes K., Vlasak R.","6602637630;7801504625;56244751900;","The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: A proposal to reorganize group 2 Coronaviridae",2002,"Journal of General Virology","83","2",,"395","402",,26,"10.1099/0022-1317-83-2-395","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036171471&doi=10.1099%2f0022-1317-83-2-395&partnerID=40&md5=bdbe048da7c3fd39d15a6725271be427","Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria","Wurzer, W.J., Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria; Obojes, K., Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria; Vlasak, R., Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria","Group 2 coronaviruses are characterized within the order Nidovirales by a unique genome organization. A characteristic feature of group 2 coronaviruses is the presence of a gene encoding the haemagglutinin-esterase (HE) protein, which is absent in coronaviruses of groups 1 and 3. At least three coronavirus strains within group 2 expressed a structural protein with sialate-4-O-acetylesterase activity, distinguishing them from other members of group 2, which encode an enzyme specific for 5-N-acetyl-9-O-acetylneuraminic acid. The esterases of mouse hepatitis virus (MHV) strains S and JHM and puffinosis virus (PV) specifically hydrolysed 5-N-acetyl-4-O-acetylneuraminic acid (Neu4,5Ac2) as well as the synthetic substrates p-nitrophenyl acetate, 4-methylumbelliferyl acetate and fluorescein diacetate. The Km values of the MHV-like esterases for the latter substrates were two- to tenfold lower than those of the sialate-9-O-acetylesterases of influenza C viruses. Another unspecific esterase substrate, α-naphthyl acetate, was used for the in situ detection of the dimeric HE proteins in SDS-polyacrylamide gels. MHV-S, MHV-JHM and PV bound to horse serum glycoproteins containing Neu4,5Ac2. De-O-acetylation of the glycoproteins by alkaline treatment or incubation with the viral esterases resulted in a complete loss of recognition, indicating a specific interaction of MHV-like coronaviruses with Neu4,5Ac2. Combined with evidence for distinct phylogenetic lineages of group 2 coronaviruses, subdivision into subgroups 2a (MHV-like viruses) and 2b (bovine coronavirus-like viruses) is suggested.",,"1 naphthyl acetate; acetic acid derivative; acetylesterase; esterase; fluorescein diacetate; glycoprotein; n acetylneuraminic acid derivative; plasma protein; sialic acid derivative; structural protein; virus hemagglutinin; virus protein; alkalinity; animal cell; article; cell interaction; controlled study; Coronavirus; deacetylation; enzyme activity; enzyme specificity; enzyme substrate; genetic code; incubation time; Influenza virus C; Michaelis constant; molecular phylogeny; mouse; Murine hepatitis coronavirus; nonhuman; polyacrylamide gel electrophoresis; priority journal; protein analysis; protein expression; protein hydrolysis; strain difference; virus characterization; virus genome; virus strain; Animalia; Bovinae; Bovine coronavirus; Coronaviridae; Coronavirus; Equus caballus; Influenza C virus; Influenza virus; Murinae; Murine hepatitis virus; Murine hepatitis virus (strain S); Nidovirales; Puffinosis virus; RNA viruses","Bos, E.C., Luytjes, W., van der Meulen, H.V., Koerten, H.K., Spaan, W.J., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Cornelissen, L.A., Wierda, C.M., van der Meer, F.J., Herrewegh, A.A., Horzinek, M.C., Egberink, H.F., de Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) Journal of Virology, 71, pp. 5277-5286; Duckmanton, L., Tellier, R., Richardson, C., Petric, M., The novel hemagglutinin-esterase genes of human torovirus and Breda virus (1999) Virus Research, 64, pp. 137-149; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M., Laude, H., Masters, P.S., Talbot, P., Coronaviridae (2000) Virus Taxonomy. 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Vlasak, R., Krystal, M., Nacht, M., Palese, P., The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities (1987) Virology, 160, pp. 419-425; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) Journal of Virology, 62, pp. 4686-4690; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proceedings of the National Academy of Sciences, USA, 85, pp. 4526-4529; Volz, D., Reid, P.E., Park, C.M., Owen, D.A., Dunn, W.L., A new histochemical method for the selective periodate oxidation of total tissue sialic acids (1987) Histochemical Journal, 19, pp. 311-318; Wessner, D.R., Shick, P.C., Lu, J.H., Cardellichio, C.B., Gagneten, S.E., Beauchemin, N., Holmes, K.V., Dveksler, G.S., Mutational analysis of the virus and monoclonal antibody binding sites in MHVR, the cellular receptor of the murine coronavirus mouse hepatitis virus strain A59 (1998) Journal of Virology, 72, pp. 1941-1948; Yokomori, K., Banner, L.R., Lai, M.M., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Yokomori, K., Stohlman, S.A., Lai, M.M., The detection and characterization of multiple hemagglutinin-esterase (HE)-defective viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178","Vlasak, R.; Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria; email: rvlasak@oeaw.ac.at",,"Society for General Microbiology",00221317,,JGVIA,"11807232","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036171471
"Arthington J.D., Jaynes C.A., Tyler H.D., Kapil S., Quigley III J.D.","55919614900;7003619713;7006590669;7003293348;7102715774;","The use of bovine serum protein as an oral support therapy following coronavirus challenge in calves",2002,"Journal of Dairy Science","85","5",,"1249","1254",,18,"10.3168/jds.S0022-0302(02)74189-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036561830&doi=10.3168%2fjds.S0022-0302%2802%2974189-1&partnerID=40&md5=d45e02562bfb32d8689be1e3bc27a630","Range Cattle Res. and Educ. Center, University of Florida, IFAS, Ona, FL 33865, United States; American Protein Corporation, Inc., Ames, IA 50010, United States; Department of Animal Sciences, Iowa State University, Ames, IA 50010, United States; College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States","Arthington, J.D., Range Cattle Res. and Educ. Center, University of Florida, IFAS, Ona, FL 33865, United States; Jaynes, C.A., American Protein Corporation, Inc., Ames, IA 50010, United States; Tyler, H.D., Department of Animal Sciences, Iowa State University, Ames, IA 50010, United States; Kapil, S., College of Veterinary Medicine, Kansas State University, Manhattan, KS 66506, United States; Quigley III, J.D., American Protein Corporation, Inc., Ames, IA 50010, United States","The objective of this experiment was to investigate the therapeutic efficacy of a supplemental bovine serum protein blend fed to calves challenged with virulent coronavirus. Twelve Holstein bull calves (approximately 3 wk of age) were allocated by initial body weight to Control (n = 5) and treated (n = 7) groups. On d 0, all calves were orally challenged with 1 × 10 7 plaque-forming units of virulent coronavirus isolate. Infection was allowed to progress for 24 h before treatment was started. On d 1, treated calves began receiving 160 g of dry bovine serum powder (16 g IgG) mixed into milk replacer powder (67 g) at both an a.m. and p.m. feeding. Control calves received only milk replacer powder (227 g) at both feedings. Response to coronavirus challenge and dietary treatment was monitored prior to a.m. and p.m. feeding by the collection of multiple clinical measures. Fecal consistency was decreased by coronavirus challenge but was not affected by dietary treatment. Mean daily rectal temperature and heart rate were not affected by dietary treatment. Average packed cell volume was higher in treated calves than in control (35.0 and 27.0%). Coronavirus challenge resulted in an immediate increase in respiration rate, decreasing by d 7. Control calves tended to have a greater average respiration rate compared with treated (28.7 vs. 26.8 breaths/min). Treated calves had a higher average feed intake than control (0.57 vs. 0.44 kg/d). These data suggest that bovine-serum supplemented milk replacer may decrease the severity of disease in young calves exposed to coronavirus.","Bovine serum; Calf; Coronavirus","Bovinae; Coronavirus; plasma protein; animal; animal disease; article; body temperature; body weight; breathing; cattle; cattle disease; diet; feces; heart rate; hematocrit; male; milk; pathophysiology; virus infection; Animals; Blood Proteins; Body Temperature; Body Weight; Cattle; Cattle Diseases; Coronavirus Infections; Diet; Feces; Heart Rate; Hematocrit; Male; Milk; Respiration","Arthington, J.D., Cattell, M.B., Quigley III, J.D., Effect of dietary IgG source (colostrum, serum, or milk-derived supplement) on the efficiency of Ig absorption in newborn Holstein calves (2000) J. Dairy Sci., 83, pp. 1463-1467; Arthington, J.D., Cattell, M.B., Quigley III, J.D., McCoy, G.C., Hurley, W.L., Passive immunoglobulin transfer in newborn calves fed colostrum or spray-dried serum protein alone or as a supplement to colostrum of varying quality (2000) J. Dairy Sci., 83, pp. 2834-2838; Bianca, W., Effects of dehydration, rehydration and overhydration on the blood and urine of oxen (1970) Br. Vet. J., 126, pp. 121-133; Breazile, J.E., The physiology of stress and its relationship to mechanisms of disease and therapeutics (1988) Vet. Clinics North America: Food Anim. Pract., 4, pp. 441-480; Brock, J.H., Arzabe, F.R., Ortega, F., Pineiro, A., The effect of limited proteolysis by trypsin and chymotrypsin on bovine colostral IgG1 (1977) Immunology, 32, pp. 215-219; Cain, C.M., Zimmerman, D.R., Effect of spray-dried plasma (SDP) on fecal shedding of hemolytic Escherichia coli. (HEC) and rotavirus by pigs in a segregated early weaned (SEW) environment (1997) J. Anim. Sci., 75 (1 SUPPL.), p. 61. , Abstr; Castrucci, G., Frigeri, F., Ferrari, M., Cilli, V., Caleffi, F., Aldrovandi, V., Nigrelli, A., The efficacy of colostrum from cows vaccinated with rotavirus in protecting calves to experimentally induced rotavirus infection (1984) Comp. Immun. Microbiol. Infect. Dis., 7, pp. 11-18; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 149, pp. 51-70; Coffey, R.D., Cromwell, G.L., The impact of environment and antimicrobial agents on the growth response of early weaned pigs to spray-dried porcine plasma (1995) J. Anim. Sci., 73, pp. 2532-2539; Gatnau, R., Zimmerman, D.R., Diaz, T., Johns, J., Determination of optimum levels of spray-dried porcine plasma (SDPP) in diets for weanling pigs (1991) J. Anim. Sci., 69 (1 SUPPL.), p. 369. , Abstr; (1988) Guide for the Care and Use of Agricultural Animals in Agricultural Research and Teaching, , Consortium for Developing a Guide for the Care and Use of Agricultural Animals in Agricultural Research and Teaching, Champaign, IL; Kapil, S., Trent, A.M., Goyal, S.M., Antibody responses in spiral colon, ileum, and jejunum of bovine coronavirus-infected neonatal calves (1994) Comp. Immunol. Microbiol. Infect. Dis., 17, pp. 139-149; Kats, L.J., Nelssen, J.L., Tokach, M.D., Goodband, R.D., Hansen, J.A., Laurin, J.L., The effect of spray-dried porcine plasma on growth performance in the early weaned pig (1994) J. Anim. Sci., 72, pp. 2075-2081; Langpap, T.J., Bergeland, M.E., Reed, D.E., Coronaviral enteritis of young calves: Virologic and pathologic findings in naturally occurring infections (1979) Am. J. Vet. Res., 40, pp. 1476-1478; Morrill, J.L., Morrill, J.M., Feyerherm, A.M., Laster, J.F., Plasma proteins and a probiotic as ingredients in milk replacer (1995) J. Dairy Sci., 78, pp. 902-907; (1994) Dairy Heifer Morbidity, Mortality, and Health Management Focusing on Preweaned Heifers, , USDA-APHIS-VS; Quigley III, J.D., Drew, M.D., Effects of oral antibiotics or bovine plasma on survival, health and growth in dairy calves challenged with Escherichia coli (2000) Food Agric. Immunol., 12, pp. 311-318; Quigley III, J.D., Fike, D.L., Edgerton, M.N., Drewery, J.J., Arthington, J.D., Effects of a colostrum replacement product derived from serum on immunoglobulin G absorption by calves. J (1998) Dairy Sci., 81, pp. 1936-1939; Reynolds, D.J., Coronavirus replication in the intestinal and respiratory tracts during infection in calves (1983) Ann. Rech. Vet., 14, pp. 445-446; (1988) SAS User's Guide: Statistics, Version 6 Edition., , SAS Inst., Inc., Cary, NC; Schalm, O.W., Cattle: Normal hematology with comments on disease (1986) Schalm's Veterinary Hematology. 4th Ed., pp. 178-207. , N. C. Jain, ed. Lea and Febiger, Philadelphia, PA; Schoenthaler, S., Kapil, S., Development and application of a bovine coronavirus antigen detection enzyme-linked immunosorbent assay (1999) Clin. Diag. Lab. Immunol., 6, pp. 130-136; Stott, G.H., Marx, D.B., Menefee, B.E., Nightengale, G.T., Colostral immunoglobulin transfer in calves. I. Period of absorption (1979) J. Dairy Sci., 62, pp. 1632-1638; Torres-Medina, A., Schlafer, D.H., Mebus, C.A., Rotaviral and coronaviral diarrhea (1985) Vet. Clinics North America: Food Anim. Pract., 1, pp. 471-493; Yokoyama, H., Peralta, R.C., Diaz, R., Sendo, S., Ikemori, Y., Kodama, Y., Passive protective effect of chicken egg yolk immunoglobulins against experimental enterotoxigenic Escherichia coli infection in neonatal piglets (1992) Infect. Immunol., 60, pp. 998-1007; Zimmerman, D.R., Porcine plasma proteins in diets of weanling pigs (1987) ISU Swine Res. Rpt. ASL-R482","Arthington, J.D.; Range Cattle Res. and Educ. Center, University of Florida, IFAS, Ona, FL 33865, United States; email: jarth@gnv.ifas.ufl.edu",,"American Dairy Science Association",00220302,,,"12086062","English","J. Dairy Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0036561830
"Wünschmann A., Frank R., Pomeroy K., Kapil S.","6701834947;57214115780;7003520694;7003293348;","Enteric coronavirus infection in a juvenile dromedary (Camelus dromedarius)",2002,"Journal of Veterinary Diagnostic Investigation","14","5",,"441","444",,16,"10.1177/104063870201400518","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1342293163&doi=10.1177%2f104063870201400518&partnerID=40&md5=fa2b82eeebe996bd3667ae79eaf19faf","Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, 1333 Cortner Avenue, St. Paul, MN 55108, United States; Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, 1800 Denison Avenue, Manhattan, KS 66506, United States","Wünschmann, A., Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, 1333 Cortner Avenue, St. Paul, MN 55108, United States; Frank, R., Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, 1333 Cortner Avenue, St. Paul, MN 55108, United States; Pomeroy, K., Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, 1333 Cortner Avenue, St. Paul, MN 55108, United States; Kapil, S., Dept. of Diagn. Med.-Pathobiology, College of Veterinary Medicine, 1800 Denison Avenue, Manhattan, KS 66506, United States","A case of an enteric coronavirus infection in a 6-week-old dromedary calf is described. The animal had diarrhea for 5 days and died despite symptomatic treatment. Numerous viral particles, approximately 140 nm in diameter, with club-like projections were detected in the feces by electron microscopy. These characteristics were consistent with a coronavirus. Immunohistochemical reactivity with 2 antigenic group II coronavirus-specific antibodies confirmed the presence of viral antigen in colonie epithelial cells. The death of the animal was attributed to a neutrophilic and emphysematous colitis that likely was caused by an infection with a Clostridium sp.",,"animal; animal disease; article; bacterial infection; camel; case report; colitis; Coronavirus; enteropathy; fatality; feces; female; isolation and purification; pathology; ultrastructure; virology; virus infection; Animals; Camels; Clostridium Infections; Colitis; Coronavirus; Coronavirus Infections; Fatal Outcome; Feces; Female; Intestinal Diseases","Chasey, D., Reynolds, D.J., Bridger, J.C., Identification of coronaviruses in exotic species of Bovidae (1984) Vet Rec, 115, pp. 602-603; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; Daginakatte, G.C., Chard-Bergstrom, C., Andrews, G.A., Kapil, S., Production, characterization, and use of monoclonal antibodies against recombinant nucleoprotein of elk coronavirus (1999) Clin Diagn Lab Immunol, 6, pp. 341-344; Davis, E., Rush, B.R., Cox, J., Neonatal enterocolitis associated with coronavirus infection in a foal: A case report (2000) J Vet Diagn Invest, 12, pp. 153-156; El Sanousi, S.M., Gameel, A.A., An outbreak of enterotoxemia in suckling camels (1993) J Vet Med Assoc, 40, pp. 525-532; Flewett, T.H., Electron microscopy in the diagnosis of infectious diarrhea (1978) J Am Vet Med Assoc, 173, pp. 538-541; Fowler, M.E., Camelids (1986) Zoo and Wild Animal Medicine, pp. 969-981. , ed. 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Feldmann BV, Zinkl JG, Jain NC. 5th ed., Lippincott Williams & Wilkins, Philadelphia. PA; Saif, L.J., Enteric viral infections of pigs and strategies for induction of mucosal immunity (1999) Adv Vet Med, 41, pp. 429-446; Tsunemitsu, H., El-Kanawati, Z.R., Smith, D.R., Isolation of coronaviruses antigenetically indistinguishable from bovine coronavirus from wild ruminants with diarrhea (1995) J Clin Microbiol, 33, pp. 3264-3269; Welsh, S.K.W., Saif, L.J., Monoclonal antibodies to a virulent strain of transmissible gastroenteritis virus: Comparison of reactivity with virulent and attenuated virus (1988) Arch Virol, 101, pp. 221-235; Wernery, U., New aspects of infectious diseases of camelids (1999) J Camel Pract Res, 6, pp. 87-91; Wernery, U., Kaaden, O.R., Bacterial diseases and viral diseases (2002) Infectious Diseases in Camelids, pp. 19-236. , ed. Wernery U, 2nd ed., Blackwell Science, Berlin, Germany; Zhang, Z., Andrews, G.A., Chard-Bergstrom, C., Application of immunohistochemistry and in situ hybridization for detection of bovine coronavirus in paraffin-embedded, formalinfixed intestines (1997) J Clin Microbiol, 35, pp. 2964-2965","Wünschmann, A.; Dept. of Vet. Diagnostic Medicine, College of Veterinary Medicine, University of Minnesota, 1333 Cortner Avenue, St. Paul, MN 55108, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12296403","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-1342293163
"Besselsen D.G., Wagner A.M., Loganbill J.K.","6603949626;7401457025;6507493409;","Detection of rodent coronaviruses by use of fluorogenic reverse transcriptase-polymerase chain reaction analysis",2002,"Comparative Medicine","52","2",,"111","116",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036011140&partnerID=40&md5=cc40c749b1281163e292dc5fb21b47a2","Department of University Animal Care, University of Arizona, Tucson, AZ 85721-0101, United States","Besselsen, D.G., Department of University Animal Care, University of Arizona, Tucson, AZ 85721-0101, United States; Wagner, A.M., Department of University Animal Care, University of Arizona, Tucson, AZ 85721-0101, United States; Loganbill, J.K., Department of University Animal Care, University of Arizona, Tucson, AZ 85721-0101, United States","Reverse transcriptase-polymerase chain reaction (RT-PCR) assays have proved useful for the detection of mouse hepatitis virus (MHV) and rat coronavirus (RAV) in acutely infected animals and contaminated biomaterials. Fluorogenic nuclease RT-PCR assays combine RT-PCR with an internal fluorogenic hybridization probe, thereby eliminating post-PCR processing and potentially enhancing specificity. Consequently, a fluorogenic nuclease RT-PCR assay specific for rodent coronaviruses was developed. Primer and probe sequences were selected from the viral genome segment that encodes the membrane (M) protein that is highly conserved among rodent coronaviruses. Use of the fluorogenic nuclease RT-PCR detected all strains of MHV and RCV that were evaluated, but did not detect other RNA viruses that naturally infect rodents. Use of the assay detected as little as two femtograms of in vitro transcribed RNA generated from cloned amplicon, and when compared directly with mouse antibody production tests, had similar sensitivity at detecting MHV-A59 in infected cell culture lysates. Finally, use of the assay detected coronavirus RNA in tissues, cage swipes, and feces obtained from mice experimentally infected with MHV, and in tissues and cage swipes obtained from rats naturally infected with RCV. These results indicate that the fluorogenic nuclease RT-PCR assay should provide a potentially high-throughput, PCR-based method to detect rodent coronaviruses in infected rodents and contaminated biological materials.",,"animal disease; animal experiment; antibody production; article; contamination; Coronavirus; male; mouse; nonhuman; reverse transcription polymerase chain reaction; virus detection; virus genome; animal; animal disease; bioassay; cell line; evaluation; experimental animal; genetics; isolation and purification; metabolism; methodology; Murine hepatitis coronavirus; polymerase chain reaction; rat; rodent disease; sensitivity and specificity; Sprague Dawley rat; virology; virus infection; fluorescent dye; Animals; Animals, Laboratory; Biological Assay; Cell Line; Coronavirus Infections; Coronavirus, Rat; Fluorescent Dyes; Mice; Murine hepatitis virus; Polymerase Chain Reaction; Rats; Rats, Sprague-Dawley; Rodent Diseases; Sensitivity and Specificity","Jacoby, R.O., Lindsey, J.R., Risks of infection among laboratory rats and mice at major biomedical research institutions (1998) ILAR J., 39, pp. 266-271; Barthold, S.W., Mouse hepatitis virus biology and epizootiology (1986) Viral and mycoplasmal infections of laboratory rodents, pp. 571-601. , P. N. Bhatt, and R. O. Jacoby (ed.). Academic Press, Inc., New York; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28. , Erratum, 43(2):203, 1993; Barthold, S.W., Smith, A.L., Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice (1984) Arch. Virol., 81, pp. 103-112; Baker, D.G., Natural pathogens of laboratory mice, rats, and rabbits and their effects on research (1998) Clin. Microbiol. Rev., 11, pp. 231-266; Bhatt, P.N., Percy, D.H., Jonas, A.M., Characterization of the virus of sialodacryoadenitis of rats: A member of the coronavirus group (1972) J. Infect. Dis., 126, pp. 123-130; Parker, J.C., Cross, S.S., Rowe, W.P., Rat coronavirus (RCV): A prevalent, naturally occurring pneumotropic virus of rats (1970) Arch. Gesamte Virusforsch., 31, pp. 293-302; Collins M.J., Jr., Parker, J.C., Murine virus contaminants of leukemia viruses and transplantable tumors (1972) J. Natl. Cancer Inst., 49, pp. 1139-1143; Nicklas, W., Kraft, V., Meyer, B., Contamination of transplantable tumors, cell lines, and monoclonal antibodies with rodent viruses (1993) Lab. Anim. Sci., 43, pp. 296-300; Smith, A.L., Winograd, D.F., Two enzyme immunoassays for the detection of antibody to rodent coronaviruses (1986) J. Virol. Methods, 14, pp. 335-3343; Smith, A.L., An immunofluorescence test for detection of serum antibody to rodent coronaviruses (1983) Lab. Anim. Sci., 33, pp. 157-160; Peters, R.L., Collins, M.J., Use of mouse hepatitis virus antigen in an enzyme-linked immunosorbent assay for rat coronaviruses (1981) Lab. Anim. Sci., 31, pp. 472-475; Peters, R.L., Collins, M.J., O'Beirne, A.J., Howton, P.A., Hourihan, S.L., Thomas, S.F., Enzyme-linked immunosorbent assay for detection of antibodies to murine hepatitis virus (1979) J. Clin. Microbiol., 10, pp. 595-597; Matthaei, K.I., Berry, J.R., France, M.P., Yeo, C., Garcia-Aragon, J., Russell, P.J., Use of polymerase chain reaction to diagnose a natural outbreak of mouse hepatitis virus infection in nude mice (1998) Lab. Anim. Sci., 48, pp. 137-144; Casebolt, D.B., Qian, B., Stephensen, C.B., Detection of enterotropic mouse hepatitis virus fecal excretion by polymerase chain reaction (1997) Lab. Anim. Sci., 47, pp. 6-10; Compton, S.R., Vivas-Gonzalez, B.E., Macy, J.D., Reverse transcriptase polymerase chain reaction-based diagnosis and molecular characterization of a new rat coronavirus strain (1999) Lab. Anim. Sci., 49, pp. 506-513; Homberger, F.R., Smith, A.L., Barthold, S.W., Detection of rodent coronaviruses in tissues and cell cultures by using polymerase chain reaction (1991) J. Clin. Microbiol., 29, pp. 2789-2793; Compton, S.R., Riley, L.K., Detection of infectious agents in laboratory rodents: Traditional and molecular techniques (2001) Comp. Med., 51, pp. 113-119; Kendall, L.V., Besselsen, D.G., Riley, L.K., Fluorogenic 5′ nuclease PCR (real time PCR) (2000) Contemp. Top. Lab. Anim. Sci., 39, p. 41; Tattersall, P., Bratton, J., Reciprocal productive and restrictive virus-cell interactions of immunosuppressive and prototype strains of minute virus of mice (1983) J. Virol., 46, pp. 944-955; Besselsen, D.G., Pintel, D.J., Purdy, G.A., Besch-Williford, C.L., Franklin, C.L., Hook R.R., Jr., Riley, L.K., Molecular characterization of newly recognized rodent parvoviruses (1996) J. Gen. Virol., 77, pp. 899-911; Fleming, J.O., Stohlman, S.A., Harmon, R.C., Lai, M.M., Frelinger, J.A., Weiner, L.P., Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus (1983) Virology, 131, pp. 296-307; Barthold, S.W., Host age and genotypic effects on enterotropic mouse hepatitis virus infection (1987) Lab. Anim. Sci., 37, pp. 36-40; Compton, S.R., Smith, A.L., Gaertner, D.J., Comparison of the pathogenicity in rats of rat coronaviruses of different neutralization groups (1999) Lab. Anim. Sci., 49, pp. 514-518; Barthold, S.W., Smith, A.L., Duration of mouse hepatitis virus infection: Studies in immunocompetent and chemically immunosuppressed mice (1990) Lab. Anim. Sci., 40, pp. 133-137; Jacobsen, G., Perlman, S., Localization of virus and antibody response in mice infected persistently with MHV-JHM (1990) Adv. Exp. Med. Biol., 276, pp. 573-578; Lavi, E., Gilden, D.H., Highkin, M.K., Weiss, S.R., Persistence of mouse hepatitis virus A59 RNA in a slow virus demyelinating infection in mice as detected by in situ hybridization (1984) J. Virol., 51, pp. 563-566; Perlman, S., Jacobsen, G., Olson, A.L., Afifi, A., Identification of the spinal cord as a major site of persistence during chronic infection with a murine coronavirus (1990) Virology, 175, pp. 418-426","Besselsen, D.G.; Department of University Animal Care, University of Arizona, Tucson, AZ 85721-0101, United States",,,00236764,,COMEF,"12022389","English","Comp. Med.",Article,"Final",,Scopus,2-s2.0-0036011140
"De Haan C.A.M., Masters P.S., Shen X., Weiss S., Rottier P.J.M.","7003682643;7006234572;36867025200;57203567044;7006145490;","The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host",2002,"Virology","296","1",,"177","189",,168,"10.1006/viro.2002.1412","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036343241&doi=10.1006%2fviro.2002.1412&partnerID=40&md5=05dc9481a2a4d28e29b6cd2f655130ec","Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL, Utrecht, Netherlands; Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States","De Haan, C.A.M., Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL, Utrecht, Netherlands; Masters, P.S., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Shen, X., Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany, NY 12201, United States; Weiss, S., Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Rottier, P.J.M., Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL, Utrecht, Netherlands","In addition to a characteristic set of essential genes coronaviruses contain several so-called group-specific genes. These genes differ distinctly among the three coronavirus groups and are specific for each group. While the essential genes encode replication and structural functions, hardly anything is known about the products and functions of the group-specific genes. As a first step to elucidate their significance, we deleted the group-specific genes from the group 2 mouse hepatitis virus (MHV) genome via a novel targeted recombination system based on host switching (L. Kuo, G. J. Godeke, M. J. Raamsman, P. S. Masters, and P. J. M. Rottier, 2000, J. Virol. 74, 1393-1406). Thus, we obtained recombinant viruses from which the two clusters of group-specific genes were deleted either separately or in combination in a controlled genetic background. As all recombinant deletion mutant viruses appeared to be viable, we conclude that the MHV group-specific genes are nonessential, accessory genes. Importantly, all deletion mutant viruses were attenuated when inoculated into their natural host, the mouse. Therefore, deletion of the coronavirus group-specific genes seems to provide an attractive approach to generate attenuated live coronavirus vaccines. © 2002 Elsevier Science (USA).","Coronavirus; Group-specific genes; Mouse hepatitis virus; Reverse genetics; Targeted recombination","corona virus vaccine; unclassified drug; virus vaccine; article; controlled study; Coronavirus; gene deletion; genetics; hepatitis virus; host; nonhuman; priority journal; virus gene; virus genome; virus recombinant; Coronavirus; Murinae; Murine hepatitis virus","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. 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Virol., 65, pp. 5605-5608; Yokomori, K., Stohlman, S.A., Lai, M.M., The detection and characterization of multiple hemagglutinin-esterase (HE)-defective viruses in the mouse brain during subacute demyelination induced by mouse hepatitis virus (1993) Virology, 192, pp. 170-178. , doi:10.1006/ viro.1993.1019; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Zoltick, P.W., Leibowitz, J.L., Oleszak, E.L., Weiss, S.R., Mouse hepatitis virus ORF 2a is expressed in the cytosol of infected mouse fibroblasts (1990) Virology, 174, pp. 605-607","De Haan, C.A.M.; Virology Division, Department of Infectious Diseases, Yalelaan 1, 3584CL Utrecht, Netherlands; email: x.haan@vet.uu.nl",,"Elsevier",00426822,,VIRLA,"12036329","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0036343241
"Gagneur A., Legrand M.C., Picard B., Baron R., Talbot P.J., De Parscau L., Sizun J.","6508170069;7102317918;11640757600;8315528400;7102670281;7006825420;35605340000;","Nosocomial infection by human coronaviruses in neonates [Infections nosocomiales à coronavirus humains chez le nouveau-né]",2002,"Archives de Pediatrie","9","1",,"61","69",,14,"10.1016/S0929-693X(01)00696-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036163132&doi=10.1016%2fS0929-693X%2801%2900696-0&partnerID=40&md5=24bf14841612f06620bc75f6cb1760fa","Unité de Réanimation Pédiatrique, Département de Pédiatrie, CHU, 29609 Brest, France; Unité de Virologie, Département de Microbiologie, CHU, 29609 Brest, France; Unité d'Hygiène Hospitalière, CHU, 29609 Brest, France; Laboratoire de Neuro-immunovirologie, INRS-institut Armand-Frappier, Université du Québec, Laval, Québec, Canada","Gagneur, A., Unité de Réanimation Pédiatrique, Département de Pédiatrie, CHU, 29609 Brest, France; Legrand, M.C., Unité de Virologie, Département de Microbiologie, CHU, 29609 Brest, France; Picard, B., Unité de Virologie, Département de Microbiologie, CHU, 29609 Brest, France; Baron, R., Unité d'Hygiène Hospitalière, CHU, 29609 Brest, France; Talbot, P.J., Laboratoire de Neuro-immunovirologie, INRS-institut Armand-Frappier, Université du Québec, Laval, Québec, Canada; De Parscau, L., Unité de Réanimation Pédiatrique, Département de Pédiatrie, CHU, 29609 Brest, France; Sizun, J., Unité de Réanimation Pédiatrique, Département de Pédiatrie, CHU, 29609 Brest, France","Human coronaviruses, with two known serogroups named 229-E and OC-43, are enveloped positive-stranded RNA viruses. The large RNA is surrounded by a nucleoprotein (protein N). The envelop contains 2 or 3 glycoproteins: spike protein (or protein S), matrix protein (or protein M) and a hemag-glutinin (or protein HE). Their pathogen role remains unclear because their isolation is difficult. Reliable and rapid methods as immunofluorescence with monoclonal antibodies and reverse transcription-polymerase chain reaction allow new researches on epidemiology. Human coronaviruses can survive for as long as 6 days in suspension and 3 hours after drying on surfaces, suggesting that they could be a source of hospital-acquired infections. Two prospective studies conducted in a neonatal and paediatric intensive care unit demonstrated a significant association of coronavirus-positive nasopharyngal samples with respiratory illness in hospitalised preterm neonates. Positive samples from staff suggested either a patient-to-staff or a staff-to-patient transmission. No cross-infection were observed from community-acquired respiratory-syncitial virus or influenza-infected children to neonates. Universal precautions with hand washing and surface desinfection could be proposed to prevent coronavirus transmission. © 2002 Éditions scientifiques et médicales Elsevier SAS.","Coronavirus; Cross infection; Infant, newborn","virus RNA; article; artificial ventilation; central venous catheterization; Coronavirus; disinfection; hospital infection; human; immunofluorescence test; newborn; newborn infection; newborn intensive care; nonhuman; parenteral nutrition; prematurity; respiratory tract infection; reverse transcription polymerase chain reaction; risk factor; RNA virus; virus detection; virus infection; virus transmission","Turner, R.B., Nosocomial viral respiratory infections in pediatric patients (1996) Hospital epidemiology and infection control, pp. 485-493. , Mayhall CG, Ed. 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Importance et diagnostic (1998) Presse Med, 27, pp. 1813-1817; Falsey, A.R., McCann, R.M., Hall, W.J., Criddle, M.M., Formica, M.A., Wycoff, D., The « common cold » in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J Am Geriatr Soc, 45, pp. 706-711; Sizun, J., Baron, R., Soupre, D., Giroux, J.D., De Parscau, L., Infections nosocomiales liées au virus respiratoire syncytial: Quelles mesures d'hygiène? (1996) Arch Pédiatr, 3, pp. 723-727; Guidelines for prevention of nosocomial pneumonia (1997) MMWR Morb Mortal Wkly Rep, 46, pp. 1-79","Sizun, J.; Unite de Reanimation Pediatrique, Departement de Pédiatrie, CHU, 29609 Brest, France; email: jacques.sizun@chu-brest.fr",,"Elsevier Masson SAS",0929693X,,APEDE,"11865552","French","Arch. Pediatr.",Article,"Final",Open Access,Scopus,2-s2.0-0036163132
"Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.","6603368848;6603867465;7005626044;7003783935;","Mutational analysis of the active centre of coronavirus 3C-like proteases",2002,"Journal of General Virology","83","3",,"581","593",,43,"10.1099/0022-1317-83-3-581","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036190639&doi=10.1099%2f0022-1317-83-3-581&partnerID=40&md5=45f38aa82e7da8292add2e7046dd8b29","Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","Hegyi, A., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Friebe, A., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Gorbalenya, A.E., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Straße 7, 97078 Würzburg, Germany","Formation of the coronavirus replication-transcription complex involves the synthesis of large polyprotein precursors that are extensively processed by virus-encoded cysteine proteases. In this study, the coding sequence of the feline infectious peritonitis virus (FIPV) main protease, 3CLpro, was determined. Comparative sequence analyses revealed that FIPV 3CLpro and other coronavirus main proteases are related most closely to the 3C-like proteases of potyviruses. The predicted active centre of the coronavirus enzymes has accepted unique replacements that were probed by extensive mutational analysis. The wild-type FIPV 3CLpro domain and 25 mutants were expressed in Escherichia coli and tested for proteolytic activity in a peptide-based assay. The data strongly suggest that, first, the FIPV 3CLpro catalytic system employs His41 and Cys144 as the principal catalytic residues. Second, the amino acids Tyr160 and His162, which are part of the conserved sequence signature Tyr160-Met161-His162 and are believed to be involved in substrate recognition, were found to be indispensable for proteolytic activity. Third, replacements of Gly83 and Asn64, which were candidates to occupy the position spatially equivalent to that of the catalytic Asp residue of chymotrypsin-like proteases, resulted in proteolytically active proteins. Surprisingly, some of the Asn64 mutants even exhibited strongly increased activities. Similar results were obtained for human coronavirus (HCoV) 3CLpro mutants in which the equivalent Asn residue (HCoV 3CLpro Asn64) was substituted. These data lead us to conclude that both the catalytic systems and substrate-binding pockets of coronavirus main proteases differ from those of other RNA virus 3C and 3C-like proteases.",,"asparagine; aspartic acid; chymotrypsin; cysteine; cysteine proteinase; glycine; histidine; methionine; peptide; polyprotein; protein precursor; proteinase; tyrosine; virus enzyme; amino acid sequence; amino acid substitution; article; assay; catalysis; complex formation; controlled study; Coronavirus; data analysis; enzyme binding; enzyme substrate; Escherichia coli; molecular recognition; mutant; mutational analysis; nonhuman; nucleotide sequence; Potyvirus; priority journal; protein degradation; protein domain; protein expression; protein processing; protein synthesis; RNA virus; sequence analysis; virus replication; virus transcription; Coronavirus; Escherichia coli; Felidae; Feline infectious peritonitis virus; Potyvirus; RNA viruses","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N., Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature, 369, pp. 72-76; Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceedings of the National Academy of Sciences, USA, 97, pp. 5516-5521; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) Journal of Virology, 63, pp. 3693-3699; Bazan, J.F., Fletterick, R.J., Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications (1988) Proceedings of the National Academy of Sciences, USA, 85, pp. 7872-7876; Bergmann, E.M., Mosimann, S.C., Chernaia, M.M., Malcolm, B.A., James, M.N., The refined crystal structure of the 3C gene product from hepatitis A virus: Specific proteinase activity and RNA recognition (1997) Journal of Virology, 71, pp. 2436-2448; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) Journal of Virology, 71, pp. 900-909; Boniotti, B., Wirblich, C., Sibilia, M., Meyers, G., Thiel, H.J., Rossi, C., Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus (1994) Journal of Virology, 68, pp. 6487-6495; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO Journal, 6, pp. 3779-3785; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Archives of Virology, 142, pp. 629-633; Chouljenko, V.N., Lin, X.Q., Storz, J., Kousoulas, K.G., Gorbalenya, A.E., Comparison of genomic and predicted amino acid sequences of respiratory and enteric bovine coronaviruses isolated from the same animal with fatal shipping pneumonia (2001) Journal of General Virology, 82, pp. 2927-2933; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses (2000) Journal of General Virology, 81, pp. 1473-1484; de Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Edited by S.G. 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Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036190639
"Jahnecke V.S., Strauß H., Lindner A., Röpke M., Banholzer E., Bekendorf T.","6506757437;7202004835;7202329155;6603737224;6508087829;6508029247;","Influence of different vaccination protocols against neonatal calf diarrhea on specific antibody responses against rotavirus, coronavirus and E. coli F5 under field conditions [Felduntersuchung zum einfluss verschiedener impfregime im rahmen der mutterschutzimpfung auf die antikörperentwicklung gegen bovine rota- und coronaviren sowie das F5-antigen von E. coli bei milchkühen]",2002,"Tierarztliche Umschau","57","1",,"32","39",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036216977&partnerID=40&md5=7ffcc5c59ec8c7a8e6712bb3a83eb3bf","Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany","Jahnecke, V.S., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany; Strauß, H., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany; Lindner, A., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany; Röpke, M., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany; Banholzer, E., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany; Bekendorf, T., Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany","Serological and colostral responses against bovine rota- and coronavirus and Escherichia coli F5 (K99) antigen of one-hundred-nine pregnant Holstein Friesian cows were measured after applying different dam vaccination protocols, including control data from nonvaccinated pregnant cows. Furthermore, total immunoglobulin (IgG) and protein (TP) levels of calves originating from vaccinated or unvaccinated dams as well as disease frequencies including diarrhea within the first 2 weeks p.n. were determined. Cows were randomly allocated to five treatment groups. Group A (n=21) and B (n=20) were primovaccinated 1999/00 with a trivalent commercial vaccine containing live attenuated bovine rota- and coronavirus plus F5 antigen of E.coli (MLV), followed by booster vaccination 6 and 3 weeks a.p. (Group A) or 3 weeks a.p. only (Group B) with MLV in 2000/01. Cows from Group C (n=23) and D (n=22) were primovaccinated in 2000/01 with a commercial vaccine containing inactivated rota- and coronavirus plus F5 antigen of E.coli (INACT) at 3 weeks a.p. and with the MLV-vaccine at 6 and 3 weeks a.p., respectively. Animals from Group E (n=23) served as unvaccinated controls. The mean specific antibody titre against all three antigens was significantly (p<0,01-0,001) elevated in the serum of all vaccinated animals compared to control cows. In addition, cows primovaccinated with the MLV (Group D) had significantly (p<0,01) higher specific antibody titres at birth compared to the animals receiving one shot of the INACT-vaccine (Group C). Colostral antibodies against all three antigens had significantly (p<0,05-0,001) increased in all MLV-vaccine treated groups whereas INACT-vaccine treated animals had only significant (p<0,01) increases of F5 titres. Compared to these animals, colostrum of MLV-vaccinated cows contained significantly higher specific antibody titres. No difference could be observed in serological and colostral responses amongst animals from Group A and B, irrespective of the number of booster vaccinations given. These results demonstrate that the MLV-vaccine can significantly enhance the specific response of dams against bovine rota- and coronavirus and E.coli F5 at primo-vaccination and yearly booster as a prerequisite for enhanced lactogenic immunity in calves against neonatal calf diarrhea.","Calf; Dam; Diarrhea; Immunity; Lactogenic; Vaccination","antibody; immunoglobulin G; inactivated vaccine; live vaccine; prolactin; protein; antibody response; antibody titer; article; bacterial count; blood analysis; cattle; colostrum; controlled study; Coronavirus; cow; diarrhea; dose response; environment; Escherichia coli; immunity; morbidity; nonhuman; pregnancy; Rotavirus; time; vaccination","Baljer, G., Bachmann, P.A., Nachweis enteropathogener Escherichia-coli-stämme und rotaviren in kotproben von kälbern mit diarrhoe (1980) Zbl. Vet. Med. B, 27, pp. 608-615; Baljer, G., Eichhorn, W., Göbel, E., Wolf, M., Bachmann, P.A., Vorkommen und verbreitung wichtiger durchfallerreger bei neugeborehen kälbern in süddeutschland im zeitraum 1984 bis 1986 (1987) Tierärztl. Umschau, 42, pp. 56-65; Berchtold, M., Zaremba, W., Grunert, E., Kälberkrankheiten (1990) Neugeborenen- und Säuglingskunde der Tiere, pp. 304-315. , (K. Walser und H. Bostedt, Hrsg.), Ferdinand Enke Verlag, Stuttgart; Bürki, F., Möstl, K., Spiegl, E., Horvath, E., Szekely, H., Reduction of rotavirus-, coronavirus- and E. coli-associated calf-diarrheas in a large-size dairy herdby means of dam vaccination with a triple vaccine (1986) J. Vet. Med. B, 33, pp. 241-252; Bürki, F., Diagnose, häufigkeit und prophylaxe der wichtigsten viralen kälberdurchfälle (1985) Wien. Tierärztl. Mschr., 12, pp. 373-377; Butler, J.E., Synthesis and distribution of immunoglobulins (1973) J. Am. Vet. Med. Ass., 163, pp. 795-798; Crouch, C.F., Oliver, S., Hearle, D.C., Buckley, A., Chapman, A.J., Francis, M.J., Lactogenic immunity following vaccination of cattle with bovine coronavirus (2001) Vaccine, 19, pp. 189-196; Crouch, C.F., Oliver, S., Francis, M.J., Serological, colostral and milk responses of cows vaccinated with a single dose of a combined vaccine against rotavirus, coronavirus and Escherichia coli F5 (K99) (2001) Vet. Rec., 149, pp. 105-108; Dauvergne, M., Laporte, J., Reynaud, G., Soulebot, J.P., Brun, A., Espinasse, J., Vaccination of dams with a combined rotavirus-coronavirus vaccine to protect newborn calves against diarrhea (1983) Proceedings of the 4th International Symposium on Neonatal Diarrhea, pp. 424-432. , VIDO, Saskatchewan, Kanada; Dirksen, G., Kälberruhr in neuer sicht (1981) Prakt. Tierarzt 59, Collegium Vet., 8, pp. 42-45; Doll, K., Weirather, P., Küchle, H.-M., Kälberdurchfall als bestandsproblem: Betriebsinterne faktoren und häufige behandlungsfehler (1995) Prakt. Tierarzt, 76, pp. 995-1004; Elze, K., Der kälberdurchfall. Ursachen, krankheitsverlauf, krankheitsbilder und gegenmaßnahmen (1999) Milchpraxis, 37, pp. 178-182; Fernandez, F.M., Conner, M.E., Hodgins, D.C., Parawani, A.V., Nielsen, P.R., Crawford, S.E., Estes, M.K., Saif, L.J., Passive immunity to bovine rotavirus in newborn calves fed colostrum supplements from cows immunized with recombinant SA11 rotavirus core-like particle (CLP) or virus-like particle (VLP) vaccines (1998) Vaccine, 16, pp. 507-516; Frank, N.A., Kaneene, J.B., Management risk factors associated with calf diarrhea in Michigan dairy herds (1993) J. Dairy Sci., 76, pp. 1313-1323; Freitag, H., Wetzel, H., Espenkoetter, E., Zur prophylaxe der rota-corona-virus-bedingten kälberdiarrhoe (1984) Tierärztl. Umschau, 10, pp. 731-736; Glawischnig, E., Greber, N., Schlerka, G., Die dauertropfinfusion bei kälbern mit hochgradiger azidose (1990) Tierärztl. Umschau, 45, pp. 562-569; Guinee, P.A.M., Jansen, W.H., Detection of enterotoxigenicity and attachment factors in Escherichia coli strains of human, porcine and bovine origin, a comparative study (1979) Infect. Immun., 13, pp. 1369-1377; Heckert, H.P., Bardella, I., Virus-bedingte kälberdurchfälle-maßnahmen zur bekämpfung (1998) Handbuch der tierischen Veredelung '98. 23. Aufl., pp. 421-429. , Kamlage Verlag, Osnabrück; Hess, R.G., Bachmann, P.A., Eichhorn, W., Frahm, K., Plank, P., Stimulierung der laktogenen immunität des rindes gegenüber rotavirusinfektionen (1982) Fortschr. Veterinärmed, 35, pp. 103-108; Kohara, J., Hirai, T., Mori, K., Ishizaki, H., Tsunemitsu, H., Enhancement of passive immunity with maternal vaccine against newborn calf diarrhea (1997) J. Vet. Med. Sci., 59, pp. 1023-1025; Kurtz, W., Muttertierimpfung mit einer rota-corona-vakzine zur bekämpfung des kälberdurchfalles - Klinische erfahrungen (1982) Tierärztl. Umschau, 37, pp. 505-506; Möstl, K., Bürki, F., Incidence of diarrhea and of rotavirus- and coronavirus-shedding in calves whose dams had been vaccinated with an experimental oil-adjuvanted vaccine containing bovine rotavirus and bovine coronavirus (1988) J. Vet. Med., 35, pp. 186-196; Myers, L.L., Snodgrass, D.R., Colostral and milk antibody titers in cows vaccinated with modified live-rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Ass., 181, pp. 486-488; Myers, L.L., Snodgrass, D.R., Colostral milk antibody titers in cows vaccinated with a modified live-rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Ass., 181, pp. 486-488; Newby, T.J., Stokes, C.R., Bourne, F.J., Immunological activities of milk (1982) Vet. Immunol. Immunopathol., 3, pp. 67-94; Newstead, D.F., Carotene and immunoglobulin concentrations in the colostrum and milk of pasture-fed cows (1976) J. Dairy Res., 43, pp. 229-237; Norcross, N.L., Secretion and composition of colostrum and milk (1982) J. Am. Vet. Med. Ass., 181, pp. 1057-1060; Plöger, W., Buittkamp, J., Neumann, G., Bechmann, Reuss, U., Untersuchungen über die ursachen der kälbersterblichkeit im nordwestdeutschen küstengebiet (1980) Tierärztl. Umschau, 35, pp. 659-671; Porter, P., Immunoglobulins in bovine mammary secretions (1972) Immunology, 23, pp. 225-238; Saif, L.J., Smith, K.L., Keynote address: A review of rotavirus immunization of cows and passive protection in calves (1984) Proceedings of the 4th International Symposium on Neonatal Diarrhea, pp. 394-423. , Vet. Infect. Dis. Organ., Saskatchewan, Canada; Snodgrass, D.R., Fahey, K.L., Wells, P.W., Campbell, I., Whitelaw, A., Passive immunity in calf rotavirus infections. Maternal vaccination increases and prolongs immunoglobulin G1 antibody secretion in milk (1980) Infect. Immun., 28, pp. 344-349; Stengel, K.-H., (1998) Immunglobulin G - Bestimmungen im Blutserum neugeborener Kälber in den ersten zehn Lebenstagen sowie im Kolostrum deter Mütter mittels eines neu entwickelten kompetitiven ELISA, , Vet.-Med. Diss., Gießen; Stepanek, J., Salajka, E., Zuffa, A., Mensik, J., Franz, J., New polyvalent vaccine against intestinal infections in newborn calves (1987) Vetrinarni-Medicina, 32, pp. 65-80; Stumpf, G., (1986) Muttertier-Schutzimpfung: Theoretische Grundlagen - Praktische Anwendung, , Vet. Med. Diss., München; Wellemans, G., Van Opdenbosch, E., Postpartum antibody levels for rota, corona and BVD virus in the cow's milk (1981) Vl. Dierg. Tijdschr., 50, pp. 46-52; Wieda, J., Bengelsdorff, H.J., Bernhardt, D., Hungerer, K.D., Antibody levels in milk of vaccinated and unvaccinated cows against organisms of neonatal diarrhea (1987) J. Vet. Med., 34, pp. 495-503; Wilson, M.R., Duncan, J.R., Heistand, F., The influence of periparturient intramammary vaccination on immunoglobulin levels in bovine mammary secretions (1972) Immunology, 23, pp. 313-320; Woode, G.N., Jones, J., Bridger, J., Levels of colostral antibodies against neonatal calf diarrhea virus (1975) Vet. Rec., 97, pp. 148-149","Jahnecke, V.S.; Direktionsbereich Tiergesundheit, Postfach 49 49, 76032 Karlsruhe, Germany",,,00493864,,,,"German","Tierarztl. Umsch.",Article,"Final",,Scopus,2-s2.0-0036216977
"Guy J.S., Smith L.G., Breslin J.J., Pakpinyo S.","7202723649;37109180900;7004753945;6507113360;","Development of a competitive enzyme-linked immunosorbent assay for detection of turkey coronavirus antibodies",2002,"Avian Diseases","46","2",,"334","341",,12,"10.1637/0005-2086(2002)046[0334:DOACEL]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035992091&doi=10.1637%2f0005-2086%282002%29046%5b0334%3aDOACEL%5d2.0.CO%3b2&partnerID=40&md5=31f06c426701a56922ea9dea0987cc35","Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","Guy, J.S., Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Smith, L.G., Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Breslin, J.J., Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Pakpinyo, S., Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","A competitive enzyme-linked immunosorbent assay (cELISA) was developed for detection of turkey coronavirus (TCV) antibodies. The cELISA utilized a recombinant baculovirus (Autographa californica nuclear polyhedrosis virus)-expressed TCV nucleocapsid (N) protein and biotin-labeled TCV N protein-specific monoclonal antibody. Sensitivity and specificity of the cELISA for detection of TCV antibodies were determined by comparison with the indirect fluorescent antibody test (IFAT) with 1269 reference, experimentally derived, and field-origin sera. Sera with discordant cELISA and IFAT results were further evaluated by western immunoblot analyses. The cELISA detected antibodies specific for TCV and infectious bronchitis virus, a closely related coronavirus, but did not detect antibodies specific for other avian viruses. A high degree of concordance was observed between the cELISA and IFAT; sensitivity and specificity of the cELISA relative to IFAT were 92.9% and 96.2%, respectively. Western immunoblot analyses provided additional evidence of cELISA specificity. The findings indicate that the cELISA is a rapid, sensitive, and specific serologic test for detection of TCV antibodies in turkeys.","Baculovirus; Enzyme-linked immunosorbent assay; Turkey coronavirus","Autographa; Autographa californica; Autographa californica; Autographa californica nucleopolyhedrovirus; Aves; Avian infectious bronchitis virus; Coronavirus; Cypovirus; Galliformes; Meleagris gallopavo; Turkey coronavirus; unidentified baculovirus; unidentified nuclear polyhedrosis viruses; monoclonal antibody; virus antibody; animal; animal disease; antibody specificity; article; biosynthesis; bird disease; blood; comparative study; Coronavirus; enzyme linked immunosorbent assay; fluorescent antibody technique; hybridoma; immunology; isolation and purification; methodology; mouse; reproducibility; sensitivity and specificity; turkey (bird); Western blotting; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antibody Specificity; Blotting, Western; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Indirect; Hybridomas; Mice; Reproducibility of Results; Sensitivity and Specificity; Turkeys","Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Breslin, J.J., Smith, L.G., Guy, J.S., Baculovirus expression of turkey coronavirus nucleocapsid protein (2001) Avian Dis., 45, pp. 136-143; Carpenter, A.B., Enzyme-linked immunoassays (1992) Manual of clinical laboratory immunology, 4th ed., pp. 2-9. , N. E. Rose, E. C. de Macario, J. L. Fahey, H. Friedman, and G. M. Penn, eds. American Society for Microbiology, Washington, DC; Carter, P.B., Beegle, K.H., Gebhard, D.H., Monoclonal antibodies: Clinical use and potential (1986) Vet. Clin. North Am., 16, pp. 1171-1179; Fletcher, R.H., Fletcher, S.W., Wagner, E.H., Sensitivity and specificity (1983) Clinical epidemiology, pp. 46-48. , Williams and Wilkins, Baltimore, MD; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis from pheasants (1996) Vet. Rec., 138, pp. 208-209; Guy, J.S., New methods for diagnosis of turkey coronavirus infections (1998) Proc. 49th North Central Avian Disease Conference and Symposium on Enteric and Emerging Diseases, pp. 8-10. , Indianapolis, IN; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Harlow, E., Lane, D., Labeling antibodies (1988) Antibodies: a laboratory manual, pp. 340-341. , E. Harlow and D. Lane, eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Ignjatovic, J., Galli, L., Structural proteins of avian infectious bronchitis virus: Role in immunity and protection (1993) Adv. Exp. Med. Biol., 342, pp. 449-453; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , S. G. Siddell, ed. Plenum Press, New York; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of poultry, 10th ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Patel, B.L., Pomeroy, B.S., Gonder, E., Cronkite, C.E., Indirect fluorescent antibody test for the diagnosis of coronaviral enteritis of turkeys (bluecomb) (1976) Am. J. Vet. Res., 37, pp. 1111-1112; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning, a laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York; Siddell, S.G., The Coronaviridae an introduction (1995) The Coronaviridae, pp. 1-9. , S. G. Siddell, ed. Plenum Press, New York; Spackman, D., Cameron, I.D.R., Isolation of infectious bronchitis virus from pheasants (1983) Vet. Rec., 113, pp. 354-355; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Wege, H., Siddel, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200","Guy, J.S.; Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"12061642","English","Avian Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0035992091
"Carman S., Josephson G., McEwen B., Maxie G., Antochi M., Eernisse K., Nayar G., Halbur P., Erickson G., Nilsson E.","7003877448;7006244591;7202047510;7801433146;6506623227;6603301154;6701383269;7005935318;7102189282;7102718272;","Field validation of a commercial blocking ELISA to differentiate antibody to transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus and to identify TGEV-infected swine herds",2002,"Journal of Veterinary Diagnostic Investigation","14","2",,"97","105",,12,"10.1177/104063870201400202","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036517228&doi=10.1177%2f104063870201400202&partnerID=40&md5=c49fed971ff2421548f63a8cde2d4df8","Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; USDA, APHIS, NVSL, Ames, IA 50010-9359, United States; Veterinary Services, Manitoba Agriculture, Winnipeg, Man. R3T 556, Canada; Iowa State University, Veterinary Diagnostic Laboratory, Ames, IA 50011, United States; Rollins Anim. Dis. Diagn. Laboratory, Raleigh, NC 27605, United States; Svanova Biotech., S-751 83 Uppsala, Sweden","Carman, S., Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; Josephson, G., Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; McEwen, B., Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; Maxie, G., Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; Antochi, M., Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada; Eernisse, K., USDA, APHIS, NVSL, Ames, IA 50010-9359, United States; Nayar, G., Veterinary Services, Manitoba Agriculture, Winnipeg, Man. R3T 556, Canada; Halbur, P., Iowa State University, Veterinary Diagnostic Laboratory, Ames, IA 50011, United States; Erickson, G., Rollins Anim. Dis. Diagn. Laboratory, Raleigh, NC 27605, United States; Nilsson, E., Svanova Biotech., S-751 83 Uppsala, Sweden","A commercially available blocking ELISA was analyzed for its ability to identify antibodies to porcine coronaviruses (transmissible gastroenteritis virus [TGEV] or porcine respiratory coronavirus [PRCV]), to differentiate antibodies to TGEV and PRCV, and to identify TGEV-infected herds. Nine sera from uninfected pigs, 34 sera from 16 pigs experimentally infected with TGEV, and sera from 10 pigs experimentally infected with PRCV were evaluated using both the TGEV/PRCV blocking ELISA and a virus neutralization (VN) assay. The ELISA was not consistently effective in identifying pigs experimentally infected with TGEV until 21 days postinfection. Sera from 100 commercial swine herds (1,783 sera; median 15 per herd) were similarly evaluated using both tests. Thirty of these commercial herds had a clinical history of TGEV infection and a positive TGEV fluorescent antibody test recorded at necropsy within the last 35 months, while 70 herds had no history of clinical TGEV infection. The blocking ELISA and the VN showed good agreement (kappa 0.84) for the detection of porcine coronavirus antibody (TGEV or PRCV). The sensitivity (0.933) of the ELISA to identify TGEV-infected herds was good when considered on a herd basis. The ELISA was also highly specific (0.943) for the detection of TGEV-infected herds when the test results were evaluated on a herd basis. When sera from specific age groups were compared, the ELISA identified a greater proportion (0.83) of pigs in herds with TGEV antibody when suckling piglets were used. In repeatability experiments, the ELISA gave consistent results when the same sera were evaluated on different days (kappa 0.889) and when sera were evaluated before and after heating (kappa 0.888). The blocking ELISA was determined to be useful for herd monitoring programs and could be used alone without parallel use of the VN assay for the assessment of large swine populations for the detection of TGEV-infected herds.",,"virus antibody; animal; animal disease; article; Coronavirus; differential diagnosis; enzyme linked immunosorbent assay; evaluation; immunology; pathogenicity; reproducibility; respiratory tract infection; sensitivity and specificity; standard; swine; swine disease; Transmissible gastroenteritis virus; Animals; Antibodies, Viral; Coronavirus; Diagnosis, Differential; Enzyme-Linked Immunosorbent Assay; Gastroenteritis, Transmissible, of Swine; Reproducibility of Results; Respiratory Tract Infections; Sensitivity and Specificity; Swine; Swine Diseases; Transmissible gastroenteritis virus","Audige, L., Beckett, S., A quantitative assessment of the validity of animal-health surveys using stochastic modelling (1999) Prev Vet Med, 38, pp. 259-276; Brown, I.H., Paton, D.J., Serological studies of transmissible gastroenteritis in Great Britain, using a competitive ELISA (1991) Vet Rec, 128, pp. 500-503; Callebaut, P., Correa, I., Pensaert, M.B., Antigenic differentiation between TGEV of swine and a related porcine respiratory coronavirus (1988) J Gen Virol, 69, pp. 1725-1730; Callebaut, P., Pensaert, M.B., Hooyberghs, J., A competitive inhibition ELISA for the differentiation of serum antibodies from pigs infected with transmissible gastroenteritis virus (TGEV) or with the TGEV-related porcine respiratory coronavirus (1989) Vet Microbiol, 20, pp. 9-19; Cannon, R.M., Roe, R.T., (1986) Livestock Disease Surveys: A Field Disease Manual for Veterinarians, , Australian Government Publishing Service, Canberra, Australia; Gardner, I.A., Stryhn, H., Lind, P., Collins, M.T., Conditional dependence between tests affects the diagnosis and surveillance of animal diseases (2000) Prev Vet Med, 45, pp. 107-122; Garwes, D.J., Stewart, F., Cartwright, S.F., Brown, I., Differentiation of porcine coronavirus from transmissible gastroenteritis virus (1988) Vet Rec, 122, pp. 86-87; Jabrane, A., Elazhary, Y., Talbot, B.G., Porcine respiratory coronavirus in Quebec: Serological studies using a competitive inhibition enzyme-linked immunosorbent assay (1992) Can Vet J, 33, pp. 727-733; Jordan, D., McEwen, S., Herd-level test performance based on uncertain estimates of individual test performance, individual true prevalence and herd true prevalence (1998) Prev Vet Med, 36, pp. 187-209; Martin, S.W., Shoukri, M., Thorburn, M., Evaluating the health status of herds based on tests applied to individuals (1992) Prev Vet Med, 14, pp. 33-43; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Petrie, A., Watson, D., (1999) Statistics for Veterinary and Animal Science, , Blackwell Scientific Ltd., London, UK; Sackett, D.L., Haynes, R.B., Guyatt, G.H., Tugwell, P., (1991) Clinical Epidemiology: A Basic Science for Clinical Medicine, 2nd Ed., , Little, Brown, and Company, Toronto, Canada; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Disease of Swine, pp. 362-386. , ed. Leman AD, Straw BE, Mengeling WL, et al., 7th ed., Iowa State University Press, Ames, IA; Sestak, K., Zhou, Z., Shoup, D.I., Saif, L.J., Evaluation of the baculovirus-expressed S glycoprotein of transmissible gastroenteritis virus (TGEV) as antigen in a competition ELISA to differentiate porcine respiratory coronavirus from TGEV antibodies in pigs (1999) J Vet Diagn Invest, 11, pp. 205-214; Shoukri, M.M., Edge, V.L., (1996) Statistical Methods for Health Sciences, , CRC Press, London, UK; Simkins, R.A., Weilnau, P.A., Van Cott, J., Competition ELISA, using monoclonal antibodies to the transmissible gastroenteritis virus (TGEV) S protein, for serological differentiation of pigs infected with TGEV or porcine respiratory coronavirus (1993) Am J Vet Res, 54, pp. 254-259; Wesley, R.D., Woods, R.D., McKean, J.D., Prevalence of coronavirus antibodies in Iowa swine (1997) Can J Vet Res, 61, pp. 305-308","Carman, S.; Animal Health Laboratory, Laboratory Services Division, University of Guelph, Guelph, Ont. N1H 6R8, Canada",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"11939346","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0036517228
"Wesley R.","7103154080;","Neutralizing antibody decay and lack of contact transmission after inoculation of 3- and 4-day-old piglets with porcine respiratory coronavirus",2002,"Journal of Veterinary Diagnostic Investigation","14","6",,"525","527",,1,"10.1177/104063870201400617","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036834898&doi=10.1177%2f104063870201400617&partnerID=40&md5=0e60fd7d2c44071f5a82912901066ce9","National Animal Disease Center, Agricultural Research Service, USDA Ames, IA 50010, United States","Wesley, R., National Animal Disease Center, Agricultural Research Service, USDA Ames, IA 50010, United States","Ten female neonatal piglets were infected with porcine respiratory coronavirus (PRCV) to measure the decay of a specific neutralizing antibody. By 42 weeks after exposure, 1 of the gilts was serologically negative (<5) for PRCV, and by 48 weeks 2 more gilts were serologically negative. These data demonstrate that young mature gilts can be serologically negative, yet they could have been exposed to PRCV. Sentinel pigs were commingled with the PRCV-infected pigs at 8 weeks after exposure, and no virus transmission occurred.",,"virus antibody; animal; animal disease; article; Coronavirus; immunology; newborn; pathogenicity; serology; swine; swine disease; vaccination; virology; virus infection; Animals; Animals, Newborn; Antibodies, Viral; Coronavirus; Coronavirus Infections; Serologic Tests; Swine; Swine Diseases; Vaccination","Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-272; Onno, M., Jestin, A., Canolet, R., Vannier, P., Rapid diagnosis of TGEV-like coronavirus in fattened pigs by indirect immunofluorescence labelling in nasal cells (1989) J Vet Med B, 36, pp. 629-634; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; Pensaert, M., Cox, E., Van Deun, K., Callebaut, P., A seroepizootiological study of porcine respiratory coronavirus in Belgian swine (1993) Vet Q, 15, pp. 16-20; Sanchez, C.M., Gebauer, F., Sune, C., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; (1991) National Swine Survey. Morbidity/mortality and Health Management of Swine in the US, p. 10. , Nov. Fort Collins, CO; Van Reeth, K., Pensaert, M., Prevalence of infections with enzootic respiratory and enteric viruses in feeder pigs entering fattening herds (1994) Vet Rec, 135, pp. 594-597; Vaughn, H.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J Clin Microbiol, 32, pp. 1809-1812; Wesley, R.D., Woods, R.D., Induction of protective immunity against transmissible gastroenteritis virus after exposure of neonatal pigs to porcine respiratory coronavirus (1996) Am J Vet Res, 57, pp. 157-162; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J Vet Diagn Investig, 2, pp. 312-317; Wesley, R.D., Woods, R.D., McKean, J.D., Prevalence of coronavirus antibodies in Iowa swine (1997) Can J Vet Res, 61, pp. 305-308; Woods, R.D., Wesley, R.D., Kapke, P.A., Neutralization of transmissible gastroenteritis virus by complement dependent monoclonal antibodies (1988) Am J Vet Res, 49, pp. 300-304",,,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12423041","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0036834898
"Alonso S., Izeta A., Sola I., Enjuanes L.","57210695335;6602523425;7003336781;7006565392;","Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus",2002,"Journal of Virology","76","3",,"1293","1308",,51,"10.1128/JVI.76.3.1293-1308.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036145528&doi=10.1128%2fJVI.76.3.1293-1308.2002&partnerID=40&md5=6b190bef696b4ccb33ca18e2925c8f48","Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain","Alonso, S., Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain; Sola, I., Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain","The transcription regulatory sequences (TRSs) of the coronavirus transmissible gastroenteritis virus (TGEV) have been characterized by using a helper virus-dependent expression system based on coronavirus-derived minigenomes to study the synthesis of subgenomic mRNAs. The TRSs are located at the 5′ end of TGEV genes and include a highly conserved core sequence (CS), 5′-CUAAAC-3′, that is essential for mediating a 100- to 1,000-fold increase in mRNA synthesis when it is located in the appropriate context. The relevant sequences contributing to TRS activity have been studied by extending the CS 5′ upstream and 3′ downstream. Sequences from virus genes flanking the CS influenced transcription levels from moderate (10- to 20-fold variation) to complete mRNA synthesis silencing, as shown for a canonical CS at nucleotide (nt) 120 from the initiation codon of the S gene that did not lead to the production of the corresponding mRNA. An optimized TRS has been designed comprising 88 nt from the N gene TRS, the CS, and 3 nt 3′ to the M gene CS. Further extension of the 5′-flanking nucleotides (i.e., by 176 nt) decreased subgenomic RNA levels. The expression of a reporter gene (β-glucuronidase) by using the selected TRS led to the production of 2 to 8 μg of protein per 106 cells. The presence of an appropriate Kozak context led to a higher level of protein expression. Virus protein levels were shown to be dependent on transcription and translation regulation.",,"messenger RNA; virus protein; article; codon; Coronavirus; gene expression system; gene silencing; helper virus; nonhuman; nucleotide sequence; priority journal; protein expression; protein synthesis; regulatory sequence; reporter gene; RNA analysis; sequence analysis; transcription regulation; translation regulation; virus genome","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Alonso, S., Sola, I., Wege, H., Teifke, J., Balach, M., Plana-Durán, J., Enjuanes, L., Heterologous gene expression in tissue culture and in vivo using a transmissible gastroenteritis coronavirus helper dependent system J. Gen. Virol., , in press; Bronstein, I., Fortin, J.J., Voyta, J.C., Juo, R.-R., Edwards, B., Olenses, C.E.M., Lijam, N., Kricka, L.J., Chemiluminescent reporter gene assays: Sensitive detection of the GUS and SEAP gene products (1994) BioTechniques, 17, pp. 172-177; Dubensky, T.W., Driver, D.A., Polo, J.M., Belli, B.A., Latham, E.M., Ibanez, C.E., Chada, S., Chang, S.M.W., Sindbis virus DNA-based expression vectors: Utility for in vitro and in vivo gene transfer (1996) J. Virol., 70, pp. 508-519; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus taxonomy. Classification and nomenclature of viruses, pp. 835-849. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. 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Cell Biol., 115, pp. 887-903; Kozak, M., Structural features in eukaryotic mRNAs that modulate the initiation of translation (1991) J. Biol. Chem., 266, pp. 19867-19870; Krishnan, R., Chang, R.Y., Brian, D.A., Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the downstream-most initiation site (1996) Virology, 218, pp. 400-405; Lai, M.M.C., Cellular factors in the transcription and replication of viral RNA genomes: A parallel to DNA-dependent RNA transcription (1998) Virology, 244, pp. 1-12; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; La Monica, N., Yokomori, K., Lai, M.M.C., Coronavirus mRNA synthesis: Identification of novel transcription initiation signals which are differentially regulated by different leader sequences (1992) Virology, 188, pp. 402-407; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus messenger RNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Shieh, C.-K., Soe, L.H., Baker, S.C., Lai, M.C., Primary structure and translation of a defective interfering RNA of murine coronavirus (1988) Virology, 166, pp. 550-560; Mathews, D.H., Sabina, J., Zuker, M., Turner, D.H., Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure (1999) J. Mol. Biol., 288, pp. 911-940; McClurkin, A.W., Norman, J.O., Studies on transmissible gastro-enteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Vet. Sci., 30, pp. 190-198; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Ozdarendeli, A., Ku, S., Rochat, S., Williams, G.D., Senanayake, S.D., Brian, D.A., Downstream sequences influence the choice between a naturally occurring noncanonical and closely positioned upstream canonical heptameric fusion motif during bovine coronavirus subgenomic mRNA synthesis (2001) J. Virol., 75, pp. 7362-7374; Pasternak, A.O., Gultyaev, A.P., Spaan, W.J., Snijder, E.J., Genetic manipulation of arterivirus alternative mRNA leader-body junction sites reveals tight regulation of structural protein expression (2000) J. Virol., 74, pp. 11642-11653; Penzes, Z., González, J.M., Calvo, E., Izeta, A., Smerdou, C., Mendez, A., Sánchez, C.M., Enjuanes, L., Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the Purdue virus cluster (2001) Virus Genes, 23, pp. 105-118; Penzes, Z., González, J.M., Izeta, A., Muntion, M., Enjuanes, L., Progress towards the construction of a transmissible gastroenteritis coronavirus self-replicating RNA using a two-layer expression system (1998) Adv. Exp. Med. Biol., 440, pp. 319-327; Penzes, Z., Wroe, C., Brown, T.D.K., Britton, P., Cavanagh, D., Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame (1996) J. Virol., 70, pp. 8660-8668; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular cloning: A laboratory manual, 2nd ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sawicki, D.L., Wang, T., Sawicki, S.G., The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus (2001) J. Gen. Virol., 82, pp. 386-396; Sawicki, S.G., Sawicki, D.L., Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis (1990) J. Virol., 64, pp. 1050-1056; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-220; Schaad, M., Baric, R.S., Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates (1994) J. Virol., 68, pp. 8169-8179; Schlaman, H.R.M., Risseeuw, E., Franke-Van Dijk, M.E.I., Hooykaas, P.J.J., Nucleotide sequence corrections of the uidA open reading frame encoding β-glucuronidase (1994) Gene, 138, pp. 259-260; Sethna, P.B., Hung, S.-L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Shieh, C.-K., Soe, L.H., Makino, S., Chang, M.-F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genome: Implications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Thiel, V., Herold, J., Schelle, B., Siddell, S., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Thiel, V., Siddell, S.G., Herold, J., Replication and transcription of HCV 229E replicons (1998) Adv. Exp. Med. Biol., 440, pp. 109-114; Van der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Wertz, G.W., Perepelitsa, V.P., Ball, L.A., Gene rearrangement attenuates expression and lethality of a nonsegmented negative strand RNA virus (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 3501-3506; Wesley, R.D., Cheung, A.K., Michael, D.M., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence of 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Zuker, M., Mathews, D.H., Turner, D.H., Algorithms and thermodynamics for RNA secondary structure prediction: A practical guide (1999) RNA biochemistry and biotechnology, pp. 11-43. , J. Barciszewski and B. F. C. Clark (ed.). NATO ASI Series, Kluwer Academic Publishers, New York, N.Y","Enjuanes, L.; Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,"American Society for Microbiology",0022538X,,JOVIA,"11773405","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036145528
"Lin T.L., Loa C.C., Wu C.C., Bryan T., Hooper T., Schrader D.","57213499631;6602648721;7501664098;7005517787;7005121335;7007179253;","Antigenic relationship of turkey coronavirus isolates from different geographic locations in the United States",2002,"Avian Diseases","46","2",,"466","472",,7,"10.1637/0005-2086(2002)046[0466:AROTCI]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035992161&doi=10.1637%2f0005-2086%282002%29046%5b0466%3aAROTCI%5d2.0.CO%3b2&partnerID=40&md5=9a473007a03afa2ee16b3dddb516c425","Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Lin, T.L., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Loa, C.C., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","The purpose of the present study was to examine the antigenicity of turkey coronavirus (TCV) isolates from various geographic areas with antibodies to different viruses. Seventeen isolates of TCV were recovered from intestinal samples submitted to Animal Disease Diagnostic Laboratory, Purdue University, from turkey farms located in different geographic areas. The prototype TCV Minnesota isolate (TCV-ATCC) was obtained from the American Type Culture Collection. Intestinal sections were prepared from turkey embryos infected with different TCV isolates and reacted with polyclonal or monoclonal antibodies to TCV, infectious bronchitis virus (IBV), bovine coronavirus (BCV), transmissible gastroenteritis virus (TGEV), reovirus, rotavirus, adenovirus, or enterovirus in immunofluorescent antibody staining. All 18 TCV isolates have the same antigenic reactivity pattern with the same panel of antibodies. Positive reactivity was seen with polyclonal antibodies to the TCV Indiana isolate, the TCV Virginia isolate, TCV-ATCC, and the IBV Massachusetts strain as well as monoclonal antibodies to the TCV North Carolina isolate or the membrane protein of IBV. Antibodies to BCV or TGEV were not reactive with any of the TCV isolates. Reactivity of antibodies to unrelated virus, rotavirus, reovirus, adenovirus, or enterovirus with different TCV isolates was all negative, except positive response was seen between enterovirus antibody and a TCV western North Carolina isolate, suggesting coinfection of turkeys with TCV and enterovirus in that particular case. The results indicated that the TCV isolates from these geographic locations in the U.S. shared close antigenicity and were antigenically related to IBV.","Antigenicity; Infectious bronchitis virus; Turkey coronaviral enteritis; Turkey coronavirus","Adenoviridae; Animalia; Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; Enterovirus; Meleagris gallopavo; Reovirus sp.; Rotavirus; Transmissible gastroenteritis virus; Turkey coronavirus; monoclonal antibody; virus antibody; virus antigen; animal; animal disease; article; bird disease; classification; comparative study; Coronavirus; cross reaction; fluorescent antibody technique; genetics; geography; immunology; turkey (bird); United States; virology; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Coronavirus, Turkey; Cross Reactions; Enteritis, Transmissible, of Turkeys; Fluorescent Antibody Technique, Direct; Fluorescent Antibody Technique, Indirect; Geography; Turkeys; United States","Akin, A., Lin, T.L., Wu, C.C., Bryan, T.A., Hooper, T., Schrader, D., Nucleocapsid protein gene sequence analysis reveals close genomic relationship between turkey coronavirus and avian infectious bronchitis virus (2001) Acta Virol., 45, pp. 31-38; Breslin, J.J., Smith, L.G., Barnes, H.J., Guy, J.S., Comparison of virus isolation, immunohistochemistry, and reverse transcriptase-polymerase chain reaction procedures for detection of turkey coronavirus (2000) Avian Dis., 44, pp. 624-631; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Brim, T.A., VanCott, J.L., Lunney, J.K., Saif, L.J., Cellular immune responses of pigs after primary inoculation with porcine respiratory coronavirus or transmissible gastroenteritis virus and challenge with transmissible gastroenteritis virus (1995) Vet. Immunol. Immunopathol., 48, pp. 35-54; Cavanagh, D., A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathol., 30, pp. 109-115; Clark, S.R., Turkey coronavirus: A current review of epidemiology, economics and clinical variations (1998) Proc. 49th North Central Avian Disease Conference and Symposium on Enteric and Emerging Diseases, pp. 5-7. , Indianapolis, IN; Dea, S., Garzon, S., Identification of coronaviruses by the use of indirect protein A-gold immunoelectron microscopy (1991) J. Vet. Diagn. Invest., 3, pp. 297-305; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1986) Avian Dis., 30, pp. 319-326; Dea, S., Tijssen, P., Detection of turkey enteric coronavirus by enzyme-linked immunosorbent assay and differentiation from other coronaviruses (1989) Am. J. Vet. 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Raven Press, New York; Ismail, M.M., Cho, K.O., Ward, L.A., Saif, L.J., Saif, Y.M., Experimental bovine coronavirus in turkey poults and young chickens (2001) Avian Dis., 45, pp. 157-163; Karaca, K., Naqi, S., Gelb J., Jr., Production and characterization of monoclonal antibodies to three infectious bronchitis virus serotypes (1992) Avian Dis., 36, pp. 903-915; Kunkel, F., Herrler, G., Structural and functional analysis of the S proteins of two human coronavirus OC 43 strains adapted to growth in different cells (1996) Arch. Virol., 141, pp. 1123-1131; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Dis., 44, pp. 498-506; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Arch. Virol., 131, pp. 455-465; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Disease of poultry, 10th ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Ritchie, A.E., Desmukh, D.R., Larsen, C.T., Pomeroy, B.S., Electron microscopy of coronavirus-like particles characteristic of turkey bluecomb disease (1973) Avian Dis., 17, pp. 546-558; VanCott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Verbeek, A., Dea, S., Tijssen, P., Genomic relationship between turkey and bovine enteric coronaviruses identified by hybridization with BCV or TCV specific cDNA probes (1991) Arch. Virol., 121, pp. 199-211; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666; Vukina, T., Barnes, H.J., Solakoglu, M.N., Intervention decision model to prevent spiking mortality of turkeys (1998) Poult Sci., 77, pp. 950-955","Lin, T.L.; Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"12061660","English","Avian Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0035992161
"González J.M., Pénzes Z., Almazán F., Calvo E., Enjuanes L.","57201828108;55761804900;6603712040;12801394500;7006565392;","Stabilization of a full-length infectious cDNA clone of transmissible gastroenteritis coronavirus by insertion of an intron",2002,"Journal of Virology","76","9",,"4655","4661",,45,"10.1128/JVI.76.9.4655-4661.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036223622&doi=10.1128%2fJVI.76.9.4655-4661.2002&partnerID=40&md5=76d66b938bebbadecb6bb6c7edc57cc0","Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","González, J.M., Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Pénzes, Z., Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Almazán, F., Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Calvo, E., Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The stable propagation of a full-length transmissible gastroenteritis coronavirus (TGEV) cDNA in Escherichia coli cells as a bacterial artificial chromosome has been considerably improved by the insertion of an intron to disrupt a toxic region identified in the viral genome. The viral RNA was expressed in the cell nucleus under the control of the cytomegalovirus promoter and the intron was efficiently removed during translocation of this RNA to the cytoplasm. The insertion in two different positions allowed stable plasmid amplification for at least 200 generations. Infectious TGEV was efficiently recovered from cells transfected with the modified cDNAs.",,"complementary DNA; virus RNA; article; artificial chromosome; cell nucleus; Coronavirus; Cytomegalovirus; Escherichia coli; gastroenteritis; gene amplification; gene disruption; gene expression; gene insertion; gene translocation; genetic transfection; intron; molecular cloning; nonhuman; nucleotide sequence; plasmid; priority journal; promoter region; Transmissible gastroenteritis virus; virus genome; virus infectivity; virus transmission","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J. Virol., 71, pp. 734-737; Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., Reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) J. Virol., 75, pp. 12359-12369; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidovirales (2000) Virus taxonomy. Classification and nomenclature of viruses, pp. 827-834. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M, Lemon, D. J. McGeoch, J. Maniloff, M. A. Mayo, C. R. Pringle, and R. B. Wickner (ed.). Academic Press, New York, N.Y; Huang, Z., Fasco, M.J., Kaminsky, L.S., Optimization of DNase I removal of contaminating DNA from RNA for use in quantitative RNA-PCR (1996) BioTechniques, 20, pp. 1012-1020; Izeta, A., Smerdou, C., Alonso, S., Penzes, Z., Méndez, A., Plana-Durán, J., Enjuanes, L., Replication and packaging of transmissible gastroenteriris coronavirus-derived synthetic minigenomes (1999) J. Virol., 73, pp. 1535-1545; Johansen, I.E., Intron insertion facilitates amplification of cloned virus cDNA in Escherichia coli while biological activity is reestablished after transcription in vivo (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 12400-12405; Jones, P., Qiu, J., Rickwood, D., (1994) RNA isolation and analysis, pp. 15-46. , BIOS Scientific Publishers Ltd, Oxford, United Kingdom; Lewin, B., (1994) Genes V, pp. 999-1032. , Oxford University Press, Oxford, United Kingdom; Löpez-Moya, J.J., Garcia, J.A., Construction of a stable and highly infectious intron-containing cDNA clone of a plum pox potyvirus and its use to infect plants by particle bombardment (2000) Virus Res., 68, pp. 99-107; Méndez, A., Smerdou, C., Izeta, A., Gebauer, F., Enjuanes, L., Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity (1996) Virology, 217, pp. 495-507; Messerle, M., Crnkovic, I., Hammerschmidt, W., Ziegler, H., Koszinowski, U.U.H., Cloning and mutagenesis of a herpesvirus genome as an infectious bacterial artificial chromosome (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 14759-14763; Penzes, Z., González, J.M., Calvo, E., Izeta, A., Smerdou, C., Mendez, A., Sánchez, C.M., Enjuanes, L., Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the Purdue virus cluster (2001) Virus Genes, 23, pp. 105-118; Ruggli, N., Tratschin, J.D., Mittelholzer, C., Hofmann, M.A., Nucleotide sequence of classical swine fever virus strain Alfort/187 and transcription of infectious RNA from stably cloned full-length cDNA (1996) J. Virol., 70, pp. 3479-3487; Senapathy, P., Shapiro, M.B., Harris, N.L., Splice junctions, branch point sites, and exons: Sequence statistics, identification, and applications to genome project (1990) Methods Enzymol., 183, pp. 252-278; Shizuya, H., Birren, B., Kim, U.J., Mancino, V., Slepak, T., Tachiiri, Y., Simon, M., Cloning and stable maintenance of 300-kilobase -pair fragments of human DNA in Escherichia coli using an F-factor-based vector (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 8794-8797; Solovyev, V.V., Salamov, A.A., Lawrence, C.B., Predicting internal exons by oligonucleotide composition and discriminant analysis of spliceable open reading frames (1994) Nucleic Acids Res., 22, pp. 5156-5163; Thiel, V., Herold, J., Schelle, B., Siddell, S., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Wang, K., Boysen, C., Shizuya, H., Simon, M.I., Hood, L., Complete nucleotide sequence of two generations of a bacterial artificial chromosome cloning vector (1997) BioTechniques, 23, pp. 992-994; Yamshchikov, V., Mishin, V., Cominelli, F., A new strategy in design of (+)RNA virus infectious clones enabling their stable propagation in E. coli (2001) Virology, 281, pp. 272-280; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: The transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611","Enjuanes, L.; Department of Molecular Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,"American Society for Microbiology",0022538X,,JOVIA,"11932433","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036223622
"Kennedy M., Citino S., Hillis McNabb A., Serino Moffatt A., Gertz K., Kania S.","7402308045;7004240019;6504202227;6504239691;36904159400;24177256900;","Detection of feline coronavirus in captive Felidae in the USA",2002,"Journal of Veterinary Diagnostic Investigation","14","6",,"520","522",,22,"10.1177/104063870201400615","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036834066&doi=10.1177%2f104063870201400615&partnerID=40&md5=a82f432a142250da406eecf7c3f58108","University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States; White Oak Conservation Center, Yulee, FL, United States; Department of Comparative Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States","Kennedy, M., University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States, Department of Comparative Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States; Citino, S., White Oak Conservation Center, Yulee, FL, United States; Hillis McNabb, A., University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States; Serino Moffatt, A., University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States; Gertz, K., University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States; Kania, S., University of Tennessee, College of Veterinary Medicine, Knoxville, TN, United States","Feline coronavirus (FCoV) is an important pathogen of domestic and nondomestic Felidae. Investigation into the prevalence of FCoV in exotic Felidae has relied primarily on serology. The usefulness of genetic detection of FCoV using reverse transcription and nested polymerase chain reaction (RT/nPCR) for viral screening was investigated. Seventy-five biologic samples, primarily leces, from captive felids from 11 institutions were tested using PCR. Serum samples collected from all but 12 of these animals were tested for antibodies to type I and type II FCoV by indirect immunofluorescence. Twenty-four animals were positive using RT/nPCR for virus. Twenty-nine animals were seropositive to type I and/or type II FCoV. From serologic data, infection with a virus antigenically related to FCoV type 1 occurred most commonly. Serology did not correlate with virus shedding because 13 animals were seronegative to FCoV type I and II but positive using RT/nPCR for virus. Conversely, 20 animals were seropositive but negative using RT/nPCR for FCoV. Some of the populations in which virus was detected had experienced health problems, including feline infectious peritonitis (FIP), necrotizing colitis, and mild enteritis. In addition to its role in FIP, this virus may play a role in gastrointestinal diseases of infected animals. This study demonstrates that FCoV is a significant infectious agent of captive felids because over half of the animals tested were positive by viral genetic detection, serology, or both. Dependence upon one method for detection of infection is unreliable.",,"virus DNA; animal; animal disease; article; Carnivora; Coronavirus; epidemiology; female; gastrointestinal disease; immunology; male; pathogenicity; pathology; polymerase chain reaction; serology; United States; virology; virus infection; zoo animal; Animals; Animals, Zoo; Carnivora; Coronavirus Infections; Coronavirus, Feline; DNA, Viral; Female; Gastrointestinal Diseases; Male; Polymerase Chain Reaction; Seroepidemiologic Studies; Serologic Tests; United States","Evermann, J.F., Roelke, M.E., Briggs, M.B., Clinical and diagnostic features: Feline coronavirus infection of cheetahs (1986) Feline Pract, 16, pp. 21-30; Greene, C.E., (1990) Infectious Diseases of the Dog and Cat, pp. 300-313. , WB Saunders Company, Philadelphia, PA; Heeney, J.L., Evermann, J.F., McKeirnan, A.J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) J Virol, 64, pp. 1964-1972; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J Clin Microbiol, 33, pp. 684-689; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J Virol, 72, pp. 4508-4515; Hoskins, J.D., Coronavirus infection in cats (1993) Veterinary Clinics of North America: Small Animal Practice, pp. 1-16. , ed. Hoskins JD, Loar AS, WB Saunders Company, Philadelphia, PA; Kennedy, M.A., Brenneman, K., Millsaps, R.K., Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis (1998) J Vet Diagn Investig, 10, pp. 93-97; Kennedy, M.A., Dolorico, T., Hillis McNabb, A., Serology and genetic detection of feline coronavirus of cheetahs (Acinonyx jubatus) in the USA (2001) J Zoo Wildl Med, 32, pp. 25-30; Murray, D.L., Kapke, C.A., Evermann, J.F., Fuller, T.K., Infectious disease and the conservation of free-ranging large carnivores (1999) Anim Conserv, 2, pp. 241-254; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract., 23, pp. 7-20; Vennema, H., Rossen, J.W.A., Wesseling, J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 91, pp. 134-140; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Watt, N.J., MacIntyre, N.J., McOrist, S., An extended outbreak of infectious peritonitis in a closed colony of European wildcats (Felis silvestris) (1993) J Comp Pathol, 108, pp. 73-79","Kennedy, M.; Department of Comparative Medicine, University of Tennessee, PO Box 1071, Knoxville, TN 37901-1071, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12423039","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0036834066
"Popova R., Zhang X.","56579161100;55715175900;","The spike but not the hemagglutinin/esterase protein of bovine coronavirus is necessary and sufficient for viral infection",2002,"Virology","294","1",,"222","236",,29,"10.1006/viro.2001.1307","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036061578&doi=10.1006%2fviro.2001.1307&partnerID=40&md5=7e80ce4618c472f5895e730efe211bc5","Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States","Popova, R., Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States; Zhang, X., Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States","The spike (S) and hemagglutinin/esterase (HE) of bovine coronavirus (BCV) are the two envelope proteins that recognize the same receptor-determinant of 9-O-acetylneuraminic acid on host cells. However, the precise and relative roles of the two proteins in BCV infectivity remain elusive. To unequivocally determine their roles in viral cytopathogenicity, we developed a system in which phenotypically chimeric viruses were generated by infecting a closely related mouse hepatitis virus (MHV) in cells that stably express an individual BCV protein (S or HE). The chimeric viruses were then used to infect human rectal tumor (HRT)-18 cells that are permissive to BCV but are nonsusceptible to MHV. Using this approach, we found that the chimeric virus containing the BCV S protein on the virion surface entered and replicated in HRT-18 cells; this was specifically blocked by prior treatment of the virus with a neutralizing antibody specific to the BCV S protein, indicating that the BCV S protein is responsible for initiating chimeric virus infection. In contrast, chimeric viruses that contain biologically active and functional BCV HE protein on the surface failed to enter HRT-18 cells, indicating that the BCV HE protein alone is not sufficient for BCV infection. Taken together, these results demonstrate that the S protein but not the HE protein of BCV is necessary and sufficient for infection of the chimeric viruses in HRT-18 cells, suggesting that BCV likely uses the S protein as a primary vehicle to infect permissive cells. © 2002 Elsevier Science (USA).",,"chimeric protein; esterase; neutralizing antibody; virus envelope protein; virus hemagglutinin; vitronectin; article; cancer cell culture; chimera; controlled study; Coronavirus; cytopathogenic effect; hepatitis virus; human; human cell; infection sensitivity; nonhuman; phenotype; priority journal; protein expression; protein function; virion; virus infection; virus pathogenesis; virus replication; Bovinae; Bovine coronavirus; Coronavirus; Murine hepatitis virus","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176, pp. 296-301; Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Boireau, P., Cruciere, C., Laporte, J., Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) J. 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Med. Virol., 44, pp. 152-161; Zhang, X.M., Hinton, D.R., Cue, D., Stohlman, S.A., Lai, M.M.C., Expression of gamma interferon by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread and pathogenicity (1997) Virology, 233, pp. 327-338; Zhang, X.M., Hinton, D.R., Parra, B., Park, S., Liao, C.L., Lai, M.M.C., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Zhang, X.; Department of Microbiology, Univ. of Arkansas for Med. Sci., 4301 W. Markham St., Little Rock, AR 72205, United States; email: zhangxuming@uams.edu",,"Elsevier",00426822,,VIRLA,"11886280","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0036061578
"Ortego J., Escors D., Laude H., Enjuanes L.","35254237800;6507259181;7006652624;7006565392;","Generation of a replication-competent, propagation-deficient virus vector based on the transmissible gastroenteritis coronavirus genome",2002,"Journal of Virology","76","22",,"11518","11529",,102,"10.1128/JVI.76.22.11518-11529.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036828087&doi=10.1128%2fJVI.76.22.11518-11529.2002&partnerID=40&md5=cdd4af2df3698254173b02616d644332","Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain","Ortego, J., Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain; Escors, D., Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain; Laude, H., Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain; Enjuanes, L., Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain","Replication-competent propagation-deficient virus vectors based on the transmissible gastroenteritis coronavirus (TGEV) genome that are deficient in the essential E gene have been developed by complementation within E+ packaging cell lines. Cell lines expressing the TGEV E protein were established using the noncytopathic Sindbis virus replicon pSINrep21. In addition, cell lines stably expressing the E gene under the CMV promoter have been developed. The Sindbis replicon vector and the ectopic TGEV E protein did not interfere with the rescue of infectious TGEV from full-length cDNA. Recombinant TGEV deficient in the nonessential 3a and 3b genes and the essential E gene (rTGEV-Δ3abΔE) was successfully rescued in these cell lines. rTGEV-Δ3abΔE reached high titers (107 PFU/ml) in baby hamster kidney cells expressing porcine aminopeptidase N (BHK-pAPN), the cellular receptor for TGEV, using Sindbis replicon and reached titers up to 5 x 105 PFU/ml in cells stably expressing E protein under the control of the CMV promoter. The virus titers were proportional to the E protein expression level. The rTGEV-Δ3abΔE virions produced in the packaging cell line showed the same morphology and stability under different pHs and temperatures as virus derived from the full-length rTGEV genome, although a delay in virus assembly was observed by electron microscopy and virus titration in the complementation system in relation to the wild-type virus. These viruses were stably grown for &gt; 10 passages in the E+ packaging cell lines. The availability of packaging cell lines will significantly facilitate the production of safe TGEV-derived vectors for vaccination and possibly gene therapy.",,"complementary DNA; microsomal aminopeptidase; virus protein; virus receptor; virus vector; animal cell; article; cell strain BHK; cell structure; controlled study; Cytomegalovirus; electron microscopy; genetic complementation; nonhuman; priority journal; promoter region; protein expression; replicon; Sindbis virus; Transmissible gastroenteritis virus; viral gene therapy; virus assembly; virus gene; virus genome; virus recombinant; virus replication; virus titration; wild type","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. 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Virol., 60, pp. 131-139; Kafri, T., Van Praag, H., Ouyang, L., Gage, F.H., Verma, I.M., A packaging cell line for lentivirus vectors (1999) J. Virol., 73, pp. 576-584; Khromykh, A.A., Sedlak, P.L., Guyatt, K.J., Hall, R.A., Westaway, E.G., Efficient trans-complementation of the flavivirus Kunjin NS5 protein but not of the NS1 protein requires its coexpression with other components of the viral replicase (1999) J. Virol., 73, pp. 10272-10280; Khromykh, A.A., Sedlak, P.L., Westaway, E.G., Trans-complementation analysis of the flavivirus Kunjin ns5 gene reveals an essential role for translation of its N-terminal half in RNA replication (1999) J. Virol., 73, pp. 9247-9255; Konetschny, C., Holzer, G.W., Falkner, F.G., Retroviral vectors produced in the cytoplasmic vaccinia virus system transduce intron-containing genes (2002) J. Virol., 76, pp. 1236-1243; Kozarsky, K.F., Wilson, J.M., Gene therapy: Adenovirus vectors (1993) Curr. Opin. Genet. 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USA, 96, pp. 4598-4603; Pushko, P., Parker, M., Ludwing, G.V., Davis, N.L., Johnston, R.E., Smith, J.F., Replication-helper systems from attenuated Venezuelan equine encephalitis virus: Expression of heterologous genes in vitro and immunization against heterologous pathogens in vivo (1997) Virology, 239, pp. 389-401; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Risco, C., Muntión, M., Enjuanes, L., Carrascosa, J.L., Two types of virus-related particles are found during transmissible gastroenteritis virus morphogenesis (1998) J. Virol., 72, pp. 4022-4031; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine, 7th Ed., pp. 362-386. , A. D. Leman, B. E. Straw, W. L. Mengeling, S. D'Allaire, and D. J. Taylor (ed.). Wolfe Publishing Ltd., Ames, Iowa; Sawicki, D.L., Wang, T., Sawicki, S.G., The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus (2001) J. Gen. Virol., 82, pp. 386-396; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-220; Thaler, S., Schnierle, B.S., A packaging cell line generating CD4-specific retroviral vectors for efficient gene transfer into primary human T-helper lymphocytes (2001) Mol. Ther., 4, pp. 273-279; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Van Marie, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J.M., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Von Seggern, D.J., Kehler, J., Endo, R.I., Nemorow, G.R., Complementation of a fibre mutant adenovirus by packaging cell lines stably expressing the adenovirus type 5 fibre protein (1998) J. Gen. Virol., 79, pp. 1461-1468; Wu, N., Ataai, M.M., Production of viral vectors for gene therapy applications (2000) Curr. Opin. Biotechnol., 11, pp. 205-208","Enjuanes, L.; Department of Cell Biology, Ctro. Nac. de Biotecnología, Campus Universidad Autónoma, Cantoblanco, 28029 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,"American Society for Microbiology",0022538X,,JOVIA,"12388713","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036828087
"Matsuyama S., Taguchi F.","7201442043;7103209890;","Communication between S1N330 and a region in S2 of murine coronavirus spike protein is important for virus entry into cells expressing CEACAM1b receptor",2002,"Virology","295","1",,"160","171",,20,"10.1006/viro.2002.1391","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036057292&doi=10.1006%2fviro.2002.1391&partnerID=40&md5=0d3bb964c3a1773d5b6c2b96ba8b6258","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo, 187-8502, Japan","Matsuyama, S., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo, 187-8502, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo, 187-8502, Japan","The soluble receptor-resistant (srr) mutants, srr7 and srr11, isolated from a murine coronavirus, mouse hepatitis virus (MHV) JHMV, have an amino acid mutation at positions 1114 (Leu to Phe) and 65 (Leu to His), respectively, in the spike (S) protein. These mutants failed to efficiently infect BHK cells expressing CEACAM1b (BHK-R2), due to their low entry into this cell line, although they infected cells expressing CEACAM1a (BHK-R1) in a manner similar to that of wild-type (wt) JHMV cl-2 (Matsuyama and Taguchi, Virology 273, 80-89, 2000). Following the repeated passage of these mutants through BHK-R2 cells, viruses were no longer isolated from srr11-infected cells, while two distinct mutants, srr7A and srr7B, were obtained from srr7-infected cells. Srr7A and srr7B grew 2 log10 higher than srr7 and induced fusion in BHK-R2 cells, being similar to wt virus. In addition to the amino acid change at position 1114 that stemmed from parental srr7, srr7A and srr7B had mutations around position 280, corresponding to the third region of the S1N330 receptor-binding site (S1N330-III) common to all MHV strains examined thus far. Srr7A and srr7B S proteins showed high fusogenicity in both BHK-R1 and BHK-R2 cells, like the wt virus, while srr7Aa and srr7Ba S proteins, which had mutations in S1N330-III but not at amino acid 1114, exhibited profoundly reduced fusion activity in these cell lines. These findings suggest that communication between S1N330-III and the amino acid at position 1114 is important for efficient fusion activity in BHK-R2 cells. S1N330-III is a possible region in the S1 involved in viral entry into cells. © 2002 Elsevier Science (USA).",,"amino acid; ceacam1b receptor; histidine; leucine; phenylalanine; protein; protein s1n330; receptor; unclassified drug; virus protein; amino acid analysis; animal cell; article; binding site; cell fusion; cell membrane permeability; cell strain BHK; controlled study; Coronavirus; isolation procedure; Murine hepatitis coronavirus; mutation; nonhuman; priority journal; protein analysis; protein expression; receptor binding; solubility; virus infection; virus isolation; virus mutant; virus strain; wild type; Coronavirus; Murinae; Murine hepatitis virus","Aoki, Y., Aizaki, H., Shimoike, T., Tani, H., Ishii, K., Saito, I., Matsuura, Y., Miyamura, T., A human liver cell line exhibits efficeint translation of HCV RNAs produced by a recombinant adenovirus expressing T7 RNA polymerase (1998) Virology, 250, pp. 140-150; Beauchemin, Nomenclature announcement. 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Invest., 66, pp. 744-754; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219; Yamada, Y.K., Yabe, M., Sequence analysis of major structural proteins of newly isolated mouse hepatitis virus (2000) Exp. Anim., 49, pp. 61-66; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implication for the requirement of a second factor for virus infection (1992) J. Virol., 66, pp. 6931-6938; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Taguchi, F.; Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; email: taguchi@ncnp.go.jp",,"Elsevier",00426822,,VIRLA,"12033774","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0036057292
"Hasoksuz M., Hoet A.E., Loerch S.C., Wittum T.E., Nielsen P.R., Saif L.J.","6603236044;6602855175;7004696614;7004009529;7402902693;7102226747;","Detection of respiratory and enteric shedding of bovine coronaviruses in cattle in an Ohio feedlot",2002,"Journal of Veterinary Diagnostic Investigation","14","4",,"308","313",,45,"10.1177/104063870201400406","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036654832&doi=10.1177%2f104063870201400406&partnerID=40&md5=b26c13951c98b3578f72f2398196900f","Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Department of Animal Sciences, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 44691-4096, United States; Istanbul University, Veterinary Faculty, Department of Microbiology, Avcilar, 34850, Istanbul, Turkey; Universidad del Zulia, Facultad de Ciencias Veterinarias, Dept. Enfermedades Transmisibles, Maracaibo, Venezuela","Hasoksuz, M., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States, Istanbul University, Veterinary Faculty, Department of Microbiology, Avcilar, 34850, Istanbul, Turkey; Hoet, A.E., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States, Universidad del Zulia, Facultad de Ciencias Veterinarias, Dept. Enfermedades Transmisibles, Maracaibo, Venezuela; Loerch, S.C., Department of Animal Sciences, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH 44691-4096, United States; Nielsen, P.R., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States; Saif, L.J., Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States","Recently, bovine coronavirus (BCV) has been isolated from new cattle arrivals to feedlots, but the association between respiratory and enteric infections with BCV in feedlot cattle remains uncertain. Fecal and nasal swab samples from 85 Ohio Agricultural Research and Development Center (OARDC) feedlot cattle averaging 7 months of age were collected at arrival (0) and at 4, 7, 14, and 21 days postarrival (DPA). An antigen capture enzyme-linked immunosorbent assay (ELISA) was used to detect concurrent shedding of BCV in fecal and nasal samples. All samples ELISA positive for BCV were matched with an equal number of BCV ELISA-negative samples and analyzed by reverse transcription-polymerase chain reaction (RT-PCR) of the N gene. Paired sera were collected at arrival and 21 DPA and tested for antibodies to BCV using an indirect ELISA. Information on clinical signs, treatments provided, and cattle weights were collected. The overall rates of BCV nasal and fecal shedding were 48% (41/85) and 53% (45/85) by ELISA and 84% (71/85) and 96% (82/85) by RT-PCR, respectively. The peak of BCV nasal and fecal shedding occurred at 4 DPA. Thirty-two cattle (38%) showed concurrent enteric and nasal shedding detected by both tests. Eleven percent of cattle had antibody titers against BCV at 0 DPA and 91% of cattle seroconverted to BCV by 21 DPA. The BCV fecal and nasal shedding detected by ELISA and RT-PCR were statistically correlated with ELISA antibody seroconversion (P < 0.0001); however, BCV fecal and nasal shedding were not significantly related to clinical signs. Seroconversion to BCV was inversely related to average daily weight gains (P < 0.06). Twenty-eight respiratory and 7 enteric BCV strains were isolated from nasal and fecal samples of 32 cattle in HRT-18 cell cultures. These findings confirm the presence of enteric and respiratory BCV infections in feedlot calves. Further studies are needed to elucidate the differences between enteric and respiratory strains of BCV and their role in the bovine respiratory disease complex of feedlot cattle.",,"animal; animal disease; animal husbandry; article; cattle; cattle disease; Coronavirus; digestive system; enzyme linked immunosorbent assay; feces; immunology; male; nose cavity; pathogenicity; respiratory system; United States; virology; virus infection; virus shedding; Animal Husbandry; Animals; Cattle; Cattle Diseases; Coronavirus Infections; Coronavirus, Bovine; Digestive System; Enzyme-Linked Immunosorbent Assay; Feces; Male; Nasal Cavity; Ohio; Respiratory System; Virus Shedding","Cho, K.O., Hasoksuz, M., Nielsen, P.R., Cross-protection studies between respiratory and calf diarrhea and winter dysentery coronavirus strains in calves and RT-PCR and nested PCR for their detection (2001) Arch Virol, 146, pp. 2401-2419; Cho, K.O., Hoet, A., Loerch, S.C., Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle (2001) Am J Vet Res, 62, pp. 1436-1441; Clark, M.A., Bovine coronavirus (1993) Br Vet J, 149, pp. 51-70; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Sem Virol, 8, pp. 33-47; Filion, L.G., Willson, P.J., Bielefeldt-Ohmann, H., The possible role of stress in the induction of pneumonic pasteurellosis (1984) Can J Comp Med, 48, pp. 268-274; Fuente, F., Luzon, M., Ruiz-Santa-Quiteria, J.A., Cryptosporidium and concurrent infections with other major enterophathogens in 1 to 30 day old diarrheic dairy calves in central Spain (1999) Vet Parasitiol, 80, pp. 179-185; Ganaba, R., Belanger, D., Dea, S., Poulin, M.B., A seroepidemiological study of the importance in cow-calf pairs of respiratory and enteric viruses in beef operations from northwestern Quebec (1995) Can J Vet Res, 59, pp. 26-33; Gelinas, A.M., Boutin, M., Sasseville, A.M.J., Dea, S., Bovine coronaviruses associated with enteric and respiratory diseases in Canadian dairy cattle display different reactivities to anti-HE monoclonal antibodies and distinct amino acid changes in their HE, S and ns4.9 protein (2001) Virus Res, 76, pp. 43-57; Hasoksuz, M., Lathrop, S.L., Al-dubaib, M.A., Antigenic variation among bovine enteric coronaviruses (BECV) and bovine respiratory coronaviruses (BRCV) detected using monoclonal antibodies (1999) Arch Virol, 144, pp. 2441-2447; Hasoksuz, M., Lathrop, S.L., Gadfield, K.J., Saif, L.J., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am J Vet Res, 60, pp. 1227-1233; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Lathrop, S.L., Wittum, T.E., Brock, K.V., Saif, L.J., Association between bovine coronavirus respiratory tract attributable to bovine coronavirus and health and growth performance of feedlot cattle (2000) Am J Vet Res, 61, pp. 1062-1066; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Saif, L.J., Antibody titers against bovine coronavirus and shedding of the virus via the respiratory tract in feedlot cattle (2000) Am J Vet Res, 61, pp. 1057-1061; Martin, S.W., Nagy, E., Shewen, P.E., Harland, R.J., The association of titer to bovine coronavirus with treatment for bovine respiratory disease and weight gain in feedlot calves (1998) Can J Vet Res, 62, pp. 257-261; Naciri, M., Lefay, M.P., Mancassola, R., Role of Cryptosporidium parvum as a pathogen in neonatal diarrhea complex in suckling and dairy calves in France (1999) Vet Parasitol, 85, pp. 245-257; Reynolds, D.J., Debney, T.G., Hall, G.A., Studies on the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Arch Virol, 85, pp. 71-83; Saif, L.J., Brock, K.V., Redman, D.R., Kohler, E.M., Winter dysentery in dairy herds: Electron microscopic and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Saif, L.J., Heckert, R.A., Enteropathogenic coronaviruses (1990) Viral Diarrheas of Man and Animals, pp. 185-252. , ed. Saif LJ, Theil KW, 1st ed., CRC Press, Boca Raton, FL; Saif, L.J., Heckert, R.A., Miller, K.L., Tarek, M.M., Cell culture propagation of bovine coronaviruses (1988) J Tiss Cult Methods, 11, pp. 139-145; Saif, L.J., Redman, D.R., Moorhead, P.D., Experimentally induced coronavirus infections in calves: Viral replication in the respiratory and intestinal tracts (1986) Am J Vet Res, 47, pp. 1426-1432; Silva, M.R., O'Reilly, K.L., Lin, X., Sensitivity comparison for detection of respiratory bovine coronaviruses in nasal samples from feedlot cattle by ELISA and isolation with the G clone of HRT-18 cells (1999) J Vet Diagn Invest, 11, pp. 15-19; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Saif, L.J., Evaluation of two antigen-capture ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Stephens, D.B., Stress and its measurement in domestic animals: A review of behavioral and physiological studies under field and laboratory situations (1980) Adv Vet Sci Comp Med, 24, pp. 179-210; Storz, J., Lin, X., Purdy, C.W., Coronavirus and Pusteurella infections in bovine shipping fever pneumonia and Evan's criteria for causation (2000) J Clin Microbiol, 38, pp. 3291-3298; Storz, J., Purdy, C.W., Lin, X., Isolation of respiratory bovine coronavirus. other cytocidal viruses, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J Am Vet Med Assoc, 216, pp. 1599-1604; Thomas, L.H., Gourlay, R.N., Stott, E.J., A search for new microorganisms in calf pneumonia by the inoculation of gnotobiotic calves (1982) Res Vet Sci, 33, pp. 170-182; Thomson, R.G., Pathology and pathogenesis of the common diseases of the respiratory tract of cattle (1974) Can Vet J, 15, pp. 249-251; Traven, M., Sundberg, J., Larsson, B., Niskanen, R., Winter dysentery diagnosed by farmers in dairy herds in central Sweden: Incidence, clinical signs and protective immunity (1993) Vet Rec, 133, pp. 315-318; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch Virol, 140, pp. 1303-1311; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J Vet Med Sci, 53, pp. 433-437; Zhang, X., Herbst, W., Kousoulas, K.G., Storz, J., Comparison of the S genes and the biological properties of respiratory and enteropathogenic bovine coronaviruses (1994) Arch Virol, 134, pp. 421-426","Hasoksuz, M.; Dept. of Vet. Preventive Medicine, Ohio Agric. R. and D. Center, Ohio State University, Wooster, OH 44691-4096, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12152810","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0036654832
"Cowley J.A., Dimmonck C.M., Walker P.J.","7102947876;6504399635;7403666485;","Gill-associated nidovirus of Penaeus monodon prawns transcribes 3′-coterminal subgenomic mRNAs that do not possess 5′-leader sequences",2002,"Journal of General Virology","83","4",,"927","935",,51,"10.1099/0022-1317-83-4-927","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036206098&doi=10.1099%2f0022-1317-83-4-927&partnerID=40&md5=10f830d98f92116e24880286d261b133","Coop. Res. Center for Aquaculture, CSIRO Livestock Industries, Long Pocket Laboratories, 120 Meiers Road, Indooroopilly, 4068, Australia","Cowley, J.A., Coop. Res. Center for Aquaculture, CSIRO Livestock Industries, Long Pocket Laboratories, 120 Meiers Road, Indooroopilly, 4068, Australia; Dimmonck, C.M., Coop. Res. Center for Aquaculture, CSIRO Livestock Industries, Long Pocket Laboratories, 120 Meiers Road, Indooroopilly, 4068, Australia; Walker, P.J., Coop. Res. Center for Aquaculture, CSIRO Livestock Industries, Long Pocket Laboratories, 120 Meiers Road, Indooroopilly, 4068, Australia","Sequence analysis of the ∼ 20 kb 5′-terminal portion of the ssRNA genome of gill-associated virus (GAV) of Penaeus monodon prawns has previously established that it contains an ORF1a-1b replicase gene equivalent to those of the coronavirus and arterivirus members of the order Nidovirales. Sequence analysis of the remaining ∼ 6.2 kb of the GAV genome downstream of ORF1a-1b to a 3′-poly(A) tail has identified two highly conserved intergenic sequences in which 29/32 nucleotides are conserved. Northern hybridization using probes to the four putative GAV ORFs and either total or poly(A)-selected RNA identified two 3′-coterminal subgenomic (sg) mRNAs of ∼ 6 kb and ∼ 5.5 kb. Primer extension and 5′-RACE analyses showed that the sgmRNAs initiate at the same 5′-AC positions in the central region of the two conserved intergenic sequences. Neither method provided any evidence that the GAV sgmRNAs are fused to genomic 5′-leader RNA sequences as is the case with vertebrate coronaviruses and arteriviruses. Intracellular double-stranded (ds)RNAs equivalent in size to the 26.2 kb genomic RNA and two sgRNAs were also identified by RNase/DNase digestion of total RNA from GAV-infected prawn tissue. The identification of only two sgmRNAs that initiate at the same position in conserved intergenic sequences and the absence of 5′-genomic leader sequences fused to these sgmRNAs confirms that GAV has few genes and suggests that it utilizes a transcription mechanism possibly similar to the vertebrate toroviruses but distinct from coronaviruses and arteriviruses.",,"deoxyribonuclease; double stranded RNA; genomic RNA; messenger RNA; primer RNA; ribonuclease; RNA directed RNA polymerase; virus protein; virus RNA; 3' untranslated region; 5' untranslated region; Arterivirus; article; controlled study; Coronavirus; Crustacea; gene amplification; gene fusion; gene identification; gene probe; genetic conservation; genetic transcription; gill; nidovirus; nonhuman; Northern blotting; nucleotide sequence; open reading frame; priority journal; RNA degradation; RNA hybridization; RNA sequence; RNA virus; sequence analysis; Torovirus; virus genome; virus infection; Arterivirus; Coronavirus; Crustacea; Decapoda (Crustacea); Gill-associated virus; Monodon; Nidovirales; Penaeus monodon; Penaeus monodon; RNA viruses; Torovirus; Vertebrata","Almeida, T.A., Pérez, J.A., Pinto, F.M., Size-fractionation of RNA by hot-agarose electrophoresis (2000) Biotechniques, 28, pp. 414-416; Baric, R.S., Yount, B., Subgenomic negative-strand RNA function during mouse hepatitis virus infection (2000) Journal of Virology, 74, pp. 4039-4046; Boonyaratpalin, S., Supamattaya, K., Kasornchandra, J., Direkbusaracom, S., Aekpanithanpong, U., Chantanachookin, C., Non-occluded baculo-like virus, the causative agent of yellow-head disease in the black tiger shrimp (Penaeus monodon) (1993) Fish Pathology, 28, pp. 103-109; Chantanachookin, C., Boonyaratpalin, S., Kasornchandra, J., Sataporn, D., Ekpanithanpong, U., Supamataya, K., Sriurairatana, S., Flegel, T.W., Histology and ultrastructure reveal a new granulosis-like virus in Penaeus monodon affected by yellow-head disease (1993) Diseases of Aquatic Organisms, 17, pp. 145-157; Cowley, J.A., Dimmock, C.M., Wongteerasupaya, C., Boonsaeng, V., Panyim, S., Walker, P.J., Yellow head virus from Thailand and gill-associated virus from Australia are closely related but distinct viruses (1999) Diseases of Aquatic Organisms, 36, pp. 153-157; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Detection of Australian gill-associated virus (GAV) and lymphoid organ virus (LOV) of Penaeus monodon by RT-nested PCR (2000) Diseases of Aquatic Organisms, 36, pp. 153-157; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses (2000) Journal of General Virology, 81, pp. 1473-1484; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: Molecular evidence for the first invertebrate nidovirus (2001) The Nidoviruses, pp. 43-48. , Edited by E. Lavi, S.R. Weiss & S.T. Hingley. 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"Glansbeek H.L., Haagmans B.L., Te Lintelo E.G., Egberink H.F., Duquesne V., Aubert A., Horzinek M.C., Rottier P.J.M.","6601911437;6701371301;6506152996;7004767057;6602303047;24368235900;7102624836;7006145490;","Adverse effects of feline IL-12 during DNA vaccination against feline infectious peritonitis virus",2002,"Journal of General Virology","83","1",,"1","10",,36,"10.1099/0022-1317-83-1-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036135793&doi=10.1099%2f0022-1317-83-1-1&partnerID=40&md5=78d30b69e25e0d7da0415f0c2bb9249b","Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Glansbeek, H.L., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Haagmans, B.L., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Te Lintelo, E.G., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Egberink, H.F., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Duquesne, V., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Aubert, A., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Horzinek, M.C., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands","Cell-mediated immunity is thought to play a decisive role in protecting cats against feline infectious peritonitis (FIP), a progressive and lethal coronavirus disease. In view of the potential of DNA vaccines to induce cell-mediated responses, their efficacy to induce protective immunity in cats was evaluated. The membrane (M) and nucleocapsid (N) proteins were chosen as antigens, because antibodies to the spike (S) protein of FIP virus (FIPV) are known to precipitate pathogenesis. However, vaccination by repeated injections of plasmids encoding these proteins did not protect kittens against challenge infection with FIPV. Also, a prime-boost protocol failed to afford protection, with priming using plasmid DNA and boosting using recombinant vaccinia viruses expressing the same coronavirus proteins. Because of the role of IL-12 in initiating cell-mediated immunity, the effects of co-delivery of plasmids encoding the feline cytokine were studied. Again, IL-12 did not meet expectations-on the contrary, it enhanced susceptibility to FIPV challenge. This study shows that DNA vaccination failed to protect cats against FIP and that IL-12 may yield adverse effects when used as a cytokine adjuvant.",,"complementary DNA; cytokine; DNA vaccine; interleukin 12; M protein; plasmid DNA; recombinant vaccine; type II site specific deoxyribonuclease; virus antibody; virus antigen; virus protein; adjuvant therapy; animal experiment; animal model; article; cat; cellular immunity; clinical protocol; controlled study; Coronavirus; drug efficacy; female; gene delivery system; genetic code; immunoprophylaxis; infection prevention; nonhuman; peritonitis; priority journal; protein expression; provocation test; vaccination; virus envelope; virus immunity; virus infection; virus pathogenesis; Animalia; Coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus; RNA viruses; Vaccinia virus","Addie, D.D., Jarrett, J.O., A study of naturally occurring coronavirus infections in kittens (1992) Veterinary Research, 130, pp. 133-137; Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Laboratory Animal Science, 34, pp. 592-597; Barlough, J.E., Johnson-Lussenburg, C.M., Stoddart, C.A., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis virus (1985) Canadian Journal of Comparative Medicine, 49, pp. 303-307; Boretti, F.S., Leutenegger, C.M., Mislin, C., Hofmann-Lehmann, R., Konig, S., Schroff, M., Junghans, C., Lutz, H., Protection against FIV challenge infection by genetic vaccination using minimalistic DNA constructs for FIV env gene and feline IL-12 expression (2000) AIDS, 14, pp. 1749-1757; Chow, Y.H., Chiang, B.L., Lee, Y.L., Chi, W.K., Lin, W.C., Chen, Y.T., Tao, M.H., Development of Th1 and Th2 populations and the nature of immune responses to hepatitis B virus DNA vaccines can be modulated by codelivery of various cytokine genes (1998) Journal of Immunology, 160, pp. 1320-1329; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J.D., Characterization of a temperature-sensitive feline infectious peritonitis coronavirus (1989) Archives of Virology, 109, pp. 185-196; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) Journal of Virology, 66, pp. 6695-6705; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A.A.P.M., Horzinek, M.C., Lutz, H., Placebo-controlled evaluation of a modified live virus vaccine against feline infectious peritonitis: Safety and efficacy under field conditions (1997) Vaccine, 15, pp. 1101-1109; Gately, M.K., Chizzonite, R., Presky, D.H., Measurement of human and mouse interleukin-12 (1997) Current Protocols in Immunology, pp. 6.16.1-6.16.15. , Edited by J. 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Yokoyama, M., Hassett, D.E., Zhang, J., Whitton, J.L., DNA immunization can stimulate florid local inflammation, and the antiviral immunity induced varies depending on injection site (1997) Vaccine, 15, pp. 553-560","Glansbeek, H.L.; Virology Division, Dept. of Infectious Dis./Immunology, Utrecht University, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: H.Glansbeek@vet.uu.nl",,"Society for General Microbiology",00221317,,JGVIA,"11752695","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036135793
"Corse E., Machamer C.E.","36957600500;7004585797;","The cytoplasmic tail of infectious bronchitis virus E protein directs golgi targeting",2002,"Journal of Virology","76","3",,"1273","1284",,63,"10.1128/JVI.76.3.1273-1284.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036145302&doi=10.1128%2fJVI.76.3.1273-1284.2002&partnerID=40&md5=359bee3c9393040271bac4832ba38304","Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","Corse, E., Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States; Machamer, C.E., Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, United States","We have previously shown that the E protein of the coronavirus infectious bronchitis virus (IBV) is localized to the Golgi complex when expressed exogenously from cDNA. Here, we report that neither the transmembrane domain nor the short lumenal domain of IBV E is required for Golgi targeting. However, an N-terminal truncation containing only the cytoplasmic domain (CTE) was efficiently localized to the Golgi complex, and this domain could retain a reporter protein in the Golgi. Thus, the cytoplasmic tail of the E protein is necessary and sufficient for Golgi targeting. The IBV E protein is palmitoylated on one or two cysteine residues adjacent to its transmembrane domain, but palmitoylation was not required for proper Golgi targeting. Using C-terminal truncations, we determined that the IBV E Golgi targeting information is present between tail amino acids 13 and 63. Upon treatment with brefeldin A, both the E and CTE proteins redistributed to punctate structures that colocalized with the Golgi matrix proteins GM130 and pl15 instead of being localized to the endoplasmic reticulum like Golgi glycosylation enzymes. This suggests that IBV E is associated with the Golgi matrix through interactions of its cytoplasmic tail and may have interesting implications for coronavirus assembly in early Golgi compartments.",,"cysteine; protein e; unclassified drug; virus protein; amino terminal sequence; article; Avian infectious bronchitis virus; carboxy terminal sequence; Coronavirus; Golgi complex; nonhuman; priority journal; protein expression; protein localization; protein structure; protein targeting","Andersson, A.M., Melin, L., Bean, A., Pettersson, R.F., A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus virus) membrane glycoprotein (1997) J. Virol., 71, pp. 4717-4727; Andersson, A.M., Pettersson, R.F., Targeting of a short peptide derived from the cytoplasmic tail of the G1 membrane glycoprotein of Uukuniemi virus virus (Bunyaviridae) to the Golgi complex (1998) J. 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"Chen C.-J., Makino S.","56288577100;7403067550;","Murine coronavirus-induced apoptosis in 17Cl-1 cells involves a mitochondria-mediated pathway and its downstream caspase-8 activation and bid cleavage",2002,"Virology","302","2",,"321","332",,34,"10.1006/viro.2002.1626","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036436730&doi=10.1006%2fviro.2002.1626&partnerID=40&md5=c085ff4b99dabc0480064bb073fa652c","Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555-1019, United States; Department of Microbiology, Institute of Molecular and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","Chen, C.-J., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555-1019, United States, Department of Microbiology, Institute of Molecular and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Makino, S., Department of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, TX 77555-1019, United States, Department of Microbiology, Institute of Molecular and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","Mouse hepatitis virus (MHV) infection in murine 17Cl-1 cells results in apoptotic cell death. Inhibition of MHV-induced apoptosis by the pancaspase inhibitor Z-VAD-FMK promoted virus production late in infection, indicating that apoptosis could be a host response to limit the production of viral progeny. Activation of the mitochondria-mediated apoptotic pathway was indicated by the activation of caspase-9 and delay of apoptosis by Bcl-2 overexpression. Analyses of the subcellular distribution of cytochrome c, procaspase-9, and Apaf-1 suggested an aberrant apoptosome formation in the vicinity of the mitochondria, which could be a cell type-specific event. An increase in the amount of Fas (APO-1/CD95), caspase-8 activation, caspase-8-mediated Bid cleavage, and subsequent translocation of truncated Bid to mitochondria, all of which relate to the Fas-mediated pathway, also occurred in MHV-infected 17Cl-1 cells, whereas the formation of the death-inducing signaling complex, a direct indication of the activation of Fas-mediated pathway, was undetectable. Caspase-8 and Bid activation appeared to be downstream of mitochondria, because Bcl-2 overexpression suppressed both events, suggesting that infected 17Cl-1 cells might have activated a receptor-mediated ""type II"" signaling pathway, in which primary and low levels of receptor-mediated pathway activation lead to the activation of the mitochondria-mediated pathway. 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Biol. Chem., 274, pp. 11549-11556","Makino, S.; Department of Microbiology, University of Texas Medical Branch, MRB 4.146, 301 University Blvd., Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,"Academic Press Inc.",00426822,,VIRLA,"12441076","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0036436730
"Phillips J.J., Chua M.M., Rall G.F., Weiss S.R.","7404582468;7006092803;35579903600;57203567044;","Murine coronavirus spike glycoprotein mediates degree of viral spread, inflammation, and virus-induced immunopathology in the central nervous system",2002,"Virology","301","1",,"109","120",,64,"10.1006/viro.2002.1551","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036396869&doi=10.1006%2fviro.2002.1551&partnerID=40&md5=7884fc9bb74cdb1b2541674bb59c45a6","Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Division of Basic Science, Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, PA 19111, United States","Phillips, J.J., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Chua, M.M., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States; Rall, G.F., Division of Basic Science, Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, PA 19111, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104-6076, United States","The mouse hepatitis virus (MHV) spike glycoprotein is a major determinant of neurovirulence. We investigated how alterations in spike affect neurovirulence using two isogenic recombinant viruses differing exclusively in spike. S4R, containing the MHV-4 spike gene, is dramatically more neurovirulent than SA59R, containing the MHV-A59 spike gene (J. J. Phillips, M. M. Chua, E. Lavi, and S. R. Weiss, 1999, J. Virol. 73, 7752-7760). We examined the contribution of differences in cellular tropism, viral spread, and the immune response to infection to the differential neurovirulence of S4R and SA59R. MHV-4 spike-mediated neurovirulence was associated with extensive viral spread in the brain in both neurons and astrocytes. Infection of primary hippocampal neuron cultures demonstrated that S4R spread more rapidly than SA59R and suggested that spread may occur between cells in close physical contact. In addition, S4R infection induced a massive influx of lymphocytes into the brain, a higher percentage of CD8+ T cells, and a higher frequency of MHV-specific CD8+ T cells relative SA59R infection. Despite this robust and viral-specific immune response to S4R infection, infection of RAG1-/- mice suggested that immune-mediated pathology also contributes to the high neurovirulence of S4R. © 2002 Elsevier Science (USA).",,"CD8 antigen; virus glycoprotein; virus protein; virus RNA; article; central nervous system; controlled study; Coronavirus; immune response; immunopathology; inflammation; Murine hepatitis coronavirus; nonhuman; priority journal; T lymphocyte; virus virulence; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus strain 4","Banker, G., Goslin, K., (1991) Culturing Nerve Cells, pp. 251-281. , G. Banker, and K. Goslin, Eds. 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Immunol., 165, pp. 2278-2286; Xue, S., Perlman, S., Antigen specificity of CD4+ T cell response in the central nervous system of mice infected with mouse hepatitis virus (1997) Virology, 238, pp. 68-78; Yamaguchi, K., Goto, N., Kyuwa, S., Hayami, M., Toyoda, Y., Protection of mice from a lethal coronavirus infection in the central nervous system by adoptive transfer of virus-specific T cell clones (1991) J. Neuroimmunol., 32, pp. 1-9","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"12359451","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0036396869
"Taguchi F., Matsuyama S.","7103209890;7201442043;","Soluble receptor potentiates receptor-independent infection by murine coronavirus",2002,"Journal of Virology","76","3",,"950","958",,39,"10.1128/JVI.76.3.950-958.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036147337&doi=10.1128%2fJVI.76.3.950-958.2002&partnerID=40&md5=6410d409c7696a5e81f270a58006d7cc","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Matsuyama, S., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Mouse hepatitis virus (MHV) infection spreads from MHV-infected DBT cells, which express the MHV receptor CEACAM1 (MHVR), to BHK cells, which are devoid of the receptor, by intercellular membrane fusion (MHVR-independent fusion). This mode of infection is a property of wild-type (wt) JHMV cl-2 virus but is not seen in cultures infected with the mutant virus JHMV srr7. In this study, we show that soluble MHVR (soMHVR) potentiates MHVR-independent fusion in JHMV srr7-infected cultures. Thus, in the presence of soMHVR, JHMV srr7-infected DBT cells overlaid onto BHK cells induce BHK cell syncytia and the spread of JHMV srr7 infection. This does not occur in the absence of soMHVR, soMHVR also enhanced wt virus MHVR-independent fusion. These effects were dependent on the concentration of soMHVR in the culture and were specifically blocked by the anti-MHVR monoclonal antibody CC1. Together with these observations, direct binding of soMHVR to the virus spike (S) glycoprotein as revealed by coimmunoprecipitation demonstrated that the effect is mediated by the binding of soMHVR to the S protein. Furthermore, fusion of BHK cells expressing the JHMV srr7 S protein was also induced by soMHVR. These results indicated that the binding of soMHVR to the S protein expressed on the DBT cell surface potentiates the fusion of MHV-infected DBT cells with nonpermissive BHK cells. We conclude that the binding of soMHVR to the S protein converts the S protein to a fusion-active form competent to mediate cell-cell fusion, in a fashion similar to the fusion of virus and cell membranes.",,"mouse hepatitis virus receptor; unclassified drug; virus receptor; article; cell fusion; cell line; cell membrane; cell strain BHK; cell surface; immunoprecipitation; Murine hepatitis coronavirus; nonhuman; priority journal; protein expression; syncytium; virus cell interaction; virus infection; virus transmission","Allan, S.J., Strauss, J., Buck, D.W., Enhancement of SIV infection with soluble receptor molecule (1990) Science, 247, pp. 1084-1088; Aoki, Y., Aizaki, H., Shimoike, T., Tani, H., Ishii, K., Saito, I., Matsuura, Y., Miyamura, T., A human liver cell line exhibits efficient translation of HCV RNAs produced by a recombinant adenovirus expressing T7 RNA polymerase (1998) Virology, 250, pp. 140-150; Balliet, J.W., Berson, J., D'Cruz, C.M., Huang, J., Crane, J., Gilbert, J.M., Bates, P., Production and characterization of a soluble, active form of Tva, the subgroup A avian sarcoma and leukosis virus receptor (1999) J. 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Gen. Virol., 81, pp. 2867-2871; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; Taguchi, F., Yamada, A., Fujiwara, K., Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: Enhanced antiviral activity of macrophages (1980) Infect. Immun., 29, pp. 42-49; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implication for the requirement of a second factor for virus infection (1992) J. Virol., 66, pp. 6931-6938; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; email: taguchi@ncnp.go.jp",,"American Society for Microbiology",0022538X,,JOVIA,"11773370","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036147337
"Pewe L., Haring J., Perlman S.","6603143496;7101956116;7102708317;","CD4 T-cell-mediated demyelination is increased in the absence of gamma interferon in mice infected with mouse hepatitis virus.",2002,"Journal of virology","76","14",,"7329","7333",,44,"10.1128/JVI.76.14.7329-7333.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036633675&doi=10.1128%2fJVI.76.14.7329-7333.2002&partnerID=40&md5=be8be8cc92835acda1cde22753194c50","Department of Pediatrics, University of Iowa, Iowa City, Iowa  52242, United States","Pewe, L., Department of Pediatrics, University of Iowa, Iowa City, Iowa  52242, United States; Haring, J., Department of Pediatrics, University of Iowa, Iowa City, Iowa  52242, United States; Perlman, S., Department of Pediatrics, University of Iowa, Iowa City, Iowa  52242, United States","Mice infected with the murine coronavirus, mouse hepatitis virus, strain JHM (MHV) develop an immune-mediated demyelinating encephalomyelitis. Adoptive transfer of MHV-immune splenocytes depleted of either CD4 or CD8 T cells to infected mice deficient in recombination activation gene 1 resulted in demyelination. We showed previously that the process of CD8 T-cell-mediated demyelination was strongly dependent on the expression of gamma interferon (IFN-gamma) by donor cells. In this report, we show, in contrast, that demyelination and lymphocyte infiltration were increased in recipients of IFN-gamma(-/-) CD4 T cells when compared to levels in mice receiving C57BL/6 CD4 T cells.",,"gamma interferon; adoptive transfer; animal; article; C57BL mouse; CD4+ T lymphocyte; central nervous system infection; demyelinating disease; gene; genetics; immunology; mouse; Murine hepatitis coronavirus; pathogenicity; pathophysiology; physiology; transplantation; virus infection; Adoptive Transfer; Animals; CD4-Positive T-Lymphocytes; Central Nervous System Viral Diseases; Coronavirus Infections; Demyelinating Diseases; Genes, RAG-1; Interferon Type II; Mice; Mice, Inbred C57BL; Murine hepatitis virus",,"Pewe, L.",,,0022538X,,,"12072531","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036633675
"Filipowicz E., Szczeklik A.","6602360721;57200719066;","Diagnostic methods for detection of respiratory RNA viruses",2002,"Acta Microbiologica Polonica","51","1",,"13","21",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035991780&partnerID=40&md5=3de4e7ca265c7e173af3c12a3d76bbf1","II Department of Medicine, ul. Skawińska 8, 31-066 Cracow, Poland","Filipowicz, E., II Department of Medicine, ul. Skawińska 8, 31-066 Cracow, Poland; Szczeklik, A., II Department of Medicine, ul. Skawińska 8, 31-066 Cracow, Poland","This article is a comprehensive description of diagnostic methods for detection of RNA respiratory viruses - respiratory syncytial virus RSV, influenza A and B viruses, parainfluenza 1, 2 and 3 viruses, coronaviruses and rhinoviruses - from cell culture to molecular biology methods. Both patients and medical personnel appear to be at risk of viral infection, specially during the winter season. Moreover, many health care units lack viral diagnostic facilities; therefore, it is essential for medical personnel to have an understanding of the etiology, mechanisms of transmission and of all disposable today diagnostic methods of RNA respiratory viruses. Patients at greatest risk of acquiring nosocomial viral respiratory disease are children, patients with immunodeficiency and patients treated in intensive care.",,"article; diagnostic test; hospital infection; immune deficiency; infection risk; Influenza virus A; Influenza virus B; intensive care; methodology; Parainfluenza virus 1; Parainfluenza virus 2; Parainfluenza virus 3; Respiratory syncytial pneumovirus; respiratory tract infection; RNA virus; virus detection; virus transmission; blood; chemistry; complement fixation test; enzyme immunoassay; enzyme linked immunosorbent assay; fluorescent antibody technique; genetics; human; isolation and purification; respiratory tract infection; reverse transcription polymerase chain reaction; RNA virus infection; virology; Antibodies, Viral; Antigens, Viral; Complement Fixation Tests; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Direct; Human; Immunoenzyme Techniques; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction; RNA Virus Infections; RNA Viruses; RNA, Viral; Antibodies, Viral; Antigens, Viral; Complement Fixation Tests; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Direct; Humans; Immunoenzyme Techniques; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; virus antibody; virus antigen; virus RNA","Aguilar, J.C., Perez-Bena, M., Garcia, M.L., Cruz, N., Erdman, D.D., Echevarria, J.E., Detection and identification of human parainfluenza viruses 1, 2, 3 and 4 in clinical samples of pediatric patients by multiplex reverse transcription-PCR (2000) J. 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Virol., 40, pp. 96-101; Johston, S.L., Viruses and asthma (1998) Allergy, 53, pp. 922-932; Johston, S.L., Pattermore, P.K., Sanderson, G., Smith, S., Campbell, M.J., Josephs, L.K., Cunningham, A., Holgate, T., The relationship between upper respiratory infections and hospital admissions for asthma: A time-trend analysis (1996) Am. J. Respir. Crit. Care. Med., 154, pp. 654-660; Kaiser, L., Couch, R.B., Galasso, G.J., Glezen, W.P., Webster, R.B., Wright, P.F., Hayden, F.G., First international symposium on influenza and other respiratory viruses: Summary and overview (1999) Antiviral Res., 42, pp. 149-176. , Kapulua, Maui, Hawaii, December 4-6. 1998; Menegus, M.A., (1991) Diagnostic Virology. Textbook of Human Virology. Second Edition, 5, pp. 156-166. , Robert B. Belshe; Munoz, F.M., Galasso, G.J., Gwaltney J.M., Jr., Hayden, F.G., Murphy, B., Webster, R., Wright, P., Couch, R.B., Current research on influenza and other respiratory viruses: II International Symposium (2000) Antiviral Res., 46, pp. 91-124; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) B.M.J., 307, pp. 982-986; Olsen, M.A., Shuck, K.M., Sambol, A., Evaluation of abbot testPack RSV for the diagnosis of respiratory syncytial virus infections (1993) Diag. Microbiol. Infect. Dis., 16, pp. 105-109; Pitkäranta, A., Starck, M., Savolainen, M., Poyry, T., Suomalainen, I., Hyypia, T., Carpen, O., Vaheri, A., RhinoVirus RNA in maxillary sinus epithelium in adult patients with acute sinusitis (2001) Clin. Infect. Dis., 33, pp. 909-911; Pitkäranta, A., Virolainen, A., Jero, J., Arrudo, E., Hayden, F.G., Detection of rhinovirus, respiratory syncytial virus, and coronavirus infections in acute otitis media by reverse Transcriptase Polymerase Chain Reaction (1998) Pediatrics, 102, pp. 291-295; Santii, J., Hyypia, T., Halonen, P., Comparison of PCR primer pairs in the detection of human rhinoviruses in nasopharyngeal aspirates (1997) J. Virol. Methods, 66, pp. 139-147; Sanak, M., Simon, H.U., Szczeklik, A., Leukotriene C4 synthetase promoter polymorphism and risk of aspirin-induced asthma (1997) Lancet, 350, pp. 1599-1600; Sanak, M., Szczeklik, A., Genetics of aspirin-induced asthma (2000) Thorax, 55 (SUPPL. 2), pp. 45-47; Savolainen, C., Hovi, T., Mulders, M.N., Molecular epidemiology of echovirus 30 in Europe: Succession of dominant sublineages within a single major genotype (2001) Arch. Virol., 146, pp. 521-537; Sokhandan, M., McFadden, R., Huang, Y.T., Mazanec, M.B., The contribution of respiratory viruses to severe exacerbations of asthma in adults (1995) Chest, 107, pp. 1570-1575; Szczeklik, A., Aspirin-induced asthma as a viral disease (1988) Clin. Allergy, 18, pp. 15-20; Teichtal, H., Buckmaster, H., Pertnikovs, E., The incidence of respiratory tract infection in adults requiring hospitalization for asthma (1997) Chest, 112, pp. 591-596; Walsh, E.E., Falsey, A.R., Swinburne, I.A., Formica, M.A., Reverse transcription polymerase chain reaction (RT-PCR) for diagnosis of respiratory syncytial virus infection in adults: Use of a single-tube ""hanging droplet"" nested PCR (2001) J. Med. Virol., 63, pp. 259-263; Vabret, A., Mouthon, F., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., Direct diagnosis of human respiratory coronaviruses 229E and OC43 by the chain polymerase chain reaction (2001) J. Virol. Methods, 97, pp. 59-66; Xiang, X., Qiu, D., Hegele, R.D., Tan, W.C., Comparison of different methods of total RNA extraction for viral detection in sputum (2001) J. Virol. Methods, 94, pp. 129-135","Szczeklik, A.; II Department of Medicine, ul. Skawińska 8, 31-066 Cracow, Poland",,,01371320,,AMPOA,"12184443","English","Acta Microbiol. Pol.",Article,"Final",,Scopus,2-s2.0-0035991780
"Biek R., Zarnke R.L., Gillin C., Wild M., Squires J.R., Poss M.","6602456236;7004222371;6603387848;7102953394;7007152976;7003445039;","Serologic survey for viral and bacterial infections in western populations of Canada lynx (Lynx canadensis)",2002,"Journal of Wildlife Diseases","38","4",,"840","845",,19,"10.7589/0090-3558-38.4.840","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038343583&doi=10.7589%2f0090-3558-38.4.840&partnerID=40&md5=aa9f4c84d62271e55753f70ee4ebe5d0","Wildlife Biology Program, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States; Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Center for Conservation Medicine, School of Veterinary Medicine, Tufts University, 200 Westboro Road, North Grafton, MA 01536, United States; Colorado Division of Wildlife, 317 W. Prospect Road, Fort Collins, CO 80523, United States; Forest Sciences Laboratory, Rocky Mountain Research Station, 800 E. Beckwith, Missoula, MT 59807, United States; Division of Biological Sciences, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States; National Park Service, Biol. Resource Management Division, 1201 Oak Ridge Drive, Fort Collins, CO 80625, United States","Biek, R., Wildlife Biology Program, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States; Zarnke, R.L., Alaska Department of Fish and Game, 1300 College Road, Fairbanks, AK 99701-1599, United States; Gillin, C., Center for Conservation Medicine, School of Veterinary Medicine, Tufts University, 200 Westboro Road, North Grafton, MA 01536, United States; Wild, M., Colorado Division of Wildlife, 317 W. Prospect Road, Fort Collins, CO 80523, United States, National Park Service, Biol. Resource Management Division, 1201 Oak Ridge Drive, Fort Collins, CO 80625, United States; Squires, J.R., Forest Sciences Laboratory, Rocky Mountain Research Station, 800 E. Beckwith, Missoula, MT 59807, United States; Poss, M., Wildlife Biology Program, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States, Division of Biological Sciences, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States","A serologic survey for exposure to pathogens in Canada lynx (Lynx canadensis) in western North America was conducted. Samples from 215 lynx from six study areas were tested for antibodies to feline parvovirus (FPV), feline coronavirus, canine distemper virus, feline calicivirus, feline herpesvirus, Yersinia pestis, and Franciscella tularensis. A subset of samples was tested for feline immunodeficiency virus; all were negative. For all other pathogens, evidence for exposure was found in at least one location. Serologic evidence for FPV was found in all six areas but was more common in southern populations. Also, more males than females showed evidence of exposure to FPV. Overall, prevalences were low and did not exceed 8% for any of the pathogens tested. This suggests that free-ranging lynx rarely encounter common feline pathogens.","Canada lynx; Canine distemper virus; Feline calicivirus; Feline coronavirus; Feline herpesvirus; Feline immunodeficiency virus; Feline parvovirus; FIV; Francisella tularensis; Lynx canadensis; Serologic survey; Yersinia pestis","Bacteria (microorganisms); Caliciviridae; Canine distemper virus; Canis familiaris; Coronavirus; Felidae; Feline calicivirus; Feline coronavirus; Feline herpesvirus 1; Feline immunodeficiency virus; Feline parvovirus; Francisella tularensis; Herpesviridae; Lynx; Lynx canadensis; Parvovirus; Yersinia; Yersinia pestis; bacterium antibody; virus antibody; animal; animal disease; article; bacterial infection; blood; Carnivora; epidemiology; female; male; North America; sex ratio; virus infection; Animals; Antibodies, Bacterial; Antibodies, Viral; Bacterial Infections; Carnivora; Female; Male; North America; Seroepidemiologic Studies; Sex Distribution; Virus Diseases","Appel, M., Robson, D.S., A microneutralization test for canine distemper virus (1973) American Journal of Veterinary Research, 34, pp. 1459-1463; Bailey, T.N., Bangs, E.E., Portner, M.F., Malloy, J.C., Mcavinchey, R.J., An apparent overexploited lynx (Felis lynx) population on the Kenai Peninsula, Alaska (USA) (1986) Journal of Wildlife Management, 50, pp. 279-290; Brown, S.L., Mckinney, F.T., Klein, G.C., Jones, W.L., Evaluation of a safranin-O-stained antigen microagglutination test for Francisella tularensis antibodies (1980) Journal of Clinical Microbiology, 11, pp. 146-148; http://www.cdc.gov/ncidod/dvbid/plague/world98.htm, CENTERS FOR DISEASE CONTROL. 1998. 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Centers for Disease Control and Prevention; Chu, M.C., (2000) Manual of Plague Laboratory Tests, , CDC Publications, Atlanta, Georgia, 130 pp; Elton, C., Nicholson, M., The ten-year cycle in numbers of lynx in Canada (1942) Journal of Animal Ecology, 11, pp. 215-244; Ericsson, M., Sandstrom, G., Sjostedt, A., Tarnvik, A., Persistence of cell-mediated immunity and decline of humoral immunity to the intracellular bacterium Francisella tularensis 25 years after natural infection (1994) Journal of Infectious Diseases, 170, pp. 110-114; Gese, E.M., Schultz, R.D., Johnson, M.R., Williams, E.S., Crabtree, R.E., Ruff, R.E., Serological survey for diseases in free-ranging coyotes (Canis latrans) in Yellowstone National Park, Wyoming (1997) Journal of Wildlife Diseases, 33, pp. 47-56; Guo, W., Evehmann, J.F., Foreyt, W.J., Knowlton, F.F., Windberg, L.A., Canine distemper virus in coyotes: A serologic survey (1986) Journal of the American Veterinary Medical Association, 189, pp. 1099-1100; Heeney, J.L., Evermann, J.F., Mckeirnan, A.J., Marker-Kraus, L., Roelke, M.E., Bush, M., Wildt, D.E., O'Brien, S.J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) Journal of Virology, 64, pp. 1964-1972; Helfer-Baker, C., Evermann, J., Mckeirnan, A., Morrison, W., Slack, R., Miller, C., Serological studies on the incidence of canine enteritis viruses (1980) Canine Practice, 7, pp. 37-42; Jellison, W.L., (1974) Tularemia in North America 1930-1974, , University of Montana Foundation, Missoula, Montana, 276 pp; Mörner, T., Addison, E., Tularemia (2001) Infectious Diseases of Wild Mammals, pp. 303-312. , E. S. Williams and I. K. Barker (eds.). Iowa State University Press, Ames, Iowa; Sandsthom, G., Mattsson, R., Nilsson, P.O., Infections with Francisella tularensis biovar palaearctica in hares (Lepus timidus, Lepus europaeus) from Sweden (1988) Journal of Wildlife Diseases, 24, pp. 422-1133; Morton, J.K., Tularemia (1981) Alaska Wildlife Diseases, pp. 46-53. , R. A. Dieterich (ed.). University of Alaska Press, Fairbanks, Alaska; Murray, D.L., Kapke, C.A., Evermann, J.F., Fuller, T.K., Infectious disease and the conservation of free-ranging large carnivores (1999) Animal Conservation, 2, pp. 241-254; Paul-Murphy, J., Work, T., Hunter, D., Mcfie, E., Fjelline, D., Serologic survey and serum biochemical reference ranges of the free-ranging mountain lion (Felis concolor) in California (1994) Journal of Wildlife Diseases, 30, pp. 205-215; Poole, K.G., Characteristics of an unharvested lynx population during a snowshoe hare decline (1994) Journal of Wildlife Management, 58, pp. 608-618; Wakelyn, L.A., Nicklen, P., Habitat selection by lynx in the Northwest Territories (1996) Canadian Journal of Zoology, 74, pp. 845-850; Reif, J.S., Seasonality, natality and herd immunity in feline panleukopenia (1976) American Journal of Epidemiology, 103, pp. 81-87; Keynolds H.V. III, Effects of harvest on grizzly bear population dynamics in the north-central Alaska Range (1999) Research Progress Report, , Alaska Department of Fish and Game. Federal Aid in Wildlife Restoration. Grants W-24-5 and W-27-1. Juneau, Alaska; Roelke, M.E., Forrester, D.J., Jacobson, E.R., Kollias, G.V., Scott, F.W., Barr, M.C., Evermaxn, J.F., Pirtle, E.C., Seroprevalence of infections disease agents in free-ranging Florida panthers (Felis concolor conji) (1993) Journal of Wildlife Diseases, 29, pp. 36-49; Ruggiero, L.F., Aubry, K.B., Buskirk, S.W., Koehler, G.M., Krebs, C.J., Mckelvey, K.S., Squires, J.R., (2000) Ecology and Conservation of Lynx in the United States, , University Press of Colorado, Boulder, Colorado, 480 pp; Schwartz, M.K., Mills, L.S., Mckelvey, K.S., Ruggiero, L.F., Allendorf, F.W., DNA reveals high dispersal synchronizing the population dynamics of Canada lynx (2002) Nature, 415, pp. 520-522; Scott, F.W., Evaluation of a feline viral rhinotracheitis-feline calicivirus disease vaccinie (1977) American Journal of Veterinary Research, 38, pp. 229-234; Slough, B.G., Estimating lynx population age ratio with pelt-length data (1996) Wildlife Society Bulletin, 24, pp. 495-499; Mowat, G., Lynx population dynamics in an untrapped refugium (1996) Journal of Wildlife Management, 60, pp. 946-961; Squires, J.R., Laurion, T., Lynx home range and movements in Montana and Wyoming: Preliminary results (2000) Ecology and Conservation of Lynx in the United States, pp. 337-349. , L. F. Ruggiero, K. B. Aubry, S. W. Buskirk, G. M. Koehler, C. J. Krebs, K. S. McKelvey and J. R. Squires (eds.). University Press of Colorado, Boulder, Colorado; Steinel, A., Parrish, C.R., Bloom, M.E., Thuyen, U., Parvovirus infections in wild carnivores (2001) Journal of Wildlife Diseases, 37, pp. 594-607; Determination of threatened status for the contiguous U.S. distinct population segment of the Canada lynx and related rule; final rule (2000) US Federal Register, 65, pp. 16051-16086; Wassmer, D.A., Guenther, D.D., Layne, J.N., Ecology of the bobcat in south-central Florida (1988) Bulletin of the Florida State Museum Biological Sciences, 33, pp. 159-228; Zarnke, R.L., Ballard, W.B., Serologic survey for selected microbial pathogens of wolves in Alaska, 1975-1982 (1987) Journal of Wildlife Diseases, 23, pp. 77-85","Poss, M.; Wildlife Biology Program, University of Montana, 32 Campus Drive, Missoula, MT 59812, United States; email: mposs@selway.umt.edu",,"Wildlife Disease Association, Inc.",00903558,,,"12528455","English","J. Wildl. Dis.",Article,"Final",,Scopus,2-s2.0-0038343583
"Siergiejko Z.","7006808718;","Infections and bronchial hyperreactivity",2002,"International Review of Allergology and Clinical Immunology","8","2",,"117","122",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036284775&partnerID=40&md5=062863b222582587facce32c9bc6c55b","Department of Allergology, University School of Medicine, M. Curie-Sklodowskiej 24a, 15-276 Białystok, Poland","Siergiejko, Z., Department of Allergology, University School of Medicine, M. Curie-Sklodowskiej 24a, 15-276 Białystok, Poland","Bronchial hyperreactivity (BHR) is a characteristic feature of many inflammatory lung diseases. The most intensive BHR can be observed in patients suffering from chronic asthma. Numerous clinical observations suggest that airway infections can induce bronchial hyperreactivity in susceptible patients, and exacerbate bronchial asthma. The most important role is played by viral infections (RSV, Rhinoviruses, Coronaviruses) and chronic bacterial infections (Mycoplasma pneumoniae, Chlamydia pneumoniae, Chlamydia trachomatis). Recently some authors have reported an increased appearance of BHR in HIV-infected patients. Among moulds Aspergillus, which causes hypersensitivity pneumonitis, can induce BHR. Though many mould allergens such as Alternaria, Cladosporium and Penicillum can play an important role in the induction of asthma and BHR, they do not cause airway infection. Numerous parasites are responsible for asthma and BHR induction, but they rarely cause airway infection.","Airway infections; Asthma; Bronchial hyperreactivity","albendazole; anthelmintic agent; Ascaris lumbricoides; asthma; bacterial infection; bronchus hyperreactivity; Chlamydia trachomatis; Chlamydophila pneumoniae; Cladosporium; Coronavirus; Dermatophagoides; helminth; helminthiasis; human; Human immunodeficiency virus infection; mould; Mycoplasma pneumonia; nonhuman; parasite; Penicillium; Respiratory syncytial pneumovirus; respiratory tract disease; respiratory tract infection; review; Rhinovirus; skin test; virus infection","Adler, A., Ngo, L., Tager, I.B., Association of tobacco smoke exposure and respiratory syncytial virus infection with airways reactivity in early childhood (2001) Pediatr. Pulmonol., 32, pp. 418-427; Bell, T.D., Chai, H., Berlow, B., Daniels, G., Immunization with killed influenza virus in children with chronic asthma (1978) Chest, 73, pp. 140-145; Bjornsson, E., Hjelm, E., Janson, C., Fridell, E., Boman, G., Serology of chlamydia in relation to asthma and bronchial hyperresponsineness (1996) Scand. J. Infect. Dis., 28, pp. 63-69; Frye, C., Heinrich, J., Wjst, M., Wichman, H.E., Increasing prevalence of bronchial hyperresponsiveness in three selected areas in East Germany (2001) Eur. Respir. J., 18, pp. 451-458; Gern, J.E., Effect of rhinovirus in asthma (1999) Conversations, 7, pp. 13-16; Gibson, P.G., Włodarczyk, J.W., Hensley, M.J., Epidemiological association of airway inflammation with asthma symptoms and airway hyperresponsiveness in childhood (1998) Am. J. Respir. Crit. Care Med., 158, pp. 36-41; Gulec, S., Ertas, F., Tutar, E., Demirel, Y., Karaoguz, R., Omurlu, K., Oral, D., Bronchial hyperreactivity in patients with mitral stenosis before and after successful percutaneous mitral balloon valvulotomy (1999) Chest, 116, pp. 1582-1586; Hardy, R.D., Jafri, H.S., Olsen, K., Hatfield, J., Iglehart, J., Rogers, B.B., Patel, P., Ramilo, O., Mycoplasma pneumoniae induces chronic respiratory infection, airway hyperreactivity, and pulmonary inflammation: A murine model of infection-associated chronic reactive airway disease (2002) Infect Immun., 70, pp. 649-654; Hopfenspirger, M.T., Parr, S.K., Hopp, R.J., Townley, R.G., Agrawal, D.K., Mycobacterial antigens attenuate late phase response, airway hyperresponsiveness, and bronchoalveolar lavage eosinophilia in a mouse model of bronchial asthma (2001) Int. Immunopharmacol., 1, pp. 1743-1751; Isaacs, D., Flowers, D., Clarke, J.R., Valman, H.B., Macnaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch. Dis. Child., 58, pp. 500-503; Jatakanon, A., Lim, S., Kharitonov, S.A., Chung, K.F., Barnes, P.J., Correlation between exhaled nitric oxide, sputum eosinophils, and methacholine responsiveness in patients with mild asthma (1998) Thorax, 53, pp. 91-95; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Leuppi, J.D., Salome, C.M., Jenkins, C.R., Koskela, H., Brannan, J.D., Anderson, S.D., Andersson, M., Woolcock, A.J., Markers of airway inflammation and airway hyperresponsiveness in patients with well-controlled asthma (2001) Eur. Respir. J., 18, pp. 444-450; Lynch, N.R., Palenque, M., Hagel, I., DiPrisco, M.C., Clinical improvement of asthma after anthelminthic treatment in a tropical situation (1997) Am. J. Respir. Crit. Care Med., 156, pp. 50-54; Mackean, M.C., Leech, M., Lambert, P.C., Hewitt, C., Myint, C., Silverman, M., A model of viral wheeze in nonasthmatic adults: Symptoms and physiology (2001) Eur. Respir. J., 18, pp. 23-32; Martin, R.J., Chu, H.W., Honour, J.M., Harbeck, R.J., Airway inflammation and bronchial hyperresponsiveness after Mycoplasma pneumoniae infection in murine model (2001) Am. J. Respir. Cell Mol. Biol., 24, pp. 577-582; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, M.A., Coronaviruses infection in acute lower respiratory tract disease of infants (1974) J. Inf. Dis., 130, pp. 502-507; Nahori, M.A., Lagranderie, M., Lefort, J., Thouron, F., Jopseph, D., Winter, N., Gicquel, B., Vargaftig, B.B., Effect of Mycobacterium bovis BCG on the development of allergic inflammation and bronchial hyperresponsiveness in hyper-IgE BP2 mice vaccinated as newborns (2001) Vaccine, 19, pp. 1484-1495; Nicolson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbations of asthma in adults (1993) BMJ, 307, pp. 982-986; Peebles R.S., Jr., Hashimoto, K., Collins, R.D., Jarzecka, K., Furlong, J., Mitchell, D.B., Sheller, J.R., Graham, B.S., Immune interaction between respiratory syncytial virus infection and allergen sensitization critically depends on timing of challenges (2001) J. Infect. Dis., 184, pp. 1374-1379; Poirier, C.D., Inhaber, N., Lalonde, R.G., Ernst, P., Prevalence of bronchial hyperresponsiveness among HIV-infected men (2001) Am. J. Respir. Crit. Care Med., 164, pp. 542-545; Reed, C., Pertussis sensitization as an animal model for the abnormal bronchial sensitivity of asthma (1968) Yale J. Biol. Med., 40, pp. 507-515; Siergiejko, Z., Pharmacologic modulation of BHR in asthma patients (1997) Biatystok; Terpstra, G.K., Raaijmakers, J.A.M., Kreukniet, J., Comparison of vaccination of mice and rats with Haemophilus influenza and Bordetella pertussis as models of atopy (1979) Clin. Exp. Pharmac. Physiol., 6, pp. 139-149; Von Mutius, E., Infection, friend or foe in the development of atopy and asthma? The epidemiological evidence (2001) Eur. Respir. J., 18, pp. 872-881; Wang, C.C., Nolan, T.J., Schad, G.A., Abraham, D., Infection of mice with the helminth Strongyloides stercoralis suppresses pulmonary allergic responses to ovalbumin (2001) Clin. Exp. Allergy, 31, pp. 495-503; Wennergren, G., Kristjansson, S., Relationship between respiratory syncytial virus bronchiolitis and future obstructive airway diseases (2001) Eur. Respir. J., 18, pp. 1044-1058; Woolcock, A.J., Salome, C.M., Yan, K., The shape of the dose response curve to histamine in asthmatic and normal subjects (1984) Am. Rev. Respir. Dis., 130, pp. 72-75; Wu, H., Lin, Y., Han, L., Bronchial hyperreactivity in patients with mitral stenosis and therapeutic effect of inhaled corticosteroids (2000) Zhonghua Jie He He Hu Xi Za Zhi, 23, pp. 545-547","Siergiejko, Z.; Department of Allergology, University School of Medicine, M. Curie-Sklodowskiej 24a, 15-276 Białystok, Poland; email: siergiejko@csk.pl",,,12329142,,IRAIF,,"English","Int. Rev. Allergol. Clin. Immunol.",Review,"Final",,Scopus,2-s2.0-0036284775
"Peterson M.J., Ferro P.J., Peterson M.N., Sullivan R.M., Toole B.E., Silvy N.J.","7402271293;7005171400;7402271586;7402484937;7007032141;7003766383;","Infectious disease survey of lesser prairie chickens in North Texas",2002,"Journal of Wildlife Diseases","38","4",,"834","839",,13,"10.7589/0090-3558-38.4.834","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038682084&doi=10.7589%2f0090-3558-38.4.834&partnerID=40&md5=2f58cd999e45ba69b15bf9c1257e3fcc","Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States; Texas Vet. Med. Diagn. Lab. System, P.O. Drawer 3040, College Station, TX 77841-6040, United States; Texas Parks and Wildlife Department, 5900 Cemetery Road, Canyon, TX 79015, United States","Peterson, M.J., Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States; Ferro, P.J., Texas Vet. Med. Diagn. Lab. System, P.O. Drawer 3040, College Station, TX 77841-6040, United States; Peterson, M.N., Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States; Sullivan, R.M., Texas Parks and Wildlife Department, 5900 Cemetery Road, Canyon, TX 79015, United States; Toole, B.E., Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States; Silvy, N.J., Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States","Lesser prairie chicken (Tympanuchus pallidicinctus) abundance, like that of most grassland birds, has declined rangewide for decades. Although habitat loss and degradation are likely ultimate causes for this decline, infectious agents, particularly microparasites, could be proximate contributors. No surveys of pathogenic bacteria or viruses have been published for this species. We surveyed 24 free-living lesser prairie chickens from Hemphill County, Texas (USA), for evidence of exposure to Salmonella typhimurium, S. pullorum, Mycoplasma gallisepticum, M. synoviae, Chlamydophila psittaci, and the avian influenza, Newcastle disease, infectious bronchitis, and reticuloendotheliosis viruses. Two of 18, and eight of 17 samples were seropositive for the Massachusetts and Arkansas serotypes of infectious bronchitis virus, respectively. Five of the eight positive individuals were juveniles, two of which were seropositive for both serotypes. All other serologic and genetic tests were negative. Because the ecological significance of these results is unknown, the pathogenesis, transmission, and/or population-level influences of infectious bronchitis and related avian coronaviruses for lesser prairie chickens deserves further study.","Avian coronavirus; Infectious bronchitis virus; Infectious disease; Lesser prairie chicken; Serologic survey; Texas; Tympanuchus pallidicinctus","Aves; Avian infectious bronchitis virus; Bacteria (microorganisms); Chlamydophila psittaci; Coronavirus; Galliformes; Gallus gallus; Mycoplasma; Mycoplasma gallisepticum; Mycoplasma synoviae; Reticuloendotheliosis virus; Salmonella typhimurium; Tympanuchus; Tympanuchus pallidicinctus; animal; animal disease; article; bacterial infection; bird; bird disease; communicable disease; female; male; microbiology; United States; virology; virus infection; Animals; Bacterial Infections; Bird Diseases; Birds; Communicable Diseases; Female; Male; Texas; Virus Diseases","Addison, E.M., Anderson, R.C., Oxyspirura lumsdeni n. sp. (Nematoda: Thelaziidae) from Tetraonidae in North America (1969) Canadian Journal of Zoology, 47, pp. 1223-1227; Alexander, D.J., Chettle, N.J., Procedures for the haemagglutination and the haemagglutination-inhibition tests for avian infectious bronchitis virus (1977) Avian Pathology, 6, pp. 9-11; Allred, J.N., Raggi, L.G., Lee, G.G., Susceptibility and resistance of pheasants, starlings, and quail to three respiratory diseases of chickens (1973) California Fish and Game, 59, pp. 161-167; Aly, M.M., Smith, E.J., Fadly, A.M., Detection of reticuloendotheliosis virus infection using the polymerase chain reaction (1993) Avian Pathology, 22, pp. 543-554; Ammann, G.A., Determining the age of pinnated and sharp-tailed grouse (1944) The Journal of Wildlife Management, 8, pp. 170-171; Anderson, R.M., May, R.M., Population biology of infectious diseases: Part I (1979) Nature, 280, pp. 361-367; The population dynamics of microparasites and their invertebrate hosts (1981) Philosophical Transactions of the Royal Society of London B, 291, pp. 451-524; Beard, C.W., Wilkes, W.J., A simple and rapid microtest procedure for determining Newcastle hemagglutination-inhibition (HI) antibody titers (1973) Proceedings of the Annual Meeting, US Animal Health Association, 77, pp. 596-600; Biondi, E., Schirvo, A., Investigations into the susceptibility of various small passerine birds to the virus of infectious bronchitis (1966) Acta Medica Veterinaria, 12, pp. 537-547; Bowers, R.G., Begon, M., Hodgkinson, D.E., Host-pathogen population cycles in forest insects?: Lessons from simple models reconsidered (1993) Oikos, 67, pp. 529-538; Cavanagh, D., A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathology, 30, pp. 109-115; Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry. 10th Edition, pp. 511-526. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. B. McDougald and Y. M. Saif (eds.). Iowa State University Press, Ames, Iowa; Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 355-368; Chawford, J.A., Status, problems, and research needs of the lesser prairie chicken (1980) Proceedings of the Prairie Grouse Symposium, pp. 1-7. , P. A. Vohs, Jr. and F. L. Knopf (eds.). Oklahoma State University, Stillwater, Oklahoma; Davidson, I., Borovsdaya, A., Perl, S., Malkinson, M., Use of the polymerase chain reaction for the diagnosis of natural infection of chickens and turkeys with Marek's disease virus and reticuloendotheliosis virus (1995) Avian Pathology, 24, pp. 69-94; Drew, M.L., Wigle, W.L., Graham, D.L., Griffin, C.P., Silvy, N.J., Fadly, A.M., Witter, R.L., Reticuloendotheliosis in captive greater and Attwater's prairie chickens (1998) Journal of Wildlife Diseases, 34, pp. 783-791; Edgar, S.A., Waggoner, R., Pathogens of Coturnix coturnix japonica (1964) Quail Quarterly, 2, pp. 11-14; Emerson, K.C., A list of Mallophaga from gallinaceous birds of North America (1951) The Journal of Wildlife Management, 15, pp. 193-195; Giesen, K.M., Lesser prairie chicken (1998) The Birds of North America, , No. 364, A. Poole and F. Gill (eds.). The Birds of North America, Philadelphia, Pennsylvania, 20 pp; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis virus from pheasants (1996) Veterinary Record, 138, pp. 208-209; Gould, F.W., (1962) Texas Plants - A Checklist and Ecological Summary, , Publication MP-585. Texas Agricultural Experiment Station, The Agricultural and Mechanical College of Texas, College Station, 112 pp; Grimes, J.E., Tully T.N., Jr., Arizmendi, F., Phalen, D.N., Elementary body agglutination for rapidly demonstrating chlamydial agglutinins in avian serum with emphasis on testing cockatiels (1994) Avian Diseases, 38, pp. 822-831; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses: A review (2000) Avian Pathology, 29, pp. 207-212; Knopf, F.L., Avian assemblages on altered grasslands (1994) Studies in Avian Biology, 15, pp. 247-257; Mote, K.D., Applegate, R.D., Bailey, J.A., Giesen, K.E., Horton, R., Sheppard, J.L., (1999) Assessment and Conservation Strategy for the Lesser Prairie-chicken (Tympanuchus Pallidicinctus), p. 51. , Kansas Department of Wildlife and Parks, Emporia, Kansas; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Edition, pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald and Y. M. Saif (eds.). Iowa State University Press, Ames, Iowa; Pence, D.B., Sell, D.L., Helminths of the lesser prairie chicken, Tympanuchus pallidicinctus (Ridgway) (Tetraonidae), from the Texas panhandle (1979) Proceedings of the Helminthological Society of Washington, 46, pp. 146-149; Peterjohn, B.G., Sauer, J.R., Population status of North American grassland birds from the North American breeding bird survey 1966-1996 (1999) Studies in Avian Biology, 19, pp. 27-44; Peterson, M.J., The endangered Attwater's prairie chicken and an analysis of prairie grouse helminthic endoparasitism (1996) Ecography, 19, pp. 424-431; Purvis, J.R., Lichtenfels, J.R., Craig, T.M., Dronen N.O., Jr., Silvy, N.J., Serologic and parasitologic survey of the endangered Attwater's prairie chicken (1998) Journal of Wildlife Diseases, 34, pp. 137-144; Schemnitz, S.D., Capturing and handling wild animals (1994) Research and Management Techniques for Wildlife and Habits, pp. 106-124. , T. A. Bookhout (ed.). The Wildlife Society, Bethescla, Maryland; Silvy, N.J., Morrow, M.E., Shanely E., Jr., Slack, R.D., An improved drop net for capturing wildlife (1990) Proceedings of the Annual Conference, Southeastern Association of Fish and Wildlife Agencies, 44, pp. 374-378; Spackman, D., Cameron, I.R.D., Isolation of infectious bronchitis virus from pheasants (1983) The Veterinary Record, 113, pp. 354-355; Stabler, R.M., Plasmodium (Giovannolaia) pedioecetii from the lesser prairie chicken. Tympanuhus pallidicinctus (1978) Journal of Parasitology, 64, pp. 1125-1126; Taylor, M.A., Guthery, F.S., (1980) Status, Ecology, and Management of the Lesser Prairie Chicken, , U.S. Department of Agriculture, Forest Service, Rocky Mountain Forest and Range Experiment Station, General Technical Report RM-77, Fort Collins, Colorado, 15 pp; (2000) National Poultry Improvement Plan and Auxiliary Provisions, , Veterinary Services, Animal and Plant Inspection Service, U.S. Department of Agriculture, Conyers, Georgia, 111 pp","Peterson, M.J.; Dept. of Wildl. and Fish. Sciences, Texas A and M University, TAMU-2258, College Station, TX 77843-2258, United States; email: mpeterson@tamu.edu",,"Wildlife Disease Association, Inc.",00903558,,,"12528454","English","J. Wildl. Dis.",Article,"Final",,Scopus,2-s2.0-0038682084
"Onodera K., Melcher U.","36724841500;7004007393;","VirOligo: A database of virus-specific oligonucleotides",2002,"Nucleic Acids Research","30","1",,"203","204",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036089478&partnerID=40&md5=10eeca2c3b5bdba7b99e88492f6f104d","Department of Biochemistry, Molecular Biology, Oklahoma State University, Stillwater, OK 74078, United States","Onodera, K., Department of Biochemistry, Molecular Biology, Oklahoma State University, Stillwater, OK 74078, United States; Melcher, U., Department of Biochemistry, Molecular Biology, Oklahoma State University, Stillwater, OK 74078, United States","VirOligo is a database of virus-specific oligonucleotides. The VirOligo database consists of two tables, Common data and Oligo data. The Oligo data table contains PCR primers and hybridization probes used for detection of viral nucleic acids and the Common data table contains the experimental conditions used in their detection. Each oligonucleotide entry contains links to PubMed, GenBank, NCBI Taxonomy databases and BLAST. As of July 2001, the VirOligo database contains a complete listing of oligonucleotides specific to viral agents associated with bovine respiratory disease that were published in English in peer-reviewed journals. The viruses are bovine herpes virus types 1, 3, 4 and 5, bovine viral diarrhea virus bovine parainfluenza 3 virus, bovine respiratory syncytial virus, bovine adenovirus, bovine rhinovirus, bovine coronavirus, bovine reovirus, bovine enterovirus and alcelaphine herpesvirus-1. The VirOligo database is being expanded to other viruses and can be accessed through the Internet at http://viroligo.okstate.edu/.",,"nucleic acid; oligonucleotide; Adenovirus; article; Bovine diarrhea virus; Bovine herpes virus; cattle disease; controlled study; Coronavirus; Enterovirus; GenBank; Herpes simplex virus 1; Internet; medical literature; MEDLINE; nonhuman; nucleic acid analysis; nucleic acid hybridization; nucleic acid probe; nucleotide sequence; Parainfluenza virus 3; peer review; polymerase chain reaction; priority journal; publication; Reovirus; Respiratory syncytial pneumovirus; respiratory tract disease; Rhinovirus; sequence database; VirOligo; virus typing; Animals; Cattle; Cattle Diseases; Databases, Nucleic Acid; DNA Primers; DNA, Viral; Information Storage and Retrieval; Internet; Oligonucleotide Probes; Oligonucleotides; RNA, Viral; Viruses; Adenoviridae; Alcelaphine herpesvirus 1; Bos taurus; Bovinae; Bovine adenovirus; Bovine coronavirus; Bovine enterovirus; Bovine parainfluenza virus 3; Bovine respiratory syncytial virus; Bovine viral diarrhea virus 1; Coronavirus; DNA viruses; Enterovirus; Herpesviridae; Human herpesvirus 1; Human parainfluenza virus 3; Pneumovirus; Reovirus sp.; Respiratory syncytial virus; Rhinovirus; RNA viruses; Simplexvirus","Petrik, J., Microarray technology: The future of blood testing? 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"Haigh J.C., Mackintosh C., Griffin F.","7103171860;7102170242;7403422543;","Viral, parasitic and prion diseases of farmed deer and bison",2002,"OIE Revue Scientifique et Technique","21","2",,"219","248",,38,"10.20506/rst.21.2.1331","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036678681&doi=10.20506%2frst.21.2.1331&partnerID=40&md5=03f4904ca79a744692d900d7b2ab344c","Dept. of Large Animal Clinic. Sci., Western Coll. of Veterinary Medicine, 52 Campus Drive, Saskatoon, Sask. S7N 5B4, Canada","Haigh, J.C., Dept. of Large Animal Clinic. Sci., Western Coll. of Veterinary Medicine, 52 Campus Drive, Saskatoon, Sask. S7N 5B4, Canada; Mackintosh, C., Dept. of Large Animal Clinic. Sci., Western Coll. of Veterinary Medicine, 52 Campus Drive, Saskatoon, Sask. S7N 5B4, Canada; Griffin, F., Dept. of Large Animal Clinic. Sci., Western Coll. of Veterinary Medicine, 52 Campus Drive, Saskatoon, Sask. S7N 5B4, Canada","The most important viral disease of farmed deer and bison is malignant catarrhal fever. The other herpesviruses which have been isolated from these species are briefly described. Other viral agents that are recognised in these animals, including adenovirus, parapox, foot and mouth disease, bluetongue, epizootic haemorrhagic disease, bovine virus diarrhoea, rotavirus and coronavirus, are also discussed. Ectoparasites of importance in this group in various parts of the world include a variety of ticks, as well as lice, keds, Oestridae, mange mites and fire ants. Helminth parasites include liver flukes (Fascioloides and Fasciola), gastrointestinal nematodes of the family Trichostrongylidae, pulmonary lungworms of the genus Dictyocaulus and extra-pulmonary lungworms of the family Protostrongylidae. Chronic wasting disease is principally important in North America, where the disease occurs in wild cervids in a limited area and has been reported in farmed deer in a small number of states in the United States of America and one province in Canada. These diseases are summarised in terms of their classification, epidemiology, clinical signs, pathology, diagnosis, treatment and control.","Bison; Chronic wasting disease; Control; Deer; Diagnosis; Infectious diseases; Lungworm; Malignant catarrhal fever; Ostertagia; Wildlife","Acari; Adenoviridae; Animalia; Bison; Bovinae; Bubalus; Cervidae; Coronavirus; Dictyocaulus; Dictyocaulus; Digenea (flukes); Fasciola; Fasciola; Fasciola hepatica; Fascioloides; Fascioloides; Formicidae; Hepatica; Hippoboscidae; Metastrongyloidea; Nematoda; Oestridae; Ostertagia; Ovis aries; Phthiraptera; Protostrongylidae; Rotavirus; Solenopsis geminata; Trematoda; Trichostrongylidae; Vermes; animal; animal disease; animal parasitosis; buffalo; deer; disease transmission; parasitology; prion disease; review; virus infection; Animals; Bison; Deer; Parasitic Diseases, Animal; Prion Diseases; Virus Diseases","Allan, S.A., Ticks (class Arachnida: order Aracina) (2001) Parasitic diseases of wild mammals, 2nd Ed., pp. 72-106. , (W.M. 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Tech.",Article,"Final",,Scopus,2-s2.0-0036678681
"Mine Y., Kovacs-Nolan J.","7103350429;6508188871;","Chicken egg yolk antibodies as therapeutics in enteric infectious disease: A review",2002,"Journal of Medicinal Food","5","3",,"159","169",,131,"10.1089/10966200260398198","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036754686&doi=10.1089%2f10966200260398198&partnerID=40&md5=faf9369b4cc58d8c8723c30e4b816870","Department of Food Science, University of Guelph, Guelph, Ont. N1G2W1, Canada","Mine, Y., Department of Food Science, University of Guelph, Guelph, Ont. N1G2W1, Canada; Kovacs-Nolan, J., Department of Food Science, University of Guelph, Guelph, Ont. N1G2W1, Canada","Passive immunization by oral administration of specific antibodies has been an attractive approach against gastrointestinal (GI) pathogens in both humans and animals. Recently, laying chickens have attracted considerable attention as an alternative source of antibodies for the prevention and treatment of infectious GI diseases. After immunization, the specific antibodies (called IgY) are transported to the egg yolk, from which the IgY then can be separated without sacrificing chickens. A chicken usually lays about 280 eggs in a year, and egg yolk contains 100-150 mg of IgY per yolk, suggesting that more than 40 g of IgY per year can be obtained from each chicken through eggs. IgY is also an alternative to antibiotics for treatment of enteric antibiotic-resistant pathogens. Oral administration of IgY has proved successful for treatment of a variety of GI infections, such as bovine and human rotaviruses, bovine coronavirus, Yersinia ruckeri, enterotoxigenic Escherichia coli, Salmonella spp., Edwardsiella tarda, Staphylococcus, and Pseudomonas. The IgY technology offers great future opportunities for designing prophylactic strategies against infectious GI diseases in humans and animals. However, there is still controversy regarding the stability of IgY through the GI tract. Finding an effective way to protect the antibodies from degradation in the GI tract would open the door for significant advances in IgY technology and nutraceutical applications.",,"antibiotic agent; Escherichia coli enterotoxin; immunoglobulin G; immunoglobulin Y; polyclonal antibody; unclassified drug; alternative medicine; antimicrobial activity; chicken; Coronavirus; Edwardsiella tarda; egg yolk; Escherichia coli; gastrointestinal tract; human; immunotherapy; intestine infection; nonhuman; passive immunization; priority journal; prophylaxis; Pseudomonas; review; Rotavirus; Salmonella; Staphylococcus; virus infection; Yersinia ruckeri; yersiniosis; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Edwardsiella tarda; Escherichia coli; Gallus gallus; Pseudomonas; Rotavirus; Salmonella; Staphylococcus; Yersinia ruckeri","Carlander, D., Kollberg, H., Wejaker, P.-E., Larsson, A., Peroral immunotherapy with yolk antibodies for the prevention and treatment of enteric infections (2000) Immunol Res, 21, pp. 1-6; Reilly, R.M., Domingo, R., Sandhu, J., Oral delivery of antibodies: Future pharmacokinetic trends (1997) Clin Pharmacokinet, 4, pp. 313-323; Crabb, J.H., Antibody-based immunotherapy of cryptosporidiosis (1998) Adv Parasitol, 40, pp. 121-149; Schade, R., Staak, C., Hendrikson, C., Erhard, M., Hugl, H., Koch, G., Larsson, A., Straughan, D., The production of avian (egg yolk) antibodies: IgY (1996) ATLA, 24, pp. 925-934; Wang, H.Y., Imanaka, T., (1995) Antibody Expression and Engineering, , American Chemical Society, Washington, DC; Carlander, D., Stalberg, J., Larsson, A., Chicken antibodies: A clinical chemistry perspective (1999) Ups J Med Sci, 104, pp. 179-189; Sim, J.S., Nakai, S., Guenter, W., (1999) Egg Nutrition and Biotechnology, , CAB publishing, Oxon, UK; Hatta, H., Ozeki, M., Tsuda, K., Egg yolk antibody IgG and its application (1997) Hen Eggs: Their Basic and Applied Science, pp. 151-178. , (Yamamoto T, Juneja LR, Hatta H, Kim M, eds.). 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Academic Press, Inc., London; Sack, R.B., Antimicrobial prophylaxis of travellers' diarrhea: A selected summary (1986) Rev Infect Dis, 8, pp. S160-S166; Svennerholm, A.M., Holmgren, J., Sack, D.A., Development of oral vaccines against enterotoxigenic Escherichia coli (1989) Vaccine, 7, pp. 196-198; Hampson, D.J., Postweaning Escherichia coli diarrhoea in pigs (1994) Escherichia coli in Domestic Animals and Humans, pp. 171-191. , (Gyles CL, ed.). CAB International, Oxon, UK; Parry, S.H., Rooke, D.M., Adhesins and colonization factors of Escherichia coli (1985) The Virulence of Escherichia coli, pp. 79-159. , (Sussman M, ed.). Academic Press, London; Hilpert, H., Gerber, H., Pahud, J.J., Ballabriga, A., Arcalis, L., Farriaux, F., De Leyer, E., Nussle, D., Bovine milk immunoglobulins (Ig): Their possible utilization in industrially prepared infant's milk formula (1977) Food and Immunology, pp. 182-196. , (Hambraeusm L, Hanson L, McFarlene H, eds.). 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K88+ infection in neonatal and early weaned piglets (1999) FEMS Immunol Med Microbiol, 23, pp. 283-288; Yokoyama, H., Peralta, R.C., Diaz, R., Sendo, S., Ikemori, Y., Kodama, Y., Passive protective effect of chicken egg yolk immunoglobulins against experimental enterotoxigenic Escherichia coli infection in neonatal piglets (1992) Infect Immun, 60, pp. 998-1007; Ikemori, Y., Peralta, R.C., Kuroki, M., Yokoyama, H., Kodama, Y., Avidity of chicken yolk antibodies to enterotoxigenic Escherichia coli fimbriae (1993) Poultry Sci, 72, pp. 2361-2365; Ikemori, Y., Kuroki, M., Peralta, R.C., Yokoyama, H., Kodama, Y., Protection of neonatal calves against fatal enteric colibacillosis by administration of egg yolk powder from hens immunized with K99-piliated enterotoxigenic Escherichia coli (1992) Am Vet Res, 53, pp. 2005-2008; Bell, C., Kriakides, A., (1998) Salmonella: A Practical Approach to the Organism and Its Control in Foods, , Blackie, A & P, New York; Isibasi, A., Ortiz, V., Vargas, M., Paniagua, J., Gonzales, C., Moreno, J., Kumate, J., Protection against Salmonella typhi infection in mice after immunization with outer membrane proteins isolated from Salmonella typhi 9, 12, d, Vi (1988) Infect Immun, 56, pp. 2953-2959; Udhayakumar, V., Muthukkaruppan, V.R., Protective immunity induced by outer membrane proteins of Salmonella typhimurium in mice (1987) Infect Immun, 55, pp. 816-821; Mine, Y., Separation of Salmonella enteritidis from experimentally contaminated liquid eggs using a hen IgY immobilized immunomagnetic separation system (1997) J Agric Food Chem, 45, pp. 3723-3727; Thorns, C.J., Sojka, M.G., Chasey, D., Detection of a novel fimbrial structure on the surface of Salmonella enteritidis by using a monoclonal antibody (1990) J Clin Microbiol, 28, pp. 2409-2414; Thorns, C.J., Sojka, M.G., McLaren, M., Dibb-Fuller, M., Characterization of monoclonal antibodies against a fimbrial structure of Salmonella enteritidis and certain other serogroup D salmonellae and their application as serotyping reagents (1992) Res Vet Sci, 53, pp. 300-308; Yokoyama, H., Umeda, K., Peralta, R.C., Hashi, T., Icatlo, F., Kuroki, M., Ikemori, Y., Kodama, Y., Oral passive immunization against experimental salmonellosis in mice using chicken egg yolk antibodies specific for Salmonella enteritidis and S. typhimurium (1998) Vaccine, 16, pp. 388-393; Yokoyama, H., Peralta, R.C., Umeda, K., Hashi, T., Icatlo, F.C., Kuroki, M., Ikemori, Y., Kodama, Y., Prevention of fatal salmonellosis in neonatal calves, using orally administered chicken egg yolk Salmonella-specific antibodies (1998) Am J Vet Res, 59, pp. 416-420; Sugita-Konishi, Y., Shibata, K., Yun, S.S., Hara-Kudo, Y., Yamaguchi, K., Kumagai, S., Immune functions of immunoglobulin Y isolated from egg yolk of hens immunized with various infectious bacteria (1996) Biosci Biotech Biochem, 60, pp. 886-888; Lee, S.B., Mine, Y., Stevenson, R.M.W., Effects of hen egg yolk immunoglobulin in passive protection of rainbow trout against Yersinia ruckeri (2000) J Agric Food Chem, 48, pp. 110-115; Stevenson, R.M.W., Flett, D., Raymond, B.T., Enteric redmouth (ERM) and other enterobacterial infections of fish (1993) Bacterial Diseases of Fish V, pp. 80-105. , (Inglis R, Roberts J, Bromage NR, eds.). 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CAB International, Oxon, UK; Gutierrez, M.A., Miyazaki, T., Hatta, H., Kim, M., Protective properties of egg yolk IgY containing anti-Edwardsiella tarda antibody against paracolo disease in the Japanese eel, Anguilla japonica Temminck & Schlegel (1993) J Fish Dis, 16, pp. 113-122; Eterradossi, N., Toquin, D., Abbassi, H., Rivallan, G., Cotte, J.P., Guittet, M., Passive protection of specific pathogen free chicks against infectious bursal disease by in-ovo injection of semi-purified egg-yolk antiviral immunoglobulins (1997) J Vet Med, B44, pp. 371-383; Shimizu, M., Nagashima, H., Sano, K., Hashimoto, K., Ozeki, M., Tsuda, K., Hatta, H., Molecular stability of chicken and rabbit immunoglobulin G (1992) Biosci Biotech Biochem, 56, pp. 270-274; Shimizu, M., Nagashima, H., Hashimoto, K., Comparative studies on molecular stability of immunoglobulin G from different species (1993) Comp Biochem Physiol, 106 B, pp. 255-261; Otani, H., Matsumoto, K., Saeki, A., Hosono, A., Comparative studies on properties of hen egg yolk IgY and rabbit serum IgG antibodies (1991) Lebensm Wiss U Technol, 24, pp. 152-158; Pilz, I., Schwarz, E., Palm, W., Small-angle X-ray studies of the human immunoglobulin molecule (1977) Eur J Biochem, 75, pp. 195-199; Akita, E.M., Nakai, S., Production and purification of Fab(fragments from chicken egg yolk immunoglobulin Y (IgY) (1993) J Immunol Methods, 162, pp. 155-164","Mine, Y.; Department of Food Science, University of Guelph, Guelph, Ont. N1G2W1, Canada; email: ymine@uoguelph.ca",,"Mary Ann Liebert Inc.",1096620X,,JMFOF,,"English","J. Med. Food",Review,"Final",,Scopus,2-s2.0-0036754686
"Pogranichniy R.M., Yoon K.-J., Harms P.A., Sorden S.D., Daniels M.","6602307133;7401607376;7005117985;7003697171;8099122300;","Case-control study on the association of porcine circovirus type 2 and other swine viral pathogens with postweaning multisystemic wasting syndrome",2002,"Journal of Veterinary Diagnostic Investigation","14","6",,"449","456",,79,"10.1177/104063870201400601","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036833573&doi=10.1177%2f104063870201400601&partnerID=40&md5=ef951369c33bce14e1bf20a2f376b316","Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Department of Statistics, Iowa State University, Ames, IA 50011, United States","Pogranichniy, R.M., Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Yoon, K.-J., Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Harms, P.A., Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Sorden, S.D., Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Daniels, M., Department of Statistics, Iowa State University, Ames, IA 50011, United States","A field-based case-control study was conducted to assess the strength of association of porcine circovirus type 2 (PCV2) and some major swine viruses with postweaning multisystemic wasting syndrome (PMWS). Cases were defined as individual pigs with a clinical history of progressive weight loss and histopathological lesions characteristic of PMWS. Controls were pigs without clinical signs and histopathological lesions typical of PMWS. A total of 31 cases and 56 controls was identified from diagnostic submissions. Serum and various tissues were collected from all animals and assayed for PCV, porcine reproductive and respiratory syndrome virus (PRRSV), porcine parvovirus, porcine enterovirus types 1-3. swine influenza virus, porcine respiratory coronavirus, transmissible gastroenteritis virus, porcine endogenous retrovirus, porcine lymphotropic herpesvirus type 1, and bovine viral diarrhea virus. The proportion of case and control pigs positive for each virus was determined and statistically compared for determining the strength of the association that each virus had with PMWS individually or in combinations. Porcine circovirus type 2 had the strongest association (OR = 9.3, P = 0.006) with PMWS among the viruses tested for. Risk for PWMS was much higher (OR = 31.2, P = 0.0009) if the animal was concurrently infected with PCV2 and PRRSV, suggesting that development of PMWS may be enhanced by cofactor(s). Because PCV2 was also found in 62.5% of the controls, PCV2 from 5 cases and 4 controls were selected and genetically compared. No significant genetic difference was observed between PCV2 from PMWS and control pigs.",,"primer DNA; virus DNA; animal; animal disease; Arterivirus; article; case control study; Circoviridae; genetics; newborn; pathogenicity; polymerase chain reaction; risk; risk factor; swine; swine disease; virology; virus infection; wasting syndrome; weaning; Animals; Animals, Newborn; Case-Control Studies; Circoviridae Infections; Circovirus; DNA Primers; DNA, Viral; Odds Ratio; Polymerase Chain Reaction; Porcine respiratory and reproductive syndrome virus; Risk Factors; Swine; Swine Diseases; Wasting Syndrome; Weaning","Akiyoshi, D.E., Denaro, M., Zhu, H., Identification of a full-length cDNA for an endogenous retrovirus of miniature swine (1998) J Virol, 72, pp. 4503-4507; Allan, G., Meehan, B., Todd, D., Novel porcine circoviruses from pigs with wasting disease syndromes (1998) Vet Rec, 142, pp. 467-468; Allan, G.M., Kennedy, S., McNeilly, F., Experimental reproduction of severe wasting disease by co-infection of pigs with porcine circovirus and porcine parvovirus (1999) J Comp Pathol, 121, pp. 1-11; Allan, G.M., McNeilly, F., Cassidy, J.P., Pathogenesis of porcine circovirus; experimental infections of colostrum deprived piglets and examination of pig foetal material (1995) Vet Microbiol, 44, pp. 49-64; Allan, G.M., McNeilly, F., Ellis, J., Experimental infection of colostrum deprived piglets with porcine circovirus 2 (PCV2) and porcine reproductive and respiratory syndrome virus (PRRSV) potentiates PCV2 replication (2000) Arch Virol, 145, pp. 2421-2429; Allan, G.M., McNeilly, F., Kennedy, S., Isolation of porcine circovirus-hke viruses from pigs with a wasting disease in the USA and Europe (1998) J Vet Diagn Invest, 10, pp. 3-10; Allan, G.M., McNeilly, F., Kennedy, S., Immunostimulation, PCV2 and PMWS (2000) Vet Rec, 147, pp. 170-171; Bolin, S.R., Ridpath, J.F., Prevalence of bovine viral diarrhea virus genotypes and antibody against those viral genotypes in fetal bovine serum (1998) J Vet Diagn Invest, 10, pp. 135-139; Breslow, N.E., Day, N.E., The analysis of case-contron studies (1984) Statistical Methods in Cancer Research, pp. 250-256. , ed. 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IA; Harms, P.A., Sorden, S.D., Halbur, P.G., Experimental reproduction of severe disease in CD/CD pigs concurrently infected with type 2 porcine circovirus and porcine reproductive and respiratory syndrome virus (2001) Vet Pathol, 38, pp. 528-539; Howard, C.J., Immunological responses to bovine virus diarrhoea virus infections (1990) Rev Sci Tech, 9, pp. 95-103; Kennedy, S., Moffett, D., McNeilly, F., Reproduction of lesions of postweaning multisystemic wasting syndrome by infection of conventional pigs with porcine circovirus type 2 alone or in combination with porcine parvovirus (2000) J Comp Pathol, 122, pp. 9-24; Kim, H.S., Kwang, J., Yoon, I.J., Enhanced replication of porcine reproductive and respiratory syndrome (PRRS) virus in a homogeneous subpopulation of MA-104 cell line (1993) Arch Virol, 133, pp. 477-483; Krakowka, S., Ellis, J.A., McNeilly, F., Activation of the immune system is the pivotal event in the production of wasting disease in pigs infected with porcine circovirus-2 (PCV2) (2001) Vet Pathol, 38, pp. 31-42; 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Zimmerman JJ, Yoon K-J, Stevenson G, Dee SA, National Pork Producers Council, Des Moines, IA","Pogranichniy, R.M.; Dept. Vet. Diagn. Prod. Anim. Med., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12423025","English","J. Vet. Diagn. Invest.",Article,"Final",,Scopus,2-s2.0-0036833573
"Escorcia M., Fortoul T.I., Petrone V.M., Galindo F., López C., Téllez G.","6508130393;55993654400;6602464807;7003471211;55183160400;10639011300;","Gastric gross and microscopic lesions caused by the UNAM-97 variant strain of infectious bronchitis virus after the eighth passage in specific pathogen-free chicken embryos",2002,"Poultry Science","81","11",,"1647","1652",,5,"10.1093/ps/81.11.1647","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036835244&doi=10.1093%2fps%2f81.11.1647&partnerID=40&md5=699bfadb542597d5036c41d474e5bd66","Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; Depto. de Biol. Celular Y Tisular, Facultad de Medicina, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico","Escorcia, M., Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; Fortoul, T.I., Depto. de Biol. Celular Y Tisular, Facultad de Medicina, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; Petrone, V.M., Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; Galindo, F., Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; López, C., Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; Téllez, G., Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico","Herein we report a description of gross and microscopic lesions found in specific pathogen-free chicken embryos caused by UNAM-97 infectious bronchitis virus (IBV) variant strain after the eighth passage. Embryos were divided into three groups and were inoculated in the chorioallantoic sac with 0.2 mL of UNAM-97, Mass 41 IBV (positive control), or sterile PBS (negative control). Forty-eight hours later the allatoic fluid was taken and used to start a cycle of eight passages through 9-d-old embryos. Seven days after the last passage, embryos were harvested and macroscopic lesions in all organs were recorded. Proventriculus and gizzard samples were obtained from all embryos and routinely processed for microscopic and ultrastructural examinations. The UNAM-97 IBV variant strain caused two macroscopic lesions uncommon for Mexican strains: thin-walled proventriculus and gizzard, as well as urate accumulation within an extra-embryonic peritoneal sac, leaving the body through the umbilical duct and accompanied by the yolk sac. At microscopic level, two relevant findings were observed to be produced by this variant. In the proventriculus, there was a decrease in the gland papillary branching, while the gizzard showed a significant reduction in mucosa thickness and tubular-to-proliferative-cell ratio, as well as an absence of hyaline secretion in the lumen. Electrodense material scattered in proventricular and gizzard cells was observed, with a structure consistent with that of coronaviruses. These pathological chicken embryo findings have not been reported as being caused by other IBV strains in Mexico.","Electron microscopy; Embryo; Histology; Infectious bronchitis virus; Variant","Aves; Avian infectious bronchitis virus; Gallus gallus; animal; animal disease; article; Avian infectious bronchitis virus; avian stomach; bird disease; chick embryo; electron microscopy; germfree animal; pathogenicity; pathology; prenatal development; randomization; ultrastructure; virology; virus culture; virus infection; Animals; Chick Embryo; Coronavirus Infections; Gizzard; Infectious bronchitis virus; Microscopy, Electron; Poultry Diseases; Proventriculus; Random Allocation; Serial Passage; Specific Pathogen-Free Organisms","Allen, T.C., Hematoxylin and eosin (1992) Laboratory Methods in Histotechnology, 3rd Ed., pp. 53-58. , E. B. Prophet, B. Mills, J. B. Arrington, and L. H. Sobin, eds., Armed Forces Institute of Pathology, Washington, DC; Camacho, E., Soto, E., Lozano, B., Sarfati, D., Gay, M., Murillo, M.A., Borrego, J.L., Murillo, J.J., Los complejos respiratorio-septicémicos de las aves en México (2000) Proceedings of the XII Curso de Actualización Avimex. Asumiendo El Reto en la Prevención Y Control de Los Complejos Respiratorios de Las Aves en El Nuevo Milenio, , CD-ROM, Laboratorios Avimex S.A. de C.V., Mexico City; Cargill, P., Contemporary European infectious bronchitis variants (1998) World's Poult. Sci. J., 14, pp. 52-53; Casaubon, M.T., Ledesma, N., Petrone, V., Fehervari, T., Del Río, J.C., Case report of avian indigestion and diuresis syndrome in stunted mexican broiler chickens (1997) XI International Congress of the World Veterinary Poultry Association, pp. 18-22. , Budapest; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry, 10th Ed., pp. 511-526. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds., Iowa State University Press, Ames, IA; Cook, J., Novel infectious bronchitis virus causes higher mortality (1996) World's Poult. Sci. J., 12, pp. 78-79; Del Río, J.C., Petrone, V.M., Escorcia, M., Téllez, G., Hallazgos histológicos entéricos en pollo de engorda inoculado con la cepa UNAM-97 de bronquitis infecciosa aviar (1999) Proceedings of the VII Congreso de la Sociedad Mexicana de Patólogos Veterinarios, pp. 18-19. , Sociedad Mexicana de Patólogos Veterinarios, Mexico City; Escorcia, M., (1999) Caracterización Molecular de Virus de Bronquitis Infecciosa Aviar de Aislamientos en México, , M.Sc. Thesis. Facultad de Medicina Veterinaria y Zootecnia, Universidad Nacional Autónoma de México, Mexico City; Escorcia, M., Jackwood, M., Lucio, B., Petrone, V.M., López, C., Fehervari, T., Téllez, G., Characterization of Mexican strains of avian infectious bronchitis isolated during 1997 (2000) Avian Dis., 44, pp. 944-947; Escorcia, M., Petrone, V.M., López, C., Lucio, B., Fehervari, T., Aislamiento y caracterización de variantes del virus de bronquitis infecciosa aviar de aves vacunadas en México (1998) Proceedings of the III Congreso Nacional de Vacunología, pp. 60-63. , El Colegio Nacional, Mexico City; García, G.J., Gay, M., Escamilla, J., Soto, E., Sarfati, D., Lozano, B., ¿Qué está pasando con la bronquitis infecciosa aviaren México? (2001) Proceedings of the XIII Curso Avimex. Respuestas a Las Patologías Críticas en la Avicultura Moderna, pp. 45-52. , Laboratorios Avimex S.A. de C.V., Mexico City; Gay, M., Suárez, A., Lozano, B., Soto, E., Sarfati, D., Escamilla, J., Alvarado, C., Morales, A., Avances en la prevención de bronquitis infecciosa en México (2000) Proceedings of the XII Curso de Actualización Avimex. Asumiendo El Reto en la Prevención Y Control de Los Complejos Respiratorios de Las Aves en El Nuevo Milenio, , CD-ROM. Laboratorios Avimex S.A. de C.V., Mexico City; Gelb, J., Jackwood, M.W., Infectious Bronchitis (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 169-174. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Read, eds. American Association of Avian Pathologists, Kennett Square, PA; Goodwin, M.A., Hafner, S., Bounous, D.I., Latimer, K.S., Player, E.C., Niagro, F.D., Campagnoli, R.P., Brow, J., Viral proventriculitis in chickens (1996) Avian Dis., 25, pp. 369-379; Gough, R.E., Randall, C.J., Dagless, M., Alexander, D.J., Cox, W.J., Pearson, D., A new strain of infectious bronchitis virus infecting domestic fowl in Great Britain Vet (1992) Rec., 130, pp. 493-494; Keeler, D.L., Reed, K.L., Nix, W.A., Gelb, J., Serotype identification of avian infectious bronchitis virus by RT-PCR of the peplomer (S1) gene (1998) Avian Dis., 42, pp. 275-284; Kusters, J.G., Niesters, G.M., Lenstra, J.A., Horzinedk, M.C., Van Der Zeust, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Lozano, B., Gay, M., Sarfati, D., Soto, E., Suárez, A., Aranda, M., Escamilla, J., García, J., Aislamiento e identificación de una posible variante o nuevo serotipo del virus de la bronquitis infecciosa en México (1998) Proceedings of the X Curso de Actualización Avimex. Salud Y Productividad Aviar, pp. 80-91. , Laboratorios Avimex S.A. de C.V., Mexico City; Mayo, M.A., Pringle, D.R., Virus taxonomy-1997 (1998) J. Gen. Virol., 79, pp. 649-657; Muneer, M.A., Newman, J.A., Halvorson, D.A., Sivanandan, V., Nagaraja, K.V., Efficacy of infectious bronchitis virus vaccines against heterologous challenge (1988) Res. Vet. Sci., 45, pp. 22-27; Page, R.K., Fletcher, O.J., Rowland, G.N., Gaudry, D., Villegas, P., Malabsorption syndrome in broiler chickens (1982) Avian Dis., 26, pp. 618-624; Petrone, V.M., Escorcia, M., Téllez, G., Hallazgos anatomopatológicos de embriones de pollo inoculados con cepa variante de bronquitis infecciosa aviar (1999) Proceedings of the VII Congreso de la Sociedad Mexicana de Patólogos Veterinarios, pp. 46-47. , Sociedad Mexicana de Patólogos Veterinarios, Mexico City; Song, Ch., Lee, Y., Lee, Ch., Sung, H., Kim, J., Mo, I., Izumiya, Y., Mikami, T., Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed by a recombinant baculovirus (1998) J. Gen. Virol., 79, pp. 719-723; Steinhauer, D.A., Holland, J.J., Direct method for quantitation of extreme polymerase error frequencies at selected single base sites in viral ARN (1986) J. Virol., 192, pp. 710-716; Zar, J., Circular distributions: Hypothesis testing (1996) Biostatistical Analysis, 3rd Ed., pp. 615-662. , J. Zar, ed. Prentice-Hall, Upper Saddle River, NJ","Escorcia, M.; Depto. de Prod. Animal: Aves, Fac. de Med. Veterinaria Y Zootecnia, Ciudad Universitaria, Coyoacán, D. F., C. P. 04510, Mexico; email: magdaescorcia@yahoo.com",,"Poultry Science Association",00325791,,,"12455591","English","Poult. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0036835244
"Pakpinyo S., Ley D.H., Barnes H.J., Vaillancourt J.P., Guy J.S.","6507113360;7005808545;7102581732;7004505622;7202723649;","Prevalence of enteropathogenic Escherichia coli in naturally occurring cases of poult enteritis-mortality syndrome",2002,"Avian Diseases","46","2",,"360","369",,17,"10.1637/0005-2086(2002)046[0360:POEECI]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035992108&doi=10.1637%2f0005-2086%282002%29046%5b0360%3aPOEECI%5d2.0.CO%3b2&partnerID=40&md5=0a5deb8af69d3948b4e07b0e405c4492","Department of Farm Animal Health and Resource Management, North Carolina State University, Raleigh, NC 27606, United States; Department of Microbiology, Pathology, and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","Pakpinyo, S., Department of Farm Animal Health and Resource Management, North Carolina State University, Raleigh, NC 27606, United States; Ley, D.H., Department of Farm Animal Health and Resource Management, North Carolina State University, Raleigh, NC 27606, United States; Barnes, H.J., Department of Farm Animal Health and Resource Management, North Carolina State University, Raleigh, NC 27606, United States; Vaillancourt, J.P., Department of Farm Animal Health and Resource Management, North Carolina State University, Raleigh, NC 27606, United States; Guy, J.S., Department of Microbiology, Pathology, and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","Enteropathogenic Escherichia coli (EPEC) previously were identified in poult enteritis-mortality syndrome (PEMS)-affected turkeys and associated as a cause of this disease. In the present study, the prevalence of EPEC in PEMS-affected turkeys was examined retrospectively with archived rissues and intestinal conrents collected from 12 PEMS-affected turkey flocks in 1998. Formalin-fixed intestinal tissues were examined by light and electron microscopy for attaching and effacing (AE) lesions characteristic of EPEC, and frozen (-75 C) intestinal conrents were examined for presence of EPEC. Escherichia coli isolates were characterized on the basis of epithelial cell attachment, fluorescent actin staining (FAS) test, and presence of E. coli attaching/effacing (EAE), shigalike toxin (SLT) type I, SLT II, and bundle-forming pilus (BFP) genes by polymerase chain reaction procedures. EPEC isolates were examined for pathogenicity and ability to induce AE lesions in experimentally inoculated young turkeys. AE lesions were identified by light microscopy in Giemsa-stained intestines from 7 of 12 PEMS-affected turkey flocks. Lesions consisted of bacterial microcolonies attached to epithelial surfaces with epithelial degeneration at sites of attachment and inflammatory infiltration of the lamina propria. Electron microscopy confirmed the identity of AE lesions in six of seven flocks determined to have AE lesions by light microscopy. EPEC were identified in 4 of 12 flocks on the basis of the presence of EAE genes and absence of SLT I and SLT II genes; all isolates lacked BFP genes. EPEC isolates produced AE lesions and variable mortality in turkeys coinfected with turkey coronavirus. In total, EPEC were associated with 10 of 12 (83%) naturally occurring PEMS cases on the basis of identification of AE lesions and/or EPEC isolates. These findings provide additional evidence suggesting a possible role for EPEC in the pathogenesis of PEMS.","Enteropathogenic Escherichia coli; Poult enteritis-mortality syndrome","Aves; Bacteria (microorganisms); Coronavirus; Escherichia coli; Escherichia coli; Meleagris gallopavo; Turkey coronavirus; animal; animal disease; article; bacterium adherence; bird disease; electron microscopy; Enterobacter infection; epithelium cell; Escherichia coli; genetics; Giemsa stain; isolation and purification; microbiology; pathogenicity; pathology; prevalence; retrospective study; turkey (bird); ultrastructure; virulence; Animals; Azure Stains; Bacterial Adhesion; Epithelial Cells; Escherichia coli; Escherichia coli Infections; Microscopy, Electron; Poult Enteritis Mortality Syndrome; Poultry Diseases; Prevalence; Retrospective Studies; Turkeys; Virulence","Ausubel, F.M., Brent, R., Kingston, R., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., Preparation of genomic DNA from bacteria (1995) Short protocols in molecular biology, 3rd ed., pp. 211-212; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of poultry, 10th ed., pp. 1025-1030. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Brown, T.P., Garcia, A., Kelley, L., Spiking mortality of turkey poults: 1. Experimental reproduction in isolation facilities (1997) Avian Dis., 41, pp. 604-609; Carver, D.K., Vaillancourt, J.P., Stringham, S.M., Descriptive epidemiology of coronavirus in commercial turkeys in North Carolina (1998) Proc. 135th Annual Convention of the American Veterinary Medicine Association, p. 191. , Baltimore, MD; Donnenberg, M.S., Nataro, J.P., Methods for studying adhesion of diarrheagenic Escherichia coli (1995) Adhesion of microbial pathogens, pp. 324-335. , R. J. Doyle and I. Ofek, eds. Academic Press, San Diego, CA; Edens, F.W., Parkhurst, C.R., Qureshi, M.A., Casas, I.A., Havenstein, G.B., Atypical Escherichia coli strains and their association with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 952-960; Edens, F.W., Qureshi, R.A., Parkhurst, C.R., Qureshi, M.A., Havenstein, G.B., Casas, I.A., Characterization of two Escherichia coli isolates associated with poult enteritis and mortality syndrome (1997) Poult. Sci., 76, pp. 1665-1673; Fisher, J., Maddox, C., Moxley, R., Kinden, D., Miller, M., Pathogenicity of a bovine attaching and effacing Escherichia coli isolate lacking shiga-like toxins (1994) Am. J. Vet. Res., 55, pp. 991-999; Fukui, H., Sueyoshi, M., Haritani, M., Nakazawa, M., Naitoh, S., Tani, H., Uda, Y., Natural infection with attaching and effacing Escherichia coli (O 103:H-) in chicks (1995) Avian Dis., 39, pp. 912-918; Gannon, V.P.J., King, R.K., Kim, J.Y., Golsteyn Thomas, E.J., Rapid and sensitive method for detection of shiga-like toxin-producing Escherichia coli in ground beef by using the polymerase chain reaction (1992) Appl. Environ. Microbiol., 58, pp. 3809-3815; Gunzburg, S.T., Tornieporth, N.G., Riley, L.W., Identification of enteropathogenic Escherichia coli by PCR-based detection of the bundle forming pilus gene (1995) J. Clin. Microbiol., 33, pp. 1375-1377; Guy, J.S., Barnes, H.J., Partial characterization of a turkey enterovirus-like virus (1991) Avian Dis., 35, pp. 197-203; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Guy, J.S., Smith, L.G., Breslin, J.J., Vaillancourt, J.P., Barnes, H.J., High mortality and growth depression experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus (2000) Avian Dis., 44, pp. 105-113; Jerse, A.E., Yu, J., Tall, B.D., Kaper, J.B., A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 7839-7843; Knutton, S., Baldwin, T., Williams, P.H., McNeish, A.S., Actin accumulation at sites of bacterial adhesion to tissue culture cells: Basis of a new diagnostic test for enteropathogenic and enterohemorrhagic Escherichia coli (1989) Infect. Immun., 57, pp. 1290-1298; Ley, D.H., Levy, M.G., Hunter, L., Corbett, W., Barnes, H.J., Cryptosporidia-positive rates of avian necropsy accessions determined by examination of auramine-stained fecal smears (1988) Avian Dis., 32, pp. 108-113; Moon, H.W., Whipp, S.C., Argenzio, R.A., Levine, M.M., Giannella, R.A., Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines (1983) Infect. Immun., 41, pp. 1340-1351; Moxley, R.A., Francis, D.H., Natural and experimental infection with an attaching and effacing strain of Escherichia coli in calves (1986) Infect. Immun., 53, pp. 339-346; Nataro, J.P., Kaper, J.B., Diarrheagenic Escherichia coli (1998) Clin. Microbiol. Rev., 11, pp. 142-201; Robins-Browne, R.M., Traditional enteropathogenic Escherichia coli of infantile diarrhea (1987) Rev. Infect. Dis., 9, pp. 28-52; Shivaprasad, H.L., Crespo, R.C., Daft, B., Read, D., Attaching and effacing E. coli associated with enteritis in poultry (1998) Proc. 135th Annual Convention of the American Veterinary Medical Association, p. 184. , Baltimore, MD; Sueyoshi, M., Fukui, H., Tanaka, S., Nakazawa, M., Ito, K., A new adherent form of an attaching and effacing Escherichia coli (EAEA+, bfp-) to the intestinal epithelium of chicks (1996) J. Vet. Med. Sci., 58, pp. 1145-1147; Turk, J., Maddox, C., Fales, W., Ostund, E., Miller, M., Johnson, G., Pace, L., Kreeger, J., Examination for heat-labile, heat-stable, and shiga-like toxins and for EAEA gene in Escherichia coli isolates obtained from dogs dying with diarrhea: 122 Cases (1992-1996) (1998) J. Am. Vet. Med. Assoc., 212, pp. 1735-1736","Guy, J.S.; Department of Microbiology, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"12061645","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0035992108
"Grandemange E., Mathevet P., Charrier E., Davot J.-L.","55953657300;7004151059;6603201530;6602615166;","Use of marbofloxacin to treat K99 Escherichia coli gastroenteritis in newborn calves",2002,"Irish Veterinary Journal","55","4",,"180","189",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036004403&partnerID=40&md5=ae314974a6821b3d026e4646f736ac9d","Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France","Grandemange, E., Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France; Mathevet, P., Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France; Charrier, E., Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France; Davot, J.-L., Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France","In an international multicentre comparative randomised trial, 184 calves aged less than five days presenting with neonatal diarrhoea were treated for three days either with marbofloxacin administered orally (1 mg/kg/d) or with a positive control (amoxicillin + clavulanic acid combination, ACA, 12.5 mg/kg/12h). The calves were selected if they had diarrhoea which was associated with one clinical sign from the following: Loss of appetite, altered general condition or clinically detectable dehydration. Faecal samples were taken from all the calves on day zero (D0) before treatment. An ELISA test was carried out on these samples to detect E. coli K99, rotavirus, coronavirus, cryptosporidium. When the result for E. coli K99 was positive, the E. coli K99 strains were cultured and sensitivity to marbofloxacin was measured by determining the Minimum Inhibitory Concentration (MIC) and sensitivity to ACA by the disk method. The animals were monitored on D0 (day of inclusion), D1, D2, D3 and D7 on the following parameters: rectal temperature, general condition, appetite, tenesmus, suck reflex, faecal consistency, presence of blood in faeces and persistence of skin fold. These parameters were evaluated based upon a predefined grading scoring system except for temperature which was recorded in °C. The main isolate was E. coli K99, which was found in approximately 50 per cent of faecal samples on D0 (46.2 per cent in the marbofloxacin-treated group and 55.4 per cent in the ACA-treated group). These bacterial strains were all sensitive to marbofloxacin (MIC50 = 0.015μg/ml) except for one strain which was resistant. In comparison, 84.8 per cent of the strains were resistant or showed intermediate sensitivity to ACA. Marbofloxacin was significantly more effective than ACA in the treatment of neonatal diarrhoea on several clinical criteria. The clinical results for marbofloxacin on D3 were higher than that of ACA with 72.5 per cent cured against 57.8 per cent, respectively (p&lt;0.05). Furthermore, the time to cure was significantly shorter for the animals in the marbofloxacin group (p=0.006) and the evolution of general condition, appetite and faecal consistency was significantly better for this group.","Calves; Cattle; Diarrhoea; Escherichia coli; Marbofloxacin, Amoxicillin and clavulanic acid combination","amoxicillin plus clavulanic acid; ampicillin; apramycin; cefalexin; cefalotin; cefquinome; ceftiofur; colistin; enrofloxacin; flumequine; gentamicin; marbofloxacin; nalidixic acid; neomycin; oxolinic acid; streptomycin; sulfanilamide; tetracycline; appetite disorder; article; bacterial strain; cattle; Coronavirus; Cryptosporidium; dehydration; enzyme linked immunosorbent assay; Escherichia coli; gastroenteritis; minimum inhibitory concentration; nonhuman; rectum temperature; Rotavirus; skinfold; symptomatology","Amedeo, J., Goillandeau, P., Roger, M.F., Etiologie des affections néonatales du veau. Incidence de la crytosporidiose (1995) Bulletin des Groupements Techniques Veterinaires, 1, pp. 35-41; Bonal, C., Moussa, A., Les entérites néonatales virales du veau, numéro spécial 'gastro-entérologie bovine' (1993) Le Point Vétérinaire, 25, pp. 33-38; Brugere-Picoux, J., Quintin-Colonna, F., La campylobactériose intestinale des bovins (1983) Recueil de Médecine Vétérinaire, 159, pp. 257-260; Fedida, M., Martel, J.L., Perrin, B., Moussa, A., Coudert, M., Enquêtes épidémiologiques réalisées en France sur les diarrhées néonatales (1983) Recueil de Médecine Vétérinaire, 159, pp. 191-201; Rings, D.M., Salmonellosis in calves (1985) Veterinary Clinics of North America: Food Animal Practice, 1, pp. 529-539; Janke, B.H., Francis, D.H., Collins, J.E., Libal, M.C., Zeman, D.H., Johnson, D.D., Neiger, R.D., Attaching and effacing Escherichia coli infection as a cause of diarrhea in young calves (1990) Journal of the Americal Veterinary Medicine Association, 196, pp. 897-901; Kirkpatrick, C.E., Cryptosporidium infection as a cause of calf diarrhea (1985) Veterinary Clinics of North America: Food Animal Practice, 1, pp. 515-528; Lucas, F., Popoff, M., Corthier, G., Entérotoxines bactériennes: Structures, modes d'action (1991) Annales de Recherches Véterinaires, 22, pp. 147-162; Mainil, J., Les colibacilloses dans l'espèce bovine (1993) Annales de Médecine Véterinaire, 137, pp. 343-350; Mainil, J., Shiga/Verocytotoxins and Shiga/verotoxigenic Escherichia coli in animals (1999) Veterinary Research, 30, pp. 235-257; Mainil, J.G., Jacqemin, E.R., Kaeckenbeeck, A.E., Pohl, P.H., Association between the effacing (eae) gene and the Shiga-like toxin-encoding genes in Escherichia coli isolates from cattle (1993) American Journal of Veterinary Research, 54, pp. 1064-1067; Murray, J.M., Salmonella: Virulence factors and enteric salmonellosis (1986) Journal of the American Veterinary Medical Association, 189, pp. 145-147; Navetat, H., Schelcher, F., Rizet, C., Espinasse, J., Les gastro-entérites paralysantes du veau: Aspects cliniques et thérapeutiques (1995) Le Point Vétérinaire, 27, pp. 84-86; Roussel, A.J., Brumbaugh, G.W., Traitement des diarrhées néonatales chez le veau (1993) Le Point Vétérinaire Numéro Spécial 'Gastro-Entérologie Bovine', 25, pp. 61-69; Schelcher, F., De Ricke, J., Martel, J.L., Valarcher, J.F., Espinasse, J., Diarrhées colibacillaires néonatales du veau (1993) Le Point Vétérinaire, Numéro Spécial 'Gastro-Entérologie Bovine', 25, pp. 19-31; Schelcher, F., Valarcher, J.F., Navetat, H., Espinasse, J., Aspects cliniques de l'infection des bovins par le virus de la maladie des muqueuses (BVDV) (1993) Bulletin des Groupements Techniques Veterinaires, 4, pp. 23-33; Schelcher, F., Valarcher, J.F., Physiopathologie des salmonelloses bovines (1997) Bulletin des Groupements Techniques Veterinaires, 2, pp. 25-30; Torres-Medina, A., Schlafer, D.H., Mebus, C.A., Rotaviral and coronaviral diarrhea (1985) Veterinary Clinics of North America: Food Animal Practice, 1, pp. 471-493","Grandemange, E.; Centre de Recherche Vetoquinol, BP189, 70204 Lure Cedex, France",,,03680762,,IVTJA,,"English","Ir. Vet. J.",Article,"Final",,Scopus,2-s2.0-0036004403
"Soñez C.A., Mugnaini M.T., Godino S., Soñez M.V., Sánchez O., Fernández S.","6506767452;8567034800;6602983016;6506205286;7004581577;7202872675;","Acute infectious gastroenteritis in Rio Cuarto: clinic, diagnosis and epidemiology with special reference to viral infections [Gastroenteritis aguda infecciosa en Rio Cuarto: clínica, diagnóstico y epidemiología con especial referencia a infecciones virales.]",2002,"Revista de la Facultad de Ciencias Médicas (Córdoba, Argentina)","59","1",,"45","55",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642337698&partnerID=40&md5=a684a631455bcdf361e7dd4836bcf8e3","Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.","Soñez, C.A., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.; Mugnaini, M.T., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.; Godino, S., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.; Soñez, M.V., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.; Sánchez, O., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.; Fernández, S., Dpto. de Anatomía, FAV, Universidad Nacional de Río Cuarto.","The objectives of the present study are to describe the clinics view of acute infectious gastroenteritis (GE) at the community, in primary and secondary attention health centers, with special references to viral aetiology (VIGE); to correlate with drinkable water and excrete treatment; to develop for the first time a fast diagnostic using electron microscopy in Río Cuarto, Córdoba, Argentina, considering the university and community collaboration in the viral diagnostic. It has been during one year, 122 cases of acute GE, over its clinics epidemiology and diagnostic aspects (1999-2000). With conventional laboratory methods, it has been determined the bacteria and micotic aetiology (NOVIGE); the virology diagnostic with electron microscopy; and the use of the statistics for the data analysis. The microbial findings has been: pathogenics bacteria (31.7%), fungus (17%), parasites (1.2%), rotavirus (16.4%), calicivirus (1.6%), adenovirus and coronavirus (1.6%). The clinics findings are presents like digestive and extra-digestive signs, separated in NOVIGE (and no-diagnosticated) and VIGE groups. The seasonal viral and no-viral distributions are present in fig. 5. There are statistics signification: the NOVIGE in summer period (49%) against the VIGE (12.5%) (p < 0.0003); the VIGE in winter period (87.5%) against the VIGE in summer period (12.5%) (p < 0.0003); the GE aetiology (VIGE and NOVIGE) in associated with age groups (p < 0.0003); the vomits preceding diarrhoea in VIGE was 58% and in NOVIGE (19.5%) (P < 0.001). It has been presented without significative differences all the clinics signs and laboratory examinations; the breeding signs for the younger 2 years group compared with the 2 years older; the age correlation (< and > 2 years) and season (winter-summer) with the 16% for the first in VIGE (62.5% rotavirus); the absence of health systems at the NOVIGE (70%) and with both (29%); and others epidemiology considerations of the sequence. With came to conclusion that in our city: 1. there are VIGE with signficative participation of rotavirus; 2. its distribution are winter and age group, also considering the other age groups and virosis; 3. the NOVIGE may difference at the clinic sign like vomit, between all the possible sintomatology; 4. the principal cause of diarrhoea and the no seasonal distribution are the NOVIGE; 5. there are not a strong relationship of diarrhoea by shortage environmental health in this study; 6. it's possible in Río Cuarto to made a fast and direct virology diagnostic using an electron microscopy.",,"fresh water; acute disease; adolescent; adult; aged; Argentina; article; child; communicable disease; comparative study; diarrhea; electron microscopy; feces; gastroenteritis; human; infant; microbiology; middle aged; newborn; preschool child; Rotavirus; season; ultrastructure; virology; virus infection; water supply; Acute Disease; Adolescent; Adult; Aged; Aged, 80 and over; Argentina; Child; Child, Preschool; Community-Acquired Infections; Diarrhea; Feces; Fresh Water; Gastroenteritis; Humans; Infant; Infant, Newborn; Microscopy, Electron; Middle Aged; Rotavirus; Rotavirus Infections; Seasons; Water Microbiology; Water Supply",,"Soñez, C.A.email: csonez@avv.unrc.edu.ar",,,00146722,,,"12934244","Spanish","Rev Fac Cien Med Univ Nac Cordoba",Article,"Final",,Scopus,2-s2.0-0642337698
"Lin T.L., Loa C.C., Tsai S.C., Wu C.C., Bryan T.A., Leon Thacker H., Hooper T., Schrader D.","7404860140;6602648721;55462024400;7501664098;7005517787;15737301500;7005121335;7007179253;","Characterization of turkey coronavirus from turkey poults with acute enteritis",2002,"Veterinary Microbiology","84","1-2",,"179","186",,10,"10.1016/S0378-1135(01)00447-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037011835&doi=10.1016%2fS0378-1135%2801%2900447-3&partnerID=40&md5=830252aa578190ad58c861c351905cb5","Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States","Lin, T.L., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Loa, C.C., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Tsai, S.C., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T.A., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Leon Thacker, H., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Department of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States","The present study was to characterize turkey coronavirus associated with turkey poult enteritis and mortality. Intestinal contents or intestines from affected turkey poults and inoculated turkey embryos contained coronaviruses as revealed by electron microscopy or were positive for turkey coronavirus by immunofluorescent antibody assay. Sucrose density gradient ultracentrifugation of the virus-containing intestinal homogenate yielded two opalescent bands corresponding to the buoyant densities of 1.14-1.15 and 1.18-1.20 g/ml, respectively. Coronaviral particles from intestinal contents or the sucrose density gradient preparation were mainly spherical in shape and had envelope and central depression. They were surrounded by a fringe of regularly spaced petal-shaped projections attached to the particles by a short stalk. Purified viruses hemagglutinated rabbit erythrocytes with a titer of 16. Major protein bands of purified viruses analyzed by SDS-PAGE were located at 200, 100-110, 50-60, and 30-35 kDa. The patterns of protein bands were consistent with those of Minnesota or Quebec turkey coronavirus isolates. A 568 bp nucleotide fragment of turkey coronavirus spike protein gene was amplified from RNA of inoculated turkey embryo intestine or purified virus. Sequence analysis of the 568 bp PCR product revealed high degree of identity with the corresponding spike protein gene sequence of human and bovine coronaviruses. The results indicated that turkey coronavirus was associated with turkey poults with acute enteritis. © 2002 Elsevier Science B.V. All rights reserved.","Characterization; Coronavirus; Enteritis; Turkey","nucleotide; RNA; animal experiment; animal model; animal tissue; article; controlled study; Coronavirus; electron microscopy; embryo; enteritis; erythrocyte; gene; gene amplification; gene sequence; immunofluorescence test; intestine; mortality; nonhuman; polyacrylamide gel electrophoresis; sequence analysis; technique; tissue homogenate; turkey (bird); virus envelope; virus morphology; Acute Disease; Animals; Animals, Newborn; Base Sequence; Centrifugation, Density Gradient; Coronavirus, Turkey; Electrophoresis, Polyacrylamide Gel; Enteritis, Transmissible, of Turkeys; Fluorescent Antibody Technique, Indirect; Intestines; Microscopy, Electron; Molecular Sequence Data; Polymerase Chain Reaction; Sequence Alignment; Sequence Analysis; Turkeys; Bovinae; Coronavirus; Oryctolagus cuniculus; Turkey coronavirus","Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanatephenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1985) Avian Dis., 30, pp. 319-326; Dea, S., Tijssen, P., Identification of the structural proteins of turkey enteric coronavirus (1988) Arch. Virol., 99, pp. 173-186; Dea, S., Tijssen, P., Viral agents associated with outbreaks of diarrhea in turkey flocks in Quebec (1988) Can. J. Vet. Res., 52, pp. 53-57; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) Am. J. Vet. Res., 35, pp. 1549-1552; Deshmukh, D.R., Sautter, J.H., Patel, B.L., Pomeroy, B.S., Histopathology of fasting and bluecomb disease in turkey poults and embryos experimentally infected with bluecomb disease coronavirus (1974) Avian Dis., 20, pp. 631-640; Gonder, E., Patel, B.L., Pomeroy, B.S., Scanning electron, light, and immunofluorescent microscopy of coronaviral enteritis of turkeys (bluecomb) (1976) Am. J. Vet. Res., 37, pp. 1435-1439; Kuenkel, F., Herrler, G., Structural and functional analysis of the S proteins of two human coronavirus OC43 strains adapted to growth in different cells (1996) Arch. Virol., 1411, pp. 1123-1131; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 1265-1267; Rekik, M.R., Dea, S., Comparative sequence analysis of a polymorphic region of the spike glycoprotein S1 subunit of enteric bovine coronavirus isolates (1994) Arch. Virol., 135, pp. 319-331; Saif, L.J., Coronavirus immunogens (1993) Vet. Microbiol., 37, pp. 285-297; Zhang, X., Kousoulas, K.G., Storz, J., Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses (1991) Virology, 183, pp. 397-404","Lin, T.L.; Dept. of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,,03781135,,VMICD,"11731170","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0037011835
"van Elden L.J.R., van Kraaij M.G.J., Nijhuis M., Hendriksen K.A.W., Dekker A.W., Rozenberg-Arska M., van Loon A.M.","6602259994;6603293814;6701777688;6506719198;7101888434;7006237405;35476145800;","Polymerase chain reaction is more sensitive than viral culture and antigen testing for the detection of respiratory viruses in adults with hematological cancer and pneumonia",2002,"Clinical Infectious Diseases","34","2",,"177","183",,123,"10.1086/338238","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037079850&doi=10.1086%2f338238&partnerID=40&md5=3beabd60ac73b6de1ea2e39a08ab4a84","Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands; Department of Hematology, University Medical Center Utrecht, Utrecht, Netherlands","van Elden, L.J.R., Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands; van Kraaij, M.G.J., Department of Hematology, University Medical Center Utrecht, Utrecht, Netherlands; Nijhuis, M., Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands; Hendriksen, K.A.W., Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands; Dekker, A.W., Department of Hematology, University Medical Center Utrecht, Utrecht, Netherlands; Rozenberg-Arska, M., Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands; van Loon, A.M., Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, Utrecht, Netherlands","We retrospectively analyzed the value of polymerase chain reaction (PCR) for the detection of respiratory viral infections in 43 patients with hematological cancer whose bronchoalveolar lavage (BAL) samples had been stored. In addition, 17 nose-throat (NT) swabs and 29 blood samples had been obtained. PCR was performed to detect parainfluenza viruses 1-3, respiratory syncytial virus, rhinovirus, influenza viruses A and B, entero-viruses, and coronaviruses. Viral cultures or antigen testing of BAL samples revealed 9 respiratory viruses in 8 patients. By use of PCR, 8 more respiratory viruses were detected in another 7 patients, increasing the rate of identification from 19% to 35% (P<.0005). Available NT swabs yielded the same results with PCR as did BAL samples. We conclude that PCR is more sensitive than viral culture or antigen or serologic testing for detection of respiratory viruses in patients with hematological malignancies, and that it offers the possibility for early, more rapid diagnosis. © 2002 Infectious Diseases Society of America.",,"adult; aged; article; blood sampling; clinical article; Coronavirus; diagnostic accuracy; Enterovirus; female; hematologic disease; human; Influenza virus A; Influenza virus B; leukemia; lung lavage; lymphoma; male; nose smear; Parainfluenza virus 1; Parainfluenza virus 2; Parainfluenza virus 3; pneumonia; polymerase chain reaction; priority journal; Rhinovirus; sensitivity and specificity; serology; throat culture; virus culture; virus detection; Adolescent; Adult; Aged; Antigens, Viral; Female; Hematologic Neoplasms; Humans; Male; Middle Aged; Pneumonia, Viral; Polymerase Chain Reaction; Retrospective Studies; RNA Virus Infections; RNA Viruses; RNA, Viral; Sensitivity and Specificity; Virus Cultivation","Englund, J.A., Sullivan, C.J., Jordan, M.C., Respiratory syncytial virus infection in immunocompromised adults (1988) Ann Intern Med, 109, pp. 203-208; Wendt, C.H., Hertz, M.I., Respiratory syncytial virus and parainfluenza virus infections in the immunocompromised host (1995) Semin Respir Infect, 10, pp. 224-231; Whimbey, E., Champlin, R.E., Couch, R.B., Community respiratory virus infections among hospitalized adult bone marrow transplant recipients (1996) Clin Infect Dis, 22, pp. 778-782; Whimbey, E., Englund, J.A., Couch, R.B., Community respiratory virus infections in immunocompromised patients with cancer (1997) Am J Med, 102 (3 A), pp. 10-18; Ljungman, P., Respiratory virus infections in bone marrow transplant recipients: The European perspective (1997) Am J Med, 102 (3 A), pp. 44-47; Doller, G., Schuy, W., Tjhen, K.Y., Direct detection of influenza virus antigen in nasopharyngeal specimens by direct enzyme immunoassay in comparison with quantitating virus shedding (1992) J Clin Microbiol, 30, pp. 866-869; Schmidt, M.L., Kudesia, G., Wake, S., Prospective comparative study of culture specimens and methods in diagnosing influenza in adults (1998) BMJ, 316, p. 275; Osiowy, C., Direct detection of respiratory syncytial virus, parainfluenza virus, and adenovirus in clinical respiratory specimens by a multiplex reverse transcription-PCR assay (1998) J Clin Microbiol, 36, pp. 3149-3154; Van Elden, L.J., Nijhuis, M., Schipper, P., Simultaneous detection of influenza viruses A and B using real-time quantitative PCR (2001) J Clin Microbiol, 39, pp. 196-200; Verdonck, L.F., Dekker, A.W., Rozenberg-Arska, M., A risk-adapted approach with a short course of ganciclovir to prevent cytomegalovirus (CMV) pneumonia in CMV-seropositive recipients of allogeneic bone marrow transplants (1997) Clin Infect Dis, 24, pp. 901-907; Andeweg, A.C., Besteboer, T.M., Huybreghs, M., Improved detection of rhinoviruses in clinical samples by using a newly developed nested reverse transcription-PCR assay (1999) J Clin Microbiol, 37, pp. 524-530; Echevarria, J.E., Erdman, D.D., Swierkosz, E.M., Simultaneous detection and identification of human parainfluenza viruses 1, 2, and 3 from clinical samples by multiplex PCR (1998) J Clin Microbiol, 36, pp. 1388-1391; Myint, S.H., Johnston, S.L., Sanderson, G., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Boom, R., Sol, C.J., Salimans, M.M., Rapid and simple method for purification of nucleic acids (1990) J Clin Microbiol, 28, pp. 495-503; Nijhuis, M., Boucher, C.A., Schuurman, R., Sensitive procedure for the amplification of HIV-1 RNA using a combined reverse-transcription and amplification reaction (1995) Biotechniques, 19, pp. 178-180; Papadopulos, N.G., Hunter, J., Sanderson, G., Rhinovirus identification by Bgl1 digestion of picornavirus RT-PCR amplicons (1999) J Virol Methods, 80, pp. 179-185; Ljungman, P., Gleaves, C.A., Meyers, J.D., Respiratory virus infection in immunocompromised patients (1989) Bone Marrow Transplant, 4, pp. 35-40; Bowden, R.A., Respiratory virus infections after marrow transplant: The Fred Hutchinson Cancer Research Center Experience (1997) Am J Med, 102 (3 A), pp. 27-30; Whimbey, E., Couch, R.B., Englund, J.A., Respiratory syncytial virus pneumonia in hospitalized adult patients with leukemia (1995) Clin Infect Dis, 21, pp. 376-379; Sparrelid, E., Ljungman, P., Ekelöf-Andström, E., Ribavirin therapy in bone marrow transplant recipients with viral respiratory tract infections (1997) Bone Marrow Transplant, 19, pp. 905-908; Ghosh, S., Champlin, R.E., Englund, J., Respiratory syncytial virus upper respiratory tract illnesses in adult blood and marrow transplant recipients: Combination therapy with aerosolized ribavirin and intravenous immunoglobulin (2000) Bone Marrow Transplant, 25, pp. 751-755; Wendt, C.H., Weisdorf, D.J., Jordan, M.C., Parainfluenza virus respiratory infection after bone marrow transplantation (1992) N Engl J Med, 326, pp. 921-926; Lewis, V.A., Champlin, R., Englund, J., Respiratory disease due to parainfluenza virus in adult bone marrow transplant recipients (1996) Clin Infect Dis, 23, pp. 1033-1037; Whimbey, E., Elting, L.S., Couch, R.B., Influenza A virus infections among hospitalized adult bone marrow transplant recipients (1994) Bone Marrow Transplant, 13, pp. 437-440; Ljungman, P., Andersson, J., Aschan, J., Influenza A in immunocompromised patients (1993) Clin Infect Dis, 17, pp. 244-247; Ghosh, S., Champlin, R., Couch, R., Rhinovirus infections in myelosuppressed adult blood and marrow transplant recipients (1999) Clin Infect Dis, 29, pp. 528-532; Folz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; González, Y., Martino, R., Badell, I., Pulmonary enterovirus infections in stem cell transplant recipients (1999) Bone Marrow Transplant, 23, pp. 511-513; Rabella, N., Rodriguez, P., Labeaga, R., Conventional respiratory viruses recovered from immunocompromised patients: Clinical considerations (1999) Clin Infect Dis, 28, pp. 1043-1048; Gonzalez, Y., Martino, R., Rabella, N., Labeaga, R., Badell, I., Sierra, J., Community respiratory virus infections in patients with hematologic malignancies (1999) Haematologica, 84, pp. 820-823; Echavarria, M., Kolavic, S.A., Cersovsky, S., Detection of adenoviruses (AdV) in culture-negative environmental samples by PCR during an AdV-associated respiratory disease outbreak (2000) J Clin Microbiol, 38, pp. 2982-2984; Gubavera, L.V., Matrosovich, M.N., Brenner, M.K., Evidence for zanavamir resistance in an immunocompromised child infected with influenza B virus (1998) J Infect Dis, 178, pp. 1257-1262; Randomised trial of efficacy and safety of inhaled zanamivir in treatment of influenza A and B virus infections (1998) Lancet, 352, pp. 1877-1881; Nicholson, K.G., Aoki, F.Y., Osterhaus, A.D.M.E., Efficacy and safety of oseltamivir in treatment of acute influenza: A randomised controlled trial (2000) Lancet, 355, pp. 1845-1850. , Neuraminidase Inhibitor Flu Treatment Investigator Group; Schiff, G.M., Sherwood, J.R., Clinical activity of pleconaril in an experimentally induced coxsackievirus A21 respiratory infection (2000) J Infect Dis, 181, pp. 20-26","van Loon, A.M.; Eijkman-Winkler Institute of Medical Microbiology, Infectious Diseases and Inflammation, Department of Virology, University Medical Center Utrecht, PO Box 85500, 3508 GA Utrecht, Netherlands; email: a.m.vanloon@lab.azu.nl",,,10584838,,,"11740705","English","Clin. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0037079850
"Nokso-Koivisto J., Kinnari T.J., Lindahl P., Hovi T., Pitkranta A.","6602762108;6507232772;23103445100;36152793900;23103866200;","Human picornavirus and coronavirus RNA in nasopharynx of children without concurrent respiratory symptoms",2002,"Journal of Medical Virology","66","3",,"417","420",,98,"10.1002/jmv.2161","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036157283&doi=10.1002%2fjmv.2161&partnerID=40&md5=66f40823fede7fdff77df0deecdf7616","Enterovirus Laboratory, Department of Microbiology, National Public Health Institute (KTL), Helsinki, Finland; Department of Otorhinolaryngology, Helsinki University, Central Hospital, Helsinki, Finland; Department of Ophthalmology, Helsinki University, Central Hospital, Helsinki, Finland; Department of Otorhinolaryngology, University of Helsinki, PL 220, 00029 HYKS, Finland","Nokso-Koivisto, J., Enterovirus Laboratory, Department of Microbiology, National Public Health Institute (KTL), Helsinki, Finland, Department of Otorhinolaryngology, University of Helsinki, PL 220, 00029 HYKS, Finland; Kinnari, T.J., Department of Otorhinolaryngology, Helsinki University, Central Hospital, Helsinki, Finland; Lindahl, P., Enterovirus Laboratory, Department of Microbiology, National Public Health Institute (KTL), Helsinki, Finland; Hovi, T., Enterovirus Laboratory, Department of Microbiology, National Public Health Institute (KTL), Helsinki, Finland; Pitkranta, A., Department of Ophthalmology, Helsinki University, Central Hospital, Helsinki, Finland","The prevalence of human rhino-, entero-, and coronaviruses was investigated by RT-PCR in nasopharyngeal aspirates from 107 children without concurrent respiratory symptoms. The children were admitted to the hospital for elective surgery. The parents filled a questionnaire about the occurrence of respiratory symptoms four weeks before and two weeks after the surgery. The rate of viral detection was 45% in children with related past or recent respiratory infection whereas 20% of the samples taken from children without any related past or recent respiratory infections were positive for picornavirus RNA, P=0.008. Thirty-one (29%) of the nasopharyngeal aspirates were positive for viral RNA, 18% for rhinovirus, and 11% for enterovirus RNA. Coronavirus RNA was not found in any of the children. Fifty-five percent of the children with virus-positive samples had an infection-related diagnosis. In addition, 81% of the children with virus-positive samples had had previously respiratory symptoms or there were concurrent respiratory symptoms in other family members. Only four of the 31 virus-positive samples were from children without infection-related diagnosis or recent past (or immediate future) respiratory symptoms. © 2002 Wiley-Liss, Inc.","Enterovirus; PCR; Respiratory infection; Rhinovirus","virus RNA; adolescent; article; child; childhood disease; clinical feature; controlled study; Coronavirus; female; human; infant; major clinical study; male; nonhuman; nose secretion; Picornavirus; questionnaire; respiratory tract infection; reverse transcription polymerase chain reaction; superinfection; virus detection; virus infection; Adolescent; Child; Child, Preschool; Coronavirus; Coronavirus Infections; Enterovirus; Female; Finland; Humans; Infant; Male; Nasopharynx; Picornaviridae Infections; Respiratory Tract Infections; Rhinovirus; RNA, Viral; Coronavirus; Enterovirus; Picornaviridae; Rhinovirus","Bernstein, J.M., Waldeyer's ring and otitis media: The nasopharyngeal tonsil and otitis media (1999) Int J Pediatr Otorhinolaryngol, 49 (SUPPL. 1), pp. S127-S132; Blomqvist, S., Skyttä, A., Roivainen, M., Hovi, T., Rapid detection of human rhinovirus in nasopharyngeal aspirates by a microwell reverse transcription-PCR-hybridization assay (1999) J Clin Microbiol, 37, pp. 2813-2816; Faden, H., Monthly prevalence of group A, B and C Streptococcus haemophilus influenzae types E and F and Pseudomonas aeruginosa nasopharyngeal colonization in the first two years of life (1998) Pediatr Infect Dis J, 17, pp. 255-256; Faden, H., Duffy, L., Wasielewski, R., Wolf, J., Krystofik, D., Tung, Y., Relationship between nasopharyngeal colonization and the development of otitis media in children (1997) J Infect Dis, 175, pp. 1440-1445; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypia, T., Hurskainen, P., Pallansch, M., Detection of enteroviruses and rhinoviruses in clinical specimens by PCR and liquid-phase hybridization (1995) J Clin Microbiol, 33, pp. 648-653; Heinonen, P., Iitia, A., Torresani, T., Lovgren, T., Simple triple-label detection of seven cystic fibrosis mutations by time-resolved fluorometry (1997) Clin Chem, 43, pp. 1142-1150; Hendley, J., Gwaltney, J.J., Mechanisms of transmission of rhinovirus infections (1988) Epidemiol Rev, 10, pp. 243-258; Horn, M., Brain, E., Gregg, I., Inglis, J., Yealland, S., Taylor, P., Respiratory viral infection and wheezy bronchitis in childhood (1979) Thorax, 34, pp. 23-28; Hudgel, D.W., Selner, J.C., McIntosh, K., Viral and bacterial infections in adults with chronic asthma (1979) Am Rev Respir Dis, 120, pp. 393-397; Ieven, M., Goossens, H., Relevance of nucleic acid amplification techniques for diagnosis of respiratory tract infections in the clinical laboratory (1997) Clin Microbiol Rev, 10, pp. 242-256; Jennings, L., Barns, G., Dawson, K., The association of viruses with acute asthma (1987) NZ Med J, 12, pp. 488-490; Johnston, S., Sanderson, G., Pattemore, P., Smith, S., Bardin, P., Bruce, C., Lambden, P., Holgate, S., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Monto, A., Studies of the community and family: Acute respiratory illness and infection (1994) Epidemiol Rev, 16, pp. 351-373; Nokso-Koivisto, J., Pitkäranta, A., Blomqvist, S., Kilpi, T., Hovi, T., Respiratory coronavirus infections in children younger than two years of age (2000) Pediatr Infect Dis J, 19, pp. 164-166; Pitkäranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-aquired sinusitis by reverse transcription-PCR (1997) J Clin Microbiol, 35, pp. 1791-1793; Vesa, S., Kleemola, M., Blomqvist, S., Takala, A., Kilpi, T., Hovi, T., Epidemiology of documented viral respiratory infections and acute otitis media in a cohort of children followed from two to twenty-four months of age (2001) Pediatr Infect Dis J, 20, pp. 574-580","Nokso-Koivisto, J.; Department of Otorhinolaryngology, University of Helsinki, PL 220, 00029 HYKS, Finland; email: johanna.nokso-koivisto@hus.fi",,,01466615,,JMVID,"11793396","English","J. Med. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036157283
"Cavanagh D., Mawditt K., Welchman D.D.B., Britton P., Gough R.E.","26642890500;6603252273;6701355953;57203302770;7102835761;","Coronaviruses from pheasants (Phasianus colchicus) are genetically closely related to coronaviruses of domestic fowl (infectious bronchitis virus) and turkeys",2002,"Avian Pathology","31","1",,"81","93",,110,"10.1080/03079450120106651","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035984704&doi=10.1080%2f03079450120106651&partnerID=40&md5=338ca27c8c4dc70d3b5cd1670bad3126","Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Veterinary Laboratories Agency, Itchen Abbas, Winchester, United Kingdom; Avian Virology, Veterinary Laboratories Agency, Weybridge, Addlestone, Surrey, United Kingdom","Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Mawditt, K., Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Welchman, D.D.B., Veterinary Laboratories Agency, Itchen Abbas, Winchester, United Kingdom; Britton, P., Institute for Animal Health, Compton Laboratory, Compton, Newbury, RG20 7NN, United Kingdom; Gough, R.E., Avian Virology, Veterinary Laboratories Agency, Weybridge, Addlestone, Surrey, United Kingdom","Reverse-transcriptase polymerase chain reactions (RT-PCRs) were used to examine RNA extracted from mouth/nasal swabs from pheasants exhibiting signs of respiratory disease. The oligonucleotides used were based on sequences of infectious bronchitis virus (IBV), the coronavirus of domestic fowl. A RT-PCR for the highly conserved region II of the 3′ untranslated region of the IBV genome detected a coronavirus in swabs from 18/21 estates. Sequence identity with the corresponding region of IBVs and coronaviruses from turkeys was > 95%. A RT-PCR for part of the S1 region of the spike protein gene was positive with 13/21 of the samples. Sequence analysis of the RT-PCR products derived from nine of the pheasant viruses revealed that some of the viruses differed from each other by approximately 24%, similar to the degree of difference exhibited by different serotypes of IBV. Further analysis of the genome of one of the viruses revealed that it contained genes 3 and 5 that are typical of IBV but absent in both the transmissible gastroenteritis virus and murine hepatitis virus groups of mammalian coronaviruses. The nucleotide sequences of genes 3 and 5 of the pheasant virus had a similar degree of identity (approximately 90%) with those of coronaviruses from turkeys and chickens, as is observed when different serotypes of IBV are compared. This work: (a) confirms that coronaviruses are present in pheasants (indeed, commonly present in pheasants with respiratory disease); (b) demonstrates that their genomes are IBV-like in their organization; and (c) shows that there is sequence heterogeneity within the group of pheasant coronaviruses, especially within the spike protein gene. Furthermore, the gene sequences of the pheasant viruses differed from those of IBV to similar extents as the sequence of one serotype of IBV differs from another. On the genetic evidence to date, there is a remarkably high degree of genetic similarity between the coronaviruses of chickens, turkeys and pheasants.",,"Animalia; Avian infectious bronchitis virus; Coronavirus; DNA viruses; Galliformes; Gallus gallus; Mammalia; Murinae; Murine hepatitis virus; Phasianidae; Phasianus colchicus; Transmissible gastroenteritis virus; virus RNA; animal; animal disease; article; Avian infectious bronchitis virus; bird; bird disease; Coronavirus; genetics; isolation and purification; molecular genetics; nucleotide sequence; phylogeny; reverse transcription polymerase chain reaction; sequence homology; species difference; turkey (bird); virology; virus gene; virus infection; wild animal; Animals; Animals, Wild; Base Sequence; Birds; Coronaviridae Infections; Coronavirus; Genes, Viral; Infectious bronchitis virus; Molecular Sequence Data; Phylogeny; Poultry Diseases; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Sequence Homology, Nucleic Acid; Species Specificity; Turkeys","Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathology, 25, pp. 817-836; Adzhar, A., Gough, R.E., Haydon, D., Shaw, K., Britton, P., Cavanagh, D., Molecular analysis of the 793/B serotype of infectious bronchitis virus in Great Britain (1997) Avian Pathology, 26, pp. 625-640; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome ('spiking mortality') of turkeys (1997) Diseases of Poultry 10th edn, pp. 1025-1031. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald & Y.M. Saif (Eds.). 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Ames, IA: Iowa State University Press; Cavanagh, D., Davis, P.J., Cook, J.K.A., Li, D., Kant, A., Koch, G., Location of the amino-acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious-bronchitis virus (1992) Avian Pathology, 21, pp. 33-43; Cavanagh, D., Mawditt, K., Britton, P., Naylor, C.J., Longitudinal field studies of infectious bronchitis virus and avian pneumovirus in broilers using type-specific polymerase chain reactions (1999) Avian Pathology, 28, pp. 593-605; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Btitton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 355-368; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Analytical Biochemistry, 162, pp. 156-159; Cook, J.K.A., Huggins, M.B., Orbell, S.J., Mawditt, K., Cavanagh, D., Infectious bronchitis virus vaccine interferes with the replication of avian pneumovirus vaccine in domestic fowl (2001) Avian Pathology, 30, pp. 233-242; Cook, J.K.A., Chesher, J., Baxendale, W., Greenwood, N., Huggins, M.B., Orbell, S.J., Protection of chickens against renal damage caused by a nephropathogenic infectious bronchitis virus (2001) Avian Pathology, 30, pp. 423-426; Dalton, K., Casais, R., Shaw, K., Stirrups, K., Evans, S., Britton, P., Brown, T.D.K., Cavanagh, D., Identification of the cis-acting sequences required for coronavirus infectious bronchitis virus defective RNA replication and rescue (2001) Journal of Virology, 75, pp. 125-133; De Wit, J.J., Technical Review: Detection of infectious bronchitis virus (2000) Avian Pathology, 29, pp. 71-93; Dhinakar Raj, G., Jones, R.C., Local antibody production in the oviduct and gut of hens infected with a variant strain of infectious bronchitis virus (1996) Veterinary Immunology and Immunopathology, 53, pp. 147-161; Dhinaker Raj, G., Jones, R.C., Infectious bronchitis virus: Immunopathogenesis of infection in the chicken (1997) Avian Pathology, 26, pp. 677-706; Enjuanes, L., Cavanagh, D., Coronaviruses (2001) The Springer Index of Viruses electronic book, , C.A. 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Giessen, Justus-Liebig University; Jia, W., Karaca, K., Parish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Archives of Virology, 140, pp. 259-271; Kusters, J.G., Niesters, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Lambrechts, C., Pensaert, M., Ducatelle, R., Challenge experiments to evaluate cross-protection induced at the trachea and kidney level by vaccine strains and Belgian nephropathogenic isolates of avian infectious bronchitis virus (1993) Avian Pathology, 22, pp. 577-590; Lee, C.W., Jackwood, M.W., Evidence of genetic diversity generated by recombination among avian coronavirus IBV (2000) Archives of Virology, 145, pp. 2135-2148; Lee, C.W., Hilt, D.A., Jackwood, M.W., Identification and analysis of the Georgia 98 serotype, a new serotype of infectious bronchitis virus (2001) Avian Diseases, 45, pp. 164-172; Li, H., Yang, H., Sequence analysis of nephropathogenic infectious bronchitis virus strains of the Massachusetts genotype in Beijing (2001) Avian Pathology, 30, pp. 535-541; Li, J., Cook, J.K.A., Brown, T.D.K., Shaw, K., Cavanagh, D., Detection of turkey rhinotracheitis virus in turkeys using the polymerase chain reaction (1993) Avian Pathology, 22, pp. 771-783; Lister, S.A., Beer, J.V., Gough, R.E., Holmes, R.G., Jones, J.M.W., Orton, R.G., Outbreaks of nephritis in pheasants (Phasianus colchicus) with a possible coronavirus aetiology (1985) Veterinary Record, 117, pp. 612-613; Liu, D.X., Cavanagh, D., Green, P., Inglis, S.C., A polycistronic mRNA specified by the coronavirus infectious bronchitis virus (1991) Virology, 184, pp. 531-544; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Diseases, 44, pp. 498-506; Meulemans, G., Boschmans, M., Decaesstecker, M., Van den Berg, T.P., Denis, P., Cavanagh, D., Epidemiology of infectious bronchitis virus in Belgian broilers: A retrospective study 1986-1995 (2001) Avian Pathology, 30, pp. 411-421; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry 10th edn, pp. 686-692. , B.W. 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"Pewe L., Perlman S.","6603143496;7102708317;","Cutting edge: CD8 T cell-mediated demyelination is IFN-γdependent in mice infected with a neurotropic coronavirus",2002,"Journal of Immunology","168","4",,"1547","1551",,56,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037083308&partnerID=40&md5=fd0585119c1c48015423324e851b6395","Medical Laboratories 2042, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Pewe, L., Medical Laboratories 2042, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Medical Laboratories 2042, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States","Mice infected with the murine coronavirus, mouse hepatitis virus, strain JHM (MHV) develop an immune-mediated demyelinating encephalomyelitis. We showed previously that adoptive transfer of MHV-immune splenocytes depleted of either CD4 or CD8 T cells to infected RAG1-/- recipients (mice deficient in recombination activation gene 1) resulted in demyelination. Herein we show that transfer of CD8 T cell-enriched splenocytes from MHV-immune IFN-γ-/- donors resulted in a substantial decrease in demyelination (4.8% of the white matter of the spinal cord compared with 26.3% in those receiving cells from C57BL/6 donors). Similar numbers of lymphocytes were present in the CNS of recipients of either C57BL/6 or IFN-γ-/- CD8 T cells, suggesting that IFN-γ was not crucial for lymphocyte entry into the CNS. Rather, IFN-γ was critical for optimal activation or migration of macrophages or microglia into the white matter in the context of CD8 T cell-mediated demyelination.",,"CD8 antigen; gamma interferon; animal cell; animal experiment; animal model; animal tissue; article; autoimmunity; controlled study; Coronavirus; cytokine production; demyelination; lymphocyte migration; macrophage activation; microglia; mouse; mouse strain; nonhuman; priority journal; spleen cell; T lymphocyte; virus infection; white matter; Adoptive Transfer; Animals; CD8-Positive T-Lymphocytes; Cell Movement; Coronavirus Infections; Encephalomyelitis, Autoimmune, Experimental; Interferon Type II; Macrophages; Mice; Mice, Inbred C57BL; Mice, Knockout; Microglia; Murine hepatitis virus; Myelin Sheath; Spinal Cord; Spleen","Huseby, E.S., Liggitt, D., Brabb, T., Schnabel, B., Ohlen, C., Goverman, J., A pathogenic role for myelin-specific CD8(+) T cells in a model for multiple sclerosis (2001) J. Exp. Med., 194, p. 669; Sun, D., Whitaker, J.N., Huang, Z., Liu, D., Coleclough, C., Wekerle, H., Raine, C.S., Myelin antigen-specific CD8+ T cells are encephalitogenic and produce severe disease in C57BL/6 mice (2001) J. Immunol., 166, p. 7579; Steinman, L., Assessment of animal models for MS and demyelinating disease in the design of rational therapy (1999) Neuron, 24, p. 511; Murray, P.D., Pavelko, K.D., Leibowitz, J., Lin, X., Rodriguez, M., CD4+ and CD8+ T cells make discrete contributions to demyelination and neurologic disease in a viral model of multiple sclerosis (1998) J. Virol., 72, p. 7320; Wu, G.F., Dandekar, A.A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. 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Virol., 73, p. 8771; Parra, B., Hinton, D., Marten, N., Bergmann, C., Lin, M.T., Yang, C.S., Stohlman, S.A., IFN-γ is required for viral clearance from central nervous system oligodendroglia (1999) J. Immunol., 162, p. 1641; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M.C., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread and pathogenicity (1997) Virology, 233, p. 327; Owens, T., Wekerle, H., Antel, J., Genetic models for CNS inflammation (2001) Nat. Med., 7, p. 161; Pewe, L., Heard, S.B., Bergmann, C.C., Dailey, M.O., Perlman, S., Selection of CTL escape mutants in mice infected with a neurotropic coronavirus: Quantitative estimate of TCR diversity in the infected CNS (1999) J. Immunol., 163, p. 6106; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted CTL response (1996) J. Gen. 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Leukocyte Biol., 58, p. 373; Willenborg, D.O., Fordham, S., Bernard, C.C., Cowden, W.B., Ramshaw, I.A., IFN-γ plays a critical down-regulatory role in the induction and effector phase of myelin oligodendrocyte glycoprotein-induced autoimmune encephalomyelitis (1996) J. Immunol., 157, p. 3223; Tran, E.H., Prince, E.N., Owens, T., IFN-γ shapes immune invasion of the central nervous system via regulation of chemokines (2000) J. Immunol., 164, p. 2759; Chu, C.Q., Wittmer, S., Dalton, D.K., Failure to suppress the expansion of the activated CD4 T cell population in interferon γ-deficient mice leads to exacerbation of experimental autoimmune encephalomyelitis (2000) J. Exp. Med., 192, p. 123; Lane, T.E., Asensio, V., Yu, N., Paoletti, A.D., Campbell, I., Buchmeier, M.J., Dynamic regulation of α- and β-chemokine expression in the central nervous system during mouse hepatitis virus-induced demyelinating disease (1998) J. Immunol., 160, p. 970; Panitch, H.S., Hirsch, R.L., Haley, A.S., Johnson, K.P., Exacerbations of multiple sclerosis in patients treated with γ interferon (1987) Lancet, 1, p. 893","Perlman, S.; Medical Laboratories 2042, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,00221767,,JOIMA,"11823480","English","J. Immunol.",Article,"Final",,Scopus,2-s2.0-0037083308
"Loa C.C., Lin T.L., Wu C.C., Bryan T., Hooper T., Schrader D.","6602648721;7404860140;7501664098;7005517787;7005121335;7007179253;","The effect of immunosuppression on protective immunity of turkey poults against infection with turkey coronavirus",2002,"Comparative Immunology, Microbiology and Infectious Diseases","25","2",,"127","138",,6,"10.1016/S0147-9571(01)00033-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036163906&doi=10.1016%2fS0147-9571%2801%2900033-9&partnerID=40&md5=f76be98c776cf56946baa199988a4336","Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States","Loa, C.C., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Lin, T.L., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Wu, C.C., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Bryan, T., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Hooper, T., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Schrader, D., Department of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States","The objective of the present study was to evaluate the protective effect of humoral and cellular immunities on turkeys infected with turkey coronavirus (TCV). Two trials were conducted with two separate hatches of turkey poults. Turkeys were experimentally immunosuppressed with cyclosporin A (CsA) or cyclophosphamide (CY) and infected with TCV. Prior to infection, treatment with CsA selectively suppressed T cell activity as revealed by 2-3 fold decreased (p < 0.1) lymphocyte proliferation responses to a T cell mitogen, concanavalin A (Con A). Treatment with CY mainly induced B cell deficiency as indicated by significant reductions (p < 0.05) in antibody responses to sheep erythrocytes 7 days after injection. Body weight gain of turkeys treated with CY was significantly lower (p < 0.05) than that of untreated turkeys at 9 days post-infection (PI). Turkeys treated with CY had 1-2 fold higher immunofluorescent antibody assay (IFA) scores for TCV antigens (p < 0.05) in the intestine than untreated turkeys at 9 or 14 days PI. These results suggested that humoral immunity against TCV infection may be important in turkeys. © 2002 Elsevier Science Ltd. All rights reserved.","Cyclophosphamide; Cyclosporin A; Enteritis; Immunity; Immunosuppression; Turkey coronavirus","concanavalin A; cyclophosphamide; cyclosporin A; virus antigen; animal cell; antibody response; article; B lymphocyte; bird disease; cell activity; cellular immunity; controlled study; Coronavirus; drug effect; female; host resistance; humoral immune deficiency; humoral immunity; immune deficiency; immunofluorescence test; infection resistance; intestine infection; lymphocyte proliferation; male; newborn; nonhuman; scoring system; sheep erythrocyte; T lymphocyte; turkey (bird); weight gain; Animals; Antibodies, Viral; Antigens, Viral; Concanavalin A; Coronavirus, Turkey; Cyclophosphamide; Cyclosporine; Enteritis, Transmissible, of Turkeys; Female; Fluorescent Antibody Technique, Indirect; Immunity, Cellular; Immunosuppressive Agents; Intestines; Lymphocyte Activation; Lymphocytes; Male; Random Allocation; Turkeys; Coronavirus; Ovis aries; Turkey coronavirus","Goodwin, M.A., Brown, J., Player, E.C., Steffens, W.L., Hermes, D., Dekich, M.A., Fringed membranous particles and viruses in faeces from healthy turkey poults and from poults with putative poult enteritis complex/spiking mortality (1995) Avian. 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Assoc., 130, pp. 360-365; El-Kanawati, Z.R., Tsunemitsu, H., Smith, D.R., Saif, L.J., Infection and cross-protection studies of winter dysentery and calf diarrhea bovine coronavirus strains in colostrum-deprived and gnotobiotic calves (1996) Am. J. Vet. Res., 57 (1), pp. 48-53; Brim, T.A., VanCott, J.L., Lunney, J.K., Saif, L.J., Cellular immune responses of pigs after primary inoculation with porcine respiratory coronavirus or transmissible gastroenteritis virus and challenge with transmissible gastroenteritis virus (1995) Vet. Immunol. Immunopathol., 48, pp. 35-54; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Disease of Poultry, pp. 511-526. , Calnek BW, Barnes HJ, Beard CW, McDougald LR, Saif YM, editors. 10th ed. Ames, Iowa: Iowa State University Press; Kapil, S., Trent, A.M., Goyal, S.M., Antibody responses in spiral colon, ileum, and jejunum of bovine corona-virus-infected neonatal calves (1994) Comp. Immun. Microbiol. Infect. 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Res., 39 (9), pp. 1463-1465; Nagaraja, K.V., Pomeroy, B.S., Immunofluorescent studies on localization of secretory immunoglobulins in the intestines of turkeys recovered from turkey coronaviral enteritis (1980) Am. J. Vet. Res., 41, pp. 1283-1284; Nagaraja, K.V., Pomeroy, B.S., Cell-mediated immunity against turkey coronaviral enteritis (bluecomb) (1980) Am. J. Vet. Res., 41 (6), pp. 915-917; Nowak, J.S., Kai, O., Peck, R., Franklin, R.M., The effect of cyclosporin A on the chicken immune system (1982) Eur. J. Immunol., 12, pp. 867-876; Elmubarak, A.K., Sharma, J.M., Lee, L.F., Sanger, V.L., Suppression of immunologic function and degeneration of lymphoid organs in cyclophosphamide-treated turkeys (1981) Am. J. Vet. Res., 42 (12), pp. 2122-2128; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1985) Avian. Dis., 30, pp. 319-326; Schreiber, S.L., Crabtree, G.R., The mechanism of action of cyclosporin A and FK506 (1992) Immunol. Today, 13 (4), pp. 136-142; Suresh, M., Sharma, J.M., Hemorrhagic enteritis virus induced changes in the lymphocyte subpopulations in turkeys and the effect of experimental immunodeficiency on viral pathogenesis (1995) Vet. Immunol. Immunopathol., 45, pp. 139-150; Miggiano, V., North, M., Buder, A., Pink, J.R.L., Genetic control of the response of chicken leukocytes to a T-cell mitogen (1976) Nature, 263, pp. 61-63; Bayyari, G.R., Huff, W.E., Rath, N.C., Balog, J.W., Newberry, L.A., Villines, J.D., Skeeles, J.K., Nestor, K.E., Effect of the genetic selection of turkeys for increased body weight and egg production on immune and physiological responses (1997) Poultry Sci., 76, pp. 289-296; Li, Z., Nestor, K.E., Saif, Y.M., Bacon, W.L., Anderson, J.W., Effect of selection for increased body weight on mitogenic responses in turkeys (1999) Poultry Sci., 78, pp. 1532-1535; Dhinakar Raj, G., Jones, R.C., Cross-reactive cellular immune responses in chickens vaccinated with live infectious bronchitis virus vaccine (1997) Avian. Pathol., 26, pp. 641-649; Seo, S.H., Collisson, E.W., Specific cytotoxic T lymphocytes are involved in in vivo clearance of infectious bronchitis virus (1997) J. Virol., 71 (7), pp. 5173-5177; Seo, S.H., Pei, J., Briles, W.E., Dzielawa, J., Collisson, E.W., Adoptive transfer of infectious bronchitis virus primed αβ T cells bearing CD8 antigen protects chicks from acute infection (2000) Virology, 269, pp. 183-189; Seo, S.H., Wang, L., Smith, R., Collisson, E.W., The carboxyl-terminal 120-residue polypeptide of infectious bronchitis virus nucleocapsid induces cytotoxic T lymphocytes and protects chickens from acute infection (1997) J. Virol., 71 (10), pp. 7889-7894; Collisson, E.W., Pei, J., Dzielawa, J., Seo, S.H., Cytotoxic T lymphocytes are critical in the control of infectious bronchitis virus in poultry (2000) Dev. Comp. Immunol., 24, pp. 187-200; Tomley, F.M., Mockett, A.P.A., Boursnell, M.G., Binns, M.M., Cook, J.A., Brown, T.D.K., Smith, G.L., Expression of the infectious bronchitis virus spike protein by recombinant vaccinia virus and induction of neutralizing antibodies in vaccinated mice (1987) J. Gen. Virol., 68, pp. 2291-2298; Song, C.S., Lee, Y.J., Lee, C.W., Sung, H.W., Kim, J.H., Mo, I.P., Izumiya, Y., Mikami, T., Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed by a recombinant baculovirus (1998) J. Gen. Virol., 79, pp. 719-723; Gonder, E., Patel, B.L., Pomeroy, B.S., Scanning electron, light, and immunofluorescent microscopy of coronaviral enteritis of turkeys (bluecomb) (1976) Am. J. Vet. Res., 37, pp. 1435-1439; Deshmukh, D.R., Sautter, J.H., Patel, B.L., Pomeroy, B.S., Histopathology of fasting and bluecomb disease in turkey poults and embryos experimentally infected with bluecomb disease coronavirus (1974) Avian. Dis., 20, pp. 631-640","Lin, T.L.; Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,,01479571,,CIMID,"11848129","English","Comp. Immunol. Microbiol. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0036163906
"Kyuwa S., Shibata S., Tagawa Y.-I., Iwakura Y., Machii K., Urano T.","7006444820;7402120346;35394959400;7102119714;7005995877;55183079300;","Acute hepatic failure in IFN-γ-deficient BALB/c mice after murine coronavirus infection",2002,"Virus Research","83","1-2",,"169","177",,13,"10.1016/S0168-1702(01)00432-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037176960&doi=10.1016%2fS0168-1702%2801%2900432-4&partnerID=40&md5=f0ce51419d6e306870158340935db681","Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan; Department of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan; Department of Veterinary Public Health, Institute of Public Health, Tokyo 108-0071, Japan; Division of Microbiology and Genetics, Center for Animal Resources and Development, Kumamoto University, Kumamoto 860-0811, Japan; Department of Biomedical Science, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan","Kyuwa, S., Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan, Department of Biomedical Science, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan; Shibata, S., Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan, Department of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan; Tagawa, Y.-I., Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan; Iwakura, Y., Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan; Machii, K., Department of Veterinary Public Health, Institute of Public Health, Tokyo 108-0071, Japan; Urano, T., Division of Microbiology and Genetics, Center for Animal Resources and Development, Kumamoto University, Kumamoto 860-0811, Japan","We previously showed that an intraperitoneal infection with mouse hepatitis virus (MHV) persists in interferon-γ (IFN-γ)-deficient C57BL/6 (B6-GKO) mice and results in subacute fatal peritonitis, which bears a resemblance to feline infectious peritonitis. To examine the role of other host factors in MHV infection in mice, IFN-γ-deficient mice with a BALB/c background (BALB-GKO) were infected intraperitoneally with MHV and compared with B6-GKO mice. In contrast to B6-GKO mice, BALB-GKO mice died within 1 week due to acute hepatic failure. The viral titer of the liver in BALB-GKO mice was significantly higher than that in B6-GKO mice. All hepatocytes in BALB-GKO mice were necrotic at 5 days post-infection, which was clearly distinct from large but limited lesion in the liver from infected B6-GKO mice. The serum alanine aminotransferase activity of infected BALB-GKO mice were higher than that of B6-GKO mice and was paralleled with the severity of the pathological changes and viral titers in infected mice. Administration of exogenous IFN-γ to BALB-GKO partially inhibited the acute death. These results indicate that BALB-GKO and B6-GKO mice clearly show different diseases following MHV infection, although wild type counterparts of both mice apparently showed the same clinical course after MHV infection. © 2002 Elsevier Science B.V. All rights reserved.","Acute hepatic failure; Genetic background; Interferon-γ-deficient mice; Mouse hepatitis virus","alanine aminotransferase; gamma interferon; animal experiment; animal tissue; article; cause of death; controlled study; disease course; drug effect; enzyme activity; enzyme blood level; experimental infection; hepatitis; liver cell; liver failure; liver necrosis; mouse; mouse strain; Murine hepatitis coronavirus; nonhuman; peritonitis; priority journal; strain difference; virus infection; virus titration; Alanine Transaminase; Animals; Coronavirus Infections; Hepatitis, Viral, Animal; Injections, Intraperitoneal; Interferon Type II; Liver Failure, Acute; Mice; Mice, Inbred BALB C; Mice, Knockout; Murine hepatitis virus; Coronavirus; Felidae; Murinae; Murine hepatitis virus","Boivin, G.P., Smith, F.N.L., Idiopathic granulomas in IFN-γ-/-, IL-10-/- Double knockout mice (1998) Lab. Anim. Sci., 48, p. 419; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Doetschman, T., Interpretation of phenotype in genetically engineered mice (1999) Lab. Anim. Sci., 49, pp. 137-143; France, M.P., Smith, A.L., Stevenson, R., Barthold, S.W., Granulomatous peritonitis and plueritis in interferon-γ gene knockout mice naturally infected with mouse hepatitis virus (1999) Aust. Vet. J., 77, pp. 600-604; Hu, C., Mayadas-Norton, T., Tanaka, K., Chan, J., Salgame, P., Mycibacterium tuberculosis infection in complement receptor 3-deficient mice (2000) J. Immunol., 165, pp. 2596-2602; Hwang, S.Y., Hertzog, P.J., Holland, K.A., Sumarsono, S.H., Tymms, M.J., Hamilton, J.A., Whitty, G., Kola, I., A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons alpha and beta and alters macrophage responses (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 11284-11288; Kamradt, A.E., Greiner, M., Ghiare, P., Kaufmann, S.H., Helicobacter pylori infection in wild-type and cytokine-deficient C57BL/6 and BALB/c mouse strains (2000) Microbes Infect., 2, pp. 593-597; Kyuwa, S., Yamaguchi, K., Hayami, M., Hilgers, J., Fujiwara, K., Spontaneous production of interleukin-2 and interleukin-3 by spleen cells from mice infected with mouse hepatitis virus type 4 (1988) J. Virol., 62, pp. 3506-3508; Kyuwa, S., Stohlman, S.A., Pathogenesis of a neurotropic murine coronavirus, strain JHM in the central nervous system of mice (1990) Semin. Virol., 1, pp. 273-280; Kyuwa, S., Machii, K., Okumura, A., Toyada, Y., Characterization of T cells expanded in vivo during primary mouse hepatitis virus infection in mice (1996) J. Vet. Med. Sci., 58, pp. 431-437; Kyuwa, S., Tagawa, Y., Shibata, S., Doi, K., Machii, K., Iwakura, Y., Murine coronavirus-induced subacute fatal peritonitis in C57BL/6 mice deficient in gamma-interferon (1998) J. Virol., 72, pp. 9286-9290; Levy, G.A., Leibowitz, J.L., Edgington, T.S., Induction of monocyte procoagulant activity by murine hepatitis virus type 3 parallels disease susceptibility in mice (1981) J. Exp. Med., 154, pp. 1150-1163; Liu, M.T., Chen, B.P., Oertel, P., Buchmeier, M.J., Armstrong, D., Hamilton, T.A., Lane, T.E., The T cell chemoattractant IFN-inducible protein 10 is essential in host defense against viral-induced neurologic disease (2000) J. Immunol., 165, pp. 2327-2330; Marten, N.W., Stohlman, S.A., Bergmann, C.C., Role of viral persistence in retaining CD8+ T cells within the central nervous system (2000) J. Virol., 74, pp. 7903-7910; Matsuyama, S., Henmi, S., Ichihara, N., Sone, S., Kikuchi, T., Ariga, T., Taguchi, F., Protective effects of murine recombinant interferon-beta administered by intravenous, intramuscular or subcutaneous route on mouse hepatitis virus infection (2000) Antivir. Res., 47, pp. 131-137; Müller, U., Steinhoff, U., Reis, L.F., Hemmi, S., Pavlovic, J., Zinkernagel, R.M., Aguet, M., Functional role of type I and type II interferons in antiviral defense (1994) Science, 264, pp. 1918-1921; Ohtsuka, N., Taguchi, F., Mouse susceptibility to mouse hepatitis virus infection is linked to viral receptor genotype (1997) J. Virol., 71, pp. 8860-8863; Potter, M.R., Noben-Trauth, N., Weis, J.H., Teuscher, C., Weis, J.J., Interleukin-4 (IL-4) and IL-13 signaling pathways do not regulate borrelia burgdorferi-induced arthritis in mice: IgG1 is not required for host control of tissue spirochetes (2000) Infect. Immun., 68, pp. 5603-5609; Stohlman, S.A., Frelinger, J.A., Resistance to fatal nervous system disease by mouse hepatitis virus, strain JHM. 1. Genetic analysis (1978) Immunogenetics, 6, pp. 277-281; Stohlman, S.A., Kyuwa, S., Cohen, M., Bergmann, C., Polo, J.M., Yeh, J., Anthony, R., Keck, J.G., Mouse hepatitis virus nucleocapsid protein-specific cytotoxic T lymphocytes are Ld restricted and specific for the carboxy terminus (1992) Virology, 189, pp. 217-224; Tagawa, Y., Sekikawa, K., Iwakura, Y., Suppression of Concanavalin A-induced hepatitis in IFN-g-/- mice, but not in TNF-a-/- mice (1997) J. Immunol., 159, pp. 1418-1428; Uetsuka, K., Nakayama, H., Goto, N., Protective effect of recombinant interferon (IFN)-alpha/beta on MHV-2cc-induced chronic hepatitis in athymic nude mice (1996) Exp. Anim., 45, pp. 293-297; Wu, G.F., Dandekar, A.A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286","Kyuwa, S.; Department of Biomedical Science, Grad. Sch. of Agric./Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan; email: akyuwa@mail.ecc.u-tokyo.ac.jp",,,01681702,,VIRED,"11864749","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0037176960
"Pratelli A., Elia G., Martella V., Palmieri A., Cirone F., Tinelli A., Corrente M., Buonavoglia C.","7004884960;7005135633;7003300496;57215621849;6602223775;6701370203;55021372100;7005623145;","Prevalence of canine coronavirus antibodies by an enzyme-linked immunosorbent assay in dogs in the south of Italy",2002,"Journal of Virological Methods","102","1-2",,"67","71",,43,"10.1016/S0166-0934(01)00450-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036189007&doi=10.1016%2fS0166-0934%2801%2900450-5&partnerID=40&md5=da4d4a1e0d1251f0efb2c054bc89fb3a","Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Istituto Di Igiene E Medicina Preventiva, Faculty of Medicine of Sassari, Sassari, Italy","Pratelli, A., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Elia, G., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Martella, V., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Palmieri, A., Istituto Di Igiene E Medicina Preventiva, Faculty of Medicine of Sassari, Sassari, Italy; Cirone, F., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Tinelli, A., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Corrente, M., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Buonavoglia, C., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy","An enzyme-linked immunosorbent assay (Elisa), using as antigen canine coronavirus-infected CrFK cell supernatant, was developed to detect antibodies against canine coronavirus (CCoV). Out of a total of 109 dog serum samples, 80 which were positive by routine virus neutralisation test were also Elisa positive. Seventeen samples which were negative by the virus neutralisation test, were positive by Elisa and by the confirmatory Western blotting test. The Elisa was substantially more sensitive than the virus neutralisation test in detecting antibodies to CCoV and may be used as an alternative technique to virus neutralisation. © 2002 Elsevier Science B.V. All rights reserved.","Antibodies; Coronavirus; Dog; Elisa","virus antibody; virus antigen; accuracy; animal cell; antibody detection; article; cell strain; controlled study; Coronavirus; dog disease; enzyme linked immunosorbent assay; intermethod comparison; Italy; nonhuman; priority journal; seroprevalence; validation process; virus detection; virus etiology; virus neutralization; Western blotting; Animals; Antibodies, Viral; Blotting, Western; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Enzyme-Linked Immunosorbent Assay; Italy; Neutralization Tests; Sensitivity and Specificity; Canine coronavirus; Canis familiaris; Coronavirus","Athanssious, R., Marsolais, G., Assaf, R., Dea, S., Descoteaux, J.P., Dulude, S., Montpetit, C., Detection of bovine coronavirus and type A rotavirus in neonatal calf diarrhea and winter dyssentery of cattle in Quebec: Evaluation of three diagnostic methods (1994) Can. Vet. J., 35, pp. 163-169; Bandai, C., Ishiguro, S., Masuya, N., Hohdatsu, T., Mochizuki, M., Canine coronavirus infections in Japan: Virological and epidemiological aspects (1999) J. Vet. Med. Sci., 61, pp. 731-736; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, D.L., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1974) Proc. Annu. Mtg. US Anim. Health Assoc., 78, pp. 359-366; Buonavoglia, C., Marsilio, F., Cavalli, A., Tiscar, P.G., L'infezione da coronavirus del cane: Indagine sulla presenza del virus in Italia, , Not. Farm. Vet. Nr. 2/9, ed. SCIVAC; Carmichael, L.E., Binn, L.N., New canine enteric viral infection (1981) Adv. Vet. Sci., 25, pp. 1-37; De Groot, R.J., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Siddell, S.G. (Ed.). Plenum Press, New York; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro-neutralisation test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Jpn. J. Vet. Sci., 49, pp. 563-565; Naylor, M.J., Harrison, G.A., Monckton, R.P., McOrist, S., Lehrbach, P.R., Deane, E.M., Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterisation of a new Australian isolate (2001) J. Clin. Microbiol., 39, pp. 1036-1041; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) J. Virol. Meth., 84, pp. 91-94; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Mol. Cell. Probes., 15, pp. 229-233; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested-PCR assay for the detection of canine coronavirus (1999) J. Virol. Meth., 80, pp. 11-15; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H.A., UytdeHaag, F.G.C.M., Osterhaus, A.D.M.E., The use of enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in the Netherlands (1991) Vet. Microbiol., 26, pp. 25-40; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M.J., Gebaues, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The Coronaviridae: An introduction (1995) Coronaviridae, pp. 1-9. , Siddell, S.G. (Ed.). Plenum Press, New York, NY; Siddell, S.G., Wege, H., Meulen, V., The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Vet. Microbiol., 42, pp. 255-259; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Tuchiya, K., Horimoto, T., Azetaka, M., Takahashi, E., Konishi, S., Enzyme-linked immunosorbent assay for the detection of canine coronavirus and its antibody in dogs (1991) Vet. Microbiol., 26, pp. 41-51; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Res., 61, pp. 145-152; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Pratelli, A.; Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,,01660934,,JVMED,"11879694","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0036189007
"Alonso S., Sola I., Teifke J.P., Reimann I., Izeta A., Balasch M., Plana-Durán J., Moormann R.J.M., Enjuanes L.","57210695335;7003336781;35495263600;7005392571;6602523425;6602693824;6604038063;7006536560;7006565392;","In vitro and in vivo expression of foreign genes by trasmissible gastroenteritis coronavirus-derived minigenomes",2002,"Journal of General Virology","83","3",,"567","579",,17,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036184604&partnerID=40&md5=1f7ca4aa52f35872fb2d0c92bd7c4acc","Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Alonso, S., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Teifke, J.P., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Reimann, I., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Balasch, M., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Plana-Durán, J., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Moormann, R.J.M., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","A helper-dependent expression system based on transmissible gastroenteritis coronavirus (TGEV) has been developed using a minigenome of 3.9 kb (M39). Expression of the reporter gene β-glucuronidase (GUS) (2-8 μg per 106 cells) and the porcine respiratory and reproductive syndrome virus (PRRSV) ORF5 (1-2 μg per 106 cells) has been shown using a TGEV-derived minigenome. GUS expression levels increased about eightfold with the m.o.i. and were maintained for more than eight passages in cell culture. Nevertheless, instability of the GUS and ORF5 subgenomic mRNAs was observed from passages five and four, respectively. About a quarter of the cells in culture expressing the helper virus also produced the reporter gene as determined by studying GUS mRNA production by in situ hybridization or immunodetection to visualize the protein synthesized. Expression of GUS was detected in the lungs, but not in the gut, of swine immunized with the virus vector. Around a quarter of lung cells showing replication of the helper virus were also positive for the reporter gene. Interestingly, strong humoral immune responses to both GUS and PRRSV ORF5 were induced in swine with this virus vector. The large cloning capacity and the tissue specificity of the TGEV-derived minigenomes suggest that these virus vectors are very promising for vaccine development.",,"beta glucuronidase; messenger RNA; vaccine; virus vector; Arterivirus; article; cell culture; controlled study; Coronavirus; gene expression; gene induction; helper virus; humoral immunity; immunization; immunodetection; in situ hybridization; in vitro study; in vivo study; intestine; lung; lung alveolus cell; molecular cloning; nonhuman; open reading frame; priority journal; protein expression; protein synthesis; reporter gene; swine; tissue specificity; vaccine production; virus genome; virus replication; Animals; Animals, Newborn; Cell Line; Gene Expression; Genes, Reporter; Genetic Vectors; Genome, Viral; Glucuronidase; Helper Viruses; In Situ Hybridization; Intestines; Lung; Open Reading Frames; Porcine respiratory and reproductive syndrome virus; RNA, Messenger; Serial Passage; Swine; Transgenes; Transmissible gastroenteritis virus; Viral Proteins; Viral Vaccines; Virus Replication; Arterivirus; Coronavirus; Porcine reproductive and respiratory syndrome virus; RNA viruses; Suidae; Sus scrofa; Transmissible gastroenteritis virus","Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic Sindbis virus RNA vectors for heterologous gene expression (1998) Proceeding of the National Academy of Sciences, USA, 95, pp. 12989-12994; Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proceeding of the National Academy of Sciences, USA, 97, pp. 5516-5521; Alonso, S., Izeta, A., Sola, I., Enjuanes, L., Transcription regulatory sequences and mRNA expression levels in transmissible gastroenteritis coronavirus (2002) Journal of Virology, 76, pp. 1293-1308; Ausubel, F.M., (1987) Current Protocols in Molecular Biology, , New York: John Wiley & Sons; Ballesteros, M.L., Sánchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis corona-virus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Boyer, J.C., Bebenek, K., Kunkel, T.A., Unequal human immunodeficiency virus type 1 reverse transcriptase error rates with RNA and DNA templates (1992) Proceeding of the National Academy of Sciences, USA, 89, pp. 6919-6923; Bronstein, I., Fortin, J.J., Voyta, J.C., Juo, R.-R., Edwards, B., Olenses, C.E.M., Lijam, N., Kricka, L.J., Chemiluminescent reporter gene assays: Sensitive detection of the GUS and SEAP gene products (1994) Bio Techniques, 17, pp. 172-177; Caul, E.O., Egglestone, S.I., Coronavirus in humans (1982) Virus Infections of the Gastrointestinal Tract, pp. 179-193. , Edited by D.A.J. 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New York: Marcel Dekker; Dubensky, T.W., Driver, D.A., Polo, J.M., Belli, B.A., Latham, E.M., Ibanez, C.E., Chada, S., Chang, S.M.W., Sindbis virus DNA-based expression vectors: Utility for in vitro and in vivo gene transfer (1996) Journal of Virology, 70, pp. 508-519; Enjuanes, L., Van der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , Edited by S. G. Siddell. New York: Plenum Press; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy. Classification and Nomenclature of Viruses, pp. 835-849. , Edited by M.H.V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E.B. Carsten, M. K. Estes, S. M. Lemon, D. J. McGeoch, J. Maniloff, M. A. Mayo, C. R. Pringle & R.B. Wickner. New York: Academic Press; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidovirales (2000) Virus Taxonomy. 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Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Ant genic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sánchez, C.M., Gebauer, F., Suñé, C., Méndez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) Journal of Virology, 73, pp. 7607-7618; Schlaman, H.R.M., Risseeuw, E., Franke-van Dijk, M.E.I., Hooykaas, P.J.J., Nucleotide sequence corrections of the uidA open reading frame encoding β-glucuronidase (1994) Gene, 138, pp. 259-260; Siddell, S.G., The Coronaviridae (1995) The Viruses, p. 418. , Edited by H. Fraenkel-Conrat & R.R. Wagner. New York: Plenum Press; Sooknanan, R., Howes, M., Read, L., Malek, L.T., Fidelity of nucleic acid amplification with avian myeloblastosis virus reverse transcriptase and T7 RNA polymerase (1994) BioTechniques, 17, pp. 1077-1085; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Casais, R., Cavanagh, D., Britton, P., Expression of reporter genes from the defective RNA CD-61 of the coronavirus infectious bronchitis virus (2000) Journal of General Virology, 81, pp. 1687-1698; Thiel, V., Siddell, S.G., Herold, J., Replication and transcription of HCV 229E replicons (1998) Advances in Experimental Medicine and Biology, 440, pp. 109-114; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) Journal of General Virology, 82, pp. 1273-1281; Thomas, M.J., Platas, A.A., Hawley, D.K., Transcriptional fidelity and proofreading by RNA polymerase II (1998) Cell, 93, pp. 627-637; Torres, J.M., Sánchez, C.M., Suñé, C., Smerdou, C., Prevec, L., Graham, F., Enjuanes, L., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213, pp. 503-516; Ward, C.D., Stokes, M.A.M., Flanagan, J.B., Direct measurement of the poliovirus RNA polymerase error frequency in vitro (1988) Journal of Virology, 62, pp. 558-562; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systemic assembly of large RNA and DNA genomes: The transmissible gastroenteritis virus model (2000) Journal of Virology, 74, pp. 10600-10611; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M.C., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338; Zurbriggen, A., Schmid, I., Graber, H.U., Vandevelde, M., Oligodendroglial pathology in canine distemper (1998) Acta Neuropathologica, 95, pp. 71-77","Enjuanes, L.; Department of Molecular/Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,00221317,,JGVIA,"11842252","English","J. Gen. Virol.",Article,"Final",,Scopus,2-s2.0-0036184604
"Hasoksuz M., Sreevatsan S., Cho K.-O., Hoet A.E., Saif L.J.","6603236044;6701704195;57193116476;6602855175;7102226747;","Molecular analysis of the S1 subunit of the spike glycoprotein of respiratory and enteric bovine coronavirus isolates",2002,"Virus Research","84","1-2",,"101","109",,45,"10.1016/S0168-1702(02)00004-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037139476&doi=10.1016%2fS0168-1702%2802%2900004-7&partnerID=40&md5=308da9154874b6460185da131e175f9f","Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States; Department of Microbiology, Veterinary Faculty, Istanbul University, Avcilar, 34850, Istanbul, Turkey; College of Veterinary Medicine, Chonnam National University, Kwangju, 500-757, South Korea; Department of Enfermedades Infecciosas, Facultad de Ciencias Veterinarias, Universidad del Zulia, Maracaibo, Venezuela","Hasoksuz, M., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States, Department of Microbiology, Veterinary Faculty, Istanbul University, Avcilar, 34850, Istanbul, Turkey; Sreevatsan, S., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States; Cho, K.-O., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States, College of Veterinary Medicine, Chonnam National University, Kwangju, 500-757, South Korea; Hoet, A.E., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States, Department of Enfermedades Infecciosas, Facultad de Ciencias Veterinarias, Universidad del Zulia, Maracaibo, Venezuela; Saif, L.J., Food Animal Health Research Program, Department of Veterinary Preventive Medicine, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691-4096, United States","It is unclear whether respiratory and enteric bovine coronavirus (BoCV) strains are distinctive in biological, antigenic and genetic characteristics. In the present study, we analyzed the nucleotide and amino acid sequence of the S1 subunit of the S glycoprotein, including the cleavage site, of both respiratory (n=5) and enteric (n=3) BoCV isolates including two paired isolates from the same feedlot animals and compared them with the prototype Mebus and two enteric and one respiratory BoCV strains from Quebec. A total of 75 polymorphic nucleotides were identified in the S1 subunit of the spike glycoprotein of BoCV isolates compared with the Mebus strain. These polymorphisms led to 42 amino acid changes at 38 distinct sites. The amino acid changes were distributed throughout the S1 subunit with clustering around residues 40-118, 146-179, and 458-531. Among these variations, only 19 amino acid substitutions altered the charge, hydrophobicity and surface probability of the protein. Based on phylogenetic analysis, our respiratory and enteric isolates clustered into two major groups with two subgroups. Although, there were only a few amino acid changes between the respiratory and enteric paired isolates, the other two respiratory isolates, one isolated from the same farm as a paired strain and the other from a different farm, showed more sequence diversity. Amino acid alterations in residues 113, 115, 118, 146, 148, 501, 510 and 531 of respiratory isolates conferred significant changes in the predicted secondary structure compared with the prototype winter dysentery (WD) and the calf diarrhea (CD) strains of BoCV. In conclusion, the data suggests that respiratory strains of BoCV may differ genetically from the classical calf enteric and adult WD strains. © 2002 Elsevier Science B.V. All rights reserved.","Allelic variation; Respiratory and enteric BoCV; S1 subunit; Sequencing","protein S; protein subunit; virus glycoprotein; amino acid sequence; amino acid substitution; article; controlled study; Coronavirus; genetic variability; hydrophobicity; molecular biology; nonhuman; nucleotide sequence; phylogeny; priority journal; protein degradation; protein polymorphism; sequence analysis; strain difference; virus isolation; Alleles; Amino Acid Substitution; Animals; Cattle; Cattle Diseases; Coronavirus, Bovine; Diarrhea; Membrane Glycoproteins; Phylogeny; Respiratory Tract Infections; Variation (Genetics); Viral Envelope Proteins; Animalia; Bovinae; Bovine coronavirus; Bovine enteric calicivirus; Coronavirus","Benfield, D.A., Saif, L.J., Cell culture propagation of coronavirus isolated from cows with winter dysentery (1990) J. Clin. Microbiol., 28, pp. 1454-1457; Cavanagh, D., The coronavirus surface glycoprotein (1995) The coronaviridiae, pp. 73-113. , S.G. Siddell (Eds.), Plenum Press. NY; Cho, K.O., Halbur, P.G., Bruna, J.D., Sorden, S.D., Yoon, K.J., Janke, B.H., Chang, K.O., Saif, L.J., Detection and isolation of coronavirus from feces of three herds of feedlot cattle during outbreaks of winter dysentery-like disease (2000) J. Am. Vet. Med. Assoc., 217, pp. 1191-1194; Cho, K.O., Hasoksuz, M., Nielsen, P.R., Chang, K.O., Lathrop, S., Saif, L.J., Cross-protection studies between respiratory and calf diarrhea and winter dysentery coronavirus strains in calves and RT-PCR and Nested PCR for their detection (2001) Arch. Virol., 146, pp. 2401-2419; Cho, K.O., Hoet, A., Lorech, S.C., Wittum, T.E., Saif, L.J., Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle (2001) Am. J. Vet. Res., 62, pp. 1436-1441; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Clark, M.A., Bovine coronavirus (1993) Br. Vet. J., 149, pp. 51-70; Cyr-Coast, K.S., Storz, J., Hussain, K.A., Schnorr, K.L., Structural proteins of bovine coronavirus strain L9: Effects of the host cell and trypsin treatment (1988) Arch. Virol., 103, pp. 35-45; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between Arteri-, Toro-, and Coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Gallagher, T.M., Buchmeier, M.J., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Gelinas, A.M., Boutin, M., Sasseville, A.M.J., Dea, S., Bovine coronaviruses associated with enteric and respiratory diseases in Canadian dairy cattle display different reactivities to anti-HE monoclonal antibodies and distinct amino acid changes in their HE, S and ns4.9 protein (2001) Virus Res., 76, pp. 43-57; Hasoksuz, M., Lathrop, S.L., Al-dubaib, M.A., Lewis, P., Saif, L.J., Antigenic variation among bovine enteric coronaviruses (BECV) and bovine respiratory coronaviruses (BRCV) detected using monoclonal antibodies (1999) Arch. Virol., 144, pp. 2441-2447; Hasoksuz, M., Lathrop, S.L., Gadfield, K.L., Saif, L.J., Isolation of bovine respiratory coronaviruses from feedlot cattle and comparison of their biological and antigenic properties with bovine enteric coronaviruses (1999) Am. J. Vet. Res., 60, pp. 1227-1233; Hasoksuz, M., Hoet, A.E., Loerch, S.C., Wittum, T.E., Nielsen, P.R., Saif, L.J., Detection of respiratory and enteric shedding of bovine coronaviruses in cattle in an Ohio feedlot (2001) J. Vet. Diagn. Invest., , Submitted; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lathrop, S.L., Wittum, T.E., Loerch, S.C., Saif, L.J., Antibody titers against Bovine coronavirus and shedding of the virus via the respiratory tract in feedlot cattle (2000) Am. J. Vet. Res., 61, pp. 1057-1061; Lin, X.Q., O'Reilly, K.L., Storz, J., Purdy, C.W., Loan, R.W., Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis (2000) Arch. Virol., 145, pp. 2335-2349; Rekik, M.R., Dea, S., Comparative sequence analysis of a polymorphic region of the spike glycoprotein S1 subunit of enteric bovine coronavirus isolates (1994) Arch. 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Plenum press, NY; Schultze, B., Gross, H.J., Brossmer, R., Herrler, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O- acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Silva, M.R., O'Reilly, K.L., Lin, X., Stine, L., Storz, J., Sensitivity comparison for detection of respiratory bovine coronaviruses in nasal samples from feedlot cattle by ELISA and isolation with the G clone of HRT-18 cells (1999) J. Vet. Diagn. Invest., 11, pp. 15-19; Storz, J., Purdy, W., Lin, X., Burrell, M., Truax, R.E., Briggs, R.E., Frank, G.H., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J. Am. Vet. Med. Assoc., 216, pp. 1539-1604; Tsunemitsu, H., Saif, L.J., Antigenic and biological comparisons of bovine coronaviruses derived from neonatal calf diarrhea and winter dysentery of adult cattle (1995) Arch. Virol., 140, pp. 1303-1311; Van Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., Carstens, E.B., Estes, M.K., Lemon, S.M., Maniloff, J., Wickner, R.B., (2000) Virus Taxonomy, p. 827. , Academic press, San Diago, CA; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: Detailed antigenic analyses of S1, S2 and HE (1992) J. Gen. Virol., 73, pp. 1725-1737; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Yoo, D., Deregt, D., A single amino acid change within antigenic domain II of the spike protein of bovine coronavirus confers resistance to virus neutralization (2001) Clin. Diagn. Lab. 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"Falsey A.R., Walsh E.E., Hayden F.G.","7003365074;7202168527;7103233446;","Rhinovirus and coronavirus infection-associated hospitalizations among older adults",2002,"Journal of Infectious Diseases","185","9",,"1338","1341",,126,"10.1086/339881","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036569143&doi=10.1086%2f339881&partnerID=40&md5=aa1dad2d9e6a402fced65a1cbddeb082","Division of Infectious Diseases and Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester General Hospital, Rochester, NY, United States; Departments of Internal Medicine and Pathology, University of Virginia School of Medicine, Charlottesville, United States","Falsey, A.R., Division of Infectious Diseases and Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester General Hospital, Rochester, NY, United States; Walsh, E.E., Division of Infectious Diseases and Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester General Hospital, Rochester, NY, United States; Hayden, F.G., Departments of Internal Medicine and Pathology, University of Virginia School of Medicine, Charlottesville, United States","Rhinoviruses and coronaviruses are recognized as the major causes of the common cold syndrome. The role of these viruses in more serious respiratory illnesses resulting in hospitalization is less well defined. During a winter when influenza A infection was prevalent, 100 elderly adults hospitalized because of cardiopulmonary illnesses were evaluated for rhinovirus and coronavirus infection. Patients who tested negative for influenza or respiratory syncytial virus had nasal swab samples tested for rhinovirus, coronavirus OC43, and coronavirus 229E by reverse-transcription polymerase chain reaction and for coronaviruses by serologic testing. Twelve percent of patients had rhinovirus or coronavirus identified (rhinovirus, 4 patients; coronavirus 229E, 4 patients; coronavirus OC43, 3 patients; and mixed rhinovirus/coronavirus 229E infection, 1 patient). All patients had significant underlying diseases. Although all patients recovered, the mean length of stay was 8 days; 4 persons had pneumonia, and 1 required ventilator support. These data suggest that rhinoviruses and coronaviruses may be associated with serious respiratory illnesses in frail older adults.",,"aged; article; artificial ventilation; cardiopulmonary insufficiency; common cold; Coronavirus; disease association; female; hospitalization; human; Influenza virus A; length of stay; major clinical study; male; nose smear; pneumonia; prevalence; priority journal; Respiratory syncytial pneumovirus; respiratory tract disease; reverse transcription polymerase chain reaction; Rhinovirus; serology; virus infection; winter; Aged; Aged, 80 and over; Common Cold; Coronavirus Infections; Female; Hospitalization; Humans; Length of Stay; Male; Middle Aged; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction","Gwaltney, J.M., Hendley, J.O., Simon, G., Jordan, W.S., Rhinovirus infections in an industrial population. I. 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Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0036569143
"Tan K., Zelus B.D., Meijers R., Liu J.-H., Bergelson J.M., Duke N., Zhang R., Joachimiak A., Holmes K.V., Wang J.-H.","35182036600;6602571243;6603806959;36066228400;7005085403;7004239483;7404864581;26540762500;7201657724;7701330874;","Crystal structure of murine sCEACAM1a[1, 4]: A coronavirus receptor in the CEA family",2002,"EMBO Journal","21","9",,"2076","2086",,84,"10.1093/emboj/21.9.2076","https://www.scopus.com/inward/record.uri?eid=2-s2.0-18344379124&doi=10.1093%2femboj%2f21.9.2076&partnerID=40&md5=8a9135d16f56c0282d95a6df95f84da7","Division of Reproductive Biology, United States; University of London, United Kingdom; Research and Development, Australia; College of Chemistry and Molecular Engineering, China; University of Sheffield, United Kingdom; Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, United States","Tan, K., Division of Reproductive Biology, United States; Zelus, B.D., Division of Reproductive Biology, United States; Meijers, R., Division of Reproductive Biology, United States; Liu, J.-H., University of London, United Kingdom; Bergelson, J.M., Research and Development, Australia; Duke, N., College of Chemistry and Molecular Engineering, China; Zhang, R., University of Sheffield, United Kingdom; Joachimiak, A., University of Sheffield, United Kingdom; Holmes, K.V., Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, United States; Wang, J.-H., Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, United States","CEACAM1 is a member of the carcinoembryonic antigen (CEA) family. Isoforms of murine CEACAM1 serve as receptors for mouse hepatitis virus (MHV), a murine coronavirus. Here we report the crystal structure of soluble murine sCEACAM1a[1, 4], which is composed of two Ig-like domains and has MHV neutralizing activity. Its N-terminal domain has a uniquely folded CC' loop that encompasses key virus-binding residues. This is the first atomic structure of any member of the CEA family, and provides a prototypic architecture for functional exploration of CEA family members. We discuss the structural basis of virus receptor activities of murine CEACAM1 proteins, binding of Neisseria to human CEACAM1, and other homophilic and heterophilic interactions of CEA family members.","Bacterial binding; CEA family; Cell adhesion; Coronavirus receptor; Crystal structure","carcinoembryonic antigen; carcinoembryonic antigen related cell adhesion molecule 1; cell adhesion molecule; unclassified drug; virus receptor; amino terminal sequence; article; bacterium adherence; binding site; crystal structure; mouse; Murine hepatitis coronavirus; Neisseria; nonhuman; priority journal; protein conformation; protein domain; protein family; protein protein interaction; Amino Acid Sequence; Animals; Antigens, CD; Carcinoembryonic Antigen; Cell Adhesion Molecules; Conserved Sequence; Coronavirus; Crystallography, X-Ray; Glycoproteins; Mice; Molecular Sequence Data; Multigene Family; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Receptors, Virus; Sequence Alignment; Bacteria (microorganisms); Coronavirus; Murinae; Murine hepatitis virus; Neisseria","Bates, P.A., Luo, J., Sternberg, M.J., A predicted three-dimensional structure for the carcinoembryonic antigen (CEA) (1992) FEBS Lett, 301, pp. 207-214; Beauchemin, N., Redefined nomenclature for members of the carcinoembryonic antigen family (1999) Exp. 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"Gagneur A., Sizun J., Vallet S., Legrand M.C., Picard B., Talbot P.J.","6508170069;35605340000;36831918800;7102317918;11640757600;7102670281;","Coronavirus-related nosocomial viral respiratory infections in a neonatal and paediatric intensive care unit: A prospective study",2002,"Journal of Hospital Infection","51","1",,"59","64",,72,"10.1053/jhin.2002.1179","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036584349&doi=10.1053%2fjhin.2002.1179&partnerID=40&md5=55df40fbe6b49fbef94abb0e83f1b08f","Pediatric Intensive Care Unit, Department of Paediatrics, University Hospital, 29609 Brest, France; Department of Microbiology, University Hospital, Brest, France; Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Université du Québec, Laval, Qué., Canada","Gagneur, A., Pediatric Intensive Care Unit, Department of Paediatrics, University Hospital, 29609 Brest, France; Sizun, J., Pediatric Intensive Care Unit, Department of Paediatrics, University Hospital, 29609 Brest, France; Vallet, S., Department of Microbiology, University Hospital, Brest, France; Legrand, M.C., Department of Microbiology, University Hospital, Brest, France; Picard, B., Department of Microbiology, University Hospital, Brest, France; Talbot, P.J., Laboratory of Neuroimmunovirology, INRS-Institut Armand-Frappier, Université du Québec, Laval, Qué., Canada","The incidence of nosocomial viral respiratory infections (NVRI) in neonates and children hospitalized in paediatric and neonatal intensive care units (PNICU) is unknown. Human coronaviruses (HCoV) have been implicated in NVRI in hospitalized preterm neonates. The objectives of this study were to determine the incidence of HCoV-related NVRI in neonates and children hospitalized in a PNICU and the prevalence of viral respiratory tract infections in staff. All neonates (age≤28 days) and children (age>28 days) hospitalized between November 1997 and April 1998 were included. Nasal samples were obtained by cytological brush at admission and weekly thereafter. Nasal samples were taken monthly from staff. Virological studies were performed, using indirect immunofluorescence, for HCoV strains 229E and OC43, respiratory syncytial virus (RSV), influenza virus types A and B, paramyxoviruses types 1, 2 and 3 and adenovirus. A total of 120 patients were enrolled (64 neonates and 56 children). Twenty-two samples from 20 patients were positive (incidence 16.7%). In neonates, seven positive samples, all for HCoV, were detected (incidence 11%). Risk factors for NVRI in neonates were: duration of hospitalization, antibiotic treatment and duration of parenteral nutrition (P <0.01). Monthly prevalence of viral infections in staff was between 0% and 10.5%, mainly with HCoV. In children, 15 samples were positive in 13 children at admission (seven RSV, five influenza and three adenovirus) but no NVRI were observed. In spite of a high rate of community-acquired infection in hospitalized children, the incidence of NVRI with common respiratory viruses appears low in neonates, HCoV being the most important pathogen of NRVI in neonates during this study period. Further research is needed to evaluate the long-term impact on pulmonary function. © 2002 The Hospital Infection Society.","Human coronavirus; Infant; Neonate; Nosocomial infection; PNICU; Virus","antibiotic agent; Adenovirus; adolescent; antibiotic therapy; article; child; controlled study; Coronavirus; female; hospital infection; hospitalization; human; immunofluorescence; incidence; infant; Influenza virus A; Influenza virus B; lung function; major clinical study; male; medical staff; newborn; newborn infection; newborn intensive care; nose smear; Paramyxovirus; parenteral nutrition; prevalence; prospective study; Respiratory syncytial pneumovirus; respiratory tract infection; risk factor; virus identification; virus strain; communicable disease; cross infection; heterozygote; infection control; intensive care; newborn intensive care; preschool child; respiratory tract infection; virology; virus infection; Adolescent; Carrier State; Child; Child, Preschool; Community-Acquired Infections; Coronavirus Infections; Cross Infection; Female; Humans; Incidence; Infant; Infant, Newborn; Infection Control; Intensive Care Units, Neonatal; Intensive Care Units, Pediatric; Male; Prospective Studies; Respiratory Tract Infections","Ford-Jones, E.L., Mindorff, C.M., Langley, J.M., Epidemiologic study of 4684 hospital-acquired infections in pediatric patients (1989) Pediatr. Infect. Dis., 8, pp. 668-675; Gaynes, R.P., Edwards, J.R., Jarvis, W.R., Culver, D.H., Tolson, J.S., Martone, W.J., Nosocomial infections among neonates in high-risk nurseries in the United States National (1996) Pediatrics, 98, pp. 357-361; Gaynes, R.P., Martone, W.J., Culver, D.H., Comparison of rates of nosocomial infections in neonatal intensive care units in the United States (1991) Am. J. Med., 91, pp. 1925-1965; Allen, U., Ford-Jones, E.L., Nosocomial infections in the pediatric patient: An update (1990) Am. J. Infect. Control, 18, pp. 176-193; Sizun, J., Soupre, D., Legrand, M.C., Neonatal nosocomial respiratory infection with coronavirus: A prospective study in a neonatal intensive care unit (1995) Acta Paediatr., 84, pp. 617-620; Hall, C.B., Nosocomial viral respiratory infections: Perennial weeds on pediatric wards (1981) Am. J. Med., 70, pp. 670-676; Goldwater, P.N., Martin, A.J., Ryan, B., A survey of nosocomial respiratory viral infections in a children's hospital: Occult respiratory infections in patients admitted during an epidemic season (1991) Infect. Control Hosp. Epidemiol., 12, pp. 231-238; Barnes, S.D., Leclair, J.M., Forman, M.S., Townsend, T.R., Laughlin, G.M., Charache, P., Comparison of nasal brush and naso-pharyngeal aspirate techniques in obtaining specimens for detection of respiratory syncytial viral antigen by immunofluorescence (1989) Pediatr. Inf. Dis. J., 8, pp. 598-601; Sizun, J., Arbour, N., Talbot, P.J., Detection of human Coronaviruses by fluorescent monoclonal antibody staining and reverse transcription-PCR in cell cultures (1998) J. Virol. Methods, 72, pp. 145-152; Sizun, J., Baron, R., Soupre, D., Giroux, J.D., de Parscau, L., Infections nosocomiales liées au virus respiratorie syncytial: Quelles measures d'hygiène? (1996) Arch. Pédiatr., 3, pp. 723-727; Chidekel, A.S., Rosen, C.L., Bazzy, A.R., Rhinovirus infection associated with serious lower respiratory illness in patients with bronchopulmonary dysplasia (1997) Pediatr. Infect. Dis. J., 16, pp. 43-47; Valenti, W.M., Clarke, T.A., Hall, C.B., Menegus, M.A., Shapiro, D.L., Concurrent outbreaks of rhinovirus and respiratory syncytial virus in an intensive care nursery: Epidemiology and associated risk factors (1982) J. Pediatr., 100, pp. 722-726; Hall, C.B., Kopelman, A.E., Douglas, R.G., Geiman, J.M., Meagher, M.P., Neonatal respiratory syncytial virus infection (1979) N. Engl. J. Med., 300, pp. 393-396; Piedra, P.A., Kasel, J.A., Norton, H.J., Description of an adenovirus type 8 outbreak in hospitalized neonates born prematurely (1992) Pediatr. Infect. Dis. J., 11, pp. 460-465; Meibalane, R., Sedmak, G.V., Sasidharan, P., Garg, P., Grausz, J.P., Outbreak of influenza in a neonatal intensive care unit (1977) J. Pediatr., 91, pp. 974-976; Modlin, J.F., Perinatal echovirus infection: Insights from a literature review of 61 cases of serious infection and 16 outbreaks in nurseries (1986) Rev. Infect. Dis., 8, pp. 918-926; Druyts-Voets, E., Van Renterghem, L., Gerniers, S., Coxsackie B virus epidemiology and neonatal infection in Belgium (1993) J. Infect., 27, pp. 311-316; Rabkin, C.S., Telzak, E.E., Ho, M.S., Outbreak of echovirus 11 infection in hospitalized neonates (1988) Pediatr. Infect. Dis. J., 7, pp. 186-190; Meissner, H.C., Murray, S.A., Kiernan, M.A., Snydman, D.R., McIntosh, K., A simultaneous outbreak of respiratory syncytial virus and parainfluenza virus type 3 in a newborn nursery (1984) J. Pediatr., 104, pp. 680-684; Moisiuk, S.E., Robson, D., Klass, L., Outbreak of parainfluenza virus type 3 in an intermediate care neonatal nursery (1998) Pediatr. Infect. Dis. 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Microbiol., 34, pp. 3007-3011; Sizun, J., Soupre, D., Giroux, J., Nasal colonization with coronavirus and apnea of the premature newborn (1993) Acta Paediatr., 82, p. 238; Myint, S., Human coronaviruses infections (1995) The Coronaviridae, pp. 389-401. , SG Siddell (Ed.), New York: Plenum Press; Freymuth, F., Vabret, A., Brouard, A., Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae infections in exacerbations of asthma in children (1999) J. Clin. Virol., 13, pp. 131-139; Vernotte, E., Legrand, M.C., Gagneur, A., Salmon, J., Sizun, J., de Parscau, L., Exacerbation de l'asthme: Le rôle déclenchant des coronavirus humains n'est pas confirmé (1999) Arch. Pédiatr., 6, pp. 583s; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Falsey, A.R., Mc Cann, R.M., Hall, W., The common cold in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J. Am. Geriatr. Soc., 45, pp. 706-711; Vabret, A., Brouard, J., Petitjean, J., Eugene-Ruellan, G., Freymuth, F., Infections à coronavirus humains. Importance et diagnostic (1998) Presse. 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Virol., 66, pp. 2743-2748; Sizun, J., Yu, M.W.N., Talbot, P.J., Survival of 229-E and OC-43 human Coronaviruses in suspension and on surfaces after drying. Effect of chemical disinfection (2000) J. Hosp. Infect., 46, pp. 55-60; Hall, C.B., Douglas, R.G., Modes of transmission of respiratory syncytial virus (1981) J. Pediatr., 99, pp. 100-110","Sizun, J.; Unite de Reanimation Pediatrique, Departement de Pediatrie, CHU, 29609 Brest, France; email: Jacques.Sizun@chu-brest.fr",,,01956701,,JHIND,"12009822","English","J. Hosp. Infect.",Article,"Final",Open Access,Scopus,2-s2.0-0036584349
"Niskanen R., Lindberg A., Tråvén M.","7003405025;55423918900;6603563444;","Failure to spread bovine virus diarrhoea virus infection from primarily infected calves Despite Concurrent Infection with Bovine Coronavirus",2002,"Veterinary Journal","163","3",,"251","259",,48,"10.1053/tvjl.2001.0657","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036559275&doi=10.1053%2ftvjl.2001.0657&partnerID=40&md5=4acc978353609fff0e52e8648e9c66ba","Dept. Ruminant Med./Vet. Epidemiol., Swedish Univ. of Agricultural Sci., S-750 07 Uppsala, Sweden; Research and Development, Swedish Dairy Association, Uppsala, Sweden","Niskanen, R., Dept. Ruminant Med./Vet. Epidemiol., Swedish Univ. of Agricultural Sci., S-750 07 Uppsala, Sweden; Lindberg, A., Research and Development, Swedish Dairy Association, Uppsala, Sweden; Tråvén, M., Dept. Ruminant Med./Vet. Epidemiol., Swedish Univ. of Agricultural Sci., S-750 07 Uppsala, Sweden","Previous reports on the spread of bovine virus diarrhoea virus (BVDV) from animals primarily infected with the agent are contradictory. In this study, the possibility of transmission of BVDV from calves simultaneously subjected to acute BVDV and bovine coronavirus (BCV) infection was investigated. Ten calves were inoculated intranasally with BVDV Type 1. Each of the 10 calves was then randomly allocated to one of two groups. In each group there were four additional calves, resulting in five infected and four susceptible calves per group. Virulent BCV was actively introduced in one of the groups by means of a transmitter calf. Two calves, susceptible to both BVDV and BCV, were kept in a separate group, as controls. All ten calves actively inoculated with BVDV became infected as shown by seroconversions, and six of them also shed the virus in nasal secretions. However, none of the other eight calves in the two groups (four in each) seroconverted to this agent. In contrast, it proved impossible to prevent the spread of BCV infection between the experimental groups and consequently all 20 study calves became infected with the virus. Following infection, BCV was detected in nasal secretions and in faeces of the calves and, after three weeks in the study, all had seroconverted to this virus. All calves, including the controls, showed at least one of the following clinical signs during days 3-15 after the trial started: fever (≥40°C), depressed general condition, diarrhoea, and cough. The study showed that BVDV primarily infected cattle, even when co-infected with an enteric and respiratory pathogen, are inefficient transmitters of BVDV. This finding supports the principle of the Scandinavian BVDV control programmes that elimination of BVDV infection from cattle populations can be achieved by identifying and removing persistently infected (PI) animals, i.e. that long-term circulation of the virus without the presence of PI animals is highly unlikely. © 2002 Elsevier Science Ltd. All rights reserved.","BVDV; Calves; Infectivity; Pestevirus; Primary infection; Transmission","animal experiment; article; Bovine diarrhea virus; cattle disease; clinical feature; controlled study; Coronavirus; coughing; depression; diarrhea; feces analysis; female; fever; health program; infection control; infection prevention; infection sensitivity; inoculation; male; nonhuman; nose secretion; pathogenesis; persistent infection; poor general condition; randomization; respiratory system; Scandinavia; seroconversion; superinfection; virus detection; virus infection; virus shedding; virus transmission; virus virulence; acute disease; animal; animal disease; cattle; cattle disease; comorbidity; disease transmission; newborn; pathogenicity; virology; virus infection; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Bovine viral diarrhea virus 1; Coronavirus; Acute Disease; Animals; Animals, Newborn; Bovine Virus Diarrhea-Mucosal Disease; Cattle; Comorbidity; Coronavirus Infections; Coronavirus, Bovine; Diarrhea Virus 1, Bovine Viral; Female; Male","Alenius, S., Niskanen, R., Juntti, N., Larsson, B., Bovine coronavirus as the causative agent of winter dysentery: Serological evidence (1991) Acta Veterinaria Scandinavica, 32, pp. 163-170; Alenius, S., Lindberg, A., Larsson, B., A national approach to the control of bovine viral diarrhoea virus (1996) Proceedings of the 3rd ESVV Symposium on Pestivirus Infections, pp. 162-169. , Lelystad, The Netherlands, September 1996, eds S. Edwards D. J. Paton G. Wensvoort, DLO Institute for Animal Science and Health, 1997; Barber, D.M.L., Nettleton, P.F., Herring, J.A., Disease in a dairy herd associated with the introduction and spread of bovine virus diarrhoea virus (1985) Veterinary Record, 117, pp. 459-464; Battaglia, M., Lutz, H., Wyler, R., Serologische Übersichtsuntersuchung über die Verbreitung des bovines Coronavirus in der Schweiz (1986) Schweizer Archiv Für Tierheilkunde, 128, pp. 213-218; Bitsch, V., Houe, H., Rønsholt, L., Farsø Madsen, K., Valbak, J., Roug, N.H., Eckehardt, C.H., Towards control and eradication of BVDV (1994) Dansk Veterinærtidsskrift, 77, pp. 445-450; Bolin, S.R., Ridpath, J.F., Differences in virulence between two noncytopathic bovine viral diarrhea viruses in calves (1992) American Journal of Veterinary Research, 53, pp. 2157-2163; Brownlie, J., Clarke, M.C., Howard, C.J., Pocock, D.H., Pathogenesis and epidemiology of bovine virus diarrhoea virus infection of cattle (1987) Annales de Recherches Veterinaires, 18, pp. 157-166; Bruschke, C., Pathogenesis and vaccinology of BVDV infections (1998), Thesis DLO Institute for Animal Science and Health, Lelystadt, The Netherlands; Carman, S., van Dreumel, T., Ridpath, J., Hazlett, M., Alves, D., Dubovi, E., Tremblay, R., Anderson, N., Severe acute bovine viral diarrhea in Ontario, 1993-1995 (1998) Journal of Veterinary Diagnostic Investigation, 10, pp. 27-35; Corapi, W., Elliot, D., French, T.W., Arthur, D.G., Bezek, D.M., Dubovi, E.J., Thrombocytopenia and hemorrhages in veal calves infected with bovine viral diarrhea virus (1990) Journal of the American Veterinary Medical Association, 196, pp. 590-596; Durham, J.K., Hassard, L.E., Armstrong, K.R., Naylor, J.M., Coronavirus-associated diarrhea (winter dysentery) in adult cattle (1989) Canadian Veterinary Journal, 30, pp. 825-827; Edwards, S., Observations of bovine viral diarrhoea virus infection in dairy herds, and the response to different control strategies (1997) Proceedings of the 3rd ESVV Symposium on Pestivirus Infections, pp. 173-176. , Lelystad, The Netherlands, September 1996, In eds S. 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B MacFerran eds: Martinus Nijhoff Publishers; Meyling, A., Jensen, A.M., Transmission of bovine virus diarrhoea virus (BVDV) by artificial insemination (AI) with semen from a persistently infected bull (1988) Veterinary Microbiology, 17, pp. 97-105; Meyling, A., Houe, H., Jensen, A.M., Epidemiology of bovine virus diarrhoea virus (1990) Revue Scientifique et Technique Office International des Epizooties, 9, pp. 75-93; Moerman, A., Straver, P.J., de Jong, M.C.M., Quak, J., Baanvinger, Th., van Oirschot, J.T., A long term epidemiological study of bovine viral diarrhoea infections in a large herd of dairy cattle (1993) Veterinary Record, 132, pp. 622-626; Niskanen, R., Lindberg, A., Larsson, B., Alenius, S., Lack of virus transmission from primarily bovine viral diarrhoea virus (BVDV) infected calves to susceptible peers (2000) Acta Veterinaria Scandinavica, 41, pp. 93-99; Olsson, S.-O., Jakobsson, L., Alenius, S., Larsson, B., A voluntary control programme against infection with bovine diarrhoea virus (BVDV) (1993) Svensk Veterinärtidning, 45, pp. 411-415; Paton, D.J., Christiansen, K.H., Alenius, S., Cranwell, M.P., Pritchard, G.C., Drew, T.W., Prevalence of antibodies to bovine virus diarrhoea virus and other viruses in bulk tank milk in England and Wales (1998) Veterinary Record, 142, pp. 385-391; Pritchard, W.R., The bovine viral diarrhea-mucosal disease complex (1963) Advances in Veterinary Science, pp. 1-47. , C. 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Diagnostics, Clinical Picture, Epidemiology and Herd Immunity, , Doctoral Thesis Department of Ruminant Medicine and Veterinary Epidemiology, Swedish University of Agricultural Sciences, Uppsala; Tråvén, M., Alenius, S., Fossum, C., Larsson, B., Primary bovine viral diarrhoea virus infection in calves following direct contact with a persistently viraemic calf (1991) Journal of Veterinary Medicine B, 38, pp. 453-462; Tråvén, M., Björnerot, L., Larsson, B., Nation-wide survey of antibodies to bovine coronavirus in Swedish dairy herd bulk milk (1998) Veterinary Record, 144, pp. 527-529; Tråvén, M., Näslund, K., Linde, N., Linde, B., Silvd, J., Nyberg, O., The Norwegian programme for eradication of bovine viral diarrhoea/mucosal disease (1994) Proceedings of the 18th World Buiatric Congress, pp. 773-775. , 26th Congress of the Italian association of Buiatrics; Waage, S., Krogsrud, J., Nyberg, O., The Norwegian programme for eradication of bovine viral diarrhoea/mucosal disease (1994) Proceedings of the 18th World Buiatirc Congress, pp. 773-775. , 26th Congress of the Italian association of Buiatrics","Niskanen, R.; Dept. Ruminant Med./Vet. Epidemiol., Swedish Univ. of Agricultural Sci., S-750 07 Uppsala, Sweden; email: Rauni.Niskanen@idmed.slu.se",,,10900233,,VTJRF,"12090767","English","Vet. J.",Article,"Final",Open Access,Scopus,2-s2.0-0036559275
"Chen H., Wurm T., Britton P., Brooks G., Hiscox J.A.","57209632300;6602454962;57203302770;7202058172;7004565877;","Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell",2002,"Journal of Virology","76","10",,"5233","5250",,81,"10.1128/JVI.76.10.5233-5250.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036238652&doi=10.1128%2fJVI.76.10.5233-5250.2002&partnerID=40&md5=bb9496095ac3a4ae41ae2124fa205ac9","School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom","Chen, H., School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Wurm, T., School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Britton, P., School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Brooks, G., School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; Hiscox, J.A., School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom","Coronavirus nucleoproteins (N proteins) localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The nucleolus is the site of ribosome biogenesis and sequesters cell cycle regulatory complexes. Two of the major components of the nucleolus are fibrillarin and nucleolin. These proteins are involved in nucleolar assembly and ribosome biogenesis and act as chaperones for the import of proteins into the nucleolus. We have found that fibrillarin is reorganized in primary cells infected with the avian coronavirus infectious bronchitis virus (IBV) and in continuous cell lines that express either IBV or mouse hepatitis virus N protein. Both N protein and a fibrillarin-green fluorescent protein fusion protein colocalized to the perinuclear region and the nucleolus. Pull-down assays demonstrated that IBV N protein interacted with nucleolin and therefore provided a possible explanation as to how coronavirus N proteins localize to the nucleolus. Nucleoli, and proteins that localize to the nucleolus, have been implicated in cell growth-cell cycle regulation. Comparison of cells expressing IBV N protein with controls indicated that cells expressing N protein had delayed cellular growth. This result could not to be attributed to apoptosis. Morphological analysis of these cells indicated that cytokinesis was disrupted, an observation subsequently found in primary cells infected with IBV. Coronaviruses might therefore delay the cell cycle in interphase, where maximum translation of viral mRNAs can occur.",,"cell antigen; fibrillarin; green fluorescent protein; guanine nucleotide binding protein; hybrid protein; nucleolin; nucleoprotein; animal cell; article; Avian infectious bronchitis virus; cell cycle; cell growth; cell line; cellular distribution; controlled study; cytokinesis; human; human cell; interphase; nonhuman; nucleolus; plasmid; priority journal; protein expression; protein localization; protein protein interaction; ribosome; RNA translation; virus cell interaction; Animals; Antigens; Cell Cycle; Cell Nucleolus; Cercopithecus aethiops; Chromosomal Proteins, Non-Histone; Coronavirus; Hela Cells; Humans; Nucleocapsid Proteins; Phosphoproteins; RNA-Binding Proteins; Transfection; Vero Cells","Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K., Watson, J.D., (1994) Molecular biology of the cell, 3rd ed., pp. 381-382. , Garland Publishing, New York, N.Y; Allain, F.H.-T., Bouvet, P., Dieckmann, T., Feigon, J., Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin (2000) EMBO J., 19, pp. 6870-6881; An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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Virol., 72, pp. 6699-6709; Watanabe, N., Yamaguchi, T., Akimoto, Y., Rattner, J., Hirano, H., Nakauchi, H., Induction of M-phase arrest and apoptosis after HIV-1 Vpr expression through uncoupling of nuclear and centrosomal cycle in HeLa cells (2000) Exp. Cell Res., 258, pp. 261-269; Wurm, T., Chen, H., Britton, P., Brooks, G., Hiscox, J.A., Localization to the nucleolus is a common feature of coronavirus nucleoproteins and the protein may disrupt host cell division (2001) J. Virol., 75, pp. 9345-9356; Zatsepina, O.V., Rousselet, A., Chan, P.K., Olson, M.O.J., Jordan, E.G., Bornens, M., The nucleolar phosphoprotein B23 redistributes in part to the spindle poles during mitosis (1999) J. Cell Sci., 112, pp. 455-466","Hiscox, J.A.; School of Animal/Microbial Sciences, University of Reading, P.O. Box 228, Reading RG6 6AJ, United Kingdom; email: j.a.hiscox@reading.ac.uk",,,0022538X,,JOVIA,"11967337","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036238652
"Kuo L., Masters P.S.","7101601942;7006234572;","Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus",2002,"Journal of Virology","76","10",,"4987","4999",,107,"10.1128/JVI.76.10.4987-4999.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036232932&doi=10.1128%2fJVI.76.10.4987-4999.2002&partnerID=40&md5=815d029c884943987120108a3094f68d","David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Avenue, Albany, NY 12201-2002, United States","Kuo, L., David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Avenue, Albany, NY 12201-2002, United States; Masters, P.S., David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Avenue, Albany, NY 12201-2002, United States","The coronavirus membrane (M) protein is the most abundant virion protein and the key component in viral assembly and morphogenesis. The M protein of mouse hepatitis virus (MHV) is an integral membrane protein with a short ectodomain, three transmembrane segments, and a large carboxy-terminal endodomain facing the interior of the viral envelope. The carboxy terminus of MHV M has previously been shown to be extremely sensitive to mutation, both in a virus-like particle expression system and in the intact virion. We have constructed a mutant, MΔ2, containing a two-amino-acid truncation of the M protein that was previously thought to be lethal. This mutant was isolated by means of targeted RNA recombination with a powerful host range-based selection allowed by the interspecies chimeric virus fMHV (MHV containing the ectodomain of the feline infectious peritonitis virus S protein). Analysis of multiple second-site revertants of the MΔ2 mutant has revealed changes in regions of both the M protein and the nucleocapsid (N) protein that can compensate for the loss of the last two residues of the M protein. Our data thus provide the first genetic evidence for a structural interaction between the carboxy termini of the M and N proteins of MHV. In addition, this work demonstrates the efficacy of targeted recombination with fMHV for the systematic genetic analysis of corona-virus structural protein interactions.",,"amino acid; membrane protein; nucleocapsid protein; RNA; article; carboxy terminal sequence; genotype; Murine hepatitis coronavirus; mutation; nonhuman; phenotype; priority journal; protein protein interaction; reverse transcription polymerase chain reaction; RNA recombination; Amino Acid Sequence; Animals; Base Sequence; Cell Line; Membrane Glycoproteins; Molecular Sequence Data; Murine hepatitis virus; Mutation; Nucleocapsid; Nucleocapsid Proteins; Protein Binding; Viral Envelope Proteins; Viral Matrix Proteins; Virus Replication","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. 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Siddell (ed.), Plenum Press, New York, N.Y; Van Marie, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Vennema, H., Godeke, G.-J., Rossen, J.W.A., Voorhout, W.F., Horzinek, M.C., Opstelten, D.-J.E., Rottier, P.J.M., Nueleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Avenue, Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"11967315","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036232932
"Muirden A.","6508347382;","Prevalence of feline leukaemia virus and antibodies to feline immunodeficiency virus and feline coronavirus in stray cats sent to an RSPCA hospital",2002,"Veterinary Record","150","20",,"621","625",,42,"10.1136/vr.150.20.621","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037129540&doi=10.1136%2fvr.150.20.621&partnerID=40&md5=47085b799f1b02c39ed7ca47a0846e6c","219 Kensington Road, Kensington, SA 5608, Australia","Muirden, A., 219 Kensington Road, Kensington, SA 5608, Australia","A total of 517 stray cats at an RSPCA veterinary hospital were tested for feline leukaemia virus (FeLV), feline coronavirus (FCoV) and feline immunodeficiency virus (FIV). The prevalence of FeLV was 3.5 per cent in all the cats, 1.4 per cent in healthy cats and 6.9 per cent in sick cats. FeLV positivity was associated only with disease of non-traumatic origin. Antibodies to FCoV were present in 22.4 per cent of the cats, and their prevalence was significantly higher in cats over two years old and in feral/semiferal cats. The prevalence of antibodies to FIV was 10.4 per cent in all the cats, 4.9 per cent in healthy cats and 16.7 per cent in sick cats. The prevalence of FIV antibodies was significantly higher in entire males and neutered males than in females, in cats over two years old compared with younger cats, and in cats suffering disease of non-traumatic origin rather than in healthy cats or cats suffering only from trauma. Sex, age and health status were each independently highly associated with FIV antibodies.",,"virus antibody; virus antibody; age; aged; animal health; antibody titer; article; cat disease; controlled study; Coronavirus; Feline immunodeficiency virus; Feline leukemia virus; female; health status; laboratory diagnosis; male; non profit hospital; nonhuman; seroprevalence; sex difference; United Kingdom; veterinary medicine; virus detection; animal; animal disease; Australia; blood; cat; cat disease; hospital; immunology; information processing; isolation and purification; prevalence; virology; Animalia; Coronavirus; Felidae; Feline coronavirus; Feline immunodeficiency virus; Feline leukemia virus; Felis catus; Animals; Antibodies, Viral; Cat Diseases; Cats; Coronavirus, Feline; Female; Hospitals, Animal; Immunodeficiency Virus, Feline; Leukemia Virus, Feline; Male; Prevalence; Records; South Australia","Addie, D.D., Jarrett, O., A study of naturally occurring feline coronavirus infections in kittens (1992) Veterinary Record, 130, pp. 133-137; Addie, D.D., Jarrett, O., Feline coronavirus antibodies in cats (1992) Veterinary Record, 131, pp. 223-224; Friend, S.C.E., Birch, C.J., Lording, P.M., Marshall, J.A., Studdert, M.J., Feline immunodeficiency virus: Prevalence, disease associations and isolation (1990) Australian Veterinary Journal, 67, pp. 237-242; Gruffydd-Jones, T.J., Hopper, C.D., Harbour, D.A., Lutz, H., Serological evidence of feline immunodeficiency virus infection in UK cats from 1975-76 (1988) Veterinary Record, 123, pp. 569-571; Hardy W.D., Jr., Feline Leukemia Virus (1980), pp. 3-28. , Amsterdam, Elsevier North Holland; Hopper, C.D., Sparkes, A.H., Gruffydd-Jones, T.J., Crispin, S.M., Muir, P., Harbour, D.A., Stokes, C.R., Clinical and laboratory findings in cats infected with feline immunodeficiency virus (1989) Veterinary Record, 125, pp. 341-346; Horzinek, M.C., Osterhaus, A.D.M.E., Feline infectious peritonitis: A worldwide serosurvey (1979) American Journal of Veterinary Research, 40, pp. 1487-1492; Hosie, M.J., Jarrett, O., Serological responses of cats to feline immunodeficiency virus (1990) AIDS, 4, pp. 215-220; Hosie, M.J., Robertson, C., Jarrett, O., Prevalence of feline leukemia virus and antibodies to feline immunodeficiency virus in cats in the United Kingdom (1989) Veterinary Record, 128, pp. 293-297; Ishida, T., Washizu, T., Toriyabe, K., Motoyoshi, S., Tomoda, I., Pedersen, N.C., Feline immunodeficiency virus infection in cats of Japan (1989) Journal of the American Veterinary Medical Association, 194, pp. 221-225; Jarrett, O., Golder, M.C., Stewart, M.F., Detection of transient and persistent feline leukemia virus infections (1982) Veterinary Record, 110, pp. 225-228; Knowles, J.O., Gaskell, R.M., Gaskell, C.J., Harvey, C.E., Lutz, H., Prevalence of feline calicivirus, feline leukemia virus and antibodies to FIV in cats with chronic stomatitis (1989) Veterinary Record, 124, pp. 336-338; Lutz, H., Pedersen, N.C., Durbin, R., Theilen, G.H., Monoclonal antibodies to three epitopic regions of feline leukemia virus p27 and their use in enzyme-linked immunosorbent assay of p27 (1983) Journal of Immunological Methods, 56, pp. 209-220; Pedersen, N.C., Ho, E.W., Brown, M.L., Yamamoto, J.K., Isolation of a T-lymphotropic virus from domestic cats with an immunodeficiency-like syndrome (1987) Science, 235, pp. 790-793; Reinacher, M., Diseases associated with spontaneous feline leukemia virus (FeLV) infection in cats (1989) Veterinary Immunology and Immunopathology, 21, pp. 85-95; Shelton, G.H., Waltier, R.M., Connor, S.C., Grant, C.K., Prevalence of feline immunodeficiency virus and feline leukemia virus infections in pet cats (1989) Journal of the American Animal Hospital Association, 25, pp. 7-12; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., Coronavirus serology in healthy pedigree cats (1992) Veterinary Record, 131, pp. 35-36; Thomas, J.B., Robinson, W.F., Chadwick, B.J., Robertson, I.D., Beetson, S.A., Association of renal disease indicators with feline immunodeficiency virus infection (1993) Journal of the American Animal Hospital Association, 29, pp. 320-326; Ueland, K., Lutz, H., Prevalence of feline leukemia virus and antibodies to feline immunodeficiency virus in cats in Norway (1992) Journal of Veterinary Medicine, 39, pp. 53-58; Yamamoto, J.K., Hansen, H., Ho, E.W., Morishita, T.Y., Okuda, T., Sawa, T.R., Nakamura, R.M., Pedersen, N.C., Epidemiologic and clinical aspects of feline immunodeficiency virus infection in cats from the continental United States and Canada and possible mode of transmission (1989) Journal of the American Veterinary Medical Association, 194, pp. 213-220","Muirden, A.219 Kensington Road, Kensington, SA 5608, Australia",,"British Veterinary Association",00424900,,VETRA,"12046785","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0037129540
"Winther B., Hayden F.G., Arruda E., Dutkowski R., Ward P., Owen Hendley J.","7003521735;7103233446;7004935664;6602164863;57198935522;7006491299;","Viral respiratory infection in schoolchildren: Effects on middle ear pressure",2002,"Pediatrics","109","5",,"826","832",,52,"10.1542/peds.109.5.826","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036252426&doi=10.1542%2fpeds.109.5.826&partnerID=40&md5=ff44cfec4b1b1a297c48e3f2a7c54abb","University of Virginia Health System, Charlottesville, VA, United States; University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil; Roche Products Ltd., Welwyn, United Kingdom; University of Virginia Health System, Department of Otolaryngology, Box 800713, Charlottesville, VA 22906, United States","Winther, B., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom, University of Virginia Health System, Department of Otolaryngology, Box 800713, Charlottesville, VA 22906, United States; Hayden, F.G., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom; Arruda, E., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom; Dutkowski, R., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom; Ward, P., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom; Owen Hendley, J., University of Virginia Health System, Charlottesville, VA, United States, University of Sao Paulo, School of Medicine, Ribeirao Preto Sao Paulo, Brazil, Roche Products Ltd., Welwyn, United Kingdom","Objective. To evaluate the effect of uncomplicated viral respiratory infections (colds) on middle ear pressure in healthy school-aged children. Methods. Children (ages 2-12) with normal tympanograms before onset of illness had bilateral tympanometry daily except weekends for 2 weeks after the onset of a cold. Nasopharyngeal secretion obtained at onset of illness was cultured for bacterial pathogens of otitis media using selective agars and tested for rhinovirus, coronavirus, respiratory syncytial virus, influenza A and B, and parainfluenza 1-3 by reverse transcriptase polymerase chain reaction technology. Tympanometry was designated as abnormal with peak pressure of ≤-5-100 daPa or ≥50 daPa and/or a compliance peak of &gt;0.2 cm3. Results. Eighty-six colds were studied, 82 in school-children (5-12 years old) and 4 in 2- to 3-year-olds. Abnormal negative middle ear pressure occurred at least once during the 2 weeks after onset in 57 (66%) of the 86 colds. Tympanometry was abnormal in the first week after onset in 50 (88%) of the 57 colds and was abnormal on a single day in 17 (30%) of the 57. The middle ear pressure abnormalities were intermittent and shifted from one ear to the other ear from day to day. Reverse transcriptase polymerase chain reaction was positive for a respiratory virus in 56 (65%) of the 86 illnesses. Rhinovirus was found in 48% and respiratory syncytial virus in 14%. Pathogenic bacteria (Streptococcus pneumoniae, Haemophilus influenzae, or Moraxella catarrhalis) were detected in nasopharyngeal secretion in 29 (34%) of the 86 colds; the bacteria were in high titer (≥103 cfu/mL) in 26 of the 29 positive specimens. None developed illness that required a visit to a physician. Age, detection of a respiratory virus, and presence of bacterial pathogen in the nasopharyngeal secretion had a negligible effect on the occurrence of abnormal tympanometry. Occurrence of negative middle ear pressure in winter-spring colds was significantly greater than in fall colds for unexplained reasons. Conclusions. Transient negative middle ear pressure occurred in two thirds of uncomplicated colds in healthy children. This negative pressure, which may facilitate secondary viral or bacterial otitis media, seems to result from viral infection of the nasopharynx and distal tube causing bilateral eustachian tube dysfunction. Tympanometry provides an objective measure of the potential beneficial effects of investigational treatments on the risk of eustachian tube dysfunction/otitis media.","Eustachian tube; Otitis media; Tympanometry; Viral respiratory infections","article; auditory tube dysfunction; bacterium culture; child; controlled study; Coronavirus; female; Haemophilus influenzae; human; Influenza virus A; Influenza virus B; major clinical study; male; measurement; middle ear pressure; Moraxella catarrhalis; nasopharynx; onset age; otitis media; Parainfluenza virus; polymerase chain reaction; priority journal; Respiratory syncytial pneumovirus; respiratory tract infection; reverse transcription polymerase chain reaction; Rhinovirus; Streptococcus pneumoniae; tympanometry; virus infection; Acoustic Impedance Tests; Adenoviridae; Bacteria; Child; Child, Preschool; Common Cold; Ear, Middle; Eustachian Tube; Humans; Nasopharynx; Otitis Media; Pressure; Respiratory Syncytial Virus, Human; Reverse Transcriptase Polymerase Chain Reaction; Seasons; Students","Dowell, S.F., March, S.M., Phillips, W.R., Gerber, M.A., Schwartz, B., Otitis media-principles of judicious use of antimicrobial agents (1987) Pediatrics, 101 (SUPPL.), pp. 165-170; Bluestone, C.D., Cantekin, E.I., Beery, Q.C., Effect of inflammation on the ventilatory function of the eustachian tube (1977) Laryngoscope, 87, pp. 493-507; Heikkinen, T., Thint, M., Chonmaitree, T., Prevalence of various respiratory viruses in the middle ear during acute otitis media (1999) N Engl J Med, 340, pp. 260-264; Pitkäranta, A., Virolainen, A., Jero, J., Arruda, E., Hayden, F.G., Detection of rhinovirus, respiratory syncytial virus, and coronavirus infections in acute otitis media by reverse transcriptase polymerase chain reaction (1998) Pediatrics, 102, pp. 291-295; Chonmaitree, T., Viral and bacterial interaction in acute otitis media (2000) Pediatr Infect Dis J, 19, pp. S24-S30; Arola, M., Ruuskanen, O., Ziegler, T., Clinical role of respiratory virus infection in acute otitis media (1990) Pediatrics, 86, pp. 848-855; Chonmaitree, T., Henrickson, K.J., Detection of respiratory viruses in the middle ear fluids of children with acute otitis media by multiplex reverse transcription: Polymerase chain reaction assay (2000) Pediatr Infect Dis J, 19, pp. 258-260; Terkildsen, K., Thomsen, K.A., The influence of pressure variations on the impedance of the human ear drum (1959) J Laryngol Otol, 73, pp. 409-418; Doyle, W.J., McBride, T.P., Swartz, J.D., Hayden, F.G., Gwaltney J.M., Jr., The response of the nasal airway, middle ear, and eustachian tube to experimental rhinovirus infection (1988) Am J Rhinol, 2, pp. 149-154; McBride, T.P., Doyle, W.J., Hayden, F.G., Gwaltney J.M., Jr., Alterations of the eustachian tube, middle ear, and nose in rhinovirus infection (1989) Arch Otolaryngol Head Neck Surg, 115, pp. 1054-1059; Elkhatieb, A., Hipskind, G., Woerner, D., Hayden, F.G., Middle ear abnormalities during natural rhinovirus colds in adults (1993) J Infect Dis, 168, pp. 618-621; Buchman, C.A., Doyle, W.J., Skoner, D., Fireman, P., Gwaltney J.M., Jr., Otologic manifestations of experimental rhinovirus infection (1994) Laryngoscope, 104, pp. 1295-1299; Hayden, F.G., Andries, K., Janssen, P.A., Safety and efficacy of intranasal pirodavir (R77975) in experimental rhinovirus infection (1992) Antimicrob Agent Chemother, 36, pp. 727-732; Tos, M., Poulsen, G., Borch, J., Etiologic factors in secretory otitis (1979) Arch Otolaryngol, 105, pp. 582-588; Sanyal, M.A., Henderson, F.W., Stempel, E.C., Collier, A.M., Denny, F.W., Effect of upper respiratory tract infection on eustachian tube ventilatory function in the preschool child (1980) J Pediatr, 97, pp. 11-15; Moody, S.A., Alper, C.M., Doyle, W.J., Daily tympanometry in children during the cold season: Association of otitis media with upper respiratory tract infections (1998) Int J Pediatr Otorhinolaryngol, 45, pp. 143-150; Jerger, J., Clinical experience with impedance audiometry (1970) Arch Otolaryngol, 92, pp. 311-324; Fillau-Nikolajsen, M., Tympanometry and secretory otitis media (1983) Acta Otolaryngol, 394 (SUPPL.), pp. 1-80; Dudley, S., Ashe, K., Winther, B., Hendley, J.O., Bacterial pathogens of otitis media and sinusitis: Detection in the nasopharynx with selective agar media (2001) J Lab Clin Med, 138, pp. 338-342; Converse G.M. III, Dillon H.C., Jr., Epidemiological studies of Streptococcus pneumoniae in infants: Methods for isolating pneumococci (1977) J Clin Microbiol, 5, pp. 293-296; Chapin, K.C., Doern, G.V., Selective media for recovery of Haemophilus influenzae from specimens contaminated with upper respiratory tract microbial flora (1983) J Clin Microbiol, 17, pp. 1163-1165; Rennie, R., Gordon, T., Yaschuk, T., Tomlin, P., Kibsey, P., Albritton, W., Laboratory and clinical evaluations of media for the primary isolation of Haemophilus species (1992) J Clin Microbiol, 30, pp. 1917-1921; Vaneechoutte, M., Verschraegen, G., Claeys, G., Van den Abeele, A.M., Selective medium for Branhamella catarrhalis with acetazolamide as a specific inhibitor of Neisseria spp. (1988) J Clin Microbiol, 26, pp. 2544-2548; Speeleveld, E., Fossépré, J.-M., Gordts, B., Van Landuyt, H.W., Comparison of three rapid methods, tributyrine, 4-methylumbelliferyl butyrate, and indoxyl acetate, for rapid identification of Moraxella catarrhalis (1994) J Clin Microbiol, 32, pp. 1362-1363; Kaulbach, H.C., White, M.V., Igarashi, Y., Hahn, B.K., Kaliner, M.A., Estimation of nasal epithelial lining fluid using urea as a marker (1993) J Allergy Clin Immunol, 92, pp. 457-465; Forbes, B.A., Hicks, K.E., Substances interfering with direct detection of Mycobacterium tuberculosis in clinical specimens by PCR: Effects of bovine serum albumin (1996) J Clin Microbiol, 34, pp. 2125-2128; Versanen, M., Piiparinen, H., Kallio, A., Vaheri, A., Detection of herpes simplex virus DNA in cerebrospinal fluid samples using the polymerase chain reaction and microplate hybridization (1996) J Virol Methods, 59, pp. 1-11; Fan, J., Henrickson, K.J., Savatski, L.L., Rapid simultaneous diagnosis of infections with respiratory syncytial viruses A and B, influenza viruses A and B, and human parainfluenza virus types 1,2 and 3 by multiplex quantitative reverse transcription-polymerase chain reaction-enzyme hybridization assay (Hexaplex) (1998) Clin Infect Dis, 26, pp. 1397-1402; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings by PCR (1993) Mol Cell Probes, 7, pp. 373-379; Toner, J.G., Mains, B., Pneumatic otoscopy and tympanometry in the detection of middle ear effusion (1990) Clin Otolaryngol, 15, pp. 121-123; Koivunen, P., Albo, O.-P., Uhari, M., Niemela, M., Luotonen, J., Minitympanometry in detecting middle ear fluid (1997) J Pediatr, 131, pp. 419-422; Bluestone, C.D., Pathogenesis of otitis media: Role of eustachian tube (1996) Pediatr Infect Dis J, 15, pp. 281-291; Clements, D.A., Langdon, L., Bland, C., Walter, E., Influenza A vaccine decreases incidence of otitis media in 6- to 30-month old children in day care (1995) Arch Pediatr Adolesc Med, 149, pp. 1113-1117; Heikkinen, T., Ruuskanen, O., Waris, M., Ziegler, T., Arola, M., Halonen, P., Influenza vaccination in the prevention of acute otitis media in children (1991) Am J Dis Child, 145, pp. 445-448; Winther, B., Hayden, F.G., Whitley, R., Oral oseltamivir reduces the risk of developing acute otitis media (AOM) following influenza infection in children (2000) Abstracts of the 40th Annual Meeting of the Interscience Conference on Antimicrobial Agents and Chemotherapy, , September 17-20; Toronto, Ontario, Canada. Abstract 977; Whitley, R.J., Hayden, F.G., Reisinger, K.S., Oral oseltamivir treatment of influenza in children (2001) Pediatr Infect Dis J, 20, pp. 127-133; Eskola, J., Kilpi, T., Palmu, A., Efficacy of a pneumococcal conjugate vaccine against acute otitis media (2001) N Engl J Med, 344, pp. 403-409; Ruohola, A., Heikkinen, T., Waris, M., Puhakka, T., Ruuskanen, O., Intranasal fluticasone propionate does not prevent acute otitis media during viral upper respiratory infection in children (2000) J Allergy Clin Immunol, 106, pp. 467-471","Winther, B.; University of Virginia Health System, Dept. Otolaryngol., Head/Neck Surg., Charlottesville, VA 22906, United States; email: bw8b@virginia.edu",,,00314005,,PEDIA,"11986442","English","Pediatrics",Article,"Final",,Scopus,2-s2.0-0036252426
"Welchman D.B., Bradbury J.M., Cavanagh D., Aebischer N.J.","6701355953;55921969600;26642890500;57200592543;","Infectious agents associated with respiratory disease in pheasants",2002,"Veterinary Record","150","21",,"658","664",,23,"10.1136/vr.150.21.658","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037172195&doi=10.1136%2fvr.150.21.658&partnerID=40&md5=effe44908150c96f8d5865a6546815db","Veterinary Laboratories Agency, Itchen Abbas, Winchester, Hampshire SO21 1BX, United Kingdom; Department of Veterinary Pathology, University of Liverpool, Leahurst, Neston CH64 7TE, United Kingdom; Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; The Game Conservancy Trust, Fordingbridge, Hampshire SP6 1EF, United Kingdom","Welchman, D.B., Veterinary Laboratories Agency, Itchen Abbas, Winchester, Hampshire SO21 1BX, United Kingdom; Bradbury, J.M., Department of Veterinary Pathology, University of Liverpool, Leahurst, Neston CH64 7TE, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom; Aebischer, N.J., The Game Conservancy Trust, Fordingbridge, Hampshire SP6 1EF, United Kingdom","In a case-control study of the infectious agents associated with natural outbreaks of respiratory disease in pheasants, 28 batches of birds from sites affected by disease and eight batches of birds from unaffected sites were examined by six veterinary laboratories in England, Wales and Scotland, and tested for mycoplasmas, other bacteria and viruses. Sinusitis was the commonest sign of disease and was associated with Mycoplasma gallisepticum as detected by PCR in the trachea (P<0.05) and conjunctiva (P<0.01). Sinusitis was also associated with pasteurella cultured from the sinus (P<0.05), antibody to avian pneumovirus (APV) (P<0.01) and avian coronaviruses as detected by reverse-transcriptase PCR (P<0.05); there was no association between disease and APV as detected by PCR. Avian coronaviruses were the most common infectious agents detected. They were genetically close to infectious bronchitis virus (IBV) but differed in their gene sequence from all the serotypes of IBV previously identified in domestic fowl, and serological tests with six known IBV types showed little cross reactivity. Mycoplasma species other than M gallisepticum were cultured in 18 batches of pheasants but, with the exception of Mycoplasma gallinaceum, were not associated with disease.",,"virus antibody; bacterial DNA; virus antigen; article; Avian infectious bronchitis virus; bacterium culture; bacterium detection; case control study; clinical feature; conjunctiva; controlled study; Coronavirus; cross reaction; disease association; domestic animal; epidemic; fowl; gene sequence; laboratory test; Mycoplasma gallisepticum; nonhuman; paranasal sinus; Pasteurella; Pneumovirinae; polymerase chain reaction; respiratory tract disease; reverse transcription polymerase chain reaction; serology; serotype; sinusitis; trachea; United Kingdom; veterinary medicine; virus detection; virus identification; animal; animal disease; bird; bird disease; classification; enzyme linked immunosorbent assay; genetics; isolation and purification; microbiology; Mycoplasma; respiratory tract disease; United Kingdom; virology; Animalia; Aves; Avian infectious bronchitis virus; Avian pneumovirus; Bacteria (microorganisms); Coronavirus; Galliformes; Mycoplasma; Mycoplasma gallinaceum; Mycoplasma gallisepticum; Mycoplasmatales; Pasteurella; Phasianidae; Pneumovirinae; Pneumovirus; Animals; Antigens, Viral; Bird Diseases; Birds; Coronavirus; DNA, Bacterial; Enzyme-Linked Immunosorbent Assay; Great Britain; Mycoplasma; Pasteurella; Pneumovirus; Respiratory Tract Diseases; Reverse Transcriptase Polymerase Chain Reaction","Adzhar, A., Shaw, K., Britton, P., Cavanagh, D., Universal oligonucleotides for the detection of infectious bronchitis virus by the polymerase chain reaction (1996) Avian Pathology, 25, pp. 817-836; Al-Ankari, A.-R., Bradbury, J.M., Naylor, C.J., Worthington, K., Payne-Johnson, C., Jones, R.C., Avian pneumovirus infection in broiler chicks incoculated with Escherichia coli at different time intervals (2001) Avian Pathology, 30, pp. 257-267; Blackall, P.J., Matsumoto, M., Yamamoto, R., Infectious coryza (1997) Diseases of Poultry, pp. 179-190. , 10th edn. Ed B. Calnek. Ames, Iowa State University Press; Bradbury, J.M., Rapid biochemical tests for characterisation of the Mycoplasmales (1977) Journal of Clinical Microbiology, 5, pp. 531-534; Bradbury, J.M., Yavari, C.A., Dare, C.M., Detection of Mycoplasma synoviae in clinically normal pheasants (2001) Veterinary Record, 148, pp. 72-74; Bradbury, J.M., Yavari, C.A., Dare, C.M., Mycoplasmas and respiratory disease in pheasants and partridges (2001) Avian Pathology, 30, pp. 391-396; Bruner, D.W., Angstrom, C.I., Price, J.I., Pasteurella anatipestifer infection in pheasants. A case report (1970) Cornell Veterinarian, 60, pp. 491-494; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Cocirculation of four types of infectious bronchitis virus (793/B, 624/I, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 593-605; Catelli, E., Cook, J.K.A., Cheshire, J., Orbell, S.J., Woods, M.A., Baxendale, W., Huggins, M.B., The use of virus isolation, histopathology and immunoperoxidase techniques to study the dissemination of a chicken isolate of avian pneumovirus in chickens (1998) Avian Pathology, 27, pp. 632-664; Catelli, E., De Marco, M.A., Delogu, M., Terregino, C., Guberti, V., Serological evidence of avian pneumovirus infection in reared and free living pheasants (2001) Veterinary Record, 149, pp. 56-58; Cavanagh, D., A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathology, 30, pp. 109-115; Cavanagh, D., Mawditt, K., Britton, P., Naylor, C.J., Longitudinal field studies of infectious bronchitis virus and avian pneumovirus in broilers using type-specific polymerase chain reactions (1999) Avian Pathology, 28, pp. 593-605; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 365-378; Cavanagh, D., Mawditt, K., Welchman, D., de Britton, P., Gough, R.E., Coronavirus from pheasants (Phasianus colchicus) are genetically closely related to coronaviruses of domestic fowl (infectious bronchitis virus) and turkeys (2002) Avian Pathology, 31, pp. 81-93; Cook, J.K.A., Avian pneumovirus infections of turkeys and chickens (2000) Veterinary Journal, 160, pp. 118-125; Cookson, K.C., Shivaprasad, H.L., Mycoplasma gallisepticum infection in chukar partridges, pheasants and peafowl (1994) Avian Diseases, 39, pp. 914-931; Crawshaw, C.J., Boycott, B.R., Infectious laryngotracheitis in peafowl and pheasants (1982) Avian Diseases, 26, pp. 397-401; Ganapathy, K., Bradbury, J.M., Pathogenicity of Mycoplasma imitans in mixed infection with infectious bronchitis virus in chickens (1999) Avian Pathology, 28, pp. 229-237; Gough, R.E., Collins, M.S., Cox, W.J., Chettle, N.J., Experimental infection of turkeys, chickens, ducks, geese, guinea fowl, pheasants and pigeons with turkey rhinotracheitis virus (1988) Veterinary Record, 123, pp. 58-59; Gough, R.E., Cox, W.J., Alexander, D.J., Examination of sera from gamebirds for antibodies against avian viruses (1990) Veterinary Record, 127, pp. 110-111; Gough, R.E., Cox, W.J., Winkler, C.E., Sharp, M.W., Spackman, D., Isolation and identification of infectious bronchitis virus from pheasants (1996) Veterinary Record, 138, pp. 208-209; Gough, R.E., Drury, S.E., Aldous, E., Laing, P.W., Isolation and identification of avian pneumovirus from pheasants (2001) Veterinary Record, 149, p. 312; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronaviruses (2000) Avian Pathology, 29, pp. 206-212; Kempf, I., DNA amplification methods for diagnosis and epidemiological investigations of avian mycoplasmosis (1998) Avian Pathology, 27, pp. 7-14; Keymer, I.F., A survey and review of the causes of mortality in British birds and the significance of wild birds as disseminators of disease (1958) Veterinary Record, 70, pp. 713-720; Keymer, I.F., Infectious sinusitis of pheasants and partridges (1961) Veterinary Record, 73, pp. 1034-1038; Khehra, R.S., Jones, R.C., Bradbury, J.M., Dual infection of turkey poults with avian pneumovirus and Mycoplasma synoviae (1999) Avian Pathology, 28, pp. 401-404; Lister, S.A., Diseases of gamebirds (1989) In Practice, 11, pp. 170-174; Lister, S.A., Beer, J.V., Gough, R.E., Holmes, R.G., Jones, J.M.W., Olrton, R.G., Outbreaks of nephritis in pheasants (Phasianus colchicus) with a possible coronavirus aetiology (1985) Veterinary Record, 117, pp. 612-613; McCullagh, P., Nelder, J.A., (1989) Generalised Linear Models, , 2nd edn. London, Chapman and Hall; Avian mycoplasmosis (Mycoplasma gallisepticum) (1996) Manual of Standards for Diagnostic Tests and Vaccines, pp. 515-517. , OIE 3rd edn. Paris, Office International des Epizooties; Pennycott, T.W., Causes of mortality and culling in adult pheasants (2000) Veterinary Record, 146, pp. 273-278; Reece, R.L., Ireland, L., Barr, D.A., Infectious sinusitis associated with Mycoplasma gallisepticum in gamebirds (quail, partridge, pheasant) (1986) Australian Veterinary Journal, 63, pp. 163-168; Rimler, R.B., Glisson, J.R., Fowl cholera (1997) Diseases of Poultry, pp. 148-150. , 10th edn. Ed B.W. Calnek, Ames, Iowa State University Press; Rosendal, S., Black, F.T., Direct and indirect immunofluorescence of unfixed and fixed Mycoplasma colonies (1972) Acta Pathologica et Microbiological Scandinavica, 80 B, pp. 615-622; Spackman, D., Cameron, I.R.D., Isolation of infectious bronchitis virus from pheasants (1983) Veterinary Record, 113, pp. 354-355; Van Empel, P.C.M., Hafez, H.M., Ornithobacterium rhinotracheale: A review (1999) Avian Pathology, 28, pp. 217-227","Welchman, D.de.B.; Veterinary Laboratories Agency, Itchen Abbas, Winchester, Hampshire SO21 1BX, United Kingdom",,"British Veterinary Association",00424900,,VETRA,"12054135","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0037172195
"Lewicki D.N., Gallagher T.M.","7006093173;7202310503;","Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors",2002,"Journal of Biological Chemistry","277","22",,"19727","19734",,45,"10.1074/jbc.M201837200","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037205452&doi=10.1074%2fjbc.M201837200&partnerID=40&md5=fcdba492ee8d6846caebe5780fef123b","Department of Microbiology and Immunology, Loyola University, Medical Center, Maywood, IL 60153, United States; Dept. of Microbiology and Immunology, Loyola University, Medical Center, 2160 South First Ave., Maywood, IL 60153, United States","Lewicki, D.N., Department of Microbiology and Immunology, Loyola University, Medical Center, Maywood, IL 60153, United States; Gallagher, T.M., Department of Microbiology and Immunology, Loyola University, Medical Center, Maywood, IL 60153, United States, Dept. of Microbiology and Immunology, Loyola University, Medical Center, 2160 South First Ave., Maywood, IL 60153, United States","Oligomeric spike (S) glycoproteins extend from coronavirus membranes. These integral membrane proteins assemble within the endoplasmic reticulum of infected cells and are subsequently endoproteolyzed in the Golgi, generating noncovalently associated S1 and S2 fragments. Once on the surface of infected cells and virions, peripheral S1 fragments bind carcinoembryonic antigen-related cell adhesion molecule (CEACAM) receptors, and this triggers membrane fusion reactions mediated by integral membrane S2 fragments. We focused on the quaternary structure of S and its interaction with CEACAMs. We discovered that soluble S1 fragments were dimers and that CEACAM binding was entirely dependent on this quaternary structure. However, two differentially tagged CEACAMs could not co-precipitate with the S dimers, suggesting that binding sites were closely juxtaposed in the dimer (steric hindrance) or that a single CEACAM generated global conformational changes that precluded additional interactions (negative cooperativity). CEACAM binding did indeed alter S1 conformations, generating alternative disulfide linkages that were revealed on SDS gels. CEACAM binding also induced separation of S1 and S2. Differentially tagged S2 fragments that were free of S1 dimers were not co-precipitated, suggesting that S1 harbored the primary oligomerization determinants. We discuss the distinctions between the S·CEACAM interaction and other virus-receptor complexes involved in receptor-triggered entry.",,"Cells; Dimers; Oligomers; Proteins; Oligomerization; Biochemistry; carcinoembryonic antigen; cell adhesion molecule; cell receptor; glycoprotein; animal cell; article; binding site; complex formation; conformational transition; Coronavirus; disulfide bond; endoplasmic reticulum; human; human cell; nonhuman; oligomerization; priority journal; protein quaternary structure; rabbit; virus envelope; virus genome; Antigens, CD; Binding Sites; Carcinoembryonic Antigen; Cell Adhesion; Cell Adhesion Molecules; Cell Membrane; Coronavirus; Cross-Linking Reagents; Dimerization; Disulfides; DNA, Complementary; Glycoproteins; Hela Cells; Humans; Mutagenesis, Site-Directed; Mutation; Precipitin Tests; Protein Binding; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Tertiary; Receptors, Virus; Recombinant Fusion Proteins; Ultracentrifugation; Animalia; Coronavirus; Oryctolagus cuniculus","Hernandez, L.D., Hoffman, L.R., Wolfsberg, T.G., White, J.M., (1986) Annu. 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A., 97, pp. 12794-12799; Gallagher, T.M., Parker, S.E., Buchmeier, M.J., (1990) J. Virol., 64, pp. 731-741; Lescar, J., Roussel, A., Wien, M.W., Navaza, J., Fuller, S.D., Wengler, G., Wengler, G., Rey, F.A., (2001) Cell, 105, pp. 137-148; Pletnev, S.V., Zhang, W., Mukhopadhyay, S., Fisher, B.R., Hernandez, R., Brown, D.T., Baker, T.S., Kuhn, R.J., (2001) Cell, 105, pp. 127-136; Singh, M., Berger, B., Kim, P.S., (1999) J. Mol. Biol., 290, pp. 1031-1041; Luo, Z., Weiss, S.R., (1998) Virology, 244, pp. 483-494; Fass, D., Davey, R.A., Hamson, C.A., Kim, P.S., Cunningham, J.M., Berger, J.M., (1997) Science, 277, pp. 1662-1666; Gallaher, W.R., (1996) Cell, 85, pp. 477-478","Gallagher, T.M.; Dept. of Microbiology, Loyola University Medical Center, 2160 South First Ave., Maywood, IL 60153, United States; email: tgallag@lumc.edu",,,00219258,,JBCHA,"11912215","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0037205452
"Ng L.F.P., Liu D.X.","7201477950;8972667300;","Membrane association and dimerization of a cysteine-rich, 16-kilodalton polypeptide released from the C-terminal region of the coronavirus infectious bronchitis virus 1a polyprotein",2002,"Journal of Virology","76","12",,"6257","6267",,26,"10.1128/JVI.76.12.6257-6267.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036107970&doi=10.1128%2fJVI.76.12.6257-6267.2002&partnerID=40&md5=26ff2cd91880c3e5cdf2fb21c72d81c8","School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore","Ng, L.F.P., School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore; Liu, D.X., School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore","More than 10 mature proteins processed from coronavirus gene 1-encoded polyproteins have been identified in virus-infected cells. Here, we report the identification of the most C-terminal cleavage product of the 1a polyprotein as a 16-kDa protein in infectious bronchitis virus-infected Vero cells. Indirect immunofluorescence demonstrated that the protein exhibits a distinct perinuclear punctate staining pattern, suggesting that it is associated with cellular membranes. Positive staining observed on nonpermeabilized cells indicates that the protein may get transported to the cell surface, but no secretion of the protein out of the cells was observed. Treatment of the membrane fraction prepared from cells expressing the 16-kDa protein with Triton X-100, a high pH, and a high concentration of salts showed that the protein may be tightly associated with intracellular membranes. Dual-labeling experiments demonstrated that the 16-kDa protein colocalized with the 5′-bromouridine 5′-triphosphate-labeled viral RNA, suggesting that it may be associated with the viral replication machinery. Sequence comparison of the 16-kDa protein with the equivalent products of other coronaviruses showed multiple conserved cysteine residues, and site-directed mutagenesis studies revealed that these conserved residues may contribute to dimerization of the 16-kDa protein. Furthermore, increased accumulation of the 16-kDa protein upon stimulation with epidermal growth factor was observed, providing preliminary evidence that the protein might be involved in the growth factor signaling pathway.",,"cysteine; epidermal growth factor; polyprotein; triton x 100; virus protein; amino acid sequence; article; carboxy terminal sequence; cell membrane; controlled study; Coronavirus; dimerization; human; human cell; immunofluorescence; nonhuman; pH; priority journal; protein localization; protein processing; protein secretion; protein transport; signal transduction; site directed mutagenesis; virus gene; Amino Acid Sequence; Animals; Base Sequence; Cell Membrane; Cercopithecus aethiops; COS Cells; Cysteine; Dimerization; Epidermal Growth Factor; Infectious bronchitis virus; Molecular Sequence Data; Peptides; Polyproteins; Vero Cells; Viral Proteins","Baker, S.C., Shieh, C.-K., Soe, L.H., Chang, M.-F., Vannier, D.M., Lai, M.M.C., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. 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Chem., 276, pp. 33220-33232","Liu, D.X.; School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore; email: dxliu@ntu.edu.sg",,,0022538X,,JOVIA,"12021359","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036107970
"Banerjee S., Narayanan K., Mizutani T., Makino S.","55851941931;7101933409;56038369800;7403067550;","Murine coronavirus replication-induced p38 mitogen-activated protein kinase activation promotes interleukin-6 production and virus replication in cultured cells",2002,"Journal of Virology","76","12",,"5937","5948",,70,"10.1128/JVI.76.12.5937-5948.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036109516&doi=10.1128%2fJVI.76.12.5937-5948.2002&partnerID=40&md5=c078621c0f642f06cb75119a4542cb64","Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Banerjee, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Narayanan, K., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Mizutani, T., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Makino, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","Analyses of mitogen-activated protein kinases (MAPKs) in a mouse hepatitis virus (MHV)-infected macrophage-derived J774.1 cell line showed activation of two MAPKs, p38 MAPK and c-Jun N-terminal kinase (JNK), but not of extracellular signal-regulated kinase (ERK). Activation of MAPKs was evident by 6 h. postinfection. However, UV-irradiated MHV failed to activate MAPKs, which demonstrated that MHV replication was necessary for their activation. Several other MHV-permissive cell lines also showed activation of both p38 MAPK and JNK, which indicated that the MHV-induced stress-kinase activation was not restricted to any particular cell type. The upstream kinase responsible for activating MHV-induced p38 MAPK was the MAPK kinase 3. Experiments with a specific inhibitor of p38 MAPK, SB 203580, demonstrated that MHV-induced p38 MAPK activation resulted in the accumulation of interleukin-6 (IL-6) mRNAs and an increase in the production of IL-6, regardless of MHV-induced general host protein synthesis inhibition. Furthermore, MHV production was suppressed in SB 203580-treated cells, demonstrating that activated p38 MAPK played a role in MHV replication. The reduced MHV production in SB 203580-treated cells was, at least in part, due to a decrease in virus-specific protein synthesis and virus-specific mRNA accumulation. Interestingly, there was a transient increase in the amount of phosphorylation of the translation initiation factor 4E (eIF4E) in infected cells, and this eIF4E phosphorylation was p38 MAPK dependent; it is known that phosphorylated eIF4E enhances translation rates of cap-containing mRNAs. Furthermore, the upstream kinase responsible for eIF4E phosphorylation, MAPK-interacting kinase 1, was also phosphorylated and activated in response to MHV infection. Our data suggested that host cells, in response to MHV replication, activated p38 MAPK, which subsequently phosphorylated eIF4E to efficiently translate certain host proteins, including IL-6, during virus-induced severe host protein synthesis inhibition. MHV utilized this p38 MAPK-dependent increase in eIF4E phosphorylation to promote virus-specific protein synthesis and subsequent progeny virus production. Enhancement of virus-specific protein synthesis through virus-induced eIF4E activation has not been reported in any other viruses.",,"4 (4 fluorophenyl) 2 (4 methylsulfinylphenyl) 5 (4 pyridyl)imidazole; initiation factor 4E; interleukin 6; messenger RNA; mitogen activated protein kinase; mitogen activated protein kinase inhibitor; stress activated protein kinase; animal cell; article; cell culture; cell line; controlled study; Coronavirus; cytokine production; enzyme activation; enzyme induction; enzyme inhibition; host cell; mouse; nonhuman; priority journal; protein phosphorylation; protein synthesis inhibition; virus replication; Animals; Cell Line; Enzyme Activation; Eukaryotic Initiation Factor-4E; Interleukin-6; JNK Mitogen-Activated Protein Kinases; Macrophages; MAP Kinase Kinase 4; Mice; Mitogen-Activated Protein Kinase Kinases; Mitogen-Activated Protein Kinases; Murine hepatitis virus; p38 Mitogen-Activated Protein Kinases; Peptide Initiation Factors; Phosphorylation; Virus Replication","An, S., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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Virol., 75, pp. 2710-2728","Makino, S.; Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,,0022538X,,JOVIA,"12021326","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036109516
"Schwegmann-Weßels C., Zimmer G., Laude H., Enjuanes L., Herrler G.","6506344309;7102982629;7006652624;7006565392;7006339246;","Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins",2002,"Journal of Virology","76","12",,"6037","6043",,37,"10.1128/JVI.76.12.6037-6043.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036102184&doi=10.1128%2fJVI.76.12.6037-6043.2002&partnerID=40&md5=bc47683518e427ab050deb4b471cad8f","Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany","Schwegmann-Weßels, C., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Zimmer, G., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Laude, H., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Enjuanes, L., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; Herrler, G., Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany","The surface glycoprotein S of transmissible gastroenteritis virus (TGEV) has two binding activities. (i) Binding to porcine aminopeptidase N (pAPN) is essential for the initiation of infection. (ii) Binding to sialic acid residues on glycoproteins is dispensable for the infection of cultured cells but is required for enteropathogenicity. By comparing parental TGEV with mutant viruses deficient in the sialic acid binding activity, we determined the contributions of both binding activities to the attachment of TGEV to cultured cells. In the presence of a functional sialic acid binding activity, the amount of virus bound to two different porcine cell lines was increased sixfold compared to the binding of the mutant viruses. The attachment of parental virus was reduced to levels observed with the mutants when sialic acid containing inhibitors was present or when the cells were pretreated with neuraminidase. In virus overlay binding assays with immobilized cell surface proteins, the mutant virus only recognized pAPN. In addition, the parental virus bound to a high-molecular-mass sialogly-coprotein. The recognition of pAPN was sensitive to reducing conditions and was not dependent on sialic acid residues. On the other hand, binding to the sialic acid residues of the high-molecular-mass glycoprotein was observed regardless of whether the cellular proteins had been separated under reducing or nonreducing conditions. We propose that binding to a surface sialoglycoprotein is required for TGEV as a primary attachment site to initiate infection of intestinal cells. This concept is discussed in the context of other viruses that use two different receptors to infect cells.",,"sialic acid; sialidase; sialoglycoprotein; animal cell; article; binding assay; cell line; cell surface; controlled study; Coronavirus; gastroenteritis; gene mutation; immobilized cell; intestine cell; nonhuman; priority journal; protein binding; transmissible gastroenteritis virus; virus pathogenesis; Animals; Antigens, CD13; Cell Line; Cell Membrane; Membrane Proteins; Receptors, Virus; Sialoglycoproteins; Swine; Transmissible gastroenteritis virus","Ballesteros, M.L., Sánchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Bernard, S., Laude, H., Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity (1995) J. Gen. 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Virol., 63, pp. 52-58; Zimmer, G., Klenk, H.-D., Herrer, G., Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin-Darby canine kidney cell line (1995) J. Biol. Chem., 270, pp. 17815-17822","Herrler, G.; Institut für Virologie, Tierarztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany; email: Georg.Herrler@tiho-hannover.de",,,0022538X,,JOVIA,"12021336","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036102184
"Farsang A., Ros C., Renström L.H.M., Baule C., Soós T., Belák S.","12140724600;7003764949;6505858466;6603434891;56458266000;56053373800;","Molecular epizootiology of infectious bronchitis virus in Sweden indicating the involvement of a vaccine strain",2002,"Avian Pathology","31","3",,"229","236",,84,"10.1080/03079450220136530","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036285374&doi=10.1080%2f03079450220136530&partnerID=40&md5=0eaf6625de9971d299539d0c0756f393","Institute for Veterinary Medicinal Products, Szállás utca 8, H-1107, Budapest, Hungary; Department of Chemistry and Biochemistry, University of Bern, Freistsrasse 3, 3012 Bern, Switzerland; ZLB Bioplasma AG, Bern, Switzerland; Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","Farsang, A., Institute for Veterinary Medicinal Products, Szállás utca 8, H-1107, Budapest, Hungary; Ros, C., Department of Chemistry and Biochemistry, University of Bern, Freistsrasse 3, 3012 Bern, Switzerland, ZLB Bioplasma AG, Bern, Switzerland; Renström, L.H.M., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Baule, C., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; Soós, T., Institute for Veterinary Medicinal Products, Szállás utca 8, H-1107, Budapest, Hungary; Belák, S., Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden","To improve the detection and molecular identification of infectious bronchitis virus (avian coronavirus), two reverse transcriptase-polymerase chain reaction (PCR) assays were developed. As 'diagnostic PCR', a set of consensus nested primers was selected from highly conserved stretches of the nucleocapsid (N) gene. As 'phylogeny' PCR, a fragment of the spike protein gene (S1) was amplified and the PCR products were directly sequenced. To study the phylogenetic relationships of the viruses from various outbreaks, studies of molecular epizootiology were performed in Sweden, a Nordic region, where the occurrence of natural cases of the disease is relatively low and the occasional use of live vaccine(s) is well recorded and monitored. The disease appeared in the region in 1994, associated with production problems among layers of various ages. During outbreaks in 1995 and 1997, both layers and broilers were affected. To reduce losses, a live attenuated vaccine has been applied since 1997. By examining 12 cases between 1994 and 1998, molecular epizootiology revealed that, before 1997, the viruses had gene sequences very similar to strains of the Massachusetts serotype. However, comparative sequence analysis of the S1 gene revealed that the identity was not 100% to any of the strains of this serotype that we analysed. A virus related to the Dutch-type strain, D274, was also identified on one farm. Surprisingly, from 1997, the year that vaccination commenced with a live Massachusetts serotype vaccine, the majority of viruses detected had S1 sequences identical to the live Massachusetts vaccine strain. This genetic relation to the vaccine virus was also confirmed by N gene sequence analysis. The studies of molecular epizootiology reveal a strong probability that the vaccination had lead to the spread of the vaccine virus, causing various disease manifestations and a confusing epizootiological situation in the poultry population.",,"Animals; Base Sequence; Chickens; Coronavirus Infections; Disease Outbreaks; DNA Primers; Infectious bronchitis virus; Membrane Glycoproteins; Molecular Sequence Data; Nucleocapsid; Phylogeny; Poultry Diseases; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Nucleic Acid; Sweden; Vaccines, Attenuated; Viral Envelope Proteins; Viral Vaccines; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; DNA viruses","Ballagi-Pordány, A., Belák, S., The use of mimic as internal standard to avoid false negative results in diagnostic PCR (1996) Molecular and Cellular Probes, 10, pp. 159-164; Ballagi-Pordány, A., Klintevall, K., Merza, M., Klingeborn, B., Belák, S., Direct detection of bovine leukemia virus infection: Practical applicability of a double polymerase chain reaction (1992) Journal of Veterinary Medicine B, 39, pp. 69-77; Belák, S., Ballagi-Pordány, A., Bovine viral diarrhea virus infection: Rapid diagnosis by the polymerase chain reaction (1991) Archives of Virology, 3, pp. 181-190; Belák, S., Ballagi-Pordány, A., Experiences on the applicability of the polymerase chain reaction in a diagnostic laboratory (1993) Molecular and Cellular Probes, 7, pp. 241-248; Boursnell, M.E.G., Brown, T.D.K., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) Journal of General Virology, 68, pp. 57-77; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the matrix/nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 42, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Co-circulation of four types of infectious bronchitis virus (793/B, 624/I, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 587-593; Cavanagh, D., Coronavirus IBV: Further evidence that the surface projections are associated with two glycopeptides (1983) Journal of General Virology, 64, pp. 1787-1791; Cavanagh, D., Coronavirus IBV: Structural characterisation of spike protein (1983) Journal of General Virology, 64, pp. 2577-2583; Cavanagh, D., Commentary. A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathology, 30, pp. 109-115; Cavanagh, D., Technical Review: Innovation and discovery: The application of nucleic acid-based technology to avian virus detection and characterisation (2001) Avian Pathology, 30, pp. 581-598; Cavanagh, D., Davis, P.J., Cook, J.K.A., Li, D., Kant, A., Koch, G., Location of the amino acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious bronchitis virus (1992) Avian Pathology, 21, pp. 33-43; Cavanagh, D., Ellis, M.M., Cook, J.K.A., Relationship between sequence variation in the S1 spike protein of infectious bronchitis virus and the extent of cross-protection in vivo (1997) Avian Pathology, 26, pp. 63-74; Cavanagh, D., Mawditt, K., Britton, P., Naylor, C.J., Longitudinal field studies of infectious bronchitis virus and avian pneumovirus in broilers using type-specific polymerase chain reactions (1999) Avian Pathology, 28, pp. 593-605; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 365-378; Cavanagh, D., Mawditt, K., Welchman, D.D.B., Britton, P., Gough, R.E., Coronaviruses from pheasants (Phasianus colchicus) are genetically closely related to coronaviruses of domestic fowl (infectious bronchitis virus) and turkeys (2002) Avian Pathology, 31, pp. 81-93; Davelaar, E.G., Kouwenhoven, B., Burger, A.G., Occurrence and significance of infectious bronchitis virus variant strains in egg and broiler production in the Netherlands (1984) Veterinary Quarterly, 6, pp. 114-120; De Wit, J.J., Technical Review. 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Comparison with an immunohistochemical technique (1999) Avian Pathology, 28, pp. 327-335; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian bronchitis virus resulting from recombination among three different strains (1995) Archives of Virology, 140, pp. 259-271; King, D.J., Identification of recent infectious bronchitis virus isolates that are serologically different from current vaccine strains (1988) Avian Disease, 32, pp. 362-364; King, D.J., Cavanagh, D., Infectious bronchitis (1991) Diseases of Poultry 9th edn, pp. 471-484. , B.W. Calnek, H.J. Barnes, C.W. Beard, W.M. Reid & H.W. Yoder, Jr. (Eds.). Ames, IA: Iowa State University Press; Kingsham, B.E., Keeler C.L., Jr., Nix, W.A., Landman, B.S., Gelb J., Jr., Identification of avian infectious bronchitis virus by direct automated cycle sequencing of the S-1 gene (2000) Avian Disease, 44, pp. 325-335; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kusters, J.G., Niester, H.G.M., Lenstra, J.A., Horzinek, M.C., Van Der Zeijst, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV (1989) Virology, 169, pp. 217-221; Kwon, H.M., Jackwood, M.W., Gelb J., Jr., Differentiation of infectious bronchitis virus serotype using polymerase chain reaction and restriction fragment length polymorphism analysis (1993) Avian Disease, 37, pp. 194-202; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Lee, C.-W., Jackwood, M.W., Evidence of genetic diversity generated by recombination among avian coronavirus IBV (2000) Archives of Virology, 145, pp. 2135-2148; Lee, C., Jackwood, M.W., Origin and evolution of Georgia 98 (GA98), a new serotype of avian infectious bronchitis virus (2001) Virus Research, 80, pp. 33-39; Li, H., Yang, H., Sequence analysis of nephropathogenic infectious bronchitis virus strains of the Massachusetts genotype in Beijing (2001) Avian Pathology, 30, pp. 535-541; Lin, Z., Kato, A., Kudou, Y., Ueda, S., A new typing method for the avian infectious bronchitis virus using polymerase chain reaction and restriction enzyme fragment length polymorphism (1991) Archives in Virology, 116, pp. 19-31; Meulemans, G., Boschmanns, M., Decaesstecker, M., Van der Berg, T.P., Denis, P., Cavanagh, D., Epidemiology of infectious bronchitis virus in Belgian broilers: A retrospective study, 1986 to 1995 (2001) Avian Pathology, 30, pp. 411-421; Schalk, A.F., Hawn, M.C., An apparently new respiratory disease of chicks (1931) Journal of American Veterinary Medical Association, 78, pp. 413-422; Saif, L.J., Coronavirus immunogens (1993) Veterinary Microbiology, 34, pp. 285-297; Sapats, S.I., Ashton, F., Wright, P.J., Ignjatovic, J., Sequence analysis of the S1 glycoprotein of infectious bronchitis viruses: Identification of a novel genotypic group in Australia (1996) Journal of General Virology, 77, pp. 413-418; Sharma, J.M., Introduction to poultry vaccines and immunity (1999) Advances in Veterinary Medicine, 41, pp. 481-494; Verhofstede, C., Fransen, K., Marissens, D., Verhelst, R., Van der Groen, G., Lauwers, S., Zissis, G., Plum, J., Isolation of HIV-1 RNA from plasma: Evaluation of eight different extraction methods (1996) Journal of Virological Methods, 60, pp. 155-159; Vilcek, S., Elvander, M., Ballagi-Pordány, A., Belák, S., Development of nested PCR assays for detection of bovine respiratory syncytial virus in clinical samples (1994) Journal of Clinical Microbiology, 32, pp. 2225-2231; Wang, L., Junker, D., Hock, L., Ebiary, E., Collison, E.W., Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus (1994) Virus Research, 34, pp. 327-338; Wang, L., Xu, Y., Collisson, E.W., Experimental confirmation of recombination upstream of the S1 hypervariable region of infectious bronchitis virus (1997) Virus Research, 49, pp. 139-145; Williams, A.K., Wang, L., Sneed, L.W., Collison, E.W., Comparative analyses of the nucleocapsid genes of several of infectious bronchitis virus and other coronaviruses (1992) Virus Research, 25, pp. 213-222; Zwaagstra, K.A., Zeijst, B.A.M., Kusters, J.G., Rapid detection and identification of avian infectious bronchitis virus (1992) Journal of Clinical Microbiology, 30, pp. 79-84","Belák, S.; Department of Virology, National Veterinary Institute, Biomedical Center, S-751 23 Uppsala, Sweden; email: sandor.belak@bmc.uu.se",,,03079457,,AVPAD,"12396345","English","Avian Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0036285374
"Elia G., Decaro N., Tinelli A., Martella V., Pratelli A., Buonavoglia C.","7005135633;6701636107;6701370203;7003300496;7004884960;7005623145;","Evaluation of antibody response to Canine coronavirus infection in dogs by Western Blotting analysis",2002,"New Microbiologica","25","3",,"275","280",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036653255&partnerID=40&md5=731ce02bf4b43ee9b0775ef621773afa","Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy","Elia, G., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Decaro, N., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Tinelli, A., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Martella, V., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Pratelli, A., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy; Buonavoglia, C., Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy","We investigated by Western Blotting the antibody responses against the three major structural proteins of Canine coronavirus (CCoV) in dogs naturally infected. A pool of Elisa positive sera were also tested to clearly identify the binding profiles of CCoV proteins. The immune response to S protein was barely detectable in naturally infected dogs, whereas anti-M and anti-N antibodies were detected with a very strong reaction and for a long time post infection. The limited response to S protein may explain the poor protection of dogs and the possibility of persisting infection.","Antibodies; Canine coronavirus; Western Blotting","virus antibody; virus protein; animal; animal disease; article; biosynthesis; blood; Coronavirus; dog; dog disease; gastrointestinal disease; immunology; metabolism; virology; virus infection; Western blotting; Animals; Antibodies, Viral; Blotting, Western; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Gastrointestinal Diseases; Viral Structural Proteins","Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? 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SCIVAC; Daginakatte, G.C., Chard-Bergstrom, C., Andrews, G.A., Kapil, S., Production, Characterization, and Uses of Monoclonal Antibodies against Recombinant Nucleoprotein of Elk Coronavirus (1999) Clinical and Diagnostic Laboratory Immunology, 6, pp. 341-344; Gonon, V., Duquesne, V., Klonjkowski, B., Monteil, M., Aubert, A., Eloit, M., Clearance of infection in cats naturally infected with feline coronaviruses is associated with an anti-S glycoprotein antibody response (1999) Journal of General Virology, 80, pp. 2315-2317; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3' end of canine corona virus genomic RNA (1992) Journal of General Virology, 73, pp. 2849-2862; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) American Journal of Veterinary Research, 37, pp. 247-256; Naylor, M.J., Harrison, G.A., Monckton, R.P., Mcorist, S., Lehrbach, P.R., Deane, E.M., Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterization of a new Australian isolate (2001) Journal of Clinical Microbiology, 39, pp. 1036-1041; Pedersen, N.C., Evermann, J.F., Mckeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) American Journal of Veterinary Research, 45, pp. 2580-2585; Pollock, R.V.H., Carmichael, L.E., Canine Viral Enteritis (1990) Infectious Disease of the Dog and Cat. First Edition, , Greene, W.B. Saunders Company; Pratelli, A., Martella, V., Elia, G., Tempesta, M., Guarda, F., Capucchio, M.T., Carmichael, L.E., Buonavoglia, C., Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus (2001) Journal of Veterinary Medicine B, 48, pp. 385-392; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Molecular and Cellular Probes, 15, pp. 229-233; Pratelli, A., Elia, G., Martella, V., Palmieri, A., Cirone, F., Tinecli, A., Corrente, M., Buonavoglia, C., Prevalence of canine coronavirus antibodies by an enzyme-linked immunosorbent assay in dogs in the south of Italy (2002) Journal of Virological Methods, 102, pp. 67-71; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein e (2000) Journal of Virology, 74, pp. 2333-2342; Ricard, C., Koetzner, C.A., Sturman, L.S., Masters, P.S., A conditional-lethal murine coronavirus mutant that fails to incorporate the spike glycoprotein into assembled virions (1995) Virus Research, 39, pp. 261-276; Rottier, P.J.M., The molecular dynamics of feline coronaviruses (1999) Veterinary Microbiology, 69, pp. 117-125; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M.J., Gebaues, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The Coronaviridae: An introduction (1995) Coronaviridae, pp. 1-9. , S.G. Siddell (ed.), Plenum Press, New York, N.Y; Siddell, S.G., Wege, H., Meulen, V., The biology of coronaviruses (1983) Journal of General Virology, 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2952; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Research, 61, pp. 145-152; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) Journal of General Virology, 75, pp. 1789-1794; Woods, R.D., Wesley, R., Kapke, P.A., Complement-dependent neutralization of transmissible gastroenteritis virus by monoclonal antibodies (1987) Advances in Experimental Medicine and Biology, 218, pp. 493-500; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Elia, G.; Dept. of Hlth. and Animal Well-being, Faculty of Veterinary Medicine, 70010 Valenzano, Bari, Italy",,,11217138,,,"12173767","English","New Microbiol.",Review,"Final",,Scopus,2-s2.0-0036653255
"Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., Hilgenfeld R.","56371191700;7004321586;6601999548;7005260816;7003783935;7006843618;","Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain",2002,"EMBO Journal","21","13",,"3213","3224",,211,"10.1093/emboj/cdf327","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036646055&doi=10.1093%2femboj%2fcdf327&partnerID=40&md5=1e1a70b75cd793ce9598d6dd2277d401","Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany","Anand, K., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Palm, G.J., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Mesters, J.R., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Siddell, S.G., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Ziebuhr, J., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Hilgenfeld, R., Department of Structural Biology, Institute of Molecular Biotechnology, D-07745 Jena, Germany","The key enzyme in coronavirus polyprotein processing is the viral main proteinase, Mpro, a protein with extremely low sequence similarity to other viral and cellular proteinases. Here, the crystal structure of the 33.1 kDa transmissible gastroenteritis (corona)virus Mpro is reported. The structure was refined to 1.96 Å resolution and revealed three dimers in the asymmetric unit. The mutual arrangement of the protomers in each of the dimers suggests that Mpro self-processing occurs in trans. The active site, comprised of Cys144 and His41, is part of a chymotrypsin-like fold that is connected by a 16 residue loop to an extra domain featuring a novel α-helical fold. Molecular modelling and mutagenesis data implicate the loop in substrate binding and elucidate S1 and S2 subsites suitable to accommodate the side chains of the P1 glutamine and P2 leucine residues of Mpro substrates. Interactions involving the N-terminus and the α-helical domain stabilize the loop in the orientation required for trans-cleavage activity. The study illustrates that RNA viruses have evolved unprecedented variations of the classical chymotrypsin fold.","3C-like; Catalytic dyad; Coronavirus; Proteinase; X-ray crystallography","chymotrypsin; cysteine; glutamine; histidine; leucine; proteinase; unclassified drug; viral main proteinase; virus enzyme; article; Coronavirus; crystal structure; dimerization; enzyme active site; enzyme structure; enzyme substrate; gastroenteritis; molecular model; molecular stability; mutagenesis; nonhuman; nucleotide sequence; optical resolution; priority journal; protein domain; protein folding; protein interaction; protein processing; sequence homology; virus morphology; Amino Acid Sequence; Binding Sites; Chymotrypsin; Crystallography, X-Ray; Cysteine Endopeptidases; Dimerization; Models, Molecular; Molecular Sequence Data; Mutagenesis; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Transmissible gastroenteritis virus; Coronavirus; RNA viruses; Transmissible gastroenteritis virus","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N., Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature, 369, pp. 72-76; Andino, R., Rieckhof, G.E., Achacoso, P.L., Baltimore, D., Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA (1993) EMBO J, 12, pp. 3587-3598; Bacon, D.J., Anderson, W.F., A fast algorithm for rendering space-filling molecule pictures (1988) J. 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D, 50, pp. 760-763; Cowtan, K.D., Main, P., Phase combination and cross validation in iterated density-modification calculations (1996) Acta Crystallogr. D, 52, pp. 43-48; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A., Horzinek, M.C., Spaan, W.J., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol, 65, pp. 2910-2920; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Enjuanes, L., Van der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis virus epidemiology (1995) The Coronaviridae, pp. 337-376. , Siddell, S.G. (ed.). Plenum Press, New York, NY; Fujinaga, M., Delbaere, L.T.J., Brayer, G.D., James, M.N.G., Refined structure of α-lytic protease at 1.7 Å resolution (1985) J. Mol. 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"Loa C.C., Lin T.L., Wu C.C., Bryan T.A., Thacker H.L., Hooper T., Schrader D.","6602648721;57213499631;7501664098;7005517787;7007150767;7005121335;7007179253;","Purification of turkey coronavirus by Sephacryl size-exclusion chromatography",2002,"Journal of Virological Methods","104","2",,"187","194",,18,"10.1016/S0166-0934(02)00069-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036089835&doi=10.1016%2fS0166-0934%2802%2900069-1&partnerID=40&md5=67360a647d39ab647cded7fff0e3e584","Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Loa, C.C., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Lin, T.L., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T.A., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Thacker, H.L., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Sephacryl S-1000 size-exclusion chromatography was used to purify turkey coronavirus (TCoV) from infected turkey embryo. TCoV was propagated in the 22-day-old turkey embryos. Intestines and intestinal contents of infected embryos were harvested and homogenized. After low speed centrifugation, the supernatant was concentrated by ultracentrifugation through a cushion of 30 or 60% sucrose solution, or by ammonium sulfate precipitation. The purification methods included sucrose gradient and Sephacryl S-1000 size-exclusion chromatography. Ultracentrifugation through a cushion of 60% sucrose solution was better than the other two methods for concentration of TCoV from intestinal homogenate. The most effective method for purifying TCoV and removing extraneous materials was size-exclusion chromatography as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. More spike-rich particles were observed in the sample purified by chromatography than those purified by sucrose gradient as examined by electron microscopy. Differentiation of turkey anti-TCoV antiserum from normal turkey serum was better achieved by ELISA plates coated with TCoV preparation purified by size-exclusion chromatography than that purified by sucrose density gradient. The results indicated that Sephacryl S-1000 chromatography was useful for purification of TCoV. © 2002 Elsevier Science B.V. All rights reserved.","Turkey coronavirus; Virus propagation; Virus purification","ammonium sulfate; sucrose; animal model; animal tissue; article; controlled study; Coronavirus; electron microscopy; embryo; enzyme linked immunosorbent assay; gel permeation chromatography; immunoblotting; intermethod comparison; intestine; nonhuman; polyacrylamide gel electrophoresis; precipitation; priority journal; sucrose density gradient centrifugation; turkey (bird); ultracentrifugation; virus infection; virus purification; Animals; Antigens, Viral; Centrifugation, Density Gradient; Chromatography, Gel; Coronavirus, Turkey; Embryo, Nonmammalian; Enteritis, Transmissible, of Turkeys; Hemagglutination Tests; Intestines; Turkeys; Ultracentrifugation; Coronavirus; Turkey coronavirus","Adams, N.R., Hofstad, M.S., Isolation of transmissible enteritis agent of turkeys in avian embryos (1971) Avian Dis., 15, pp. 426-433; Ali, A., Reynolds, D.L., The in vitro propagation of stunting syndrome agent (1998) Avian Dis., 42, pp. 657-666; Caul, E.O., Ashley, C.R., Egglestone, S.I., An improved method for the routine identification of faecal viruses using ammonium sulphate precipitation (1978) FEMS Microbio. Lett., 4, pp. 1-4; Dea, S., Marsolais, G., Beaubien, J., Ruppanner, R., Coronaviruses associated with outbreaks of transmissible enteritis of turkeys in Quebec: Hemagglutination properties and cell cultivation (1985) Avian Dis., 30, pp. 319-326; Dea, S., Tijssen, P., Identification of the structural proteins of turkey enteric coronavirus (1988) Arch. Virol., 99, pp. 173-186; Dea, S., Tijssen, P., Isolation and trypsin-enhanced propagation of turkey enteric (bluecomb) coronaviruses in a continuous human rectal adenocarcinoma cell line (1989) Am. J. Vet. Res., 50, pp. 1310-1318; Deshmukh, D.R., Larsen, C.T., Pomeroy, B.S., Survival of bluecomb agent in embryonating turkey eggs and cell cultures (1973) Am. J. Vet. Res., 34, pp. 673-675; Deshmukh, D.R., Pomeroy, B.S., Physicochemical characterization of a bluecomb coronavirus of turkeys (1974) Am. J. Vet. Res., 35, pp. 1549-1552; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hofstad, M.S., Adams, N., Frey, M.L., Studies on a filtrable agent associated with infectious enteritis (bluecomb) of turkeys (1969) Avian Dis., 13, pp. 386-393; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lowry, O.H., Rosenbough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275; Nagano, H., Yagyu, K., Ohta, S., Purification of infectious bronchitis coronavirus by Sephacryl S-1000 gel chromatography (1989) Vet. Microbio., 21, pp. 115-123; Naqi, S.A., Panigraphy, B., Hall, C.F., Purification and concentration of viruses associated with transmissible (coronaviral) enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 548-552; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 1265-1267; Saif, L.J., Coronavirus immunogens (1993) Vet. Microbiol., 37, pp. 285-297; Tompkins, W.A.F., Watrach, A.M., Schmale, J.D., Schulta, R.M., Harris, J.A., Cultural and antigenic properties of newly established cell strains derived from adenocarcinomas of the human colon and rectum (1974) J. Natl. Cancer Inst., 52, pp. 1101-1106","Lin, T.L.; Dept. of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; email: tlin@addl.purdue.edu",,,01660934,,JVMED,"12088828","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0036089835
"Van Reeth K., Van Gucht S., Pensaert M.","57191565576;6603007124;55905425400;","In vivo studies on cytokine involvement during acute viral respiratory disease of swine: Troublesome but rewarding",2002,"Veterinary Immunology and Immunopathology","87","3-4",,"161","168",,73,"10.1016/S0165-2427(02)00047-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036088568&doi=10.1016%2fS0165-2427%2802%2900047-8&partnerID=40&md5=7c36171b538cd95aacb192ef36a30ea1","Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium","Van Reeth, K., Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium; Van Gucht, S., Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium; Pensaert, M., Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium","The early cytokines interferon-α (IFN-α), tumour necrosis factor-α (TNF-α), interleukin-1, -6 and -8 (IL-1, -6, -8) are produced during the most early stage of an infection. The activities of these cytokines have been studied extensively in vitro and in rodents, but in vivo studies on the role of these cytokines in infectious diseases of food animals are few. This review concentrates on in vivo studies of cytokine involvement in infectious respiratory diseases of swine, with an emphasis on viral infections. First evidence for the role of early cytokines in pneumonia in swine came from experimental infections with Mycoplasma hyopneumoniae and Actinobacillus pleuropneumoniae. The role of TNF-α and IL-1 in the symptoms and pathology of porcine pleuropneumonia has recently been proven by use of an adenovirus vector expressing the anti-inflammatory IL-10. In the authors' laboratory, studies were undertaken to investigate the relationship between viral respiratory disease and bioactive lung lavage levels of IFN-α, TNF-α, IL-1 and IL-6. Out of three respiratory viruses - porcine respiratory coronavirus (PRCV), porcine reproductive and respiratory syndrome virus (PRRSV) and swine influenza virus (SIV) - only SIV induced acute respiratory disease and severe lung damage by itself. Disease and lung pathology were tightly associated with the simultaneous production of IFN-α, TNF-α, IL-1 and IL-6. In challenge studies of SIV-vaccinated pigs, levels of IFN-α, TNF-α and IL-6, but not IL-1 were correlated with clinical and virological protection. Multifactorial respiratory disease was reproduced by combined inoculations with PRCV or PRRSV followed by LPS from Escherichia coli. In comparison with the respective single inoculations, which were subclinical, there was a true potentiation of disease and production of TNF-α, IL-1 and IL-6. TNF-α and IL-6 were best correlated with disease. In further studies, we will use more specific strategies to dissect the role of cytokines during viral infections. © 2002 Elsevier Science B.V. All rights reserved.","Early cytokines; Pathogenesis; Swine; Viral respiratory disease","adenovirus vector; alpha interferon; cytokine; interleukin 1; interleukin 10; interleukin 6; interleukin 8; tumor necrosis factor alpha; Actinobacillus pleuropneumoniae; Arterivirus; conference paper; Coronavirus; cytokine production; disease association; disease severity; immunopathology; in vitro study; inoculation; livestock; lung injury; lung lavage; Mycoplasma hyopneumoniae; nonhuman; pneumonia; protection; provocation test; respiratory tract infection; swine disease; Swine influenza virus; symptom; virus infection; Acute Disease; Animals; Coronavirus Infections; Cytokines; Influenza A virus; Lipopolysaccharides; Lung; Lung Diseases; Orthomyxoviridae Infections; Pneumonia of Swine, Mycoplasmal; Pneumonia, Bacterial; Porcine Reproductive and Respiratory Syndrome; Swine; Swine Diseases; Actinobacillus; Actinobacillus pleuropneumoniae; Adenoviridae; Animalia; Coronavirus; Escherichia coli; Influenza virus; Mycoplasma; Mycoplasma hyopneumoniae; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Rodentia; Simian immunodeficiency virus; Suidae; Sus scrofa; Swine influenza virus","Albina, E., Carrat, C., Charley, B., Interferon-alpha response to swine arterivirus (PoAV), the porcine reproductive and respiratory syndrome virus (1998) J. Interf. Cytok. Res., 18, pp. 485-490; Asai, T., Okada, M., Ono, M., Irisawa, T., Mori, Y., Yokomizo, Y., Sato, S., Increased levels of tumor necrosis factor and interleukin-1 in bronchoalveolar lavage fluids from pigs infected with Mycoplasma hyopneumoniae (1993) Vet. Immunol. Immunopathol., 38, pp. 253-260; Asai, T., Okada, M., Ono, M., Mori, Y., Yokomizo, Y., Sato, S., Detection of interleukin-6 and prostaglandin E2 in bronchoalveolar lavage fluids of pigs experimentally infected with Mycoplasma hyopneumoniae (1994) Vet. Immunol. Immunopathol., 44, pp. 97-102; Baarsch, M.J., Scamurra, R.W., Burger, K., Foss, D.L., Maheswaran, S.K., Murtaugh, M.P., Inflammatory cytokine expression in swine experimentally infected with Actinobacillus pleuropneumoniae (1995) Infect. Immun., 63, pp. 3587-3594; Baarsch, M.J., Foss, D.L., Murtaugh, M.P., Pathophysiologic correlates of acute porcine pleuropneumonia (2000) Am. J. Vet. Res., 61, pp. 684-690; Bogdan, C., The function of type I interferons in antimicrobial immunity (2000) Curr. Opin. Immunol., 12, pp. 419-424; Choi, C., Kwon, D., Min, K., Chae, C., In situ hybridization for the detection of inflammatory cytokines (IL-1, TNF-α and IL-6) in pigs naturally infected with Actinobacillus pleuropneumoniae (1999) J. Comp. Pathol., 121, pp. 349-356; Dinarello, C.A., Proinflammatory cytokines (2000) Chest, 118, pp. 503-508; Fossum, C., Wattrang, E., Fuxler, L., Jensen, K.T., Wallgren, P., Evaluation of various cytokines (IL-6, IFN-α, IFN-γ, TNF-α) as markers for acute bacterial infection in swine - A possible role for serum interleukin-6 (1998) Vet. Immunol. Immunopathol., 64, pp. 161-172; Harding, J.C., Baarsch, M.J., Murtaugh, M.P., Association of tumour necrosis factor and acute phase reactant changes with post-arrival disease in swine (1997) J. Vet. Med. B, 44, pp. 405-413; Hayden, F.G., Fritz, R.S., Lobo, M.C., Alvord, W.G., Strober, W., Straus, S.E., Local and systemic cytokine responses during experimental human influenza A virus infection (1998) J. Clin. Invest., 101, pp. 643-649; Huang, H., Potter, A.A., Campos, M., Leighton, F.A., Willson, P.J., Haines, D.M., Yates, W.D.G., Pathogenesis of porcine Actinobacillus pleuropneumonia. Part II. Roles of proinflammatory cytokines (1999) Can. J. Vet. Res., 63, pp. 69-78; Kips, J.C., Tavernier, J., Pauwels, R.A., Tumor necrosis factor causes bronchial hyperresponsiveness in rats (1992) Am. Rev. Resp. Dis., 145, pp. 332-336; Lentsch, A.B., Ward, P.A., Regulation of experimental lung inflammation (2001) Resp. Physiol., 128, pp. 17-22; Morrison, D.F., Foss, D.L., Murtaugh, M.P., Interleukin-10 gene therapy-mediated amelioration of bacterial pneumonia (2000) Infect. Immun., 68, pp. 4752-4758; Murtaugh, M.P., Baarsch, M.J., Zhou, Y., Scamurra, R.W., Lin, G., Inflammatory cytokines in animal health and disease (1996) Vet. Immunol. Immunopathol., 54, pp. 45-55; Nelson, S., Bagby, G.J., Bainton, B.G., Wilson, N.A., Thompson, J.J., Summer, W.R., Compartmentalization of intraalveolar and systemic lipopolysaccharide-induced tumor necrosis factor and the pulmonary inflammatory response (1989) J. Infect. Dis., 159, pp. 189-194; Neuner, P., Klosner, G., Schauer, E., Pourmojib, M., Macheiner, W., Grunwald, C., Knobler, R., Schwarz, T., Pentoxyfylline in vivo down-regulates the release of IL-1 beta, IL-6, IL-8 and tumour necrosis factor-alpha by human peripheral blood mononuclear cells (1994) Immunology, 83, pp. 262-267; Strieter, R.M., Kunkel, S.L., Acute lung injury: The role of cytokines in the elicitation of neutrophils (1994) J. Invest. Med., 42, pp. 640-651; Thorn, J., The inflammatory response in humans after inhalation of bacterial endotoxin: A review (2001) Inflamm. Res., 50, pp. 254-261; Van Reeth, K., Nauwynck, H., Proinflammatory cytokines and viral respiratory disease in pigs (2000) Vet. Res., 31, pp. 187-213; Van Reeth, K., Labarque, G., Nauwynck, H., Pensaert, M., Differential production of proinflammatory cytokines in the pig lung during different respiratory virus infections: Correlations with pathogenicity (1999) Res. Vet. Sci., 67, pp. 47-52; Van Reeth, K., Nauwynck, H., Pensaert, M., A potential role for tumour necrosis factor-α in synergy between porcine respiratory coronavirus and bacterial lipopolysaccharide in the induction of respiratory disease in pigs (2000) J. Med. Microbiol., 49, pp. 613-620; Van Reeth, K., Labarque, G., De Clercq, S., Pensaert, M., Efficacy of vaccination of pigs with different H1N1 swine influenza viruses using a recent challenge strain and different parameters of protection (2001) Vaccine, 19, pp. 4479-4486","Van Reeth, K.; Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium; email: kristien.vanreeth@rug.ac.be",,,01652427,,VIIMD,"12072230","English","Vet. Immunol. Immunopathol.",Conference Paper,"Final",,Scopus,2-s2.0-0036088568
"Banja B.K., Sahoo N., Das P.K., Ray S.K.","57213393903;57211708587;55573941800;16744099700;","Clinico-therapeutic apsects of gastro-enteritis in dogs",2002,"Indian Veterinary Journal","79","8",,"837","840",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036692521&partnerID=40&md5=7662e6fd014502cda408f357614df0c8","Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India","Banja, B.K., Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India; Sahoo, N., Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India; Das, P.K., Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India; Ray, S.K., Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India","Haemorrhagic diarrhoea and vomition were the important dinical manifestations of CPV infection. Vomition and diarrhoea were seen in majority of dogs suffering from coronavirus infection. Other clinical signs noticed in the single or mixed infection were inappetance, haematemesis, fever and dehydration. Clinical signs of mixed infection were indistinguishable from that of single infection and the duration of illness was prolonged in the later. The symptomatic treatment with intravenous administration of ringer's lactate solution of dextrose normal saline @ 45-90 ml/kg b.w., metoclopramide @ 1.0 mg/kg b.w., adrenochrome monosemicarbazone @ 0.1 -0.2 mg/kg b.w. and gentamycin @ 4.0 mg/kg b.w. saved 90.1 (171/46), 100 (171/11) and 80.9(171/34) dogs suffering from CPV (Single), CCV (Single) and CPV and CCV (Mixed) infections within five days of therapy respectively.",,"carbazochrome; gentamicin; glucose; metoclopramide; Ringer lactate solution; sodium chloride; animal experiment; appetite disorder; article; bleeding; canine parvovirus; clinical feature; controlled study; dehydration; diarrhea; dog; dose calculation; fever; gastroenteritis; hematemesis; mixed infection; nonhuman; Parvovirus; virus infection; vomiting","Appel, M.J.G., Cooper, B.J., Greisen, H., Carmichael, L.E., (1978) J. Am. Vet. Med. Assoc., 173, p. 1516; Binn, L.N., Marchwicki, R.H., Eckermann, E.H., Fritz, T.E., (1981) Amer. Vet. Res., 42, p. 1665; Black, J.W., Holscher, M.A., Powell, H.S., Byerly, C.S., (1979) Vet. Med. Small Anim. Clinician, 74, p. 47; Brander, G.C., Pugh, D.M., Bywater, R.J., Jenkins, W.L., (1991) Veterinary Applied Pharmacology and Therapeutics, , The English language Book Society and Bailliera Tindall, London; Ettinger, S.J., Feldman, E.C., (1995) Text book of Veterinary internal Medicine: Diseases of the dog and cat, 4th end., , W.B. Saunders Company, London; Eugster, A.K., Bendele, R.A., Jones, L.P., (1978) J. Am. Vet. Med. Assoc., 173, p. 1340; Glickman, L.T., Domanski, L.M., Patronek, G.J., Vinsintainer, F., (1985) J. Am. Vet. Med. Assoc., 187, p. 589; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., (1976) Amer., J. Vet. Res., 37, p. 247; Mohan, R., Nauriyal, D.C., Singh, K.B., Mangat, A.P.S., Singh, G.K., (1992) Indian J. Vet. Med., 12, p. 1; Rai, A., Nauriyal, D.C., Mohan, R., (1993) Indian Vet. Med., 13, p. 99; Ramadass, P., Meerarani, S., Viswanathan, S., Padmanaban, V.D., Nachimuthu, K., (1996) Indian Vet. J., 73, p. 1214; Sabine, M., Herbert, L., Love, D.N., (1982) Vet. Rec., 110, p. 551; Stann, S.F., Digiacomo, R.F., Giddens W.E., Jr., Evermann, J.F., (1984) J. Am. Vet. Med. Assoc., 185, p. 651; Tingapaloapong, M., Whitmire, R.E., Watts, D.M., Burke, D.S., Binn, L.N., Tesaprateep, T., Laungtongkum, S., Marchwicki, R.H., (1982) Am. J. Vet. Res., 43, p. 1687","Banja, B.K.; Technical Officer, Centr. Inst. of Freshw. Aquaculture, Kausalyagange, Bhubaneswar, India",,,00196479,,,,"English","Indian Vet. J.",Article,"Final",,Scopus,2-s2.0-0036692521
"Lin X.-Q., O'Reilly K.L., Storz J.","36768282000;7103313844;7006694594;","Antibody responses of cattle with respiratory coronavirus infections during pathogenesis of shipping fever pneumonia are lower with antigens of enteric strains than with those of a respiratory strain",2002,"Clinical and Diagnostic Laboratory Immunology","9","5",,"1010","1013",,7,"10.1128/CDLI.9.5.1010-1013.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036731907&doi=10.1128%2fCDLI.9.5.1010-1013.2002&partnerID=40&md5=99548b05342962d0915fe6fe736b0983","Dept. of Pathobiological Sciences, Louisiana State University, School of Veterinary Medicine, Baton Rouge, LA 70803, United States","Lin, X.-Q., Dept. of Pathobiological Sciences, Louisiana State University, School of Veterinary Medicine, Baton Rouge, LA 70803, United States; O'Reilly, K.L., Dept. of Pathobiological Sciences, Louisiana State University, School of Veterinary Medicine, Baton Rouge, LA 70803, United States; Storz, J., Dept. of Pathobiological Sciences, Louisiana State University, School of Veterinary Medicine, Baton Rouge, LA 70803, United States","The serum antibody responses of cattle with respiratory coronavirus infections during the pathogenesis of shipping fever pneumonia were analyzed with different bovine coronavirus antigens, including those from a wild-type respiratory bovine coronavirus (RBCV) strain (97TXSF-Lu 15-2) directly isolated from lung tissue from a fatally infected bovine, a wild-type enteropathogenic bovine coronavirus (EBCV) strain (Ly 138-3), and the highly cell culture-adapted, enteric prototype strain (EBCV L9-81). Infectivity-neutralizing (IN) and hemagglutinin-inhibiting (HAI) activities were tested. Sequential serum samples, collected during the onset of the respiratory coronavirus infection and at weekly intervals for 5 weeks thereafter, had significantly higher IN and HAI titers for antigens of RBCV strain 97TXSF-Lu15-2 than for the wild-type and the highly cell culture-adapted EBCV strains, with P values ranging from <0.0001 to 0.0483. The IN and HAI antibody responses against the two EBCV strains did not differ significantly, but the lowest titers were detected with EBCV strain L9-81.",,"neutralizing antibody; virus antigen; adolescent; antibody response; antibody titer; article; cattle; cattle disease; controlled study; Coronavirus; hemagglutination inhibition; hemagglutination inhibition test; human; human cell; nonhuman; pathogenesis; priority journal; virus neutralization; virus strain; Animals; Antibodies, Viral; Antigens, Viral; Cattle; Coronavirus Infections; Coronavirus, Bovine; Intestines; Lung; Neutralization Tests; Pasteurellosis, Pneumonic; Serotyping","Cavanagh, D., Naqui, S.A., Infectious bronchitis (1997) Diseases of poultry, 10th ed., pp. 511-521. , B. W. Calnek (ed.). Iowa State University Press, Ames, Iowa; Chouljenko, V.N., Kousoulas, K.G., Lin, X.Q., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic portion (9.5kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Chouljenko, V.N., Lin, X.Q., Storz, J., Kousoulas, K.G., Gorbalenya, A.E., Comparison of genomic and predicted amino acid sequences of respiratory and enteric bovine coronaviruses isolated from the same animal with fatal shipping fever pneumonia (2001) J. Gen. Virol., 82, pp. 2927-2933; Dea, S., Michaud, L., Milane, G., Comparison of bovine coronavirus isolates associated with neonatal calf diarrhea and winter dysentery in adult dairy cattle in Québec (1995) J. Gen. Virol., 76, pp. 1263-1270; Deregt, D., Gifford, G.A., Ijaz, M.K., Watts, T.C., Gilchrist, J.E., Haines, D.M., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo virus-neutralizing activity (1989) J. Gen. Virol., 70, pp. 993-998; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Doughri, A.M., Storz, J., Hajer, I., Fernando, H.S., Morphology and morphogenesis of a coronavirus infecting intestinal epithelial cells of newborn calves (1976) Exp. Mol. Pathol., 25, pp. 355-370; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 183, pp. 442-445; Kusters, J.G., Niesters, H.G.M., Leustra, J.A., Horzinek, M.C., Van der Zeist, B.A.M., Phylogeny of antigenic variants of avian coronavirus IBV Virology, 192, pp. 217-221; Lin, X., O'Reilly, K.L., Burrell, M.L., Storz, J., Infectivity-neutralizing and hemagglutinin-inhibiting antibody responses of respiratory coronavirus infections of cattle in pathogenesis of shipping fever pneumonia (2000) Clin. Diagn. Lab. Immunol., 8, pp. 357-362; Lin, X.Q., Chouljenko, V.N., Kousoulas, K.G., Storz, J., Temperature-sensitive acetylesterase activity of haemagglutinin-esterase specified by respiratory bovine coronaviruses (2000) J. Med. Microbiol., 49, pp. 1119-1127; Lin, X.Q., O'Reilly, K.L., Storz, J., Purdy, C.W., Loan, R.W., Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis (2000) Arch. Virol., 145, pp. 520-532; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a corona-like agent (1973) Am. J. Vet. Res., 34, pp. 145-150; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the feces (1988) Vet. Rec., 123, pp. 300-301; Schultze, B., Herrler, G., Bovine coronavirus uses N-acetyl-9-O-acetyl- neuraminic acid as a receptor determinant to initiate the infection of cultured cells (1992) J. Gen. Virol., 74, pp. 901-906; Schultze, B., Gross, H.-J., Brossmer, R., Herrier, G., The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant (1991) J. Virol., 65, pp. 6232-6237; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine corona-virus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Storz, J., Lin, X., Purdy, C.W., Chouljenko, V.N., Kousoulas, K.G., Enright, F.M., Gilmore, W.C., Loan, R.W., Coronavirus and Pasteurella infections in bovine shipping fever pneumonia and Evans' criteria for causation (2000) J. Clin. Microbiol., 38, pp. 3291-3298; Storz, J., Purdy, C.W., Lin, X.Q., Burrell, M., Truax, R.E., Briggs, R.E., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J. Am. Vet. Med. Assoc., 216, pp. 1599-1604; Storz, J., Zhang, X.M., Rott, R., Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains (1992) Arch. Virol., 125, pp. 193-204; Storz, J., Herrler, G., Snodgrass, D.R., Hussain, K.A., Zhang, X.M., Clark, M.A., Rott, R., Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine corona-virus (1991) J. Gen. Virol., 72, pp. 2817-2820; Storz, J., Rott, R., Reactivity of antibodies in human serum with antigens of an enteropathogenic bovine coronavirus (1981) Med. Microbiol. Immunol., 169, pp. 169-178; Storz, J., Rott, R., Kaluza, G., Enhancement of plaque formation and cell fusion of an enteropathogenic coronavirus by trypsin treatment (1981) Infect. Immun., 31, pp. 1214-1222; Storz, J., Rott, R., Über die verbreitung der coronavirusinfektion bei rindern in ausgewählten gebieten Deutschlands: Antikörpernachweis durch mikroimmundiffusion und neutralisation (1980) Dtsch. Tierärztl. Wochenschr., 87, pp. 252-254; Zhang, X.M., Kousoulas, K.G., Storz, J., The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and function comparison between virulent and avirulent strains (1991) Virology, 185, pp. 847-852","O'Reilly, K.L.; Dept. of Pathobiological Sciences, Louisiana State University, School of Veterinary Medicine, Baton Rouge, LA 70803, United States; email: koreilly@lsu.edu",,,1071412X,,CDIME,"12204951","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0036731907
"Naylor M.J., Walia C.S., McOrist S., Lehrbach P.R., Deane E.M., Harrison G.A.","7103407832;6506357489;57213024418;6603728862;7006255983;35560324800;","Molecular characterization confirms the presence of a divergent strain of canine coronavirus (UWSMN-1) in Australia",2002,"Journal of Clinical Microbiology","40","9",,"3518","3522",,21,"10.1128/JCM.40.9.3518-3522.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036708361&doi=10.1128%2fJCM.40.9.3518-3522.2002&partnerID=40&md5=0b8949c007b2ddc0e6249f70b35472c7","Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia","Naylor, M.J., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; Walia, C.S., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; McOrist, S., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; Lehrbach, P.R., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; Deane, E.M., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; Harrison, G.A., Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia","Canine coronavirus (CCV) UWSMN-1 was originally identified from an outbreak of fatal gastroenteritis in breeding colonies. In this report, we examined whether UWSMN-1 represents a novel divergent strain or is the result of recombination events between canine and feline coronavirus strains. Sequencing of various regions of the spike and polymerase genes confirms that UWSMN-1 is widely divergent from other CCV and feline coronavirus strains. These data raise the possibility that this strain is the first member of a novel third subtype of CCV.",,"article; Australia; Coronavirus; gastroenteritis; genetic variability; molecular dynamics; nonhuman; nucleotide sequence; priority journal; structural gene; animal; animal disease; chemistry; classification; DNA sequence; dog; dog disease; genetics; molecular genetics; nucleotide sequence; phylogeny; sequence alignment; structural gene; virology; virus infection; Animal; Australia; Base Sequence; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Genes, pol; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Sequence Alignment; Sequence Analysis, DNA; Viral Envelope Proteins; Animals; Australia; Base Sequence; Dogs; Molecular Sequence Data; Phylogeny; Sequence Alignment; Sequence Analysis, DNA; membrane protein; spike glycoprotein, coronavirus; virus envelope protein","Appel, M.J.G., Does canine coronavirus augment the effects of subsequent parvovirus infection? (1988) Vet. Med. Small Anim. Clin., 83, pp. 360-366; Binn, L.N., Lazar, E., Keenan, K.P., Huxsoll, D., Marchwicki, R.H., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhea (1975) Proc. Annu. Mtg. U.S. Anim. Health Assoc., 78, pp. 359-366; Carmichael, L.E., (1978) Infectious canine enteritis caused by corona-like virus: current status and request for information, , Baker Institute Laboratory Report, series 2, no. 9. James A. Baker Institute for Animal Health, Ithaca, N.Y; Finlaison, D.S., Faecal viruses of dogs - An electron microscope study (1995) Vet. Microbiol., 46, pp. 295-305; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Kokubu, T., Taharaguchi, S., Katayama, S., Hatano, M., Takahashi, T., Iwamoto, K., Masubuchi, K., Inaba, Y., Nucleotide sequence of the spike protein of canine coronavirus strain 5821 (1998) J. Jpn. Vet. Med. Assoc., 51, pp. 251-255; Lai, M.M.C., Baric, R.C., Makino, S., Keck, J.G., Engbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronavirus (1985) J. Virol., 56, pp. 449-456; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High frequency RNA recombination of murine coronavirus (1986) J. Virol., 57, pp. 729-739; Marshall, J.A., Healy, D.S., Studdert, M.J., Scott, P.C., Kennett, M.L., Ward, B.K., Gust, I.D., Viruses and virus-like particles in the faeces of dogs with and without diarrhoea (1984) Aust. Vet. J., 61, pp. 33-38; Naylor, M.J., Harrison, G.A., McOrist, S., Monckton, R.P., Lehrbach, P.R., Deane, E.M., Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterization of a new Australian isolate (2001) J. Clin. Microbiol., 39, pp. 1036-1041; Naylor, M.J., Monckton, R.P., Lehrbach, P.R., Deane, E.M., Canine coronavirus in Australian dogs (2001) Aust. Vet. J., 79, pp. 27-30; Saif, L.J., Coronavirus immunogens (1993) Vet. Microbiol., 37, pp. 285-297; Schnagl, R.D., Holmes, I.H., Coronavirus-like particles in stools from dogs from some country areas of Australia (1978) Vet. Rec., 102, pp. 528-529; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Res., 61, pp. 145-152; Wesseling, J.G., Vennema, H., Godeke, G.J., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Naylor, M.J.; Cancer Research Program, Garvan Institute of Medical Research, St Vincent's Hospital, Sydney, NSW 2010, Australia; email: m.naylor@garvan.org.au",,,00951137,,JCMID,"12202609","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0036708361
"Loa C.C., Lin T.L., Wu C.C., Bryan T., Hooper T., Schrader D.","6602648721;7404860140;7501664098;7005517787;7005121335;7007179253;","Specific mucosal IgA immunity in turkey poults infected with turkey coronavirus",2002,"Veterinary Immunology and Immunopathology","88","1-2",,"57","64",,9,"10.1016/S0165-2427(02)00135-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037031759&doi=10.1016%2fS0165-2427%2802%2900135-6&partnerID=40&md5=4fa87f2d743cabc4b6df18b504c9b498","Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","Loa, C.C., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Lin, T.L., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Wu, C.C., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Bryan, T., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Hooper, T., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States; Schrader, D., Department of Veterinary Pathobiology, Animal Disease Diagnostic Laboratory, Purdue University, West Lafayette, IN 47907-1175, United States","The objective of this study was to elucidate the kinetics and magnitudes of specific IgA antibody responses in intestines of turkey poults infected with turkey coronavirus (TCV). Turkey poults were orally inoculated with TCV at 10 days of age. Intestinal segment cultures were administered for duodenum, jejunum, and ileum and the IgA antibody responses were analyzed at 1, 2, 3, 4, 6, or 9 weeks post-infection (PI) in two different experiments. The kinetics of virus-specific IgA antibody responses in duodenum, jejunum, and ileum were similar: gradually increased from 1 week PI, reached the peak at 3 or 4 weeks PI, and declined afterward. The virus-specific IgA antibody responses in duodenum, jejunum, and ileum showed negative correlation with duration of TCV antigen in the corresponding locations of intestine with Spearman's correlation coefficient of -0.85 (p=0.034), -0.74 (p=0.096), and -0.75 (p=0.084), respectively. Moreover, the virus-specific IgA antibody responses in serum were positively correlated with that of duodenum (coefficient=0.829,p=0.042), jejunum (coefficient=0.829,p=0.042), and ileum (coefficient=0.771,p=0.072) segment cultures, suggesting that the induction of specific IgA response in serum was predictive of an IgA response in intestine. The results indicate that intestinal mucosal IgA antibodies to TCV are elicited in turkeys following infection with TCV. The local mucosal antibodies may provide protective immunity for infected turkeys to recover from TCV infection. © 2002 Elsevier Science B.V. All rights reserved.","Humoral; Immune responses; Immunoglobulin A; Mucosal immunity; Turkey coronavirus; Turkey poult enteritis","immunoglobulin A antibody; animal model; antibody response; article; bird disease; controlled study; Coronavirus; correlation coefficient; duodenum; infection prevention; inoculation; intestine; jejunum; kinetics; mucosal immunity; nonhuman; turkey (bird); virus infection; Animals; Antibody Specificity; Antigens, Viral; Coronavirus; Enteritis, Transmissible, of Turkeys; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Direct; Immunity, Mucosal; Immunoglobulin A; Intestinal Mucosa; Intestine, Small; Kinetics; Microscopy, Electron; Poultry Diseases; Specific Pathogen-Free Organisms; Turkeys; Coronavirus; Turkey coronavirus","Beetham, P.K., Glick, B., Dick, J.W., A comparison of three isolation methods for obtaining immunoglobulin A from turkey bile (1993) Avian Dis., 37, pp. 1026-1031; Dea, S., Garzon, S., Identification of coronaviruses by the use of indirect protein A-gold immunoelectron microscopy (1991) J. Vet. Diagn. Invest., 3, pp. 297-305; Deshmukh, D.R., Sautter, J.H., Patel, B.L., Pomeroy, B.S., Histopathology of fasting and bluecomb disease in turkey poults and embryos experimentally infected with bluecomb disease coronavirus (1975) Avian Dis., 20 (4), pp. 631-640; Dohms, J.E., Saif, Y.M., Pitts, J.E., Isolation of turkey immunoglobulin-A (1978) Avian Dis., 22 (1), pp. 151-156; Khoury, C.A., Brown, K.A., Kim, J.E., Offit, P.A., Rotavirus-specific intestinal immune response in mice assessed by enzyme-linked immunospot assay and intestinal fragment culture (1994) Clin. Diagn. Lab. Immunol., 1 (6), pp. 722-728; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Dis., 44, pp. 498-506; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T., Thacker, H.L., Hooper, T., Schrader, D., Humoral and cellular immune responses in turkey poults infected with turkey coronavirus (2001) Poultry Sci., 80, pp. 1416-1424; Losonsky, G.A., Fantry, G.T., Reymann, M., Lim, Y., Validation of a gastrointestinal explant system for measurement of mucosal antibody production (1999) Clin. Diagn. Lab. Immunol., 6 (6), pp. 803-807; McPherson, G., (2001) Applying and Interpreting Statistics: A Comprehensive Guide, 2nd Edition, pp. 457-458. , Springer, New York; Nagaraja, K.V., Pomeroy, B.S., Secretory antibodies against turkey coronaviral enteritis (1978) Am. J. Vet. Res., 39, pp. 1463-1465; Nagaraja, K.V., Pomeroy, B.S., Immunofluorescent studies on localization of secretory immunoglobulins in the intestines of turkeys recovered from turkey coronaviral enteritis (1980) Am. J. Vet. Res., 41, pp. 1283-1284; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Edition, pp. 686-692. , Calnek, B.W., Barnes, H.J., Beard, C.W., McDougald, L.R., Saif, Y.M. (Eds.). Iowa State University Press, Ames, IA; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (bluecomb) (1975) Am. J. Vet. Res., 36, pp. 1265-1267; Reed, L.J., Muench, H., A simple method for estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; VanCott, J.L., Brim, T.A., Simkins, R.A., Saif, L.J., Isotype-specific antibody-secreting cells to transmissible gastroenteritis virus and porcine respiratory coronavirus in gut- and bronchus-associated lymphoid tissues of suckling pigs (1993) J. Immunol., 150, pp. 3990-4000; Yu, M., Ismail, M.M., Qureshi, M.A., Dearth, R.N., Barnes, H.J., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome: The role of a small round virus and a turkey coronavirus (2000) Avian Dis., 44, pp. 297-304; Yuan, L., Ward, L.A., Rosen, B.I., To, T.L., Saif, L.J., Systemic and intestinal antibody-secreting cell responses and correlates of protective immunity to human rotavirus in a gnotobiotic pig model of disease (1996) J. Virol., 70 (5), pp. 3075-3083","Lin, T.L.; Dept. of Veterinary Pathobiology, School of Veterinary Medicine, Purdue University, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,,01652427,,VIIMD,"12088645","English","Vet. Immunol. Immunopathol.",Article,"Final",Open Access,Scopus,2-s2.0-0037031759
"Isaacs D., Joshi P.","7102241286;18935311200;","Respiratory infections and asthma",2002,"Medical Journal of Australia","177","6 SUPPL.",,"S50","S51",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037120585&partnerID=40&md5=d1c4e80a04f2b21b97a7701cdbe0277d","Dept. of Immunol. and Infect. Dis., Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW 2145, Australia; University of Sydney, Sydney, NSW, Australia","Isaacs, D., Dept. of Immunol. and Infect. Dis., Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW 2145, Australia, University of Sydney, Sydney, NSW, Australia; Joshi, P., Dept. of Immunol. and Infect. Dis., Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW 2145, Australia, University of Sydney, Sydney, NSW, Australia","What we know: Respiratory viral infections caused by rhinoviruses, coronaviruses, influenza, parainfluenza and respiratory syncytial viruses (RSVs) are important triggers of asthma attacks. Mycoplasma and Chlamydia infections can also provoke asthma attacks, although less commonly. RSV infections probably do not cause asthma, but are potent triggers of wheezing, with the result that RSV infection often reveals underlying asthma in children. RSV infection does not cause atopy. Bacterial respiratory infections in infancy appear to protect against later atopy. What we need to know: Does RSV infection in infancy alter a child's TH1/TH2 responses to later infections with other respiratory pathogens? What are the mechanisms (immunological or mechanical) by which respiratory pathogens cause wheezing? What is the role of respiratory infections in exacerbations of asthma? Can epidemiology shed light on this? Do viruses such as RSV cause asthma or uncover underlying asthma? Do children respond differently to RSV than to other viruses? Does atopy affect those responses? Do bacterial respiratory infections truly protect against future atopy?",,"immunoglobulin G; immunoglobulin M; macrolide; asthma; atopy; Australia; bacterial infection; bacterial pneumonia; child; Chlamydia; Chlamydophila pneumoniae; communicable disease; conference paper; controlled study; Coronavirus; disease association; disease exacerbation; disease severity; human; infant; Influenza virus; Mycoplasma; Mycoplasma pneumoniae; native species; nonhuman; Parainfluenza virus; pathogenicity; peak expiratory flow; Respiratory syncytial pneumovirus; respiratory tract infection; Rhinovirus; Th1 cell; Th2 cell; virus infection; wheezing; Asthma; Child; Child, Preschool; Chlamydophila pneumoniae; Humans; Infant; Pneumonia, Bacterial; Pneumonia, Mycoplasma; Respiratory Syncytial Virus Infections; Respiratory Tract Infections","Johnston, S.L., Pattemore, P.K., Sanderson, S., Community study of role of viral exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Gern, J.E., Galagan, D.M., Jarjour, N.N., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Anderson, G.P., Therapeutic prospects for early asthma (2002) Med J Aust, 177 (SUPPL.), pp. S66-S69. , Sep 16:; Joshi, P., A cohort study of cytokines and atopy (2001), [PhD thesis]. University of Sydney; Joshi, P., Kakakios, A., Jayasekera, J., Isaacs, D., A comparison of IL-2 levels in nasopharyngeal and endotracheal aspirates of babies with respiratory syncytial viral bronchiolitis (1998) J Allergy Clin Immunol, 102, pp. 618-620; Wang, S.-Z., Forsyth, R.D., Asthma and respiratory syncytial virus infection in infancy: Is there a link? (1998) Clin Exp Allergy, 28, pp. 927-935; Welliver, R.C., RSV and chronic asthma (1995) Lancet, 346, pp. 789-790; McConnochie, K.M., Roghmann, K.J., Predicting clinically significant lower respiratory tract illness in childhood following mild bronchiolitis (1985) Am J Dis Child, 139, pp. 625-631; Stein, R.T., Sherrill, D., Morgan, W.J., Respiratory syncytial virus in early life and risk of wheeze and allergy by age 13 years (1999) Lancet, 354, pp. 541-545; Hammerschlag, M.R., Chlamydia pneumoniae and the lung (2000) Eur Respir J, 16, pp. 1001-1007; Johnston, S.L., Is Chlamydia pneumoniae important in asthma? The first controlled trial of therapy leaves the question unanswered (2001) Am J Respir Crit Care Med, 164, pp. 513-514; Black, P.N., Francesco, B., Jenkins, R., Trial of roxithromycin in subjects with asthma and serological evidence of infection with Chlamydia pneumoniae (2001) Am J Respir Crit Care Med, 164, pp. 536-541; Amayasu, H., Yoshida, S., Ebana, S., Clarithromycin suppresses bronchial hyperresponsiveness associated with eosinophilic inflammation in patients with asthma (2000) Ann Allergy Asthma Immunol, 6, pp. 594-598; File T.M., Jr., Tan, J.C., Plouffe, J.F., The role of atypical pathogens: Mycoplasma pneumoniae, Chlamydia pneumoniae, and Legionella pneumophila in respiratory infection (1998) Infect Dis Clin North Am, 12, pp. 569-592; Micillo, E., Bianco, A., D'Auria, D., Respiratory infections and asthma (2000) Allergy, 55 (SUPPL. 61), pp. 42-45; Von Mutius, E., Illis, S., Hirsch, T., Frequency of infections and risk of asthma, atopy and airway hyperresponsiveness in children (1999) Eur Respir J, 14, pp. 4-11; Peat, J.K., Veale, A., Impact and aetiology of respiratory infections, asthma and airway disease in Australian Aborigines (2001) J Paediatr Child Health, 37, pp. 108-112","Isaacs, D.; Dept. of Immunol. and Infect. Dis., Children's Hospital at Westmead, Locked Bag 4001, Westmead, NSW 2145, Australia; email: davidi@chw.edu.au",,,0025729X,,MJAUA,"12225258","English","Med. J. Aust.",Conference Paper,"Final",,Scopus,2-s2.0-0037120585
"Lin T.L., Loa C.C., Wu C.C.","57213499631;6602648721;7501664098;","Existence of gene 5 indicates close genomic relationship of Turkey coronavirus to infectious bronchitis virus",2002,"Acta Virologica","46","2",,"107","116",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036377387&partnerID=40&md5=dd98b62e64927f064fa37fd376cd81eb","Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States","Lin, T.L., Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Loa, C.C., Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; Wu, C.C., Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States","A segment of genomic RNA extending from the 3′-end of the membrane (M) protein gene to the 5′-end of the nucleocapsid (N) protein gene of Turkey coronavirus (TCV) was amplified by reverse transcription-polymerase chain reaction (RT-PCR). The primers were derived from the corresponding sequences of Infectious bronchitis virus (IBV). The PCR products were cloned and sequenced and their nucleic acid structure and similarity to the published sequences of IBV were analyzed. Gene 5 containing two overlapping open reading frames (ORFs), 5a and 5b, was localized between M and N genes of TCV. The overall nucleotide sequences of the amplified regions from TCV isolates shared 88.4% to 91.8% similarity to the corresponding region of IBV strains. The consensus transcription-associated sequence of IBV, CTTAACAA, was highly conserved in the TCV genome with regard to nucleotide sequence and location in terms of the initiation codons of the genes 5 and N. The similarities between the predicted amino acid sequences of ORFs 5a and 5b of TCV isolates and the homologous genes of IBV strains were 85.4% to 94.0%. The results indicate the existence of gene 5 in the genome of TCV and a close relatedness of the TCV gene 5 to the IBV gene 5 in location and nucleotide sequence.","Avian infectious bronchitis virus; Gene 5; Genomic relatedness; Turkey coronavirus","amino acid sequence; article; Avian infectious bronchitis virus; Coronavirus; gene 5; nonhuman; nucleotide sequence; open reading frame; sequence homology; virus gene; virus nucleocapsid; Amino Acid Sequence; Animals; Base Sequence; Chick Embryo; Cloning, Molecular; Coronavirus, Turkey; DNA, Viral; Genes, Viral; Genome, Viral; Infectious bronchitis virus; Molecular Sequence Data; Nucleocapsid Proteins; Open Reading Frames; Phylogeny; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Species Specificity; Turkeys; Aves; Avian infectious bronchitis virus; Coronavirus; Turkey coronavirus","Akin, A., Lin, T.L., Wu, C.C., Bryan, T.A., Hooper, T., Schrader, D., Nucleocapsid protein gene sequence analysis reveals close genomic relationship between turkey coronavirus and avian infectious bronchitis virus (2001) Acta Virol., 45, pp. 31-38; Akin, A., Wu, C.C., Lin, T.L., Amplification and cloning of complete infectious bursal disease virus genomic RNA segments by a long and accurate PCR (1999) J. Virol. Methods, 82, pp. 55-61; Andreasen, J.R., Jackwood M.W., Jr., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis., 35, pp. 216-220; Barnes, W.M., PCR amplification of up to 35-kb DNA with high fidelity and high yield from bacteriophage templates (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 2216-2220; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J. Gen. Virol., 68, pp. 57-77; Chomczynski, P., Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction (1987) Anal. Biochem., 162, pp. 156-159; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete genomic sequence of the transmissible gastroenteritis virus (1995) Adv. Exp. Med. Biol., 380, pp. 459-461; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry. 10th ed., pp. 686-692. , Calnek B, Barnes HJ, Beard CW, McDougald LR, Saif YM (Eds): Iowa State University Press, Ames, Iowa; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Casais, R., Cavanagh, D., Britton, P., Expression of reporter genes from the defective RNA CD-61 of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81, pp. 1687-1698; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) J. Gen. Virol., 72, pp. 1659-1666","Lin, T.L.; Dept. of Veterinary Pathobiology, Purdue University, 1175 ADDL, West Lafayette, IN 47907-1175, United States; email: tllin@purdue.edu",,,0001723X,,AVIRA,"12387503","English","Acta Virol.",Article,"Final",,Scopus,2-s2.0-0036377387
"Sasseville A.M.-J., Boutin M., Gélinas A.-M., Dea S.","6603215910;7003272229;6602090251;7006056287;","Sequence of the 3′-terminal end (8.1 kb) of the genome of porcine haemagglutinating encephalomyelitis virus: Comparison with other haemagglutinating coronaviruses",2002,"Journal of General Virology","83","10",,"2411","2416",,17,"10.1099/0022-1317-83-10-2411","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036771641&doi=10.1099%2f0022-1317-83-10-2411&partnerID=40&md5=8658cbc845f173799ec9281621eb7674","INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada","Sasseville, A.M.-J., INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada; Boutin, M., INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada; Gélinas, A.-M., INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada; Dea, S., INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada","A cytopathogenic coronavirus, serologically identified as porcine haemagglutinating encephalomyelitis virus (HEV), has recently been associated with acute outbreaks of wasting and encephalitis in nursing piglets from pig farms in southern Québec and Ontario, Canada. The 3′-terminal end of the genome of the prototype HEV-67N strain and that of the recent Québec IAF-404 field isolate, both propagated in HRT-18 cells, were sequenced. Overall, sequencing data indicated that HEV has remained antigenically and genetically stable since its first isolation in North America in 1962. Compared with the prototype strain of bovine enteropathogenic coronavirus (BCoV), HEV, as well as the human respiratory coronavirus (HCoV-OC43) showed a major deletion in their ORF4 gene. Deduced amino acid sequences for both HEV strains revealed 89/88,80, 93/92 and 95/94% identities with the structural proteins HE, S, M and N of BCoV and HCoV-OC43, respectively. Major variations were observed in the S1 portion of the S gene of both HEV strains, with only 73/71% amino acid identities compared with those of the two other haemagglutinating coronaviruses.",,"structural protein; virus protein; virus protein; amino acid sequence; article; Canada; controlled study; Coronavirus; disease association; encephalitis; gene deletion; gene sequence; genetic stability; genetic variability; human; human cell; nonhuman; North America; nucleotide sequence; open reading frame; porcine haemagglutinating encephalomyelitis virus; priority journal; rectum tumor; sequence homology; serology; swine disease; tumor cell line; virus genome; virus hemagglutination; virus identification; virus isolation; virus strain; wasting syndrome; animal; cattle; DNA sequence; genetics; isolation and purification; molecular genetics; swine; virology; virus genome; virus infection; Bovinae; Coronavirus; RNA viruses; Suidae; Sus scrofa; Amino Acid Sequence; Animals; Cattle; Coronavirus; Coronavirus Infections; Genome, Viral; Humans; Molecular Sequence Data; Open Reading Frames; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Swine; Viral Nonstructural Proteins; Viral Structural Proteins","Abraham, S., Kienzle, T.E., Lapps, W., Brian, D.A., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1991) Virology, 176, pp. 296-301; Andries, K., Pensaert, M.B., Virus isolated and immunofluorescence in different organs of pigs infected with hemagglutinating encephlomyelitis virus (1980) American Journal of Veterinary Research, 41, pp. 215-218; Boireau, P., Cruciere, C., Laporte, J., Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains (1990) Journal of General Virology, 71, pp. 487-492; Boutin, M., Sasseville, A.M.-J., Dea, S., Defection and identification of hemagglutinating coronaviruses using group-specific single and multiplex RT-PCR (2001), pp. 391-392. , Proceedings of the X International Symposium of Veterinary Laboratory Diagnostics, Salsomaggiore, Parma, Italy, July 4-7; Breslin, J.J., Smith, L.G., Fuller, F.G., Guy, J.S., Sequences analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Research, 65, pp. 187-198; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gouch, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 365-378; Dea, S., Tijssen, P., Antigenic and polypeptide structure of turkey enteric coronaviruses as defined by monoclonal antibodies (1989) Journal of General Virology, 70, pp. 1725-1741; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) Journal of Virology, 64, pp. 3112-3118; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Gelinas, A., Boutin, M., Sasseville, A.M.-J., Dea, S., Bovine coronaviruses associated with enteric and respiratory diseases in Canadian dairy cattle display different reactivities to anti-HE monoclonal antibodies and distinct amino acid changes in their HE, S and ns 4.9 protein (2001) Virus Research, 76, pp. 43-57; Greig, A.S., Bouillant, A.M., Studies on the hemagglutination phenomenon of hemagglutinating encephalomyelitis virus (HEV) of pigs (1972) Canadian Journal of Comparative Medicine, 36, pp. 366-370; Hogue, B.G., Brian, D.A., Structural proteins of human respiratory coronavirus OC43 (1986) Virus Research, 5, pp. 131-144; Ismail, M.M., Cho, K.O., Hasoksuz, M., Saif, L.J., Saif, Y.M., Antigenic and genomic relatedness of turkey-origin coronaviruses, bovine coronavirus, and infectious bronchitis virus of chickens (2002) Avian Diseases, 45, pp. 978-984; Kamahora, T., Soe, L., Lai, M.M., Sequencing analysis of the nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Research, 12, pp. 1-9; Kienzle, T.E., Abraham, S., Hogue, B.G., Brian, D.A., Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein (1990) Journal of Virology, 64, pp. 1834-1838; King, B., Potts, B.J., Brian, D.A., Bovine coronavirus hemagglutinin protein (1985) Virus Research, 2, pp. 53-59; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Lin, T.I., Tsai, S.C., Wu, C.C., Bryan, T.A., Thaker, H.L., Hooper, T., Schrader, D., Characterization of turkey coronaviruses from turkey poults with acute enteritis (2002) Veterinary Microbiology, 84, pp. 179-186; Loa, C.C., Lin, T.L., Wu, C.C., Bryan, T.A., Thacker, H.L., Hooper, T., Schrader, D., Detection of antibody to turkey coronavirus by antibody-capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Diseases, 44, pp. 498-506; Michaud, L., Dea, S., Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec isolates (1993) Archives of Virology, 131, pp. 455-465; Mounir, S., Talbot, P.J., Sequence analysis of the membrane protein gene of human coronavirus OC43 and evidence for O-glycosylation (1992) Journal of General Virology, 73, pp. 2731-2736; Mounir, S., Talbot, P.J., Human coronavirus OC43 RNA 4 lacks two open reading frames located downstream of the S gene of bovine coronavirus (1993) Virology, 192, pp. 355-360; Mounir, S., Talbot, P.J., Molecular characterization of the S protein gene of human coronavirus OC43 (1993) Journal of General Virology, 74, pp. 1981-1987; Parker, M.D., Yoo, D., Cox, G.J., Babiuk, L.A., Primary structure of the S peplomer gene of bovine coronavirus and surface expression in insect cells (1990) Journal of General Virology, 71, pp. 263-270; Parker, M.D., Yoo, D., Babiuk, L.A., Expression and secretion of the bovine coronavirus hemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses (1990) Journal of Virology, 64, pp. 1625-1629; Pensaert, M., Andries, K., Hemagglutinating encephalomyelitis virus (1993) Diseases of Swine, Section 2, Viral Diseases, pp. 268-273. , 7th edn, Ames, Iowa: ISU Press; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) Journal of General Virology, 69, pp. 2939-2952; Storz, J., Stine, L., Liem, A., Anderson, G.A., Coronavirus isolation from nasal swab samples in cattle with signs of respiratory tract disease after shipping (1996) Journal of the American Veterinary Medical Association, 208, pp. 1452-1455; Vautherot, J.F., Madelaine, M.F., Boireau, P., Laporte, J., Bovine coronavirus peplomer glycoproteins: Detailed antigenic analyses of S1, S2 and HE (1992) Journal of General Virology, 73, pp. 1725-1737; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine coronavirus (1991) Journal of General Virology, 72, pp. 1659-1666; Vieler, E., Schlapp, T., Anders, C., Herbst, W., Genomic relationship of porcine hemagglutinating encephalomyelitis virus to bovine coronavirus and human coronavirus OC43 as studied by the use of bovine coronavirus S gene-specific probes (1995) Archives of Virology, 140, pp. 1215-1223; Vieler, E., Schlapp, T., Herbst, W., The region between the M and S genes of porcine haemagglutinating encephalomyelitis virus is highly similar to human coronavirus OC43 (1996) Journal of General Virology, 77, pp. 1443-1447; Vlasak, R., Luytjes, W., Leider, J., Spaan, W., Palese, P., The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity (1988) Journal of Virology, 62, pp. 4686-4690; Von Heijne, G., A new method for predicting signal sequence cleavage amino acid sites (1986) Nucleic Acids Research, 14, pp. 4683-4690; Yoo, D., Parker, M.D., Song, J., Cox, G.J., Deregt, D., Babiuk, L.A., Structural analysis of the conformational domains involved in neutralization of bovine coronavirus using deletion mutants of the spike glycoprotein S1 subunit expressed by recombinant baculoviuses (1991) Virology, 183, pp. 91-98","Dea, S.; INRS-Institut Armand-Frappier, Centre Microbiologie Biotechnologie, Université du Québec, 531 boul. des Prairies, Laval, Qué. H7V 1B7, Canada; email: serge.dea@inrs-iaf.uquebec.ca",,"Society for General Microbiology",00221317,,JGVIA,"12237422","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036771641
"Takamura K., Matsumoto Y., Shimizu Y.","57192335035;15741458600;7404067558;","Field study of bovine coronavirus vaccine enriched with hemagglutinating antigen for winter dysentery in dairy cows",2002,"Canadian Journal of Veterinary Research","66","4",,"278","281",,18,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036808726&partnerID=40&md5=9bedf5f563ab76f61e3f4ab279dfa74e","Kyoto Biken Laboratories Inc., 24-15 Makishima-cho, Uji 611-0041, Japan","Takamura, K., Kyoto Biken Laboratories Inc., 24-15 Makishima-cho, Uji 611-0041, Japan; Matsumoto, Y., Kyoto Biken Laboratories Inc., 24-15 Makishima-cho, Uji 611-0041, Japan; Shimizu, Y., Kyoto Biken Laboratories Inc., 24-15 Makishima-cho, Uji 611-0041, Japan","A field study of a vaccine; prepared by solubilizing cells infected with bovine coronavirus, Triton X-100, and mixing with an oil adjuvant, was performed at 9 farms over 4 prefectures. The cattle tested were Holstein dairy cows aged 2 to 10 years. A vaccination group consisted of 157 animals (including 132 pregnant cows) and a non-vaccinated control group consisted of 50 animals. The cows received 2 intramuscular injections of vaccine (2 mL) at 3-week intervals. Vaccinated cows did not develop abnormalities, such as a decrease in milk production volume, and all pregnant animals calved normally. The geometric mean of the hemagglutination inhibition antibody titer was 34.2 before vaccination in test cows. The titer had increased to 105.6, 3 weeks after the 1st injection and peaked at 755.6, 1 month after the 2nd injection. A high antibody titer persisted at 396.0; 241.0; and 201.5, at 3, 6, and 9 months after the 2nd injection, respectively. This confirms the safety and high antibody-response induced by this prototype vaccine. Therefore, this vaccine may be useful for the prevention of winter dysentery caused by bovine coronavirus infection.",,"adjuvant; antigen; virus vaccine; active immunization; antibody titer; article; breeding; controlled study; Coronavirus; dairy cattle; dairying; drug safety; drug synthesis; female; hemagglutination inhibition; Japan; milk yield; nonhuman; RNA virus infection; solubilization; Animals; Antibodies, Viral; Antigens, Viral; Cattle; Cattle Diseases; Cold; Coronavirus Infections; Coronavirus, Bovine; Dairying; Dysentery; Female; Hemagglutination Inhibition Tests; Injections, Intramuscular; Seasons; Time Factors; Treatment Outcome; Vaccination; Viral Vaccines; Animalia; Bos taurus; Bovinae; Bovine coronavirus; Coronavirus; RNA viruses","Mebus, C.A., Stair, E.L., Rhode, M.B., Twiehaus, M.J., Neonatal calf diarrhea: Propagation, attenuation, and characteristics of a coronavirus-like agent (1973) Am. J. Vet. Res, 34, pp. 145-150; Saif, L.J., Redman, D.R., Brock, K.V., Kohler, E.M., Heckert, R.A., Winter dysentery in adult dairy cattle: Detection of coronavirus in the faeces (1988) Vet. Rec, 123, pp. 300-301; Taniguti, S., Iwamoto, H., Fukuura, H., Ito, H., Gekai, N., Nagato, Y., Recurrence of bovine coronavirus infection in cows (1986) J. Jpn. Vet. Med. Assoc, 39, pp. 298-302; Tsunemitsu, H., Yonemichi, H., Hirai, T., Isolation of bovine coronavirus from feces and nasal swabs of calves with diarrhea (1991) J. Vet. Med. Sci, 53, pp. 433-437; Woode, G.N., Bridger, J.C., Viral enteritis of calves (1975) Vet. Rec, 25, pp. 85-88; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in southern Britain (1986) Vet. Rec, 119, pp. 34-39; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Aetiology of diarrhoea in young calves (1986) Vet. Rec, 119, pp. 31-34; Takahashi, E., Inaba, Y., Sato, K., Epizootic diarrhea of adult cattle associated with a coronavirus-like agent (1980) Vet. Microbiol, 5, pp. 151-154; Myers, L.L., Snodgrass, D.R., Colostral and milk antibody titers in cows vaccinated with a modified live-rotavirus-coronavirus vaccine (1982) J. Am. Vet. Med. Assoc, 181, pp. 486-488; Freitag, H., Wetzel, H., Espenkoetter, E., Prophylaxis of diarrhoea due to rotavirus and coronavirus in calves (1984) Tierarztl. Umsch, 39, pp. 731-734; Garcfa Sánchez, J., Muzquiz, J.L., Gironés, O., Halaihel, N.G., Immunization against bovine rotavirus and coronavirus in pregnant cows. II. Antibody titers in the mammary secretion of vaccinated animals. III. Antibody titers in the blood serum of the calves (1991) Veterinaria, 8, pp. 289-298. , 217-224; Waltner-Toews, D., Martin, S.W., Meek, A.H., McMillan, I., Crouch, C.F., A field trial to evaluate the efficacy of a combined rotavirus-coronavirus/Escherichia coli vaccine in dairy cattle (1985) Can. J. Comp. Med, 49, pp. 1-9; Collins, J.K., Riegel, C.A., Olson, J.D., Fountain, A., Shedding of enteric coronavirus in adult cattle (1987) Am. J. Vet. Res, 48, pp. 361-365; Takamura, K., Okada, N., Ui, S., Hirahara, T., Shimizu, Y., Protection studies on winter dysentery caused by bovine coronavirus in cattle using antigens prepared from infected cell lysates (2000) Can. J. Vet. Res, 64, pp. 138-140; Thurber, E.T., Bass, E.P., Beckenhauer, W.H., Field trial evaluation of a reo-coronavirus calf diarrhea vaccine (1977) Can. J. Comp. Med, 41, pp. 131-136","Takamura, K.; Kyoto Biken Laboratories Inc., 24-15 Makishima-cho, Uji 611-0041, Japan; email: kblboad@kyotobiken.co.jp",,,08309000,,CJVRE,"12418784","English","Can. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0036808726
"Das Sarma J., Scheen E., Seo S.-H., Koval M., Weiss S.R.","6602813975;6507002821;7202469910;7007019356;57203567044;","Enhanced green fluorescent protein expression may be used to monitor murine coronavirus spread in vitro and in the mouse central nervous system",2002,"Journal of NeuroVirology","8","5",,"381","391",,57,"10.1080/13550280260422686","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842859786&doi=10.1080%2f13550280260422686&partnerID=40&md5=20a87924323e1d1c3e4696a8b6150627","Department of Physiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States","Das Sarma, J., Department of Physiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Scheen, E., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Seo, S.-H., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Koval, M., Department of Physiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA, United States","Targeted recombination was used to select mouse hepatitis virus isolates with stable and efficient expression of the gene encoding the enhanced green fluorescent protein (EGFP). The EGFP gene was inserted into the murine coronavirus genome in place of the nonessential gene 4. These viruses expressed the EGFP gene from an mRNA of slightly slower electrophoretic mobility than mRNA 4. EGFP protein was detected on a Western blot of infected cell lysates and EGFP activity (fluorescence) was visualized by microscopy in infected cells and in viral plaques. Expression of EGFP remained stable through at least six passages in tissue culture and during acute infection in the mouse central nervous system. These viruses replicated with similar kinetics and to similar final extents as wild-type virus both in tissue culture and in the mouse central nervous system (CNS). They caused encephalitis and demyelination in animals as wild-type virus; however, they were somewhat attenuated in virulence. Isogenic EGFP-expressing viruses that differ only in the spike gene and express either the spike gene of the highly neurovirulent MHV-4 strain or the more weakly neurovirulent MHV-A59 strain were compared; the difference in virulence and patterns of spread of viral antigen reflected the differences between parental viruses expressing each of these spike genes. Thus, EGFP-expressing viruses will be useful in the studies of murine coronavirus pathogenesis in mice.","Murine coronavirus; Viral genetics; Viral pathogenesis","green fluorescent protein; messenger RNA; virus antigen; green fluorescent protein; membrane protein; messenger RNA; photoprotein; recombinant protein; spike glycoprotein, coronavirus; virus antigen; virus envelope protein; animal cell; animal experiment; animal model; article; cell lysate; central nervous system infection; controlled study; demyelination; electrophoretic mobility; encephalitis; fluorescence microscopy; gene expression; gene insertion; in vitro study; male; monitoring; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein expression; tissue culture; virus attenuation; virus genome; virus isolation; virus pathogenesis; virus plaque; virus recombination; virus replication; virus strain; virus virulence; Western blotting; wild type; animal; biosynthesis; brain; C57BL mouse; cat; central nervous system; comparative study; disease model; genetic reassortment; genetic recombination; genetics; L cell; mouse; pathogenicity; virology; virulence; virus culture; virus infection; Animalia; Coronavirus; Murinae; Murine hepatitis virus; Murine hepatitis virus strain 4; Animals; Antigens, Viral; Brain; Cats; Central Nervous System; Coronavirus Infections; Disease Models, Animal; Green Fluorescent Proteins; L Cells (Cell Line); Luminescent Proteins; Male; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Reassortant Viruses; Recombinant Proteins; Recombination, Genetic; RNA, Messenger; Serial Passage; Viral Envelope Proteins; Virulence; Virus Replication","Bond, C.W., Leibowitz, J.L., Robb, J.A., Pathogenic murine coronaviruses. II. Characterization of virus-specific proteins of murine coronaviruses JHMV and A59V (1979) Virology, 94, pp. 371-384; Cormack, B.P., Valdivia, R.H., Falkow, S., FACS-optimized mutants of the green fluorescent protein (GFP) (1996) Gene, 173, pp. 33-38; Das Sarma, J., Fu, L., Tsai, J.C., Weiss, S.R., Lavi, E., Demyelination determinants map to the spike glycoprotein gene of coronavirus mouse hepatitis virus (2000) J. Virol., 74, pp. 9206-9213; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Gombold, J.L., Weiss, S.R., Mouse hepatitis virus A59 increases steady state levels of MHC mRNAs in primary glial cell cultures and in the murine central nervous system (1992) Microb. Pathogen., 13, pp. 493-505; Haas, J., Park, E.C., Seed, B., Codon usage limitation in the expression of HIV-1 envelope glycoprotein (1996) Curr. Biol., 6, pp. 315-324; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. NeuroVirol., 2, pp. 101-110; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M.C., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab. Invest., 62, pp. 570-578; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein (1997) Virology, 239, pp. 1-10; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J. Virol., 72, pp. 9628-9636; Luytjes, W., Bredenbeek, P.J., Noten, A.F., Horzinek, M.C., Spaan, W.J.M., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Matthews, A.E., Weiss, S.R., Shlomchik, M.J., Hannum, L.G., Gombold, J.L., Paterson, Y., Antibody is required for clearance of infectious murine hepatitis virus A59 from the central nervous system, but not the liver (2001) J. Immunol., 167, pp. 5254-5263; Navas, S., Seo, S.H., Chua, M.M., Sarma, J.D., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J. Virol., 75, pp. 2452-2457; Ontiveros, E., Kuo, L., Masters, P.S., Perlman, S., Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS (2001) Virology, 289, pp. 230-238; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Phillips, J.J., Chua, M., Seo, S.H., Weiss, S.R., Multiple regions of the murine coronavirus spike glycoprotein influence neurovirulence (2001) J. Neuro Virol., 7, pp. 421-431; Sanger, F., Nicklen, S., Coulson, A.P., DNA sequencing with chain-terminating inhibitors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 5463-5467; Schwarz, B., Routledge, E., Siddell, S.G., Murine coronavirus nonstructural protein ns2 is not essential for virus replication in transformed cells (1990) J. Virol., 64, pp. 4784-4791; Slifka, M.K., Pagarigan, R., Mena, I., Feuer, R., Whitton, J.L., Using recombinant coxsackievirus B3 to evaluate the induction and protective efficacy of CD8+ T cells during picornavirus infection (2001) J. Virol., 75, pp. 2377-2387; Smith, B.N., Banfield, B.W., Smeraski, C.A., Wilcox, C.L., Dudek, F.E., Enquist, L.W., Pickard, G.E., Pseudorabies virus expressing enhanced green fluorescent protein: A tool for in vitro electrophysiological analysis of transsynaptically labeled neurons in identified central nervous system circuits (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 9264-9269; Sutherland, R.M., Chua, M.M., Lavi, E., Weiss, S.R., Paterson, Y., CD4+ and CD8+ T cells are not major effectors of mouse hepatitis virus A59-induced demyelinating disease (1997) J. NeuroVirol., 3, pp. 225-228; Yokomori, K., Lai, M.M.C., Mouse hepatitis virus S sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608","Weiss, S.R.; Department of Microbiology, University of Pennsylvania, School of Medicine, Philadelphia, PA 19104, United States; email: weisssr@mail.med.upenn.edu",,,13550284,,JNVIF,"12402164","English","J. Neurovirol.",Article,"Final",Open Access,Scopus,2-s2.0-1842859786
"Truyen U., Blewaska S., Schultheiss U.","35300805300;57213069272;56585916000;","Antiviral potency of interferon-omega (IFN-ω) against selected canine and feline viruses [Untersuchung der antiviralen wirksamkeit von interferon-omega (IFN-ω) gegen ausgewählte viren von hund und katze]",2002,"Praktische Tierarzt","83","10",,"862","865",,19,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036775598&partnerID=40&md5=0fa263508c50252e210feec369ba3a40","Zentralinstitut, Tiergesundheitsdienst Bayern e. V., Senator-Gerauer-Str. 23, 85586 Poing, Germany","Truyen, U., Zentralinstitut, Tiergesundheitsdienst Bayern e. V., Senator-Gerauer-Str. 23, 85586 Poing, Germany; Blewaska, S., Zentralinstitut, Tiergesundheitsdienst Bayern e. V., Senator-Gerauer-Str. 23, 85586 Poing, Germany; Schultheiss, U., Zentralinstitut, Tiergesundheitsdienst Bayern e. V., Senator-Gerauer-Str. 23, 85586 Poing, Germany","In this study the antiviral potency of recombinant feline interferon-omega (IFN-ω) was examined for selected canine and feline viruses in two feline cell lines. Replication of canine parvovius, feline panleukopenia virus, feline calicivirus and two isolates of feline herpesvirus and feline coronavirus in Crandell-Reese feline kidney Zellen (CRFK) and felis catus whole fetus Zellen (fcwf) was assessed by determining virus titers in tissue culture supernatants of infected cells grown with and without 50.000 U / mlinterferon-ω. Virus titers were consistently reduced in IFN-ω treated cells and the effect was more pronounced in fcwf cells. Reduction in virus titers varied between 2 fold (feline calicivirus) and 2 000 fold (feline herpesvirus). The study shows that IFN-ω appears to be an efficient antiviral substance for the antiviral therapy of a broad spectrum of relevant virus diseases of the dog and cat.","Antiviral activity in vitro; Feline herpesvirus; Feline parvovirus; Felines calicivirus; Felines coronavirus; Interferon-ω","antivirus agent; recombinant interferon; recombinant omega interferon; unclassified drug; animal cell; article; cat; cell line; controlled study; dog; drug potency; Herpes virus; nonhuman; Parvovirus; virus infection; virus isolation; virus replication; virus titration","Gonon, V., Duquesne, V., Klonjkowski, B., Monteil, M., Aubert, A., Eloit, M., Clearance of infection in cats naturally infected with feline coronaviruses is associated with an anti-S glycoprotein antibody response (1999) J. Gen. Virol., 80, pp. 2315-2317; Geißler, K., Schneider, K., Platzer, G., Truyen, B., Kaaden, O.-R., Truyen, U., Genetic and antigenic heterogeneity among feline calicivirus isolates from distinct disease clusters (1997) Virus Res., 48, pp. 193-206; Mochizuki, M., Nakatani, H., Yoshida, M., Inhibitory effects of recombinant feline interferon on the replication of feline enteropathogenic viruses in vitro (1994) Vet. Microbiol., 39, pp. 145-152; Parrish, C.R., Mapping specific functions in the capsid structure of canine parvovirus and feline panleukopenia virus using infectious plasmid clones (1991) Virology, 166, pp. 293-307; Truyen, U., Parrish, C.R., Canine and feline host ranges of canine parvovirus and feline panleukopenia virus. Distinct host cell tropisms of each virus in vitro and in vivo (1992) J. Virol., 66, pp. 5399-5408; Truyen, U., Stockhofe-Zurwieden, N., Kaaden, O.-R., Pohlenz, J., A case report: Encephalitis in lions. Pathological and virological findings (1990) Dtsch. Tierärztl. Wschr., 97, pp. 89-91","Truyen, U.; Zentralinstitut, Tiergesundheitsdienst Bayern e. V., Senator-Gerauer-Str. 23, 85586 Poing, Germany; email: uwe.truyen@tgd.bayern.de",,,0032681X,,,,"German","Prakt. Tierarzt",Article,"Final",,Scopus,2-s2.0-0036775598
"Collins A.R.","24439435400;","In vitro detection of apoptosis in monocytes/macrophages infected with human coronavirus",2002,"Clinical and Diagnostic Laboratory Immunology","9","6",,"1392","1395",,33,"10.1128/CDLI.9.6.1392-1395.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036842775&doi=10.1128%2fCDLI.9.6.1392-1395.2002&partnerID=40&md5=4f79d2f316a2bd6da40cd918cc2e3a79","Department of Microbiology, Sch. of Med. and Biomedical Sciences, State Univ. of New York at Buffalo, 3435 Main St., Buffalo, NY 14214, United States","Collins, A.R., Department of Microbiology, Sch. of Med. and Biomedical Sciences, State Univ. of New York at Buffalo, 3435 Main St., Buffalo, NY 14214, United States","Human coronavirus (HCoV) strain 229E infection, but not HCoV strain OC43 infection, of monocytes/macrophages from healthy donors and patients with multiple sclerosis in remission resulted in increased apoptosis, as measured by DNA changes and annexin V staining. Apoptosis correlated with the differential release of infectious virus. HCoV strain 229E titers were 103.5 to 106 50% tissue culture-infective doses (TCID50)/ml, and HCoV strain OC43 titers were only 101.2 to 102.7 TCID50/ml.",,"lipocortin 5; apoptosis; article; controlled study; Coronavirus; DNA determination; human; human cell; macrophage; monocyte; multiple sclerosis; priority journal; tissue culture; virus infection; virus strain; Antigens, Viral; Apoptosis; Cells, Cultured; Coronavirus; Cytokines; Flow Cytometry; Humans; Macrophages; Monocytes; Multiple Sclerosis","Bonavia, A., Arbour, N., Yong, V.W., Talbot, P.J., Infection of primary cultures of human neural cells by human coronaviruses 229E and OC43 (1997) J. Virol., 71, pp. 800-806; Burks, J.S., DeVald, B.V., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934; Collins, A.R., Human macrophages are susceptible to coronavirus OC43 (1998) Adv. Exp. Biol. Med., 440, pp. 635-639; Edwards, J.A., Denis, F., Talbot, P.J., Activation of glial cells by human coronavirus OC43 infection (2000) J. Neuroimmunol., 108, pp. 73-81; Glass, W.G., Liu, M.T., Kuziel, W.A., Lane, T.E., Reduced macrophage infiltration and demyelination of mice lacking the chemokine receptor CCR5 following infection with a neurotropic coronavirus (2001) Virology, 288, pp. 8-17; Ho, W.-Z., Lioy, J., Song, L., Cutilli, J.R., Polin, R.A., Douglas, S.D., Infection of cord blood monocyte-derived macrophages with human immunodeficiency virus type 1 (1992) J. Virol., 66, pp. 573-579; Holmes, K.V., Coronaviruses (2001) Fields Virology, 4th Ed., pp. 1187-1203. , D. M. Knipe and P. M. Howley (ed.). Lippincott, Williams & Wilkins, Philadelphia, Pa; Liu, M.T., Keirstead, H.S., Lane, T.E., Neutralization of the chemokine CXCL10 reduces inflammatory cell invasion and demyelination and improves neurological function in a viral model of multiple sclerosis (2001) J. Immunol., 167, pp. 4091-4097; Oleszak, E.L., Zaczynska, E., Bhattacharjee, M., Butunoi, C., Legido, A., Katsetos, C.D., Inducible nitric oxide synthase and nitrotyrosine are found in monocytes/macrophages and/or astrocytes in acute, but not in chronic, multiple sclerosis (1998) Clin. Diagn. Lab. Immunol., 5, pp. 438-445; Patterson, S., Macnaughton, M.R., Replication of human respiratory coronavirus strain 229E in human macrophages (1982) J. Gen. Virol., 60, pp. 307-314; Pearson, J., Mims, C.A., Differential susceptibility of cultured neural cells to the human coronavirus OC43 (1985) J. Virol., 53, pp. 1016-1019; Perera, L.P., Waldmann, T.A., Activation of human monocytes induces differential resistance to apoptosis with rapid down regulation of caspase-8/FLICE (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 14308-14313; Rautenschlein, S., Sharma, J.M., Immunopathogenesis of haemorrhagic enteritis virus (HEV) in turkeys (2000) Dev. Comp. Immunol., 24, pp. 237-246; Schwarts, T., Fu, L., Lavi, E., Programmed cell death in MHV-induced demyelination (2001) Adv. Exp. Med. Biol., 494, pp. 163-167; Sizun, J., Arbour, N., Talbot, P.J., Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture (1998) J. Virol. Methods, 72, pp. 145-152; Smyth, P.G., Berman, S.A., Burstajn, S., Markers of apoptosis: Methods for elucidating the mechanism of apoptotic cell death from the nervous system (2002) BioTechniques, 32, pp. 648-665; Thanawongnuwech, R., Halbur, P.G., Thacher, E.L., The role of pulmonary intravascular macrophages in porcine reproductive and respiratory syndrome virus infection (2000) Anim. Health Res. Rev., 1, pp. 95-102; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M., Expression of interferon-gamma by a coronavirus defective interfering RNA vector and its effect on viral replication, spread and pathogenicity (1997) Virology, 233, pp. 327-338; Ziaber, J., Baj, Z., Pasnik, J., Chmielewski, H., Tehorzewski, H., Increased expression of neutral endopeptidase (NEP) and aminopeptidase N (APN) on peripheral blood mononuclear cells in patients with multiple sclerosis (2000) Immunol. Lett., 71, pp. 127-129","Collins, A.R.; Department of Microbiology, Sch. of Med. and Biomedical Sciences, State Univ. of New York at Buffalo, 3435 Main St., Buffalo, NY 14214, United States; email: acollins@acsu.buffalo.edu",,,1071412X,,CDIME,"12414783","English","Clin. Diagn. Lab. Immunol.",Article,"Final",Open Access,Scopus,2-s2.0-0036842775
"Yount B., Denison M.R., Weiss S.R., Baric R.S.","6603564156;7101971810;57203567044;7004350435;","Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59",2002,"Journal of Virology","76","21",,"11065","11078",,195,"10.1128/JVI.76.21.11065-11078.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036838992&doi=10.1128%2fJVI.76.21.11065-11078.2002&partnerID=40&md5=8a4b33bd7842c404171fe68eccb340d8","Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States","Yount, B., Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Denison, M.R., Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Weiss, S.R., Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Baric, R.S., Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States","A novel method was developed to assemble a full-length infectious cDNA of the group II coronavirus mouse hepatitis virus strain A59 (MHV-A59). Seven contiguous cDNA clones that spanned the 31.5-kb MHV genome were isolated. The ends of the cDNAs were engineered with unique junctions and assembled with only the adjacent cDNA subclones resulting in an intact MHV-A59 cDNA construct of ∼31.5 kb in length. The interconnecting restriction site junctions that are located at the ends of each cDNA are systematically removed during the assembly of the complete full-length cDNA product, allowing reassembly without the introduction of nucleotide changes. RNA transcripts derived from the full-length MHV-A59 construct were infectious, although transfection frequencies were enhanced 10- to 15-fold in the presence of transcripts encoding the nucleocapsid protein N. Plaque-purified virus derived from the infectious construct replicated efficiently and displayed similar growth kinetics, plaque morphology, and cytopathology in murine cells as did wild-type MHV-A59. Molecularly cloned viruses recognized the MHV receptor (MHVR) for docking and entry, and pretreatment of cells with monoclonal antibodies against MHVR blocked virus entry and replication. Cells infected with molecularly cloned MHV-A59 virus expressed replicase (gene 1) proteins identical to those of laboratory MHV-A59. Importantly, the molecularly cloned viruses contained three marker mutations that had been derived from the engineered component clones. Full-length infectious constructs of MHV-A59 will permit genetic modifications of the entire coronavirus genome, particularly in the replicase gene. The method has the potential to be used to construct viral, microbial, or eukaryotic genomes approaching several million base pairs in length and used to insert restriction sites at any given nucleotide in a microbial genome.",,"complementary DNA; monoclonal antibody; RNA directed RNA polymerase; virus RNA; animal cell; article; base pairing; controlled study; Coronavirus; DNA determination; DNA isolation; DNA modification; DNA replication; gene expression; gene insertion sequence; gene mutation; genetic code; genetic engineering; genetic transfection; genome; Hepatitis virus; molecular cloning; molecular recognition; mouse; nonhuman; priority journal; protein assembly; RNA transcription; virus adsorption; virus genome; virus replication; virus strain; Animals; Cell Line; Cricetinae; DNA, Viral; Mice; Murine hepatitis virus; Phenotype; RNA Replicase; Tumor Cells, Cultured; Viral Proteins","Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic sindbis virus RNA vectors for heterologous gene expression (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 12989-12994; Ahlquist, P., French, R., Janda, M., Loesch-Fries, L.S., Multicomponent RNA plant virus infection derived from cloned viral cDNA (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 7066-7070; Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Baric, R.S., Yount, B., Subgenomic negative-strand function during mouse hepatitis virus infection (2000) J. Virol., 74, pp. 4039-4046; Baric, R.S., Sullivan, E., Hensley, L., Yount, B., Chen, W., Persistent infection promotes cross-species transmissibility of mouse hepatitis virus (1999) J. Virol., 73, pp. 638-649; Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. 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Virol., 74, pp. 10600-10611; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis gene 5b protein is a new virion envelope glycoprotein (1994) Virology, 202, pp. 1018-1023; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Baric, R.S.; Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7435, United States; email: rbaric@sph.unc.edu",,,0022538X,,JOVIA,"12368349","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036838992
"De Haan C.A.M., Volders H., Koetzner C.A., Masters P.S., Rottier P.J.M.","7003682643;6507537974;6602982748;7006234572;7006145490;","Coronaviruses maintain viability despite dramatic rearrangements of the strictly conserved genome organization",2002,"Journal of Virology","76","24",,"12491","12502",,41,"10.1128/JVI.76.24.12491-12502.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036893517&doi=10.1128%2fJVI.76.24.12491-12502.2002&partnerID=40&md5=69449c091864221d985b2e3ff800c7cc","Department of Infectious Diseases, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Virology Division, Department of Infectious Diseases, Yalelaan 1, 3584CL Utrecht, Netherlands","De Haan, C.A.M., Department of Infectious Diseases, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Virology Division, Department of Infectious Diseases, Yalelaan 1, 3584CL Utrecht, Netherlands; Volders, H., Department of Infectious Diseases, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Koetzner, C.A., Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Masters, P.S., Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Rottier, P.J.M., Department of Infectious Diseases, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands","Despite their high frequency of RNA recombination, the plus-strand coronaviruses have a characteristic, strictly conserved genome organization with the essential genes occurring in the order 5′-polymerase (pol)-S-E-M-N-3′. We have investigated the significance of this remarkable conservation by rearrangement of the murine coronavirus genome through targeted recombination. Thus, viruses were prepared with the following gene order: 5′-pol-S-M-E-N-3′, 5′-pol-S-N-E-M-3′, 5′-pol-M-S-E-N-3′, and 5′-pol-E-M-S-N-3′. All of these viruses were surprisingly viable, and most viruses replicated in cell culture with growth characteristics similar to those of the parental virus. The recombinant virus with the gene order 5′-pol-E-M-S-N-3′ was also tested for the ability to replicate in the natural host, the mouse. The results indicate that the canonical coronavirus genome organization is not essential for replication in vitro and in vivo. Deliberate rearrangement of the viral genes may be useful in the generation of attenuated coronaviruses, which due to their reduced risk of generating viable viruses by recombination with circulating field viruses, would make safer vaccines.",,"animal model; animal tissue; article; cell culture; controlled study; Coronavirus; female; gene frequency; gene rearrangement; genome analysis; in vitro study; in vivo study; mouse; nonhuman; priority journal; RNA recombination; virogenesis; virus cell interaction; virus replication; virus survival; Amino Acid Sequence; Animals; Base Sequence; Cells, Cultured; Female; Gene Rearrangement; Genome, Viral; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Murine hepatitis virus; Recombination, Genetic; RNA, Viral; Viral Proteins; Virus Replication","Ball, L.A., Pringle, C.R., Flanagan, B., Perepelitsa, V.P., Wertz, G.W., Phenotypic consequences of rearranging the P, M, and G genes of vesicular stomatitis virus (1999) J. 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Virol., 8, pp. 33-47; Enjuanes, L., Sola, I., Almazan, F., Ortego, J., Izeta, A., Gonzalez, J.M., Alonso, S., Sanchez, C., Coronavirus derived expression systems (2001) J. Biotechnol., 88, pp. 183-204; Fischer, F., Peng, D., Hingley, S.T., Weiss, S.R., Masters, P.S., The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication (1997) J. Virol., 71, pp. 996-1003; Flanagan, E.B., Zamparo, J.M., Ball, L.A., Rodriguez, L.L., Wertz, G.W., Rearrangement of the genes of vesicular stomatitis virus eliminates clinical disease in the natural host: New strategy for vaccine development (2001) J. 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Virol, 40, pp. 350-357; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med., 280, pp. 215-218; Sethna, P.B., Hung, S.L., Brian, D.A., Coronavirus subgenomic minus-strand RNAs and the potential for mRNA replicons (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 5626-5630; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.), Plenum Press, New York, N. Y; Snijder, E.J., Meulenberg, J.J., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Van der Most, R.G., De Groot, R.J., Spaan, W.J., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Marle, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Wertz, G.W., Perepelitsa, V.P., Ball, L.A., Gene rearrangement attenuates expression and lethality of a nonsegmented negative strand RNA virus (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 3501-3506","De Haan, C.A.M.; Virology Division, Department of Infectious Diseases, Yalelaan 1, 3584CL Utrecht, Netherlands; email: x.haan@vet.uu.nl",,,0022538X,,JOVIA,"12438575","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036893517
"Matsuyama S., Taguchi F.","7201442043;7103209890;","Receptor-induced conformational changes of murine coronavirus spike protein",2002,"Journal of Virology","76","23",,"11819","11826",,57,"10.1128/JVI.76.23.11819-11826.2002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036889416&doi=10.1128%2fJVI.76.23.11819-11826.2002&partnerID=40&md5=18d9009ab159191cabce663d3f407924","National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Matsuyama, S., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; Taguchi, F., National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan","Although murine coronavirus mouse hepatitis virus (MHV) enters cells by virus-cell membrane fusion triggered by its spike (S) protein, it is not well known how the S protein participates in fusion events. We reported that the soluble form of MHV receptor (soMHVR) transformed a nonfusogenic S protein into a fusogenic one (F. Taguchi and S. Matsuyama, J. Virol. 76:950-958, 2002). In the present study, we demonstrate that soMHVR induces the conformational changes of the S protein, as shown by the proteinase digestion test. A cl-2 mutant, srr7, of the MHV JHM virus (JHMV) was digested with proteinase K after treatment with soMHVR, and the resultant S protein was analyzed by Western blotting using monoclonal antibody (MAb) 10G, specific for the membrane-anchored S2 subunit. A 58-kDa fragment, encompassing the two heptad repeats in S2, was detected when srr7 was digested after soMHVR treatment, while no band was seen when the virus was untreated. The appearance of the proteinase-resistant fragment was dependent on the temperature and time of srr7 incubation with soMHVR and also on the concentration of soMHVR. Coimmunoprecipitation indicated that the direct binding of soMHVR to srr7 S protein induced these conformational changes; this was also suggested by the inhibition of the changes following pretreatment of soMHVR with anti-MHVR MAb CC1. soMHVR induced conformational changes of the S proteins of wild-type (wt) JHMV cl-2, as well as revertants from srr7, srr7A and srr7B; however, a major proportion of these S proteins were resistant to proteinase K even without soMHVR treatment. The implications of this proteinase-resistant fraction are discussed. This is the first report on receptor-induced conformational changes of the membrane-anchored fragment of the coronavirus S protein.",,"monoclonal antibody; protein S; proteinase K; virus receptor; animal cell; article; concentration (parameters); conformational transition; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein conformation; receptor binding; temperature dependence; virus cell interaction; Western blotting; Animals; Cell Line; Cricetinae; Endopeptidase K; Membrane Fusion; Membrane Glycoproteins; Mice; Murine hepatitis virus; Mutation; Peptide Fragments; Peptide Mapping; Protein Binding; Protein Conformation; Protein Subunits; Receptors, Virus; Solubility; Viral Envelope Proteins","Beauchemin, N., Draber, P., Dveksler, G., Gold, P., Gray-Owen, S., Grunert, F., Hammarstrom, S., Zimmermann, W., Redefined nomenclature for members of the carcinoembryonic antigen family (1999) Exp. 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Virol., 71, pp. 9024-9031; Sattentau, O.J., Moore, J.P., Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding (1991) J. Exp. Med., 174, pp. 407-415; Sodroski, J.G., HIV-1 entry inhibitors in the side pocket (1999) Cell, 99, pp. 243-246; Sturman, L.S., Ricard, C.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments (1985) J. Virol., 56, pp. 904-911; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Taguchi, F., Fusion formation by uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Taguchi, F., Biological functions of mouse hepatitis virus (MHV) spike (S) protein and implication of S protein-MHV receptor interaction in virus virulence (1999) Curr. Top. Virol., 1, pp. 245-252; Taguchi, F., Ikeda, T., Shida, H., Molecular cloning and expression of a spike protein of neurovirulent murine coronavirus JHMV variant cl-2 (1992) J. Gen. Virol., 73, pp. 1065-1072; Taguchi, F., Matsuyama, S., Soluble receptor potentiates receptor-independent infection by murine coronavirus (2002) J. Virol., 76, pp. 950-958; Taguchi, F., Matsuyama, S., Saeki, K., Difference in Bgp-independent fusion activity among mouse hepatitis viruses (1999) Arch. Virol., 144, pp. 2041-2049; Taguchi, F., Shimazaki, Y.K., Functional analysis of an epitope in the S2 subunit of murine coronavirus spike protein: Involvement in fusion activity (2000) J. Gen. Virol., 81, pp. 2867-2871; Taguchi, F., Siddell, S.G., Wege, H., Ter Meulen, V., Characterization of a variant virus selected in rat brain after infection by coronavirus mouse hepatitis virus JHM (1985) J. Virol., 54, pp. 429-435; Taguchi, F., Yamada, A., Fujiwara, K., Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: Enhanced antiviral activity of macrophages (1980) Infect. Immun., 29, pp. 42-49; White, J.M., Viral and cellular membrane fusion proteins (1990) Annu. Rev. Physiol., 52, pp. 675-697; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implication for the requirement of a second factor for virus infection (1992) J. Virol., 66, pp. 6931-6938","Taguchi, F.; National Institute of Neuroscience, NCNP, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan; email: taguchi@ncnp.go.jp",,,0022538X,,JOVIA,"12414924","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0036889416
"Pratelli A., Tinelli A., Decaro N., Camero M., Elia G., Gentile A., Buonavoglia C.","7004884960;6701370203;6701636107;6701658830;7005135633;57216061594;7005623145;","PCR assay for the detection and the identification of atypical canine coronavirus in dogs",2002,"Journal of Virological Methods","106","2",,"209","213",,17,"10.1016/S0166-0934(02)00165-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036883664&doi=10.1016%2fS0166-0934%2802%2900165-9&partnerID=40&md5=e157497806988ab237319e784e18f625","Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy","Pratelli, A., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Tinelli, A., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Decaro, N., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Camero, M., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Elia, G., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Gentile, A., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Buonavoglia, C., Department of Animal Health and Well-being, Faculty of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy","Comparative sequence analysis of the PCR products of the M gene and fragments of the pol1a and pol1b genes of canine coronavirus (CCoV) have demonstrated that two separate clusters of CCoV are present in dogs. This note describes a PCR assay to identify atypical CCoV strains with nucleotide substitutions in the M gene. A total of 177 faecal samples from dogs CCoV positive previously with the PCR assay were analysed. Sixty-two of the 177 samples were amplified with the PCR described in the present study and were thus considered atypical CCoVs. The specificity of the PCR typing assay was confirmed by sequence analysis of the PCR products. © 2002 Elsevier Science B.V. All rights reserved.","Coronavirus; Dog; Genotypes; PCR","nucleotide; article; Coronavirus; dog; feces analysis; nonhuman; polymerase chain reaction; priority journal; sampling; sequence analysis; virus detection; virus identification; virus strain; Animals; Base Sequence; Coronavirus Infections; Coronavirus, Canine; DNA, Viral; Dogs; Feces; Molecular Sequence Data; Polymerase Chain Reaction; Viral Matrix Proteins; Canine coronavirus; Canis familiaris; Coronavirus","Bandai, C., Ishiguro, S., Masuya, N., Hohdatsu, T., Mochizuki, M., Canine coronavirus infections in Japan: Virological and epidemiological aspects (1999) J. Vet. Med. Sci., 61, pp. 731-736; Buonavoglia, C., Sagazio, P., Cirone, F., Tempesta, M., Marsilio, F., Isolamento e caratterizzazione di uno stipite di virus della peritonite infettiva felina (1995) Veterinaria, 9 (1), pp. 91-94; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidoviridales (2000) Virus Taxonomy, pp. 827-834. , M.H.V. Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle, & R.B. Wickner. New York: Academic Press; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) Am. J. Vet. Res., 37, pp. 247-256; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , S.G. Siddell. New York: Plenum Press; Naylor, M.J., Harrison, G.A., Monckton, R.P., McOrist, S., Lehrbach, P.R., Deane, E.M., Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterization of a new Australian isolate (2001) J. Clin. Microbiol., 39, pp. 1036-1041; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) J. Virol. Meth., 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) J. Virol. Meth., 84, pp. 91-94; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Mol. Cell. Probes, 15, pp. 229-233; Pratelli, A., Martella, V., Elia, G., Tempesta, M., Guarda, F., Capucchio, M.T., Carmichael, L.E., Buonavoglia, C., Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus (2001) J. Vet. Med. B, 48, pp. 385-392; Siddell, S.G., The Coronaviridae: An introduction (1995) Coronaviridae, pp. 1-9. , S.G. Siddell. New York: Plenum Press; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.D., Gaskell, C.J., Canine coronavirus infection in the dog following oronasal inoculation (1991) Res. Vet. Sci., 51, pp. 11-18; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Vet. Microbiol., 42, pp. 255-259","Pratelli, A.; Department of Animal Health, Faculty of Veterinary Med. of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,,01660934,,JVMED,"12393151","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0036883664
"Alamelu M.S., Bhat M.N., Sastry K.N.V.","7801528230;57191431532;35860212700;","Sero survey of canine coronavirus infection in dogs",2002,"Indian Journal of Animal Sciences","72","12",,"1096","1097",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036976033&partnerID=40&md5=01e674b02de68874d5ff3af42f1cc251","University of Agricultural Sciences, Bangalore, Karnataka 560 024, India; Dept. of Anim. Husb./Vet. Science, Malavalli-Karnataka 571 430, India","Alamelu, M.S., University of Agricultural Sciences, Bangalore, Karnataka 560 024, India, Dept. of Anim. Husb./Vet. Science, Malavalli-Karnataka 571 430, India; Bhat, M.N., University of Agricultural Sciences, Bangalore, Karnataka 560 024, India; Sastry, K.N.V., University of Agricultural Sciences, Bangalore, Karnataka 560 024, India","Apparently healthy dogs (328) screened for the presence of canine corona virus antibody in the serum samples by indirect haemagglutination test. Two hundred and thirty-nine (72.9%) of the samples were positive of CCV antibody. High antibody titer ranging from 1:80 to 1: 320 were noticed in 35 (10.7%).","Canine coronavirus; Dogs; Sero survey","Cytomegalovirus antibody; virus antigen; antibody detection; antibody titer; article; blood sampling; controlled study; Coronavirus; dog; hemagglutination test; nonhuman; seroprevalence; virus infection; Canine coronavirus; Canis familiaris; Coronavirus; Cytomegalovirus","Calvo, M.M., Marcotegui, M.A., Miro, G., Santurde, G., Simarro, I., Preliminary data on canine coronavirus (1992) Medicina Veterinaria, 9, pp. 157-160. , fide Veterinary Bulletin 62: 5557; Chang, C.F., Lai, S.S., Liu, P.C., Chen, R.S., Tu, C.H., Li, N.J., Lee, L.H., Chen, K.Y., Canine coronaviral infection in Taiwan (1992) Journal of the Chinese Society of Veterinary Medicine, 18, pp. 117-123. , fide Veterinary Bulletin 63: 3112; Helfer-Baker, C., Evermann, J.F., McKeirtnan, A.J., Morrason, W.B., Slack, R.L., Miller, C.W., Serological studies on the incidence of canine enteritis viruses (1980) Canine Practice, 7, pp. 37-42; Herbst, W., Zhang, X.M., Schliesser, T., Seroprevalence of coronavirus infection of dogs in the German Federal Republic (1988) Berliner und Munchener Tierartliche Wockenschrift, 101, pp. 381-383. , fide Veterinary Bulletin 59: 403; Mochizuki, M., Sugiura, R., Akuzawa, M., Micro-neutralisation test with canine coronavirus for detection of coronavirus antibodies in dogs and cats (1987) Japanese Journal of Veterinary Sciences, 49, pp. 563-565; Rimmelzwaan, G.F., Groen, J., Egberink, H., Borst, G.H.A., Uytde Haag, F.G.C.M., Osterhaus, A.D.M.E., The use of enzyme-linked immunosorbent assay systems for serology and antigen detection in parvovirus, coronavirus and rotavirus infections in dogs in The Netherlands (1991) Veterinary Microbiology, 26, pp. 25-40; Tamura, Y., Makie, H., Tanaka, S., An indirect haemagglutination test for the detection of antibodies to Clostridium chauvoei (1985) Veterinary Microbiology, 10, pp. 315-324; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Veterinary Record, 132, pp. 7-11","Alamelu, M.S.; Dept. of Anim. Husb./Vet. Science, Malavalli-Karnataka 571 430, India",,,03678318,,,,"English","Indian J. Anim. Sci.",Article,"Final",,Scopus,2-s2.0-0036976033
"Miguel B., Pharr G.T., Wang C.","7004041418;7006705599;7501632658;","The role of feline aminopeptidase N as a receptor for infectious bronchitis virus",2002,"Archives of Virology","147","11",,"2047","2056",,17,"10.1007/s00705-002-0888-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036904752&doi=10.1007%2fs00705-002-0888-1&partnerID=40&md5=e2f50797da22f823dab3868236eda437","Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, P.O. Box 6100, Mississippi State, MS 39762, United States; Department of Microbiology, Cornell Univ. Duck Res. Laboratory, P.O. Box 217, Easport, NY 11941-0217, United States","Miguel, B., Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, P.O. Box 6100, Mississippi State, MS 39762, United States, Department of Microbiology, Cornell Univ. Duck Res. Laboratory, P.O. Box 217, Easport, NY 11941-0217, United States; Pharr, G.T., Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, P.O. Box 6100, Mississippi State, MS 39762, United States; Wang, C., Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, P.O. Box 6100, Mississippi State, MS 39762, United States","Feline aminopeptidase N (fAPN) has been shown to serve as a receptor for feline, canine, porcine and human coronaviruses. Our objective was to determine if fAPN can serve as a receptor for infectious bronchitis virus (IBV). Feline kidney cells that express fAPN and hamster kidney fibroblasts that do not express fAPN were inoculated with IBV and monitored for replication by indirect fluorescent assay and confocal microscopy and in chicken embryonated eggs. The results showed that the feline cells were permissive to IBV but the hamster cells were not. The hamster cells became permissive to IBV after transfection with a fAPN cDNA suggesting that the feline APN molecule plays a role in IBV entry.",,"Animals; Antigens, CD13; Cats; Cell Line; Chick Embryo; Cricetinae; Female; Infectious bronchitis virus; Kidney; Receptors, Virus; Recombination, Genetic; Transfection; Virus Replication; Avian infectious bronchitis virus; Cricetinae; Felidae; Gallus gallus; Suidae","Antonov, V.K., Vorotyntseva, T.I., Bessmertnaya, L.Y., Mikhailova, A.G., Zilberman, M.I., Role of intestinal brush border membrane aminopeptidase N in dipeptide transport (1984) FEBS Lett, 171, pp. 227-232; Ashmun, R.A., Look, A.T., Metalloprotease activity of CD13/aminopeptidase N on the surface of human myeloid cells (1990) Blood, 75, pp. 462-469; Banner, L.R., Keck, J.G., Lai, M.M., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Barlough, J.E., Stoddart, C.A., Sorresso, G.P., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with canine coronavirus and subsequent challenge with feline infectious peritonitis virus (1984) Lab Anim Sci, 34, pp. 592-597; Barlough, J.E., Johnson-Lussenburg, C.M., Stoddart, C.A., Jacobson, R.H., Scott, F.W., Experimental inoculation of cats with human coronavirus 229E and subsequent challenge with feline infectious peritonitis virus (1985) Can J Comp Med, 49, pp. 303-307; Barnes, K., Kenny, A.J., Turner, A.J., Localization of aminopeptidase N and dipeptidyl peptidase IV in pig striatum and in neuronal and glial cell cultures (1994) Eur J Neurosci, 6, pp. 531-537; Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies amino-peptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J Virol, 71, pp. 734-737; Danielsen, E.M., Hansen, G.H., Cowell, G.M., Biosynthesis of intestinal microvillar proteins. Forskolin reduces surface expression of aminopeptidase (1987) N Eur J Cell Biol, 44, pp. 273-277; Delmas, B., Gelfi, J., Haridon, R.L., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Delmas, B., Gelfi, J., Sjostrom, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1993) Adv Exp Med Biol, 342, pp. 293-298; Delmas, B., Gelfi, J., Kut, E., Sjostrom, H., Noren, O., Laude, H., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) J Virol, 68, pp. 5216-5224; Feracci, H., Bernadac, A., Hovsepian, S., Fayet, G., Maroux, S., Aminopeptidase N is a marker for the apical pole of porcine thyroid epithelial cells in vivo and in culture (1981) Cell Tissue Res, 221, pp. 137-146; Fu, K., Baric, R.S., Evidence for variable rates of recombination in the MHV genome (1992) Virology, 189, pp. 88-102; Gal-Garber, O., Uni, Z., Chicken intestinal aminopeptidase: Partial sequence of the gene, expression and activity (2000) Poult Sci, 79, pp. 41-45; Hansen, G.H., Danielsen, E.M., Sjostrom, H., Noren, O., Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity (1989) Eur J Cell Biol, 49, pp. 154-161; Hegyi, A., Kolb, A.F., Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N (1998) J Gen Virol, 79, pp. 1387-1391; Herrewegh, A.A., Smeenk, I., Horzinek, M.C., Rottier, P.J., De Groot, R.J., Feline coronavirus type II strains 79-1683 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J Virol, 72, pp. 4508-4514; Jackwood, M.W., Hilt, D.A., Production and immunogenicity of multiple antigenic peptide (MAP) constructs derived from the S1 glycoprotein of infectious bronchitis virus (IBV) (1995) Adv Exp Med Biol, 380, pp. 213-219; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of infectious bronchitis virus resulting from recombination among three different strains (1995) Arch Virol, 140, pp. 259-271; Koch, G., Hartog, L., Kant, A., Van Roozelaar, D.J., Antigenic domains on the peplomer protein of avian infectious bronchitis virus: Correlation with biological functions (1990) J Gen Virol, 71, pp. 1929-1935; Kolb, A.F., Maile, J., Heister, A., Siddell, S.G., Characterization of functional domains in the human coronavirus HCV 229E receptor (1996) J Gen Virol, 77, pp. 2515-2521; Kolb, A.F., Hegyi, A., Siddell, S.G., Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N (1997) J Gen Virol, 78, pp. 2795-2802; Kolb, A.F., Hegyi, A., Maile, J., Heister, A., Hagemann, M., Siddell, S.G., Molecular analysis of the coronavirus-receptor function of aminopeptidase N (1998) Adv Exp Med Biol, 440, pp. 61-67; Kottier, S.A., Cavanagh, D., Britton, P., First experimental evidence of recombination in infectious bronchitis virus. Recombination in IBV (1995) Adv Exp Med Biol, 380, pp. 551-556; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kunz, D., Buhling, F., Hutter, H.J., Aoyagi, T., Ansorge, S., Aminopeptidase N (CD13, EC 3.3.4.11.2) occurs on the surface of resting and concanavalin A-stimulated lymphocytes (1993) Biol Chem Hoppe Seyler, 374, pp. 291-296; Kusters, J.G., Jager, E.J., Niesters, H.G., Van der Zeijst, B.A., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Kwon, H.M., Jackwood, M.W., Molecular cloning and sequence comparison of the S1 glycoprotein of the Gray and JMK strains of avian infectious bronchitis virus (1995) Virus Genes, 9, pp. 219-229; Lee, C.W., Jackwood, M.W., Evidence of genetic diversity generated by recombination among avian coronavirus IBV (2000) Arch Virol, 145, pp. 2135-2148; Lendeckel, U., Wex, T., Kahne, T., Frank, K., Reinhold, D., Ansorge, S., Expression of the aminopeptidase N (CD13) gene in the human T cell lines HuT78 and H9 (1994) Cell Immunol, 153, pp. 214-226; Look, A.T., Ashmun, R.A., Shapiro, L.H., Peiper, S.C., Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N (1989) J Clin Invest, 83, pp. 1299-1307; Midorikawa, T., Abe, R., Yamagata, Y., Nakajima, T., Ichishima, E., Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey (1998) Comp Biochem Physiol B Biochem Mol Biol, 119, pp. 513-520; Olsen, J., Kokholm, K., Noren, O., Sjostrom, H., Structure and expression of aminopeptidase N (1997) Adv Exp Med Biol, 421, pp. 47-57; Olsen, J., Kokholm, K., Troelsen, J.T., Laustsen, L., An enhancer with cell-type dependent activity is located between the myeloid and epithelial aminopeptidase N (CD13) promoters (1997) Biochem J, 322, pp. 899-908; Riemann, D., Kehlen, A., Thiele, K., Lohn, M., Langner, J., Induction of aminopeptidase N/CD13 on human lymphocytes after adhesion to fibroblast-like synoviocytes, endothelial cells, epithelial cells, and monocytes/macrophages (1997) J Immunol, 158, pp. 3425-3432; Shapiro, L.H., Ashmun, R.A., Roberts, W.M., Look, A.T., Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells (1991) J Biol Chem, 266, pp. 11999-12007; Song, C.S., Lee, Y.J., Lee, C.W., Sung, H.W., Kim, J.H., Mo, I.P., Izumiya, Y., Mikami, T., Induction of protective immunity in chickens vaccinated with infectious bronchitis virus S1 glycoprotein expressed in a recombinant baculovirus (1998) J Gen Virol, 79, pp. 719-723; Tresnan, D.B., Holmes, K.V., Feline aminopeptidase N is a receptor for all group I coronaviruses (1998) Adv Exp Med Biol, 440, pp. 69-75; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J Virol, 70, pp. 8669-8674; Villegas, P., Purchase, H.G., Titration of biological suspensions (1998) Isolation and Identification of Avian Pathogens, 4th Edn., pp. 124-128. , Hitchner SB, Domermuth CH, Purchase HG, Williams JE (eds). American Association of Avian Pathologists, College Station, Texas; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wang, L., Xu, Y., Collisson, E.W., Experimental confirmation of recombination upstream of the S1 hypervariable region of infectious bronchitis virus (1997) Virus Res, 49, pp. 139-145; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Wang, C.; Department of Basic Sciences, College of Veterinary Medicine, Mississippi State University, P.O. Box 6100, Mississippi State, MS 39762, United States; email: wang@cvm.msstate.edu",,,03048608,,ARVID,"12417943","English","Arch. Virol.",Short Survey,"Final",,Scopus,2-s2.0-0036904752
"Mazumder R., Iyer L.M., Vasudevan S., Aravind L.","7005832714;35551273700;7103140554;7006093805;","Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily",2002,"Nucleic Acids Research","30","23",,"5229","5243",,110,"10.1093/nar/gkf645","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036920683&doi=10.1093%2fnar%2fgkf645&partnerID=40&md5=d07235edd906451e431508c8415a88f5","Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States","Mazumder, R., Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States; Iyer, L.M., Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States; Vasudevan, S., Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States; Aravind, L., Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States","2′,3′ Cyclic nucleotide phosphodiesterases are enzymes that catalyze at least two distinct steps in the splicing of tRNA introns in eukaryotes. Recently, the biochemistry and structure of these enzymes, from yeast and the plant Arabidopsis thaliana, have been extensively studied. They were found to share a common active site, characterized by two conserved histidines, with the bacterial tRNA-ligating enzyme LigT and the vertebrate myelin-associated 2′,3′ phosphodiesterases. Using sensitive sequence profile analysis methods, we show that these enzymes define a large superfamily of predicted phosphoesterases with two conserved histidines (hence 2H phosphoesterase superfamily). We identify several new families of 2H phosphoesterases and present a complete evolutionary classification of this superfamily. We also carry out a structure-function analysis of these proteins and present evidence for diverse interactions for different families, within this superfamily, with RNA substrates and protein partners. In particular, we show that eukaryotes contain two ancient families of these proteins that might be involved in RNA processing, transcriptional co-activation and post-transcriptional gene silencing. Another eukaryotic family restricted to vertebrates and insects is combined with UBA and SH3 domains suggesting a role in signal transduction. We detect these phosphoesterase modules in polyproteins of certain retroviruses, rotaviruses and coronaviruses, where they could function in capping and processing of viral RNAs. Furthermore, we present evidence for multiple families of 2H phosphoesterases in bacteria, which might be involved in the processing of small molecules with the 2′,3′ cyclic phosphoester linkages. The evolutionary analysis suggests that the 2H domain emerged through a duplication of a simple structural unit containing a single catalytic histidine prior to the last common ancestor of all life forms. Initially, this domain appears to have been involved in RNA processing and it appears to have been recruited to perform various other functions in later stages of evolution.",,"2',3' cyclic nucleotide 3' phosphodiesterase; bacterial RNA; histidine; myelin; polyprotein; RNA; transfer RNA; virus protein; virus RNA; Arabidopsis; biochemistry; classification; controlled study; Coronavirus; enzyme active site; enzyme analysis; enzyme mechanism; enzyme structure; eukaryote; gene silencing; genetic conservation; insect; intron; nonhuman; plant; prediction; priority journal; progenote; protein domain; protein family; protein function; protein interaction; Retrovirus; review; RNA capping; RNA processing; RNA splicing; Rotavirus; sequence analysis; signal transduction; structure activity relation; transcription initiation; vertebrate; yeast; 2',3'-Cyclic-Nucleotide Phosphodiesterases; Amino Acid Sequence; Archaea; Bacteria; Binding Sites; Catalytic Domain; Conserved Sequence; Eukaryotic Cells; Evolution, Molecular; Histidine; Models, Molecular; Molecular Sequence Data; Phylogeny; Protein Structure, Tertiary; Sequence Alignment; Structure-Activity Relationship; Viruses; Arabidopsis; Arabidopsis thaliana; Bacteria (microorganisms); Coronavirus; Eukaryota; Hexapoda; Insecta; RNA viruses; Rotavirus; unidentified retrovirus; Vertebrata","Aravind, L., Koonin, E.V., The HD domain defines a new superfamily of metal-dependent phosphohydrolases (1998) Trends Biochem. 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J., 351, pp. 527-535; van Nues, R.W., Beggs, J.D., Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae (2001) Genetics, 157, pp. 1451-1467; Fraser, I.D., Tavalin, S.J., Lester, L.B., Langeberg, L.K., Westphal, A.M., Dean, R.A., Marrion, N.V., Scott, J.D., A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events (1998) EMBO J., 17, pp. 2261-2272; Trendelenburg, G., Hummel, M., Riecken, E.O., Hanski, C., Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain (1996) Biochem. Biophys. Res. Commun., 225, pp. 313-319; Aravind, L., Watanabe, H., Lipman, D.J., Koonin, E.V., Lineage-specific loss and divergence of functionally linked genes in eukaryotes (2000) Proc. Natl Acad. Sci. USA, 97, pp. 11319-11324; Shuman, S., Schwer, B., RNA capping enzyme and DNA ligase: A superfamily of covalent nucleotidyl transferases (1995) Mol. Microbiol., 17, pp. 405-410; Chen, D., Luongo, C.L., Nibert, M.L., Patton, J.T., Rotavirus open cores catalyze 5′-capping and methylation of exogenous RNA: Evidence that VP3 is a methyltransferase (1999) Virology, 265, pp. 120-130; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-219; Metcalf, W.W., Wanner, B.L., Evidence for a fourteen-gene, phnC to phnP locus for phosphonate metabolism in Escherichia coli (1993) Gene, 129, pp. 27-32; Wattenhofer, M., Shibuya, K., Kudoh, J., Lyle, R., Michaud, J., Rossier, C., Kawasaki, K., Berry, A., Isolation and characterization of the UBASH3A gene on 21q22.3 encoding a potential nuclear protein with a novel combination of domains (2001) Hum. Genet., 108, pp. 140-147; Pawson, J., Scott, J.D., Signaling through scaffold, anchoring and adaptor proteins (1997) Science, 278, pp. 2075-2080; Hofmann, K., Bucher, P., The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway (1996) Trends Biochem. Sci., 21, pp. 172-173; Kruh, G.D., Zeng, H., Rea, P.A., Liu, G., Chen, Z.S., Lee, K., Belinsky, M.G., MRP subfamily transporters and resistance to anticancer agents (2001) J. Bioenerg. Biomembr., 33, pp. 493-501; Doolittle, R.F., Handy, J., Evolutionary anomalies among the aminoacyl-tRNA synthetases (1998) Curr. Opin. Genet. Dev., 8, pp. 630-636; Leipe, D.D., Wolf, Y.I., Koonin, E.V., Aravind, L., Classification and evolution of P-loop GTPases and related ATPases (2002) J. Mol. Biol., 317, pp. 41-72; Aravind, L., Koonin, E.V., DNA polymerase beta-like nucleotidyltransferase superfamily: Identification of three new families, classification and evolutionary history (1999) Nucleic Acids Res., 27, pp. 1609-1618","Aravind, L.; Natl. Center for Biotechnol. Info., National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, United States; email: aravind@ncbi.nlm.nih.gov",,,03051048,,NARHA,"12466548","English","Nucleic Acids Res.",Review,"Final",Open Access,Scopus,2-s2.0-0036920683
"Pratelli A., Elia G., Martella V., Tinelli A., Decaro N., Marsilio F., Buonavoglia D., Tempesta M., Buonavoglia C.","7004884960;7005135633;7003300496;6701370203;6701636107;55788078800;7004335810;7005599031;7005623145;","M gene evolution of canine coronavirus in naturally infected dogs",2002,"Veterinary Record","151","25",,"758","761",,29,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037153957&partnerID=40&md5=12adb8abea5fc77f731d1126e60184ee","Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Dept. of Animal Pathol./Biotechnol., Faculty of Veterinary Medicine, University of Teramo, via Crucioli 122, 64100 Teramo, Italy; Dept. of Pathology/Infectious Dis., Faculty of Veterinary Medicine, University of Messina, via S. Cecilia 30, 98123 Messina, Italy","Pratelli, A., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Elia, G., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Martella, V., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Tinelli, A., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Decaro, N., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Marsilio, F., Dept. of Animal Pathol./Biotechnol., Faculty of Veterinary Medicine, University of Teramo, via Crucioli 122, 64100 Teramo, Italy; Buonavoglia, D., Dept. of Pathology/Infectious Dis., Faculty of Veterinary Medicine, University of Messina, via S. Cecilia 30, 98123 Messina, Italy; Tempesta, M., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy; Buonavoglia, C., Dept. of Animal Hlth./Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy","Two stray pups (A and B), three and five months old, respectively, both naturally infected with canine coronavirus (CCoV), were studied for 180 days. The virus was detected intermittently in the pups' faeces by PCR for periods of 156 and 146 days, respectively. Sequence analysis of a fragment of the gene encoding the M protein revealed that the viruses detected at the onset of the infection were very similar to typical strains of CCoV, whereas from 42 days after infection in pup A and 40 days after infection in pup B the viruses had nucleotide and amino acid mutations resembling sequences in feline coronavirus.",,"amino acid; M protein; nucleotide; amino acid sequence; animal cell; article; cat; controlled study; Coronavirus; dog disease; feces analysis; gene mutation; gene sequence; genetic code; molecular evolution; nonhuman; nucleotide sequence; polymerase chain reaction; sequence analysis; sequence homology; virus detection; virus infection; virus strain; Animals; Base Sequence; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Feces; Molecular Sequence Data; Polymerase Chain Reaction; Animalia; Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline coronavirus; Felis catus","Appel, M.J., Copper, B.J., Greisen, H., Scott, F., Carmichael, L.E., Canine viral enteritis I. Status report on corona- and parvo-like viral enteritides (1979) Cornell Veterinarian, 69, pp. 123-133; Bandai, C., Ishiguro, S., Masuya, N., Hohdatsu, T., Mochizuki, M., Canine coronavirus infections in Japan: Virological and epidemiological aspects (1999) Journal of Veterinary Medical Science, 61, pp. 731-736; Binn, L.N., Lazar, E.C., Keenan, K.P., Huxsoll, DL., Marchwicki, B.S., Strano, A.J., Recovery and characterization of a coronavirus from military dogs with diarrhoea (1974) Proceedings of the 78th Meeting of the US Animal Health Association, pp. 359-366. , Roanoke, USA, October 1974; Binn, L.N., Alford, J.P., Marchwicki, R.H., Keefe, TJ., Beattie, R.J., Wall, H.G., Studies of respiratory disease in random-source laboratory dogs (1979) Laboratory Animal Science, 29, pp. 48-52; Carmichael, L.E., Binn, L.N., New enteric viruses in the dog (1981) Advances in Veterinary Science and Comparative Medicine, 25, pp. 1-37; Cartwright, S., Lucas, M., Vomiting and diarrhoea in dogs (1972) Veterinary Record, 91, pp. 571-572; Childs, J.C., Stohlman, S.A., Kingsford, L., Russell, R., Antigenic relationships of murine coronaviruses (1983) Archives of Virology, 78, pp. 81-87; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van Der Ziejst, B.A.M., Spaan, W.J.M., cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) Journal of General Virology, 68, pp. 2639-2646; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Seminars in Virology, 8, pp. 33-47; Dolja, V.V., Carrington, J.C., Evolution of positive-strand RNA viruses (1992) Seminars in Virology, 3, pp. 315-326; Egberts, H.J.A., Brinkhoff, M.G.M., Mouwen, J.M.V.M., Van Dijk, J.E., Koninkx, J.F.J.G., Biology and pathology of the intestinal M-cell. A review (1985) Veterinary Quarterly, 7, pp. 333-337; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidovirales (2000) Virus Taxonomy, pp. 827-834. , 7th edn. Eds M. H. V. Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carstens, M, K. Estes, S. M, Lemon, J. Maniloff, M. A. Mayo, D, J. McGeoch, C. R. Pringle, R. B. Wickner. New York, Academic Press; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) Journal of General Virology, 73, pp. 2849-2862; Jarvis, T.C., Kirkegaard, K., The polymerase in its labyrinth: Mechanisms and implications of RNA recombination (1991) Trends in Genetics, 7, pp. 186-191; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine cronavirus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) American Journal of Veterinary Research, 37, pp. 247-256; Lavi, E., Fishman, P.S., Highkin, M.K., Weiss, S.R., Limbic encephalitis after inhalation of a murine coronavirus (1988) Laboratory Investigation, 58, pp. 31-36; Lefevre, M.E., Hammer, R., Joel, D.D., Macrophages of the mammalian small intestine: A review (1979) Journal of the Reticuloendothelial Society, 26, pp. 553-573; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) In the Coronaviridae, pp. 33-49. , Ed S. G. Siddell. New York, Plenum Press; Pedersen, N.C., Evermann, J.F., McKeirnan, A.J., Ott, R.L., Pathogenicity studies of feline coronavirus isolates 79-1146 and 79-1683 (1984) American Journal of Veterinary Research, 45, pp. 2580-2585; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) Journal of Virological Methods, 84, pp. 91-94; Pratelli, A., Ella, G., Martella, V., Palmieri, A., Cirone, F., Tinelli, A., Corrente, M., Buonavoglia, C., Prevalence of canine coronavirus antibodies in dogs in the south of Italy by enzyme-linked immunosorbent assay (2002) Journal of Virological Methods, 102, pp. 67-71; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Molecular and Cellular Probes, 15, pp. 229-233; Pratelli, A., Martella, V., Elia, G., Tempesta, M., Guarda, F., Capucchio, M.T., Carmichael, L.E., Buonavoglia, C., Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus (2001) Journal of Veterinary Medicine B, 48, pp. 385-392; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) Journal of Virological Methods, 80, pp. 11-15; Reynolds, D.J., Debney, T.G., Hall, G.A., Thomas, L.H., Parsons, K.R., Studies of the relationship between coronaviruses from the intestinal and respiratory tracts of calves (1985) Archives of Virology, 8, pp. 71-83; Risco, C., Antón, I.M., Sune, C., Pedregosa, A.M., Martín-alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion (1995) Journal of Virology, 69, pp. 5269-5277; Siddell, S.G., The coronaviridae, an introduction (1995) The Coronaviridae, pp. 1-10. , Ed S. G. Siddell. New York, Plenum Press; Takeuchi, A., Binn, L.N., Jervis, H.R., Keenan, K.P., Hildebrandt, P.K., Valas, R.B., Bland, F.F., Electron microscope study of experimental enteric infection on neonatal dogs with a canine coronavirus (1976) Laboratory Investigation, 34, pp. 539-549; Tennant, B.J., Gaskell, R.M., Gaskell, C.J., Studies on the survival of canine coronavirus under different environmental conditions (1994) Veterinary Microbiology, 42, pp. 255-259; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Veterinary Record, 132, pp. 7-11; Tennant, B.J., Gaskell, R.M., Kelly, D.F., Carter, S.C., Gaskell, C.J., Canine coronavirus infection in dogs following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18; Thomas, L.H., Gourlay, R.N., Stott, E.J., Howard, C.J., Bridger, H.C., A search for new microorganisms in calf pneumonia by the inoculation of gnotobiotic calves (1982) Research in Veterinary Science, 33, pp. 170-182; Underdahl, N.R., Mebus, A., Stair, E.L., Rhodes, M.B., McGill, L.D., Twiehaus, M.J., Isolation of transmissible gastroenteritis virus from lungs of marker-weight swine (1974) American Journal of Veterinary Research, 35, pp. 1209-1216; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Pathologic changes and immunofluorescence (1981) American Journal of Veterinary Research, 49, pp. 558-560","Pratelli, A.; Dept. of Animal Health/Wellbeing, Faculty of Veterinary Medicine, University of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Italy",,,00424900,,VETRA,"12521247","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0037153957
"Yang J., Wang Z.H., Chen J.J., Hou J.L.","57192453306;56331927200;35204859000;7401966390;","Clinical detection of polymerase gene of SARS-associated coronavirus",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","5",,"424","427",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042657444&partnerID=40&md5=2f033987d8dec47a8eaf308a9c08fe72","Department of Infectious Diseases, Nanfang Hospital, First Military Medical University, Guangzhou, 510515, China","Yang, J., Department of Infectious Diseases, Nanfang Hospital, First Military Medical University, Guangzhou, 510515, China; Wang, Z.H., Department of Infectious Diseases, Nanfang Hospital, First Military Medical University, Guangzhou, 510515, China; Chen, J.J., Department of Infectious Diseases, Nanfang Hospital, First Military Medical University, Guangzhou, 510515, China; Hou, J.L., Department of Infectious Diseases, Nanfang Hospital, First Military Medical University, Guangzhou, 510515, China","OBJECTIVE: To analyze the heterogeneity of polymerase gene fragment of SARS-associated coronavirus from SARS patients, and establish a RT-PCR method for detecting SARS-associated coronavirus. METHODS: RT-PCR was performed using SARS coronavirus-specific primers to amplify the polymerase gene fragment of SARS-associated coronavirus from specimens of suspected and established SARS cases. The amplicons were cloned and sequenced. All the obtained sequences were compared with the sequence of published SARS-associated coronavirus, and alignment was proceeded with other coronavirus sequences. RESULTS: Specific amplicons can be amplified from the sputum samples, throat swab and plasma of most SARS patients, and 8 were random selected and sequenced. All of them possessed 100% homology with the published SARS-associated coronavirus sequence, while all the negative controls were RT-PCR negative. Nucleotide-sequence and amino acid-sequence alignment of the fragment BNI109 with other six known coronavirus show that the fragment BNI109 is more close to bovine coronavirus(BCV) and murine hepatitis virus(MHV). The BNI109 fragment showed 75% homology with BCV and MHV at amino acid level. CONCLUSION: The polymerase fragment BNI109 of SARS coronavirus is highly conservative and is suitable for detecting SARS-associated coronavirus using RT-PCR method.",,"RNA directed RNA polymerase; amino acid sequence; animal; article; genetics; human; isolation and purification; molecular genetics; nucleotide sequence; reverse transcription polymerase chain reaction; SARS coronavirus; Amino Acid Sequence; Animals; Base Sequence; Humans; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA Replicase; SARS Virus",,"Yang, J.email: yangjie@fimmu.com",,,10002588,,,"12754118","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-0042657444
"Tan X.Y., Fan Z., Wang H.J., Shi L., Yin B., Ni A.P., Qin C., Zou K., Shen Y., Yuan J.G., Qiang B.Q., Peng X.Z.","55248826200;36119952800;7501748483;57199773830;7101984277;7004451149;7102688076;57205864718;57215789155;7403401529;7005510394;7401594285;","Cloning, expression and purification of SARS coronavirus PUMC2 strain nucleocapsid protein",2003,"Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae","25","5",,"504","507",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2942648895&partnerID=40&md5=fd263f87df8c40635055aaa7a5dd8a8c","National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China","Tan, X.Y., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Fan, Z., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Wang, H.J., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Shi, L., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Yin, B., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Ni, A.P., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Qin, C., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Zou, K., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Shen, Y., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Yuan, J.G., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Qiang, B.Q., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China; Peng, X.Z., National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing, 10005, China","OBJECTIVE: To clone, express and purify nucleocapsid protein from SARS coronavirus PUMC2 strain. METHODS: According to the published SARS coronavirus genome sequences, the full length cDNA of N protein from SARS coronavirus PUMC2 strain was cloned by RT-PCR and the cDNA was cloned into the pET32a expression vector. The recombinant N protein was expressed in E. coli BL21 (DE3), and purified by Ni(2+)-NTA. RESULTS: Prokaryoticly expressed and purified N protein of SARS coronavirus PUMC2 strain was obtained. CONCLUSIONS: The SARS coronavirus recombinant N protein obtained by genetic engineering methods can be used for further functional study of SARS coronavirus N protein.",,"complementary DNA; hybrid protein; nucleocapsid protein; nucleocapsid protein, Coronavirus; virus DNA; virus RNA; amino acid sequence; article; biosynthesis; DNA sequence; Escherichia coli; gene vector; genetics; isolation and purification; molecular cloning; molecular genetics; nucleotide sequence; reverse transcription polymerase chain reaction; SARS coronavirus; virus genome; Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Complementary; DNA, Viral; Escherichia coli; Genetic Vectors; Genome, Viral; Molecular Sequence Data; Nucleocapsid Proteins; Recombinant Fusion Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sequence Analysis, DNA",,"Tan, X.Y.",,,1000503X,,,"14650145","Chinese","Zhongguo Yi Xue Ke Xue Yuan Xue Bao",Article,"Final",,Scopus,2-s2.0-2942648895
"Zhou B.P., Chen X.C., Wang H.S., Li M.Z., Hu Y.W., Du F., Xu L.M., Yang G.L.","7401906727;55109589100;8453456500;26662456500;56163053400;7101840604;35212429100;7405754750;","Identification and molecular cloning and sequence analysis of a novel coronavirus from patients with SARS by RT-PCR",2003,"Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology","17","2",,"137","139",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0842343391&partnerID=40&md5=7bd22c47e247f6c4d7a88bdd334c325d","Shenzhen Eastlake Hospital, Shenzhen, 518020, China","Zhou, B.P., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Chen, X.C., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Wang, H.S., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Li, M.Z., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Hu, Y.W., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Du, F., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Xu, L.M., Shenzhen Eastlake Hospital, Shenzhen, 518020, China; Yang, G.L., Shenzhen Eastlake Hospital, Shenzhen, 518020, China","OBJECTIVE: To investigate the etiologic agents of the SARS and develop diagnostic method for this disease. METHODS: Thirty-six nasopharyngeal aspirate specimens from 27 patients with SARS in Shenzhen were collected. The samples were aliquotted to three parts and subjected to molecular assays for human metapneumovirus, chlamydia and a novel coronavirus, which was reported recently to be the etiologic agent of SARS. Nested RT-PCR was used to amplify the RNA polymerase gene of the novel coronavirus and the PCR products were sequenced directly or after cloned to pMD18-T vector. RESULTS: Human metapneumovirus and chlamydia genes were detected in none of the specimens using the RT-PCR and nested-PCR, respectively. The novel coronavirus gene were amplified in 6 of 36 specimens, the sequence analysis indicated that this novel coronavirus is unrelated to any other coronavirus reported previously. The nucleotide and deduced amino acid alignment between this coronavirus and others was not more than 40% and 70% to 82%, respectively, while the nucleotide sequence cloned from the 6 patients were identical. CONCLUSIONS: The SARS patients in Shenzhen were infected with coronavirus and this novel coronavirus is associated with SARS. The sequence analysis indicated that the coronavirus from SARS patients in Shenzhen is the same as that identified from other areas such as Canada and Hong Kong. A specific diagnostic nested RT-PCR was developed to identify this novel coronavirus infection.",,"virus DNA; virus RNA; adolescent; adult; aged; article; child; DNA sequence; female; genetic variability; genetics; human; isolation and purification; male; middle aged; molecular cloning; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; virology; Adolescent; Adult; Aged; Child; Cloning, Molecular; DNA, Viral; Female; Humans; Male; Middle Aged; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome; Variation (Genetics)",,"Zhou, B.P.",,,10039279,,,"12869994","Chinese","Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0842343391
"Navas-Martin S., Weiss S.R.","10043670100;57203567044;","SARS: Lessons Learned from Other Coronaviruses",2003,"Viral Immunology","16","4",,"461","474",,29,"10.1089/088282403771926292","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347992844&doi=10.1089%2f088282403771926292&partnerID=40&md5=e5dec6c5360f96fe40428a8ffd0e7021","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Navas-Martin, S., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA, United States, Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States","The identification of a new coronavirus as the etiological agent of severe acute respiratory syndrome (SARS) has evoked much new interest in the molecular biology and pathogenesis of coronaviruses. This review summarizes present knowledge on coronavirus molecular biology and pathogenesis with particular emphasis on mouse hepatitis virus (MHV). MHV, a member of coronavirus group 2, is a natural pathogen of the mouse; MHV infection of the mouse is considered one of the best models for the study of demyelinating disease, such as multiple sclerosis, in humans. As a result of the SARS epidemic, coronaviruses can now be considered as emerging pathogens. Future research on SARS needs to be based on all the knowledge that coronavirologists have generated over more than 30 years of research.",,"envelope protein; guanine nucleotide binding protein; M protein; RNA directed RNA polymerase; spike protein; unclassified drug; virus protein; Coronavirus; demyelinating disease; epidemic; human; molecular biology; multiple sclerosis; Murine hepatitis coronavirus; open reading frame; review; SARS coronavirus; severe acute respiratory syndrome; taxonomy; virology; virus gene; virus pathogenesis; virus replication; Coronavirus; Murinae; Murine hepatitis virus; RNA viruses; SARS coronavirus","Abbott, A., Cyranoski, D., Biologists seek to head off future sources of infection (2003) Nature, 423, p. 3; Almazan, F., Gonzalez, J.M., Penzes, Z., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. 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Virol., 76, pp. 11065-11078; Yu, X., Bi, W., Weiss, S.R., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zelus, B.D., Schickli, J.H., Blau, D.M., Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8 (2003) J. Virol., 77, pp. 830-840","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Mary Ann Liebert Inc.",08828245,,VIIME,"14733734","English","Viral Immunol.",Review,"Final",,Scopus,2-s2.0-0347992844
"Li L.H., Shi Y.L., Li P., Xu D.X., Wan G.P., Gu X.Q., Zhang X.L., Ma Q.J., Cao C.","55768805700;57199386357;57214070350;57198944528;57206189748;56295552900;35551884700;7402813647;7401501779;","Detection and analysis of SARS coronavirus-specific antibodies in sera from non-SARS children",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","10",,"1085","1087",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542435964&partnerID=40&md5=d25531b3fc43903e9e845363ba088c46","Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China","Li, L.H., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Shi, Y.L., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Li, P., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Xu, D.X., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Wan, G.P., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Gu, X.Q., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Zhang, X.L., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Ma, Q.J., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China; Cao, C., Department of Clinical Laboratory, Guangzhou General Hospital of Guangzhou Command, Guangzhou, 510010, China","OBJECTIVE: To examine the presence of severe acute respiratory syndrome (SARS) coronavirus-specific antibodies in the sera from non-SARS children. METHODS: Indirect immunofluorescent assay and double-antigen sandwich enzyme-linked immunosorbent assay (ELISA) were used to detect the virus-specific antibodies in sera of 1,060 non-SARS children in Guangzhou. RESULTS: All the serum samples from the 1,060 non-SARS children were negative for both IgG and IgM antibodies against SARS coronavirus as determined by indirect immunofluorescent assay, with only two serum samples showing weak positivity for SARS coronavirus-specific antibodies identified by double-antigen sandwich ELISA. CONCLUSION: No SARS coronavirus-specific antibody are present in the sera of non-SARS children.",,"virus antibody; adolescent; article; blood; child; enzyme linked immunosorbent assay; female; fluorescent antibody technique; human; immunology; infant; male; newborn; preschool child; SARS coronavirus; Adolescent; Antibodies, Viral; Child; Child, Preschool; Enzyme-Linked Immunosorbent Assay; Female; Fluorescent Antibody Technique, Indirect; Humans; Infant; Infant, Newborn; Male; SARS Virus",,"Li, L.H.email: linhaili@hotmail.com",,,10002588,,,"14559701","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-1542435964
"Ni A.P., Wang Z., Liu Y., Liu S.D., Han Y.H., Shen Y., Qiang B.Q.","7004451149;7410037669;56253506700;56099611400;57199690746;57131490100;7005510394;","Isolation and identification of SARS-coronavirus in nasal and throat swabs collected from clinically diagnosed SARS patients",2003,"Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae","25","5",,"520","524",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2942640462&partnerID=40&md5=6368d8e1ccee56b4617a86ac74680b6c","Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China","Ni, A.P., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Wang, Z., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Liu, Y., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Liu, S.D., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Han, Y.H., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Shen, Y., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China; Qiang, B.Q., Department of Clinical Laboratory, PUMC Hospital, CAMS and PUMC, Beijing, 100730, China","OBJECTIVE: To isolate and identify SARS-coronavirus in nasal and throat swabs collected from clinically diagnosed severe acute respiratory syndrome (SARS) patients. METHODS: Nasal and throat swab specimens were inoculated onto well of 24-well plate containing confluent monolayers of Vero and MRC-5 cells. Isolates were identified with serology, electron microscopy and genome sequence. RESULTS: One hundred and fifty-eight nasal and throat swabs specimens from 79 SARS patients in Peking Union Medical College Hospital between April and May, 2003 were cultured for SARS-coronavirus. Cytopathic effect (CPE) was found in three nasal swab specimens inoculated in Vero cells. Acute and convalescent phase serum specimens collected from SARS patients were found with seroconversions and/or a fourfold or greater rises in indirect fluorescence antibodies (IgG and IgM) titers when the 3 isolates (infected Vero cells) were used as antigen. Coronavirus was observed in the culture supernatant by negative-stain electron microscopy. Genome sequence confirmed the isolates were SARS-coronavirus. CONCLUSIONS: The 3 isolates from nasal and throat swabs samples collected from 79 clinically diagnosed SARS patients were SARS coronavirus.",,"virus antibody; adolescent; adult; aged; article; blood; female; human; immunology; isolation and purification; laboratory diagnosis; larynx; male; middle aged; nasopharynx; SARS coronavirus; severe acute respiratory syndrome; virology; Adolescent; Adult; Aged; Aged, 80 and over; Antibodies, Viral; Female; Humans; Larynx; Male; Middle Aged; Nasopharynx; SARS Virus; Severe Acute Respiratory Syndrome; Specimen Handling",,"Ni, A.P.email: niap@csc.pumch.ac.cn",,,1000503X,,,"14650149","Chinese","Zhongguo Yi Xue Ke Xue Yuan Xue Bao",Article,"Final",,Scopus,2-s2.0-2942640462
"Tobler K., Ackermann M., Griot C.","6701508835;7102624625;7003744370;","SARS-agent and lessons to be learned from pathogenic coronaviruses of animals [SARS, mögliche zoonose im spannungsfeld tierpathogener coronaviren]",2003,"Schweizer Archiv fur Tierheilkunde","145","7",,"316","322",,6,"10.1024/0036-7281.145.7.316","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141832180&doi=10.1024%2f0036-7281.145.7.316&partnerID=40&md5=f012ea7d91fa9e08d487ad27ae7c8d49","Virologisches Institut, Universität Zürich, Switzerland; Inst. F. Viruskrankheiten I., Mittelhäusern, Switzerland; Virologisches Institut, Veterinärmedizinische Fak., Universität Zürich, Winterthurerstrasse 266a, 8057 Zürich, Switzerland","Tobler, K., Virologisches Institut, Universität Zürich, Switzerland; Ackermann, M., Virologisches Institut, Universität Zürich, Switzerland, Virologisches Institut, Veterinärmedizinische Fak., Universität Zürich, Winterthurerstrasse 266a, 8057 Zürich, Switzerland; Griot, C., Inst. F. Viruskrankheiten I., Mittelhäusern, Switzerland","Severe acute respiratory syndrome (SARS) is an emerging disease, which was first recognized in Guangdong Province, China, in November 2002. In the meantime, SARS has been recognized in patients on all five continents. A novel coronavirus, which is not related to the hitherto known coronaviruses, has been proven to be associated with the disease. Our genomic analyses strongly suggest that the new SARS-coronavirus did not emerge through mutation or recombination and that it has probably been transmitted from a so far not identified animal species to humans. Therefore, it is most likely that SARS virus is a zoonotic agent. A broad body of knowledge originating from research in veterinary medicine indicates that development of vaccines against the SARS-coronavirus may be problematic.The potential danger of such vaccines should not be neglected during the process of vaccine development.","Coronavirus; Emerging disease; SARS; Vaccine; Zoonosis","virus vaccine; virus vaccine; genome analysis; nonhuman; review; SARS coronavirus; severe acute respiratory syndrome; veterinary medicine; virus mutation; virus recombination; zoonosis; animal; communicable disease; disease transmission; human; immunology; pathogenicity; severe acute respiratory syndrome; virology; zoonosis; Animalia; Coronavirus; SARS coronavirus; Animals; Communicable Diseases, Emerging; Humans; SARS Virus; Severe Acute Respiratory Syndrome; Viral Vaccines; Zoonoses","(2003) SARS-associated Coronavirus, , http://www.bcgsc.bc.ca, 13. April; (2003) Coronavirus Never before Seen in Humans Is the Cause of SARS, , http://www.who.int/csr/sarsarchive/2003_04_16/en/, 16. April; Benbacher, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B., Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus (1997) J. Virol., 71, pp. 734-737; Bridgen, A., Kocherhans, R., Tobler, K., Carvajal, A., Ackermann, M., Further analysis of the genome of porcine epidemic diarrhoea virus (1998) Coronaviruses and Arteriviruses, pp. 781-786. , Eds. Enjuanes et al., Plenum Press, NewYork; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Eng. J. Med., , http://www.nejm.org/earlyrelease/sars.asp; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Lande, H., Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF (1994) Virology, 198, pp. 466-476; Fulker, R., Wasmoen, T., Atchinson, R., Chu, H.-J., Acree, W., Efficacy of an inactivated vaccine against clinical disease caused by canine coronavirus (1995) Corona- and Related Viruses, pp. 229-234. , Eds. P.J. Talbot and G.A. Levy, Plenum Press, NewYork; Gaertner, D., Compton, S., Winograd, D., Letter to the editor (1993) Lab. Anim. Sci., 5, pp. 403-404; Griot, C., (2002) Emerging Diseases: Wahrnehmung und Realität am Beispiel West Nil Fieber, , http://www.animal-health-online.de; Haas, W., Buchholz, U., Schnitzler, J., Mielke, M., Amman, A., Schweres akutes respiratorisches Snydrom (SARS) unklarer Ursache (2003) Deutsches Ärzteblatt, 100, p. 860; Haijema, B.J., Volders, H., Rottier, P.J.M., Switching species tropism: An effective way to manipulate the feline coronavirus genome (2003) J. Virol., 8, pp. 4528-4583; Horzinek, M.C., Lutz, H., An update on feline infectious peritonitis (2001) Vet. Sci. Tom., p. 1. , http://www.vetscite.org/cgi-bin/pw.exe/vst/reviews/index_1_0800.htm; Jemmi, T., Danuser, J., Griot, C., Zoonosen als Risiko im Umgang mit Tieren und tierischen Produkten (2000) Schweiz. Arch. Tierheilk., 142, pp. 665-671; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., , http://www.nejm.org/earlyrelease/sars.asp; Lai, M.C., Holmes, K., Coronaviridae: The viruses and their replication (2001) Fields Virology, pp. 1163-1185. , Eds. Fields et al, Lippincott Williams and Wikins; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Eng. J. Med., , http://www.nejm.org/earlyrelease/sars.asp; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, , http://image.thelancet.com/extras/03art3477web.pdf; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N. Eng. J. Med., , http://www.nejm.org/early-release/sars.asp; (2003) SARS - Worldwide, (51). , http://www.promedmau.org, 16. April Archiv Nr. 20030416.0925; Siddell, S.G., The coronaviridae, an introduction (1995) The Coronaviridae, pp. 1-10. , Ed. S. G. Siddell, Plenum Press, New York; Tobler, K., Ackermann, M., Comparison of the di- and trinucleotide frequencies from the genomes of nine different coronaviruses (1998) Coronaviruses and Arteriviruses, pp. 801-804. , Eds. Enjuanes et al., Plenum Press, New York; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., , http://www.nejm.org, March 31, 2003; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373","Ackermann, M.; Virologisches Institut, Veterinärmedizinische Fak., Universität Zürich, Winterthurerstrasse 266a, 8057 Zürich, Switzerland; email: ma@vetvir.unizh.ch",,"Verlag Hans Huber AG",00367281,,SATHA,"12894604","German","Schweiz. Arch. Tierheilkd.",Review,"Final",,Scopus,2-s2.0-0141832180
"Wang Y., Ma W.L., Song Y.B., Xiao W.W., Zhang B., Huang H., Wang H.M., Ma X.D., Zheng W.L.","16044156100;7402704123;7404919409;7202456517;7406903776;57215154182;7501750971;57199215475;7403566536;","Gene sequence analysis of SARS-associated coronavirus by nested RT-PCR",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","5",,"421","423",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041655540&partnerID=40&md5=d138349f19ec236ae9d89fc8ebf7d1ff","Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China","Wang, Y., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Ma, W.L., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Song, Y.B., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Xiao, W.W., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Zhang, B., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Huang, H., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Wang, H.M., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Ma, X.D., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China; Zheng, W.L., Institute of Genetic Engineering, First Military Medical University, Guangzhou, 510515, China","OBJECTIVE: To explore an effective means for the detection of Severe Acute Respiratory Syndrome (SARS)- associated coronavirus. METHODS: The RNAs of the virus contained in the sputum samples from established SARS patients were extracted and reversely transcripted, followed by nested PCR using the reversely transcripted cDNA as the template. The PCR products were cloned then into the pMD18-T vectors, followed by sequence analysis. RESULTS: Specific fragments were amplified from the sputum samples of SARS patients, which were confirmed by DNA cloning and sequencing to belong to SARS-associated coronavirus. The Result of Blast shows only the difference in one nucleic acid from the TOR2 strain of SARS-associated coronavirus. CONCLUSION: Sequence analysis has confirmed the existence of SARS-associated coronavirus in the sputum samples of SARS patients, and nested RT-PCR is a quick, easy, and convenient way for the detection of the virus.",,"virus RNA; article; chemistry; genetics; human; isolation and purification; methodology; molecular genetics; nucleotide sequence; reverse transcription polymerase chain reaction; SARS coronavirus; Base Sequence; Humans; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus",,"Wang, Y.",,,10002588,,,"12754117","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-0041655540
"Wu B.Q., Zhong H.H., Gao J.P., Liu S.P., Heng W.J., E W., Gu J.","55468120500;7201453063;55702681400;57191660518;7004522378;6601990084;55343448700;","Gene detection of severe acute respiratory syndrome-related coronavirus",2003,"Zhonghua bing li xue za zhi Chinese journal of pathology","32","3",,"212","214",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642318102&partnerID=40&md5=c08fd04c2e66edb7972139e8cdd1e713","Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China","Wu, B.Q., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; Zhong, H.H., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; Gao, J.P., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; Liu, S.P., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; Heng, W.J., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; E, W., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China; Gu, J., Department of Pathology, Health Science Center, Peking University, Beijing, 100083, China","OBJECTIVE: To develop a newly real-time RT-polymerase chain reaction assay for severe acute respiratory syndrome (SARS) related coronavirus in human whole blood. METHODS: A pair of primers and a probe (molecular beacon) had been designed that were specific for the recognition of a highly conservative region between 15 301 and 15 480 of the SARS-related coronavirus polymerase gene sequences obtained from GenBank (G130027616). RESULTS: In the real-time RT-PCR assay, the extent of SARS related coronavirus amplification was measured in terms of the increase in fluorescence during the amplification process. The 145 bp fragment of PCR product was further confirmed by conventional PCR assay and proved by DNA sequencing to be identical to the target sequence to which the probe was hybridized. CONCLUSION: This assay has a broad application for clinical diagnosis and surveillance investigation.",,"article; genetics; human; molecular genetics; nucleotide sequence; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; Base Sequence; Humans; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome",,"Wu, B.Q.",,,05295807,,,"12882684","Chinese","Zhonghua Bing Li Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0642318102
"Liu Y.N., Fan B.X., Fang X.Q., Yu B.X., Chen L.A.","56365029300;7102879209;7401433179;7402092729;7409440903;","The quantitative detection of anti-coronavirus antibody titer in medical personnel closely contacted with severe acute respiratory syndrome patients",2003,"Zhonghua jie he he hu xi za zhi = Zhonghua jiehe he huxi zazhi = Chinese journal of tuberculosis and respiratory diseases","26","10",,"583","585",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347933272&partnerID=40&md5=252ad37a734b6f74b7f729d94a7438a9","The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China","Liu, Y.N., The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China; Fan, B.X., The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China; Fang, X.Q., The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China; Yu, B.X., The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China; Chen, L.A., The General Hospital of Chinese People's Liberation Army, Beijing, 100853, China","OBJECTIVE: To study the serum anti-coronavirus antibody titer in medical personnel who had closely contacted with severe acute respiratory syndrome (SARS) patients. METHODS: The serum anti-coronavirus IgG antibody titer in medical personnel who had closely contacted with SARS patients, healthy individuals, patients with community acquired pneumonia and patients recovered from SARS was detected by using an enzyme-linked immunosorbent assay (ELISA) method. The antibody titer was expressed as the value of absorbency (A) with common logarithm conversion. RESULTS: The serum anti-coronavirus IgG antibody titer in patients recovered from SARS was 0.07 +/- 0.13, which was significantly higher as compared with those in other groups. The antibody titer in medical personnel was -1.18 +/- 0.20, which was also significantly higher as compared with those in community acquired pneumonia patients and healthy persons. In the healthy persons, the antibody titer of serum samples obtained from Beijing in May, 2003 was -1.61 +/- 0.13, which was significantly higher than that of samples obtained from Beijing in 2001 when SARS was not found -1.76 +/- 0.25 and that of samples from Shandong province where SARS was not found in May, 2003 -1.95 +/- 0.44. There was no significant difference in the antibody titer between patients of bacterial pneumonia and patients of atypical pneumonia, which was -1.99 +/- 0.31 and -2.05 +/- 0.23 respectively. CONCLUSION: Close contact with SARS patients can cause the serum anti-coronavirus antibody titer to increase significantly in medical personnel, a phenomenon deserves further study.",,"immunoglobulin A; immunoglobulin G; virus antibody; adolescent; adult; aged; article; blood; disease transmission; female; health care personnel; human; immunology; male; middle aged; SARS coronavirus; severe acute respiratory syndrome; Adolescent; Adult; Aged; Antibodies, Viral; Female; Health Personnel; Humans; Immunoglobulin A; Immunoglobulin G; Male; Middle Aged; SARS Virus; Severe Acute Respiratory Syndrome",,"Liu, Y.N.",,,10010939,,,"14633437","Chinese","Zhonghua Jie He He Hu Xi Za Zhi",Article,"Final",,Scopus,2-s2.0-0347933272
"Sun H., Luo H., Yu C., Sun T., Chen J., Peng S., Qin J., Shen J., Yang Y., Xie Y., Chen K., Wang Y., Shen X., Jiang H.","7404827410;55454058600;7404977287;7402923095;55717786100;55462083500;7402896300;7404929839;55720009300;8677139000;26643583800;7601499551;7402721498;34868049700;","Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus",2003,"Protein Expression and Purification","32","2",,"302","308",,27,"10.1016/j.pep.2003.08.016","https://www.scopus.com/inward/record.uri?eid=2-s2.0-9144255691&doi=10.1016%2fj.pep.2003.08.016&partnerID=40&md5=b3d25f891828b3983406c0c8f0871203","Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shanghai Inst. Biochem. Cell Biol., Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China","Sun, H., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, H., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Yu, C., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Sun, T., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Chen, J., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Peng, S., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Qin, J., Shanghai Inst. Biochem. Cell Biol., Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Shen, J., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Yang, Y., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Xie, Y., Shanghai Inst. Biochem. Cell Biol., Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Chen, K., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Wang, Y., Shanghai Inst. Biochem. Cell Biol., Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Shen, X., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Jiang, H., Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China","Severe acute respiratory syndrome (SARS) is an acute respiratory illness, which has broken out in China. It has been known that SARS coronavirus (SARS_CoV) is a novel human coronavirus and is responsible for SARS infection. Belonging to one of the major proteins associated with SARS_CoV, SARS 3C-like protease (SARS_3CLpro) functions as a cysteine protease engaging in the proteolytic cleavage of the viral precursor polyprotein to a series of functional proteins required for coronavirus replication and is considered as an appealing target for designing anti-SARS agents. To facilitate the studies regarding the functions and structures of SARS_3CLpro, in this report the synthetic genes encoding 3CLpro of SARS_CoV were assembled, and the plasmid was constructed using pQE30 as vector and expressed in Escherichia coli M15 cells. The highly yielded (∼15 mg/L) expressed protease was purified by use of NTA-Ni2+ affinity chromatography and FPLC system, and its sequence was determined by LC/MS with the residue coverage of 46.4%. © 2003 Elsevier Inc. All rights reserved.","3C like protease; Expression; Mass spectrometric characterization; Molecular cloning; Purification; SARS coronavirus; Severe Acute Respiratory Syndrome (SARS)","Coronavirus; Escherichia coli; Escherichia coli; SARS coronavirus","Kathryn, V.H., SARS coronavirus: A new challenge for prevention and therapy (2003) J. Clin. Invest., 111, pp. 1605-1609; Peins, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., SARS study group, Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Kathryn, V.H., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Kamps, B.S., Hoffmann, C., (2003) ""SARS Reference"" Second Ed., , www.SARSReference.com, Flying Publisher; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997; Dougherty, W.G., Semler, B.L., Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes (1993) Microbiol. Rev., 57, pp. 781-822; Eleout, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Viral replicase gene products suffice for coronavirus discontinuous transcription (2001) J. Virol., 75, pp. 6676-6681; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M.C., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooks-Wilson, A., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Holmes, K.V., Enjuanes, L., Perspective: The SARS coronavirus: A postgenomic era (2003) Science, 300, pp. 1377-1378; Krokhin, O., Li, Y., Andonov, A., Feldman, H., Flick, R., Jones, S., Stroeher, U., Standing, K.G., Mass spectrometric characterization of proteins from the SARS virus: A preliminary report (2003) Mol. Cell. Proteomics, 2, pp. 346-356; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main protease (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Anand, K., Plam, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Higenfeld, R., Structure of coronavirus main protease reveals combination of a chymotrypsin fold with an extra alpha-helical domain (2002) EMBO J., 21, pp. 3213-3224; Liu, D.X., Brown, T.D., Characterization and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein (1995) Virology, 209, pp. 420-427; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Hegyi, A., Ziebuhr, J., Conservation of substrate specificities among coronavirus main proteases (2002) J. Gen. Virol., 83, pp. 595-599; Kim, J.C., Spence, R.A., Currier, P.F., Lu, X., Denison, M.R., Coronavirus protein processing and RNA synthesis is inhibited by the cysteine protease inhibitor E64d (1995) Virology, 208, pp. 1-8; Someya, Y., Takeda, N., Miyamura, T., Identification of active-site amino acid residues in the Chiba virus 3C-like protease (2002) J. Virol., 76, pp. 5949-5958; Xiong, B., Gui, C.S., Xu, X.Y., Luo, C., Chen, J., Luo, H.B., Chen, L.L., Jiang, H.J., A 3D model of SARS_CoV 3CL protease and its inhibitors design by virtural screening (2003) Acta Pharmacol. Sin., 24, pp. 497-504; Shen, X., Xue, J.H., Yu, C.Y., Luo, H.B., Qin, L., Yu, X.J., Chen, J., Jiang, H.L., Small envelope protein E of SARS: Cloning, expression, purification, CD determination, and bioinformatics analysis (2003) Acta Pharmacol. Sin., 24, pp. 505-511; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, Second Ed., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Yu, L., Zeng, R., Shao, X., Wang, N., Xu, Y., Xia, Q., Identification of differentially expressed proteins between human hepatoma and normal liver cell lines by two-dimensional electrophoresis and liquid chromatography-ion trap mass spectrometry (2000) Electrophoresis, 21, pp. 3058-3068","Shen, X.; Drug Discovery and Design Center, State Key Lab. of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; email: xshen@mail.shcnc.ac.cn",,"Academic Press Inc.",10465928,,PEXPE,"14965777","English","Protein Expr. Purif.",Article,"Final",Open Access,Scopus,2-s2.0-9144255691
"Liu S., Pei J., Chen H., Zhu X., Liu Z., Ma W., He F., Lai L.","57191659009;7103299043;55553726625;7406186996;7406676695;57210001078;16052644500;7202615995;","Modeling of the SARS coronavirus main proteinase and conformational flexibility of the active site",2003,"Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences","35 Suppl",,,"62","65",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0043237494&partnerID=40&md5=8c203592619919833dfeaf76f1c166ea","State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China","Liu, S., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Pei, J., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Chen, H., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Zhu, X., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Liu, Z., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Ma, W., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; He, F., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China; Lai, L., State Key Laboratory of Structural Chemistry of Stable and Unstable Species, College of Chemistry and Molecular Engineering &amp; Center for Theoretical Biology, Peking University, Beijing, 100871, China","SARS coronavirus 3CL proteinase is the key enzyme for virus replication which may serve as the target for drug discovery against SARS. A 3D structure model has been built for SARS coronavirus 3CL proteinase by comparative protein modeling. A homodimer model of the proteinase was also built. Analysis of the dimeric interface suggests the 3CL proteinase may have dimer form in solution. The conformational flexibility of the active site has been simulated by molecular dynamics combined with multi-canonical sampling. The active site loops have two typical conformations which may be related to the conformational movement associated with the enzymatic reaction.",,"3C like proteinase, Coronavirus; 3C-like proteinase, Coronavirus; cysteine proteinase; amino acid sequence; article; binding site; chemical structure; chemistry; dimerization; enzymology; molecular genetics; protein conformation; SARS coronavirus; Amino Acid Sequence; Binding Sites; Cysteine Endopeptidases; Dimerization; Models, Molecular; Molecular Sequence Data; Protein Conformation; SARS Virus",,"Liu, S.",,,1671167X,,,"12914221","Chinese","Beijing Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-0043237494
"Hong T., Wang J.W., Sun Y.L., Duan S.M., Chen L.B., Qu J.G., Ni A.P., Liang G.D., Ren L.L., Yang R.Q., Guo L., Zhou W.M., Chen J., Li D.X., Xu W.B., Xu H., Guo Y.J., Dai S.L., Bi S.L., Dong X.P., Ruan L.","57207234159;57206681376;35225971300;57215374665;35225733900;57207417110;7004451149;56350288300;57206977231;8731276000;57207229515;55255529400;57196110852;26632045000;57207174567;8571413000;57206256557;35225761100;7101633642;57198935666;7006832508;","Chlamydia-like and coronavirus-like agents found in dead cases of atypical pneumonia by electron microscopy",2003,"Zhonghua yi xue za zhi","83","8",,"632","636",,20,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038403369&partnerID=40&md5=e226a3ea722d5343577452a59dac4274","Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China","Hong, T., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Wang, J.W., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Sun, Y.L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Duan, S.M., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Chen, L.B., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Qu, J.G., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Ni, A.P., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Liang, G.D., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Ren, L.L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Yang, R.Q., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Guo, L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Zhou, W.M., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Chen, J., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Li, D.X., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Xu, W.B., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Xu, H., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Guo, Y.J., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Dai, S.L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Bi, S.L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Dong, X.P., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China; Ruan, L., Institute of Viral Disease Control and Prevention, China CDC, Beijing, 100052, China","OBJECTIVE: To explore the causative agents of the atypical pneumonia (also SARS) occurred recently in some regions of our country. METHOD: Organ samples of 7 dead cases of SARS were collected from Guangdong, Shanxi, Sichuan Provinces and Beijing for electron microscopic examination. 293 cell line was inoculated with the materials derived from the lungs to isolate causative agent(s). The agents in the organs and cell cultures were revealed by immunoassay. RESULTS: Both Chlamydia-like and coronavirus-like particles were found in EM. Inclusion bodies containing elementary bodies, reticulate antibodies and intermediate bodies of Chlamydia-like agent were visualized in multiple organs from the 7 dead cases, including lungs (7 cases), spleens (2 cases), livers (2 cases), kidneys (3 cases) and lymph nodes (1 cases), by ultrathin section electron microscopy (EM). In some few sections, coronavirus-like particles were concurrently seen. A coronavirus RNA- polymerase segment (440 bp) was amplified from the lung tissues of two cases of the SARS. After inoculated with materials from the lung samples, the similar Chlamydia-like particles were also found in the inoculated 293 cells. Since the Chlamydia-like agents visualized in both organs and cell cultures could not react with the genus specific antibodies against Chlamydia and monoclonal antibodies against C. pneumoniae and C. psittaci, the results might well be suggestive of a novel Chlamydia-like agent. CONCLUSION: Since the novel Chlamydia-like agent was found co-existing with a coronavirus-like agent in the dead cases of SARS, it looks most likely that both the agents play some roles in the disease. At the present time, however, one can hardly determining how did these agents interact each other synergetically, or one follows another, need further study.",,"article; Chlamydia; Coronavirus; electron microscopy; human; isolation and purification; microbiology; pathology; severe acute respiratory syndrome; virology; Chlamydia; Coronavirus; Humans; Microscopy, Electron; Severe Acute Respiratory Syndrome",,"Hong, T.email: hungt@public3.bta.net.cn",,,03762491,,,"12887816","Chinese","Zhonghua Yi Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0038403369
"Yang M., Hon K.L., Li K., Fok T.F., Li C.K.","7404926192;8134452900;7404990071;7006455238;15122650100;","The effect of SARS coronavirus on blood system: its clinical findings and the pathophysiologic hypothesis.",2003,"Zhongguo shi yan xue ye xue za zhi / Zhongguo bing li sheng li xue hui = Journal of experimental hematology / Chinese Association of Pathophysiology","11","3",,"217","221",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042352136&partnerID=40&md5=f1efff1f5dbde9142a7a01738af7f2a5","Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China","Yang, M., Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China; Hon, K.L., Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China; Li, K., Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China; Fok, T.F., Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China; Li, C.K., Department of Paediatrics, The Prince of Wales Hospital, The Chinese University of Hong Kong, China","Severe acute respiratory syndrome (SARS) has recently recognized as a new human infectious disease. A novel coronavirus was identified as the causative agent of SARS. This report summarizes the hematological findings in SARS patients and proposes a hypothesis for the pathophysiology of SARS coronavirus related abnormal hematopoiesis. Hematological changes in patients with SARS were common and included lymphopenia (68% - 90% of adults; 100% of children, n = 10), thrombocytopenia (20% - 45% of adults, 50% of children), and leukopenia (20% - 34% of adults, 70% of children). The possible mechanisms of this coronavirus on blood system may include (1) directly infect blood cells and bone marrow stromal cells via CD13 or CD66a; and/or (2) induce auto-antibodies and immune complexes to damage these cells. In addition, lung damage in SARS patients may also play a role on inducing thrombocytopenia by (1) increasing the consumption of platelets/megakaryocytes; and/or (2) reducing the production of platelets in the lungs. Since the most common hematological changes in SARS patients were lymphopenia and immunodeficiency. We postulate that hematopoietic growth factors such as G-CSF, by mobilizing endogenous blood stem cells and endogenous cytokines, could become a hematological treatment for SARS patients, which may enhance the immune system against these virus.",,"CD66 antigens; cell adhesion molecule; differentiation antigen; leukocyte antigen; microsomal aminopeptidase; adult; article; child; hematologic disease; hematopoiesis; human; immunology; pathophysiology; physiology; SARS coronavirus; severe acute respiratory syndrome; virology; Adult; Antigens, CD; Antigens, CD13; Antigens, Differentiation; Cell Adhesion Molecules; Child; Hematologic Diseases; Hematopoiesis; Humans; SARS Virus; Severe Acute Respiratory Syndrome",,"Yang, M.email: yang1091@cuhk.edu.hk",,,10092137,,,"12844398","English","Zhongguo Shi Yan Xue Ye Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0042352136
"Zhu R.N., Qian Y., Deng J., Zhao L.Q., Wang F., Cao L., Wang T.Y., Chen D.K., Zhang Q.","35270852500;7402872810;10638840600;35270945000;56147311100;57198528505;55709760800;57211845652;57210044011;","SARS-associated coronavirus gene fragments were detected from a suspected pediatric SARS patient",2003,"Zhonghua er ke za zhi. Chinese journal of pediatrics","41","9",,"641","644",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342597694&partnerID=40&md5=328f333ea139e4428ac5ca1e8f2ec375","Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China","Zhu, R.N., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Qian, Y., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Deng, J., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Zhao, L.Q., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Wang, F., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Cao, L., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Wang, T.Y., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Chen, D.K., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China; Zhang, Q., Beijing Municipal Laboratory of Infection and Immunity, Capital Institute of Pediatrics, Beijjing, 100020, China","A Special ""Fever and Cough"" Clinic was set up at the Children's Hospital Affiliated to Capital Institute of Pediatrics for children with symptoms of fever and cough in late April when the severe acute respiratory syndrome (SARS) epidemic was at its peak in Beijing to separate the children with fever from others during their visit to the Outpatient Department. OBJECTIVE: For patients with fever, normal or low count of white blood cell and with suspected pneumonia suggested by X-ray, it was urgent to determine the etiological agents of the diseases before they were admitted to the hospital. METHODS: Throat swabs or nasopharyngeal aspirate specimens were collected from those patients and common respiratory virus antigens including influenza virus A and B, respiratory syncytial virus, adenovirus, parainfluenza virus types I, II, and III were tested by indirect immunofluorescent assay. The patients with atypical pneumonia diagnosed by X-ray and evidences of common respiratory virus infection were admitted to the regular ward for children with respiratory diseases. Children with pneumonia demonstrated by X-ray and negative for common respiratory viruses were admitted to the isolated ward for suspected SARS patients for the first step and further viral etiological studies were requested. RT-PCR was performed for those patients to detect gene fragments of human metapneumovirus (HMPV), rhinovirus (RhV) and enterovirus (EV) in their specimens. Nested RT-PCR was also developed to detect SARS coronavirus gene fragment from the specimens. Primer sequences for SARS virus detection with the PCR were selected according to the primer sequences published online by WHO on April 18, 2003. All the primers derived from the sequence at the 1b frame of coronavirus replicase gene and products with a size of 368 or 348 bp were expected with 2 different primer pairs. RESULTS: Amplicons with the sizes of 368 bp and 348 bp were obtained from a throat swab specimen collected from a 17 years old girl, who was admitted to the isolated ward because of high fever (39.5 degrees C) for 7 days, cough for 2 days, low WBC count, and pneumonia shown by X-ray when she visited the ""Fever and Cough"" Clinic, and without known history of contact with probable SARS patient. Antigens for the common respiratory viruses were all negative, RT-PCR for HMPV, RhV and EV were also negative while RT-PCR with different primer pairs for SARS virus were all positive which indicated that SARS coronavirus gene fragments were amplified from the specimen from this girl. The amplified fragment with a size of 368 bp was sequenced and the sequence was compared with those in the GenBank. The sequence shared 100% homology with the sequences from 1b frame of replicase genes from all 17 of SARS coronaviruses published in the GenBank so far, and shared very low homology with 2 reference strains of human coronavirus as well as other animal coronaviruses. The serum collected before her discharge from the hospital (19 days after the onset of the disease) showed SARS specific IgM and IgG antibodies. CONCLUSION: These data indicate that the patient was a confirmed case of SARS. It is of great importance to differentiate SARS patients from those infected with common respiratory viruses during SARS epidemic, especially for pediatric patients, because most of the patients visiting the outpatient department present with the symptoms of fever, cough and normal WBC count. The data mentioned above indicate that antigen and gene detections for those common respiratory viruses are useful methods for the differentiation to avoid the spread of SARS.",,"virus antibody; adolescent; amino acid sequence; article; case report; China; DNA sequence; female; fluorescent antibody technique; genetics; human; immunology; molecular genetics; reverse transcription polymerase chain reaction; SARS coronavirus; sequence homology; severe acute respiratory syndrome; virology; Adolescent; Amino Acid Sequence; Antibodies, Viral; China; Female; Fluorescent Antibody Technique, Indirect; Humans; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Severe Acute Respiratory Syndrome",,"Zhu, R.N.",,,05781310,,,"14733796","Chinese","Zhonghua Er Ke Za Zhi",Article,"Final",,Scopus,2-s2.0-2342597694
"Ziebuhr J., Bayer S., Cowley J.A., Gorbalenya A.E.","7003783935;7005617717;7102947876;7005626044;","The 3C-like proteinase of an invertebrate nidovirus links coronavirus and potyvirus homologs",2003,"Journal of Virology","77","2",,"1415","1426",,45,"10.1128/JVI.77.2.1415-1426.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037228215&doi=10.1128%2fJVI.77.2.1415-1426.2003&partnerID=40&md5=be56d57d824fee0ec4b4c732c69076d6","Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, Netherlands","Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Bayer, S., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Cowley, J.A.; Gorbalenya, A.E., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, Netherlands","Gill-associated virus (GAV), a positive-stranded RNA virus of prawns, is the prototype of newly recognized taxa (genus Okavirus, family Roniviridae) within the order Nidovirales. In this study, a putative GAV cysteine proteinase (3C-like proteinase [3CLpro]), which is predicted to be the key enzyme involved in processing of the GAV replicase polyprotein precursors, pp1a and pp1ab, was characterized. Comparative sequence analysis indicated that, like its coronavirus homologs, 3CLpro has a three-domain organization and is flanked by hydrophobic domains. The putative 3CLpro domain including flanking regions (ppla residues 2793 to 3143) was fused to the Escherichia coli maltose-binding protein (MBP) and, when expressed in E. coli, was found to possess N-terminal autoprocessing activity that was not dependent on the presence of the 3CLpro C-terminal domain. N-terminal sequence analysis of the processed protein revealed that cleavage occurred at the location 2827LVTHE ↓ VRTGN2836. The trans-processing activity of the purified recombinant 3CLpro (pp1a residues 2832 to 3126) was used to identify another cleavage site, 6441KVNHE ↓ LYHA6450, in the C-terminal pp1ab region. Taken together, the data tentatively identify VxHE ↓ (L,V) as the substrate consensus sequence for the GAV 3CLpro. The study revealed that the GAV and potyvirus 3CLpros possess similar substrate specificities which correlate with structural similarities in their respective substrate-binding sites, identified in sequence comparisons. Analysis of the proteolytic activities of MBP-3CLpro fusion proteins carrying replacements of putative active-site residues provided evidence that, in contrast to most other 3C/3CLpros but in common with coronavirus 3CLpros, the GAV 3CLpro employs a Cys2968-His2879 catalytic dyad. The properties of the GAV 3CLpro define a novel RNA virus proteinase variant that bridges the gap between the distantly related chymotrypsin-like cysteine proteinases of coronaviruses and potyviruses.",,"cysteine proteinase; maltose binding protein; virus DNA; virus enzyme; virus RNA; amino terminal sequence; article; binding site; carboxy terminal sequence; consensus sequence; Coronavirus; DNA flanking region; DNA sequence; enzyme active site; enzyme binding; enzyme specificity; enzyme substrate; Escherichia coli; gene activity; gill associated virus; nonhuman; nucleotide sequence; Potyvirus; priority journal; protein degradation; protein expression; RNA virus; sequence analysis; sequence homology; species comparison; Amino Acid Sequence; Base Sequence; Catalytic Domain; Coronavirus; Cysteine Endopeptidases; DNA Primers; Molecular Sequence Data; Nidovirales; Potyvirus; Recombinant Proteins; Sequence Homology, Amino Acid; Viral Proteins","Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N., Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases (1994) Nature, 369, pp. 72-76; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain (2002) EMBO J., 21, pp. 3213-3224; Barrette-Ng, I.H., Ng, K.K., Mark, B.L., Van Aken, D., Cherney, M., Garen, C., Kolodenko, Y., James, M.N., Structure of arterivirus nsp4: The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole (2002) J. Biol. Chem., 277, pp. 39960-39966; Bergmann, E.M., Mosimann, S.C., Chernaia, M.M., Malcolm, B.A., James, M.N., The refined crystal structure of the 3C gene product from hepatitis A virus: Specific proteinase activity and RNA recognition (1997) J. Virol., 71, pp. 2436-2448; Boonyaratpalin, S., Supamataya, K., Kasornchandra, J., Direkbusaracom, S., Aekpanithanpong, U., Chantanachookin, C., Non-occluded baculo-like virus, the causative agent of yellow-head disease in the black tiger shrimp (Penaeus monodon) (1993) Fish Pathol., 28, pp. 103-109; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Chantanachookin, C., Boonyaratpalin, S., Kasornchandra, J., Sataporn, D., Ekpanithanpong, U., Supamataya, K., Riurairatana, S., Flegel, T.W., Histology and ultrastructure reveal a new granulosis-like virus in Penaeus monodon affected by yellow-head disease (1993) Dis. Aquat. Org., 17, pp. 145-157; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses (2000) J. Gen. Virol., 81, pp. 1473-1484; Cowley, J.A., Dimmock, C.M., Walker, P.J., Gill-associated nidovirus of Penaeus monodon prawns transcribes 3′-coterminal subgenomic mRNAs that do not possess 5′-leader sequences (2002) J. Gen. Virol., 83, pp. 927-935; Cowley, J.A., Dimmock, C.M., Wongteerasupaya, C., Boonsaeng, V., Panyim, S., Walker, P.J., Yellow head virus from Thailand and gill-associated virus from Australia are closely related but distinct prawn viruses (1999) Dis. Aquat. Org., 36, pp. 153-157; Cowley, J.A., Walker, P.J., The complete genome sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses (2002) Arch. Virol., 147, pp. 1977-1987; De Vries, A.A., Horzinek, M.C., Rottier, P.J., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Dodson, G., Wlodawer, A., Catalytic triads and their relatives (1998) Trends Biochem. Sci., 23, pp. 347-352; Gorbalenya, A.E., Big nidovirus genome. When count and order of domains matter (2001) Adv. Exp. Med. Biol., 494, pp. 1-17; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Snijder, E.J., Viral cysteine proteinases (1996) Perspect. Drug Discov. Des., 6, pp. 64-86; Hegyi, A., Friebe, A., Gorbalenya, A.E., Ziebuhr, J., Mutational analysis of the active centre of coronavirus 3C-like proteases (2002) J. Gen. Virol., 83, pp. 581-593; Henikoff, S., Henikoff, J.G., Position-based sequence weights (1994) J. Mol. Biol., 243, pp. 574-578; Herold, J., Siddell, S., Zlebuhr, J., Characterization of coronavirus RNA polymerase gene products (1996) Methods Enzymol., 275, pp. 68-89; Heusipp, G., Grötzinger, C., Herold, J., Siddell, S.G., Ziebuhr, J., Identification and subcellular localization of a 41 kDa, polyprotein lab processing product in human coronavirus 229E-infected cells (1997) J. Gen. Virol., 78, pp. 2789-2794; Kang, H., Lee, Y.J., Goo, J.H., Park, W.J., Determination of the substrate specificity of turnip mosaic virus NIa protease with a genetic method (2001) J. Gen. Virol., 82, pp. 3115-3117; Kanjanahaluethai, A., Baker, S.C., Identification of mouse hepatitis virus papain-like proteinase 2 activity (2000) J. Virol., 74, pp. 7911-7921; Kraut, J., Serine proteases: Structure and mechanism of catalysis (1977) Annu. Rev. 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Biol., 273, pp. 1032-1047; Mulford, A.L., Lyng, F., Mothersill, C., Austin, B., Development and characterization of primary cell cultures from the hematopoietic tissues of the Dublin Bay prawn, Nephrops norvegicus (2000) Methods Cell Sci., 22, pp. 265-275; Ng, L.F., Liu, D.X., Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site (2000) Virology, 272, pp. 27-39; Nicolas, O., Laliberte, J.F., The complete nucleotide sequence of turnip mosaic potyvirus RNA (1992) J. Gen. Virol., 73, pp. 2785-2793; Rost, B., PHD: Predicting one-dimensional protein structure by profile-based neural networks (1996) Methods Enzymol., 266, pp. 525-539; Rost, B., Casadio, R., Fariselli, P., Sander, C., Transmembrane helices predicted at 95% accuracy (1995) Protein Sci., 4, pp. 521-533; Ryan, M.D., Flint, M., Virus-encoded proteinases of the picornavirus super-group (1997) J. Gen. Virol., 78, pp. 699-723; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Snijder, E.J., Wassenaar, A.L., Van Dinten, L.C., Spaan, W.J., Gorbalenya, A.E., The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases (1996) J. Biol. Chem., 271, pp. 4864-4871; Sosnovtseva, S.A., Sosnovtsev, S.V., Green, K.Y., Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein (1999) J. Virol., 73, pp. 6626-6633; Spann, K.M., Cowley, J.A., Walker, P.J., Lester, R.J., Gill-associated virus (GAV), a yellow head-like virus from Penaeus monodon cultured in Australia (1997) Dis. Aquat. Org., 31, pp. 169-179; Spann, K.M., Vickers, J.E., Lester, R.J., Lymphoid organ virus of Penaeus monodon from Australia (1995) Dis. Aquat. Org., 23, pp. 127-134; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The CLUSTAL X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Res., 25, pp. 4876-4882; Thompson, J.D., Higgins, D.G., Gibson, T.J., Improved sensitivity of profile searches through the use of sequence weights and gap excision (1994) Comput. Appl. Biosci., 10, pp. 19-29; Vance, V.B., Moore, D., Turpen, T.H., Bracker, A., Hollowell, V.C., The complete nucleotide sequence of pepper mottle virus genomic RNA: Comparison of the encoded polyprotein with those of other sequenced potyviruses (1992) Virology, 191, pp. 19-30; Wassenaar, A.L., Spaan, W.J., Gorbalenya, A.E., Snijder, E.J., Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease (1997) J. Virol., 71, pp. 9313-9322; Wei, L., Huhn, J.S., Mory, A., Pathak, H.B., Sosnovtsev, S.V., Green, K.Y., Cameron, C.E., Proteinase-polymerase precursor as the active form of feline calicivirus RNA-dependent RNA polymerase (2001) J. Virol., 75, pp. 1211-1219; Yao, Z., Jones, D.H., Grose, C., Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction (1992) PCR Methods Appl., 1, pp. 205-207; Yeh, S.D., Jan, F.J., Chiang, C.H., Doong, T.J., Chen, M.C., Chung, P.H., Bau, H.J., Complete nucleotide sequence and genetic organization of papaya ringspot virus RNA (1992) J. Gen. Virol., 73, pp. 2531-2541; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879","Ziebuhr, J.; Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; email: ziebuhr@vim.uni-wuerzburg.de",,,0022538X,,JOVIA,"12502857","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037228215
"Wang H.B., Liu J.H., Ouyang X.L., Yu Y., Ma S.X., Li X.J., Lu L.C., Tian Y.P., Liu H.Y., Xu H.M., Yao W.","36121868600;36068589700;7102723394;57214104243;7403725254;7501700632;36819715100;55545340300;37079935200;57198604211;55420677000;","Detection of the anti-SARS-coronavirus specific antibody levels in 156 SARS patients",2003,"Zhongguo shi yan xue ye xue za zhi / Zhongguo bing li sheng li xue hui = Journal of experimental hematology / Chinese Association of Pathophysiology","11","5",,"441","443",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142860795&partnerID=40&md5=7c89a4627348ec6549b71b413f82be33","Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China","Wang, H.B., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Liu, J.H., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Ouyang, X.L., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Yu, Y., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Ma, S.X., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Li, X.J., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Lu, L.C., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Tian, Y.P., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Liu, H.Y., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Xu, H.M., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China; Yao, W., Department of Blood transfusion, The General Hospital of PLA, Center for Clinical Blood Transfusion of PLA, Beijing, 100853, China","The objective of this study was to explore the development of IgG and IgM against SARS CoV and characteristics of changes of antibody titers in patients with severe acute respiratory syndrome (SARS) and to search the opportunity for collecting specific anti-serum from convalescent patients with SARS. The anti-SARS-coronavirus specific antibody levels in 156 SARS patients were measured with ELISA. The results showed that the total positive rates of IgG and IgM were 75.6% and 41.7% respectively, and the negative rate of both IgG and IgM was 23.7%. The average titers of IgG and IgM antibody in positive samples were 18.23 +/- 24.72 and 2.18 +/- 1.13, respectively. There was no significant correlation between the titers of IgG/IgM and sex, age, course of diseases and duration of body temperature recovery. It was concluded that not all SARS patients could produce the anti-SARS-coronavirus specific antibody. The titers of the anti-body are diversified even if the antibodies have been emerged in them. In order to obtain effective anti-serum, the titers of antibody must be tested just before collection of convalescent serum, and it ensures the therapeutic effect and provides a measurable index for clinical transfusion.",,"immunoglobulin G; immunoglobulin M; virus antibody; adolescent; adult; aged; article; blood; female; human; immunology; male; middle aged; SARS coronavirus; severe acute respiratory syndrome; Adolescent; Adult; Aged; Antibodies, Viral; Female; Humans; Immunoglobulin G; Immunoglobulin M; Male; Middle Aged; SARS Virus; Severe Acute Respiratory Syndrome",,"Wang, H.B.",,,10092137,,,"14575532","Chinese","Zhongguo Shi Yan Xue Ye Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-2142860795
"Li L., Wo J., Shao J., Zhu H., Wu N., Li M., Yao H., Hu M., Dennin R.H.","55540790300;23500565900;56418813900;57202225407;57039481000;26643238600;57214294470;57210839491;7004615980;","SARS-coronavirus replicates in mononuclear cells of peripheral blood (PBMCs) from SARS patients",2003,"Journal of Clinical Virology","28","3",,"239","244",,47,"10.1016/S1386-6532(03)00195-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141522446&doi=10.1016%2fS1386-6532%2803%2900195-1&partnerID=40&md5=f73bbe02a889bb11f75bf32b49d24b0e","Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Inst. of Med. Microbiol. and Hygiene, University of Luebeck, Ratzeburger Allee 160, D-23538 Luebeck, Germany","Li, L., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Wo, J., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Shao, J., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Zhu, H., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Wu, N., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Li, M., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Yao, H., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Hu, M., Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; Dennin, R.H., Inst. of Med. Microbiol. and Hygiene, University of Luebeck, Ratzeburger Allee 160, D-23538 Luebeck, Germany","Background: The etiologic agent of severe acute respiratory syndrome (SARS) is a recently identified, positive single-stranded RNA (ssRNA) coronavirus (SARS-CoV). Little is known about the dynamic changes of the viral replicative form in SARS cases. Objectives: Evaluate whether SARS-CoV can infect and replicate in peripheral blood mononuclear cells (PBMCs) of infected persons and reveal any dynamic changes to the virus during the course of the disease. Study design: Peripheral blood mononuclear cells collected from SARS cases infected by the same infectious source were tested for both negative-stranded RNA (minus-RNA, ""replicative intermediates"") and positive-stranded RNA (genomic RNA) of SARS-CoV during the course of hospitalization by reverse transcription-polymerase chain reaction (RT-PCR). Results: SARS-CoV minus-RNA was detected in PBMCs from SARS patients. The viral replicative forms in PBMCs were detectable during a period of 6 days post-onset of the disease, while the plus-RNA were detectable for a longer period (8-12 days post-onset). Conclusions: SARS-coronavirus can infect and replicate within PBMCs of SARS patients, but viral replication in PBMCs seems subject to self-limitation. © 2003 Elsevier B.V. All rights reserved.","Peripheral blood mononuclear cells (PBMCs); Replicative negative-stranded RNA; SARS-coronavirus; Severe acute respiratory syndrome (SARS)","genomic RNA; adult; article; blood sampling; case report; Coronavirus; disease duration; female; hospitalization; human; male; mononuclear cell; priority journal; reverse transcription polymerase chain reaction; RNA replication; RNA structure; SARS coronavirus; severe acute respiratory syndrome; upper respiratory tract infection; virus detection; virus diagnosis; virus identification; virus infection; virus isolation; virus pneumonia; virus replication","Baric, R.S., Yount, B., Subgenomic negative-strand RNA function during mouse hepatitis virus infection (2000) J. Virol., 74, pp. 4039-4046; Bernhard-Nocht Institute, Hamburg, Germany; 9 April 2003 at http://www.bni-hamburg.de/. Bernhard-Nocht Institute, Hamburg, Germany; 9 April 2003 at http://www.bni-hamburg.de/; Lai MMC, Holmes KV. In: Knipe DM, Howley PM, editors. Fields virology. 4th ed. New York: Lippincott Williams and Wilkins; 2001 [Chapter 35]; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Marra MA, Steven JM, Jones SJM, Caroline R, Astell CR, et al. The genome sequence of the sars-associated coronavirus. Science 1 May 2003 at http://www.sciencexpress.org/ 1 May 2003/Page 1/10.1126/science.1085953; Paul A, Rota PA, Oberste MS, Monroe SS, et al. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 1 May 2003 at http://www.sciencexpress.org/ 1 May 2003/Page 2/10.1126/science.1085952; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Sawicki, G.S., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-219; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985","Wo, J.; Key Lab. of Infectious Diseases, First Affiliated Hospital, Zhejiang University, Qingchun Road 79, Hangzhou, Zhejiang 310003, China; email: wojianer@zju.edu.cn",,"Elsevier",13866532,,JCVIF,"14522061","English","J. Clin. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141522446
"Zhang Q.L., Ding Y.Q., Hou J.L., He L., Huang Z.X., Wang H.J., Cai J.J., Zhang J.H., Zhang W.L., Geng J., Li X., Kang W., Yang L., Shen H., Li Z.G., Han H.X., Lu Y.D.","36496080400;7404137178;7401966390;56517322000;7406222466;57196429736;56517361800;57196377853;55706395100;57212700356;55924516600;36852704100;57211687323;35084245300;37078698600;8440811700;7405480785;","Detection of severe acute respiratory syndrome (SARS)-associated coronavirus RNA in autopsy tissues with in situ hybridization",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","11",,"1125","1127",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142660311&partnerID=40&md5=4b40a10b8336413f4ab5f346a0632172","Department of Pathology, First Military Medical University, Guangzhou, 510515, China","Zhang, Q.L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Ding, Y.Q., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Hou, J.L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; He, L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Huang, Z.X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Wang, H.J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Cai, J.J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Zhang, J.H., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Zhang, W.L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Geng, J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Li, X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Kang, W., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Yang, L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Shen, H., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Li, Z.G., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Han, H.X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Lu, Y.D., Department of Pathology, First Military Medical University, Guangzhou, 510515, China","OBJECTIVE: To explore the distribution of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) in SARS autopsy tissues at the molecular level. METHODS: In situ hybridization was used to detect the expression and location of SARS-CoV RNA polymerase gene in autopsy tissues from SARS-Cov-infected subjects, including the lung, spleen, lymph nodes, pituitary, pancreas, parathyroid, adrenal glands, gastrointestinal tract, skin, brain, liver, kidney, blood vessels, striated muscles of the limbs, bone marrow, heart, ovary, uterus and testicles. RESULT: SARS-CoV RNA was detected in the cytoplasm of the alveolar epithelia, infiltrating mononuclear phagocytes in the lungs, serous gland epithelium of the trachea/bronchus, monocytes in the spleen and lymph nodes, acinar cells in the pancreas, acidophilic cells in the parathyroid and pituitary, adrenal cortical cells, epithelia of the alimentary tracts, gastric parietal cells, sweat gland cells, brain neurons, hepatocytes near the central vein, epithelia of the distal renal tubules, bone marrow promyelocytes, and endothelia of the small veins. CONCLUSIONS: SARS-CoV invades various organs of the body and distributes in a similar fashion to CD13, the receptor of human coronavirus 229E. The detection of SARS-CoV in the sweat glands, alimentary tracts and epithelia of the distal convoluted tubules of the kidney may help identify the transmission routes of SARS-CoV.",,"virus RNA; article; autopsy; disease transmission; genetics; human; in situ hybridization; isolation and purification; kidney distal tubule; methodology; SARS coronavirus; severe acute respiratory syndrome; sweat gland; virology; Autopsy; Humans; In Situ Hybridization; Kidney Tubules, Distal; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Sweat Glands",,"Zhang, Q.L.email: zqllc8@fimmu.com",,,10002588,,,"14625166","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-2142660311
"Velayudhan B.T., Shin H.-J., Lopes V.C., Hooper T., Halvorson D.A., Nagaraja K.V.","6507918935;7404012633;35850065600;7005121335;7006046864;7005914633;","A reverse transcriptase-polymerase chain reaction assay for the diagnosis of turkey coronavirus infection",2003,"Journal of Veterinary Diagnostic Investigation","15","6",,"592","596",,5,"10.1177/104063870301500616","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347604983&doi=10.1177%2f104063870301500616&partnerID=40&md5=ee545046da65e64cc65dc846f7299454","Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States; Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States","Velayudhan, B.T., Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States; Shin, H.-J., Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States; Lopes, V.C., Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States; Hooper, T., Dept. of Veterinary Pathobiology, Purdue University, West Lafayette, IN 47907-1175, United States; Halvorson, D.A., Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States; Nagaraja, K.V., Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States","This study reports on the development of a reverse transcriptase- polymerase chain reaction (RT-PCR) for the specific detection of turkey coronavirus (TCoV). Of the several sets of primers tested, 1 set of primers derived from the P gene and 2 sets derived from the N gene of TCoV could amplify the TCoV genome in the infected samples. The RT-PCR was sensitive and specific for TCoV and did not amplify other avian RNA and DNA viruses tested except the infectious bronchitis virus (IBV). To overcome the problem of IBV amplification, a set of separate primers was designed from the spike protein gene of IBV. The RT-PCR under the same conditions as above could effectively differentiate between TCoV and IBV. The closely related bovine coronavirus and transmissible gastroenteritis virus of pigs were differentiated from TCoV using the same RT-PCR with slight modifications. The results of RT-PCR correlated well with the results of the immunofluorescent test for the same samples tested at the Purdue University Animal Disease Laboratory, West Lafayette, Indiana. The nucleotide sequence and projected amino acid sequence comparison of the P gene of different isolates of TCoV from 5 different states in the United States revealed a close association among the different isolates of TCoV.",,"Animalia; Aves; Avian infectious bronchitis virus; Bovinae; Bovine coronavirus; Coronavirus; DNA viruses; Meleagris gallopavo; Transmissible gastroenteritis virus; Turkey coronavirus","Akin, A., Lin, T.L., Wu, C.C., Nucleocapsid protein gene sequence analysis reveals close genomic relationship between turkey coronavirus and avian infectious bronchitis virus (2001) Acta Virol, 45, pp. 31-38; Breslin, J.J., Smith, L.G., Barnes, H.J., Guy, J.S., Comparison of virus isolation, immunohistochemistry, and reverse transcriptase-polymerase reaction procedures for detection of turkey coronavirus (2000) Avian Dis, 44, pp. 624-631; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid protein gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res, 65, pp. 187-193; Cavanagh, D., Structural polypeptides of coronavirus IBV (1981) J Gen Virol, 53, pp. 93-103; Dea, S., Tijssen, P., Detection of turkey enteric coronavirus by enzyme-linked immunosorbent assay and differentiation from other coronaviruses (1989) Am J Vet Res, 50, pp. 226-231; Dea, S., Verbeek, A.J., Tijssen, P., Antigenic and genomic relationships among turkey and bovine enteric coronaviruses (1990) J Virol, 64, pp. 3112-3118; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis-and mortality syndrome-affected turkeys (1997) Avian Dis, 41, pp. 583-590; Ignjatovic, J., Galli, L., Structural proteins of avian infectious bronchitis virus: Role in immunity and protection (1993) Adv Exp Med Biol, 342, pp. 449-453; Jiang, X., Wang, J., Graham, D.Y., Estes, M.K., Detection of Norwalk virus in stool by polymerase chain reaction (1992) J Clin Microbiol, 30, pp. 2529-2534; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , ed. Siddel SG Plenum Press, New York, NY; Loa, C.C., Lin, T.L., Wu, C.C., Detection of antibody to turkey coronavirus by antibody capture enzyme-linked immunosorbent assay utilizing infectious bronchitis virus antigen (2000) Avian Dis, 44, pp. 498-506; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (blue comb disease) (1997) Diseases of Poultry, pp. 686-692. , ed. Calnek BW, Barnes HJ, Beard CW, et al., 10th ed. Iowa State University Press, Ames, IA; Patel, B.L., Deshmukh, D.R., Pomeroy, B.S., Fluorescent antibody test for rapid diagnosis of coronaviral enteritis of turkeys (blue comb) (1975) Am J Vet Res, 36, pp. 1265-1267; Siddel, S.G., The Coronaviridae an introduction (1995) Coronaviridae, pp. 1-9. , ed. Siddel SG, Plenum Press, New York, NY; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res, 60, pp. 181-189; Verbeek, A., Dea, S., Tijssen, P., Genomic relationship between turkey and bovine enteric coronaviruses identified by hybridization with BCV or TCV specific cDNA probes (1991) Arch Virol, 121, pp. 199-221; Verbeek, A., Tijssen, P., Sequence analysis of the turkey enteric coronavirus nucleocapsid and membrane protein genes: A closed genomic relationship with bovine coronavirus (1991) J Gen Virol, 72, pp. 1659-1666; Wilde, J., Eiden, J., Yolken, R., Removal of inhibitory substances from human fecal specimens for detection of group A rotaviruses by reverse transcriptase polymerase chain reactions (1990) J Clin Microbiol, 28, pp. 1300-1307","Nagaraja, K.V.; Dept. of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, 1971 Commonwealth Avenue, Saint Paul, MN 55108, United States",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"14667027","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0347604983
"Chan P.K.S., Ip M., Ng K.C., Chan R.C.W., Wu A., Lee N., Rainer T.H., Joynt G.M., Sung J.J.Y., Tam J.S.","32067487100;55503091500;7403178624;7403110830;7402998681;55503117200;7004489495;7005588815;35405352400;24788939600;","Severe Acute Respiratory Syndrome-associated Coronavirus Infection",2003,"Emerging Infectious Diseases","9","11",,"1453","1454",,36,"10.3201/eid0911.030421","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744223315&doi=10.3201%2feid0911.030421&partnerID=40&md5=fbf7d06c52ef2ea9e8718e536c760e59","Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, New Territories, Hong Kong","Chan, P.K.S., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong, Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, New Territories, Hong Kong; Ip, M., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Ng, K.C., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Chan, R.C.W., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Wu, A., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Lee, N., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Rainer, T.H., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Joynt, G.M., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Sung, J.J.Y., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Tam, J.S., Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong","Whether severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infection can be asymptomatic is unclear. We examined the seroprevalence of SARS-CoV among 674 healthcare workers from a hospital in which a SARS outbreak had occurred. A total of 353 (52%) experienced mild self-limiting illnesses, and 321 (48%) were asymptomatic throughout the course of these observations. None of these healthcare workers had antibody to SARS CoV, indicating that subclinical or mild infection attributable to SARS-CoV in adults is rare.",,"virus antibody; adult; article; Coronavirus; disease course; epidemic; female; health care personnel; human; major clinical study; male; nonhuman; nucleotide sequence; respiratory tract disease; SARS coronavirus; seroprevalence; severe acute respiratory syndrome; symptomatology; virus pneumonia","Tomlinson, B., Cockram, C., SARS: Experience at Prince of Wales Hospital, Hong Kong (2003) Lancet, 361, pp. 1486-1487; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2003; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Chan, P.K.S., Chu, W.C.W., Kwan, Y.W., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Li, T.S.T., Buckley, T.A., Yap, F.H.Y., Sung, J.J.Y., Joynt, G.M., Severe acute respiratory syndrome (SARS): Infection control (2003) Lancet, 361, p. 1386; Seto, W.H., Tsang, D., Yung, R.W.H., Ching, T.Y., Ng, T.K., Ho, M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520","Chan, P.K.S.; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, New Territories, Hong Kong; email: paulkschan@cuhk.edu.hk",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14718090","English","Emerg. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-10744223315
"Poon L.L.M., Chan K.H., Wong O.K., Yam W.C., Yuen K.Y., Guan Y., Lo Y.M.D., Peiris J.S.M.","7005441747;7406034307;56672516300;7004281720;36078079100;7202924055;7401935391;7005486823;","Early diagnosis of SARS Coronavirus infection by real time RT-PCR",2003,"Journal of Clinical Virology","28","3",,"233","238",,110,"10.1016/j.jcv.2003.08.004","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141763635&doi=10.1016%2fj.jcv.2003.08.004&partnerID=40&md5=0b90a876212a66e8f16ce03e27c01734","Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Department of Microbiology, Queen Mary Hospital, Pokfulam, Hong Kong; Department of Chemical Pathology, Chinese University of Hong Kong, Shatin, Hong Kong","Poon, L.L.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Chan, K.H., Department of Microbiology, Queen Mary Hospital, Pokfulam, Hong Kong; Wong, O.K., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Yam, W.C., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Yuen, K.Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Guan, Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; Lo, Y.M.D., Department of Chemical Pathology, Chinese University of Hong Kong, Shatin, Hong Kong; Peiris, J.S.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong","Background: A novel coronavirus was recently identified as the aetiological agent of Severe Acute Respiratory Syndrome (SARS). Molecular assays currently available for detection of SARS-coronavirus (SARS-Cov) have low sensitivity during the early stage of the illness. Objective: To develop and evaluate a sensitive diagnostic test for SARS by optimizing the viral RNA extraction methods and by applying real-time quantitative RT-PCR technology. Study design: 50 nasopharyngeal aspirate (NPA) samples collected from days 1-3 of disease onset from SARS patients in whom SARS CoV infections was subsequently serologically confirmed and 30 negative control samples were studied. Samples were tested by: (1) our first generation conventional RT-PCR assay with a routine RNA extraction method (Lancet 361 (2003) 1319), (2) our first generation conventional RT-PCR assay with a modified RNA extraction method, (3) a real-time quantitative RT-PCR assay with a modified RNA extraction method. Results: Of 50 NPA specimens collected during the first 3 days of illness, 11 (22%) were positive in our first generation RT-PCR assay. With a modification in the RNA extraction protocol, 22 (44%) samples were positive in the conventional RT-PCR assay. By combining the modified RNA extraction method and real-time quantitative PCR technology, 40 (80%) of these samples were positive in the real-time RT-PCR assay. No positive signal was observed in the negative controls. Conclusion: By optimizing RNA extraction methods and applying quantitative real time RT-PCR technologies, the sensitivity of tests for early diagnosis of SARS can be greatly enhanced. © 2003 Published by Elsevier B.V.","Early diagnosis; Real time RT-PCR; SARS Coronavirus","article; aspiration; controlled study; Coronavirus; diagnostic accuracy; diagnostic test; early diagnosis; evaluation; human; intermethod comparison; major clinical study; patient selection; priority journal; reverse transcription polymerase chain reaction; RNA extraction; sample size; SARS coronavirus; severe acute respiratory syndrome; upper respiratory tract infection; virus detection; virus diagnosis; virus identification; virus isolation; virus pneumonia","Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) New Engl J Med, 348, pp. 1967-1976; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van den Hoogen, B.G., Peiris, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Kaiser, L., Briones, M.S., Hayden, F.G., Performance of virus isolation and Directigen Flu A to detect influenza A virus in experimental human infections (1999) J Clin Virol, 14, pp. 191-197; Kuiken, T., Fouchier, R.A., Schutten, M., Rimmelzwaan, G.F., Van Amerongen, G., Van Riel, D., Laman, J.D., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) New Engl J Med, 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.I., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Poon, L.L., Wong, O.K., Chan, K.H., Luk, W., Yuen, K.Y., Peiris, J.S., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 953-955; Poon LL, Chan KH, Wong OK, Cheung TK, Ng I, Seto WH, Zheng BJ et al., Detection of SARS Coronavirus in SARS patients by conventional and real-time quantitative RT-PCR assays. Clin Chem 2003b, submitted for publication; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Identification of severe acute respiratory syndrome in Canada (2003) New Engl J Med, 348, pp. 1995-2005; Riley, S., Fraser, C., Donnelly, C.A., Ghani, A.C., Abu-Raddad, L.J., Hedley, A.J., Leung, G.M., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) New Engl J Med, 348, pp. 1977-1985","Poon, L.L.M.; Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong; email: llmpoon@hkucc.hku.hk",,"Elsevier",13866532,,JCVIF,"14522060","English","J. Clin. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141763635
"Yi Y.P., Li C.F., Shi Y.L., Li L.H., Li P., Huang W., Wang S.Q., Ma Q.J., Cao C.","7202372661;10044061200;57199386357;55768805700;56461680300;55574189398;57191716588;7402813647;7401501779;","Over-expression in Escherichia coli and purification of nucleocaspid and membrane protein of SARS coronavirus",2003,"Sheng wu gong cheng xue bao = Chinese journal of biotechnology","19","4",,"392","396",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-5644230417&partnerID=40&md5=dd958047c94c9797f4051a58f59323bb","Beijing Institute of Biotechnology, Beijing, 100850, China","Yi, Y.P., Beijing Institute of Biotechnology, Beijing, 100850, China; Li, C.F., Beijing Institute of Biotechnology, Beijing, 100850, China; Shi, Y.L., Beijing Institute of Biotechnology, Beijing, 100850, China; Li, L.H., Beijing Institute of Biotechnology, Beijing, 100850, China; Li, P., Beijing Institute of Biotechnology, Beijing, 100850, China; Huang, W., Beijing Institute of Biotechnology, Beijing, 100850, China; Wang, S.Q., Beijing Institute of Biotechnology, Beijing, 100850, China; Ma, Q.J., Beijing Institute of Biotechnology, Beijing, 100850, China; Cao, C., Beijing Institute of Biotechnology, Beijing, 100850, China","Genes encoding nucleocaspid (N) and membrane (M) protein of SARS coronavirus were obtained by RT-PCR and were cloned into expression vector pET22b and pBV222. DNA sequencing showed that the genes cloned from a patient in Beijing were identical to the gene sequences from reported Toronto strain. The genes were over-expressed in E. coli either as inclusion body or as soluble form. The recombinant proteins were purified by ion-exchange, or ion-exchange followed by metal chelate affinity chromatography. The recombinant N protein was demonstrated highly antigenic and could be employed as antigen to detect SARS antibodies in ELISA system for SARS diagnosis.",,"nucleocapsid protein; virus protein; affinity chromatography; article; enzyme linked immunosorbent assay; Escherichia coli; genetics; ion exchange chromatography; isolation and purification; metabolism; reverse transcription polymerase chain reaction; SARS coronavirus; Chromatography, Affinity; Chromatography, Ion Exchange; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Nucleocapsid Proteins; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Viral Structural Proteins",,"Yi, Y.P.",,,10003061,,,"15969052","Chinese","Sheng Wu Gong Cheng Xue Bao",Article,"Final",,Scopus,2-s2.0-5644230417
"Elia G., Fiermonte G., Pratelli A., Martella V., Camero M., Cirone F., Buonavoglia C.","7005135633;7003522893;7004884960;7003300496;6701658830;6602223775;7005623145;","Recombinant M protein-based ELISA test for detection of antibodies to canine coronavirus",2003,"Journal of Virological Methods","109","2",,"139","142",,16,"10.1016/S0166-0934(03)00064-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242669953&doi=10.1016%2fS0166-0934%2803%2900064-8&partnerID=40&md5=f54dd6a72d64c98f5358fc2e2ee00d07","Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Lab. of Biochem./Molecular Biology, Department of Pharmaco-Biology, University of Bari, Bari, Italy","Elia, G., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Fiermonte, G., Lab. of Biochem./Molecular Biology, Department of Pharmaco-Biology, University of Bari, Bari, Italy; Pratelli, A., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Martella, V., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Camero, M., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Cirone, F., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Buonavoglia, C., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy","The membrane (M) protein of canine coronavirus (CCoV) was cloned and expressed in E. coli. The purified recombinant protein was then evaluated for its antigenicity and reliability in an enzyme-linked immunosorbent assay (ELISA) for detection of CCoV antibodies in dog sera. Fifty serum samples, screened previously by whole virus ELISA and Western blotting, were tested. When the performance of the new test was compared with those of whole virus ELISA and Western blotting, an excellent correlation was found with the latter two assays. The ELISA based on recombinant M protein represents an alternative and valid test for detection of antibodies to CCoV in dog sera. © 2003 Elsevier Science B.V. All rights reserved.","Canine coronavirus; ELISA; Recombinant M protein","membrane protein; recombinant protein; virus antibody; antibody detection; antibody screening; antigenicity; article; blood analysis; blood sampling; Coronavirus; correlation analysis; dog; enzyme linked immunosorbent assay; Escherichia coli; intermethod comparison; molecular cloning; nonhuman; priority journal; protein expression; reliability; Western blotting; Canine coronavirus; Canis familiaris; Coronavirus","Buonavoglia, C., Marsilio, F., Cavalli, A., Tiscar, P.G., L'infezione da coronavirus del cane: Indagine sulla presenza del virus in Italia (1994) Not. Farm. Vet. Nr. 2/94, ed. SCIVAC; Carmichael, L.E., Binn, L.N., New canine enteric viral infection (1981) Adv. Vet. Sci., 25, pp. 1-37; De Hann, C.A., Vennema, H., Rottier, P.J., Assembly of the coronavirus envelope: Homotypic interactions between the M proteins (2000) J. Virol., 74, pp. 4967-4978; Elia, G., Decaro, N., Tinelli, A., Martella, V., Pratelli, A., Buonavoglia, C., Evaluation of antibody response to canine coronavirus infection in dogs by Western blotting analysis (2002) New Microbiol., 25 (3), pp. 275-280; Fiermonte, G., Walker, J.E., Palmieri, F., Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria (1993) Biochem. J., 294, pp. 293-299; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Horsburgh, B.C., Brierley, I., Brown, T.D.K., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Murphy, F.A., Virus taxonomy (1996) Fundamental Virology, 1, pp. 15-57. , B.N. Fields, D.M. Knipe, Howley P.M. third ed. Philadelphia, PA: Lippincott-Raven Publishers; Pratelli, A., Elia, G., Martella, V., Palmieri, A., Cirone, F., Tinelli, A., Corrente, M., Buonavoglia, C., Prevalence of canine coronavirus antibodies by an enzyme-linked immunosorbent assay in dogs in the south of Italy (2002) J. Virol. Methods, 102, pp. 67-71; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein (2000) Eur. J. Virol., 74, pp. 2333-2342; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S.G. Siddel. New York: Plenum Press; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M.J., Gebaues, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Siddell, S.G., The coronaviridae, an introduction (1995) The Coronaviridae, pp. 1-10. , S.G. Siddell. New York: Plenum Press; Siddell, S.G., Wege, H., Meulen, V., The biology of coronaviruses (1983) J. Gen. Virol., 64, pp. 761-776; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794; Woods, R.D., Wesley, R., Kapke, P.A., Complement-dependent neutralization of transmissible gastroenteritis virus by monoclonal antibodies (1987) Adv. Exp. Med. Biol., 218, pp. 493-500","Pratelli, A.; Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,"Elsevier",01660934,,JVMED,"12711056","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0242669953
"Tsang O.T.-Y., Chau T.-N., Choi K.-W., Tso E.Y.-K., Lim W., Chiu M.-C., Tong W.-L., Lee P.-O., Lam B.H.S., Ng T.-K., Lai J.-Y., Yu W.-C., Lai S.-T.","6602450830;7102000078;37098634700;6603816466;7202378277;7101865538;7202449348;19735398300;7102023583;7402229817;57216111385;7403914214;7402937038;","Coronavirus-positive Nasopharyngeal Aspirate as Predictor for Severe Acute Respiratory Syndrome Mortality",2003,"Emerging Infectious Diseases","9","11",,"1381","1387",,58,"10.3201/eid0911.030400","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744233001&doi=10.3201%2feid0911.030400&partnerID=40&md5=d8796ca543786a829d63aabe82b9f17a","Princess Margaret Hospital, Hong Kong, Hong Kong; Public Health Laboratory Centre, Hong Kong, Hong Kong; Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Lai King, Kowloon, Hong Kong","Tsang, O.T.-Y., Princess Margaret Hospital, Hong Kong, Hong Kong; Chau, T.-N., Princess Margaret Hospital, Hong Kong, Hong Kong; Choi, K.-W., Princess Margaret Hospital, Hong Kong, Hong Kong; Tso, E.Y.-K., Princess Margaret Hospital, Hong Kong, Hong Kong; Lim, W., Public Health Laboratory Centre, Hong Kong, Hong Kong; Chiu, M.-C., Princess Margaret Hospital, Hong Kong, Hong Kong; Tong, W.-L., Princess Margaret Hospital, Hong Kong, Hong Kong; Lee, P.-O., Princess Margaret Hospital, Hong Kong, Hong Kong; Lam, B.H.S., Princess Margaret Hospital, Hong Kong, Hong Kong; Ng, T.-K., Princess Margaret Hospital, Hong Kong, Hong Kong; Lai, J.-Y., Princess Margaret Hospital, Hong Kong, Hong Kong; Yu, W.-C., Princess Margaret Hospital, Hong Kong, Hong Kong; Lai, S.-T., Princess Margaret Hospital, Hong Kong, Hong Kong, Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Lai King, Kowloon, Hong Kong","Severe acute respiratory syndrome (SARS) has caused a major epidemic worldwide. A novel coronavirus is deemed to be the causative agent. Early diagnosis can be made with reverse transcriptase-polymerase chain reaction (RT-PCR) of nasopharyngeal aspirate samples. We compared symptoms of 156 SARS-positive and 62 SARS-negative patients in Hong Kong; SARS was confirmed by RT-PCR. The RT-PCR-positive patients had significantly more shortness of breath, a lower lymphocyte count, and a lower lactate dehydrogenase level; they were also more likely to have bilateral and multifocal chest radiograph involvement, to be admitted to intensive care, to need mechanical ventilation, and to have higher mortality rates. By multivariate analysis, positive RT-PCR on nasopharyngeal aspirate samples was an independent predictor of death within 30 days.",,"lactate dehydrogenase; adult; article; artificial ventilation; clinical feature; comorbidity; Coronavirus; dyspnea; epidemic; female; Hong Kong; human; intensive care; lactate dehydrogenase blood level; lung aspiration; lymphocytopenia; major clinical study; male; mortality; multivariate analysis; nasopharyngeal aspiration; outcomes research; respiratory distress syndrome; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; thorax radiography","Updated Interim U.S. Case Cefinition of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/casedefinition.htm; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.N., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Severe Acute Respiratory Syndrome - Press Briefing, , http://www.who.int/csr/sars/2003_04_16/en/, Wednesday, 16 April, 13:30 Palais des Nations; Recommendations for Laboratories Testing by RT-PCR for Presence of SARS Coronavirus -RNA, , http://www.who.int/csr/sars/coronarecommendations/en/; Sampling for Severe Acute Respiratory Syndrome (SARS) Diagnostic Tests, , http://www.who.int/csr/sars/sampling/en/#sampling","Lai, S.-T.; Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Lai King, Kowloon, Hong Kong; email: lstpmh@netvigator.com",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14718079","English","Emerg. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-10744233001
"Lin Y., Shen X., Yang R.F., Li Y.X., Ji Y.Y., He Y.Y., Shi M.D., Lu W., Shi T.L., Wang J., Wang H.X., Jiang H.L., Shen J.H., Xie Y.H., Wang Y., Pei G., Shen B.F., Wu J.R., Sun B.","57199187973;7402721498;55547041600;35227517800;12771705200;14833732700;7201371117;36077781100;7202756564;55742696200;7501732532;34868049700;7404929839;8677139000;7601499551;6603216929;7401582245;7409253402;24734369900;","Identification of an epitope of SARS-coronavirus nucleocapsid protein.",2003,"Cell research","13","3",,"141","145",,37,"10.1038/sj.cr.7290158","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0942275650&doi=10.1038%2fsj.cr.7290158&partnerID=40&md5=d14094cad941047630fe6f1fe7b3a74b","Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China","Lin, Y., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Shen, X., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Yang, R.F., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Li, Y.X., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Ji, Y.Y., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; He, Y.Y., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Shi, M.D., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Lu, W., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Shi, T.L., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Wang, J., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Wang, H.X., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Jiang, H.L., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Shen, J.H., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Xie, Y.H., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Wang, Y., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Pei, G., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Shen, B.F., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Wu, J.R., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Sun, B., Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China","The nucleocapsid (N) protein of severe acute respiratory syndrome-coronavirus (SARS-CoV) is a major virion structural protein. In this study, two epitopes (N1 and N2) of the N protein of SARS-CoV were predicted by bioinformatics analysis. After immunization with two peptides, the peptides-specific antibodies were isolated from the immunized rabbits. The further experiments demonstrated that N1 peptide-induced polyclonal antibodies had a high affinity to bind to E. coli expressed N protein of SARS-CoV. Furthermore, it was confirmed that N1 peptide-specific IgG antibodies were detectable in the sera of severe acute respiratory syndrome (SARS) patients. The results indicated that an epitope of the N protein has been identified and N protein specific Abs were produced by peptide immunization, which will be usefull for the study of SARS-CoV.",,"epitope; immunoglobulin G; nucleocapsid protein; peptide fragment; virus antibody; amino acid sequence; animal; antibody specificity; article; blood; chemistry; enzyme linked immunosorbent assay; gene vector; genetics; human; immunization; immunology; isolation and purification; molecular genetics; protein binding; rabbit; SARS coronavirus; Western blotting; Amino Acid Sequence; Animals; Antibodies, Viral; Antibody Specificity; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Epitopes; Genetic Vectors; Humans; Immunization; Immunoglobulin G; Molecular Sequence Data; Nucleocapsid Proteins; Peptide Fragments; Protein Binding; Rabbits; SARS Virus",,"Lin, Y.",,,10010602,,,"12862314","English","Cell Res.",Article,"Final",Open Access,Scopus,2-s2.0-0942275650
"Haring J.S., Perlman S.","7101956116;7102708317;","Bystander CD4 T cells do not mediate demyelination in mice infected with a neurotropic coronavirus",2003,"Journal of Neuroimmunology","137","1-2",,"42","50",,17,"10.1016/S0165-5728(03)00041-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037376323&doi=10.1016%2fS0165-5728%2803%2900041-9&partnerID=40&md5=e042799b1e3b3d2517b1967513e979e7","Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Haring, J.S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States","Demyelination following infection of mice with the neurotropic coronavirus mouse hepatitis virus strain JHM (MHV) is immune-mediated. It has been demonstrated that MHV-specific CD4 and CD8 T cells are capable of causing demyelination independent of the other T cell subset. Recent work has also demonstrated that activated bystander CD8 T cells mediate significant demyelination. The ability of bystander CD4 T cells to mediate demyelination was investigated using CD4 T cell transgenic mice. The results indicated that bystander CD4 T cells were unable to cause demyelination in MHV-infected mice, despite being recruited into the central nervous system (CNS) and irrespective of activation status. These results suggest that CD4 T cells must recognize antigen in the CNS in order to cause demyelination. © 2003 Elsevier Science B.V. All rights reserved.","Cell trafficking; Demyelination; T lymphocytes; Transgenic/knockout; Viral","CD4 antigen; animal cell; animal experiment; animal model; animal tissue; article; central nervous system; controlled study; Coronavirus; demyelination; mouse; nonhuman; priority journal; T lymphocyte; transgenic mouse; virus activation; virus infection","Bauer, J., Bradl, M., Hickey, W., Forss-peter, S., Breitscopf, H., Linington, C., Wekerle, H., Lassmann, H., T-cell apoptosis in inflammatory brain lesions: Destruction of T cells does not depend on antigen recognition (1998) Am. J. Pathol., 153, pp. 715-724; Brabb, T., Von Dassow, P., Ordonez, N., Schnabel, B., Duke, B., Goverman, J., In situ tolerance within the central nervous system as a mechanism for preventing autoimmunity (2000) J. Exp. Med., 192, pp. 871-880; Brehm, M.A., Pinto, A.K., Daniels, K.A., Schneck, J.P., Welsh, R.M., Selin, L.K., T cell immunodominance and maintenance of memory regulated by unexpectedly cross-reactive pathogens (2002) Nat. Immunol., 3, pp. 627-634; Deshpande, S., Zheng, M., Lee, S., Banerjee, K., Gangappa, S., Kumaraguru, U., Rouse, B., Bystander activation involving T lymphocytes in herpetic stromal keratitis (2001) J. Immunol., 167, pp. 2902-2910; Ehl, S., Hombach, J., Aichele, P., Hengartner, H., Zinkernagel, R.M., Bystander activation of cytotoxic T Cells: Studies on the mechanism and evaluation of in vivo significance in a transgenic mouse model (1997) J. Exp. Med., 185, pp. 1241-1251; Fleming, J.O., Trousdale, M.D., El-Zaatari, F., Stohlman, S.A., Weiner, L.P., Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies (1986) J. Virol., 58, pp. 869-875; Gangappa, S., Deshpande, S., Rouse, B., Bystander activations of CD4+ T cells can represent an exclusive means of immunopathology in a virus infection (1999) Eur. J. Immunol., 29, pp. 3674-3682; Haring, J.S., Pewe, L.L., Perlman, S., High magnitude, virus-specific CD4 T-cell response in the central nervous system of coronavirus-infected mice (2001) J. Virol., 75, pp. 3043-3047; Haring, J., Pewe, L., Perlman, S., Bystander CD8 T cell-mediated demyelination after viral infection of the central nervous system (2002) J. Immunol., 169, pp. 1550-1555; Hickey, W.F., Hsu, B.L., Kimura, H., T-lymphocyte entry into the central nervous system (1991) J. Neurosci. Res., 28, pp. 254-260; Houtman, J.J., Fleming, J.O., Dissociation of demyelination and viral clearance in congenitally immunodeficient mice infected with murine coronavirus JHM (1996) J. Neurovirol., 2, pp. 101-110; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Huseby, E., Liggitt, D., Brabb, T., Schnabel, B., Ohlen, C., Governman, J., A pathogenic role for myelin-specific CD8+ T cells in a model for multiple sclerosis (2001) J. Exp. Med., 194, pp. 669-676; Krakowski, M., Owens, T., Naive T lymphocytes traffic to inflamed central nervous system, but require antigen recognition for activation (2000) Eur. J. Immunol., 30, pp. 1002-1009; Lane, T.E., Liu, M.T., Chen, B.P., Asensio, V.C., Samawi, R.M., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., A central role for CD4+ T-cells and RANTES in virus-induced central nervous system inflammation and demyelination (2000) J. Virol., 74, pp. 1415-1424; Liu, M.T., Chen, B.P., Oertel, P., Buchmeier, M.J., Armstrong, D., Hamilton, T.A., Lane, T.E., The T cell chemoattractant IFN-inducible protein 10 is essential in host defense against viral-induced neurologic disease (2000) J. Immunol., 165, pp. 2327-2330; Liu, M.T., Armstrong, D., Hamilton, T.A., Lane, T.E., Expression of Mig (monokine induced by interferon-gamma) is important in T lymphocyte recruitment and host defense following viral infection of the central nervous system (2001) J. Immunol., 166, pp. 1790-1795; Liu, M.T., Keirstead, H.S., Lane, T.E., Neutralization of the chemokine CXCL10 reduces inflammatory cell invasion and demyelination and improves neurological function in a viral model of multiple sclerosis (2001) J. Immunol., 167, pp. 4091-4097; Marten, N.W., Stohlman, S.A., Atkinson, R.D., Hinton, D.R., Fleming, J.O., Bergmann, C.C., Contributions of CD8+ T cells and viral spread to demyelinating disease (2000) J. Immunol., 164, pp. 4080-4088; Marten, N.W., Stohlman, S.A., Bergmann, C.C., Role of viral persistence in retaining CD8(+) T cells within the central nervous system (2000) J. Virol., 74, pp. 7903-7910; Miller, S.D., Vanderlugt, C., Begolka, W., Pao, W., Yauch, R., Neville, K., Katz-Levy, Y., Kim, B., Persistent infection with Theiler's virus leads to CNS autoimmunity via epitope spreading (1997) Nat. Med., 3, pp. 1133-1136; Morkowski, S., Goldrath, A.W., Eastman, S., Ramachandra, L., Freed, D.C., Whiteley, P., Rudensky, A., T cell recognition of major histocompatibility complex class II complexes with invariant chain processing intermediates (1995) J. Exp. Med., 182, pp. 1403-1413; Perlman, S., Schelper, R., Bolger, E., Ries, D., Late onset, symptomatic, demyelinating encephalomyelitis in mice infected with MHV-JHM in the presence of maternal antibody (1987) Microb. Pathog., 2, pp. 185-194; Pewe, L., Perlman, S., Immune response to the immunodominant epitope of mouse hepatitis virus is polyclonal, but functionally monospecific in C57Bl/6 mice (1999) Virology, 255, pp. 106-116; Pewe, L., Perlman, S., Cutting edge: CD8 T cell-mediated demyelination is IFN-g dependent in mice infected with a neurotropic coronavirus (2002) J. Immunol., 168, pp. 1547-1551; Pewe, L., Heard, S.B., Bergmann, C.C., Dailey, M.O., Perlman, S., Selection of CTL escape mutants in mice infected with a neurotropic coronavirus: Quantitative estimate of TCR diversity in the infected CNS (1999) J. Immunol., 163, pp. 6106-6113; Pewe, L., Haring, J., Perlman, S., CD4 T-cell-mediated demyelination is increased in the absence of gamma interferon in mice infected with mouse hepatitis virus (2002) J. Virol., 76, pp. 7329-7333; Selin, L., Nahill, S., Welsh, R., Cross-reactivities in memory cytotoxic T lymphocyte recognition of heterologous viruses (1994) J. Exp. Med., 179, pp. 1933-1943; Selin, L., Varga, S., Wong, I., Welsh, R., Protective heterologous antiviral immunity and enhanced immunopathogenesis mediated by memory T cell populations (1998) J. Exp. Med., 188, pp. 1705-1715; Stohlman, S.A., Bergmann, C.C., Perlman, S., Mouse hepatitis virus (1999) Persistent Viral Infections, pp. 537-557. , R. Ahmed, & I. Chen. New York: Wiley; Varga, S., Welsh, R., Detection of a high frequency of virus-specific CD4+ T cells during acute infection with lymphocytic choriomeningitis virus (1998) J. Immunol., 161, pp. 3215-3218; Varga, S.M., Welsh, R., High frequency of virus-specific interleukin-2-producing CD4+ T cells and Th1 predominance during lymphocytic choriomeningitis virus infection (2000) J. Virol., 74, pp. 4429-4432; Wang, F., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-41; Watanabe, R., Wege, H., Ter Meulen, V., Adoptive transfer of EAE-like lesions from rats with coronavirus-induced demyelinating encephalomyelitis (1983) Nature, 305, pp. 150-153; Whitmire, J.K., Asano, M.S., Murali-Krishna, K., Suresh, M., Ahmed, R., Long-term CD4 Th1 and Th2 memory following acute lymphocytic choriomeningitis virus infection (1998) J. Virol., 72, pp. 8281-8288; Williams, K.C., Hickey, W.F., Traffic of hematogenous cells through the central nervous system (1995) Curr. Top. Microbiol. Immunol., 202, pp. 221-245; Wong, P., Goldrath, A., Rudensky, A., Competition for specific intrathymic ligands limits positive selection in a TCR transgenic model of CD4+ T cell development (2000) J. Immunol., 164, pp. 6252-6259; Wu, G.F., Perlman, S., Macrophage infiltration, but not apoptosis, is correlated with immune-mediated demyelination following murine infection with a neurotropic coronavirus (1999) J. Virol., 73, pp. 8771-8780; Wu, G.F., Dandekar, A.A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286; Xue, S., Sun, N., Van Rooijen, N., Perlman, S., Depletion of blood-borne macrophages does not reduce demyelination in mice infected with a neurotropic coronavirus (1999) J. Virol., 73, pp. 6327-6334","Perlman, S.; Department of Pediatrics, University of Iowa, Medical Laboratories 2042, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,"Elsevier",01655728,,JNRID,"12667646","English","J. Neuroimmunol.",Article,"Final",Open Access,Scopus,2-s2.0-0037376323
"Chow K.Y., Hon C.C., Hui R.K., Wong R.T., Yip C.W., Zeng F., Leung F.C.","7202180875;7003617137;7103304764;24759484000;7101665559;7202911544;55440652300;","Molecular advances in severe acute respiratory syndrome-associated coronavirus (SARS-CoV).",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","4",,"247","262",,10,"10.1016/S1672-0229(03)01031-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13844281686&doi=10.1016%2fS1672-0229%2803%2901031-3&partnerID=40&md5=48141ac24b2ff23699fc2bc83cc6c6db","Department of Zoology, The University of Hong Kong, Hong Kong SAR, China","Chow, K.Y., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Hon, C.C., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Hui, R.K., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Wong, R.T., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Yip, C.W., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Zeng, F., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China; Leung, F.C., Department of Zoology, The University of Hong Kong, Hong Kong SAR, China","The sudden outbreak of severe acute respiratory syndrome (SARS) in 2002 prompted the establishment of a global scientific network subsuming most of the traditional rivalries in the competitive field of virology. Within months of the SARS outbreak, collaborative work revealed the identity of the disastrous pathogen as SARS-associated coronavirus (SARS-CoV). However, although the rapid identification of the agent represented an important breakthrough, our understanding of the deadly virus remains limited. Detailed biological knowledge is crucial for the development of effective countermeasures, diagnostic tests, vaccines and antiviral drugs against the SARS-CoV. This article reviews the present state of molecular knowledge about SARS-CoV, from the aspects of comparative genomics, molecular biology of viral genes, evolution, and epidemiology, and describes the diagnostic tests and the anti-viral drugs derived so far based on the available molecular information.",,"virus vaccine; animal; drug design; genetics; human; immunology; isolation and purification; molecular evolution; review; SARS coronavirus; severe acute respiratory syndrome; virology; Animals; Drug Design; Evolution, Molecular; Humans; SARS Virus; Severe Acute Respiratory Syndrome; Viral Vaccines",,"Chow, K.Y.",,,16720229,,,"15629054","English","Genomics Proteomics Bioinformatics",Review,"Final",Open Access,Scopus,2-s2.0-13844281686
"Zelus B.D., Schickli J.H., Blau D.M., Weiss S.R., Holmes K.V.","6602571243;6603027057;15729433700;57203567044;7201657724;","Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAM1 receptors or by pH 8",2003,"Journal of Virology","77","2",,"830","840",,83,"10.1128/JVI.77.2.830-840.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037223630&doi=10.1128%2fJVI.77.2.830-840.2003&partnerID=40&md5=4666928a625fafc249d0e9ad7ad42f64","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Zelus, B.D., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Schickli, J.H., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Blau, D.M., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., Philadelphia, PA 19104, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","The spike glycoprotein (S) of the murine coronavirus mouse hepatitis virus (MHV) binds to viral murine CEACAM receptor glycoproteins and causes membrane fusion. On virions, the 180-kDa S glycoprotein of the MHV-A59 strain can be cleaved by trypsin to form the 90-kDa N-terminal receptor-binding subunit (S1) and the 90-kDa membrane-anchored fusion subunit (S2). Incubation of virions with purified, soluble CEACAM1a receptor proteins at 37°C and pH 6.5 neutralizes virus infectivity (B. D. Zelus, D. R. Wessner, R. K. Williams, M. N. Pensiero, F. T. Phibbs, M. deSouza, G. S. Dveksler, and K. V. Holmes, J. Virol. 72:7237-7244, 1998). We used liposome flotation and protease sensitivity assays to investigate the mechanism of receptor-induced, temperature-dependent virus neutralization. After incubation with soluble receptor at 37°C and pH 6.5, virions became hydrophobic and bound to liposomes. Receptor binding induced a profound, apparently irreversible conformational change in S on the viral envelope that allowed S2, but not S1, to be degraded by trypsin at 4°C. Various murine CEACAM proteins triggered conformational changes in S on recombinant MHV strains expressing S glycoproteins of MHV-A59 or MHV-4 (MHV-JHM) with the same specificities as seen for virus neutralization and virus-receptor activities. Increased hydrophobicity of virions and conformational change in S2 of MHV-A59 could also be induced by incubating virions at pH 8 and 37°C, without soluble receptor. Surprisingly, the S protein of recombinant MHV-A59 virions with a mutation, H716D, that precluded cleavage between S1 and S2 could also be triggered to undergo a conformational change at 37°C by soluble receptor at neutral pH or by pH 8 alone. A novel 120-kDa subunit was formed following incubation of the receptor-triggered SA59H716D virions with trypsin at 4°C. The data show that unlike class 1 fusion glycoproteins of other enveloped viruses, the murine coronavirus S protein can be triggered to a membrane-binding conformation at 37°C either by soluble receptor at neutral pH or by alkaline pH alone, without requiring previous activation by cleavage between S1 and S2.",,"carcinoembryonic antigen cell adhesion molecule 1 receptor; glycoprotein; liposome; protein; protein subunit; proteinase; trypsin; unclassified drug; animal cell; article; conformational transition; controlled study; hydrophobicity; molecular biology; molecular weight; mouse; Murine hepatitis coronavirus; nonhuman; pH; priority journal; protein expression; receptor binding; solubility; temperature; virion; virus neutralization; virus recombinant; virus strain; 3T3 Cells; Animals; Antigens, CD; Antigens, Differentiation; Carcinoembryonic Antigen; Cell Adhesion Molecules; Coronavirus; Heat; Hydrogen-Ion Concentration; Liposomes; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Protein Binding; Protein Conformation; Viral Envelope Proteins","Baker, K.A., Dutch, R.E., Lamb, R.A., Jardetzky, T.S., Structural basis for paramyxovirus-mediated membrane fusion (1999) Mol. 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Harwood Academic Publishers, Amsterdam, The Netherlands","Holmes, K.V.; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; email: kathryn.holmes@uchsc.edu",,,0022538X,,JOVIA,"12502799","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037223630
"Wu G., Yan S.","7404976281;7401744517;","Prediction of amino acid pairs sensitive to mutations in the spike protein from SARS related coronavirus",2003,"Peptides","24","12",,"1837","1845",,16,"10.1016/j.peptides.2003.10.008","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0842287567&doi=10.1016%2fj.peptides.2003.10.008&partnerID=40&md5=bb69214adaad2b723f9ff6f197b4898d","DreamSciTech Consult. Co. Ltd., 301, Building 12, Nanyou A-zone, Jainnan Road, CN-518054, Shenzhen, China","Wu, G., DreamSciTech Consult. Co. Ltd., 301, Building 12, Nanyou A-zone, Jainnan Road, CN-518054, Shenzhen, China; Yan, S., DreamSciTech Consult. Co. Ltd., 301, Building 12, Nanyou A-zone, Jainnan Road, CN-518054, Shenzhen, China","In this study, we analyzed the amino acid pairs affected by mutations in two spike proteins from human coronavirus strains 229E and OC43 by means of random analysis in order to gain some insight into the possible mutations in the spike protein from SARS-CoV. The results demonstrate that the randomly unpredictable amino acid pairs are more sensitive to the mutations. The larger is the difference between actual and predicted frequencies, the higher is the chance of mutation occurring. The effect induced by mutations is to reduce the difference between actual and predicted frequencies. The amino acid pairs whose actual frequencies are larger than their predicted frequencies are more likely to be targeted by mutations, whereas the amino acid pairs whose actual frequencies are smaller than their predicted frequencies are more likely to be formed after mutations. These findings are identical to our several recent studies, i.e. the mutations represent a process of degeneration inducing human diseases. © 2003 Elsevier Inc. All rights reserved.","Amino acid pairs; Coronavirus; Mutations; SARS","amino acid; SARS spike glycoprotein; spike protein; unclassified drug; virus protein; article; controlled study; gene frequency; gene mutation; gene targeting; nonhuman; prediction; priority journal; SARS coronavirus; severe acute respiratory syndrome; virus strain; Coronavirus; human coronavirus; SARS CoV","Bairoch, A., Apweiler, R., The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 2000 (2000) Nucleic. 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Biophys., 6, pp. 401-406; Wu, G., Yan, S.M., Estimation of amino acid pairs sensitive to variants in human phenylalanine hydroxylase protein by means of a random approach (2002) Peptides, 23, pp. 2085-2090; Wu, G., Yan, S., Analysis of amino acid pairs sensitive to variants in human collagen α5(IV) chain precursor by means of a random approach (2003) Peptides, 24, pp. 347-352; Wu, G., Yan, S., Determination of amino acid pairs sensitive to variants in human β-glucocerebrosidase by means of a random approach (2003) Protein Eng., 16, pp. 195-199; Wu, G., Yan, S.M., Determination of amino acid pairs in human haemoglobulin-chain sensitive to variants by means of a random approach (2003) Comp. Clin. Pathol., 12, pp. 21-25; Wu, G., Yan, S., Determination of amino acid pairs sensitive to variants in human Bruton's tyrosine kinase by means of a random approach (2003) Mol. Simul., 29, pp. 249-254; Wu, G., Yan, S., Determination of amino acid pairs sensitive to variants in human coagulation factor IX precursor by means of a random approach (2003) J. Biomed. Sci., 10, pp. 451-454; Wu, G., Yan, S., Determination of amino acid pairs in human p53 protein sensitive to mutations/variants by means of a random approach (2003) J. Mol. Mod., 9, pp. 337-341","Wu, G.; DreamSciTech Consult. Co. Ltd., 301, Building 12, Nanyou A-zone, Jainnan Road, CN-518054, Shenzhen, China; email: hongguanglishibahao@yahoo.com",,"Elsevier Inc.",01969781,,PEPTD,"15127935","English","Peptides",Article,"Final",Open Access,Scopus,2-s2.0-0842287567
"Sakulwira K., Vanapongtipagorn P., Theamboonlers A., Oraveerakul K., Poovorawan Y.","6507369253;7801599062;7005850197;6602379064;7102786191;","Prevalence of canine coronavirus and parvovirus infections in dogs with gastroenteritis in Thailand",2003,"Veterinarni Medicina","48","6",,"163","168",,14,"10.17221/5764-VETMED","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038298024&doi=10.17221%2f5764-VETMED&partnerID=40&md5=cc255aab54e5c03a67fc39dfd66c057f","Department of Anatomy, Faculty of Veterinary Science, Chulalongkorn University, Bangkok, Thailand; Viral Hepatitis Research Unit, Department of Pediatrics, Chulalongkorn University and Hospital, Bangkok, Thailand; Division of Virology, Department of Pathology, Faculty of Veterinary Science, Chulalongkorn University, Bangkok, Thailand","Sakulwira, K., Department of Anatomy, Faculty of Veterinary Science, Chulalongkorn University, Bangkok, Thailand; Vanapongtipagorn, P., Viral Hepatitis Research Unit, Department of Pediatrics, Chulalongkorn University and Hospital, Bangkok, Thailand; Theamboonlers, A., Viral Hepatitis Research Unit, Department of Pediatrics, Chulalongkorn University and Hospital, Bangkok, Thailand; Oraveerakul, K., Division of Virology, Department of Pathology, Faculty of Veterinary Science, Chulalongkorn University, Bangkok, Thailand; Poovorawan, Y., Viral Hepatitis Research Unit, Department of Pediatrics, Chulalongkorn University and Hospital, Bangkok, Thailand","Canine coronavirus (CCV) and canine parvovirus type 2 (CPV-2) are the causative agents of gastroenteritis in dogs. Seventy fecal samples from dogs with signs of gastroenteritis (vomiting and diarrhea), twenty-five fecal samples from healthy dogs and one CPV-2 vaccine strain were amplified by semi-nested polymerase chain reaction (PCR) and semi-nested reverse transcriptase polymerase chain reaction (RT-PCR), aimed at specifically studying the gene encoding the most abundant capsid protein VP2 of CPV-2 and spike protein of CCV. The specificity of the CCV RT-PCR product was evaluated by sequencing. Positive specimens comprised 44 samples (62.8%) and 9 samples (12.8%) for CPV-2 and CCV, respectively. In nine CCV positive samples, seven displayed co-infection between CCV and CPV-2. Our CCV sequence (AF482001) showed a 94.9% nucleotide identity to CCV reported in GenBank accession number D13096. High prevalence of CCV and CPV-2 infections was found in 1-2 month- and 3-6 month-old dogs, respectively. Molecular biology of these viruses is important primarily for epidemic control and preventive measures. © 2018 Czech Academy of Agricultural Sciences.","Canine coronavirus; Canine parvovirus type 2; Gastroenteritis; PCR","capsid protein; nucleotide; spike protein; unclassified drug; virus protein; virus vaccine; article; Coronavirus; diarrhea; dog; epidemic; feces analysis; female; gastroenteritis; gene amplification; gene sequence; male; nonhuman; Parvovirus; polymerase chain reaction; prevalence; prophylaxis; reverse transcription polymerase chain reaction; Thailand; virus infection; virus strain; vomiting; Canine coronavirus; Canine parvovirus; Canine parvovirus 2; Canis familiaris; Coronavirus; Parvovirus","Bandai, C., Ishiguro, S., Masuya, N., Hohdatsu, T., Mochizuki, M., Canine coronavirus infections in Japan: virological and epidemiological aspects (1999) J. Vet. Med. Sci, 61, pp. 731-736; Cha, T.A., Kolberg, J., Irvine, B., Stempien, M., Beall, E., Yano, M., Choo, O.L., Han, J.H., Use of a signature nucleotide sequence of hepatitis C virus for detection of viral RNA in human serum and plasma (1991) J. Clin. Microbiol, 9, pp. 2528-2534; Fulker, R., Wasmoen, T., Atchison, R., Chu, H.J., Acree, W., Efficacy of an inactivated vaccine against clinical disease caused by canine coronavirus (1995) Adv. Exp. Med. Biol, 380, pp. 229-234; Gamble, D.A., Lobbiani, A., Gramegna, M., Moore, L.E., Colucci, G., Development of a nested PCR assay for detection of feline infectious peritonitis virus in clinical specimens (1997) J. Clin. Microbiol, 35, pp. 673-675; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3' end of canine coronavirus genomic RNA (1992) J. Gen. Virol, 73, pp. 2849-2862; Mochizuki, M., San Gabriel, M.C., Nakatani, H., Yoshida, M., Comparison of polymerase chain reaction with virus isolation and hemagglutination assays for the detection of canine parvoviruses in fecal specimens (1993) Res. Vet. Sci, 55, pp. 60-63; Mochizuki, M., Hashimoto, M., Ishida, T., Recent epidemiological status of canine viral enteric infections and Giardia infection in Japan (2001) J. Vet. Med. Sci, 63, pp. 573-575; Pollock, R.V.H., Carmichael, L.E., Canine viral enteritis (1983) Vet. Clin. North Am. Small Anim. Pract, 13, pp. 551-566; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buona-voglia, C., Development of a nested PCR assay for the detection of canine coronavirus (1999) J. Virol. Methods, 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) J. Virol. Methods, 84, pp. 91-94; Sakulwira, K., Oraveerakul, K., Poovorawan, Y., Detection and genotyping of canine parvovirus in enteritic dogs by PCR and RFLP (2001) Science Asia, 27, pp. 143-147; Schunck, B., Kraft, W., Truyen, U., A simple touch-down polymerase chain reaction for the detection of canine parvovirus and feline panleukopenia virus in feces (1995) J. Virol. Methods, 55, pp. 427-433; Tingpalapong, M., Whitmire, R.E., Wafts, D.M., Burke, D.S., Binn, L.N., Tesaprateep, T., Laungtongkum, S., March-wicki, R.H., Epizootic of viral enteritis in dogs in Thailand (1982) Am. J. Vet. Res, 43, pp. 1687-1690; Truyen, U., Gruenberg, A., Chang, S.F., Obermaier, B., Veijalainen, P., Parrish, C.R., Evolution of the feline-subgroup parvoviruses and the control of canine host range in vivo (1995) J. Virol, 69, pp. 4702-4710; Uwatoko, K., Sunairi, M., Nakajima, M., Yamaura, K., Rapid method utilizing the polymerase chain reaction for detection of canine parvovirus in feces of diarrheic dogs (1995) Vet. Microbiol, 43, pp. 315-323","Poovorawan, Y.; Viral Hepatitis Research Unit, Department of Pediatrics, Faculty of Medicine, Chulalongkorn University and HospitalThailand; email: Yong.P@chula.ac.th",,"Czech Academy of Agricultural Sciences",03758427,,,,"English","Vet. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0038298024
"Ismail M.M., Tang Y., Saif Y.M.","36793864500;57199306900;35563198200;","Pathogenicity of Turkey coronavirus in Turkeys and chickens",2003,"Avian Diseases","47","3",,"515","522",,41,"10.1637/5917","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141683646&doi=10.1637%2f5917&partnerID=40&md5=36db77a19121a64f87da6ed626c839e8","Food Animal Health Research Program, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Dept. of Poultry and Fish Diseases, Coll. of Vet. Med. at Kafri-Elsheikh, Tanta University, Tanta, Egypt; Coll. of Anim. Sci. and Technology, Jiangxi Agricultural University, Nanchang City, 330045, China","Ismail, M.M., Food Animal Health Research Program, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States, Dept. of Poultry and Fish Diseases, Coll. of Vet. Med. at Kafri-Elsheikh, Tanta University, Tanta, Egypt; Tang, Y., Food Animal Health Research Program, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States, Coll. of Anim. Sci. and Technology, Jiangxi Agricultural University, Nanchang City, 330045, China; Saif, Y.M., Food Animal Health Research Program, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","We designed this study to compare the replication potential of turkey coronavirus (TCV) and its effect in chickens and turkeys and to study the effect of single and combined infection of turkey poults with TCV and astrovirus. We studied the pathogenicity of TCV in experimentally inoculated turkey poults and chickens by observing the clinical signs and gross lesions. Two trials were conducted with 1-day-old and 4-wk-old specific-pathogen-free turkey poults and chickens. One-day-old turkey poults developed diarrhea at 48 hr postinoculation. Poults euthanatized at 3, 5, and 7 days postinoculation had flaccid, pale, and thin-walled intestines with watery contents. The 4-wk-old turkeys had no clinical signs or gross lesions. One-day-old and 4-wk-old chicks developed no clinical signs or gross lesions although the TCV was detected in gut contents of the birds throughout the experimental period (14 days). In another experiment, mean plasma D-xylose concentrations in 3-day-old turkey poults inoculated with TCV, turkey astrovirus, or a combination of both viruses were significantly lower than in the uninoculated controls.","Astrovirus; Bluecomb; Chickens; D-xylose; Diarrhea; Enteritis; Poult enteritis-mortality syndrome; Turkey coronavirus; Turkeys","Animalia; Astroviridae; Aves; Coronavirus; Gallus gallus; Meleagris gallopavo; Turkey astrovirus; Turkey coronavirus","Adams, N.R., Hofstad, M.S., Isolation of transmissible enteritis agent of turkeys in avian embryos (1971) Avian Dis., 15, pp. 426-433; Andreasen, J.R., Jackwood, M.W., Hilt, D.A., Polymerase chain reaction amplification of the genome of infectious bronchitis virus (1991) Avian Dis., 35, pp. 216-220; Barnes, H.J., Guy, J.S., Poult enteritis-mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry, 10th Ed., pp. 1025-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Breslin, J.J., Smith, L.G., Fuller, F.G., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene region of turkey coronavirus (1999) Intervirology, 4, pp. 22-29; Breslin, J.J., Smith, L.G., Fuller, F.J., Guy, J.S., Sequence analysis of the turkey coronavirus nucleocapsid gene and 3′ untranslated region identifies the virus as a close relative of infectious bronchitis virus (1999) Virus Res., 65, pp. 187-193; Brown, T.P., Emory, W.H., Howell D.R., Jr., Acute enteritis in turkey poults, chickens and cattle as subclinical carriers (1995) Proc. 132nd Annual Meeting of the American Veterinary Medical Association, p. 26; Butterworth C.E., Jr., Perez-Santiago, E., DeJesus, J.M., Santini, R., Studies on the oral and parental administration of D(+)xylose (1959) N. Engl. J. Med., 261, pp. 157-163; Cavanagh, D., Mawditt, K., Shanna, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathol., 30, pp. 355-368; Doerfler, R.E., Cain, L.D., Edens, F.W., Parkhurst, C.R., Qureshi, M.A., Havenstein, G.B., D-xylose absorption as a measurement of malabsorption in poult enteritis and mortality syndrome (2000) Poult. Sci., 79, pp. 656-660; Eberts, T.J., Sample, R.H.B., Glick, M.R., Ellis, G.H., A simplified, colorimetric micromethod for xylose in Serum or urine, with phloroglucinol (1979) Clin. Chem., 25, pp. 1440-1443; Goodwin, M.A., Latimer, K.S., Nersessian, B.N., Fletcher, O.J., Quantitation of intestinal D-xylose absorption in normal and reovirus-inoculated turkeys (1984) Avian Dis., 28, pp. 959-967; Goodwin, M.A., Latimer, K.S., Nersessian, B.N., Fletcher, O.J., Quantitation of intestinal D-xylose absorption in normal turkeys (1984) Poult. Sci., 63, pp. 1742-1747; Guy, J.S., Turkey coronavirus is more closely related to avian infectious bronchitis virus than to mammalian coronavirus: A review (2000) Avian Pathol., 29, pp. 207-212; Guy, J., Barnes, H.J., Smith, L.J., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Ismail, M.M., Cho, K.O., Hasoksuz, M., Saif, L.J., Saif, Y.M., Antigenic and genomic relatedness of turkey-origin coronaviruses, bovine coronaviruses, and infectious bronchitis virus of chickens (2001) Avian Dis., 45, pp. 978-984; Moran E.T., Jr., Digestion and absorption of carbohydrates in fowl and events through prenatal development (1985) J. Nutr., 115, pp. 665-674; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Phelps, P.V., Edens, F.W., Gildersleeve, R.P., The post hatch physiology of the turkey poult. III. Yolk depletion and serum metabolites (1987) Comp. Biochem. Physiol., 87 A, pp. 409-415; Reynolds, D.L., Saif, Y.M., Astrovirus: A cause of an enteric disease in turkey poults (1986) Avian Dis., 30, pp. 728-735; Shawky, S.A., Saif, Y.M., Swayne, D.E., Role of circulating maternal anti-rotavirus IgG in protection of intestinal mucosal surface in turkey poults (1993) Avian Dis., 37, pp. 1041-1050; Snedecor, G.W., Cochran, W.G., One way classifications; analysis of variance (1980) Statistical Methods, 7th Ed., pp. 215-237. , The Iowa State University Press, Ames, IA; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from eleven coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Yu, M., Ismail, M.M., Qureshi, M.A., Dearth, R.N., Barnes, H.J., Saif, Y.M., Viral agents associated with poult enteritis and mortality syndrome: The role of a small round virus and a turkey coronavirus (2000) Avian Dis., 44, pp. 297-304; Yu, M., Tang, Y., Guo, M., Zhang, Q., Saif, Y.M., Characterization of a small round virus associated with the poult enteritis and mortality syndrome (2000) Avian Dis., 44, pp. 600-610","Saif, Y.M.; Food Animal Health Research Program, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"14562877","English","Avian Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0141683646
"Calibeo-Hayes D., Denning S.S., Stringham S.M., Guy J.S., Smith L.G., Watson D.W.","6504505071;7003871040;35585802200;7202723649;37109180900;35568492000;","Mechanical transmission of turkey coronavirus by domestic houseflies (Musca domestica Linnaeaus)",2003,"Avian Diseases","47","1",,"149","153",,24,"10.1637/0005-2086(2003)047[0149:MTOTCB]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037249822&doi=10.1637%2f0005-2086%282003%29047%5b0149%3aMTOTCB%5d2.0.CO%3b2&partnerID=40&md5=4354c9a5700eb3e7b830224f001db4f2","Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; Dept. Microbiol., Pathol.,/P., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States","Calibeo-Hayes, D., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; Denning, S.S., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; Stringham, S.M., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States; Guy, J.S., Dept. Microbiol., Pathol.,/P., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States; Smith, L.G., Dept. Microbiol., Pathol.,/P., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27695, United States; Watson, D.W., Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States","Domestic houseflies (Musca domestica Linnaeaus) were examined for their ability to harbor and transmit turkey coronavirus (TCV). Laboratory-reared flies were experimentally exposed to TCV by allowing flies to imbibe an inoculum comprised of turkey embryo-propagated virus (NC95 strain). TCV was detected in dissected crops from exposed flies for up to 9 hr postexposure; no virus was detected in crops of sham-exposed flies. TCV was not detected in dissected intestinal tissues collected from exposed or sham-exposed flies at any time postexposure. The potential of the housefly to directly transmit TCV to live turkey poults was examined by placing 7-day-old turkey poults in contact with TCV-exposed houseflies 3 hr after flies consumed TCV inoculum. TCV infection was detected in turkeys placed in contact with TCV-exposed flies at densities as low as one fly/bird (TCV antigens detected at 3 days post fly contact in tissues of 3/12 turkeys); however, increased rates of infection were observed with higher fly densities (TCV antigens detected in 9/12 turkeys after contact with 10 flies/bird). This study demonstrates the potential of the housefly to serve as a mechanical vector of TCV.","Housefly; Turkey coronavirus","Animalia; Aves; Coronavirus; Meleagris gallopavo; Musca domestica; Musca domestica; Turkey coronavirus","Axtell, R.C., Poultry integrated pest management: Status and future (1999) Integrated Pest Manage. Rev., 4, pp. 53-73; Barnes, H.J., Guy, J.S., Poult enteritismortality syndrome ('spiking mortality') of turkeys (1997) Diseases of Poultry, 10th Ed., pp. 1025-1031. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Bishopp, F.C., Laake, E.W., Dispersion of flies by flight (1921) J. Agric. Res., 21, pp. 729-766; Breslin, J.J., Smith, L.G., Barnes, H.J., Guy, J.S., Comparison of virus isolation, immunohistochemistry, and reverse transcriptase-polymerase chain reaction procedures for detection of turkey coronavirus (2000) Avian Dis., 44, pp. 624-631; Breslin, J.J., Smith, L.G., Guy, J.S., Baculovirus expression of turkey coronavirus nucleocapsid protein (2001) Avian Dis., 45, pp. 136-143; Gough, P.M., Jorgenson, R.D., Identification of porcine transmissible gastroenteritis virus in house flies (Musca domestica Linneaus) (1983) Am. J. Vet. Res., 44, pp. 2078-2082; Graczyk, T.K., Cranfield, M.R., Fayer, F., Bixler, H., House flies (Musca domestica) as transport hosts of Cryptosporidium parvum (1999) Am. J. Trop. Med., 61, pp. 500-504; Greenberg, B., (1973) Flies and Disease, Vol. II. Biology and Disease Transmission, 2. , Princeton University Press, Princeton, NJ; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Hainsworth, F.R., Fisher, G., Precup, E., Rates of energy processing by blowfies: The uses for a joule vary with food quality and quantity (1990) J. Exp. Biol., 150, pp. 257-268; Nagaraja, K.V., Pomeroy, B.S., Coronaviral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Reed, L.J., Muench, H., A simple method of estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Sinha, M., Digestive enzymes in the gut and salivary glands of Sarcophaga ruficornis Fab. and Musca domestica L. (Diptera: Insecta) (1976) Appl. Entomol. Zool., 11, pp. 260-262; Terra, W.R., Espinosa-Fuentes, F.P., Ferreira, C., Midgut amylase, lysozyme, aminopeptidase, and trehalase from larvae and adults of Musca domestica (1988) Arch. Insect Biochem. Physiol., 9, pp. 283-297; Watson, D.W., Guy, J.S., Stringham, S.M., Limited transmission of turkey coronavirus (TCV) in young turkeys by adult darkling beetles, Alphitobius diaperinus Panzer (Tenebrionidae) (2000) J. Med. Entomol., 37, pp. 480-483; West, L.S., (1951) The House Fly: Its Natural History, Medical Importance, and Control, , Comstock Publ., Cornell University Press, Ithaca, NY","Watson, D.W.; Department of Entomology, Coll. of Agric. and Life Sciences, North Carolina State University, Raleigh, NC 27695, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"12713170","English","Avian Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0037249822
"Zeng F.Y., Chan C.W.M., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C., Hui K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B., Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.","7202911544;7404813871;36941301400;53263321000;7202180875;7003617137;7103304764;56007009300;7202621838;16065173000;57207147544;7202924055;7201780588;7005441747;35338760600;36078079100;7005486823;55440652300;","The complete genome sequence of severe acute respiratory syndrome coronavirus strain HKU-39849 (HK-39)",2003,"Experimental Biology and Medicine","228","7",,"866","873",,52,"10.1177/15353702-0322807-13","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041466151&doi=10.1177%2f15353702-0322807-13&partnerID=40&md5=1a59312c31dc4bc7adaedc05fae4f3ff","Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Department of Zoology, Kadoorie Biol. Sciences Building, University of Hong Kong, Hong Kong, Hong Kong","Zeng, F.Y., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Chan, C.W.M., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Chan, M.N., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Chen, J.D., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Chow, K.Y.C., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Hon, C.C., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Hui, K.H., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Li, J., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Li, V.Y.Y., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Wang, C.Y., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Wang, P.Y., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Zheng, B., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Poon, L.L.M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Chan, K.H., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Leung, F.C., Department of Zoology, University of Hong Kong, Hong Kong, Hong Kong, Department of Zoology, Kadoorie Biol. Sciences Building, University of Hong Kong, Hong Kong, Hong Kong","The complete genomic nucleotide sequence (29.7kb) of a Hong Kong severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) strain HK-39 is determined. Phylogenetic analysis of the genomic sequence reveals it to be a distinct member of the Coronaviridae family. 5′ RACE assay confirms the presence of at least six subgenomic transcripts all containing the predicted intergenic sequences. Five open reading frames (ORFs), namely ORF1a, 1b, S, M, and N, are found to be homologues to other CoV members, and three more unknown ORFs (X1, X2, and X3) are unparalleled in all other known CoV species. Optimal alignment and computer analysis of the homologous ORFs has predicted the characteristic structural and functional domains on the putative genes. The overall nucleotides conservation of the homologous ORFs is low (<5%) compared with other known CoVs, implying that HK-39 is a newly emergent SARS-CoV phylogenetically distant from other known members. SimPlot analysis supports this finding, and also suggests that this novel virus is not a product of a recent recombinant from any of the known characterized CoVs. Together, these results confirm that HK-39 is a novel and distinct member of the Coronaviridae family, with unknown origin. The completion of the genomic sequence of the virus will assist in tracing its origin.","5′-RACE assay; Coronavirus; Genomic sequence; SARS; Subgenomic transcripts","acute respiratory tract disease; article; Coronavirus; Coronavirus hku 39849; gene sequence; genetic transcription; genome; Hong Kong; nonhuman; nucleotide sequence; open reading frame; phylogeny; protein domain; SARS coronavirus; sequence alignment; sequence homology; severe acute respiratory syndrome; virus gene; virus strain; 3' untranslated region; 5' untranslated region; amino acid sequence; chemistry; classification; DNA sequence; genetics; methodology; molecular genetics; nucleic acid amplification; SARS coronavirus; severe acute respiratory syndrome; virology; virus genome; Coronaviridae; Coronavirus; RNA viruses; SARS coronavirus; complementary DNA; virus protein; virus RNA; 3' Untranslated Regions; 5' Untranslated Regions; Amino Acid Sequence; Base Sequence; Conserved Sequence; DNA, Complementary; Genome, Viral; Molecular Sequence Data; Nucleic Acid Amplification Techniques; Open Reading Frames; Phylogeny; RNA, Viral; SARS Virus; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Severe Acute Respiratory Syndrome; Transcription, Genetic; Viral Proteins","Peiris, J., Lai, S., Poon, L., Guan, Y., Yam, L., Lim, W., Nicholls, J., Yuen, K., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., Novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy. Classification and Nomenclature of Viruses, pp. 835-849. , Van Regenmortel MHV, Fauquet CM, Bishop DHL, Carsten EB, Esters MK, Lemon SM, McGeoch DJ, Maniloff J, Mayo MA, Pringle CR, Wickner RB, Eds. New York: Academic Press; Pachuk, C.J., Bredenbeek, P.J., Zoltick, P.W., Spaan, W.J., Weiss, S.R., Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59 (1989) Virology, 171, pp. 141-148; Boursnell, M.E., Brown, T.D., Foulds, I.J., Green, P.F., Tomley, F.M., Binns, M.M., Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus (1987) J Gen Virol, 68, pp. 57-77; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Yoo, D., Pei, Y., Full-length genomic sequence of bovine coronavirus (31 kb). Completion of the open reading frame 1a/1b sequences (2001) Adv Exp Med Biol, 494, pp. 73-76; Eleouet, J.F., Rasschaert, D., Lambert, P., Levy, L., Vende, P., Laude, H., Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus (1995) Virology, 206, pp. 817-822; Kocherhans, R., Bridgen, A., Ackermann, M., Tobler, K., Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence (2001) Virus Genes, 23, pp. 137-144; Brierley, I., Digard, P., Inglis, S.C., Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot (1989) Cell, 19, pp. 537-547; Bredenbeek, P.J., Pachuk, C.J., Noten, A.F., Charite, J., Luytjes, W., Weiss, S.R., Spaan, W.J., The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59: A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism (1990) Nucleic Acids Res, 18, pp. 1825-1832; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Herold, J., Siddell, S.G., An ""elaborated"" pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA (1993) Nucleic Acids Res, 21, pp. 5838-5842; Denison, M.R., Zoltick, P.W., Leibowitz, J.L., Pachuk, C.J., Weiss, S.R., Identification of polypeptides encoded in open reading frame 1b of the putative polymerase gene of the murine coronavirus mouse hepatitis virus A59 (1991) J Virol, 85, pp. 3072-3082; Liu, D.X., Brierley, I., Tibbles, K.W., Brown, T.D., A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products (1994) J Virol, 68, pp. 5772-5780; Opstelten, D.J., De Groote, P., Horzinek, M.C., Rottier, P.J., Folding of the mouse hepatitis virus spike protein and its association with the membrane protein (1994) Arch Virol Suppl, 9, pp. 319-328; Rottier, P.J.M., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 115-139. , Siddell SG, Ed. New York: Plenum Press; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , Siddell SG, Ed. New York: Plenum Press; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gasteroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J Virol, 70, pp. 4773-4777; Jacobs, L., Van der Zeijst, B.A.M., Horzinek, M.C., Characterization and translation of transmissible gastroenteritis virus mRNAs (1986) J Virol, 57, pp. 1010-1015; Rasschaert, D., Gelfi, J., Laude, H., Enteric coronavirus TGEV: Partial sequence of the genomic RNA, its organization and expression (1987) Biochimie, 69, pp. 591-600; Wesley, R.D., Cheung, A.K., Michael, D.D., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence for three mRNA species between the peplomer and matrix protein genes (1989) Virus Res, 13, pp. 87-100; Shibata, Y., Carninci, P., Watahiki, A., Shiraki, T., Konno, H., Muramatsu, M., Hayashizaki, Y., Cloning full-length, cap-trapper-selected cDNAs by using the single-strand linker ligation method (2001) BioTechniques, 30, pp. 1250-1253; Lupas, A., Van Dyke, M., Stock, J., Predicting coiled coils from protein sequences (1991) Science, 252, pp. 1162-1164; Lee, C.W., Jackwood, M.W., Evidence of genetic diversity generated by recombination among avian coronavirus IBV (2000) Arch Virol, 145, pp. 2135-2148; Brown, J.D.K., Boursnell, M.E.G., Binns, M.M., Tomley, F.M., Cloning and sequencing of the 5′ terminal sequences from avian infectious bronchitis virus genomic RNA (1989) J Gen Virol, 67, pp. 221-228; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J Gen Virol, 79, pp. 715-718; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res, 17, pp. 4846-4861; Den Boon, J.A., Snijder, E.J., Chimside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togaviurs but belongs to the coronavirus-like superfamily (1991) J Virol, 65, pp. 2910-2920; Faaberg, K.S., Plagemann, P.G.W., The envelope proteins of lactate dehydrogenase-elevating virus and their membrane topology (1995) Virology, 212, pp. 512-525; Zhow, M.L., Collisson, E.W., The amino and carboxyl domains of the infectious bronchitis virus nucleocapsid protein interact with 3′ genome RNA (2000) Virus Res, 67, pp. 31-39; Kumar, S., Tamura, K., Jakobsen, I.B., Nei, B., MEGA2: Molecular evolutionary genetics analysis software (2001) Bioinformatics","Leung, F.C.; Department of Zoology, Kadoorie Biol. Sciences Building, University of Hong Kong, Hong Kong, Hong Kong; email: fcleung@hkucc.hku.hk",,"Society for Experimental Biology and Medicine",15353702,,EBMMB,"12876307","English","Exp. Biol. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0041466151
"Kennedy M., Kania S., Styllanldes E., Bertschinger H., Keet D., van Vuuren M.","7402308045;24177256900;6503928331;7006248477;6701663433;7004572625;","Detection of feline coronavirus infection in southern African nondomestic felids",2003,"Journal of Wildlife Diseases","39","3",,"529","535",,8,"10.7589/0090-3558-39.3.529","https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042567322&doi=10.7589%2f0090-3558-39.3.529&partnerID=40&md5=47142ac5533018b21f2b26796794d9ac","Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996, United States; Dept. of Veterinary Tropical Disease, Faculty of Veterinary Science, University of Pretoria, Pretoria, South Africa; Veterinary Wildlife Unit, Faculty of Veterinary Science, University of Pretoria, Pretoria, South Africa; Office of the State Veterinarian, PO Box 12, Skukuza 1350, South Africa","Kennedy, M., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996, United States; Kania, S., Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996, United States; Styllanldes, E., Dept. of Veterinary Tropical Disease, Faculty of Veterinary Science, University of Pretoria, Pretoria, South Africa; Bertschinger, H., Veterinary Wildlife Unit, Faculty of Veterinary Science, University of Pretoria, Pretoria, South Africa; Keet, D., Office of the State Veterinarian, PO Box 12, Skukuza 1350, South Africa; van Vuuren, M., Dept. of Veterinary Tropical Disease, Faculty of Veterinary Science, University of Pretoria, Pretoria, South Africa","Feline coronavirus (FCoV) infects members of the Felidae family with results ranging from seroconversion with no disease to fatal feline infectious peritonitis (FIP). Infection of non-domestic felids with FCoV is of concern, particularly in endangered populations such as cheetahs (Acinonyx jubatus). In this investigation, we tested 342 animals in the Republic of South Africa and Namibia, including 140 animals from wild populations, for evidence of FCoV infection by serology and/or reverse transcription/nested polymerase chain reaction (RT/nPCR) on feces from 1999 through 2001. Past or current infection was evaluated. Of these, 195 animals had evidence of infection and included 41 animals from wild populations. Serology (indirect immunofluorescence) did not always correlate with viral RNA detection, as seronegative animals were occasionally virus-positive, while many seropositive animals were not shedding virus. Serology indicated the infecting virus was most closely related to type I FCoV. Antibody levels in the majority of animals were low, even in those actively infected. Ten of 48 animals tested at more than one time point by RT/nPCR were shedding virus at multiple time points possibly indicating persistent infection. Infection in free-ranging animals was also notable, as over a quarter of the free-ranging animals tested had evidence of current or previous FCoV infection. Testing by serology and RT/nPCR is recommended for screening for FCoV infection. © Wildlife Disease Association 2003.","Acinonyx jubatus; Cheetah; Indirect immumofluorescence; Polymerase chain reaction; South Africa; Survey","Acinonyx jubatus; Animalia; Coronavirus; Felidae; Feline coronavirus; Felis catus","Evermann, J.F., Feline coronavirus infection of cheetahs (1986) Feline Practice, 16, pp. 21-30; Evermann, J.F., Heeney, J.L., McKeirnan, A.J., O'Brien, S.J., Comparative features of a coronavirus isolated from a cheetah with feline infectious peritonitis (1989) Virus Research, 13, pp. 15-28; Heeney, J.L., Evermann, J.F., McKeirnan, A.J., Marker-Kraus, L., Roelke, M.E., Bush, M., Wildt, D.E., O'Brien, S.J., Prevalence and implications of feline coronavirus infections of captive and free-ranging cheetahs (Acinonyx jubatus) (1990) Journal of Virology, 64, pp. 1964-1972; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronavirus: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., Degroot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) Journal of Virology, 72, pp. 4508-4515; Hofmann-Lehmann, R., Fehr, D., Grob, M., Elgizoli, M., Packer, C., Martenson, J.S., O'Brien, S.J., Lutz, H., Prevalence of antibodies to feline parvovirus, calicivirus, herpesvirus, coronavirus, and immunodeficiency virus of feline leukemia virus antigen and the interrelationship of these viral infections in free-ranging lions in East Africa (1996) Clinical and Diagnostic Laboratory Immunology, 3, pp. 554-562; Hoskins, J.D., Coronavirus infection in cats (1993) Veterinary Clinics of North America: Small Animal Practice, pp. 1-16. , J. D. Hoskins and A. S. Loar (eds.). W. B. Saunders Company, Philadelphia, Pennsylvania; Juan-Salles, C., Domingo, M., Herraez, P., Fernandez, A., Fernandez, J., An outbreak of feline infectious peritonitis in captive servals (Felis serval): Clinical, pathological, and immunohistochemical findings (1997) Proceedings of the American Association of Zoo Veterinarians, pp. 224-226. , C. K. Baer (ed.). Houston, Texas; Kennedy, M.A., Brenneman, K., Millsaps, R.K., Black, J., Potgieter, L.N.D., Correlation of genomic detection of feline coronavirus with various diagnostic assays for feline infectious peritonitis (1998) Journal of Veterinary Diagnostic Investigation, 10, pp. 93-97; Kennedy, M.A., Citino, S., Dolorico, T., Hillis McNabb, A., Moffatt, A.S., Kania, S., Detection of feline coronavirus infection in captive cheetahs (Acinonyx jubatus) in the USA by polymerase chain reaction (2000) Journal of Zoo and Wildlife Medicine, 32, pp. 25-30; Kennedy, M.A., Boedeker, N., Gibbs, P., Kania, S., Deletions in the 7a ORF associated with an epidemic of feline infectious peritonitis (2001) Veterinary Microbiology, 81, pp. 227-234; Kennedy, M.A., Citino, S., McNabb, A.H., Moffatt, A.S., Gertz, K., Kania, S., Detection of feline coronavirus in captive Felidae in the USA (2002) Journal of Veterinary Diagnostic Investigation, 14, pp. 520-522; Murray, D.L., Kapke, C.A., Evermann, J.F., Fuller, T.K., Infectious disease and the conservation of free-ranging large carnivores (1999) Animal Conservation, 2, pp. 241-254; O'Brien, S.J., Roelke, M.E., Marker, A., Newman, C.A., Winkler, C.A., Meltzer, D.L.L., Evermann, J.F., Wildt, D.E., Genetic basis for species vulnerability in the cheetah (1985) Science, 227, pp. 1428-1434; Paul-Murphy, J., Work, T., Hunter, D., McFie, E., Fjelline, D., Serologic survey and serum biochemical reference ranges of the free-ranging mountain lion (Felis concolor) in California (1994) Journal of Wildlife Diseases, 30, pp. 205-215; Pfeifer, M.L., Evermann, J.F., Roelke, M.E., Gallina, A.M., Ott, R.L., McKeirnan, A.J., Feline infectious peritonitis in a captive cheetah (1983) Journal of the American Veterinary Medical Association, 183, pp. 1317-1319; Roelke, M.E., Forrester, D.J., Jacobson, E.R., Kollias, G.V., Scott, F.W., Barr, M.C., Evermann, J.F., Pirtle, E.C., Seroprevalence of infectious disease agents in free-ranging Florida panthers (Felis concolor coryi) (1993) Journal of Wildlife Diseases, 29, pp. 36-49; Spencer, J.A., Morkel, P., Serological survey of sera from lions in Etosha National Park (1993) South-Africa Tydskrif Natuurnav, 23, pp. 60-62; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Practice, 23, pp. 40-44; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Watt, N.J., MacIntyre, N.J., McOrist, S., An extended outbreak of infectious peritonitis in a closed colony of European wildcats (Felis silvestris) (1993) Journal of Comparative Pathology, 108, pp. 73-79","Kennedy, M.; Department of Comparative Medicine, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996, United States; email: mkenned2@utk.edu",,"Wildlife Disease Association, Inc.",00903558,,,"14567213","English","J. Wildl. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-3042567322
"He L., Ding Y.Q., Che X.Y., Zhang Q.L., Huang Z.X., Wang H.J., Shen H., Li Z.G., Cai J.J., Zhang J.H., Geng J., Li X., Zhang W.L., Han H.X., Kang W., Yang L., Lu Y.D.","56517322000;7404137178;57190064389;36496080400;7406222466;57196429736;35084245300;7409076066;56517361800;57196377853;57212700356;55924516600;55706395100;8440811700;36852704100;57211687323;7405480785;","Expression of the monoclonal antibody against nucleocapsid antigen of SARS-associated coronavirus in autopsy tissues from SARS patients",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","11",,"1128","1130",,11,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142762638&partnerID=40&md5=6b1c6414606f898d5fa926f89294c2d5","Department of Pathology, First Military Medical University, Guangzhou, 510515, China","He, L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Ding, Y.Q., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Che, X.Y., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Zhang, Q.L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Huang, Z.X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Wang, H.J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Shen, H., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Li, Z.G., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Cai, J.J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Zhang, J.H., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Geng, J., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Li, X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Zhang, W.L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Han, H.X., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Kang, W., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Yang, L., Department of Pathology, First Military Medical University, Guangzhou, 510515, China; Lu, Y.D., Department of Pathology, First Military Medical University, Guangzhou, 510515, China","OBJECTIVE: To investigate the presence and distribution of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) in autopsy tissues obtained from patients died of SARS. METHODS: Immunohistochemical technique was applied in 4 fatal SARS cases to examine the autopsy tissues including the lungs, spleen, lymph nodes, brain, pituitary, heart, liver, kidney, pancreas, trachea, esophagus, gastrointestinal tract, adrenal glands, parathyroids, skin and bone marrow. RESULTS: Immunohistochemistry identified positive monoclonal antibody against SARS-CoV nuceeocapsid (N) protein in the alveolar epithelium and the infiltrating monocytes or macrophages in the lung, spleen and lymph nodes; the presence of the antibody was also detected in the serous gland epithelium of the trachea/bronchus, squamous epithelium of the esophagus, the gastric parietal cells, the epithelium of the intestinal tract, acidophilic cells in the parathyroids and pituitary, acinus cells in the pancreas, adrenal cortical cells, sweat gland cells, small vessel endothelium, bone marrow promyelocytes, epithelial cells of the distal convoluted tubule of the kidney, brain neurons, and the hepatocytes near the central vein. CONCLUSIONS: A variety of organs and tissues can be infected by SARS-CoV, and the positive expression of SARS-CoV N protein in the epithelial cells of the gastrointestinal tract, the distal convoluted tubule of the kidney and the sweat gland cells is significant for studying the transmission routes of SARS.",,"monoclonal antibody; article; autopsy; chemistry; disease transmission; human; immunohistochemistry; immunology; isolation and purification; SARS coronavirus; severe acute respiratory syndrome; virus nucleocapsid; Antibodies, Monoclonal; Autopsy; Humans; Immunohistochemistry; Nucleocapsid; SARS Virus; Severe Acute Respiratory Syndrome",,"He, L.email: hely@fimmu.com",,,10002588,,,"14625168","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-2142762638
"Piao Y.J., Xu X.J., Piao Z.X.","7006148728;56193890700;7005919647;","Ultrastructural observation of rat thymus tissue with coronavirus infection",2003,"Di 1 jun yi da xue xue bao = Academic journal of the first medical college of PLA","23","5",,"414","415, 420",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142857237&partnerID=40&md5=6bf8fe729bcc7d74e35726596a30b48b","Department of Histology and Embryology, First Military Medical University, Guangzhou, 510515, China","Piao, Y.J., Department of Histology and Embryology, First Military Medical University, Guangzhou, 510515, China; Xu, X.J., Department of Histology and Embryology, First Military Medical University, Guangzhou, 510515, China; Piao, Z.X., Department of Histology and Embryology, First Military Medical University, Guangzhou, 510515, China","OBJECTIVE: To investigate the ultrastructure of rat thymus tissues with rat coronavirus (RCV) infection for clarifying the mechanism responsible for the morphological changes of the cells infected by RCV. METHODS: Routine electron microscopy was performed for observing RCV-infected rat thymus tissues. RESULTS: Following RCV infection, endoplasmic reticulum (ER) pools of different dimensions were observed in the cytoplasm of the thymic epithelial reticular cells, merging subsequently with each other into larger ER lakes filled with particles of mature RCV, or viral inclusion bodies. After germination on the ER membrane, the viruses entered the matrix of the ER lake to mature and were eventually excreted to the extracellular space. The RCV particles were spherical in shape with a diameter of 100-130 nm and two distinct membranes, the outer one being the envelope and the inner one the nuclear capsid to enclose the viroplasm. Between the envelop and nuclear capsid was a electron-lucent middle layer comprising one to two thin membranous structures. Large quantity of short spike-like projections starting from the nucleus capsid penetrated the middle layer and the envelop to reach the glycoprotein coat and formed a corona-like structure. Mature RCV particles were distributed around the ER pools, cytoplasm, and intercellular space, and the RCVs in the endosome/lysosome were devoid of the envelop and nuclear capsid. CONCLUSION: The ER lakes are involved in the maturation of the viruses, and the envelop and nuclear capsid of the virus entering the cells from extracellular space are removed and degraded in the endosome/lysosome. Replications of virus occurs in plasma of the thymic epithelial reticular cells, and no RCV can be detected in the thymocytes.",,"animal; article; Coronavirus; electron microscopy; endoplasmic reticulum; isolation and purification; pathology; rat; thymus; ultrastructure; virus infection; Wistar rat; Animals; Coronavirus Infections; Coronavirus, Rat; Endoplasmic Reticulum; Microscopy, Electron; Rats; Rats, Wistar; Thymus Gland",,"Piao, Y.J.email: piaoyj@fimmu.com",,,10002588,,,"12754115","Chinese","Di Yi Jun Yi Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-2142857237
"Pakpinyo S., Ley D.H., Barnes H.J., Vaillancourt J.P., Guy J.S.","6507113360;7005808545;7102581732;7004505622;7202723649;","Enhancement of enteropathogenic escherichia coli pathogenicity in young turkeys by concurrent turkey coronavirus infection",2003,"Avian Diseases","47","2",,"396","405",,9,"10.1637/0005-2086(2003)047[0396:EOEECP]2.0.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041379720&doi=10.1637%2f0005-2086%282003%29047%5b0396%3aEOEECP%5d2.0.CO%3b2&partnerID=40&md5=253d88cfa055437de8152b3d9200cfc8","Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Department of Medicine, Faculty of Veterinary Sciences, Chulalongkorn University, Bangkok, 10330, Thailand","Pakpinyo, S., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States, Department of Medicine, Faculty of Veterinary Sciences, Chulalongkorn University, Bangkok, 10330, Thailand; Ley, D.H., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Barnes, H.J., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Vaillancourt, J.P., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Guy, J.S., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States","In a previous study, turkey coronavirus (TCV) and enteropathogenic Escherichia coli (EPEC) were shown to synergistically interact in young turkeys coinfected with these agents. In that study, inapparent or mild disease was observed in turkeys inoculated with only TCV or EPEC, whereas severe growth depression and high mortality were observed in dually inoculated turkeys. The purpose of the present study was to further evaluate the pathogenesis of combined TCV/EPEC infection in young turkeys and determine the role of these agents in the observed synergistic interaction. Experiments were conducted to determine 1) effect of EPEC dose, with and without concurrent TCV infection, and 2) effect of TCV exposure, before and after EPEC exposure, on development of clinical disease. Additionally, the effect of combined infection on TCV and EPEC shedding was determined. No clinical sign of disease and no attaching and effacing (AE) lesions characteristic of EPEC were observed in turkeys inoculated with only EPEC isolate R98/5, even when turkeys were inoculated with 1010 colony forming units (CFU) EPEC (high dose exposure). Only mild growth depression was observed in turkeys inoculated with only TCV; however, turkeys inoculated with both TCV and 104 CFU EPEC (low dose exposure) developed severe disease characterized by high mortality, marked growth depression, and AE lesions. Inoculation of turkeys with TCV 7 days prior to EPEC inoculation produced more severe disease (numerically greater mortality, significantly lower survival probability [P &lt; 0.05], increased frequency of AE lesions) than that observed in turkeys inoculated with EPEC prior to TCV or simultaneously inoculated with these agents. Coinfection of turkeys with TCV and EPEC resulted in significantly increased (P &lt; 0.05) shedding of EPEC, but not TCV, in intestinal contents of turkeys. These findings indicate that TCV infection predisposes young turkeys to secondary EPEC infection and potentiates the expression of EPEC pathogenicity in young turkeys.","Escherichia coli; Poult enteritis-mortality syndrome; Turkey coronavirus","Aves; Coronavirus; Escherichia coli; Escherichia coli; Meleagris gallopavo; Turkey coronavirus; animal; animal disease; article; bacterium adherence; bird disease; Coronavirus; Enterobacter infection; Escherichia coli; feces; intestine; microbiology; pathogenicity; pathology; physiology; turkey (bird); virology; Animals; Bacterial Adhesion; Coronavirus, Turkey; Enteritis, Transmissible, of Turkeys; Escherichia coli; Escherichia coli Infections; Feces; Intestines; Poultry Diseases; Turkeys","Barnes, H.J., Guy, J.S., Poult enteritis - Mortality syndrome (""spiking mortality"") of turkeys (1997) Diseases of Poultry, 10th Ed., pp. 1025-1030. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Bland, J.M., Altman, D.G., Survival probabilities (the Kaplan-Meier method) (1998) Br. Med. J., 317, p. 1572; Breslin, J.J., Smith, L.G., Barnes, H.J., Guy, J.S., Comparison of virus isolation, immunohistochemistry, and reverse transcriptase-polymerase chain reaction procedures for detection of turkey coronavirus (2000) Avian Dis., 44, pp. 624-631; Fainstein, V., Musher, D.M., Cate, T.R., Bacterial adherence of pharyngeal cells during viral infection (1980) J. Infect. Dis., 141, pp. 172-176; Fischer, J., Maddox, C., Moxley, R., Kinden, D., Miller, M., Pathogenicity of a bovine attaching effacing Escherichia coli isolate lacking shiga-like toxins (1994) Am. J. Vet. Res., 55, pp. 991-999; Fukui, H., Sueyoshi, M., Haritani, M., Nakazawa, M., Naitoh, S., Tani, H., Uda, Y., Natural infection with attaching and effacing Escherichia coli (O 103:H-) in chicks (1995) Avian Dis., 39, pp. 912-918; Gannon, V.P.J., Rashed, M., King, R.K., Golsteyn-Thomas, E.J., Detection and characterization of the eae gene of shiga-like toxin-producing Escherichia coli using polymerase chain reaction (1991) J. Clin. Microbiol., 31, pp. 1268-1274; Guy, J.S., Barnes, H.J., Smith, L.G., Breslin, J., Antigenic characterization of a turkey coronavirus identified in poult enteritis- and mortality syndrome-affected turkeys (1997) Avian Dis., 41, pp. 583-590; Guy, J.S., Smith, L.G., Breslin, J.J., Vaillancourt, J.P., Barnes, H.J., High mortality and growth depression experimentally produced in young turkeys by dual infection with enteropathogenic Escherichia coli and turkey coronavirus (2000) Avian Dis., 44, pp. 105-113; Hess, R.G., Bachmann, P.A., Baljer, G., Mayr, A., Pospischil, A., Schmid, G., Synergism in experimental mixed infections of newborn colostrum-deprived calves with bovine rotavirus and enterotoxigenic Escherichia coli (ETEC) (1984) Zentralbl. Veterinaermed. Reihe B, 31, pp. 585-596; Jerse, A.E., Yu, J., Tall, B.D., Kaper, J.B., A genetic locus of enteropathogenic Escherichia coli necessary for production of attaching and effacing lesions in tissue culture cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 7839-7843; Leece, J.G., Balsbaugh, R.K., Clare, D.A., King, M.W., Rotavirus and hemolytic enteropathogenic Escherichia coli in weanling diarrhea of pigs (1982) J. Clin. Microbiol., 16, pp. 715-723; Moon, H.W., Whipp, S.C., Argenzio, R.A., Levine, M.M., Giannella, R.A., Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines (1983) Infect. Immun., 41, pp. 1340-1351; Moxley, R.A., Francis, D.H., Natural and experimental infection with an attaching and effacing strain of Escherichia coli in calves (1986) Infect. Immun., 53, pp. 339-346; Nagaraja, K.V., Pomeroy, B.S., Corona-viral enteritis of turkeys (bluecomb disease) (1997) Diseases of Poultry, 10th Ed., pp. 686-692. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. saif, eds. Iowa State University Press, Ames, IA; Naqi, S.A., Hall, C.F., Lewis, D.H., The intestinal microflora of turkeys: Comparison of apparently healthy and bluecomb-infected turkey poults (1971) Avian Dis., 15, pp. 14-21; Nataro, J.P., Kaper, J.B., Diarrheagenic Escherichia coli (1998) Clin. Microbiol. Rev., 11, pp. 142-201; Newsome, P.M., Coney, K.A., Synergistic rotavirus and Escherichia coli diarrheal infection in mice (1985) Infect. Immun., 47, pp. 573-574; Pakpinyo, S., Ley, D.H., Barnes, H.J., Vaillancourt, J.P., Guy, J.S., Prevalence of enteropathogenic Escherichia coli in naturally occurring cases of poult enteritis-mortality syndrome (2002) Avian Dis., 46, pp. 360-369; Pomeroy, K.A., Patel, B.L., Larsen, C.T., Pomeroy, B.S., Combined immunofluorescence and transmission electron microscopic studies of sequential intestinal samples from turkey embryos and poults infected with turkey enteritis coronavirus (1978) Am. J. Vet. Res., 39, pp. 1348-1354; Reed, L.J., Muench, H., A simple method of estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Shivaprasad, H.L., Crespo, R.C., Daft, B., Read, D., Attaching and effacing E. coli associated with enteritis in poultry (1998) Proc. 135th Annual Convention of the American Veterinary Medicine Association, p. 184. , Baltimore, MD; Snodgrass, D.R., Smith, M.L., Krautil, F.L., Interaction of rotavirus and enterotoxigenic Escherichia coli in conventionally-reared dairy calves (1982) Vet. Microbiol., 7, pp. 51-60; Turk, J., Maddox, C., Fales, W., Ostund, E., Miller, M., Johnson, G., Pace, L., Kreeger, J., Examination for heat-labile, heat-stable, and shiga-like toxins and for eaeA gene in Escherichia coli isolates obtained from dogs dying with diarrhea: 122 Cases (1992-1996) (1998) J. Am. Vet. Med. Assoc., 212, pp. 1735-1736; Tzipori, S., Makin, T., Smith, M., Krautil, F.L., Enteritis in foals induced by rotavirus and enterotoxigenic Escherichia coli (1982) Aust. Vet. J., 58, pp. 20-23; Wray, C., Dawson, M., Afshar, A., Lucas, M., Experimental Escherichia coli and rotavirus infection in lambs (1981) Res. Vet. Sci., 30, pp. 379-381","Guy, J.S.; Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"12887199","English","Avian Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0041379720
"Tsai J.C., Zelus B.D., Holmes K.V., Weiss S.R.","7403610594;6602571243;7201657724;57203567044;","The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain",2003,"Journal of Virology","77","2",,"841","850",,46,"10.1128/JVI.77.2.841-850.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037219357&doi=10.1128%2fJVI.77.2.841-850.2003&partnerID=40&md5=5c3fa52c4dff841e4a03803ed2ce2959","Department of Microbiology, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80626, United States; Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Tsai, J.C., Department of Microbiology, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Zelus, B.D., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80626, United States; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80626, United States; Weiss, S.R., Department of Microbiology, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States, Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Using isogenic recombinant murine coronaviruses expressing wild-type murine hepatitis virus strain 4 (MHV-4) or MHV-A59 spike glycoproteins or chimeric MHV-4/MHV-A59 spike glycoproteins, we have demonstrated the biological functionality of the N-terminus of the spike, encompassing the receptor binding domain (RBD). We have used two assays, one an in vitro liposome binding assay and the other a tissue culture replication assay. The liposome binding assay shows that interaction of the receptor with spikes on virions at 37°C causes a conformational change that makes the virions hydrophobic so that they bind to liposomes (B. D. Zelus, J. H. Schickli, D. M. Blau, S. R. Weiss, and K. V. Holmes, J. Virol. 77: 830-840, 2003). Recombinant viruses with spikes containing the RBD of either MHV-A59 or MHV-4 readily associated with liposomes at 37°C in the presence of soluble mCEACAM1a, except for S4R, which expresses the entire wild-type MHV-4 spike and associated only inefficiently with liposomes following incubation with soluble mCEACAM1a. In contrast, soluble mCEACAM1b allowed viruses with the MHV-A59 RBD to associate with liposomes more efficiently than did viruses with the MHV-4 RBD. In the second assay, which requires virus entry and replication, all recombinant viruses replicated efficiently in BHK cells expressing mCEACAM1a. In BHK cells expressing mCEACAM1b, only viruses expressing chimeric spikes with the MHV-A59 RBD could replicate, while replication of viruses expressing chimeric spikes with the MHV-4 RBD was undetectable. Despite having the MHV-4 RBD, S4R replicated in BHK cells expressing mCEACAM1b; this is most probably due to spread via CEACAM1 receptor-independent cell-to-cell fusion, an activity displayed only by S4R among the recombinant viruses studied here. These data suggest that the RBD domain and the rest of the spike must coevolve to optimize function in viral entry and spread.",,"carcinoembryonic antigen cell adhesion molecule 1 receptor; glycoprotein; liposome; protein; unclassified drug; amino terminal sequence; animal cell; article; binding affinity; cell strain; conformational transition; controlled study; hydrophobicity; in vitro study; molecular biology; Murine hepatitis coronavirus; nonhuman; priority journal; protein domain; protein expression; protein interaction; receptor binding; solubility; temperature; virion; virus recombinant; virus replication; virus strain; Animals; Antigens, CD; Antigens, Differentiation; Base Sequence; Carcinoembryonic Antigen; Cell Adhesion Molecules; Cell Line; Coronavirus; Cricetinae; DNA Primers; Liposomes; Membrane Glycoproteins; Mice; Protein Binding; Protein Conformation; Viral Envelope Proteins","Baric, R.S., Sullivan, E., Hensley, L., Yount, B., Chen, W., Persistent infection promotes cross-species transmissibility of mouse hepatitis virus (1999) J. 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Virol., 67, pp. 1-8; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Dveksler, G.S., Pensiero, M.N., Dieffenbach, C.W., Cardellichio, C.B., Basile, A.A., Elia, P.E., Holmes, K.V., Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 1716-1720; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Gallagher, T.M., A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor (1997) J. 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Virol., 73, pp. 7607-7618; Sawa, H., Kamada, K., Sato, H., Sendo, S., Kondo, A., Saito, I., Edlund, M., Obrink, B., C-CAM expression in the developing rat central nervous system (1994) Brain Res. Dev. Brain Res., 78, pp. 35-43; Spaan, W.J.M., Cavanagh, D., Horzinek, M.C., Coronaviruses. Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stauber, R., Pfleiderera, M., Siddell, S.G., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for infectivity (1993) J. Gen. Virol., 74, pp. 183-191; Taguchi, F., Kubo, H., Takahashi, H., Suzuki, H., Localization of neurovirulence determinant for rats on the S1 subunit of murine coronavirus JHMV (1995) Virology, 208, pp. 67-74; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Weiner, L.P., Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus) (1973) Arch. Neurol., 28, pp. 298-303; Weismiller, D.G., Sturman, L.S., Buchmeier, M.J., Fleming, J.O., Holmes, K.V., Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions (1990) J. Virol., 64, pp. 3051-3055; Wessner, D.R., Shick, P.C., Lu, J.H., Cardellichio, C.B., Gagneten, S.E., Beauchemin, N., Holmes, K.V., Dveksler, G.S., Mutational analysis of the virus and monoclonal antibody binding sites in MHVR, the cellular receptor of the murine coronavirus mouse hepatitis virus strain A59 (1998) J. Virol., 72, pp. 1941-1948; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Yokomori, K., Lai, M.M.C., The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection (1992) J. Virol., 66, pp. 6931-6938; Zelus, B.D., Schickli, J.H., Blau, D.M., Weiss, S.R., Holmes, K.V., Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAM1 receptors or by pH 8 (2003) J. Virol., 77, pp. 830-840; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Weiss, S.R.; Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, 36th and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"12502800","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037219357
"Yan X.G., Wan Z.Y., Zhang X., Zheng Q.X., Zheng K., Huang J.C., Huang P., Lu J.H.","8066291300;7101835882;35224294000;35212667000;25937079000;56965768400;7403658890;8079348400;","Isolation and identification of SARS virus in Guangdong province",2003,"Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology","17","3",,"213","216",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-10244274705&partnerID=40&md5=64b5966072125fbf199f9f867d064677","Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China","Yan, X.G., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Wan, Z.Y., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Zhang, X., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Zheng, Q.X., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Zheng, K., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Huang, J.C., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Huang, P., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China; Lu, J.H., Center for Diseases Control and Prevention of Guangdong province, Guangzhou, 510300, China","BACKGROUND: To isolate and identify pathogen of atypical pneumonia in Guangdong. METHODS: Pathogens were isolated from variety of samples collected from atypical pneumonia patient by using MDCK cells, and identified with serological and molecular methods. RESULTS: A novel coronavirus was isolated from patients with atypical pneumonia, from which an RNA fragment of 279 nt was amplified by nested RT-PCR. And sequence assay showed that only 39-65 percent of sequence of the virus was homogenous to known coronavirus, but almost 100% homogenous (with one base exception, 12a to t) to SARS-associated coronavirus isolated from patients outside Guangdong, such as in Beijing, Hong Kong, Taiwan, Germany, Italy and so on. Indirect immunofluorescence test showed a specific antigen-antibody reactivity between the coronavirus and convalescent-phase sera of SARS patients. CONCLUSION: The pathogen of the atypical pneumonia in Guangdong province was a novel type of coronavirus, which could be isolated by using MDCK cells.",,"animal; article; cell line; China; classification; dog; genetics; human; isolation and purification; molecular genetics; nucleotide sequence; phylogeny; SARS coronavirus; severe acute respiratory syndrome; virology; virus pneumonia; Animals; Base Sequence; Cell Line; China; Dogs; Humans; Molecular Sequence Data; Phylogeny; Pneumonia, Viral; SARS Virus; Severe Acute Respiratory Syndrome",,"Yan, X.G.",,,10039279,,,"15340560","Chinese","Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-10244274705
"Wang C.E., Li Y.C., Wu X.H., Cao J.T., Yan G., Li J.F., Si B.Y., Yu M., Qin E.D., Zhu Q.Y.","7501641866;57207039200;57198469674;36983495900;56286561400;55720545200;36124063300;56512847900;6701908544;7403313352;","Ultrastructural characteristics of SARS associated virus in infected cells",2003,"Zhonghua bing li xue za zhi Chinese journal of pathology","32","3",,"209","211",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642306240&partnerID=40&md5=3a0ba8054f455fea7b5b461c34cf013a","Institute of Microbiology and Epidemiology, Beijing, 100071, China","Wang, C.E., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Li, Y.C., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Wu, X.H., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Cao, J.T., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Yan, G., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Li, J.F., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Si, B.Y., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Yu, M., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Qin, E.D., Institute of Microbiology and Epidemiology, Beijing, 100071, China; Zhu, Q.Y., Institute of Microbiology and Epidemiology, Beijing, 100071, China","OBJECTIVE: Electron microscopical study of infected cells to identify the pathogenic agent of SARS. METHODS: Vero E6 cells infected with lung autopsy samples or nasopharyngeal swabs from SARS patients of Beijing and Guangzhou were inoculated. The supernatant and cultured cells exhibiting identifiable cytopathic effect (CPE) were prepared for electron microscopic study. RESULTS: Examination of CPE cells on thin-section revealed characteristic coronavirus particles within the cisternae of endoplasmic reticulum, Golgi apparatus, vesicles and extracellular space. They were mainly spherical or oval in shape, annular or dense, about 80 nm in diameter. Negative-stain electron microscopy identified coronavirus particles in culture supernatant, 80 - 120 nm in diameter, with club-shaped surface projections. Elongated, rod-, kidney- or other irregular shaped virons with the size of 100 - 200 nm by 60 - 90 nm were also found in the cultured cells infected with the lung samples from the Guangdong patients. Infectious virons entered cells by endocytosis or membrane fusion and released through a budding process. CONCLUSION: These data indicate a novel coronavirus as the causative agent of SARS. Most viral particles showed typical characteristics of coronavirus. The potential role of special shape viruses is expected to be further investigated.",,"animal; article; Cercopithecus; electron microscopy; human; SARS coronavirus; severe acute respiratory syndrome; ultrastructure; Vero cell; virology; Animals; Cercopithecus aethiops; Humans; Microscopy, Electron; SARS Virus; Severe Acute Respiratory Syndrome; Vero Cells",,"Wang, C.E.email: wangcuie1994@yahoo.com.cn",,,05295807,,,"12882683","Chinese","Zhonghua Bing Li Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0642306240
"Davidson A., Siddell S.","7402001807;7005260816;","Potential for antiviral treatment of severe acute respiratory syndrome.",2003,"Current opinion in infectious diseases","16","6",,"565","571",,15,"10.1097/00001432-200312000-00009","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2442522568&doi=10.1097%2f00001432-200312000-00009&partnerID=40&md5=138ebcdada53716f8017c0fe7d5ba3d7","Department of Pathology and Microbiology, Medical and Veterinary Sciences, University of Bristol, Bristol, United Kingdom","Davidson, A., Department of Pathology and Microbiology, Medical and Veterinary Sciences, University of Bristol, Bristol, United Kingdom; Siddell, S., Department of Pathology and Microbiology, Medical and Veterinary Sciences, University of Bristol, Bristol, United Kingdom","PURPOSE OF REVIEW: Severe acute respiratory syndrome is a new, sometimes lethal disease of humans that is caused by a novel coronavirus. To date there have been over 750 related deaths and there is clearly an urgent need to develop specific antiviral drugs to combat this disease. In this review, the authors shall focus on the molecular biology of the coronavirus and suggest how this information can be used to identify possible targets for antiviral drugs. RECENT FINDINGS: Within a remarkably short period of time, the severe acute respiratory syndrome coronavirus has been isolated, its genome has been sequenced and the structure of at least one key viral enzyme has been deduced. In addition, bioinformatic analysis has predicted a number of enzymatic activities associated with proteins of the viral replicase-transcriptase complex. In some cases, these functions have been confirmed by biochemical analysis. Thus, there has been significant progress in the rational approach to anti-severe acute respiratory syndrome coronavirus drug design. This approach, combined with the random screening of licensed compounds or existing compound libraries, should result in the identification of novel lead compounds and the expeditious development of antiviral drugs. SUMMARY: Although the initial severe acute respiratory syndrome epidemic has been controlled by conventional measures, the animal reservoir for the coronavirus progenitor has not been identified. It is therefore likely that the virus will be reintroduced into the human population in the future. When this happens, the most economical and effective way to contain the virus will be the therapeutic use of antiviral drugs.",,"antivirus agent; biology; disease model; drug design; human; review; severe acute respiratory syndrome; Antiviral Agents; Computational Biology; Disease Models, Animal; Drug Design; Humans; Severe Acute Respiratory Syndrome",,"Davidson, A.",,,09517375,,,"14624107","English","Curr. Opin. Infect. Dis.",Review,"Final",,Scopus,2-s2.0-2442522568
"Wu H.J., Zhao X.Y., Wang F.","57209957969;57209958371;57209962939;","Clinical observation on treatment of 40 SARS uncertain patients with integrative traditional Chinese and Western medicine",2003,"Zhongguo Zhong xi yi jie he za zhi Zhongguo Zhongxiyi jiehe zazhi = Chinese journal of integrated traditional and Western medicine / Zhongguo Zhong xi yi jie he xue hui, Zhongguo Zhong yi yan jiu yuan zhu ban","23","8",,"572","574",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142166199&partnerID=40&md5=a9258ce61892f8101848b41e131409ba","Beijing Municipal Hospital of Integrative Chinese and Western Medicine, Beijing, 100039., China","Wu, H.J., Beijing Municipal Hospital of Integrative Chinese and Western Medicine, Beijing, 100039., China; Zhao, X.Y., Beijing Municipal Hospital of Integrative Chinese and Western Medicine, Beijing, 100039., China; Wang, F., Beijing Municipal Hospital of Integrative Chinese and Western Medicine, Beijing, 100039., China","OBJECTIVE: To observe the clinic symptom improving time in uncertain SARS patients and the therapeutic effect of integrative Chinese and western medicine (ICWM) in treating SARS. METHODS: The clinic symptoms, chest film and tongue figure of 40 uncertain SARS patients treated with ICWM were observed and T-lymphocyte subsets, serum coronavirus nucleic acid and antibody in 20 patients were tested dynamically. RESULTS: All the symptoms, such as fever, sweating, fatigue, cough without phlegm, etc. were obviously improved after treatment. Lung shadow in chest film began to be absorbed 4.54 +/- 2.85 days, and obviously absorbed 7.74 +/- 4.68 days after treatment. CD3, CD4 and CD8 in 20 patients, which were lower than the normal range when hospitalization, began to increase 3 days later and gradually recovered to the normal in 6-10 days. Serum coronavirus nucleic acid was positive in 3 patients, coronavirus antibody positive in two and both were positive in one. CONCLUSION: ICWM can improve the symptoms and regulate the immune function in uncertain SARS patients.",,"herbaceous agent; adult; aged; article; Chinese medicine; drug combination; female; human; immunology; male; middle aged; phytotherapy; severe acute respiratory syndrome; uncertainty; Adult; Aged; Drug Therapy, Combination; Drugs, Chinese Herbal; Female; Humans; Male; Medicine, Chinese Traditional; Middle Aged; Phytotherapy; Severe Acute Respiratory Syndrome; Uncertainty",,"Wu, H.J.email: Wangfanbj@sohu.com",,,10035370,,,"14503052","Chinese","Zhongguo Zhong Xi Yi Jie He Za Zhi",Article,"Final",,Scopus,2-s2.0-0142166199
"Khater F.J., Moorman J.P.","6701701287;7005818719;","Severe Acute Respiratory Syndrome: An Overview",2003,"Southern Medical Journal","96","9",,"906","910",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1442350649&partnerID=40&md5=73e35f9ba6f7c613fc586d247d9ef49f","Department of Internal Medicine, Division of Infectious Diseases, James H. Quillen College of Medicine, Johnson City, TN 37614, United States","Khater, F.J.; Moorman, J.P., Department of Internal Medicine, Division of Infectious Diseases, James H. Quillen College of Medicine, Johnson City, TN 37614, United States","Severe acute respiratory syndrome (SARS) is a severe pulmonary infection that has been identified in multiple outbreaks around the world after emerging from mainland China in early 2003, The syndrome is caused by SARS-associated coronavirus, a novel human infection. SARS-associated coronavirus is spread by multiple mechanisms, including direct contact and large-droplet aerosolization, and may be spread by droplet nuclei as well. Clinical disease is characterized by fever, dry cough, interstitial infiltrates, and variable progression to respiratory failure, No treatment has clearly been shown to be effective. Aggressive infection control measures to prevent viral spread are key to outbreak management.","Coronavirus; Epidemic; Infection control; Pneumonia; Severe acute respiratory syndrome","beta lactam antibiotic; macrolide; oseltamivir; quinoline derived antiinfective agent; ribavirin; aerosol; China; clinical feature; disease course; epidemic; human; infection control; lung infection; review; SARS coronavirus; severe acute respiratory syndrome; virus transmission","Communicable Disease Surveillance & Response (CSR): Severe Acute Respiratory Syndrome (SARS) - WHO Guidelines/recommendations/descriptions, , http://www.who.int/csr/sars/guidelines/en/; Update: Severe acute respiratory syndrome - United States, June 18, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (24), p. 570; Update: Severe acute respiratory syndrome - Toronto, Canada, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (23), pp. 547-550; Cluster of severe acute respiratory syndrome cases among protected health-care workers: Toronto, Canada, April 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (19), pp. 433-436; Riley, S., Fraser, C., Donnelly, C.A., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966; Dye, C., Gay, N., Epidemiology: Modeling the SARS epidemic (2003) Science, 300, pp. 1884-1885. , comment; Severe acute respiratory syndrome: Singapore, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (18), pp. 405-411; Severe acute respiratory syndrome: Taiwan, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (20), pp. 461-466; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772. , HKU/UCH SARS Study Group; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Severe acute respiratory syndrome (SARS) and coronavirus testing: United States, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (14), pp. 297-302; Updated interim surveillance case definition for severe acute respiratory syndrome (SARS): United States, April 29, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (17), pp. 391-393","Moorman, J.P.; Department of Internal Medicine, Division of Infectious Diseases, James H. Quillen College of Medicine, Johnson City, TN 37614, United States; email: moorman@mail.etsu.edu",,"Lippincott Williams and Wilkins",00384348,,SMJOA,"14513989","English","South. Med. J.",Review,"Final",,Scopus,2-s2.0-1442350649
"Squires R.A.","8752989900;","An update on aspects of viral gastrointestinal diseases of dogs and cats",2003,"New Zealand Veterinary Journal","51","6",,"252","261",,9,"10.1080/00480169.2003.36379","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346256574&doi=10.1080%2f00480169.2003.36379&partnerID=40&md5=3ba28da3535ab1534a7d8718f5458c3f","Institute of Veterinary, Animal and Biomedical Sciences, Massey University, Private Bag 11222, Palmerston North, New Zealand","Squires, R.A., Institute of Veterinary, Animal and Biomedical Sciences, Massey University, Private Bag 11222, Palmerston North, New Zealand","Viruses commonly cause gastrointestinal illnesses in dogs and cats that range in severity from mild diarrhoea to malignant neoplasia. Perpetual evolution of viruses is reflected in changing disease patterns, so that familiar viruses are sometimes discovered to cause new or unexpected diseases. For example, canine parvovirus (CPV) has regained the ability to infect felids and cause a panleucopenia-like illness. Feline panleucopenia virus (FPV) has been shown to cause “fading” in young kittens and has recently been implicated as a possible cause of feline idiopathic cardiomyopathy. Molecular scrutiny of viral diseases sometimes permits deeper understanding of pathogenesis and epizootiology. Feline gastrointestinal lymphomas have not, in the past, been strongly associated with retroviral infections, yet some of these tumours harbour retroviral proviruses. Feline leukaemia virus (FeLV) may play a role in lymphomagenesis, even in cats diagnosed as uninfected using conventional criteria. There is strong evidence that feline immunodeficiency virus (FIV) can also be oncogenic. The variant feline coronaviruses that cause invariably-fatal feline infectious peritonitis (FIP) arise by sporadic mutation of an ubiquitous and only mildly pathogenic feline enteric coronavirus (FECV); a finding that has substantial management implications for cat breeders and veterinarians. Conversely, canine enteric coronavirus (CECV) shows considerable genetic and antigenic diversity but causes only mild, self-limiting diarrhoea in puppies. Routine vaccination against this virus is not recommended. Although parvoviruses, coronaviruses and retroviruses are the most important known viral causes of canine and feline gastrointestinal disease, other viruses play a role. Feline and canine rotaviruses have combined with human rotaviruses to produce new, reassortant, zoonotic viruses. Some companion animal rotaviruses can infect humans directly. Undoubtedly, further viral causes of canine and feline gastrointestinal disease await discovery. © 2003 Taylor and Francis Group, LLC.","Cat; Companion animal; Coronavirus; Dog; Enteritis; Feline immunodeficiency virus; Feline leukaemia virus; Lymphoma; Panleucopenia; Parvovirus; Retrovirus; Rotavirus; Torovirus","ampicillin; antibiotic agent; antiemetic agent; cholinergic receptor blocking agent; corona virus vaccine; endotoxin antibody; feline panleukopenia virus vaccine; flunixin meglumine; gentamicin; glucocorticoid; immunomodulating agent; inactivated vaccine; intercat; live vaccine; metoclopramide; parvovirus vaccine; primucell; recombinant granulocyte colony stimulating factor; recombinant interferon; recombinant interferon omega; recombinant protein; trimethoprim plus sulfonamide; unclassified drug; virbagen; virus vaccine; breeding; cancer diagnosis; cat disease; Coronavirus; diarrhea; dog disease; Enterovirus; Feline immunodeficiency virus; Feline leukemia virus; Feline panleukopenia virus; fluid therapy; gastrointestinal infection; gastrointestinal tumor; genetic variability; lymphoma; nonhuman; Oncovirinae; Parvovirus; provirus; Retrovirus; Retrovirus infection; review; Torovirus; vaccination; veterinary medicine; virus carcinogenesis; virus infection; virus strain; zoonosis; Animalia; Canine coronavirus; Canine parvovirus; Canis familiaris; Corona virus; Coronavirus; Enteric coronavirus; Enterovirus; Felidae; Feline coronavirus; Feline immunodeficiency virus; Feline leukemia virus; Feline panleukopenia virus; Felis catus; leukaemia virus; Oncovirinae; Parvovirus; Rotavirus; Torovirus; unidentified retrovirus","Addie, D.D., Jarrett, O., Control of feline coronavirus infections in breeding catteries by serotesting, isolation, and early weaning (1995) Feline Practice, 23, pp. 92-95; Addie, D.D., Jarrett, O., Feline coronavirus infection (1998) Infectious Diseases of the Dog and Cat. 2Nd Edtn, pp. 58-69. , Greene CE, WB Saunders Company, Philadelphia; Addie, D.D., Toth, S., Thompson, H., Greenwood, N., Jarrett, J.O., Detection of feline parvovirus in dying pedigree kittens (1998) Veterinary Record, 142, pp. 353-356; Barr, F., Feline infectious peritonitis (1998) Journal of Small Animal Practice, 39, pp. 501-504; Barrett, T., Morbillivirus infections, with special emphasis on morbilliviruses of carnivores (1999) Veterinary Microbiology, 69, pp. 3-13; Batt, R.M., Rutgers, H.C., Sancak, A.A., Enteric bacteria: Friend or foe? (1996) Journal of Small Animal Practice, 37, pp. 261-267; Beatty, J.A., Callanan, J.J., Terry, A., Jarrett, O., Neil, J.C., Molecular and immunophenotypical characterization of a feline immunodeficiency virus (FIV)-associated lymphoma: A direct role for FIV in B-lymphocyte transformation? (1998) Journal Ofvirology, 72, pp. 767-771; Beatty, J.A., Lawrence, C.E., Callanan, J.J., Grant, C.K., Gault, E.A., Neil, J.C., Jarrett, O., Feline immunodeficiency virus (FlV)-associated lymphoma: A potential role for immune dysfunction in tumourigenesis (1998) Veterinary Immunology and Immunopathology, 65, pp. 309-322; Buonavoglia, C., Marsilio, F., Tempesta, M., Buonavoglia, D., Tiscar, P.G., Cavalli, A., Compagnucci, M., Use of a feline panleukopenia modified live virus vaccine in cats in the primary-stage of feline immunodeficiency virus infection (1993) Zentralblatt für Veterinärmedizin. Reihe B, 40, pp. 343-346; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J.D., Characterization of a temperature sensitive feline infectious peritonitis coronavirus (1989) Archives Ofvirology, 109, pp. 185-196; Dalsgaard, K., Uttenthal, A., Jones, T.D., Xu, F., Merryweather, A., Hamilton, W.D., Langeveld, J.P., Rodgers, P.B., Plant-derived vaccine protects target animals against a viral disease (1997) Nature Biotechnology, 15, pp. 248-252; De Mari, K., Maynard, L., Eun, H.M., Lebreux, B., Treatment of canine parvoviral enteritis with interferon-omega in a placebo-controlled field trial (2003) Veterinary Record, 152, pp. 105-108; Ek-Kommonen, C., Sihvonen, L., Pekkanen, K., Rikula, U., Nuotio, L., Outbreak of canine distemper in vaccinated dogs in Finland (1997) Veterinary Record, 141, pp. 380-383; Endo, Y., Cho Kw Nishigaki, K., Momoi, Y., Nishimura, Y., Mizuno, T., Goto, Y., Watari, T., Hasegawa, A., Molecular characteristics of malignant lymphomas in cats naturally infected with feline immunodeficiency virus (1997) Veterinary Immunology and Immunopathology, 57, pp. 153-167; Erles, K., Toomey, C., Brooks, H.W., Brownlie, J., Detection of a group-2 coronavirus in dogs with canine infectious respiratory disease (2003) Virology, 310, pp. 216-223; Esfandiari, J., Klingeborn, B., A comparative study of a new rapid and one-step test for the detection of parvovirus in faeces from dogs, cats and mink (2000) Journal of Veterinary Medicine. 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Infectious Diseases and Veterinary Public Health, 47, pp. 145-153; Fehr, D., Holznagel, E., Bolla, S., Hauser, B., Herrewegh, A., Horzinek, M.C., Lutz, H., Evaluation of the safety and efficacy of a modified-live FIPV vaccine under field conditions (1995) Feline Practice, 23, pp. 83-88; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) Journal of the American Veterinary Medical Association, 210, pp. 1307-1312; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) Journal of the American Veterinary Medical Association, 210, pp. 1313-1318; Foley, J.E., Foley, P., Pedersen, N.C., The persistence of a SIS disease in a metapopulation (1999) Journal of Applied Ecology, 36, pp. 555-563; Fulker, R., Wasmoen, T., Atchison, R., Chu, H.J., Acree, W., Efficacy of an inactivated vaccine against clinical disease caused by canine coronavirus (1995) Advances in Experimental Medicine and Biology, 380, pp. 229-234; Gabor, L.J., Malik, R., Canfield, P.J., Clinical and anatomical features of lymphosarcoma in 118 cats (1998) Australian Veterinary Journal, 76, pp. 725-732; Gabor, L.J., Jackson, M.L., Trask, B., Malik, R., Canfield, P.J., Feline leukaemia virus status of Australian cats with lymphosarcoma (2001) Australian Veterinary Journal, 79, pp. 476-481; Gabor, L.J., Love, D.N., Malik, R., Canfield, P.J., Feline immunodeficiency virus status of Australian cats with lymphosarcoma (2001) Australian Veterinary Journal, 79, pp. 540-545; Gamoh, K., Senda, M., Shimazaki, Y., Makie, H., Inoue, Y., Itoh, O., Chronological antigenic survey of canine parvovirus in Japan (2003) Veterinary Record, 152, pp. 142-143; Gerber, J.D., Overview of the development of a modified-live temperature-sensitive FIP virus-vaccine (1995) Feline Practice, 23, pp. 62-66; Glickman, L.T., Domanski, L.M., Patronek, G.J., Visintainer, F., Breed-related risk factors for canine parvovirus enteritis (1985) Journal of the American Veterinary Medical Association, 187, pp. 589-594; Greene, C.E., Feline panleukopenia (1998) Infectious Diseases of the Dog and Cat. 2Nd Edtn, pp. 52-57. , Greene CE, WB Saunders Company, Philadelphia; Greene, C.E., Schultz, R.D., Ford, R.B., Canine vaccination (2001) Veterinary Clinics of North America - Small Animal Practice, 31, pp. 473-492; Grooters, A.M., Biller, D.S., Ward, H., Miyabayashi, T., Couto, C.G., Ultrasonographic appearance of feline alimentary lymphoma (1994) Veterinary Radiology and Ultrasound, 35, pp. 468-472; Guilford, W.G., Strombeck, D.R., Gastrointestinal tract infections, parasites and toxicoses (1996) Strombecks Small Animal Gastroenterology. 3Rd Edtn, pp. 411-432. , Guilford WG, Center SA, Strombeck DR, Williams DA, Meyer DJ, WB Saunders Company, Philadelphia; Gumbrell, R.C., Parvovirus infection in dogs (1979) New Zealand Veterinary Journal, 27, p. 113; Hardy, W.D., Jr., McClelland, A.J., Zuckerman, E.E., Snyder, H.W., Jr., Macewen, E.G., Francis, D., Essex, M., Development of virus non-producer lymphosarcomas in pet cats exposed to FeLV (1980) Nature, 288, pp. 90-92; Harvey, C.J., Lopez Jw Hendrick, M.J., An uncommon intestinal manifestation of feline infectious peritonitis: 26 cases (1986-1993) (1996) Journal of the American Veterinary Medical Association, 209, pp. 1117-1120; Henderson, B., Wilson, M., Commensal communism and the oral cavity (1998) Journal of Dental Research, 77, pp. 1674-1683; Hoskins, J.D., Canine viral diseases (2000) Textbook of Veterinary Internal Medicine, pp. 418-423. , Ettinger SJ, Feldman EC, WB Saunders Company, Philadelphia; Hoskins, J.D., Taylor, H.W., Lomax, T.L., Independent evaluation of a modified-live feline infectious peritonitis virus-vaccine under experimental conditions (Louisiana experience) (1995) Feline Practice, 23, pp. 72-73; Hueffer, K., Parker, J.S., Weichert, W.S., Geisel, R.E., Sgro, J.Y., Parrish, C.R., The natural host range shift and subsequent evolution of canine parvovirus resulted from virus-specific binding to the canine transferrin receptor (2003) Journal of Virology, 77, pp. 1718-1726; Hutson, C.A., Rideout, B.A., Pedersen, N.C., Neoplasia associated with feline immunodeficiency virus-infection in cats of Southern California (1991) Journal of the American Veterinary Medical Association, 199, pp. 1357-1362; Ikeda, Y., Mochizuki, M., Naito, R., Nakamura, K., Miyazawa, T., Mikami, T., Takahashi, E., Predominance of canine parvovirus (CPV) in unvaccinated cat populations and emergence of new antigenic types of CPVs in cats (2000) Virology, 278, pp. 13-19; Ikeda, Y., Nakamura, K., Miyazawa, T., Takahashi, E., Mochizuki, M., Feline host range of canine parvovirus: Recent emergence of new antigenic types in cats (2002) Emerging Infectious Diseases, 8, pp. 341-346; Ishiwata, K., Minagawa, T., Kajimoto, T., Clinical effects of the recombinant feline interferon-omega on experimental parvovirus infection in Beagle dogs (1998) Journal Ofveterinary Medical Science, 60, pp. 911-917; Jones, B.R., Robinson, A.J., Fray, L.M., Lee, E.A., A longitudinal serological survey of parvovirus infection in dogs (1981) New Zealand Veterinary Journal, 30, pp. 19-20; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine coronavirus 1-71: Studies by virologic, histologic, histochemical, and immunofluorescent techniques (1976) American Journal of Veterinary Research, 37, pp. 247-256; 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Infectious Diseases and Veterinary Public Health, 48, pp. 385-392; Pratelli, A., Martella, V., Decaro, N., Tinelli, A., Camero, M., Cirone, F., Elia, G., Buonavoglia, C., Genetic diversity of a canine coronavirus detected in pups with diarrhoea in Italy (2003) Journal of Virologicalmethods, 110, pp. 9-17; Reeves, N.P., Vaccination against naturally-occurring FIP in a single large cat shelter (1995) Feline Practice, 23, pp. 81-82; Richards, J., Rodan, I., Feline vaccination guidelines (2001) Veterinary Clinics of North America - Small Animal Practice, 31, pp. 455-472; Salminen, S., Isolauri, E., Onnela, T., Gut flora in normal and disordered states (1995) Chemotherapy, 41, pp. 5-15; Scott, F.W., Corapi, W.V., Olsen, C.W., Independent evaluation of a modified-live FIPV vaccine under experimental conditions (Cornell experience) (1995) Feline Practice, 23, pp. 74-76; Smith, C.H., Meers, J., Wilks, C.R., Rice, M., Jones, B.R., A survey for torovirus in New Zealand cats with protruding nictitating membranes (1997) New Zealand Veterinary Journal, 45, pp. 41-43; Steinel, A., Munson, L., Van Vuuren, M., Truyen, U., Genetic characterization of feline parvovirus sequences from various carnivores (2000) Journal of General Virology, 81, pp. 345-350; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Veterinary Record, 132, pp. 7-11; Teske, E., Van Straten, G., Van Noort, R., Rutteman, G.R., Chemotherapy with cyclophosphamide, vincristine, and prednisolone (COP) in cats with malignant lymphoma: New results with an old protocol (2002) Journal Ofveterinary Internal Medicine, 16, pp. 179-186; Truyen, U., Evermann, J.F., Vieler, E., Parrish, C.R., Evolution of canine parvovirus involved loss and gain of feline host range (1996) Virology, 215, pp. 186-189; Truyen, U., Geissler, K., Parrish, C.R., Hermanns W Siegl, G., No evidence for a role of modified live virus vaccines in the emergence of canine parvovirus (1998) Journal of General Virology, 79, pp. 1153-1158; Vail, D.M., Moore, A.S., Ogilvie, G.K., Volk, L.M., Feline lymphoma (145 cases): Proliferation indices, cluster of differentiation-3 immunoreactivity, and their association with prognosis in 90 cats (1998) Journal of Veterinary Internal Medicine, 12, pp. 349-354; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Wang, L., Junker, D., Collisson EW Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Wang, J., Kyaw-Tanner, M., Lee, C., Robinson, W.F., Characterisation of lymphosarcomas in Australian cats using polymerase chain reaction and immunohistochemical examination (2001) Australian Veterinary Journal, 79, pp. 41-46; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: Comparisons with dengue hemorrhagic fever (1981) Comparative Immunology, Microbiology and Infectious Diseases, 4, pp. 175-189; Wilson, R.B., Holladay, J.A., Cave, J.S., A neurologic syndrome associated with use of a canine coronavirus-parvovirus vaccine in dogs (1986) Compendium on Continuing Education for the Practicing Veterinarian, 8, pp. 117-124; Zarnke, R.L., Evermann, J., Ver Hoef, J.M., McNay, M.E., Boertje, R.D., Gardner, C.L., Adams, L.G., Dale Bw Burch, J., Serologic survey for canine coronavirus in wolves from Alaska (2001) Journal of Wildlife Diseases, 37, pp. 740-745; Zenger, E., FeLV, FIV: Making a diagnosis (2000) Feline Practice, 28, pp. 16-18","Squires, R.A.; Institute of Veterinary, Animal and Biomedical Sciences, Massey University, Private Bag 11222, Palmerston North, New Zealand; email: R.A.Squires@massey.ac.nz",,,00480169,,,,"English","New Zealand Vet. J.",Article,"Final",,Scopus,2-s2.0-0346256574
"Kotaniemi-Syrjänen A., Vainionpää R., Reijonen T.M., Waris M., Korhonen K., Korppi M.","7801323910;7003996023;6603823557;7003873654;7004849753;7005965262;","Rhinovirus-induced wheezing in infancy - The first sign of childhood asthma?",2003,"Journal of Allergy and Clinical Immunology","111","1",,"66","71",,320,"10.1067/mai.2003.33","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037253135&doi=10.1067%2fmai.2003.33&partnerID=40&md5=598a4768c03580014083a79990dd7c7b","Department of Pediatrics, Kuopio University Hospital, PO Box 1777, FIN-70211 Kuopio, Finland","Kotaniemi-Syrjänen, A., Department of Pediatrics, Kuopio University Hospital, PO Box 1777, FIN-70211 Kuopio, Finland; Vainionpää, R.; Reijonen, T.M.; Waris, M.; Korhonen, K.; Korppi, M.","Background: Although known as common causes of upper respiratory infections, rhinoviruses, enteroviruses, and coronaviruses are poorly studied as inducers of wheezing in infants, and their possible role in the development of childhood asthma has not been investigated. Objective: The purposes of this study were to assess the occurrence of RV, enterovirus, and coronavirus infections in wheezing infants and to evaluate the association of these viral findings with early school-age asthma. Methods: In 1999, outcome in relation to asthma was studied in 82 of 100 initially recruited children who had been hospitalized for wheezing in infancy during the period 1992-1993. In 2000, etiologic viral studies regarding the index episode of wheezing were supplemented by rhinovirus, enterovirus, and coronavirus detection by RT-PCR from frozen nasopharyngeal aspirates in 81 of the children for whom adequate samples were available. Of these children, 66 had participated in the follow-up in 1999. Results: Rhinoviruses were identified in 27 (33%) of the 81 children, enteroviruses in 10 (12%), and coronaviruses in none. Rhinoviruses were present as single viral findings in 22 (81%) of the 27 rhinovirus-positive cases, and rhinovirus infections were associated with the presence of atopic dermatitis in infancy. Enteroviruses were commonly encountered in mixed infections and had no association with atopy. As single viral findings, rhinoviruses were associated with the development of asthma (P = .047; odds ratio, 4.14; 95% CI, 1.02-16.77 versus rhinovirus-negative cases [by logistic regression adjusted for age, sex, and atopic dermatitis on entry)]. Conclusion: Our results present rhinoviruses as important inducers of wheezing even in infancy. The association with atopy and subsequent asthma calls for reevaluation of the role of rhinoviruses in the development of asthma.","Asthma; Atopy; Coronavirus; Enterovirus; Polymerase chain reaction; Rhinovirus; Wheezing","article; asthma; atopic dermatitis; atopy; child; Coronavirus; disease association; Enterovirus; female; human; infant; logistic regression analysis; major clinical study; male; mixed infection; outcomes research; priority journal; reverse transcription polymerase chain reaction; Rhinovirus; statistical analysis; upper respiratory tract infection; virus detection; virus infection; wheezing","Kellner, G., Popow-Kraupp, T., Kundi, M., Binder, C., Kunz, C., Clinical manifestations of respiratory tract infections due to respiratory syncytial virus and rhinoviruses in hospitalized children (1989) Acta Paediatr Scand, 78, pp. 390-394; Juvén, T., Mertsola, J., Waris, M., Leinonen, M., Meurman, O., Roivainen, M., Etiology of community-acquired pneumonia in 254 hospitalized children (2000) Pediatr Infect Dis J, 19, pp. 293-298; Duff, A.L., Pomeranz, E.S., Gelber, L.E., Price, G.W., Farris, H., Hayden, F.G., Risk factors for acute wheezing in infants and children: Viruses, passive smoke, and IgE antibodies to inhalant allergens (1993) Pediatrics, 92, pp. 535-540; Johnston, S.L., Xie, P., Johnson, W., Comparison of standard virology and PCR in diagnosis of rhinovirus and respiratory syncytial virus infections in nasal aspirates from children hospitalized with wheezing illness and bronchiolitis (1996) Am J Respir Crit Care Med, 153, pp. A503; Rakes, G.P., Arruda, E., Ingram, J.M., Hoover, G.E., Zambrano, J.C., Hayden, F.G., Rhinovirus and respiratory syncytial virus in wheezing children requiring emergency care (1999) Am J Respir Crit Care Med, 159, pp. 785-790; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Ruohola, A., Heikkinen, T., Waris, M., Puhakka, T., Ruuskanen, O., Intranasal fluticasone propionate does not prevent acute otitis media during viral upper respiratory infection in children (2000) J Allergy Clin Immunol, 106, pp. 467-471; McIntosh, K., Halonen, P., Ruuskanen, O., Report of a workshop on respiratory viral infections: Epidemiology, diagnosis, treatment and prevention (1993) Clin Infect Dis, 16, pp. 151-164; Hyypiä, T., Puhakka, T., Ruuskanen, O., Mäkelä, M., Arola, A., Arstila, P., Molecular diagnosis of human rhinovirus infections: Comparison with virus isolation (1998) J Clin Microbiol, 36, pp. 2081-2083; Lönnrot, M., Sjöroos, M., Salminen, K., Maaronen, M., Hyypiä, T., Hyöty, H., Diagnosis of enterovirus and rhinovirus infections by RT-PCR and time-resolved fluorometry with lanthanide chelate labeled probes (1999) J Med Virol, 59, pp. 378-384; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Reijonen, T.M., Korppi, M., One-year follow-up of young children hospitalized for wheezing: The influence of early anti-inflammatory therapy and risk factors for subsequent wheezing and asthma (1998) Pediatr Pulmonol, 26, pp. 113-119; Reijonen, T.M., Kotaniemi-Syrjänen, A., Korhonen, K., Korppi, M., Predictors of asthma three years after hospital admission for wheezing in infancy (2000) Pediatrics, 106, pp. 1406-1412; Reijonen, T.M., Korppi, M., Kleemola, M., Savolainen, K., Kuikka, L., Mononen, I., Nasopharyngeal eosinophil cationic protein in bronchiolitis: Relation to viral findings and subsequent wheezing (1997) Pediatr Pulmonol, 24, pp. 35-41; Carlsen, K.H., Exercise-induced asthma in children and adolescents and its relationship to sports (2001) Textbook of Pediatric Asthma: An International Perspective, pp. 211-222. , Naspitz CK, Szefler SJ, Tinkelman DG, Warner JO, editors. London: Martin Dunitz; Remes, S., Korppi, M., Remes, K., Pekkanen, J., Prevalence of asthma at school age: A clinical population-based study in eastern Finland (1996) Acta Pediatr, 85, pp. 59-63; Halonen, P., Rocha, E., Hierholzer, J., Holloway, B., Hyypiä, T., Hurskainen, P., Detection of enteroviruses and rhinoviruses in clinical specimens by PCR and liquid-phase hybridization (1995) J Clin Microbiol, 33, pp. 648-653; Santti, J., Hyypiä, T., Halonen, P., Comparison of PCR primer pairs in the detection of human rhinoviruses in nasopharyngeal aspirates (1997) J Virol Methods, 66, pp. 139-147; Kamahora, T., Soe, L.H., Lai, M.M., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res, 12, pp. 1-9; Sigurs, N., Bjarnason, R., Sigurbergsson, F., Kjellman, B., Respiratory syncytial virus bronchiolitis in infancy is an important risk factor for asthma and allergy at age 7 (2000) Am J Respir Crit Care Med, 161, pp. 1501-1507; Isaacs, D., Flowers, D., Clarke, J.R., Valman, H.B., MacNaughton, M.R., Epidemiology of coronavirus respiratory infections (1983) Arch Dis Child, 58, pp. 500-503; Mäkelä, M.J., Puhakka, T., Ruuskanen, O., Leinonen, M., Saikku, P., Kimpimäki, M., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Nokso-Koivisto, J., Kinnari, T.J., Lindahl, P., Hovi, T., Pitkäranta, A., Human picornavirus and coronavirus RNA in nasopharynx of children without concurrent respiratory symptoms (2002) J Med Virol, 66, pp. 417-420; Gern, J.E., Busse, W.W., Association of rhinovirus infections with asthma (1999) Clin Microbiol Rev, 12, pp. 9-18; Staunton, D.E., Merluzzi, V.J., Rothlein, R., Barton, R., Marlin, S.D., Springer, T.A., A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses (1989) Cell, 56, pp. 849-853; Vignola, A.M., Campbell, A.M., Chanez, P., Bousquet, J., Paul-Lacoste, P., Michel, F.-B., HLA-DR and ICAM-1 Expression on bronchial epithelial cells in asthma and chronic bronchitis (1993) Am Rev Respir Dis, 148, pp. 689-694; Subauste, M.C., Jacoby, D.B., Richards, S.M., Proud, D., Infection of a human respiratory epithelial cell line with rhinovirus: Induction of cytokine release and modulation of susceptibility to infection by cytokine exposure (1995) J Clin Invest, 96, pp. 549-557; Einarsson, O., Geba, G.P., Zhu, Z., Landry, M., Elias, J.A., Interleukin-11: Stimulation in vivo and in vitro by respiratory viruses and induction of airways hyperresponsiveness (1996) J Clin Invest, 97, pp. 915-924; Gern, J.E., Vrtis, R., Grindle, K.A., Swenson, C., Busse, W.W., Relationship of upper and lower airway cytokines to outcome of experimental rhinovirus infection (2000) Am J Respir Crit Care Med, 162, pp. 2226-2231; Martinez, F.D., Wright, A.L., Taussig, L.M., Holberg, C.J., Halonen, M., Morgan, W.J., Asthma and wheezing in the first six years of life (1995) N Engl J Med, 332, pp. 133-138; Timonen, K.L., Pekkanen, J., Korppi, M., Vahteristo, M., Salonen, R.O., Prevalence and characteristics of children with chronic respiratory symptoms in eastern Finland (1995) Eur Respir J, 8, pp. 1155-1160","Kotaniemi-Syrjänen, A.; Department of Pediatrics, Kuopio University Hospital, PO Box 1777, FIN-70211 Kuopio, Finland",,"Mosby Inc.",00916749,,JACIB,"12532098","English","J. Allergy Clin. Immunol.",Article,"Final",,Scopus,2-s2.0-0037253135
"Wunderli W., Furrer H.","57203627034;35225781600;","Respiratory tract viruses [Respiratorische Viren.]",2003,"Therapeutische Umschau. Revue thérapeutique","60","10",,"615","624",,,"10.1024/0040-5930.60.10.615","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142714172&doi=10.1024%2f0040-5930.60.10.615&partnerID=40&md5=82fe4bba0433493eb299fe4d35756713","Zentrallabor für Virologie, Universitätsspital Genf., Switzerland","Wunderli, W., Zentrallabor für Virologie, Universitätsspital Genf., Switzerland; Furrer, H., Zentrallabor für Virologie, Universitätsspital Genf., Switzerland","The respiratory tract is the site of entrance of many viruses. However, not all of them cause symptomatic respiratory infections. In the past the clinical significance of some viruses was underestimated. Viruses leading to population-wide epidemics like influenzavirus or to nosocomial outbreaks like respiratory syncytial virus or SARS-associated coronavirus have a great impact on public health and the respective preventive measures are of paramount importance. The advent of new diagnostic tools led to discoveries and additional information about some ""banal"" viruses causing severe diseases in special hosts such as infants and immunosuppressed patients. In addition new viral pathogens were discovered and found to cause respiratory infections, metapneumovirus and SARS-associated coronavirus being the most important ones.",,"virus antibody; article; blood; cross infection; human; isolation and purification; opportunistic infection; polymerase chain reaction; respiratory tract infection; virus; virus culture; virus infection; Antibodies, Viral; Cross Infection; Humans; Opportunistic Infections; Polymerase Chain Reaction; Respiratory Tract Infections; Virus Cultivation; Virus Diseases; Viruses",,"Wunderli, W.email: werner.wunderli@hcuge.ch",,,00405930,,,"14610900","German","Ther Umsch",Article,"Final",,Scopus,2-s2.0-2142714172
"Wang Y., Xie Y., Chen W.","7601491596;7403959832;7409646480;","Immunoinformatic analysis for the epitopes on SARS virus surface protein",2003,"Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences","35 Suppl",,,"70","71",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042736265&partnerID=40&md5=9d2308dd32cb03e85ab13ca6faa8bc10","Department of Immunology, Peking University Health Science Centre, Beijing, 100083, China","Wang, Y., Department of Immunology, Peking University Health Science Centre, Beijing, 100083, China; Xie, Y., Department of Immunology, Peking University Health Science Centre, Beijing, 100083, China; Chen, W., Department of Immunology, Peking University Health Science Centre, Beijing, 100083, China","SARS virus is a recently found coronavirus, which cause human atypical pneumonia through the binding of its spike protein to the receptor on human cells. By using the methods of immunoinformatics, we analyzed the virus surface protein and found that the epitopes, which can be recognized by human immune system, are strikingly changed or disappeared to compare with other common human coronavirus. This result may imply that the escape of SARS virus from human immune surveillance may be the causality plays a very of SARS virus infection. The immunoinformatics is a powerful fool for us to in screen the epitope specificial for SARS virus and identifying the candidate sites for peptide vaccine of SARS virus.",,"epitope; virus envelope protein; article; immunology; SARS coronavirus; Epitopes; SARS Virus; Viral Envelope Proteins",,"Wang, Y.email: wangyuedan@hotmail.com",,,1671167X,,,"12914223","Chinese","Beijing Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-0042736265
"Xu G., Lu H., Li J., Li Y., Feng Z., Hou N., Wang G., Zhao Z.D., Zhang G., Yan C., Li H., Gao X., Xu X., Wang G., Zhuang H.","8691026400;7404843258;36063614900;55719104600;8316649400;57210042949;7407150793;55726165200;57211382596;7401746372;57188722743;55712089200;56004310800;7407149871;7202081074;","Primary investigation on the changing mode of plasma specific IgG antibody in SARS patients and their physicians and nurses",2003,"Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences","35 Suppl",,,"23","25",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042736368&partnerID=40&md5=e7549ed3f48d9de9ed2a5a843b749ef9","Peking University First Hospital, Beijing, 100034, China","Xu, G., Peking University First Hospital, Beijing, 100034, China; Lu, H., Peking University First Hospital, Beijing, 100034, China; Li, J., Peking University First Hospital, Beijing, 100034, China; Li, Y., Peking University First Hospital, Beijing, 100034, China; Feng, Z., Peking University First Hospital, Beijing, 100034, China; Hou, N., Peking University First Hospital, Beijing, 100034, China; Wang, G., Peking University First Hospital, Beijing, 100034, China; Zhao, Z.D., Peking University First Hospital, Beijing, 100034, China; Zhang, G., Peking University First Hospital, Beijing, 100034, China; Yan, C., Peking University First Hospital, Beijing, 100034, China; Li, H., Peking University First Hospital, Beijing, 100034, China; Gao, X., Peking University First Hospital, Beijing, 100034, China; Xu, X., Peking University First Hospital, Beijing, 100034, China; Wang, G., Peking University First Hospital, Beijing, 100034, China; Zhuang, H., Peking University First Hospital, Beijing, 100034, China","OBJECTIVES: To primarily investigate the changing mode of anti-SARS coronavirus IgG antibody in clinically diagnosed SARS patients and the possibility of subclinical infection in physicians and nurses through close association with SARS patients. METHODS: The plasma levels of anti-SARS coronavirus IgG antibody of 57 normal subjects, 127 physicians and nurses worked in SARS wards for one month and 73 SARS patients with different course of SARS were measured by enzyme linked immunosorbent assay. RESULTS: Plasma anti-SARS coronavirus IgG antibody was not detected in normal subjects and the clinical personnel. After 0-7 days, 8-10 days, 11-14 days, 15-20 days of onset of disease, the positive rates were 0.33%, 52%, 86% respectively, and the general positive rate was 61%. CONCLUSION: The specificity and sensitivity of ELISA to detect plasma anti-SARS IgG antibody were satisfactory. Cases with positive reaction could be diagnosed as patients already infected by the virus. The specific IgG antibody didn't emerge in some patients in the early stage of the disease, and the negative results didn't indicate that they were not infected. And follow-up investigation should be made in those patients. Unlike common epidemic infectious diseases, SARS probably hadn't the potentiality of subclinical infection.",,"immunoglobulin G; virus antibody; adult; article; blood; China; enzyme linked immunosorbent assay; female; human; immunology; male; middle aged; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; Adult; Antibodies, Viral; China; Enzyme-Linked Immunosorbent Assay; Female; Humans; Immunoglobulin G; Male; Middle Aged; SARS Virus; Sensitivity and Specificity; Severe Acute Respiratory Syndrome",,"Xu, G.",,,1671167X,,,"12914210","Chinese","Beijing Da Xue Xue Bao",Article,"Final",,Scopus,2-s2.0-0042736368
"Shek C.C., Ng P.C., Fung G.P., Cheng F.W., Chan P.K., Peiris M.J., Lee K.H., Wong S.F., Cheung H.M., Li A.M., Hon E.K., Yeung C.K., Chow C.B., Tam J.S., Chiu M.C., Fok T.F.","35171390400;17137242500;7004213707;7202811097;32067487100;7005486823;8965968100;7404590679;7201839464;7403291810;7005164603;57205870909;7402578582;24788939600;7101866205;7006455238;","Infants born to mothers with severe acute respiratory syndrome.",2003,"Pediatrics","112","4",,"","",,48,"10.1542/peds.112.4.e254","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041887419&doi=10.1542%2fpeds.112.4.e254&partnerID=40&md5=d7538c5d076440b172ea81f180d11e25","Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong","Shek, C.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Ng, P.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Fung, G.P., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Cheng, F.W., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Chan, P.K., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Peiris, M.J., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Lee, K.H., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Wong, S.F., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Cheung, H.M., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Li, A.M., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Hon, E.K., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Yeung, C.K., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Chow, C.B., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Tam, J.S., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Chiu, M.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong; Fok, T.F., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, New Territories, Lai Chi Kok, Hong Kong","Severe acute respiratory syndrome (SARS) is a newly discovered infectious disease caused by a novel coronavirus. During the community outbreak in Hong Kong, 5 liveborn infants were born to pregnant women with SARS. A systematic search for perinatal transmission of the SARS-associated coronavirus, including serial reverse transcriptase-polymerase chain reaction assays, viral cultures, and paired serologic titers, failed to detect the virus in any of the infants. In addition, none of the infants developed clinical, radiologic, hematologic, or biochemical evidence suggestive of SARS. One preterm infant developed jejunal perforation and another developed necrotizing enterocolitis with ileal perforation shortly after birth. This case series is the first report to describe the clinical course of the first cohort of liveborn infants born to pregnant women with SARS.",,"antiinflammatory agent; antivirus agent; methylprednisolone; ribavirin; adult; article; case report; cesarean section; cohort analysis; disease transmission; epidemic; female; Hong Kong; human; ileum disease; intestine perforation; intrauterine growth retardation; isolation and purification; jejunum disease; male; necrotizing enterocolitis; neonatal respiratory distress syndrome; newborn; pregnancy; pregnancy complication; prematurity; SARS coronavirus; severe acute respiratory syndrome; virology; Adult; Anti-Inflammatory Agents; Antiviral Agents; Cesarean Section; Cohort Studies; Disease Outbreaks; Disease Transmission, Vertical; Enterocolitis, Necrotizing; Female; Fetal Growth Retardation; Hong Kong; Humans; Ileal Diseases; Infant, Newborn; Infant, Premature; Intestinal Perforation; Jejunal Diseases; Male; Methylprednisolone; Pregnancy; Pregnancy Complications, Infectious; Respiratory Distress Syndrome, Newborn; Ribavirin; SARS Virus; Severe Acute Respiratory Syndrome",,"Shek, C.C.",,,10984275,,,"14523207","English","Pediatrics",Article,"Final",Open Access,Scopus,2-s2.0-0041887419
"Hu J., Wang J., Xu J., Li W., Han Y., Li Y., Ji J., Ye J., Xu Z., Zhang Z., Wei W., Li S., Wang J., Wang J., Yu J., Yang H.","8249689300;57202343794;7407003499;57201905404;35310510700;57202364500;36983919500;57208010895;55502690600;8312674300;57198566868;7409241896;55552724800;57200022156;8679878600;34573719100;","Evolution and variation of the SARS-CoV genome.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"216","225",,2,"10.1016/S1672-0229(03)01027-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13744254994&doi=10.1016%2fS1672-0229%2803%2901027-1&partnerID=40&md5=edbc16338038296cb33b424c2e4285b2","College of Life Sciences, Peking University, Beijing, 100871, China","Hu, J., College of Life Sciences, Peking University, Beijing, 100871, China; Wang, J., College of Life Sciences, Peking University, Beijing, 100871, China; Xu, J., College of Life Sciences, Peking University, Beijing, 100871, China; Li, W., College of Life Sciences, Peking University, Beijing, 100871, China; Han, Y., College of Life Sciences, Peking University, Beijing, 100871, China; Li, Y., College of Life Sciences, Peking University, Beijing, 100871, China; Ji, J., College of Life Sciences, Peking University, Beijing, 100871, China; Ye, J., College of Life Sciences, Peking University, Beijing, 100871, China; Xu, Z., College of Life Sciences, Peking University, Beijing, 100871, China; Zhang, Z., College of Life Sciences, Peking University, Beijing, 100871, China; Wei, W., College of Life Sciences, Peking University, Beijing, 100871, China; Li, S., College of Life Sciences, Peking University, Beijing, 100871, China; Wang, J., College of Life Sciences, Peking University, Beijing, 100871, China; Wang, J., College of Life Sciences, Peking University, Beijing, 100871, China; Yu, J., College of Life Sciences, Peking University, Beijing, 100871, China; Yang, H., College of Life Sciences, Peking University, Beijing, 100871, China","Knowledge of the evolution of pathogens is of great medical and biological significance to the prevention, diagnosis, and therapy of infectious diseases. In order to understand the origin and evolution of the SARS-CoV (severe acute respiratory syndrome-associated coronavirus), we collected complete genome sequences of all viruses available in GenBank, and made comparative analyses with the SARS-CoV. Genomic signature analysis demonstrates that the coronaviruses all take the TGTT as their richest tetranucleotide except the SARS-CoV. A detailed analysis of the forty-two complete SARS-CoV genome sequences revealed the existence of two distinct genotypes, and showed that these isolates could be classified into four groups. Our manual analysis of the BLASTN results demonstrates that the HE (hemagglutinin-esterase) gene exists in the SARS-CoV, and many mutations made it unfamiliar to us.",,"amino acid substitution; article; biology; codon; comparative study; DNA base composition; genetic variability; genetics; horizontal gene transfer; molecular evolution; nucleotide sequence; phylogeny; protein motif; SARS coronavirus; virus genome; Amino Acid Motifs; Amino Acid Substitution; Base Composition; Codon; Computational Biology; DNA Mutational Analysis; Evolution, Molecular; Gene Transfer, Horizontal; Genome, Viral; Phylogeny; SARS Virus; Variation (Genetics)",,"Hu, J.",,,16720229,,,"15629034","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-13744254994
"Mozer-Lisewska I., Góralski M., Zeromski J.","6602163975;57209955396;7006255390;","Severe acute respiratory syndrome (SARS)--present status [Ciezki ostry zespół oddechowy (SARS)--stan obecny.]",2003,"Postpy higieny i medycyny doświadczalnej","57","6",,"739","752",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342596595&partnerID=40&md5=86c48ebcaf733aa66cb88b977ab96cf7","Klinika Obserwacyjno-Zakaźna Instytutu Pediatrii, Akademii Medycznej im. K. Marcinkowskiego w Poznaniu., Poland","Mozer-Lisewska, I., Klinika Obserwacyjno-Zakaźna Instytutu Pediatrii, Akademii Medycznej im. K. Marcinkowskiego w Poznaniu., Poland; Góralski, M., Klinika Obserwacyjno-Zakaźna Instytutu Pediatrii, Akademii Medycznej im. K. Marcinkowskiego w Poznaniu., Poland; Zeromski, J., Klinika Obserwacyjno-Zakaźna Instytutu Pediatrii, Akademii Medycznej im. K. Marcinkowskiego w Poznaniu., Poland","Basic facts about SARS are presented, including epidemiology, clinical symptoms and the course of disease, multinational search of etiological factor, diagnostic approaches and others. The role of molecular biology in elucidating structure, features and phylogenetic aspects of SARS coronavirus is underlined.",,"human; pathogenicity; review; SARS coronavirus; severe acute respiratory syndrome; virology; Humans; SARS Virus; Severe Acute Respiratory Syndrome",,"Mozer-Lisewska, I.",,,00325449,,,"15002168","Polish","Postepy Hig Med Dosw",Review,"Final",,Scopus,2-s2.0-2342596595
"Wu Q., Zhang Y., Lü H., Wang J., He X., Liu Y., Ye C., Lin W., Hu J., Ji J., Xu J., Ye J., Hu Y., Chen W., Li S., Wang J., Wang J., Bi S., Yang H.","7404602222;7601323407;55488128800;36078440500;55583771300;57192562195;54943580400;57211371580;8249689300;36983919500;56115674400;55468394300;12775742400;7409640047;7409241896;55552724800;57200022156;7101633642;34573719100;","The E protein is a multifunctional membrane protein of SARS-CoV.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","2",,"131","144",,3,"10.1016/S1672-0229(03)01017-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2942704360&doi=10.1016%2fS1672-0229%2803%2901017-9&partnerID=40&md5=080c198384227c5303e59724e253b660","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Wu, Q., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Lü, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; He, X., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Liu, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ye, C., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Lin, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Hu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ji, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ye, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Hu, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Chen, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Bi, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","The E (envelope) protein is the smallest structural protein in all coronaviruses and is the only viral structural protein in which no variation has been detected. We conducted genome sequencing and phylogenetic analyses of SARS-CoV. Based on genome sequencing, we predicted the E protein is a transmembrane (TM) protein characterized by a TM region with strong hydrophobicity and alpha-helix conformation. We identified a segment (NH2-_L-Cys-A-Y-Cys-Cys-N_-COOH) in the carboxyl-terminal region of the E protein that appears to form three disulfide bonds with another segment of corresponding cysteines in the carboxyl-terminus of the S (spike) protein. These bonds point to a possible structural association between the E and S proteins. Our phylogenetic analyses of the E protein sequences in all published coronaviruses place SARS-CoV in an independent group in Coronaviridae and suggest a non-human animal origin.",,"membrane protein; spike glycoprotein, coronavirus; virus envelope protein; amino acid sequence; article; cluster analysis; codon; comparative study; DNA sequence; gene structure; genetics; metabolism; molecular genetics; nucleotide sequence; phylogeny; protein conformation; SARS coronavirus; sequence alignment; sequence homology; virus genome; Amino Acid Sequence; Base Sequence; Cluster Analysis; Codon; Gene Components; Genome, Viral; Membrane Glycoproteins; Membrane Proteins; Molecular Sequence Data; Phylogeny; Protein Conformation; SARS Virus; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology; Viral Envelope Proteins",,"Wu, Q.",,,16720229,,,"15626343","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-2942704360
"Oh J.S., Song D.S., Park B.K.","7402155170;7402443633;37043845100;","Identification of a putative cellular receptor 150 kDa polypeptide for porcine epidemic diarrhea virus in porcine enterocytes.",2003,"Journal of veterinary science (Suwon-si, Korea)","4","3",,"269","275",,34,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542497429&partnerID=40&md5=5a5d7acfd12fec47c124865c79eaabb2","Department of Microbiology, Virology Lab, College of Veterinary Medicine and School of Agricultural Biotechnology, Seoul National University, Seoul, 151-742, South Korea","Oh, J.S., Department of Microbiology, Virology Lab, College of Veterinary Medicine and School of Agricultural Biotechnology, Seoul National University, Seoul, 151-742, South Korea; Song, D.S., Department of Microbiology, Virology Lab, College of Veterinary Medicine and School of Agricultural Biotechnology, Seoul National University, Seoul, 151-742, South Korea; Park, B.K., Department of Microbiology, Virology Lab, College of Veterinary Medicine and School of Agricultural Biotechnology, Seoul National University, Seoul, 151-742, South Korea","Porcine epidemic diarrhea virus (PEDV) causes an acute enteritis in pigs of all ages, often fatality for neonates. PEDV occupies an intermediate position between two well characterized members of the coronavirus group I, human coronavirus (HCoV-229E)and transmissible gastroenteritis virus (TGEV) which uses aminopeptidase N (APN), a 150 kDa protein, as their receptors. However, the receptor of the PEDV has not been identified yet. A virus overlay protein binding assay (VOPBA) was used to identify PEDV binding protein in permissive cells. The binding ability of PEDV to porcine APN (pAPN) and the effects of pAPN on infectivity of PEDV in Vero cells were also investigated. VOPBA identified a 150 kDa protein, as a putative PEDV receptor in enterocytes and swine testicle (ST) cells. Further the PEDV binding to pAPN was blocked by anti-pAPN and pAPN enhanced PEDV infectivity in Vero cells. In conclusion, these results suggested that pAPN may act as a receptor of PEDV.",,"microsomal aminopeptidase; virus receptor; animal; animal disease; article; Cercopithecus; Coronavirus; digestive system disease; enzyme linked immunosorbent assay; enzymology; intestine cell; male; metabolism; protein binding; swine; swine disease; Vero cell; virology; virus infection; Animals; Antigens, CD13; Cercopithecus aethiops; Coronavirus; Coronavirus Infections; Digestive System Diseases; Enterocytes; Enzyme-Linked Immunosorbent Assay; Male; Protein Binding; Receptors, Virus; Swine; Swine Diseases; Vero Cells",,"Oh, J.S.",,,1229845X,,,"14685034","English","J. Vet. Sci.",Article,"Final",,Scopus,2-s2.0-1542497429
"Zhao J.M., Zhou G.D., Sun Y.L., Wang S.S., Yang J.F., Meng E.H., Pan D., Li W.S., Zhou X.S., Wang Y.D., Lu J.Y., Li N., Wang D.W., Zhou B.C., Zhang T.H.","7410309303;7403685731;55737733200;7410348870;57192461900;23478230400;57210512538;57196303672;57198478574;57203771307;57199240153;55361807200;55713349900;55455919000;7404374192;","Clinical pathology and pathogenesis of severe acute respiratory syndrome",2003,"Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology","17","3",,"217","221",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-24644477231&partnerID=40&md5=a72bad45260e2f7d18d1de03a2873f05","The No. 302 Hospital of PLA, Beijing, 100039, China","Zhao, J.M., The No. 302 Hospital of PLA, Beijing, 100039, China; Zhou, G.D., The No. 302 Hospital of PLA, Beijing, 100039, China; Sun, Y.L., The No. 302 Hospital of PLA, Beijing, 100039, China; Wang, S.S., The No. 302 Hospital of PLA, Beijing, 100039, China; Yang, J.F., The No. 302 Hospital of PLA, Beijing, 100039, China; Meng, E.H., The No. 302 Hospital of PLA, Beijing, 100039, China; Pan, D., The No. 302 Hospital of PLA, Beijing, 100039, China; Li, W.S., The No. 302 Hospital of PLA, Beijing, 100039, China; Zhou, X.S., The No. 302 Hospital of PLA, Beijing, 100039, China; Wang, Y.D., The No. 302 Hospital of PLA, Beijing, 100039, China; Lu, J.Y., The No. 302 Hospital of PLA, Beijing, 100039, China; Li, N., The No. 302 Hospital of PLA, Beijing, 100039, China; Wang, D.W., The No. 302 Hospital of PLA, Beijing, 100039, China; Zhou, B.C., The No. 302 Hospital of PLA, Beijing, 100039, China; Zhang, T.H., The No. 302 Hospital of PLA, Beijing, 100039, China","BACKGROUND: To explore the pathological features and pathogenesis of severe acute respiratory syndrome (SARS) to provide evidence for the clinical treatment and prevention of SARS. METHODS: Pathological features of 2 cases of full autopsy and 4 cases of needle biopsy tissue samples from the patients who died from SARS were studied by light and electron microscopy. The distribution and quantity of lymphocyte subpopulations in the lungs and immune organs from SARS patients were analyzed by immunohistochemistry. The location and semi-quantitative analysis of SARS coronavirus in the tissue specimens were studied by electron microscopy, in situ hybridization and immunohistochemistry. RESULTS: In total of 6 cases, diffuse alveolar damage and alveolar cell proliferation were common. The major pathological changes of 2 autopsy cases of SARS in lung tissues were acute pulmonary interstitial and alveolar exudative inflammation, and 2 autopsy and one biopsy lung tissues showed alveolar hyaline membrane formation. Terminal bronchiolar and alveolar desquamation of lung tissues in one autopsy and 2 biopsy cases were noted. Among 6 cases, 2 biopsy cases presented early pulmonary fibrosis and alveolar organization. Meanwhile, the immune organs, including lymph nodes and spleens from 2 autopsy cases of SARS whose disease courses were less than 12 days showed extensive hemorrhagic necrosis, reactive macrophage/histocyte proliferation, with relative depression of mononuclear and granulocytic clones in the bone marrows. However, spleen and bone marrow biopsy tissue samples from 4 dead SARS cases whose clinical course lasted from 21 to 40 days presented repairing changes. SARS coronaviruses were mainly identified in type I and II alveolar epithelia, macrophages, and endothelia; meanwhile, some renal tubular epithelial cells, cardiomyocytes, mucosal and crypt epithelial cells of gastrointestinal tracts, parenchymal cells in adrenal glands, lymphocytes, testicular epithelial cells and Leydig's cells were also detected by electron microscopy combined with in situ hybridization. The semi-quantitative analysis of lymphocyte subpopulations revealed that the proportion of CD8+ T lymphocytes were about 80% of the total infiltrative inflammatory cells in the pulmonary interstitium, with a few CD4+ lymphocytes CD3+, CD4+, CD8+ or CD20+ lymphocyte subpopulations were obviously decreased and there was imbalance in number and proportion, while CD57+, CD68+, S-100+ and HLA-DR+ cells were relatively increased in lymph nodes and spleens. CONCLUSIONS: Histologically, the pulmonary changes could be divided into acute inflammatory exudative, terminal bronchiolar and alveolar desquamative and proliferative repair stages or types during the pathological process of SARS. SARS coronavirus was found in multi-target cells in vivo, which means that SARS coronavirus might cause multi-organ damages which were predominant in lungs. There were varying degrees of decrease and imbalance in number and proportion of lymphocyte subpopulations in the immune organs of the patients with SARS. However, these changes may be reversible. It was found that cellular immune responses were predominant in the lungs of SARS cases, which might play an important role in getting rid of coronaviruses in infected cells and inducing immune mediated injury.",,"aged; article; female; human; immunology; isolation and purification; lung; lymphocyte subpopulation; male; middle aged; pathology; SARS coronavirus; severe acute respiratory syndrome; ultrastructure; virology; Aged; Female; Humans; Lung; Lymphocyte Subsets; Male; Middle Aged; SARS Virus; Severe Acute Respiratory Syndrome",,"Zhao, J.M.email: jmzhao@hotmail.com",,,10039279,,,"15340561","Chinese","Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-24644477231
"Zhong Y.F., Gao X.M., Wang S.L., Xie Z.G., Ma Y., Fang W.G., Zou W.Z., Li X.L., Zhang Q.Y., Wang W., Zhao Z.D., Gu J.","7401809046;55712089200;37002202500;7402267402;57191373887;55648692000;7102660939;57192496005;57199110214;7501760568;55726165200;55343448700;","Pathologic study of circulating blood leukocytes in severe acute respiratory syndrome",2003,"Zhonghua yi xue za zhi","83","24",,"2137","2141",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342596535&partnerID=40&md5=735568589d79f5cf258040d7f8e52056","Department of Pathology, Peking University Health Science Center, Beijing, 100083, China","Zhong, Y.F., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Gao, X.M., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Wang, S.L., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Xie, Z.G., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Ma, Y., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Fang, W.G., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Zou, W.Z., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Li, X.L., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Zhang, Q.Y., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Wang, W., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Zhao, Z.D., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China; Gu, J., Department of Pathology, Peking University Health Science Center, Beijing, 100083, China","OBJECTIVE: To study the pathologic characteristics and pathogenesis of circulating blood leucocytes infected by severe acute respiratory syndrome associated coronavirus (SARS CoV or SCV) in SARS patients. METHODS: Blood samples of 22 SARS patients were studied, and 4 healthy blood samples were observed as negative controls. The white blood cells were collected from whole blood. The ultrastructural characteristics were observed by transmission electron microscopy. CD45RO antibody was used for pre-embedding immunoelectron microscopy. The SARS viral sequence was detected with real-time polymerase chain reaction (RT-PCR). RESULTS: Coronavirus-like particles were founded in the leukocytes in 6 of the 22 blood samples. Five of them gave positive results in the real-time PCR. The number of granulocytes was increased (P < 0.05) and that of lymphocytes was decreased (P < 0.05) respectively. Immunoelectron microscopy showed that CD45RO positive T lymphocyte decreased to 6% - 7%. Circulating lymphocytes had the highest percentage of infection. The morphologic characteristics of coronavirus-like particles were spherical or oval in shape, about 80 - 120 nm in diameter, with a dense round core and a clear halo around the core. A distinct membrane and club-shaped surface projections were seen in the periphery. The particles were located in the cytoplasm, the cisternae of endoplasmic reticulum, Golgi apparatus and vesicles. Virus entered cells by endocytosis or membrane fusion and was released through a budding process. CONCLUSION: Our data suggested that lymphocytes, particularly T cells, were probably the target cells of SARS CoV. The viruses may actively infected the immune cells during SARS CoV acute infection phase and the destruction of target cells may be one of the important reasons for the death of the circulating leukocytes in SARS.",,"article; blood; electron microscopy; female; human; leukocyte; leukocyte count; lymphocyte; male; pathology; severe acute respiratory syndrome; ultrastructure; Female; Humans; Leukocyte Count; Leukocytes; Lymphocytes; Male; Microscopy, Electron; Severe Acute Respiratory Syndrome",,"Zhong, Y.F.",,,03762491,,,"14720422","Chinese","Zhonghua Yi Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-2342596535
"Xu J., Hu J., Wang J., Han Y., Hu Y., Wen J., Li Y., Ji J., Ye J., Zhang Z., Wei W., Li S., Wang J., Wang J., Yu J., Yang H.","56115674400;8249689300;36078440500;35310510700;12775742400;49664305200;57202364500;36983919500;57208010895;8312674300;57198566868;7409241896;55552724800;57200022156;8679878600;34573719100;","Genome organization of the SARS-CoV.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"226","235",,4,"10.1016/S1672-0229(03)01028-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13744262562&doi=10.1016%2fS1672-0229%2803%2901028-3&partnerID=40&md5=026012c3575641a9e0c1bf43abb61d3e","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Xu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Hu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Han, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Hu, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wen, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ji, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ye, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wei, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Annotation of the genome sequence of the SARS-CoV (severe acute respiratory syndrome-associated coronavirus) is indispensable to understand its evolution and pathogenesis. We have performed a full annotation of the SARS-CoV genome sequences by using annotation programs publicly available or developed by ourselves. Totally, 21 open reading frames (ORFs) of genes or putative uncharacterized proteins (PUPs) were predicted. Seven PUPs had not been reported previously, and two of them were predicted to contain transmembrane regions. Eight ORFs partially overlapped with or embedded into those of known genes, revealing that the SARS-CoV genome is a small and compact one with overlapped coding regions. The most striking discovery is that an ORF locates on the minus strand. We have also annotated non-coding regions and identified the transcription regulating sequences (TRS) in the intergenic regions. The analysis of TRS supports the minus strand extending transcription mechanism of coronavirus. The SNP analysis of different isolates reveals that mutations of the sequences do not affect the prediction results of ORFs.",,"amino acid substitution; article; biological model; biology; DNA base composition; genetic transcription; genetics; isoelectric point; methodology; molecular genetics; molecular weight; nucleotide sequence; open reading frame; SARS coronavirus; sequence analysis; virus genome; Amino Acid Substitution; Base Composition; Base Sequence; Computational Biology; Genome, Viral; Isoelectric Point; Models, Genetic; Molecular Sequence Data; Molecular Weight; Open Reading Frames; SARS Virus; Sequence Analysis; Transcription, Genetic",,"Xu, J.",,,16720229,,,"15629035","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-13744262562
"Al Marri M.R.H.A., Al Khal A.L.","55958884400;6507333591;","The dilemma of Severe Acute Respiratory Syndrome (SARS): Is it SARS or just a cold or the flu?",2003,"Qatar Medical Journal","12","1",,"56","58",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042388394&partnerID=40&md5=06f7a95bade886e5b4cc4dce166cb47c","Pulmonary Intensive Care/Sleep Med., Army Medical Services, Hamad Medical Corporation, Doha, Qatar; Department of Medicine, Hamad Medical Corporation, Doha, Qatar","Al Marri, M.R.H.A., Pulmonary Intensive Care/Sleep Med., Army Medical Services, Hamad Medical Corporation, Doha, Qatar, Department of Medicine, Hamad Medical Corporation, Doha, Qatar; Al Khal, A.L., Department of Medicine, Hamad Medical Corporation, Doha, Qatar","SARS is a term used to describe a serious respiratory illness. Its main symptoms are high fever (>38° C), dry cough, shortness of breath or difficulty in breathing. Changes in chest X-rays indicative of pneumonia also occur. SARS appears to be less infectious than influenza. The incubation period is believed to be short, around three to six days (maximum 10 days). The global death rate for probable SARS cases is 4%. The cause of SARS has now been documented by WHO to be ""SARS coronavirus"" (SARS CoV) a new member of the coronavirus family. Most patients identified up to date have been previously healthy adults aged 25-70 years. Based on currently available evidence, close contact with an infected person poses the highest risk of the infective agent spreading from one person to another. SARS is a new disease which has its origins in Guangdong Province, China. The earliest known cases were identified in mid-November 2002. Since then, probable cases of SARS have been reported in at least 28 countries.",,"article; China; cold; Coronavirus; coughing; disease severity; disease transmission; dyspnea; fever; health survey; high risk population; human; incubation time; influenza; mortality; pneumonia; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; symptom; thorax radiography; world health organization","Update 14: On cases and countries (2003), http://www.who.int/csr/sars/archive/2003_03_29/en, Severe Acute respiratory syndrome. Geneva: World Health Organization, March; Drazen, J.M., Case Cluster of the severe acute respiratory syndrome (2003) NEMJ, 348 (20), pp. e6-e7; Update 3: Disease outbreak reported (2003), http://www.who.int/csr/sars/archive/2003_02_26/en, Acute respiratory syndrome in China. Geneva: World Health Organization, February; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; WHO issues a global alert about cases of atypical pneumonia (2003), http://www.who.int/csr/sars/archive/2003_02_26/en, Geneva: World health Organization, 12th March; (2003), http://app.moh.gov.sg/new/new01.asp, Update on atypical pneumonia cases in Singapore 14th March Available at; (2003), http://www.who.int/csr/sars/archive/2003_03_29/en, Update 14 - Update on cases and countries 29th March; (2003), http://www.who.int/csr/sars/archive/2003_04_2/en, Update 17 - Travel advice - Hong Kong Special Administrative Region of China, and Guangdong Province, China. 2nd April; Update: Outbreak of severe acute respiratory syndrome-worldwide, 2003 (2003) MMWR Morb. Mortal Wkly. Rep., 52, pp. 241-248; http://www.cdc.gov/travel/other/sars_can.htm, CDC. Interim travel alert: Toronto, Ontario, Canada. Available at; http://www.who.int/csr/sars/case, Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS). Available at: definition/en/ http://www.who.int/csr/sars/ ; http://www.cdc.gov/ncidod","Al Marri, M.R.H.A.P.O. Box 6398, Doha, Qatar",,"Hamad Medical Corporation",02538253,,QMJAA,,"English","Qatar Med. J.",Article,"Final",,Scopus,2-s2.0-0042388394
"Antonio G.E., Wong K.T., Chu W.C.W., Hui D.S.C., Cheng F.W.T., Yuen E.H.Y., Chung S.S.C., Fok T.F., Sung J.J.Y., Ahuja A.T.","7003714763;7404760076;56588365400;7101862411;7202811097;7006166110;7404293373;7006455238;35405352400;35449659800;","Imaging in severe acute respiratory syndrome (SARS)",2003,"Clinical Radiology","58","11",,"825","832",,8,"10.1016/S0009-9260(03)00308-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242300085&doi=10.1016%2fS0009-9260%2803%2900308-8&partnerID=40&md5=31113c05b49f395ad8947bf2ff0a87fe","Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Medicine/Therapeutics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Paediatrics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Surgery, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong","Antonio, G.E., Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Wong, K.T., Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Chu, W.C.W., Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Hui, D.S.C., Department of Medicine/Therapeutics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Cheng, F.W.T., Department of Paediatrics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Yuen, E.H.Y., Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Chung, S.S.C., Department of Surgery, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Fok, T.F., Department of Paediatrics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Sung, J.J.Y., Department of Medicine/Therapeutics, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; Ahuja, A.T., Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong","Severe acute respiratory syndrome (SARS) is a highly infectious disease caused by a novel coronavirus, and has become pandemic within a short period of time. Imaging plays an important role in the diagnosis, management and follow-up of patients with SARS. The current status of imaging in SARS is presented in this review. © 2003 The Royal College of Radiologists. Published by Elsevier Ltd. All rights reserved.","Computed tomography; Radiography; SARS; Severe acute respiratory syndrome","corticosteroid; methylprednisolone; ribavirin; computer assisted tomography; Coronavirus; diagnostic accuracy; diagnostic procedure; drug pulse therapy; epidemic; follow up; human; image analysis; imaging system; mortality; pathogenesis; patient care; patient monitoring; priority journal; prognosis; respiratory tract infection; review; SARS coronavirus; severe acute respiratory syndrome; thorax radiography; treatment outcome","Cumulative number of reported probable cases of severe acute respiratory syndrome (SARS) (2003), http://www.who.int/csr/sars/country/2003_05_14/en, World Health Organisation. (Accessed May 15, at); Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966. , http://content.nejm.org/cgi/reprint/NEJMoa030781v3.pdf; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Case definition of severe acute respiratory syndrome (SARS) (2003), http://www.who.int/csr/sars/casedefinition/en, World Health Organisation. (Available at Accessed 20 May); Preliminary clinical description of severe acute respiratory syndrome (2003), http://www.who.int/csr/sars/clinical/en, World Health Organisation. (Accessed 21 March); Diagnosis/Evaluation for SARS (2003), http://www.cdc.gov/ncidod/sars/diagnosis.htm, Centers for Disease Control and Prevention, USA. (Accessed April 7, at); Wong, K.T., Antonio, G.E., Hui, D.S., Severe acute respiratory syndrome: Radiographic appearances and pattern of progression in 138 patients (2003) Radiology, 228, pp. 401-406; Wong, K.T., Antonio, G.E., Hui, D.S., Thin-section CT of severe acute respiratory syndrome: Evaluation of 73 patients exposed to or with the disease (2003) Radiology, 228, pp. 395-400; Antonio, G.E., Wong, K.T., Hui, D.S., Imaging of severe acute respiratory syndrome in Hong Kong (2003) AJR Am. J. Roentgenol., 181, pp. 11-17; Antonio, G.E., Wong, K.T., Hui, D.S., Thin-section CT in patients with severe acute respiratory syndrome following hospital discharge: Preliminary experience (2003) Radiology, 228, pp. 810-815; Goodman, L.R., Goren, R.A., Teptick, S.K., The radiographic evaluation of pulmonary infection (1980) Med. Clin. North Am., 64, pp. 553-574; Macfarlane, J.T., Miller, A.C., Roderick Smith, W.H., Comparative radiographic features of community acquired Legionnaire's disease, pneumococcal pneumonia, mycoplasma pneumonia, and psittacosis (1984) Thorax, 39, pp. 28-33; Kim, E.A., Lee, K.S., Primack, S.L., Viral pneumonias in adults: Radiologic and pathologic findings (2002) RadioGraphics, 22 (SUPPL.), pp. 137S-149S; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Leung, A.N., Müller, N.L., Pineda, P.R., FitzGerald, J.M., Primary tuberculosis in childhood: Radiographic manifestations (1992) Radiology, 182, pp. 87-91; Leatherman, J.W., Iber, C., Davies, S.F., Cavitation in bacteremic pneumococcal pneumonia (1984) Am. Rev. Respir. Dis., 129, pp. 317-321; Amorosa, N.M., Genieser, N.B., Rocke, K.J., Feasibility of high-resolution, low dose chest CT in evaluation of the pediatric chest (1994) Pediatr. Radiol., 26, pp. 6-10; Lucaya, J., Le Pointe, H.D., High-resolution CT of the lung in children (2002) Pediatric Chest Imaging, pp. 55-91. , Lucaya J, Strife JL Berlin: Springer","Antonio, G.E.; Dept. Diagn. Radiology/Organ Imaging, The Chinese University of Hongkong, Prince of Wales Hospital, Shatin, Hong Kong; email: gregantonio@cuhk.edu.hk",,"W.B. Saunders Ltd",00099260,,CLRAA,"14581005","English","Clin. Radiol.",Review,"Final",Open Access,Scopus,2-s2.0-0242300085
"Soares C.","57196723737;","Caught off guard",2003,"Scientific American","288","6",,"18","19",,1,"10.1038/scientificamerican0603-18","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038580454&doi=10.1038%2fscientificamerican0603-18&partnerID=40&md5=1a69dd94d8a4f33c1e7ab58c05b4977e",,"Soares, C.","The article discusses the causes and effects of severe acute respiratory syndrome (SARS). SARS kills about 5 percent of its victims and another 10 to 15 percent survive only because of modern intensive-care practices. The disease is caused by a new coronavirus, one of a family of large RNA viruses that invades immune cells. In SARS, the resulting inflammation of lung tissue can lead to severe pneumonia and even hemorrhage.",,"Drug therapy; Hospitals; Vaccines; Disease outbreak; Disease control; Coronavirus; RNA viruses; article; China; disease transmission; epidemic; health care organization; human; severe acute respiratory syndrome; United States; world health organization; China; Disease Outbreaks; Humans; National Institutes of Health (U.S.); Severe Acute Respiratory Syndrome; United States; World Health Organization",,,,"Scientific American Inc.",00368733,,SCAMA,"12764925","English","Sci. Am.",Review,"Final",,Scopus,2-s2.0-0038580454
"Wang Y.S., Shen H., Sun S.H., Jiang L.H., Liu Y., Zhu Z.W., Xiao D.J., Huang P., Yang B., Du X.Y., Zhang Y.C.","36667742100;57199935042;55479096500;56311027600;57192562653;7404802549;12773486100;57198537539;7404472939;7402552078;35231947500;","Analysis of false-positive associated with antibody tests for SARS-CoV in SLE patients",2003,"Shi yan sheng wu xue bao","36","4",,"314","317",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3843104884&partnerID=40&md5=8e173f44ccbeddc22f2222e65ae64cb0","Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China","Wang, Y.S., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Shen, H., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Sun, S.H., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Jiang, L.H., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Liu, Y., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Zhu, Z.W., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Xiao, D.J., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Huang, P., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Yang, B., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Du, X.Y., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China; Zhang, Y.C., Centrol Laboratory, Jinan Centrol Hospital, Clinical Medical College of Shandong University, Jinan, 250013., China","To discuss the false-positive of serological diagnostic testing for coronavirus antibody in patients with systemic lupus erythematosus(SLE), 66 normal individual and 31 SLE with non-SARS patients were detected for SARS-associated coronavirus (SARS-CoV) antibody and RNA by enzymelinked immunosorbent assays(ELISA) and reverse transcriptase-polymerase chain reaction(RT-PCR). The result showed 2/66 cases(3.0%) were positive of SARS-CoV-IgG antibody and 66 cases were negative of SARS-CoV-IgM antibody in the 66 cases healthy controls; in 31 cases with SLE, positive rates of SARS-CoV-IgG and IgM antibody were 58.1% (18/31) and 29% (9/31), respectively, in which 7 cases(22.6%) were positive of both SARS-CoV-IgG and IgM antibody. All samples of positive SARS-CoV-IgG and IgM antibody were negative by RT-PCR. The ELISA kit coated by non-purification antigen may induce the false-positive of SARS-CoV antibody in patients with SLE. This result suggested that the specificity of ELISA tests for SARS was excellent and has low false-positive rates when using SARS-CoV-IgG and IgM antibody tests. A possible cause of false-positive of SARS-CoV-IgG and IgM antibody in SLE patients is coated antigens with SARS-CoV and Vero-E6 cells in ELISA methods.",,"autoantibody; immunoglobulin G; immunoglobulin M; virus antibody; adolescent; adult; article; blood; enzyme linked immunosorbent assay; human; immunology; laboratory diagnosis; reverse transcription polymerase chain reaction; SARS coronavirus; systemic lupus erythematosus; virology; Adolescent; Adult; Antibodies, Viral; Autoantibodies; Enzyme-Linked Immunosorbent Assay; False Positive Reactions; Humans; Immunoglobulin G; Immunoglobulin M; Lupus Erythematosus, Systemic; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus",,"Wang, Y.S.",,,00015334,,,"14574997","Chinese","Shi Yan Sheng Wu Xue Bao",Article,"Final",,Scopus,2-s2.0-3843104884
"Xu Z., Zhang H., Tian X., Ji J., Li W., Li Y., Tian W., Han Y., Wang L., Zhang Z., Xu J., Wei W., Zhu J., Sun H., Zhang X., Zhou J., Li S., Wang J., Wang J., Bi S., Yang H.","36007796100;57192483081;13609877900;36983919500;57207126461;57202364500;57199662994;35310510700;7409189230;8312674300;7407003499;57198566868;8312674600;57214427420;54923054800;57191735715;7409241896;55552724800;57200022156;7101633642;34573719100;","The R protein of SARS-CoV: analyses of structure and function based on four complete genome sequences of isolates BJ01-BJ04.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","2",,"155","165",,4,"10.1016/S1672-0229(03)01019-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2942700499&doi=10.1016%2fS1672-0229%2803%2901019-2&partnerID=40&md5=c5ac0d76ce9554d31cf39d44e8813750","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Xu, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Tian, X., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ji, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Tian, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Han, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, L., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wei, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Sun, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, X., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhou, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Bi, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","The R (replicase) protein is the uniquely defined non-structural protein (NSP) responsible for RNA replication, mutation rate or fidelity, regulation of transcription in coronaviruses and many other ssRNA viruses. Based on our complete genome sequences of four isolates (BJ01-BJ04) of SARS-CoV from Beijing, China, we analyzed the structure and predicted functions of the R protein in comparison with 13 other isolates of SARS-CoV and 6 other coronaviruses. The entire ORF (open-reading frame) encodes for two major enzyme activities, RNA-dependent RNA polymerase (RdRp) and proteinase activities. The R polyprotein undergoes a complex proteolytic process to produce 15 function-related peptides. A hydrophobic domain (HOD) and a hydrophilic domain (HID) are newly identified within NSP1. The substitution rate of the R protein is close to the average of the SARS-CoV genome. The functional domains in all NSPs of the R protein give different phylogenetic results that suggest their different mutation rate under selective pressure. Eleven highly conserved regions in RdRp and twelve cleavage sites by 3CLP (chymotrypsin-like protein) have been identified as potential drug targets. Findings suggest that it is possible to obtain information about the phylogeny of SARS-CoV, as well as potential tools for drug design, genotyping and diagnostics of SARS.",,"RNA directed RNA polymerase; amino acid sequence; article; biology; cluster analysis; comparative study; DNA base composition; DNA sequence; gene structure; genetics; molecular evolution; molecular genetics; mutation; nucleotide sequence; phylogeny; protein tertiary structure; SARS coronavirus; virus genome; Amino Acid Sequence; Base Composition; Base Sequence; Cluster Analysis; Computational Biology; Conserved Sequence; Evolution, Molecular; Gene Components; Genome, Viral; Molecular Sequence Data; Mutation; Phylogeny; Protein Structure, Tertiary; RNA Replicase; SARS Virus; Sequence Analysis, DNA",,"Xu, Z.",,,16720229,,,"15626345","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-2942700499
"Li S., Lin L., Wang H., Yin J., Ren Y., Zhao Z., Wen J., Zhou C., Zhang X., Li X., Wang J., Zhou Z., Liu J., Shao J., Lei T., Fang J., Xu N., Liu S.","57207248052;55676528000;56608115200;7401693537;57198461840;57199102301;49664305200;12773498800;23029398300;7501700961;8272121600;56141101800;55705826000;8272122100;8322357900;7402966086;55771049200;7409459608;","The epitope study on the SARS-CoV nucleocapsid protein.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"198","206",,8,"10.1016/S1672-0229(03)01025-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13744249411&doi=10.1016%2fS1672-0229%2803%2901025-8&partnerID=40&md5=ebd3af314f28a0e6e932cc9a0fc8a85e","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Lin, L., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yin, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ren, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhao, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wen, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhou, C., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, X., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, X., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhou, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Liu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Shao, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Lei, T., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Fang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xu, N., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Liu, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","The nucleocapsid protein (N protein) has been found to be an antigenic protein in a number of coronaviruses. Whether the N protein in severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is antigenic remains to be elucidated. Using Western blot and Enzyme-linked Immunosorbent Assay (ELISA), the recombinant N proteins and the synthesized peptides derived from the N protein were screened in sera from SARS patients. All patient sera in this study displayed strong positive immunoreactivities against the recombinant N proteins, whereas normal sera gave negative immunoresponses to these proteins, indicating that the N protein of SARS-CoV is an antigenic protein. Furthermore, the epitope sites in the N protein were determined by competition experiments, in which the recombinant proteins or the synthesized peptides competed against the SARS-CoV proteins to bind to the antibodies raised in SARS sera. One epitope site located at the C-terminus was confirmed as the most antigenic region in this protein. A detailed screening of peptide with ELISA demonstrated that the amino sequence from Codons 371 to 407 was the epitope site at the C-terminus of the N protein. Understanding of the epitope sites could be very significant for developing an effective diagnostic approach to SARS.",,"epitope; nucleocapsid protein; peptide fragment; recombinant protein; article; chemistry; enzyme linked immunosorbent assay; genetics; human; immunology; isolation and purification; metabolism; plasmid; SARS coronavirus; synthesis; Western blotting; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Epitopes; Humans; Nucleocapsid Proteins; Peptide Fragments; Plasmids; Recombinant Proteins; SARS Virus",,"Li, S.",,,16720229,,,"15629032","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-13744249411
"Fang L.Q., Zhang P.H., Yang B.A., Wu X.M., Zhao Q.M., Liu W., Liu H., Deng Y.Q., Zhan L., Han W.G., Lu F.S., Wu J.S., Yang H., Zhu Q.Y., Cao W.C.","7402470349;7404158642;56306611900;57207327955;7402763934;36078712200;57116622000;12141082300;24382182100;35386466200;7402967940;37099387600;7406561423;7403313352;57199658059;","The application of indirect immuno-fluorescence assay in the diagnosis of severe acute respiratory syndrome",2003,"Zhonghua liu xing bing xue za zhi = Zhonghua liuxingbingxue zazhi","24","6",,"484","486",,6,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642314203&partnerID=40&md5=c11937fcb44a55d1551377724b49ede9","Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China","Fang, L.Q., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Zhang, P.H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Yang, B.A., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Wu, X.M., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Zhao, Q.M., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Liu, W., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Liu, H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Deng, Y.Q., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Zhan, L., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Han, W.G., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Lu, F.S., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Wu, J.S., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Yang, H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Zhu, Q.Y., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China; Cao, W.C., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing, 100071, China","OBJECTIVE: To explore the temporal profile of serum antibody against coronavirus in patients with severe acute respiratory syndrome (SARS), and to evaluate the reliability of indirect immuno-fluorescence assay (IFA) in the diagnosis of SARS. METHODS: Clinically confirmed SARS patients, suspected SARS patients, and controls were included in the study. IFA was used to detect the serum antibody against SARS coronavirus. General information about the subjects was collected using a standard questionnaire. RESULTS: The positive rates of specific IgG and IgM against SARS virus within 10 days after onset of the disease were 55.1% and 16.3% respectively and then increased up to 89.8% for IgG and 65.3% for IgM. After 25 days of the onset of the disease, 90.9% patients became positive for both IgG and IgM. Results from chi-square for trend test revealed that the positive rates of both IgG and IgM increased with time (chi(2) for trend = 16.376, P = 0.00005 for IgG; chi(2) for trend = 28.736, P = 0.00000 for IgM). Sensitivity, specificity and agreement value of IFA regarding the diagnosis of SARS were all higher than 90%. CONCLUSION: IFA can be used to assist diagnosis of SARS after 10 days of the onset of disease.",,"immunoglobulin G; immunoglobulin M; virus antibody; article; blood; enzyme linked immunosorbent assay; fluorescent antibody technique; human; immunology; methodology; SARS coronavirus; severe acute respiratory syndrome; Antibodies, Viral; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique, Indirect; Humans; Immunoglobulin G; Immunoglobulin M; SARS Virus; Severe Acute Respiratory Syndrome",,"Fang, L.Q.",,,02546450,,,"12848915","Chinese","Zhonghua Liu Xing Bing Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0642314203
"Lang Z.-W., Zhang L.-J., Zhang S.-J., Meng X., Li J.-Q., Song C.-Z., Sun L., Zhou Y.-S., Dwyer D.E.","7005478031;12772909900;57195222009;57199654941;7410057743;7403252919;57212624530;57191653017;7201791996;","A clinicopathological study of three cases of severe acute respiratory syndrome (SARS)",2003,"Pathology","35","6",,"526","531",,38,"10.1080/00313020310001619118","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347416720&doi=10.1080%2f00313020310001619118&partnerID=40&md5=968cad8521683b8b6ed91b84a823cf85","Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; World Health Organisation China, Chaoyang District, Beijing, China; Centre for Infectious Diseases, Microbiology Laboratory Services, Westmead Hospital, Westmead, NSW, Australia; Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, Beijing 100054, China","Lang, Z.-W., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China, Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, Beijing 100054, China; Zhang, L.-J., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Zhang, S.-J., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Meng, X., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Li, J.-Q., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Song, C.-Z., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Sun, L., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Zhou, Y.-S., Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, China; Dwyer, D.E., World Health Organisation China, Chaoyang District, Beijing, China, Centre for Infectious Diseases, Microbiology Laboratory Services, Westmead Hospital, Westmead, NSW, Australia","Aims: The severe acute respiratory syndrome (SARS) caused a large outbreak of atypical pneumonia in Beijing, China from early March 2003. We report the pathological features from three patients who died of SARS. Methods: Autopsies were performed on three patients who died 9-15 days after the onset of the illness, and the clinical and laboratory features reviewed. Tissue sections were stained with haematoxylin and eosin (H&E), and in situ reverse transcriptase polymerase chain reaction (RT-PCR) on lung sections was performed using SARS coronavirus-specific primers. Results: The typical gross pathological change in the lungs was diffuse haemorrhage on the lung surface. Histopathological examination revealed serous, fibrinous and haemorrhagic inflammation in most pulmonary alveoli, with capillary engorgement and some capillary microthrombosis. The pulmonary alveoli were thickened with interstitial mononuclear inflammatory infiltrates, diffuse alveolar damage, desquamation of pneumocytes and hyaline-membrane formation; fibrinoid material and erythrocytes were present in alveolar spaces. There were thromboemboli in some bronchial arterioles. Haemorrhagic necrosis and reduced numbers of lymphocytes were observed in lymph nodes and spleen. In situ RT-PCR detected SARS coronavirus RNA in type II alveolar cells, interstitial cells and bronchiolar epithelial cells from all three patients. Conclusion: Severe immunological damage in lung tissue is responsible for the clinical features of SARS.","Autopsy; Lung disease; SARS coronavirus; Severe acute respiratory syndrome (SARS)","aged; arteriole; article; autopsy; bronchiole; case report; chill; China; coughing; desquamation; epidemic; epithelium cell; erythrocyte; female; fever; histopathology; human; immunopathology; inflammation; inflammatory infiltrate; laboratory test; lung alveolus; lung alveolus cell; lung alveolus cell type 2; lung disease; lung parenchyma; lymph node; lymphocyte; male; microthrombus; nucleotide sequence; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; spleen; thromboembolism; tissue section; virus pneumonia","Summary Table of SARS Cases by Country (1 Nov 2002 - 7 Aug 2003), Severe Acute Respiratory Syndrome (SARS), , www.who.int/csr/sars, World Health Organization Communicable Disease Surveillance & Response (CSR), World Health Organization Website; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Guenther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1985-2005; Ruan, Y., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Tsang, K.W., Ho, P.K., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Fouchier, R.A.M., Kuiken, T., Schutten, M., Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Bellingan, G.J., The pulmonary physician in critical care: 6. The pathogenesis of ALI/ARDS (2002) Thorax, 57, pp. 540-546; Zhao, J.M., Zhou, G.D., Sun, Y.L., Pathological and etiological findings in a dead case of severe acute respiratory syndrome in China (2003) Med J Chin PLA, 28, pp. 5379-5382; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto Area (2003) JAMA, 289, pp. 1-9; Jacobse-Geels, H., Daha, M.R., Horzinek, M., Isolation and characterization of feline C3 and evidence for the immune complex pathogenesis of feline infectious peritonitis (1980) J Immunol, 125, pp. 1606-1610","Lang, Z.-W.; Department of Pathology, Beijing Youan Hospital, Cap. University of Medical Sciences, Beijing 100054, China; email: langzw@21cn.com",,"Carfax Publishing Company",00313025,,PTLGA,"14660106","English","Pathology",Article,"Final",Open Access,Scopus,2-s2.0-0347416720
"Leung T.F., Wong G.W.K., Hon K.L.E., Fok T.F.","55443283900;55664161600;8134452900;7006455238;","Severe acute respiratory syndrome (SARS) in children: Epidemiology, presentation and management",2003,"Paediatric Respiratory Reviews","4","4",,"334","339",,20,"10.1016/S1526-0542(03)00088-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345169965&doi=10.1016%2fS1526-0542%2803%2900088-5&partnerID=40&md5=2cfa79492e9d4846aa1028ee40a3363a","Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, China","Leung, T.F., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, China; Wong, G.W.K., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, China; Hon, K.L.E., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, China; Fok, T.F., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, New Territories, China","Severe acute respiratory syndrome (SARS) is a newly recognised and highly contagious respiratory infection caused by a new strain of coronavirus. The disease can result in progressive respiratory failure in adults and the mortality rate has been reported to be 8-15%. This infection spreads by droplet transmission and children appear to acquire SARS through close household contact exposure to infected adults. Disease severity is, however, much milder in the paediatric age group. The common laboratory findings in infected children and adolescents include lymphopaenia and elevated levels of lactate dehydrogenase and creatinine phosphokinase. Air space consolidation is commonly seen during the course of the illness although chest radiographs are normal on presentation in half of the cases. The pathophysiology of SARS appears to be related to immunological dysregulation in response to the coronavirus infection. The optimal treatment of SARS in children remains to be determined. No case fatality in infected children has been reported. The early and proper isolation of infected adults, meticulous infection control measures in the hospital setting, exhaustive contact tracing and quarantine measures are important steps in preventing the spread of the disease among health care workers and into the community. The development of a sensitive and rapid test for early diagnosis is underway. Further controlled trials are necessary to define the optimal treatment of this infection in children. © 2003 Elsevier Ltd. All rights reserved.","Coronavirus; Respiratory distress; Respiratory infection; SARS","corticosteroid; creatine kinase; glycyrrhizic acid; lactate dehydrogenase; ribavirin; child; childhood disease; childhood mortality; community; Coronavirus; creatine kinase blood level; disease course; disease severity; drug efficacy; early diagnosis; environmental exposure; health care personnel; hospital hygiene; human; infection control; lactate dehydrogenase blood level; lymphocytopenia; pathophysiology; patient care; priority journal; respiratory failure; reverse transcription polymerase chain reaction; review; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; thorax radiography; virus pneumonia; virus transmission","Acute respiratory syndrome in China (2003), http://www.who.int/csr/don/2003_02_11/en, World Health Organization. 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Dis., 9, pp. 713-717; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; WHO collaborative multi-centre research project on severe acute respiratory syndrome (SARS) diagnosis (2003), http://www.who.int/csr/sars/project/en, World Health Organization. (accessed 9 May); Periris, J.S., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory (2003) N. Engl. J. Med., 348, pp. 1953-1966; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Siddell, S.G., Snijder, E.J., Coronaviruses, toroviruses, and arteriviruses (1998) Tropley and Wilson's Microbiology and Microbial Infections, pp. 463-484. , Mahy BWJ, Collier L. (eds) London: Edward Arnold; Wege, H., Siddell, S., ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Interpreting SARS test results (2003), http://www.cdc.gov/ncidod/sars/testresultsc.htm, Centers for Disease Control and Prevention. (accessed 9 May); Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Chiu, W.K., Cheung, P.C., Ng, K.L., Severe acute respiratory syndrome in children: Experience in a regional hospital in Hong Kong (2003) Pediatr. Crit. Care Med., 4, pp. 279-283; Hon, E.K., Leung, C.W., Cheng, W.T., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Rainer, T.H., Cameron, P.A., Smit, D., Evaluation of WHO criteria for identifying patients with severe acute respiratory syndrome out of hospital: Prospective observational study (2003) BMJ, 326, pp. 1354-1358; Fisher, D.A., Lim, T.K., Lim, Y.T., Atypical presentations of SARS (2003) Lancet, 361, p. 1740; Wong, R.S.M., Wu, A., To, K.F., Haematological manifestations in patients with severe acute respiratory syndrome: Retrospective analysis (2003) BMJ, 326, pp. 1358-1362; Wong, G.W.K., Hui, D.S.C., Severe acute respiratory syndrome (SARS): Epidemiology, diagnosis and treatment (2003) Thorax, 58, pp. 558-560; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Cinatl, J., Morgenstern, B., Bauer, G., Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus (2003) Lancet, 361, pp. 2045-2046; Seto, W.H., Tsang, D., Yung, R.W., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Hospital infection control guidance for severe acute respiratory syndrome (SARS) (2003), http://www.who.int/csr/sars/infectioncontrol/en, World Health Organization. (accessed 3 June); First data on stability and resistance of SARS coronavirus compiled by members of WHO laboratory network (2003), http://www.who.int/csr/sars/survival_2003_05_04/en, World Health Organization. (accessed 4 May)","Wong, G.W.K.; Department of Paediatrics, Prince of Wales Hospital, Chinese Univresity of Hong Kong, Shatin, New Territories, China; email: wingkinwong@cuhk.edu.hk",,"W.B. Saunders Ltd",15260542,,PRRAE,"14629957","English","Paediatr. Respir. Rev.",Article,"Final",Open Access,Scopus,2-s2.0-0345169965
"Lai M.D., Zhu Y.M., Gu X.M.","7401808601;7406072612;24334813600;","Severe acute respiratory syndrome",2003,"Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences","32","3",,"167","170",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4344608907&partnerID=40&md5=da8dad4ef2caec29e585f32567eda8db","Department of Pathology, College of Medical Sciences, Zhejiang University, Hangzhou, 310031, China","Lai, M.D., Department of Pathology, College of Medical Sciences, Zhejiang University, Hangzhou, 310031, China; Zhu, Y.M., Department of Pathology, College of Medical Sciences, Zhejiang University, Hangzhou, 310031, China; Gu, X.M., Department of Pathology, College of Medical Sciences, Zhejiang University, Hangzhou, 310031, China","OBJECTIVE: Severe acute respiratory syndrome(SARS), caused by SARS- associated coronavirus(SCV), is the first severe infectious disease in this century. SARS is pathologically characterized by interstitial exudative inflammation of lung with the formation of hyaline membrane in acute phase. Haemorrhagic inflammation exists in extrapulmonary organs. Clinical diagnosis is a dynamic process and includes the suspected case, probable case and definite case. Diagnostic standard of SARS will be revised with further understanding of the disease. Chinese term of SARS has been recommended in the paper.",,"human; nomenclature; pathology; review; severe acute respiratory syndrome; Humans; Severe Acute Respiratory Syndrome; Terminology",,"Lai, M.D.",,,10089292,,,"12881856","Chinese","Zhejiang Da Xue Xue Bao Yi Xue Ban",Review,"Final",,Scopus,2-s2.0-4344608907
"Onishchenko G.G., Vasil'ev N.T., Maksimov V.A., Markov V.I., Merkulov V.A., Pistsov M.N., Berezhnoi A.M., Syromiatnikova S.I., Zubov V.V.","57208582795;57196548270;7202539670;7201577228;7102815475;6506415100;7006401995;6506948700;7101887929;","Isolation and identification of the infective agent of severe acute respiratory syndrome (SARS) from a patient with atypical pneumonia [Vydelenie i identifikatsiia vozbuditelia tiazhelogo ostrogo respiratornogo sindroma (TORS) ot bol'nogo atipichnoi pnevmoniei.]",2003,"Zhurnal mikrobiologii, epidemiologii, i immunobiologii",,"5",,"109","112",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142694214&partnerID=40&md5=29964e5cdd457607d1f1571dc46cf99e","Ministry of Health of the Russian Federation, Moscow, Russian Federation","Onishchenko, G.G., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Vasil'ev, N.T., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Maksimov, V.A., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Markov, V.I., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Merkulov, V.A., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Pistsov, M.N., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Berezhnoi, A.M., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Syromiatnikova, S.I., Ministry of Health of the Russian Federation, Moscow, Russian Federation; Zubov, V.V., Ministry of Health of the Russian Federation, Moscow, Russian Federation","The virological, morphological, molecular biological and immunochemical study of the infective agent isolated from the patient with the symptoms of atypical pneumonia, hospitalized in the infectious department of the clinical hospital in Blagoveshchensk, was carried out. Thus the fact of the appearance of SARS virus on the territory of Russia was proved. The isolated infective agent, identified as coronavirus strain CoD, was partly characterized and deposited to the virus collection of the Center of Special Laboratory Diagnostics and Treatment of Quarantine and Exotic Infectious Diseases.",,"virus RNA; animal; article; blood; Cercopithecus; cytopathogenic effect; genetics; human; immunology; isolation and purification; male; pathology; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; ultrastructure; Vero cell; virology; virus pneumonia; Animals; Cercopithecus aethiops; Cytopathogenic Effect, Viral; Humans; Male; Pneumonia, Viral; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Vero Cells",,"Onishchenko, G.G.",,,03729311,,,"14565137","Russian","Zh. Mikrobiol. Epidemiol. Immunobiol.",Article,"Final",,Scopus,2-s2.0-2142694214
"Stadler K., Masignani V., Eickmann M., Becker S., Abrignani S., Klenk H.-D., Rappuoli R.","7003816836;6603149430;55913596100;55446677800;57206904667;24432172000;56976632300;","SARS — beginning to understand a new virus",2003,"Nature Reviews Microbiology","1","3",,"209","218",,208,"10.1038/nrmicro775","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1642509113&doi=10.1038%2fnrmicro775&partnerID=40&md5=00bc275089df5c9cb72ce65eaba4189e","IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy; Institute of Virology, University of Marburg, 35037 Marburg, Germany, Germany","Stadler, K., IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy; Masignani, V., IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy; Eickmann, M., Institute of Virology, University of Marburg, 35037 Marburg, Germany, Germany; Becker, S., Institute of Virology, University of Marburg, 35037 Marburg, Germany, Germany; Abrignani, S., IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy; Klenk, H.-D., Institute of Virology, University of Marburg, 35037 Marburg, Germany, Germany; Rappuoli, R., IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy","The 114-day epidemic of the severe acute respiratory syndrome (SARS) swept 29 countries, affected a reported 8, 098 people, left 774 patients dead and almost paralysed the Asian economy. Aggressive quarantine measures, possibly aided by rising summer temperatures, successfully terminated the first eruption of SARS and provided at least a temporal break, which allows us to consolidate what we have learned so far and plan for the future. Here, we review the genomics of the SARS coronavirus (SARS-CoV), its phylogeny, antigenic structure, immune response and potential therapeutic interventions should the SARS epidemic flare up again. © 2003 Nature Publishing Group.",,"virus protein; animal; classification; genetics; genomics; human; immunology; metabolism; phylogeny; physiology; review; SARS coronavirus; severe acute respiratory syndrome; virology; virus genome; Animals; Genome, Viral; Genomics; Humans; Phylogeny; SARS Virus; Severe Acute Respiratory Syndrome; Viral Proteins","Peiris, J.S.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Donnelly, C.A., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Hon, K.L., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Peiris, J.S.M., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Acute respiratory syndrome in China (2003), [online], cited 15 Oct; Summary of probable SARS cases with onset of illness from 1 November 2002 to 31 July 2003 (2003), [online], cited 15 Oct; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., A Nnvel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med, 348, pp. 1953-1966; Fouchier, R.A., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Kuiken, T., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Riley, S., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966; Lipsitch, M., Transmission dynamics and control of severe acute respiratory syndrome (2003) Science, 300, pp. 1966-1970; Guan, Y., Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China (2003) Science, 302, pp. 276-278; Normile, D., Enserink, M., SARS in China: Tracking the roots of a killer (2003) Science, 301, pp. 297-299; Severe acute respiratory syndrome (SARS) in Singapore (2003), http://www.who.int/csr/don/2003_09_24/en/, [online], (cited 15 Oct 2003); Enjuanes, L., (2002) Virus Taxonomy, pp. 835-849. , (eds Regenmortel, M. H. V. et all), Academic Press, New York; Marra, M.A., The genome sequence of the SARS- associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Zeng, F.Y., The complete genome sequence of severe acute respiratory syndrome coronavirus strain HKU-39849 (HK-39) (2003) Exp. Biol. Med., 228, pp. 866-873; Thiel, V., Mechanisms and enzymes involved in SARS coronavirus genome expression (2003) J. Gen. Virol., 84, pp. 2305-2315; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Viral replicase gene products suffice for coronavirus discontinuous transcription (2001) J. Virol., 75, pp. 6676-6681; Von Grotthuss, M., Wyrwicz, L.S., Rychlewski, L., MRNA cap-1 methyltransferase in the SARS genome (2003) Cell, 113, pp. 701-702; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Van Der Most, R.G., Spaan, W.J.M., (1995) The Coronaviridae, pp. 11-31. , (ed. Siddell, S. G., Plenum Press, New York; De Haan, C.A.M., Masters, P.S., Shen, X., Weiss, S., Rottier, P.J.M., The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host (2002) Virology, 296, pp. 177-189; Sola, I., Engineering the transmissible gastroenteritis virus genome as an expression vector inducing lactogenic immunity (2003) J. Virol., 77, pp. 4357-4369; Sarma, J.D., Scheen, E., Seo, S.H., Koval, M., Weiss, S.R., Enhanced green fluorescent protein expression may be used to monitor murine coronavirus spread in vitro and in the mouse central nervous system (2002) J. Neurovirol., 8, pp. 381-391; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3' end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J. Gen. Virol., 79, pp. 715-718; Lai, M.M., Holmes, K.V., (2001) Fields' Virology, pp. 1163-1185. , (eds Knipe, M. D. & Howley, M. P, Lippincott Williams & Wilkins, Philadelphia; Ruan, Y.J., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Snijder, E.J., Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage (2003) J. Mol. Biol., 331, pp. 991-1004; Anand, K., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra a-helical domain (2002) EMBO J, 21, pp. 3213-3224; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Krokhin, O., Mass Spectrometric Characterization of proteins from the SARS virus: A preliminary report (2003) Mol. Cell Proteomics, 2, pp. 346-356; Cavanagh, D., (1995) The Coronaviridae, pp. 73-113. , (ed. Siddell, S. G., Plenum Press, New York; Kuo, L., Godeke, G.J., Raamsman, M.J.B., Masters, P.S., Rottier, P.J.M., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Haijema, B.J., Volders, H., Rottier, P.J.M., Switching species tropism: An effective way to manipulate the feline coronavirus genome (2003) J. Virol., 77, pp. 4528-4538; Yu, X.J., Putative hAPN receptor binding sites in SARS- CoV spike protein (2003) Acta Pharmacol. Sin., 24, pp. 481-488; Tresnan, D.B., Holmes, K.V., Feline aminopeptidase N is a receptor for all group I coronaviruses (1998) Adv. Exp. Med. Biol., 440, pp. 69-75; Holmes, K.V., Zelus, B.D., Schickli, J.H., Weiss, S.R., Receptor specificity and receptor-induced conformational changes in mouse hepatitis virus spike glycoprotein (2001) Adv. Exp. Med. Biol., 494, pp. 173-181; Bosch, B.J., Van Der Zee, R., De Haan, C.A.M., Rottier, P.J.M., The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex (2003) J. Virol., 77, pp. 8801-8811; Bos, E.C., Luytjes, W., Spaan, W.J., The function of the spike protein of mouse hepatitis virus strain A59 can be studied on virus-like particles: Cleavage is not required for infectivity (1997) J. Virol., 71, pp. 9427-9433; Gombold, J.L., Hingley, S.T., Weiss, S.R., Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal (1993) J. Virol., 67, pp. 4504-4512; Taguchi, F., Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2 (1993) J. Virol., 67, pp. 1195-1202; Hingley, S.T., Leparc-Goffart, I., Seo, S.H., Tsai, J.C., Weiss, S.R., The virulence of mouse hepatitis virus strain A59 is not dependent on efficient spike protein cleavage and cell-to-cell fusion (2002) J. Neurovirol., 8, pp. 400-410; Steuben, R., Pfleiderera, M., Siddell, S., Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity (1993) J. Gen. Virol., 74, pp. 183-191; Cinatl, J., Treatment of SARS with human interferons (2003) Lancet, 362, pp. 293-294; Cinatl, J., Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus (2003) Lancet, 361, pp. 2045-2046; Olsen, C.W., A review of feline infectious peritonitis virus: Molecular biology, immunopathogenesis, clinical aspects, and vaccination (1993) Vet. Microbiol., 36, pp. 1-37; Saitou, N., Nei, M., The neighbor-joining method: A new method for reconstructing phylogenetic trees (1987) Mol. Biol. Evol., 4, pp. 406-425","Rappuoli, R.; IRIS, Chiron S.r.l., Via Fiorentina 1, Siena, 53100, Italy; email: rino_rappuoli@chiron.com",,,17401526,,,"15035025","English","Nat. Rev. Microbiol.",Article,"Final",,Scopus,2-s2.0-1642509113
"Sit S.C., Yau E.K., Lam Y.Y., Ng D.K., Fong N.C., Hui Y.W., Cheng W.F., Leung C.W., Chiu M.C.","8555268700;36750314300;7202563852;7201645744;7005458457;18339782900;36990979400;7402612619;7101866205;","A young infant with severe acute respiratory syndrome.",2003,"Pediatrics","112","4",,"","",,17,"10.1542/peds.112.4.e257","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141940747&doi=10.1542%2fpeds.112.4.e257&partnerID=40&md5=760c4223000a3048240b4ef72e56e3b8","Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong","Sit, S.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Yau, E.K., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Lam, Y.Y., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Ng, D.K., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Fong, N.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Hui, Y.W., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Cheng, W.F., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Leung, C.W., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Chiu, M.C., Department of Paediatrics and Adolescent Medicine, Princess Margaret Hospital, Kowloon, Hong Kong","Severe acute respiratory syndrome (SARS), a new contagious respiratory disease associated with a novel coronavirus, has spread worldwide and become a global health concern after its first outbreak in Guangdong Province of the People's Republic of China in November 2002. The clinical presentation and the radiologic, hematologic, biochemical, and microbiologic findings of a 56-day-old male infant with SARS are described. Some clinical and laboratory features are similar to those reported in adult and pediatric patients. However, this infant had a more severe clinical course as compared with the older children. This is the youngest patient with symptomatic SARS reported to date.",,"antiinfective agent; antivirus agent; lactate dehydrogenase; ribavirin; article; blood; case report; China; drug combination; human; infant; leukocytosis; male; neutrophil; newborn; onset age; prematurity; radiography; severe acute respiratory syndrome; Age of Onset; Anti-Bacterial Agents; Antiviral Agents; China; Drug Therapy, Combination; Humans; Infant; Infant, Newborn; Infant, Premature; L-Lactate Dehydrogenase; Leukocytosis; Male; Neutrophils; Ribavirin; Severe Acute Respiratory Syndrome",,"Sit, S.C.email: jscsit@hotmail.com",,,10984275,,,"14523208","English","Pediatrics",Article,"Final",Open Access,Scopus,2-s2.0-0141940747
"Lu X.Y., Guo L.Z.","7404839768;12786609600;","A novel coronavirus---SARS virus",2003,"Zhonghua yu fang yi xue za zhi [Chinese journal of preventive medicine]","37","4",,"281","283",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4544343153&partnerID=40&md5=d00e4cdcf70c3b3956cbffe9d075e5da","Center for Disease Control and Prevention, Atlanta, United States","Lu, X.Y., Center for Disease Control and Prevention, Atlanta, United States; Guo, L.Z., Center for Disease Control and Prevention, Atlanta, United States",[No abstract available],,"article; genetics; human; isolation and purification; SARS coronavirus; severe acute respiratory syndrome; virology; Humans; SARS Virus; Severe Acute Respiratory Syndrome",,"Lu, X.Y.",,,02539624,,,"15354324","Chinese","Zhonghua Yu Fang Yi Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-4544343153
"Taguchi F.","7103209890;","SARS coronavirus",2003,"Uirusu. Journal of virology","53","2",,"201","209",,,"10.2222/jsv.53.201","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2642543323&doi=10.2222%2fjsv.53.201&partnerID=40&md5=82acc02f0d2639b4601356b665fa5154","Msashi-Murayama, Laboratory of Respiratory Virol Diseases and SARS, Department of Virology III, National Institute of Infectious Diseases, 4-7-1 Gakuen, Tokyo, 208-0011., Japan","Taguchi, F., Msashi-Murayama, Laboratory of Respiratory Virol Diseases and SARS, Department of Virology III, National Institute of Infectious Diseases, 4-7-1 Gakuen, Tokyo, 208-0011., Japan",[No abstract available],,"virus protein; virus receptor; virus RNA; animal; biosynthesis; chemistry; classification; defective virus; genetic recombination; genetic transcription; genetics; human; mutation; pathogenicity; physiology; review; SARS coronavirus; severe acute respiratory syndrome; virology; virus genome; virus replication; Animals; Defective Viruses; Genome, Viral; Humans; Mutation; Receptors, Virus; Recombination, Genetic; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Transcription, Genetic; Viral Proteins; Virus Replication",,"Taguchi, F.",,,00426857,,,"15071959","Japanese","Uirusu",Review,"Final",Open Access,Scopus,2-s2.0-2642543323
"Gu S.Q., Zhu Q.R.","57203755333;57199825410;","Progresses in studies on SARS-associated coronavirus",2003,"Zhonghua er ke za zhi. Chinese journal of pediatrics","41","8",,"635","639",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342625907&partnerID=40&md5=108d02c8634151ec67545c80258d2ffb",,"Gu, S.Q.; Zhu, Q.R.",[No abstract available],,"China; electron microscopy; genetics; growth, development and aging; Hong Kong; human; review; SARS coronavirus; severe acute respiratory syndrome; ultrastructure; virology; China; Hong Kong; Humans; Microscopy, Electron; SARS Virus; Severe Acute Respiratory Syndrome",,"Gu, S.Q.",,,05781310,,,"14744401","Chinese","Zhonghua Er Ke Za Zhi",Review,"Final",,Scopus,2-s2.0-2342625907
"Narayanan K., Kim K.H., Makino S.","7101933409;7409323179;7403067550;","Characterization of N protein self-association in coronavirus ribonucleoprotein complexes",2003,"Virus Research","98","2",,"131","140",,34,"10.1016/j.virusres.2003.08.021","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345490757&doi=10.1016%2fj.virusres.2003.08.021&partnerID=40&md5=37e330fca48d275bc09e7f72ff7f5fbd","Dept. of Microbiology and Immunology, Univ. of TX Med. Branch at Galveston, Galveston, TX 77555-1019, United States; Department of Microbiology, Inst. of Molec. and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Department of Microbiology, College of Medicine, Ajou University, Suwon, Kyonggi, South Korea","Narayanan, K., Dept. of Microbiology and Immunology, Univ. of TX Med. Branch at Galveston, Galveston, TX 77555-1019, United States, Department of Microbiology, Inst. of Molec. and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States; Kim, K.H., Department of Microbiology, Inst. of Molec. and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States, Department of Microbiology, College of Medicine, Ajou University, Suwon, Kyonggi, South Korea; Makino, S., Dept. of Microbiology and Immunology, Univ. of TX Med. Branch at Galveston, Galveston, TX 77555-1019, United States, Department of Microbiology, Inst. of Molec. and Cellular Biology, University of Texas at Austin, Austin, TX 78712-1095, United States","Mouse hepatitis virus (MHV) nucleocapsid (N) protein binds to the large, single-stranded, positive-sense viral genomic RNA to form a helical nucleocapsid structure in mature virions. In addition N protein binds the intracellular form of the genomic RNA, all of the MHV subgenomic mRNAs, and expressed non-MHV RNA transcripts to form ribonucleoprotein (RNP) complexes in infected cells. Among the intracellular viral RNP complexes, only the genomic RNP complex is packaged into virus particles. The present study demonstrated that N protein in the MHV virion nucleocapsid and in the intracellular genome-length RNP complex that bound to viral envelope M protein was tightly self-associated such that its association was retained even after extensive RNase A-treatment of the RNP complexes. The RNase A-resistant tight N protein association in the virion nucleocapsid was not mediated by an intermolecular disulfide bridge between N proteins. In contrast, N protein association in the majority of the intracellular RNP complexes was susceptible to RNase A-treatment. Because the RNP complexes that specifically interact with the M protein are selectively packaged into MHV particles, the present data suggested that there was a distinct difference between N protein association in viral genomic RNP complexes that undergo packaging into virus particles and the subgenomic RNP complexes that are not packaged into MHV particles. © 2003 Elsevier B.V. All rights reserved.","Coronavirus; N protein; Ribonucleoprotein (RNP) complexes","disulfide; M protein; nucleocapsid protein; ribonuclease A; ribonucleoprotein; virus envelope protein; animal cell; animal model; article; controlled study; Coronavirus; mouse; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein protein interaction; virion; virus cell interaction; virus genome; virus nucleocapsid; virus particle; Coronavirus; Murine hepatitis virus","Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Biol., 494, pp. 577-582; Narayanan, K., Makino, S., Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging (2001) J. Virol., 75 (19), pp. 9059-9067; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) J. 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Cell Biol., 33 (2), pp. 281-293; Van Der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65 (6), pp. 3219-3226; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15 (8), pp. 2020-2028; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Makino, S.; Dept. of Microbiology and Immunology, Univ. of TX Med. Branch at Galveston, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,"Elsevier",01681702,,VIRED,"14659560","English","Virus Res.",Article,"Final",Open Access,Scopus,2-s2.0-0345490757
"Lee H.K.K., Tso E.Y.K., Chau T.N., Tsang O.T.Y., Choi K.W., Lai T.S.T.","57207324910;6603816466;7102000078;6602450830;37098634700;35559048100;","Asymptomatic Severe Acute Respiratory Syndrome-associated Coronavirus Infection [1]",2003,"Emerging Infectious Diseases","9","11",,"1491","1492",,31,"10.3201/eid0911.030401","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242292065&doi=10.3201%2feid0911.030401&partnerID=40&md5=6afe42aae078aa2ca080544f3013cb27","Princess Margaret Hospital, Hong Kong, Hong Kong; Infectious Diseases Team, Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Hong Kong, Hong Kong","Lee, H.K.K., Princess Margaret Hospital, Hong Kong, Hong Kong; Tso, E.Y.K., Princess Margaret Hospital, Hong Kong, Hong Kong; Chau, T.N., Princess Margaret Hospital, Hong Kong, Hong Kong; Tsang, O.T.Y., Princess Margaret Hospital, Hong Kong, Hong Kong; Choi, K.W., Princess Margaret Hospital, Hong Kong, Hong Kong; Lai, T.S.T., Princess Margaret Hospital, Hong Kong, Hong Kong, Infectious Diseases Team, Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Hong Kong, Hong Kong",[No abstract available],,"case report; clinical feature; Coronavirus; disease predisposition; enzyme linked immunosorbent assay; epidemiological data; health care personnel; Hong Kong; human; immunofluorescence; infection control; letter; nurse; physician; reverse transcription polymerase chain reaction; SARS coronavirus; serodiagnosis; severe acute respiratory syndrome; treatment outcome; virus pneumonia; world health organization","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; So, L.K.Y., Lau, A.C.W., Yam, L.Y.C., Cheung, T.M.T., Poon, E., Yung, R.W.H., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Vu, T.H., Cabau, J.F., Nguyen, N.T., Lenoi, M., SARS in northern Vietnam (2003) N Engl J Med, 348, p. 2035; Seto, W.H., Tsang, D., Yung, R.W.H., Ching, T.Y., Ng, T.K., Ho, M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520","Lai, T.S.T.; Infectious Diseases Team, Dept. of Medicine and Geriatrics, Princess Margaret Hospital, Hong Kong, Hong Kong; email: laist@ha.org.hk",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14725258","English","Emerg. Infect. Dis.",Letter,"Final",Open Access,Scopus,2-s2.0-0242292065
"Rose J.","35427522400;","Coronaviruses and SARS: Research needs for understanding the risks associated with transmission",2003,"Water 21",,"AUG.",,"21","24",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042473329&partnerID=40&md5=998167915fa2c19b30dba2de00bbb0ec",,"Rose, J.","A report on the severe acute respiratory syndrome (SARS) virus with a potential link to water and wastewater is presented. It has been reported that the SARS virus can be found in concentrations as high as 108 virus particles per ml in sputum in some patients after nine days. Decisions are being made at the global level by the World Health Organization and others that can affect a country's economy.",,"Disease control; Disinfection; Mutagenesis; Sewage; Infections; Viruses; virus; SARS coronavirus; Severe acute respiratory syndrome virus","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol., 78, pp. 81-83. , Anonymous; Belshe, R., (1984) Textbook of Human Virology, , PSG Publishing Company Inc; Cyranoski, D., Abbott, A., Virus detectives seek source of SARS in China's wild animals (2003) Nature, 423, p. 467; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, L.J., Anderson, R.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Drosten, C., Gunther, S., Presier, W., Van Der Werf, S., Brodt, H., Becker, S., Rabenau, H., Doerr, H.W., (2003) New England J. Med., pp. 1-10. , www.nejm.org, April 25 DROSTEN; Fields, B.N., Knipe, D.M., (1986) Fundamental Virology, , Raven Press; Haas, C.H., Rose, J.B., Gerba, C.P., (1999) Quantitiative Microbial Risk Assessment, , John Wiley and Sons, NY, NY; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc Soc Exp Biol Med 1966, 121, pp. 190-193; Hoshino, Y., Scott, F.W., Coronavirus-like particles present in the faeces of normal cats (1980) Arch. Virol., 63, pp. 147-152; Ijaz, M.K., Brunner, A.H., Sattar, S.A., Nair, R.C., Johnson-Lussenburg, C.M., Survival characteristics of human coronavirus 229E (1985) J. Gen. Virol., 66, pp. 2743-2748; Kapikian, A.Z., The coronaviruses (1975) Dev Biol Stand, 28, pp. 42-64; Knobler, R.L., Lampert, P.W., Oldstone, M.B.A., Virus persistence and recurring demyelination produced by a temperature-sensitive mutant of MHV-4 (1982) Nature (Land.), 298, pp. 279-280; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) New England J. Med., 348 (20), pp. 1947-1958; Lipstich, M., Cohen, T., Cooper, B., Robins, J.M., Ma, S., James, L., Gopalakrishna, G., Murray, M., Transmission dynamics and control of severe acute respiratory syndrome (2003) Science, 300, pp. 1966-1970; McIntosh, K., Coronaviruses: A comparative review (1974) Curr Top Microbiol 1974, 63, pp. 85-129; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Law, K.I., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) The Lancet, 361, pp. 1767-1772; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in canada (2003) New England J. Med., , www.nejm.org, April 25 LOW1-LOW11; Ruan, Y., Wei, C.L., Ee, L.A., Vega, V.B., Thoreau, H., Yun, S.T.S., Chia, J., Liu, E.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolated and common mutations associated with putative origins of infection (2003) The Lancet, 361, pp. 1779-1785; Saknimit, M., Inatsuki, I., Sugiyama, Y., Yagami, K., Virucidal efficacy of physico-chemical treatments against coronaviruses and parvoviruses of laboratory animals (1988) Jikken Dobutsu Jul, 37 (3), pp. 341-345; Sattar, S.A., Springthorpe, V.S., Karim, Y., Loro, P., Chemical disinfection of non-porous inanimate surfaces experimentally contaminated with four human pathogenic viruses (1989) Epidemiol Infect., 102, pp. 493-505; Sizun, J., Yu, M.W., Talbot, P.J., Survival of human coronaviruses 229E and OC43 in suspension and after drying on surfaces: A possible source of hospital-acquired infections (2000) J. Hasp. Infect., 46 (1), pp. 55-60; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common-cold virus in organ cultures (1965) Br Med J 1965, 1, pp. 1467-1470",,,"IWA Publishing",15619508,,WATEC,,"English","Water 21",Article,"Final",,Scopus,2-s2.0-0042473329
"Reich B.","7006146821;","SARS (severe acute respiratory syndrome). From which animal does this Coronavirus originate? [SARS (schweres akutes respiratorisches Syndrom). Von welchem Tier stammt das Coronavirus?]",2003,"Pneumologie (Stuttgart, Germany)","57","5",,"247","249",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042020055&partnerID=40&md5=87794f698041ce9eb544ba84af318a77",,"Reich, B.",[No abstract available],,"animal; article; disease transmission; Germany; human; isolation and purification; SARS coronavirus; severe acute respiratory syndrome; ultrastructure; zoonosis; Animals; Germany; Humans; SARS Virus; Severe Acute Respiratory Syndrome; Zoonoses",,"Reich, B.",,,09348387,,,"12825583","German","Pneumologie",Article,"Final",,Scopus,2-s2.0-0042020055
"Holmes K.V.","7201657724;","SARS coronavirus: A new challenge for prevention and therapy",2003,"Journal of Clinical Investigation","111","11",,"1605","1609",,140,"10.1172/JCI18819","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038819069&doi=10.1172%2fJCI18819&partnerID=40&md5=8ea83b23a0848ae78e84307cb699d208","Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States","Holmes, K.V., Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States",[No abstract available],,"corticosteroid; monoclonal antibody; neutralizing antibody; virus vaccine; epidemic; fatality; high risk population; human; infection risk; nonhuman; nucleotide sequence; pathophysiology; prevalence; priority journal; review; SARS coronavirus; severe acute respiratory syndrome; symptomatology; viral contamination; virus genome; virus mutation; virus replication; virus shedding; virus transmission; virus virulence; animal; biological model; genetics; infection control; pathogenicity; phylogeny; physiology; severe acute respiratory syndrome; Animals; Humans; Infection Control; Models, Biological; Phylogeny; SARS Virus; Severe Acute Respiratory Syndrome","(2003) Severe Acute Respiratory Syndrome (SARS): Multi-country Outbreak, , http//www.who.int/csr/don/2003_03-16/en/; Preliminary clinical description of severe acute respiratory syndrome (2003) MMWR Morb. Mortal. Wkly. Rep., 52, pp. 255-256; WHO recommended measures for persons undertaking international travel from areas affected by severe acute respiratory syndrome (SARS) (2003) Wkly. Epidemiol. Rec., 78, pp. 97-120; Gerberding, J.L., Faster. But fast enough? Responding to the epidemic of severe acute respiratory syndrome (2003) N. Engl. J. Med., , In press; Lee, N., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., , In press; Poutanen, S.M., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., , In press; Tsang, K.W., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., , In press; Peiris, J.S.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Chan-Yeung, M., Yu, W.C., Outbreak of severe acute respiratory syndrome in Hong Kong Special Administrative Region: Case report (2003) BMJ, 326, pp. 850-852; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., , In press; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., , In press; Fouchier, R.A.M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Holmes, K.V., Coronaviruses (2001) Fields' Virology, pp. 1187-1203. , D. Knipe, et al., editors. Lippincott Williams & Wilkins. Philadelphia, Pennsylvania, USA; Bradburne, A.F., Tyrrell, D.A.J., Coronaviruses of man (1971) Prog. Med. Virol., 13, pp. 373-403; Chilvers, M.A., The effects of coronavirus on human nasal ciliated respiratory epithelium (2001) Eur. Respir. J., 18, pp. 965-970; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Kapikian, A.Z., The coronaviruses (1975) Dev. Biol. Stand., 28, pp. 42-64; Battaglia, M., Passarani, N., Di Matteo, A., Gerna, G., Human enteric coronaviruses: Further characterization and immunoblotting of viral proteins (1987) J. Infect. Dis., 155, pp. 140-143; Macnaughton, M.R., Davies, H.A., Human enteric coronaviruses: Brief review (1981) Arch. Virol., 70, pp. 301-313; Lai, M.M.C., Holmes, K.V., Coronaviridae and their replication (2001) Fields' Virology, pp. 1163-1185. , D. Knipe, et al., editors. Lippincott Williams & Wilkins. Philadelphia, Pennsylvania, USA; Herrewegh, A.A., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; De Arriba, M.L., Carvajal, A., Pozo, J., Rubio, P., Mucosal and systemic isotype-specific antibody responses and protection in conventional pigs exposed to virulent or attenuated porcine epidemic diarrhoea virus (2002) Vet. Immunol. Immunopathol., 85, pp. 85-97; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, , doi:10.1126/science1085952; Marra, M.A., The genome sequence of the SARS-associated coronavirus (2003) Science, , doi:10.1126/science1085953; Matsuyama, S., Taguchi, F., Receptor-induced conformational changes of murine coronavirus spike protein (2002) J. Virol., 76, pp. 11819-11826; Zelus, B.D., Schickli, J.H., Blau, D.M., Weiss, S.R., Holmes, K.V., Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37C either by soluble murine CEACAM1 receptors or by pH 8 (2003) J. Virol., 77, pp. 830-840; Lewicki, D.N., Gallagher, T.M., Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors (2002) J. Biol. Chem., 277, pp. 19727-19734; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185; Denison, M.R., The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis (1999) J. Virol., 73, pp. 6862-6871; Hegyi, A., Ziebuhr, J., Conservation of substrate specificities among coronavirus main proteases (2002) J. Gen. Virol., 83, pp. 595-599; Gosert, R., Kanjanahaluethai, A., Egger, D., Bienz, K., Baker, S.C., RNA replication of mouse hepatitis virus takes place at double-membrane vesicles (2002) J. Virol., 76, pp. 3697-3708; Sawicki, D., Wang, T., Sawicki, S., The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus (2001) J. Gen. Virol., 82, pp. 385-396; Sethna, P.B., Brian, D.A., Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes (1997) J. Virol., 71, pp. 7744-7749; (1996) Fundamental Virology, p. 544. , B.N. Fields, D.M. Knipe, and P.M. Howley, editors. 3rd edition. Lippincott-Raven. Philadelphia, Pennsylvania, USA/New York, New York, USA","Holmes, K.V.; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Avenue, Denver, CO 80262, United States; email: Kathryn.holmes@uchsc.edu",,"The American Society for Clinical Investigation",00219738,,JCINA,"12782660","English","J. Clin. Invest.",Review,"Final",Open Access,Scopus,2-s2.0-0038819069
[No author name available],[No author id available],"From the Centers for Disease Control and Prevention. Severe Acute Respiratory Syndrome (SARS) and coronavirus testing--United States, 2003.",2003,"JAMA : the journal of the American Medical Association","289","17",,"2203","2206",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038701036&partnerID=40&md5=05e7761bcbbba0fccd25bcb3e4fa57e5",,"",[No abstract available],,"adult; article; case report; China; communicable disease; Coronavirus; diagnosis, measurement and analysis; female; Hong Kong; human; infection control; isolation and purification; male; middle aged; pregnancy; pregnancy complication; risk factor; SARS coronavirus; severe acute respiratory syndrome; Singapore; travel; United States; virology; Adult; China; Communicable Diseases, Emerging; Coronavirus; Female; Hong Kong; Humans; Infection Control; Laboratory Techniques and Procedures; Male; Middle Aged; Pregnancy; Pregnancy Complications, Infectious; Risk Factors; SARS Virus; Severe Acute Respiratory Syndrome; Singapore; Travel; United States",,,,,00987484,,,"12734120","English","JAMA",Article,"Final",,Scopus,2-s2.0-0038701036
[No author name available],[No author id available],"Novel coronavirus associated with SARS outbreak.",2003,"Gastroenterology","124","7",,"1724","1725",,,"10.1016/S0016-5085(03)00658-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038680237&doi=10.1016%2fS0016-5085%2803%2900658-9&partnerID=40&md5=0ed162594ec2963af4f8154354e0a988",,"",[No abstract available],,"virus RNA; article; human; isolation and purification; SARS coronavirus; severe acute respiratory syndrome; Humans; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome",,,,,00165085,,,"12806600","English","Gastroenterology",Article,"Final",Open Access,Scopus,2-s2.0-0038680237
"Parry J.","24605791400;","Hong Kong and US scientists believe illness is a coronavirus.",2003,"BMJ (Clinical research ed.)","326","7392",,"727","",,2,"10.1136/bmj.326.7392.727","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037420535&doi=10.1136%2fbmj.326.7392.727&partnerID=40&md5=51e134c95053d3b247919d62e5fa05c7",,"Parry, J.",[No abstract available],,"article; communicable disease; epidemic; Hong Kong; human; severe acute respiratory syndrome; virology; virus infection; Communicable Diseases, Emerging; Coronavirus Infections; Disease Outbreaks; Hong Kong; Humans; Severe Acute Respiratory Syndrome",,"Parry, J.",,,14685833,,,"12676826","English","BMJ",Article,"Final",Open Access,Scopus,2-s2.0-0037420535
"Kuiken T., Fouchier R., Rimmelzwaan G., Osterhaus A.","26643529400;7006060466;7005416180;55533604400;","Emerging viral infections in a rapidly changing world",2003,"Current Opinion in Biotechnology","14","6",,"641","646",,58,"10.1016/j.copbio.2003.10.010","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344255702&doi=10.1016%2fj.copbio.2003.10.010&partnerID=40&md5=0ba73e77be5a0ab06dbdf3111f84e9e7","Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands","Kuiken, T., Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands; Fouchier, R., Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands; Rimmelzwaan, G., Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands; Osterhaus, A., Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands","Emerging viral infections in both humans and animals have been reported with increased frequency in recent years. Recent advances have been made in our knowledge of some of these, including severe acute respiratory syndrome-associated coronavirus, influenza A virus, human metapneumovirus, West Nile virus and Ebola virus. Research efforts to mitigate their effects have concentrated on improved surveillance and diagnostic capabilities, as well as on the development of vaccines and antiviral agents. More attention needs to be given to the identification of the underlying causes for the emergence of infectious diseases, which are often related to anthropogenic social and environmental changes. Addressing these factors might help to decrease the rate of emergence of infectious diseases and allow the transition to a more sustainable society.",,"antivirus agent; live vaccine; recombinant vaccine; virus vaccine; disease association; disease transmission; Ebola virus; environmental change; health survey; human; infection; Influenza virus A; nonhuman; polymerase chain reaction; priority journal; review; SARS coronavirus; severe acute respiratory syndrome; sociology; virus infection; West Nile flavivirus; Animalia; Coronavirus; Ebola virus; Flavivirus; Human metapneumovirus; Influenza A virus; Influenza virus; Metapneumovirus; SARS coronavirus; West Nile virus","McMichael, A.J., (2001) Human Frontiers, Environments and Disease: Past Patterns, Uncertain Futures, , Cambridge, UK: Cambridge University Press; (2003) WHO Issues a Global Alert about Cases of Atypical Pneumonia. WHO Press Release, , http://www.who.int/csr/sars/archive/2003_03_12, 12 March; World Health Organization: Summary of Probable SARS Cases with Onset of Illness from 1 November 2002 to 31 July 2003, , http:/www.who.int/csr/sars/country/table2003_09_23/en; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Cheung, M.T., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325. , This is the first publication to suggest a previously unknown coronavirus as the cause of SARS. Development of serological and molecular biological tests specific for this virus allowed further investigation to confirm the etiology; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Lim, W., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Günther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Fouchier, R.A., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Chan, S.Y., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , Together with Rota et al. [8•], these papers provide the first publication of the genome of SARS-CoV. Phylogenetic analysis shows that this virus belongs to a new, fourth group of coronaviruses. The genome sequence data allowed the rapid development of PCR-based assays to detect the virus and distinguish it from other coronaviruses; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Peñaranda, S., Chen, M.H., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , See [7•]; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240. , In this study, SARS-CoV is confirmed as the primary cause of SARS by reproducing similar histopathological changes, including characteristic syncytia, in experimentally infected macaques. Knowledge of the etiology allowed the scientific community to focus its attention on this virus for the development of diagnostic tests, vaccine production and antiviral therapy; Kuiken, T., Fouchier, R.A., Schutten, M., Rimmelzwaan, G.F., Van Amerongen, G., Van Riel, D., Laman, J.D., Lim, W., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270. , SARS-CoV infection was diagnosed in 75% of 436 SARS patients from six countries, and the replication of SARS in experimentally infected macaques was shown in detail. These results strengthen the conclusion of Fouchier et al. [9••]. Furthermore, the demonstrated tropism of SARS-CoV for alveolar epithelial cells may explain the pulmonary fibrosis observed later in the disease; Peiris, J.S., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Law, K.I., Chan, C.S., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772. , In this unique prospective study of 75 SARS patients, the SARS-CoV load from the respiratory tract peaked at 10 days after onset of symptoms, while pulmonary disease worsened in the second week after onset. Therefore, lung damage during that phase cannot be explained by uncontrolled viral replication; Guan, Y., Zheng, B.J., He, Y.Q., Liu, X.L., Zhuang, Z.X., Cheung, C.L., Luo, S.W., G.Yj, Isolation and characterization of viruses related to the SARS coronavirus from animals in Southern China (2003) Science, , Published online 4 September 2003; 10.1126/science.1087139; http://www.promedmail.org, SARS - worldwide: (173) Singapore, laboratory confirmation. 14th September 2003; Archive number 20030914.2320; Gambaryan, A., Webster, R., Matrosovich, M., Differences between influenza virus receptors on target cells of duck and chicken (2002) Arch. Virol., 147, pp. 1197-1208; Centers for Disease Control and Prevention: Update: Influenza activity - United States and worldwide, 2002 - 03 season, and composition of the 2003 - 04 influenza vaccine (2003) Morb Mortal Wkly Rep, 52, pp. 516-521; Li, K.S., Xu, K.M., Peiris, J.S., Poon, L.L., Yu, K.Z., Yuen, K.Y., Shortridge, K.F., Guan, Y., Characterization of H9 subtype influenza viruses from the ducks of Southern China: A candidate for the next influenza pandemic in humans? (2003) J. Virol., 77, pp. 6988-6994. , This study shows that there is easy two-way transmission of influenza viruses between different types of poultry. These findings indicate that the gene pool for influenza viruses is larger and more dynamic than previously thought; Van Den Hoogen, B.G., De Jong, J.C., Groen, J., Kuiken, T., De Groot, R., Fouchier, R.A.M., Osterhaus, A.D.M.E., A newly discovered human pneumovirus isolated from young children with respiratory tract disease (2001) Nat. Med., 7, pp. 719-724. , In this seminal paper, a previously unknown human paramyxovirus associated with human respiratory disease is identified and named human metapneumovirus. The data on virus diagnosis provided in this paper allowed its subsequent detection in many other parts of the world; Van Den Hoogen, B.G., Bestebroer, T.M., Osterhaus, A.D.M.E., Fouchier, R.A.M., Analysis of the genomic sequence of a human metapneumovirus (2002) Virology, 295, pp. 119-132. , Analysis of the sequences of all hMPV open reading frames, intergenic sequences, and partial sequences of the genomic termini show a high percentage of sequence identity between hMPV and avian pneumovirus, which belongs to the genus Metapneumovirus. These data indicate that hMPV should be classified as the first mammalian member of the genus Metapneumovirus; Van Den Hoogen, B.G., Doornum Gjj, V., Fockens, J.C., Cornelissen, J.J., Wep, B., De Groot, R., Adme, O., Ram, F., Prevalence and clinical symptoms of human metapneumovirus (hMPV) in hospitalized patients J Infect Dis, 2003. , in press; Boivin, G., Abed, Y., Pelletier, G., Ruel, L., Moisan, D., Côté, S., Peret, T.C.T., Anderson, L.J., Virological features and clinical manifestations associated with human metapneumovirus: A new paramyxovirus responsible for acute respiratory-tract infections in all age groups (2002) J. Infect. Dis., 186, pp. 1330-1334. , The newly discovered hMPV was found not only in children, but also in older patients. The important finding was that, whereas immunocompentent adults generally presented with a flu-like syndrome or a common cold, hMPV infection in the very young, the very old, and immunocompromised patients was associated with severe lower respiratory tract disease; Peret, T.C.T., Boivin, G., Li, Y., Couillard, M., Humphrey, C., Osterhaus, A.D.M.E., Erdman, D.D., Anderson, L.J., Characterization of human metapneumoviruses isolated from patients in North America (2002) J. Infect. Dis., 185, pp. 1660-1663; Petersen, L.R., Marfin, A.A., Gubler, D.J., West Nile virus (2003) JAMA, 290, pp. 524-528; Campbell, G.L., Marfin, A.A., Lanciotti, R.S., Gubler, D.J., West Nile virus (2002) Lancet Infect. Dis., 2, pp. 519-529. , This is a good contemporary review of different aspects of West Nile virus infection, with an emphasis on disease in humans; Lanciotti, R.S., Ebel, G.D., Deubel, V., Kerst, A.J., Murri, S., Meyer, R., Bowen, M., Crabtree, M.B., Complete genome sequences and phylogenetic analysis of West Nile virus strains isolated from the United States, Europe, and the Middle East (2002) Virology, 298, pp. 96-105; (2003) Dead Birds Submitted for West Nile Virus Diagnosis by Health Region Canada As of September 09, , http://dsol-smed.hc-sc.gc.ca/wnv/map600_e.phtml; (2003) West Nile Virus in the United States As of September 9, , http://www.cdc.gov/ncidod/dvbid/westnile/surv&control03Maps.htm; Loroño-Pino, M.A., Blitvich, B.J., Fárfan-Ale, J.A., Puerto, F.I., Blanco, J.M., Marlenee, N.L., Rosado-Paredes, E.P., Calisher, C.H., Serologic evidence of West Nile virus infection in horses, Yucatan State, Mexico (2003) Emerg. Infect. Dis., 9, pp. 857-859; Blitvich, B.J., Fernandez-Salas, I., Contreras-Cordero, J.F., Marlenee, N.L., Gonzalez-Rojas, J.I., Komar, N., Gubler, D.J., Beaty, B.J., Serologic evidence of West Nile virus infection in horses, Coahuila State, Mexico (2003) Emerg. Infect. Dis., 9, pp. 853-856; Dupuis, A.P., Marra, P.P., Kramer, L.D., Serologic evidence of West Nile virus transmission, Jamaica, West Indies (2003) Emerg Infect. Dis., 9, pp. 860-863; Peterson, A.T., Vieglais, D.A., Andreasen, J.K., Migratory birds modeled as critical transport agents for West Nile virus in North America (2003) Vector Borne Zoonotic Dis., 3, pp. 27-37; McLean, R.G., Ubico, S.R., Bourne, D., Komar, N., West Nile virus in livestock and wildlife (2002) Curr. Top. Microbiol. Immunol., 267, pp. 271-308. , This is a good overview of natural and experimental WNV infection of wildlife and domestic animals. The use of wild birds, sentinel chickens and horses for surveillance of WNV infection is also reviewed; West Nile Virus, , http://www.hc-sc.gc.ca/english/westnile/index.html; West Nile Virus, , http://www.cdc.gov/ncidod/dvbid/westnile/index.htm; Okware, S.I., Omaswa, F.G., Zaramba, S., Opio, A., Lutwama, J.J., Kamugisha, J., Rwaguma, E.B., Lamunu, M., An outbreak of Ebola in Uganda (2002) Trop. Med. Int. Health, 7, pp. 1068-1075; Walsh, P.D., Abernethy, K.A., Bermejo, M., Beyers, R., De Wachter, P., Akou, M.E., Huijbregts, B., Kilbourn, A.M., Catastrophic ape decline in western equatorial Africa (2003) Nature, 422, pp. 611-614. , Major declines in the numbers of gorillas and chimpanzees between 1983 and 2000 were attributed to commercial hunting and Ebola virus infection, based on the relationship between ape distribution and the distance to Gabon's major urban centers and to human Ebola outbreak sites. This study, performed under difficult field conditions, indicates that action is needed urgently in terms of law enforcement, protected area management, and Ebola prevention to prevent the extinction of these ape species in the wild; Colebunders, R., Borchert, M., Ebola haemorrhagic fever - A review (2000) J. Infect., 40, pp. 16-20; Blitvich, B.J., Marlenee, N.L., Hall, R.A., Calisher, C.H., Bowen, R.A., Roehrig, J.T., Komar, N., Beaty, B.J., Epitope-blocking enzyme-linked immunosorbent assays for the detection of serum antibodies to West Nile virus in multiple avian species (2003) J. Clin. Microbiol., 41, pp. 1041-1047; Sullivan, N.J., Geisbert, T.W., Geisbert, J.B., Xu, L., Yang, Z.Y., Roederer, M., Koup, R.A., Nabel, G.J., Accelerated vaccination for Ebola virus haemorrhagic fever in non-human primates (2003) Nature, 424, pp. 681-684. , Effective immunization of cynomolgus macaques against a lethal Ebola virus challenge was reduced from six months to four weeks by use of a single dose of an adenoviral vector encoding the Ebola glycoprotein. The efficacy of this single vaccine injection may help to control outbreaks in both humans and great apes; Cinatl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H., Doerr, H.W., Treatment of SARS with human interferons (2003) Lancet, 362, pp. 293-294; Selected Indicators of Food and Agriculture Development in Asia-Pacific Region 1991-2001, , http://www.fao.org/DOCREP/005/AC832E/ac832e00.htm; http://statline.cbs.nl/StatWeb, Statistics Netherlands; Alexander, D.J., Orthomyxovirus infection (1993) Virus Infections of Birds, pp. 287-316. , Edited by McFerran JB, McNulty MS. Amsterdam: Elsevier Science Publishers; Bee, M., Haagmans, B.L., Kuiken, T., Ram, F., Rimmelzwaan, G.F., Van Amerongen, G., Jsm, P., Adme, O., Experimental SARS coronavirus infection of cats and ferrets (2003) Nature, , in press","Osterhaus, A.; Department of Virology, Erasmus Medical Center, PO Box 1738, 3000 DR Rotterdam, Netherlands; email: a.osterhaus@erasmusmc.nl",,"Elsevier Ltd",09581669,,CUOBE,"14662395","English","Curr. Opin. Biotechnol.",Review,"Final",,Scopus,2-s2.0-0344255702
"Kwan B.C.-H., Leung C.-B., Szeto C.-C., Wang A.Y.-M., Li P.K.-T.","16060862800;16750769500;35495407200;13606226000;25928016800;","Severe Acute Respiratory Syndrome in a Hemodialysis Patient",2003,"American Journal of Kidney Diseases","42","5",,"1069","1074",,10,"10.1016/j.ajkd.2003.07.022","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142250922&doi=10.1016%2fj.ajkd.2003.07.022&partnerID=40&md5=140f7aa70a6a9b94ff4abf1246d6cec1","Dept. of Medicine and Therapeutics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, Hong Kong","Kwan, B.C.-H.; Leung, C.-B.; Szeto, C.-C.; Wang, A.Y.-M.; Li, P.K.-T., Dept. of Medicine and Therapeutics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, Hong Kong","Severe acute respiratory syndrome (SARS) is a highly infective disease caused by a newly identified coronavirus. We described the clinical course of the first long-term hemodialysis patient who developed SARS in the literature, and our experience in performing hemodialysis for this patient. Such patients may present with a less typical clinical picture, making diagnosis difficult. In this patient, the course of disease and duration of viral shedding was apparently prolonged, thus highlighting the need for increased infection control. Despite worsening the anemia in renal failure patients by causing hemolysis, ribavirin is well tolerated after dosage adjustment. Difficulties of diagnosis, infection control, and treatment of SARS in renal failure patients are discussed in this report. © 2003 by the National Kidney Foundation, Inc.","Atypical pneumonia; Coronavirus; Renal failure; Severe acute respiratory syndrome (SARS)","antibiotic agent; antivirus agent; calcium carbonate; cefotaxime; corticosteroid; erythropoietin; ferrous sulfate; folic acid; hemoglobin; labetalol; levofloxacin; methylprednisolone; nifedipine; prednisolone; ribavirin; acute disease; adult; anemia; article; blood transfusion; case report; China; Coronavirus; coughing; dialysis; disease severity; dyspnea; hemodialysis; human; infection control; kidney failure; male; polymerase chain reaction; respiratory tract infection; serology; severe acute respiratory syndrome; systemic lupus erythematosus; thorax radiography; travel; virus detection; virus infection","Lee, N.L., Hui, D.S., Wu, A.K., A major outbreak of severe respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/, May 1; So, L.K., Lau, A.C., Yam, L.Y., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; (2003) Hospital Infection Control Guidance for Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/infectioncontrol/en/, April 24; (2003) SARS Bulletin, , http://www.info.gov.hk/dh/diseases/ap/eng/bulletin0512.pdf, May 12; Okuda, K., Hayashi, H., Yokozeki, K., Kobayashi, S., Kashima, T., Irie, Y., Acute hepatitis C among renal failure patients on chronic haemodialysis (1998) J Gastroenterol Hepatol, 13, pp. 62-67; (2003) Management of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/management/en/, April 11; Aronoff, G.R., Brier, M., Erbeck, K.M., Ouseph, R., Drug dosing in dialysis patients (2000) Dialysis and Transplantation - A Companion to Brenner & Rector's The Kidney, pp. 358-372. , Owen WF, Pereira BJ, Sayegh MH (eds). Philadelphia, PA, Saunders; Bruchfeld, A., Stahle, L., Andersson, J., Schvarcz, R., Ribavirin treatment in dialysis patients with chronic hepatitis C virus infection - A pilot study (2001) J Viral Hepatol, 8, pp. 287-292; Kramer, T.H., Gaar, G.G., Ray, C.G., Minnich, L., Copeland, J.G., Connor, J.D., Hemodialysis clearance of intravenously administered Ribavirin (1990) Antimicrob Agents Chemother, 34, pp. 489-490; Hoenich, N.A., Katopodis, K.P., Clinical characterization of a new polymeric membrane for use in renal replacement therapy (2002) Biomaterials, 23, pp. 3853-3858; Svensson, J.O., Bruchfeld, A., Schvarcz, R., Stahle, L., Determination of Ribavirin in serum using highly selective solid-phase extraction and high-performance liquid chromatography (2000) Ther Drug Monit, 22, pp. 215-218; Peiris, J.S., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772","Li, P.K.-T.; Dept. of Medicine and Therapeutics, Prince of Wales Hospital, Chinese University of Hong Kong, Shatin, Hong Kong; email: philipli@cuhk.edu.hk",,"W.B. Saunders",02726386,,AJKDD,"14582051","English","Am. J. Kidney Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0142250922
"Liu G., Hu S., Hu Y., Chen P., Yin J., Wen J., Wang J., Lin L., Liu J., You B., Yin Y., Li S., Wang H., Ren Y., Ji J., Zhao X., Sun Y., Zhang X., Fang J., Wang J., Liu S., Yu J., Zhu H., Yang H.","18134311200;7404287173;12775742400;57199133296;7401693537;49664305200;8272121600;55676528000;55705826000;57199280134;36124437600;57207248052;56608115200;57198461840;36983919500;8236324400;55506885800;54923054800;7402966086;57200022156;7409459608;8679878600;35265383000;34573719100;","The C-terminal portion of the nucleocapsid protein demonstrates SARS-CoV antigenicity.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"193","197",,7,"10.1016/S1672-0229(03)01024-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13744261436&doi=10.1016%2fS1672-0229%2803%2901024-6&partnerID=40&md5=8d7651ae6194c191c790a7d0f7ff304d","College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China","Liu, G., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Hu, S., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Hu, Y., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Chen, P., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Yin, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Wen, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Wang, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Lin, L., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Liu, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; You, B., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Yin, Y., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Li, S., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Wang, H., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Ren, Y., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Ji, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Zhao, X., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Sun, Y., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Zhang, X., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Fang, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Wang, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Liu, S., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Yu, J., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Zhu, H., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China; Yang, H., College of Life Sciences, Hebei Agricultural University, Baoding, 071001, China","In order to develop clinical diagnostic tools for rapid detection of the SARS-CoV (severe acute respiratory syndrome-associated coronavirus) and to identify candidate proteins for vaccine development, the C-terminal portion of the nucleocapsid (NC) gene was amplified using RT-PCR from the SARS-CoV genome, cloned into a yeast expression vector (pEGH), and expressed as a glutathione S-transferase (GST) and Hisx6 double-tagged fusion protein under the control of an inducible promoter. Western analysis on the purified protein confirmed the expression and purification of the NC fusion proteins from yeast. To determine its antigenicity, the fusion protein was challenged with serum samples from SARS patients and normal controls. The NC fusion protein demonstrated high antigenicity with high specificity, and therefore, it should have great potential in designing clinical diagnostic tools and provide useful information for vaccine development.",,"hybrid protein; nucleocapsid protein; virus antigen; article; enzyme linked immunosorbent assay; gene vector; genetics; human; immunology; isolation and purification; metabolism; molecular cloning; SARS coronavirus; virus genome; yeast; Antigens, Viral; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Genetic Vectors; Genome, Viral; Humans; Nucleocapsid Proteins; Recombinant Fusion Proteins; SARS Virus; Yeasts",,"Liu, G.",,,16720229,,,"15629031","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-13744261436
"Whitby N., Whitby M.","7801575966;35977511300;","SARS: a new infectious disease for a new century.",2003,"Australian family physician","32","10",,"779","783",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642303778&partnerID=40&md5=d3f3425e29291439f23e1630ed115225","Carindale Medical Clinic, Brisbane, Queensland.","Whitby, N., Carindale Medical Clinic, Brisbane, Queensland.; Whitby, M., Carindale Medical Clinic, Brisbane, Queensland.","BACKGROUND: A new infectious disease swept the world in early 2003, causing restrictions on international travel and economic downturn in affected countries. OBJECTIVE: This article aims to provide an overview of the epidemic of severe acute respiratory syndrome (SARS). DISCUSSION: SARS is caused by a new coronavirus thought to be of animal origin. The virus induces symptoms of atypical pneumonia, clinically indistinguishable from similar syndromes. The severity is such that a 15% mortality rate has been reported. No treatment has yet been identified as reliably successful. Transmission is by droplet spread, requiring close contact. Stringent infection control precautions in health care institutions, broad isolation measures in affected communities and international surveillance with barrier restrictions to travel have led to termination of the epidemic. As of July 11, 2003, 8437 people in 32 countries have been affected, with 813 deaths reported.",,"Australia; communicable disease; female; forecasting; health; human; infection control; isolation and purification; male; review; risk assessment; SARS coronavirus; severe acute respiratory syndrome; standard; survival rate; travel; world health organization; Australia; Communicable Disease Control; Communicable Diseases, Emerging; Female; Forecasting; Humans; Male; Risk Assessment; SARS Virus; Severe Acute Respiratory Syndrome; Survival Rate; Travel; World Health; World Health Organization",,"Whitby, N.email: noelaw@carindalemedical.com.au",,,03008495,,,"2003168881","English","Aust Fam Physician",Review,"Final",,Scopus,2-s2.0-0642303778
"Savarino A., Boelaert J.R., Cassone A., Majori G., Cauda R.","55792833800;7006517306;7101897223;7006326755;7006356239;","Effects of chloroquine on viral infections: An old drug against today's diseases?",2003,"Lancet Infectious Diseases","3","11",,"722","727",,201,"10.1016/S1473-3099(03)00806-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242355070&doi=10.1016%2fS1473-3099%2803%2900806-5&partnerID=40&md5=f2d51653f89d89646016dbc098b944cc","Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Rome, Italy; Unit of Infectious Diseases, AZ Sint-Jan, Brugge, Belgium; Department of Infectious Diseases, Istituto Superiore di Sanità, Rome, Italy; Department of Parasitology, Istituto Superiore di Sanità, Rome, Italy; Laboratory of Viral Immunology, Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Largo Agostino Gemelli 8, I-00168 Rome, Italy","Savarino, A., Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Rome, Italy, Laboratory of Viral Immunology, Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Largo Agostino Gemelli 8, I-00168 Rome, Italy; Boelaert, J.R., Unit of Infectious Diseases, AZ Sint-Jan, Brugge, Belgium; Cassone, A., Department of Infectious Diseases, Istituto Superiore di Sanità, Rome, Italy; Majori, G., Department of Parasitology, Istituto Superiore di Sanità, Rome, Italy; Cauda, R., Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Rome, Italy","Chloroquine is a 9-aminoquinoline known since 1934. Apart from its well-known antimalarial effects, the drug has interesting biochemical properties that might be applied against some viral infections. Chloroquine exerts direct antiviral effects, inhibiting pH-dependent steps of the replication of several viruses including members of the flaviviruses, retroviruses, and coronaviruses. Its best-studied effects are those against HIV replication, which are being tested in clinical trials. Moreover, chloroquine has immunomodulatory effects, suppressing the production/release of tumour necrosis factor α and interleukin 6, which mediate the inflammatory complications of several viral diseases. We review the available information on the effects of chloroquine on viral infections, raising the question of whether this old drug may experience a revival in the clinical management of viral diseases such as AIDS and severe acute respiratory syndrome, which afflict mankind in the era of globalisation.",,"8 aminoquinoline derivative; antiretrovirus agent; chloroquine; didanosine; hydroxychloroquine; hydroxyurea; interleukin 6; tumor necrosis factor alpha; zidovudine; acquired immune deficiency syndrome; antimalarial activity; antiviral activity; biochemistry; clinical trial; Coronavirus; cytokine production; drug effect; Flavivirus; human; Human immunodeficiency virus; Human immunodeficiency virus infection; immunomodulation; nonhuman; pH; priority journal; respiratory tract disease; Retrovirus; review; risk benefit analysis; severe acute respiratory syndrome; side effect; virus infection; virus replication","Canadian Consensus Conference on hydroxychloroquine (2000) J Rheumatol, 27, pp. 2919-2921; Savarino, A., Gennero, L., Sperber, K., Boelaert, J.R., The anti-HIV-1 activity of chloroquine (2001) J Clin Virol, 20, pp. 131-135; Boelaert, J.R., Piette, J., Sperber, K., The potential place of chloroquine in the treatment of HIV-1-infected patients (2001) J Clin Virol, 20, pp. 137-140; Ohkuma, S., Poole, B., Cytoplasmic vacuolation of mouse peritoneal macrophages and the uptake into lysosomes of weakly basic substances (1981) J Cell Biol, 90, pp. 656-664; Pescarmona, G.P., Morra, E., Aldieri, E., Ghigo, D., Bosia, A., Movements of vesicles in eukaryotic cells: Role of intravesicle protons as a fuel and modulation of their concentration by drugs or metabolic changes (1998) MRS Bull, 489, pp. 212-217; Vezmar, M., Georges, E., Reversal of MRP-mediated doxorubicin resistance with quinoline-based drugs (2000) Biochem Pharmacol, 59, pp. 1245-1252; Vezmar, M., Georges, E., Direct binding of chloroquine to the multidrug resistance protein (MRP): Possible role for MRP in chloroquine drug transport and resistance in tumor cells (1998) Biochem Pharmacol, 56, pp. 733-742; Byrd, T.F., Horwitz, M.A., Chloroquine inhibits the intracellular multiplication of Legionella pneumophila by limiting the availability of iron. 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Van den Borne, B.E., Dijkmans, B.A., De Rooij, H.H., Le Cessie, S., Verweij, C.L., Chloroquine and hydroxychloroquine equally affect tumor necrosis factor-α interleukin 6 and interferon-γ production by peripheral blood mononuclear cells (1997) J Rheumatol, 24, pp. 55-60; Karres, I., Kremer, J.-P., Dietl, I., Steckholzer, U., Jochum, M., Ertel, W., Chloroquine inhibits proinflammatory cytokine release into human whole blood (1998) Am J Physiol, 274, pp. R1059-R1064; Picot, S., Peyron, F., Donadille, A., Vuillez, J.-P., Barbe, G., Ambroise-Thomas, P., Chloroquine-induced inhibition of the production of TNF, but not of IL-6, is affected by disruption of iron metabolism (1993) Immunology, 80, pp. 127-133; Weber, S.M., Levitz, S.M., Chloroquine interferes with lipopolysaccharide-induced TNF-α gene expression by a nonlysosomotropic mechanism (2000) J Immunol, 165, pp. 1534-1540; Jeong, J.-Y., Choi, J.W., Jeon, K.-I., Jue, D.-M., Chloroquine decreases cell-surface expression of tumour necrosis factor receptors in human histiocytic U-937 cells (2002) Immunol, 105, pp. 83-91; Nooteboom, A., Hendriks, T., Otteholler, I., Van der Linden, C.J., Permeability characteristics of human endothelial monolayers seeded on different extracellular matrix proteins (2000) Mediators Inflamm, 9, pp. 235-241; Bernstein, H.N., Ocular safety of hydroxychloroquine (1991) Ann Ophthalmol, 23, pp. 292-296; Bernstein, H.N., Ophthalmologic considerations and testing in patients receiving long-term antimalarial therapy (1983) Am J Med, 75, pp. 25-34; Herman, K., Leys, A., Spileers, W., (Hydroxy)-chloroquine retinal toxicity: Two case reports and safety guidelines (2002) Bull Soc Beige Ophtalmol, 284, pp. 21-29; Klinger, G., Morad, Y., Westall, C.A., Ocular toxicity and antenatal exposure to chloroquine or hydroxychloroquine for rheumatic diseases (2001) Lancet, 358, pp. 813-814; Sperber, K., Kalb, T.H., Stecher, V.J., Banerjee, R., Mayer, L., Inhibition of human immunodeficiency virus type 1 replication by hydroxychloroquine in T cells and monocytes (1993) AIDS Res Hum Retroviruses, 9, pp. 91-98; Pardridge, W.M., Yang, J., Diagne, A., Chloroquine inhibits HIV-1 replication in human peripheral blood lymphocytes (1998) Immunol Lett, 64, pp. 45-47; Savarino, A., Gennero, L., Chen, H.C., Anti-HIV effects of chloroquine: Mechanisms of inhibition and spectrum of activity (2001) AIDS, 15, pp. 2221-2229; Sperber, K., Louie, M., Kraus, T., Hydroxychloroquine treatment of patients with human immunodeficiency virus type 1 (1995) Clin Ther, 17, pp. 622-636; Sperber, K., Chiang, G., Chen, H., Comparison of hydroxychloroquine with zidovudine in asymptomatic patients infected with HIV-1 (1997) Clin Ther, 19, pp. 913-923; Debiaggi, M., Bruno, R., Sacchi, P., Filice, G., Antiviral activity of chloroquine against HIV-1 strains resistant to antiretroviral drugs Antiviral Res, , in press; Chiang, G., Sassaroli, M., Louie, M., Chen, H., Stecher, V.J., Sperber, K., Inhibition of HIV-1 replication by hydroxychloroquine: Mechanism of action and comparison with zidovudine (1996) Clin Ther, 18, pp. 1080-1092; Boelaert, J.R., Sperber, K., Antiretroviral therapy (1998) Lancet, 352, pp. 1224-1225; Boelaert, J.R., Sperber, K., Piette, J., Chloroquine exerts an additive in vitro anti-HIV-1 effect, when combined to zidovudine and hydroxyurea (2001) Biochem Pharmacol, 61, pp. 1531-1535; Paton, N.I., Aboulhab, J., Karim, F., Hydroxychloroquine, hydroxycarbamide, and didanosine as economic treatment for HIV-1 (2002) Lancet, 359, pp. 1667-1668; Boelaert, J.R., Dom, G.M., Huitema, A.D., Beijnen, J.H., Lange, J.M., The boosting of didanosine by allopurinol permits a halving of the didanosine dosage (2002) AIDS, 16, pp. 2221-2223; Mofenson, L.M., McIntyre, J.A., Advances and research directions in the prevention of mother-to-child HIV-1 transmission (2000) Lancet, 355, pp. 2237-2244; Boelaert, J.R., Yaro, S., Augustijns, P., Chloroquine accumulates in breast milk cells. Potential impact as adjuvant to antiretroviral prophylaxis for postnatal mother-to-child transmission of HIV-1 (2001) AIDS, 15, pp. 2205-2206; DeCock, K.M., Fowler, M.G., Mercier, E., Prevention of mother-to-child transmission of HIV-1 in resource-poor countries: Translating research into policy and practice (2000) JAMA, 283, pp. 1175-1182; Corbett, E.L., Steketee, R.W., Ter Kuile, P.O., Latif, A.S., Kamali, A., Hayes, R.J., HIV-1/AIDS and the control of other infectious diseases in Africa (2002) Lancet, 359, pp. 2177-2187; Clerici, M., Burro, S., Lukwiya, M., Immune activation in Africa is environmentally driven and is associated with upregulation of CCR5 (2000) AIDS, 14, pp. 2083-2092; Bentwich, Z., Maartens, G., Torten, D., Lal, A.A., Lal, R.B., Concurrent infections and HIV pathogenesis (2000) AIDS, 14, pp. 2071-2081; Montano, M.A., Nixon, C.P., Ndung'u, T., Elevated tumor necrosis factor-α activation of human immunodeficiency virus subtype I in southern Africa is associated with an NF-kB enhancer gain-of-function (2000) J Infect Dis, 181, pp. 76-81; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; So, L.K., Lau, A.C., Yam, L.Y., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Blau, D., Holmes, K., Human Coronavirus HCoV-229E enters susceptible cells via the endocytic pathway (2001) The Nidoviruses, Coronaviruses and Arteriviruses, pp. 193-197. , Lavi E (ed). New York: Kluwer; Nauwynck, H.J., Duan, X., Favoreel, H.W., Van Oostveldt, P., Pensaert, M.B., Entry of porcine reproductive and respiratory syndrome virus into porcine alveolar macrophages via receptor-mediated endocytosis (1999) J Gen Virol, 80 (PART 2), pp. 297-305; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Shanley, T.P., Warner, R.L., Ward, P.A., The role of cytokines and adhesion molecules in the development of inflammatory injury (1995) Mol Med Today, 1, pp. 40-45; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Van Reeth, K., Van Gucht, S., Pensaert, M., In vivo studies on cytokine involvement during acute viral respiratory disease of swine: Troublesome but rewarding (2002) Vet Immunol Immunopathol, 87, pp. 161-168; Fenollar, F., Fournier, P.E., Carrieri, M.P., Habib, G., Messana, T., Raoult, D., Risks factors and prevention of Q rever endocarditis (2001) Clin Infect Dis, 33, pp. 312-316; Ladner, J., Leroy, V., Karita, E., Van de Perre, P., Dabis, F., Malaria, HIV and pregnancy (2003) AIDS, 17, pp. 275-356; Savarino, A., Bottarel, F., Malavasi, F., Dianzani, U., Role of CD38 in HIV-1 infection: An epiphenomenon of T-cell activation or an active player in virus/host interactions? (2000) AIDS, 14, pp. 1079-1089","Savarino, A.; Laboratory of Viral Immunology, Department of Infectious Diseases, Universita Cattolica del Sacro Cuore, Largo Agostino Gemelli 8, I-00168 Rome, Italy; email: asavarino@medscape.com",,"Lancet Publishing Group",14733099,,LIDAB,"14592603","English","Lancet Infect. Dis.",Note,"Final",,Scopus,2-s2.0-0242355070
"Ivan A., Azoicai D.","7103361311;7003615092;","SARS (Severe Acute Respiratory Syndrome). Emergent transmissible disease [SARS (severe acute respiratory syndrome). Maladie transmisibila emergenta.]",2003,"Revista medico-chirurgicala a Societaţii de Medici ş̧i Naturaliş̧ti din Iaş̧i","107","2",,"250","252",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042712437&partnerID=40&md5=eea2cc334f9e79733aa14ccd48386ad4","Catedra de Epidemiologie, Facultatea de Medicina, Universitatea de Medicina şi Farmacie Gr.T. Popa Iaşi., Romania","Ivan, A., Catedra de Epidemiologie, Facultatea de Medicina, Universitatea de Medicina şi Farmacie Gr.T. Popa Iaşi., Romania; Azoicai, D., Catedra de Epidemiologie, Facultatea de Medicina, Universitatea de Medicina şi Farmacie Gr.T. Popa Iaşi., Romania","Of the reemergent transmissible diseases of the past decades, SARS is probably not the last to express the alterations occurring in the relationships of the human being with its global ecosystem. The life of contemporary man is characterized, among others, by a huge thirst for traveling, for varied reasons, consequence of the globalization process. SARS virus, mutant belonging to Coronaviridae, occurred in one of the most densely populated areas of the world. There are two main moments marking the reemergence and evolution of SARS: firstly, the onset of the epidemic in China in November 2002 followed by the worldwide spread of the epidemiological process, and secondly the discovery of SARS virus as a mutant of coronaviruses in March-April 2003 in USA, Canada, and Hong Kong. The possibilities of general and special prevention, and particularly vaccine prevention are likely to bring this disease under control.",,"animal; Canada; China; communicable disease; disease transmission; epidemic; Hong Kong; human; review; risk factor; severe acute respiratory syndrome; zoonosis; Animals; Canada; China; Communicable Diseases, Emerging; Disease Outbreaks; Hong Kong; Humans; Risk Factors; Severe Acute Respiratory Syndrome; Zoonoses",,"Ivan, A.",,,03008738,,,"14755924","Romanian; Moldavian; Moldovan","Rev Med Chir Soc Med Nat Iasi",Review,"Final",,Scopus,2-s2.0-3042712437
"Ostrowski S., Van Vuuren M., Lenain D.M., Durand A.","7006413777;7004572625;6506871144;7102442320;","A serologic survey of wild felids from central west Saudi Arabia",2003,"Journal of Wildlife Diseases","39","3",,"696","701",,38,"10.7589/0090-3558-39.3.696","https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042563656&doi=10.7589%2f0090-3558-39.3.696&partnerID=40&md5=38f6d5dcdbba08c35be4e1e3652af555","Natl. Commn. Wildlife Conserv./Devt., National Wildlife Research Center, PO Box 1086, Taif, Saudi Arabia; Dept. of Veterinary Trop. Diseases, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort 0110, South Africa","Ostrowski, S., Natl. Commn. Wildlife Conserv./Devt., National Wildlife Research Center, PO Box 1086, Taif, Saudi Arabia; Van Vuuren, M., Dept. of Veterinary Trop. Diseases, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort 0110, South Africa; Lenain, D.M., Natl. Commn. Wildlife Conserv./Devt., National Wildlife Research Center, PO Box 1086, Taif, Saudi Arabia; Durand, A., Dept. of Veterinary Trop. Diseases, Faculty of Veterinary Science, University of Pretoria, Private Bag X04, Onderstepoort 0110, South Africa","Forty-five wildcats (Felis silvestris), 17 sand cats (Felis margarita), and 17 feral domestic cats were captured in central west Saudi Arabia, between May 1998 and April 2000, with the aim to assess their exposure to feline immunodeficiency virus/punia lentivirus (FIV/PLV), feline leukaemia virus (FeLV), feline herpesvirus (FHV-1), feline calicivirus (FCV), feline coronavirus (FCoV), and feline panleukopenia virus (FPLV). Serologic prevalence in wildcats, sand cats, and feral domestic cats were respectively: 6%, 0%, 8% for FIV\PLV; 3%, 8%, 0% for FeLV; 5%, 0%, 15% for FHV-1; 25%, 0%, 39% for FCV; 10%, 0%, 0% for FCoV; and 5%, 0%, 8% for FPLV. We recorded the first case of FeLV antigenemia in a wild sand cat. Positive results to FIV/PLV in wildcats and feral cats confirmed the occurrence of a feline lentivirus in the sampled population. © Wildlife Disease Association 2003.","Feline calicivirus; Feline coronavirus; Feline herpesvirus; Feline lentivirus; Feline panleukopenia virus; Felis catus; Felis margarita; Felis silvestris; Feral cat; Sand cat; Wildcat","Caliciviridae; Coronavirus; Felidae; Feline calicivirus; Feline coronavirus; Feline herpesvirus 1; Feline immunodeficiency virus; Feline lentiviruses; Feline panleukopenia virus; Felis; Felis catus; Felis margarita; Felis silvestris; Herpesviridae; Lentivirus; Margarites","Artois, M., Redmond, M., Viral diseases as a threat to free-living wild cats (Felis silvestris) in continental Europe (1994) The Veterinary Record, 134, pp. 651-652; Barr, M.C., Pough, M.B., Jacobson, R.H., Scott, F.W., Comparison and interpretation of diagnostic tests for feline immunodeficiency virus infection (1991) Journal of the American Veterinary Medicine Association, 199, pp. 1377-1381; Daniels, M.J., Golder, M.C., Jarrett, O., MacDonald, D.W., Feline viruses in wildcats from Scotland (1999) Journal of Wildlife Disease, 35, pp. 121-124; Essop, M.F., Mda, N., Flamand, J., Harley, E.H., Mitochondrial DNA comparisons between the African wild cat, European wild cat and the domestic cat (1997) South African Journal of Wildlife Research, 27, pp. 71-72; Fromont, E., Artois, M., Pontier, D., Cat population structure and circulation of feline viruses (1996) Acta Oecologica, 17, pp. 609-620; Fromont, E., Sager, A., Leger, F., Bourguemestre, F., Jouquelet, E., Stahl, P., Pontier, D., Artois, M., Prevalence and pathogenicity of retroviruses in wildcats in France (2000) The Veterinary Record, 146, pp. 317-319; Harrison, D.L., Bates, P.J.J., (1991) The Mammals of Arabia, p. 354. , Harrison Zoological Museum Publication, 2nd Edition, London, UK; Horzinek, M.C., Vaccination: A philosophical view (1999) Advances in Veterinary Medicine, 41, pp. 1-6; Jessup, D.A., Pettan, K.C., Lowenstine, L.J., Pedersen, N.C., Feline leukemia virus infection and renal spirochetosis in a free-ranging cougar (Felis concolor) (1993) Journal of Zoo and Wildlife Medicine, 24, pp. 73-79; Kania, S.A., Kennedy, M.A., Potgieter, L.N.D., Serologic reactivity using conserved envelope epitopes in feline lentivirus-infected felids (1997) Journal of Veterinary Diagnostic Investigation, 9, pp. 125-129; Kennedy-Stoskopf, S., Emerging viral infections in large cats (1999) Zoo and Wild Animal Medicine, pp. 401-410. , Current Therapy 4, M. E. Fowler and R. E. Miller (eds.). W.B. Saunders Co., Philadelphia, Pennsylvania; Kingdon, J., (1990) Arabian Mammals, p. 279. , Academic Press, London, UK; Lenain, D.M., (2000) Fox Populations of a Protected Area in Saudi Arabia, p. 192. , M.Ph. Thesis, University of Hertfordshire, Herts, UK; MacDonald, D.W., Kerby, G., Passanisi, W.C., Wild cats and feral cats (1991) Great Cats, pp. 162-169. , J. Seidensticker and S. Lumpkin (eds.). Merehurst, London, UK; Mcorist, S., Boid, R., Jones, T.W., Easterbee, N., Hubbard, A.L., Jarrett, O., Some viral and protozoal diseases in the European wildcat (Felis silvestris) (1991) Journal of Wildlife Disease, 27, pp. 693-696; Mendelssohn, H., Felids in Israel (1989) Cat News, 10, pp. 2-4; Nowell, K., Jackson, P., Wild cats: Status, survey and conservation plan (1996) International Union for the Conservation of Nature, p. 382. , (Editors). Gland, Switzerland; Olfermann, E.W., (1996) Population Ecology of the Rueppell's Fox (Vulpes Rueppelli, Schinz 1825) and the Red Fox (Vulpes Vulpes, Linnaeus 1758) in a Semi-Desert Environment in Saudi Arabia, p. 291. , Ph.D. Thesis, University of Bielefeld, Bielefeld, Germany; Osofsky, S.A., Hirsch, K.J., Zuckerman, E.E., Hardy, W.D., Feline lentivirus and feline oncovirus status of free-ranging lions (Panthera leo), leopards (Panthera pardus) and cheetahs (Acinonyx jubatus) in Botswana: A regional perspective (1996) Journal of Zoo and Wildlife Medicine, 27, pp. 453-467; Paul-Murphy, J., Work, T., Hunter, D., Mcfie, E., Flelline, D., Serologic survey and serum biochemical reference ranges of the free-ranging mountain lion (Felis concolor) in California (1994) Journal of Wildlife Diseases, 30, pp. 205-215; Roelke, M.E., Forrester, D.J., Jacobson, E.R., Kollias, G.V., Scott, F.W., Barr, M.C., Evermann, J.F., Pirtle, E.C., Seroprevalence of infectious disease agents in free-ranging Florida panthers (Felis concolor coryi) (1993) Journal of Wildlife Diseases, 29, pp. 36-49; Roelke-Parker, M.E., Munson, L., Packer, C., Kock, R., Cleaveland, S., Carpentfr, M., O'Brien, S.J., Apple, M.J.C., A canine distemper virus epidemic in Serengeti lions (Panthera leo) (1996) Nature, 379, pp. 441-445; Thrushfield, M., (1995) Veterinary Epidemiology, p. 479. , Blackwell Science, Oxford, UK; Van Vuuren, M., Serological studies of bovine respiratory syncitial virus in feedlot cattle in South Africa (1990) Journal of the South African Veterinary Association, 61, pp. 168-169","Ostrowski, S.; Natl. Commn. Wildlife Conserv./Devt., National Wildlife Research Center, PO Box 1086, Taif, Saudi Arabia; email: ostrowski@nwrc-sa.org",,"Wildlife Disease Association, Inc.",00903558,,,"14567233","English","J. Wildl. Dis.",Article,"Final",,Scopus,2-s2.0-3042563656
"Oh V., Lim T.K.","7004458562;7401710185;","Singapore's experience of SARS",2003,"Clinical Medicine","3","5",,"448","451",,12,"10.7861/clinmedicine.3-5-448","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142260380&doi=10.7861%2fclinmedicine.3-5-448&partnerID=40&md5=20c977869c9d8d46ba817f0ed7d3b08c","Department of Medicine, National University Hospital, Singapore, Singapore; Division of Respiratory Medicine, National University Hospital, Singapore, Singapore; Department of Medicine, National University Hospital, 5 Lower Kent Ridge Road, Singapore 119074, Singapore","Oh, V., Department of Medicine, National University Hospital, Singapore, Singapore; Lim, T.K., Division of Respiratory Medicine, National University Hospital, Singapore, Singapore, Department of Medicine, National University Hospital, 5 Lower Kent Ridge Road, Singapore 119074, Singapore","The coronavirus that causes severe acute respiratory syndrome (SARS) is transmitted mainly via respiratory droplets. Typical presenting symptoms are akin to those of ordinary pneumonia. Young patients start with fever, chills, malaise, headache, or myalgia; cough and dyspnoea follow. Older persons and those taking corticosteroids may have neither fever nor respiratory symptoms. Exceptional suspicion is needed to identify SARS early in the illness. During an outbreak, even patients with low suspicion of SARS should be promptly isolated, and all contacts quarantined. Health workers need training in the use of appropriate barriers against droplets and other body fluids. Any fever cluster in patients or carers requires immediate action: discharges, visits, and transfers between wards and hospitals should be stopped. Halting hospital admissions and ten-day quarantine of suspected cases create wide buffer zones. To counter a possible resurgence of SARS, a system of prepared isolation and quarantine facilities is important.","Coronavirus; Health workers; Personal protective equipment; Quarantine; Severe acute respiratory syndrome (SARS); Surveillance; Visitors","acute respiratory tract disease; Coronavirus; experience; health care personnel; hospital admission; hospital discharge; infection control; patient care; patient transport; review; SARS coronavirus; severe acute respiratory syndrome; Singapore; virus transmission","Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) Morb Mortal Wkly Rep, 52, pp. 226-228; (2003) Cumulative Number of Reported Probable Cases of SARS, , www.who.int/csr/sars/country/2003_06_20/en/, June, Word Health Organization; Lipsitch, M., Cohen, T., Cooper, B., Robins, J.M., Transmission dynamics and control of severe acute respiratory syndrome (2003) Science, 300, pp. 1966-1970; Riley, S., Fraser, C., Donnelly, C.A., Ghani, A.C., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966; (2003) Update 84 - Can SARS be Eradicated or Eliminated?, , www.who.int/csr/don/2003-06-19/en/print.html, June; (2003) Preliminary Clinical Description of Severe Acute Respiratory Syndrome, , www.who.int/csr/sars/clinical/en/; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., Chan, P., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Hsu, L.Y., Lee, C.C., Green, J.A., Ang, B., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9, pp. 713-717; Rainer, T.H., Cameron, P.A., Smit, D., Ong, K.L., Evaluation of WHO criteria for identifying patients with severe acute respiratory syndrome out of hospital: Prospective observational study (2003) BMJ, 326, pp. 1354-1358; Fisher, D., Lim, T.K., Lim, Y.T., Singh, K.S., Tambyah, P.A., Atypical presentations of SARS (2003) Lancet, 361, p. 1740; Wong, R.S., Wu, A., To, K.F., Lee, N., Haematological manifestations in patients with severe acute respiratory syndrome: Retrospective analysis (2003) BMJ, 326, pp. 1358-1362; (2003) Management of Severe Acute Respiratory Syndrome (SARS), , www.who.int/csr/sars/management/en/, April; Seto, W.H., Tsang, D., Yung, R.W., Ching, T.Y., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Cluster of severe acute respiratory syndrome cases among protected health-care workers - Toronto, Canada, April 2003 (2003) Morb Mortal Wkly Rep, 52, pp. 433-436","Lim, T.K.; Department of Medicine, National University Hospital, 5 Lower Kent Ridge Road, Singapore 119074, Singapore",,"Royal College of Physicians",14702118,,CMLUB,"14601945","English","Clin. Med.",Review,"Final",,Scopus,2-s2.0-0142260380
"Mackie P.L.","8295357900;","The classification of viruses infecting the respiratory tract",2003,"Paediatric Respiratory Reviews","4","2",,"84","90",,45,"10.1016/S1526-0542(03)00031-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038617774&doi=10.1016%2fS1526-0542%2803%2900031-9&partnerID=40&md5=8d3fc4cca055e1efbe123f2985a1f4a5","Department of Microbiology, Yorkhill NHS Trust, Glasgow G3 8SJ, United Kingdom","Mackie, P.L., Department of Microbiology, Yorkhill NHS Trust, Glasgow G3 8SJ, United Kingdom","Following the boom in respiratory virology in the 1960s, species of rhinoviruses, coronaviruses, enteroviruses, adenoviruses, parainfluenza viruses and respiratory syncytial virus were added to influenza and measles viruses as causes of respiratory tract infection. In restricted patient groups, such as the immunocompromised, members of the family of herpesviruses including herpes simplex, cytomegalovirus, varicella-zoster virus, Epstein-Barr virus and human herpes virus 6 have also been associated with respiratory disease. This list of pathogens was extended last year with the discovery of a novel virus, the human metapneumovirus. More than 200 antigenically distinct viruses have been documented as causes of sporadic or epidemic respiratory infections in infants, children and adults. However, this varied and diverse group can be divided among six distinct families. Understanding some of the basic biology of these families gives an insight into possible strategies for diagnosis, control and therapy. © 2003 Elsevier Science Ltd. All rights reserved.","Classification; DNA viruses; Respiratory tract infections; RNA viruses","antivirus agent; Adenovirus; Coronavirus; Cytomegalovirus; Enterovirus; Epstein Barr virus; Herpes simplex virus; Herpes virus; human; Human herpesvirus 6; immune deficiency; Influenza virus; Measles virus; Metapneumovirus; Orthomyxovirus; Parainfluenza virus; Paramyxovirus; Picornavirus; priority journal; Respiratory syncytial pneumovirus; respiratory tract infection; review; Rhinovirus; subspecies; Varicella zoster virus; virology; virus classification; virus infection","http://www.ncbi.nlm.nih.gov/ICTV/, The International Committee on the Taxonomy of Viruses website; Collins, P.I., Chanock, R.M., Murphy, B.R., Respiratory syncytial virus (2001) Fields Virology, 1, pp. 1443-1486. , Knipe DM, Howley PM (eds) 4th edn, Philadelphia: Lippincott Williams & Wilkins; Chanock, R.M., Murphy, B.R., Collins, P.L., Parainfluenza viruses (2001) Fields Virology, 1, pp. 1341-1379. , Knipe DM, Howley PM (eds) 4th edn, Philadelphia: Lippincott Williams & Wilkins; Johnson, P.R., Collins, P.L., The fusion glycoproteins of human respiratory syncytial virus of subgroups A and B: Sequence conservation provides a structural basis for antigenic relatedness (1988) J. Gen. Virol., 69, pp. 2623-2628; Cane, P.A., Matthews, D.A., Pringle, C.R., Identification of variable domains of the attachment (G) protein of subgroup A respiratory syncytial viruses (1991) J. Gen. Virol., 72, pp. 2091-2096; Cane, P.A., Pringle, C.R., Molecular epidemiology of respiratory syncytial virus: Rapid identification of subgroup A lineages (1992) J. Virol. Methods, 40, pp. 297-306; Martinello, R.A., Chen, M.D., Weibel, C., Kahn, J.S., Correlation between respiratory syncytial virus genotype and severity of illness (2002) J. Infect. Dis., 186, pp. 839-842; Murphy, B.R., Collins, P.L., Live-attenuated virus vaccines for respiratory syncytial virus and parainfluenza viruses: Applications of reverse genetics (2002) J. Clin. Invest., 110, pp. 21-27; Collins, P.L., Rational design of live-attenuated recombinant vaccine virus for human respiratory syncytial virus by reverse genetics (1999) Virology, 54, pp. 423-451; van den Hoogen, B.G., de Jong, J.C., Groen, J., A newly discovered human pneumovirus isolated from young children with respiratory tract disease (2001) Nat. Med., 7, pp. 719-724; van den Hoogen, B.G., Bestebroer, T.M., Osterhaus, D.M.E., Fouchier, R.A.M., Analysis of the genomic sequence of a human metapneumovirus (2002) Virology, 295, pp. 119-132; Peret, T.C.T., Boivin, G., Yan, L., Characterization of human metapneumovirus isolated from patients in North America (2002) J. Infect. Dis., 185, pp. 1660-1663; Potter, C.W., Influenza (2000) Principles and Practice of Clinical Virology, pp. 253-277. , Zuckerman AJ, Banatvala JE, Pattison, JMR (eds) 4th edn. John Wiley, Chichester; Horimoto, T., Kawaoka, Y., Pandemic threat posed by avian influenza A viruses (2001) Clin. Microbiol. Rev., 14, pp. 129-149; Peiris, M., Yuen, K.Y., Leung, C.W., Human infection with influenza H9N2 (1999) Lancet, 354, pp. 916-917; Monto, A.S., Robinson, D.P., Herlocher, M.L., Zanamivir in the prevention of influenza among healthy adults (1999) JAMA, 282, pp. 31-35; Treanor, J.J., Hayden, F.G., Vrooman, P.S., Efficacy and safety of oral neuraminidase inhibitor oseltamivir in treating acute influenza (2000) JAMA, 283, pp. 1016-1024; Pillay, D., Developments in the treatment of acute viral infections: What's the problem? (2002) Curr. Opin. Infect. Dis., 15, pp. 591-592; Minor, P.D., Morgan-Capner, P., Muir, P., Enteroviruses (2000) Principles and Practice of Clinical Virology, pp. 428-434. , Zuckerman AJ, Banatvala JE, Pattison, JMR (eds) 4th edn. John Wiley, Chichester; Chonmaitree, T., Mann, L., Respiratory infections (1995) Human Enterovirus Infections, pp. 255-270. , Rotbart HA (ed) Washington DC: ASM Press; Ishiko, H., Shimada, Y., Yonaha, M., Molecular diagnosis of human enteroviruses by phylogeny-based classification by use of the VP4 sequence (2002) J. Infect. Dis., 185, pp. 744-754; Shafran, S.D., Halota, W., Gilbert, D., Bernstein, J., Meislin, H., Reiss, M., Pleconaril is effective for enteroviral meningitis in adolescents and adults: A randomised placebo-controlled multicenter trial (2002) Proceedings of the 39th Interscience Conference on Antimicrobial Agents and Chemotherapy, , Abstract 1904; Falsey, A.R., Walsh, E.E., Hayden, F.G., Rhinovirus and coronavirus infection-associated hospitalisations among older adults (2002) J. Infect. Dis., 185, pp. 1338-1341; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel common cold virus in organ cultures (1965) BMJ, 1, pp. 1467-1470; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Vabret, A., Mouthon, F., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., Direct diagnosis of human coronaviruses 229E and OC43 by the polymerase chain reaction (2001) J. Virol. Methods, 97, pp. 59-66; Flint, S.J., Enquist, L.W., Krug, R.M., Racniello, V.R., Skalka, A.M., Genome replication strategies: DNA viruses (2000) Principles of Virology -Molecular Biology, Pathogenesis, and Control, pp. 323-324. , Washington DC: ASM Press; Wadell, G., Adenoviruses (2000) Principles and Practice of Clinical Virology, pp. 310-312. , Zuckerman AJ, Banatvala JE, Pattison JMR (eds) 4th edn. John Wiley, Chichester; Ryan, M.A.K., Grapy, G.C., Smith, B., McKeehan, J.A., Hawksworth, A.W., Malasig, M.D., Large epidemic of respiratory illness due to adenovirus types 7 and 3 in healthy young adults (2002) Clin. Infect. Dis., 34, pp. 577-582; Howard, D.S., Gordon, L., Phillips, I.I., Adenovirus infections in hematopoietic stem cell transplant recipients (1999) Clin. Infect. Dis., 29, pp. 494-501; Hoffman, J.A., Shah, A., Ross, L.A., Kapoor, N., Adenoviral infections and a prospective trial of Cidofovir in pediatric hematopoietic stem cell transplantation (2001) Biol. Blood Marrow Transplant, 7, pp. 388-394; Atsuko, H., Asanuma, H., Rinki, M., Use of an inactivated varicella vaccine in recipients of hematopoietic-cell transplants (2002) New Engl. J. Med., 347, pp. 26-34; Gerna, G., Advances in diagnosis of herpesvirus infections: Clinical and therapeutic correlations (2002) Curr. Opin. Org. Transplant, 7, pp. 308-313","Mackie, P.L.; Department of Microbiology, Yorkhill NHS Trust, Glasgow G3 8SJ, United Kingdom; email: virology@supanet.com",,"W.B. Saunders Ltd",15260550,,PRRAE,"12758044","English","Paediatr. Respir. Rev.",Review,"Final",,Scopus,2-s2.0-0038617774
"Doan D.N.P., Dokland T.","57197008912;6701590227;","Structure of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus",2003,"Structure","11","11",,"1445","1451",,53,"10.1016/j.str.2003.09.018","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242542003&doi=10.1016%2fj.str.2003.09.018&partnerID=40&md5=b43ff3c3ee218cbca0bf3771bb796051","Inst. of Molecular and Cell Biology, Singapore 117609, Singapore","Doan, D.N.P., Inst. of Molecular and Cell Biology, Singapore 117609, Singapore; Dokland, T., Inst. of Molecular and Cell Biology, Singapore 117609, Singapore","Porcine reproductive and respiratory syndrome virus (PRRSV) is an enveloped RNA virus of the Arteriviridae family, genomically related to the coronaviruses. PRRSV is the causative agent of both severe and persistent respiratory disease and reproductive failure in pigs worldwide. The PRRSV virion contains a core made of the 123 amino acid nucleocapsid (N) protein, a product of the ORF7 gene. We have determined the crystal structure of the capsid-forming domain of N. The structure was solved to 2.6 Å resolution by SAD methods using the anomalous signal from sulfur. The N protein exists in the crystal as a tight dimer forming a four-stranded β sheet floor superposed by two long α helices and flanked by two N- and two C-terminal α helices. The structure of N represents a new class of viral capsid-forming domains, distinctly different from those of other known enveloped viruses, but reminiscent of the coat protein of bacteriophage MS2.",,"coat protein; nucleocapsid protein; alpha helix; amino terminal sequence; Arterivirus; article; bacteriophage; beta sheet; carboxy terminal sequence; crystal structure; electron diffraction; nonhuman; priority journal; protein domain; protein structure; virus capsid; Arteriviridae; Arterivirus; Porcine reproductive and respiratory syndrome virus; RNA viruses; Suidae","Blaha, T., The ""colorful"" epidemiology of PRRS (2000) Vet. Res., 31, pp. 77-83; Choi, H.-K., Tong, L., Minor, W., Dumas, P., Boege, U., Rossmann, M.G., Wengler, G., Structure of Sindbis virus core protein reveals a chymotrypsin-like serine protease and the organization of the virion (1991) Nature, 354, pp. 37-43; Cowtan, K., Main, P., Miscellaneous algorithms for density modification (1998) Acta Crystallogr. D Biol. Crystallogr., 54, pp. 487-493; Dauter, Z., New approaches to high-throughput phasing (2002) Curr. Opin. Struct. Biol., 12, pp. 674-678; Dea, S., Gagnon, C.A., Mardassi, H., Pirzadeh, B., Rogan, D., Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: Comparison of the North American and European isolates (2000) Arch. Virol., 145, pp. 659-688; Doan, D., Dokland, T., Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the structural domain of the nucleocapsid N protein from porcine reproductive and respiratory syndrome virus (PRRSV) (2003) Acta Crystallogr. D Biol. Crystallogr., 59, pp. 1504-1506; Dokland, T., Freedom and restraint: Themes in virus capsid assembly (2000) Structure, 8, pp. 157-R167; Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D Biol. Crystallogr., 55, pp. 938-940; Garboczi, D.N., Ghosh, P., Utz, U., Fan, Q.R., Biddison, W.E., Wiley, D.C., Structure of the complex between human T-cell receptor, viral peptide and HLA-A2 (1996) Nature, 384, pp. 134-141; Gouet, P., Courcelle, E., Stuart, D.I., Metoz, F., ESPript: Analysis of multiple sequence alignments in PostScript (1999) Bioinformatics, 15, pp. 305-308; Holm, L., Sander, C., Dali: A network tool for protein structure comparison (1995) Trends Biochem. Sci., 20, pp. 345-347; Huang, C.C., Couch, G.S., Pettersen, E.F., Ferrin, T.E., Chimera: An extensible molecular modeling application constructed using standard components (1996) Pac. Symp. Biocomput., 1, p. 724; Jones, T.A., Zou, J.-Y., Cowan, S.W., Kjeldgaard, M., Improved methods for the building of protein models in electron density and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119; Kraulis, P.J., Molscript: A program to produce both detailed and schematic plots of protein structure (1991) J. Appl. Crystallogr., 24, pp. 946-950; Le Gall, A., Legeay, O., Bourhy, H., Arnauld, C., Albina, E., Jestin, A., Molecular variation in the nucleoprotein gene (ORF7) of the porcine reproductive and respiratory syndrome virus (PRRSV) (1998) Virus Res., 54, pp. 9-21; Lescar, J., Roussel, A., Wien, M.W., Navaza, J., Fuller, S.D., Wengler, G., Wengler, G., Rey, F.A., The Fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH (2001) Cell, 105, pp. 137-148; Mardassi, H., Massie, B., Dea, S., Intracellular synthesis, processing and transport of proteins encoded by ORFs 5 to 7 of porcine reproductive and respiratory syndrome virus (1996) Virology, 221, pp. 98-112; Meng, X.J., Heterogeneity of porcine reproductive and respiratory syndrome virus: Implications for current vaccine efficacy and future vaccine development (2000) Vet. Microbiol., 12, pp. 309-329; Mengeling, W.L., Lager, K.M., Vorwald, A.C., Koehler, D.F., Comparative safety and efficacy of attenuated single-strain and multi-strain vaccines for porcine reproductive and respiratory syndrome (2003) Vet. Microbiol., 93, pp. 25-38; Merrit, E.A., Bacon, D.J., Raster3D photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524; Meulenberg, J.J., Hulst, M.M., De Meijer, E.J., Moonen, P.L., Den Besten, A., De Kluyver, E.P., Wenswoort, G., Moormann, R.J., Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS), is related to LDV and EAV (1993) Virology, 192, pp. 62-72; Meulenberg, J.J., Bende, R.J., Pol, J.M., Wenswoort, G., Moormann, R.J., Nucleocapsid protein N of Lelystad virus: Expression by recombinant baculovirus, immunological properties, and suitability for detection of serum antibodies (1995) Clin. Diagn. Lab. 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Virus Res., 41, pp. 99-192; Rey, F.A., Heinz, F.X., Mandl, C., Kunz, C., Harrison, S.C., The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution (1995) Nature, 375, pp. 291-298; Saper, M.A., Bjorkman, P.J., Wiley, D.C., Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution (1991) J. Mol. Biol., 219, pp. 277-319; Snijder, E.J., Meulenberg, J.J.M., The molecular biology or arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Strauss, J.H., Strauss, E.G., (2002) Viruses and Human Disease, , San Diego: Academic Press; Terwilliger, T.C., Automated structure solution, density modification and model building (2002) Acta Crystallogr. D Biol. Crystallogr., 58, pp. 1937-1940; Terwilliger, T.C., Automated main-chain model building by template matching and iterative fragment extension (2003) Acta Crystallogr. D Biol. Crystallogr., 59, pp. 38-44; Valegård, K., Liljas, L., Fridborg, K., Unge, T., The three-dimensional structure of the bacterial virus MS2 (1990) Nature, 345, pp. 36-41; Wenswoort, G., Lelystad virus and the porcine epidemic abortion and respiratory syndrome (1993) Vet. Res., 24, pp. 117-124; Wootton, S., Yoo, D., Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages (2003) J. Virol., 77, pp. 4546-4557; Wootton, S., Koljesar, G., Yang, L., Yoon, K.J., Yoo, D., Antigenic importance of the carboxy-terminal beta-strand of the porcine reproductive and respiratory syndrome virus nucleocapsid protein (2001) Clin. Diagn. Lab. Immunol., 8, pp. 598-603; Wootton, S.K., Rowland, R.R., Yoo, D., Phosphorylation of the porcine reproductive and respiratory syndrome virus nucleocapsid protein (2002) J. Virol., 76, pp. 10569-10576; Zimmermann, J.J., Yoon, K.J., Wills, R.W., Swenson, S.L., General overview of PRRSV: A perspective from the United States (1997) Vet. Microbiol., 55, pp. 187-196","Dokland, T.; Inst. of Molecular and Cell Biology, Singapore 117609, Singapore; email: dokland@imcb.a-star.edu.sg",,"Cell Press",09692126,,STRUE,"14604534","English","Structure",Article,"Final",Open Access,Scopus,2-s2.0-0242542003
"Li J., Luo C., Deng Y., Han Y., Tang L., Wang J., Ji J., Ye J., Jiang F., Xu Z., Tong W., Wei W., Zhang Q., Li S., Li W., Li H., Li Y., Dong W., Wang J., Bi S., Yang H.","8644253500;57198602476;8214333500;35310510700;57198909361;36078440500;36983919500;57208010895;8214334100;55502690600;56249426300;57198566868;15752326700;57207249958;57201905404;57196366091;55876190000;57198833517;57200022156;7101633642;34573719100;","The structural characterization and antigenicity of the S protein of SARS-CoV.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","2",,"108","117",,1,"10.1016/S1672-0229(03)01015-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-16644403174&doi=10.1016%2fS1672-0229%2803%2901015-5&partnerID=40&md5=86b576a1a74a90bcf01deee4bcbbfdfa","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Li, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Luo, C., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Deng, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Han, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Tang, L., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ji, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Ye, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Jiang, F., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xu, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Tong, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wei, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhang, Q., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Dong, W., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Bi, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","The corona-like spikes or peplomers on the surface of the virion under electronic microscope are the most striking features of coronaviruses. The S (spike) protein is the largest structural protein, with 1,255 amino acids, in the viral genome. Its structure can be divided into three regions: a long N-terminal region in the exterior, a characteristic transmembrane (TM) region, and a short C-terminus in the interior of a virion. We detected fifteen substitutions of nucleotides by comparisons with the seventeen published SARS-CoV genome sequences, eight (53.3%) of which are non-synonymous mutations leading to amino acid alternations with predicted physiochemical changes. The possible antigenic determinants of the S protein are predicted, and the result is confirmed by ELISA (enzyme-linked immunosorbent assay) with synthesized peptides. Another profound finding is that three disulfide bonds are defined at the C-terminus with the N-terminus of the E (envelope) protein, based on the typical sequence and positions, thus establishing the structural connection with these two important structural proteins, if confirmed. Phylogenetic analysis reveals several conserved regions that might be potent drug targets.",,"membrane protein; spike glycoprotein, coronavirus; virus antigen; virus envelope protein; amino acid sequence; article; biology; comparative study; DNA base composition; DNA sequence; enzyme linked immunosorbent assay; genetics; immunology; metabolism; molecular genetics; mutation; phylogeny; protein tertiary structure; SARS coronavirus; sequence homology; Amino Acid Sequence; Antigens, Viral; Base Composition; Computational Biology; Enzyme-Linked Immunosorbent Assay; Membrane Glycoproteins; Molecular Sequence Data; Mutation; Phylogeny; Protein Structure, Tertiary; SARS Virus; Sequence Analysis, DNA; Sequence Homology; Viral Envelope Proteins",,"Li, J.",,,16720229,,,"15626341","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-16644403174
"Ren Y., Ding H.G., Wu Q.F., Chen W.J., Chen D., Bao Z.Y., Yang L., Zhao C.H., Wang J.","56307074300;57206946373;7404602222;35236384200;57199413823;7202908341;57198990801;55476832700;36078145500;","Detection of SARS-CoV RNA in stool samples of SARS patients by nest RT-PCR and its clinical value",2003,"Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae","25","3",,"368","371",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0842278590&partnerID=40&md5=b5043dbc3c86003de1ec09d40b05c7f8","Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China","Ren, Y., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Ding, H.G., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Wu, Q.F., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Chen, W.J., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Chen, D., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Bao, Z.Y., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Yang, L., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Zhao, C.H., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China; Wang, J., Department of Infectious Diseases, Beijing You'an Hospital, Capital University of Medicine Science, Beijing, 100054, China","OBJECTIVE: To investigate of severe acute respiratory syndrome (SARS) convalescent stool shedding by RT-PCR. METHODS: One hundred and three stool samples from 46 SARS patients were collected on May 16th, 20th, and 23rd, 2003. For each sample, RNA was extracted using commercial kit and 7 Nest RT-PCR using a 14-pair different SARS-associated coronavirus (SARS-CoV) special primers were carried out simultaneously. RESULTS: Among these 46 SARS patients, 17 cases (37.0%) were stool SARS-CoV RT-PCR negative, and 29 cases (63.0%) were SARS-CoV RT-PCR positive. The duration of positive cases lasted (31.76 +/- 10.78) d (12-64 d). The longest stool shedding case in this study lasted 64 days. Two serial stool samples and for each sample 2 RT-PCR tests using different primers were positive in this case. CONCLUSIONS: Our study observed longest stool shedding of SARS patients to be 64 days after initial onset of SARS. The average stool shedding was 32 days. Hence it is important to think highly of SARS convalescent patient stool sterilization.",,"virus RNA; adolescent; adult; article; disease transmission; feces; female; human; isolation and purification; male; methodology; middle aged; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; time; virology; Adolescent; Adult; Feces; Female; Humans; Male; Middle Aged; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Time Factors",,"Ren, Y.email: renyi@staff.healthoo.com",,,1000503X,,,"12905760","Chinese","Zhongguo Yi Xue Ke Xue Yuan Xue Bao",Article,"Final",,Scopus,2-s2.0-0842278590
"Rebel K., Poulet H.","57081425100;6603472294;","Eurifel® FeLV, a non replicative vector vaccine (canarypoxvirus) [Eurifel® FeLV, eine nicht vermehrungsfähige vektorvakzine (kanarienpockenvirus)]",2003,"Tierarztliche Umschau","58","1",,"33","40",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037255831&partnerID=40&md5=c26bdc4c337ceef12f09e568ae15fb5e","Merial GmbH, Am Söldnermoos 6, D-85399 Hallbergmoos, Germany","Rebel, K., Merial GmbH, Am Söldnermoos 6, D-85399 Hallbergmoos, Germany; Poulet, H.","Feline retroviruses are one of the most common infectious causes for death in cats. Especially the FeLV virus is still common in cats despite the success in controlling the FeLV infection. The incidence of the FeLV infection is correlating with the density of the cat population and the life circumstances of the animals. The infection rate concerning FeLV is about 5% in healthy cats and much higher in sick cats, between 11,3% and 19,4% depending on the country (Braley, 1994). 30-40% of FeLV infected cats develop a persistent infection. Especially these cats get sick because of FeLV associated diseases (Hoover und Mullins, 1991). It has been shown in a clinical virological study over a period of 10 years with a group of cats infected with FeLV, FIV (feline immunodeficiency virus) and feline coronavirus, that FeLV has the main impact on the mortality of these cats (Addie et al., 2000). The importance of FeLV justifies the vaccination against this infection and the development of new technologies for more efficacious FeLV vaccines with better safety.",,"eurifel; virus vaccine; article; cat disease; controlled study; density; incidence; infection control; infection rate; mortality; nonhuman; Retrovirus; vaccination; Animalia; Coronavirus; Felidae; Feline coronavirus; Feline immunodeficiency virus; Felis catus; unidentified retrovirus","Addie, D.D., Long-term impact on a closed household of pet cats of natural infection with feline coronavirus, feline leukaemia virus and feline immunodeficiency virus (2000) Vet. Rec., 146, pp. 419-424; Braley, J., FeLV and FIV: Survey shows prevalence in the United States and Europe (1994) Feline Practice, 22, pp. 25-29; Clements-Mann, M.L., Immune responses to human immunodeficiency virus (HIV) type 1 induced by Kanarienpocken expressing HIV-1MN gp120, HIV-1SF2 recombinant gp120, or both vaccines in seronegative adults (1998) J. Inf. Dis., 177, pp. 1230-1246; Devauchelle, P., (2001) Dynamique de la Réaction Inflammatoire Induite chez le Chat par l'Administration Sous-cutanée d'un Vaccin non Adjuvé, , Poster CNVSPA Congress Lille; Donahue, P.R., Strong sequence conservation among horizontally transmissible minimally pathogenic feline leukemia viruses (1988) J. Virol., 62, pp. 722-731; Egan, M.A., Induction of human immunodeficiency virus type 1 (HIV-1) specific cytolytic T lymphocytes responses in seronegative adults by a non-replicating, host-range restricted Kanarienpocken vector (ALVAC) carrying the HIV-1MN env gene (1995) J. Inf. Dis., 171, pp. 1623-1627; Flynn, J.N., Feline leukaemia virus: Protective immunity is mediated by virus-specific cytotoxic T lymphocytes (2000) Immunology, 101, pp. 120-125; Gruffydd-Jones, T.J., A comparative study of the efficacy of a canarypox based recombinant leukaemia vaccine against a natural FeLV challenge in cats (1999) Proc of the 24th World Small Animal Vet Congress, , Lyon, France, Sep 23-26; Hardy, W.D., Feline oncoretroviruses (1993) The Retroviridae, 2, pp. 109-180. , 1993, (JA Levy, Edr) Plenum Press, New York; Hoover, E.A., Passive immunity to feline leukaemia: Evaluation of immunity from dams naturally infected and experimentally vaccinated (1977) Infect. Immun., 16 (1), pp. 54-59; Hoover, E.A., Mullins, J.I., Feline leukemia virus infection and diseases (1991) J. Am. Vet. Med. Ass., 199, pp. 1287-1297; Jarrett, O., The frequency of occurrence of feline leukaemia subgroups in cats (1978) Int. J. Cancer, 21, pp. 334-337; Jarrett, O., Russel, P.H., Differential growth and transmission in cats of feline leukaemia viruses of subgroups A and B (1978) Int. J. Cancer, 21, pp. 446-472; Madewell, B.R., Feline vaccine-associated fibrosarcoma: An ultrastructural study of 20 tumors (1996-1999) (2001) Vet. Pathol. Mar., 38 (2), pp. 196-202; (1999) Merial Eigene Studien, , Technical Dossier; Plotkin, S.A., The safety and use of canarypox vectored vaccines (1995) Dev. Biol. Stand. Basel, Karger, 84, pp. 165-170; Rojko, J.L., Kociba, G.J., Pathogenesis of infection by the feline leukemia virus (1991) J. Am. Vet. Med. Assoc., 199, pp. 1305-1310; Roy-Burman, P., Endogenous env elements: Partners in generation of pathogenic feline leukemia viruses (1995) Virus Genes, 11, pp. 147-161; Sparkes, A.H., Feline leukaemia virus: A review of immunity and vaccination (1997) J. Small Anim. Pract., 38 (5), pp. 187-194; Stewart, M.A., Nucleotide sequences of a feline virus subgroup A envelope gene and long terminal repeat and evidence for the recombinational origin of subgroup B viruses (1986) J. Virol., 58, pp. 825-834; Tartaglia, J., Protection of cats against feline leukemia virus by vaccination with Kanarienpocken virus recombinant, ALVAC-FL (1993) J. Virol., 67, pp. 2370-2375; Taylor, J., Applications of canarypox (ALVAC) vectors in human and veterinary vaccination (1994) Dev. Biol. Stand. Basel, Karger, 82, pp. 131-135; Taylor, J., Biological and immunogenic properties of a canarypox-rabies recombinant, ALVAC-RG (vCP65) in non-avian species (1995) Vaccine, 13 (6), pp. 539-549","Rebel, K.; Merial GmbH, Am Söldnermoos 6, D-85399 Hallbergmoos, Germany",,,00493864,,,,"German","Tierarztl. Umsch.",Article,"Final",,Scopus,2-s2.0-0037255831
"Shu Y.L., Duan Z.J., Wang Z., Sun M.S., Zhang J., Zhang L.L., Ma X.J., Peng J.P., Jin Q., Hou Y.D.","7103239481;57207232334;55850283300;14625672900;57196388027;25936982500;57199216492;56187585800;57214296001;7402198565;","Development of the cDNA chip for SARS virus and a primary study on the possible molecular mechanism of interferon alpha2b inhibiting the SARS virus replication",2003,"Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology","17","3",,"209","212",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-66049094052&partnerID=40&md5=fe2a3c065fdbc674b1aa73ffed911cf2","State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China","Shu, Y.L., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Duan, Z.J., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Wang, Z., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Sun, M.S., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Zhang, J., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Zhang, L.L., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Ma, X.J., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Peng, J.P., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Jin, Q., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China; Hou, Y.D., State Research Center for Biotechnological Engineering, Beijing Jin Di Ke Biotechnology Institute, Beijing, 100176, China","BACKGROUND: To study the molecular mechanism of interferon alpha2b(IFNalpha2b) inhibiting the SARS virus replication. SARS-associated coronavirus (SARS virus) cDNA chip was developed and applied to detect the virus RNA transcription levels in the interferon-treated and untreated cell cultures, and the mechanism of anti-SARS virus activity of interferon alpha2b in cell culture system was explored. METHODS: SARS virus cDNA chip was prepared by comparing the published SARS virus genome sequence, and the cDNA chip was used to study the interferon alpha2b function during SARS virus replication. RESULTS: SARS virus cDNA chip was successfully prepared by using PCR method. The results showed that the cDNA chip could be used to detect the viral RNA transcription level. Interferon alpha2b could inhibit almost all the SARS virus gene transcription. An unknown gene at the position 28130-28426 bp, named as U gene, may play an important role during the viral replication. CONCLUSION: A SARS virus whole genome cDNA chip was established. It could be used to study the virus molecular biology and antiviral drug screening. The results also showed that interferon alpha2b could inhibit almost the whole virus gene transcription by using the cDNA chip.",,"alpha2b interferon; virus RNA; article; DNA microarray; drug effect; evaluation; genetics; human; isolation and purification; methodology; physiology; SARS coronavirus; severe acute respiratory syndrome; virology; virus replication; Humans; Interferon Alfa-2b; Oligonucleotide Array Sequence Analysis; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Virus Replication",,"Shu, Y.L.",,,10039279,,,"15340559","Chinese","Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-66049094052
"Bi S., Qin E., Xu Z., Li W., Wang J., Hu Y., Liu Y., Duan S., Hu J., Han Y., Xu J., Li Y., Yi Y., Zhou Y., Lin W., Xu H., Li R., Zhang Z., Sun H., Zhu J., Yu M., Fan B., Wu Q., Lin W., Tang L., Yang B., Li G., Peng W., Li W., Jiang T., Deng Y., Liu B., Shi J., Deng Y., Wei W., Liu H., Tong Z., Zhang F., Zhang Y., Wang C., Li Y., Ye J., Gan Y., Ji J., Li X., Tian X., Lu F., Tan G., Yang R., Liu B., Liu S., Li S., Wang J., Wang J., Cao W., Yu J., Dong X., Yang H.","7101633642;6701908544;36007796100;56127183500;57200029227;12775742400;34267728900;57215374665;8249689300;35310510700;7407003499;57202364500;57203794385;36154255100;57198652365;8571413000;36152908600;8312674300;57214427420;8312674600;56512847900;7102879235;7404602222;57211371580;57198909361;56306611900;54684251100;8266260600;55718638800;57213459095;8214333500;14019808300;55491813100;12141082300;57198566868;57191744060;57205922887;55360405200;7601323407;8266261300;7502086390;57208010895;15318951200;36983919500;55718189300;13609877900;7402967940;57207324580;57201305076;24366565200;7409459608;7409241896;55552724800;57200022156;57199658059;8679878600;57198936340;34573719100;","Complete genome sequences of the SARS-CoV: the BJ Group (Isolates BJ01-BJ04).",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"180","192",,9,"10.1016/S1672-0229(03)01023-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-13744254043&doi=10.1016%2fS1672-0229%2803%2901023-4&partnerID=40&md5=ccfe0b11df3bf9894d2ffd62c7e4c8ed","Center of Disease Control and Prevention, Beijing, 100050, China","Bi, S., Center of Disease Control and Prevention, Beijing, 100050, China; Qin, E., Center of Disease Control and Prevention, Beijing, 100050, China; Xu, Z., Center of Disease Control and Prevention, Beijing, 100050, China; Li, W., Center of Disease Control and Prevention, Beijing, 100050, China; Wang, J., Center of Disease Control and Prevention, Beijing, 100050, China; Hu, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Liu, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Duan, S., Center of Disease Control and Prevention, Beijing, 100050, China; Hu, J., Center of Disease Control and Prevention, Beijing, 100050, China; Han, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Xu, J., Center of Disease Control and Prevention, Beijing, 100050, China; Li, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Yi, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Zhou, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Lin, W., Center of Disease Control and Prevention, Beijing, 100050, China; Xu, H., Center of Disease Control and Prevention, Beijing, 100050, China; Li, R., Center of Disease Control and Prevention, Beijing, 100050, China; Zhang, Z., Center of Disease Control and Prevention, Beijing, 100050, China; Sun, H., Center of Disease Control and Prevention, Beijing, 100050, China; Zhu, J., Center of Disease Control and Prevention, Beijing, 100050, China; Yu, M., Center of Disease Control and Prevention, Beijing, 100050, China; Fan, B., Center of Disease Control and Prevention, Beijing, 100050, China; Wu, Q., Center of Disease Control and Prevention, Beijing, 100050, China; Lin, W., Center of Disease Control and Prevention, Beijing, 100050, China; Tang, L., Center of Disease Control and Prevention, Beijing, 100050, China; Yang, B., Center of Disease Control and Prevention, Beijing, 100050, China; Li, G., Center of Disease Control and Prevention, Beijing, 100050, China; Peng, W., Center of Disease Control and Prevention, Beijing, 100050, China; Li, W., Center of Disease Control and Prevention, Beijing, 100050, China; Jiang, T., Center of Disease Control and Prevention, Beijing, 100050, China; Deng, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Liu, B., Center of Disease Control and Prevention, Beijing, 100050, China; Shi, J., Center of Disease Control and Prevention, Beijing, 100050, China; Deng, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Wei, W., Center of Disease Control and Prevention, Beijing, 100050, China; Liu, H., Center of Disease Control and Prevention, Beijing, 100050, China; Tong, Z., Center of Disease Control and Prevention, Beijing, 100050, China; Zhang, F., Center of Disease Control and Prevention, Beijing, 100050, China; Zhang, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Wang, C., Center of Disease Control and Prevention, Beijing, 100050, China; Li, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Ye, J., Center of Disease Control and Prevention, Beijing, 100050, China; Gan, Y., Center of Disease Control and Prevention, Beijing, 100050, China; Ji, J., Center of Disease Control and Prevention, Beijing, 100050, China; Li, X., Center of Disease Control and Prevention, Beijing, 100050, China; Tian, X., Center of Disease Control and Prevention, Beijing, 100050, China; Lu, F., Center of Disease Control and Prevention, Beijing, 100050, China; Tan, G., Center of Disease Control and Prevention, Beijing, 100050, China; Yang, R., Center of Disease Control and Prevention, Beijing, 100050, China; Liu, B., Center of Disease Control and Prevention, Beijing, 100050, China; Liu, S., Center of Disease Control and Prevention, Beijing, 100050, China; Li, S., Center of Disease Control and Prevention, Beijing, 100050, China; Wang, J., Center of Disease Control and Prevention, Beijing, 100050, China; Wang, J., Center of Disease Control and Prevention, Beijing, 100050, China; Cao, W., Center of Disease Control and Prevention, Beijing, 100050, China; Yu, J., Center of Disease Control and Prevention, Beijing, 100050, China; Dong, X., Center of Disease Control and Prevention, Beijing, 100050, China; Yang, H., Center of Disease Control and Prevention, Beijing, 100050, China","Beijing has been one of the epicenters attacked most severely by the SARS-CoV (severe acute respiratory syndrome-associated coronavirus) since the first patient was diagnosed in one of the city's hospitals. We now report complete genome sequences of the BJ Group, including four isolates (Isolates BJ01, BJ02, BJ03, and BJ04) of the SARS-CoV. It is remarkable that all members of the BJ Group share a common haplotype, consisting of seven loci that differentiate the group from other isolates published to date. Among 42 substitutions uniquely identified from the BJ group, 32 are non-synonymous changes at the amino acid level. Rooted phylogenetic trees, proposed on the basis of haplotypes and other sequence variations of SARS-CoV isolates from Canada, USA, Singapore, and China, gave rise to different paradigms but positioned the BJ Group, together with the newly discovered GD01 (GD-Ins29) in the same clade, followed by the H-U Group (from Hong Kong to USA) and the H-T Group (from Hong Kong to Toronto), leaving the SP Group (Singapore) more distant. This result appears to suggest a possible transmission path from Guangdong to Beijing/Hong Kong, then to other countries and regions.",,"article; comparative study; genetics; haplotype; human; mutation; open reading frame; phylogeny; SARS coronavirus; virus genome; Genome, Viral; Haplotypes; Humans; Mutation; Open Reading Frames; Phylogeny; SARS Virus",,"Bi, S.email: dongxp@public.fhnet.cn.net",,,16720229,,,"15629030","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-13744254043
"Graat J.M., Schouten E.G., Heijnen M.-L.A., Kok F.J., Pallast E.G.M., De Greeff S.C., Dorigo-Zetsma J.W.","6506164385;7006854308;6701597045;25654998100;6508086325;6506789815;6701884668;","A prospective, community-based study on virologic assessment among elderly people with and without symptoms of acute respiratory infection",2003,"Journal of Clinical Epidemiology","56","12",,"1218","1223",,50,"10.1016/S0895-4356(03)00171-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0348110571&doi=10.1016%2fS0895-4356%2803%2900171-9&partnerID=40&md5=4f069b8c0e9248a5e4d55592244cf32a","Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; Dept. of Infect. Dis. Epidemiology, Natl. Inst. Pub. Hlth. the Environ., Antonie van Leeuwenhoeklaan 9, 3728 BA, Bilthoven, Netherlands; Diagn. Lab. Infect. Dis. P., Natl. Inst. Pub. Hlth. the Environ., Antonie van Leeuwenhoeklaan 9, 3728 BA, Bilthoven, Netherlands","Graat, J.M., Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; Schouten, E.G., Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; Heijnen, M.-L.A., Dept. of Infect. Dis. Epidemiology, Natl. Inst. Pub. Hlth. the Environ., Antonie van Leeuwenhoeklaan 9, 3728 BA, Bilthoven, Netherlands; Kok, F.J., Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; Pallast, E.G.M., Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; De Greeff, S.C., Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; Dorigo-Zetsma, J.W., Diagn. Lab. Infect. Dis. P., Natl. Inst. Pub. Hlth. the Environ., Antonie van Leeuwenhoeklaan 9, 3728 BA, Bilthoven, Netherlands","Background and Objective: Community-based elderly studies concerning microbiology of acute respiratory infections are scarce. Data on subclinical infections are even totally absent, although asymptomatic persons might act as a source of respiratory infections. Methods: In a 1-year community-based study, we prospectively investigated the possible virologic cause of acute respiratory infections in 107 symptomatic case episodes and 91 symptom-free control periods. Participants, persons ≥60 years, reported daily the presence of respiratory symptoms in a diary. Virologic assessment was performed by polymerase chain reaction (PCR) and serology. Results: In 58% of the case episodes a pathogen was demonstrated, the most common being rhinoviruses (32%), coronaviruses (17%), and influenzaviruses (7%). The odds ratio for demonstrating a virus in cases with symptoms vs. controls without symptoms was 30.0 (95% confidence interval 10.2-87.6). In 4% of the symptom-free control periods a virus was detected. Conclusion: This study supports the importance of rhinovirus infections in community-dwelling elderly persons, whereas asymptomatic elderly persons can also harbor pathogens as detected by PCR, and thus might be a source of infection for their environment. © 2003 Elsevier Inc. All rights reserved.","Acute respiratory infections; Community based; Elderly; Etiology; Rhinovirus; Virology","adult; aged; article; confidence interval; controlled study; Coronavirus; Enterovirus; female; human; infection risk; Influenza virus A; Influenza virus B; major clinical study; male; Parainfluenza virus 1; Parainfluenza virus 2; Parainfluenza virus 3; polymerase chain reaction; priority journal; prospective study; respiratory tract infection; Rhinovirus; serology; symptomatology; virology; virus detection; virus examination; virus pathogenesis","Miller, R.A., The aging immune system: Primer and prospectus (1996) Science, 273, pp. 70-74; Nicholson, K.G., Kent, J., Hammersley, V., Cancio, E., Acute viral infections of upper respiratory tract in elderly people living in the community: Comparative, prospective, population based study of disease burden (1997) BMJ, 315, pp. 1060-1064; Graat, J.M., Schouten, E.G., Kok, F.J., Effect of daily vitamin e and multivitamin-mineral supplementation on acute respiratory tract infections in elderly persons - A randomized controlled trial (2002) JAMA, 288, pp. 715-721; Makela, M.J., Puhakka, T., Ruuskanen, O., Leinonen, M., Saikku, P., Kimpimaki, M., Blomqvist, S., Arstila, P., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Chernoff, R., Meeting the nutritional needs of the elderly in the institutional setting (1994) Nutr Rev, 52, pp. 132-136; Drinka, P.J., Gravenstein, S., Krause, P., Langer, E.H., Barthels, L., Dissing, M., Shult, P., Scihlling, M., Non-influenza respiratory viruses may overlap and obscure influenza activity (1999) J Am Geriatr Soc, 47, pp. 1087-1093; Falsey, A.R., McCann, R.M., Hall, W.J., Tanner, M.A., Criddle, M.M., Formica, M.A., Irvine, C.S., Treanor, J.J., Acute respiratory tract infection in daycare centers for older persons (1995) J Am Geriatr Soc, 43, pp. 30-36; MacFarlane, J.T., Colville, A., Guion, A., MacFarlane, R.M., Rose, D.H., Prospective study of aetiology and outcome of adult lower-respiratory- tract infections in the community (1993) Lancet, 341, pp. 511-514; Carrat, F., Tachet, A., Rouzioux, C., Housset, B., Valleron, A.J., Evaluation of clinical case definitions of influenza: Detailed investigation of patients during the 1995-1996 epidemic in France (1999) Clin Infect Dis, 28, pp. 283-290; Monto, A.S., Napier, J.A., Metzner, H.L., The Tecumseh study of respiratory illness: I. Plan of study and observations on syndromes of acute respiratory disease (1971) Am J Epidemiol, 94, pp. 269-279; Nicholson, K.G., Baker, D.J., Farquhar, A., Hurd, D., Kent, J., Smith, S.H., Acute upper respiratory tract viral illness and influenza immunization in homes for the elderly (1990) Epidemiol Infect, 105, pp. 609-618; Andeweg, A.C., Bestebroer, T.M., Huybreghs, M., Kimman, T.G., De-Jong, J.C., Improved detection of rhinoviruses in clinical samples by using a newly developed nested reverse transcription-PCR assay (1999) J Clin Microbiol, 37, pp. 524-530; Cubie, H.A., Inglis, J.M., Leslie, E.E., Edmunds, A.T., Totapally, B., Detection of respiratory syncytial virus in acute bronchiolitis in infants (1992) J Med Virol, 38, pp. 283-287; Myint, S., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Lambden, P.R., Holgate, S.T., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with and without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Heijnen, M.L.A., Van Den Brandhof, W.E., Bartelds, A.I.M., Peeters, M.F., Wilbrink, B., ARI-EL studie: Acute respiratoire infecties in de eerste lijn (2002) Infect Bull, 13 (3), pp. 104-110; Monto, A.S., Sullivan, K.M., Acute respiratory illness in the community. Frequency of illness and the agents involved (1993) Epidemiol Infect, 110, pp. 145-160; Rockwood, K., Stadnyk, K., MacKnight, C., McDowell, I., Hebert, R., Hogan, D.B., A brief clinical instrument to classify frailty in elderly people (1999) Lancet, 353, pp. 205-206; Fleming, D.M., Cross, K.W., Respiratory syncytial virus or influenza? (1993) Lancet, 342, pp. 1507-1510; Lieberman, D., Shvartzman, P., Korsonsky, I., Aetiology of respiratory tract infections: Clinical assessment versus serological tests (2001) Br J Gen Pract, 51, pp. 998-1000; Shi, Y., Xia, X., Song, Y., Feng, G., Hu, L., Zhang, X., Tong, M., Assessment of polymerase chain reaction and serology for detection of chlamydia pneumoniae in patients with acute respiratory tract infection (2002) Chin Med J, 115 (2), pp. 184-187; Meijer, A., Dagnelie, C.F., De-Jong, J.C., De-Vries, A., Besterbroer, T.M., Van-Loon, A.M., Bartelds, A.I.M., Ossewaarde, J.M., Low prevalence of Chlamydia pneumoniae and Mycoplasma pneumoniae among patients with symptoms of respiratory tract infections in Dutch general practices (2000) Eur J Epidemiol, 16, pp. 1099-1106; Garrett, C.T., Porter-Jordan, K., Nasim, S., Polymerase chain reaction (1992) Clinical Virology Manual, pp. 309-318. , S. Specter, & G. Lancz. Amsterdam: Elsevier Science Publishers B.V; Dorigo-Zetsma, J.W., Zaat, S.A.J., Vriesema, A.J.M., Dankert, J., Demonstration by a nested PCR for Mycoplasma pneumoniae that M-pneumoniae load in the throat is higher in patients hospitalised for M-pneumoniae infection than in non-hospitalised subjects (1999) J Med Microbiol, 48, pp. 1115-1122","Schouten, E.G.; Div. of Hum. Nutr. and Epidemiology, Wageningen University, Bomenweg 4, 6703 HD, Wageningen, Netherlands; email: Evert.Schouten@wur.nl",,"Elsevier Inc.",08954356,,JCEPE,"14680673","English","J. Clin. Epidemiol.",Article,"Final",,Scopus,2-s2.0-0348110571
"Rowland R.R.R., Yoo D.","7102266919;7103242554;","Nucleolar-cytoplasmic shuttling of PRRSV nucleocapsid protein: A simple case of molecular mimicry or the complex regulation by nuclear import, nucleolar localization and nuclear export signal sequences",2003,"Virus Research","95","1-2",,"23","33",,76,"10.1016/S0168-1702(03)00161-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142123454&doi=10.1016%2fS0168-1702%2803%2900161-8&partnerID=40&md5=8acfdfa49bd07ad891773a8c581a1552","Dept. of Diagn. Med./Pathobiology, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States; Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","Rowland, R.R.R., Dept. of Diagn. Med./Pathobiology, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States; Yoo, D., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. N1G 2W1, Canada","The order Nidovirales, which includes the arteriviruses and coronaviruses, incorporate a cytoplasmic replication scheme; however, the nucleocapsid (N) protein of several members of this group localizes to the nucleolus suggesting that viral proteins influence nuclear processes during replication. The relatively small, 123 amino acid, N protein of porcine reproductive and respiratory syndrome virus (PRRSV), an arterivirus, presents an ideal model system for investigating the properties and mechanism of N protein nucleolar localization. The PRRSV N protein is found in both cytoplasmic and nucleolar compartments during infection and after transfection of gene constructs that express N-enhanced green fluorescent protein (EGFP) fusion proteins. Experiments using oligopeptides, truncated polypeptides and amino acid-substituted proteins have identified several domains within PRRSV N protein that participate in nucleo-cytoplasmic shuttling, including a cryptic nuclear localization signal (NLS) called NLS-1, a functional NLS (NLS-2), a nucleolar localization sequence (NoLS), as well as a possible nuclear export signal (NES). The purpose of this paper is to review our current understanding of PRRSV N protein shuttling and propose a shuttling scheme regulated by RNA binding and post-translational modification. © 2003 Elsevier B.V. All rights reserved.","Nuclear localization; Nucleocapsid; PRRSV","amino acid; cell protein; cytoplasm protein; green fluorescent protein; guanine nucleotide binding protein; hybrid protein; nucleocapsid protein; oligopeptide; peptide; virus protein; amino acid sequence; amino acid substitution; amino terminal sequence; Arterivirus; carboxy terminal sequence; gene construct; molecular mimicry; molecular model; mouse strain; Nidovirales; nonhuman; nuclear import; nuclear localization signal; nucleocytoplasmic transport; nucleolus; priority journal; protein determination; protein domain; protein expression; protein localization; protein phosphorylation; protein processing; review; RNA binding; swine; virus replication; Arterivirus; Nes; Nidovirales; Porcine reproductive and respiratory syndrome virus; Suidae","Adachi, Y., Copeland, T.D., Hatanaka, M., Oroszlan, S., Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23 (1993) J. 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Q., 13, pp. 121-130; Wootton, S.K., Yoo, D., Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages (2003) J. Virol., 77, pp. 4546-4557; Wootton, S.K., Nelson, E.A., Yoo, D., Antigenic structure of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus (1998) Clin. Diagn. Lab. Immunol., 5, pp. 773-779; Wootton, S., Koljesar, G., Yang, L., Yoon, K.J., Yoo, D., Antigenic importance of the carboxy-terminal beta-strand of the porcine reproductive and respiratory syndrome virus nucleocapsid protein (2001) Clin. Diagn. Lab. Immunol., 8, pp. 598-603; Wootton, S.K., Rowland, R.R., Yoo, D., Phosphorylation of the porcine reproductive and respiratory syndrome virus nucleocapsid protein (2002) J. Virol., 76, pp. 10569-10576; Wurm, T., Chen, H., Hodgson, T., Britton, P., Brooks, G., Hiscox, J.A., Localization to the nucleolus is a common feature of coronavirus nucleoproteins and the protein may disrupt host cell division (2001) J. Virol., 75, pp. 9345-9356; Xiao, C.Y., Jans, P., Jans, D.A., Negative charge at the protein kinase CK2 site enhances recognition of the SV40 large T-antigen NLS by importin: Effect of conformation (1998) FEBS, 440, pp. 297-301; Yamanaka, T., Kodama, T., Doi, T., Subcellular localization of HCV core protein regulates its ability for p53 activation and p21 suppression (2002) Biochem. Biophys. Res. Commun., 294, pp. 528-534; Yasui, K., Wakita, T., Tsukiyama-Kohara, K., Funahashi, S.I., Ichikawa, M., Kajita, T., Moradpour, D., Kohara, M., The native form and maturation process of hepatitis C virus core protein (1998) J. Virol., 72, pp. 6048-6055","Rowland, R.R.R.; Dept. of Diagn. Med./Pathobiology, Kansas State University, 1800 Denison Ave., Manhattan, KS 66506, United States; email: browland@vet.ksu.edu",,"Elsevier",01681702,,VIRED,"12921993","English","Virus Res.",Article,"Final",,Scopus,2-s2.0-0142123454
"Krokhin O., Li Y., Andonov A., Feldmann H., Flick R., Jones S., Stroeher U., Bastien N., Dasuri K.V., Cheng K., Simonsen J.N., Perreault H., Wilkins J., Ens W., Plummer F., Standing K.G.","34571359400;35187394200;6701413300;7202115850;7006769609;57194562205;6603000295;6602480468;9746796200;7402998132;7007029925;7003487803;7201997316;7005033835;7102012709;7005202598;","Mass spectrometric characterization of proteins from the SARS virus: a preliminary report.",2003,"Molecular & cellular proteomics : MCP","2","5",,"346","356",,110,"10.1074/mcp.M300048-MCP200","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141926488&doi=10.1074%2fmcp.M300048-MCP200&partnerID=40&md5=0701f22ab5434a5a40d7f2b9cb5c8ba3","Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada","Krokhin, O., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Li, Y., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Andonov, A., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Feldmann, H., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Flick, R., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Jones, S., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Stroeher, U., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Bastien, N., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Dasuri, K.V., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Cheng, K., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Simonsen, J.N., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Perreault, H., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Wilkins, J., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Ens, W., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Plummer, F., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada; Standing, K.G., Department of Physics, University of Manitoba, Winnipeg MB R3T 2N2, Canada","A new coronavirus has been implicated as the causative agent of severe acute respiratory syndrome (SARS). We have used convalescent sera from several SARS patients to detect proteins in the culture supernatants from cells exposed to lavage another SARS patient. The most prominent protein in the supernatant was identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) as a approximately 46-kDa species. This was found to be a novel nucleocapsid protein that matched almost exactly one predicted by an open reading frame in the recently published nucleotide sequence of the same virus isolate (>96% coverage). A second viral protein corresponding to the predicted approximately 139-kDa spike glycoprotein has also been examined by MALDI-TOF MS (42% coverage). After peptide N-glycosidase F digestion, 12 glycosylation sites in this protein were confirmed. The sugars attached to four of the sites were also identified. These results suggest that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics, and that the spike glycoprotein may present a particularly attractive target for prophylactic intervention in combating SARS.",,"membrane protein; nucleocapsid protein; spike glycoprotein, coronavirus; virus envelope protein; virus protein; amino acid sequence; animal; article; chemistry; human; immunology; mass spectrometry; methodology; molecular genetics; molecular weight; SARS coronavirus; sequence alignment; severe acute respiratory syndrome; Amino Acid Sequence; Animals; Humans; Membrane Glycoproteins; Molecular Sequence Data; Molecular Weight; Nucleocapsid Proteins; SARS Virus; Sequence Alignment; Severe Acute Respiratory Syndrome; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Viral Envelope Proteins; Viral Proteins",,"Krokhin, O.",,,15359476,,,"12775768","English","Mol. Cell Proteomics",Article,"Final",Open Access,Scopus,2-s2.0-0141926488
"Ren Y., Zhou Z., Liu J., Lin L., Li S., Wang H., Xia J., Zhao Z., Wen J., Zhou C., Wang J., Yin J., Xu N., Liu S.","57198461840;56141101800;55705826000;55676528000;57207248052;56608115200;11139508800;57199102301;49664305200;12773498800;8272121600;7401693537;55771049200;7409459608;","A strategy for searching antigenic regions in the SARS-CoV spike protein.",2003,"Genomics, proteomics & bioinformatics / Beijing Genomics Institute","1","3",,"207","215",,5,"10.1016/S1672-0229(03)01026-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2942622512&doi=10.1016%2fS1672-0229%2803%2901026-X&partnerID=40&md5=156160c2f696c688a0603fb34579cec1","Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","Ren, Y., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhou, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Liu, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Lin, L., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Li, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, H., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xia, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhao, Z., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wen, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Zhou, C., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Wang, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Yin, J., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Xu, N., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China; Liu, S., Beijing Genomics Institute, Chinese Academy of Sciences, Beijing, 101300, China","In the face of the worldwide threat of severe acute respiratory syndrome (SARS) to human life, some of the most urgent challenges are to develop fast and accurate analytical methods for early diagnosis of this disease as well as to create a safe anti-viral vaccine for prevention. To these ends, we investigated the antigenicity of the spike protein (S protein), a major structural protein in the SARS-coronavirus (SARS-CoV). Based upon the theoretical analysis for hydrophobicity of the S protein, 18 peptides were synthesized. Using Enzyme-Linked Immunosorbent Assay (ELISA), these peptides were screened in the sera from SARS patients. According to these results, two fragments of the S gene were amplified by PCR and cloned into pET-32a. Both S fragments were expressed in the BL-21 strain and further purified with an affinity chromatography. These recombinant S fragments were confirmed to have positive cross-reactions with SARS sera, either by Western blot or by ELISA. Our results demonstrated that the potential epitope regions were located at Codons 469-882 in the S protein, and one epitope site was located at Codons 599-620. Identification of antigenic regions in the SARS-CoV S protein may be important for the functional studies of this virus or the development of clinical diagnosis.",,"membrane protein; peptide fragment; recombinant protein; spike glycoprotein, coronavirus; virus antigen; virus envelope protein; article; chemistry; enzyme linked immunosorbent assay; gene vector; genetics; high performance liquid chromatography; human; immunology; mass spectrometry; metabolism; molecular cloning; molecular weight; polyacrylamide gel electrophoresis; SARS coronavirus; Antigens, Viral; Chromatography, High Pressure Liquid; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Genetic Vectors; Humans; Mass Spectrometry; Membrane Glycoproteins; Molecular Weight; Peptide Fragments; Recombinant Proteins; SARS Virus; Viral Envelope Proteins",,"Ren, Y.",,,16720229,,,"15629033","English","Genomics Proteomics Bioinformatics",Article,"Final",Open Access,Scopus,2-s2.0-2942622512
"Regula G., Scherba G., Mateus-Pinilla N.E., Lichtensteiger C.A., Miller G.Y., Weigel R.M.","56253559600;7004886311;6506670553;7003282754;7404980678;7102627545;","The impact of endemic porcine reproductive and respiratory syndrome virus and other pathogens on reproductive performance in swine",2003,"Journal of Swine Health and Production","11","1",,"13","18",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037226990&partnerID=40&md5=0fd86e88b6f526459f8468d3340a4262","Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States","Regula, G., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; Scherba, G., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; Mateus-Pinilla, N.E., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; Lichtensteiger, C.A., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; Miller, G.Y., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; Weigel, R.M., Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States","Objectives: To evaluate the impact of endemic infection with porcine reproductive and respiratory syndrome virus (PRRSV), swine influenza virus (SIV), transmissible gastroenteritis virus-porcine respiratory coronavirus (TGEV-PRCV), pseudorabies virus (PRV), Mycoplasma hyopneumoniae, and Actinobacillus pleuropneumoniae (APP) on the reproductive performance of sows. Methods: Seventeen groups of 30 to 60 sows and gilts in seven herds were monitored over a 2-year period by serological testing for the pathogens listed above. Litter size, number of stillborn (including mummies), average weaning weight, preweaning deaths, and interfarrowing interval were recorded for the sows that were tested. Multiple linear regression analyses were performed to evaluate the association of the measures of reproductive performance with serological test results. Results: Infection with PRRSV was consistently associated with poorer reproductive performance. Sows that had antibodies to PRRSV had, on average, 0.1 to 0.9 more stillborn piglets per litter than did seronegative animals. The average interfarrowing interval was 3 to 10 days longer for PRRSV-seropositive sows. A consistent correlation between reproductive performance and serological results could not be found for SIV, TGEV-PRCV, PRV, M hyopneu-moniae, or APP. Implications: Even in herds where no clinical signs of the disease are present, reproductive performance may be substantially inferior in sows with high levels of antibody against PRRSV.","Endemic infection; Porcine reproductive and respiratory syndrome virus; Reproduction; Swine","Actinobacillus pleuropneumoniae; Animalia; Coronavirus; Influenza virus; Mycoplasma hyopneumoniae; Mycoplasma pneumoniae; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Simian immunodeficiency virus; Suid herpesvirus 1; Suidae; Sus scrofa; Swine influenza virus; Transmissible gastroenteritis virus","Pejsak, Z., Stadejek, T., Markowska-Daniel, I., Clinical signs and economic losses caused by porcine reproductive and respiratory syndrome virus in a large breeding herd (1997) Vet Microbiol, 55, p. 317322; Easterday, B.C., Swine influenza (1986) Diseases of Swine. 6th Ed, pp. 244-255. , Leman AD, Straw BE, Glock RD, Mengeling WL, Penny RHC, Scholl E, eds. Ames, Iowa: The Iowa State University Press; Miller, G.Y., Kliebenstein, J.B., The economic impact of clinical transmissible gastroenteritis for swine producers participating in the Missouri mail-in-record program (1983) Prey Vet Med, 3, pp. 475-488; Ross, R.F., Mycoplasmal diseases (1986) Diseases of Swine. 6th Ed, pp. 469-483. , Leman AD, Straw BE, Glock RD, Mengeling WL, Penny RHC, Scholl E, eds. Ames, Iowa: The Iowa State University Press; Zimmerman, J.J., Yoon, K.J., Wills, R.W., Swenson, S.L., General overview of PRRSV: A perspective from the United States (1997) Vet Micro, 55, pp. 187-196; Mullan, B.P., Davies, G.T., Cutler, R.S., Simulation of the economic impact of transmissible gastroenteritis on commercial pig production in Australia (1994) Aust Vet J, 71, pp. 151-154; Poulson, D., Marsh, W.E., Morrison, R.B., Dial, G., A methodology for evaluating the financial consequences of a disease outbreak of transmissible gastroenteritis and pseudorabies virus (1993) Prev Vet Med, 16, pp. 61-63; Rougoor, C.W., Dijkhuizen, A.A., Huirne, R.B.M., Marsh, W.E., Impact of different approaches to calculate the economics of disease in pig herding (1996) Prey Vet Med, 26, pp. 315-328; Christianson, W.T., Joo, H.S., Porcine reproductive and respiratory syndrome: A review (1994) Swine Health Prod, 2, pp. 10-28; Parsons, T.D., Pitcher, P.M., Johnstone, C., Economic analysis of an epizootic of pseudorabies and subsequent production following the institution of a vaccine program in a Pennsylvania swine herd (1990) JAVMA, 197, pp. 188-191; Fedorka-Cray, P.J., Anderson, G.A., Cray, W.C., Grey, J.T., Breisch, S.A., Actinobacillus (Haemophilus) pleuropneumoniae. Part II. Virulence factors, immunity, and vaccines (1994) Comp Cont Ed Pract Vet, 16, pp. 117-120; Baysinger, A.K., Dewey, C.E., Straw, B.E., Brumm, M.C., Schmitz, J., Doster, A., Kelling, C., The effect of PRRSV on reproductive parameters in swine herds (1997) Swine Health Prod, 5, pp. 173-176; Regula, G., Lichtensteiger, C.A., Mateus-Pinilla, N.E., Scherba, G., Miller, G.Y., Weigel, R.M., Comparison of serologic testing and slaughter evaluation for assessing the effects of subclinical infection on growth in pigs (2000) JAVMA, 217, pp. 888-895; Beal, V.C., (1983) Regulatory Statistics. Vol 1. 6th Ed, pp. 19-21. , United States Department of Agriculture, Animal and Plant Health Inspection Service, Veterinary Services; Whittemore, C., (1993) The Science and Practice of Pig Production, , Essex, United Kingdom: Longman Scientific and Technical; Neter, J., Wasserman, W., Kutner, M.H., (1985) Applied Linear Statistical Models: Regression, Analysis of Variance, and Experimental Designs, , Homewood, Illinois: Irwin; Goldberg, T.L., Weigel, R.M., Hahn, E.C., Scherba, G., Associations between genetics, herd characteristics and clinical disease in field outbreaks of porcine reproductive and respiratory syndrome virus (2000) Prey Vet Med, 43, pp. 293-302; (1992) National Swine Survey: Morbidity/mortality and Health Management of Swine in the United States, , Fort Collins, Colo: Centers for Epidemiology and Animal Health, Animal and Plant Health Inspection Service. United States Department of Agriculture Publication N101. 0192; (1995) Swine '95: Grower/Finisher, Part I: Reference of 1995 Swine Management Practices, , Fort Collins, Colo: Centers for Epidemiology and Animal Health, Animal and Plant Health Inspection Service. United States Department of Agriculture Publication N 186. 995","Weigel, R.M.; Dept. of Veterinary Pathobiology, College of Veterinary Medicine, University of Illinois, 2001 S Lincoln Avenue, Urbana, IL 61802, United States; email: weigel@uiuc.edu",,,1537209X,,,,"English","J. Swine Health Prod.",Article,"Final",,Scopus,2-s2.0-0037226990
"Kapitonov V.V., Jurka J.","7006217715;7007141579;","The esterase and PHD domains in CR1-like non-LTR retrotransposons",2003,"Molecular Biology and Evolution","20","1",,"38","46",,57,"10.1093/molbev/msg011","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037225253&doi=10.1093%2fmolbev%2fmsg011&partnerID=40&md5=64a18ffa879102cbd64e906928a8e950",,"Kapitonov, V.V.; Jurka, J.","Most active non-LTR (long terminal repeat) retrotransposons carry two open reading frames (ORFs) encoding ORF1p and ORF2p proteins. The ORF2p proteins are relatively well studied and are known to contain endonuclease/reverse transcriptase domains. At the same time, the biological function of ORF1p proteins remains poorly understood, except in that they nonspecifically bind single-stranded mRNA/DNA molecules. CR1-like elements form the most widely distributed clade/superfamily of non-LTR retrotransposons. We found that ORF1p proteins encoded by diverse CR1-like elements contain conserved esterase domain (ES) or plant homeodomain (PHD). This indicates that CR1-like ORF1p proteins are either lipolytic enzymes or are involved in protein-protein interactions related to chromatin remodeling. Sequence conservation of ES suggests that interaction with cellular membranes is an important phase in life circles of CR1-like elements. Presumably such interaction helps in penetrating host cells. As a consequence, the presence of multiple young CR1 families characterized by ∼10% intrafamily and 40% interfamily identities may be explained by a relatively frequent horizontal transfer of these CR1-like elements. Unexpectedly, ES links together non-LTR retrotransposons and single-stranded RNA viruses like influenza C and coronaviruses, which are known to depend on their own ES.","CR1 clade; Esterase; Non-LTR retrotransposon; ORF1p; PHD homeodomain","esterase; homeodomain protein; vegetable protein; virus RNA; article; controlled study; Coronavirus; Drosophila; host cell; Influenza virus C; lipolysis; long terminal repeat; nonhuman; open reading frame; protein domain; protein family; protein protein interaction; retroposon; sequence analysis; zebra fish; Coronavirus; Danio rerio; Influenza virus; Influenzavirus C; RNA viruses","Aasland, R., Gibson, T.J., Stewart, A.F., The PHD finger: Implications for chromatin-mediated transcriptional regulation (1995) Trends Biochem. Sci., 20, pp. 56-59; Aasland, R., Stewart, A.F., The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1 (1995) Nucleic Acids Res., 23, pp. 3168-3174; Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res., 25, pp. 3389-3402; Arpigny, J.L., Jaeger, K.E., Bacterial lipolytic enzymes: Classification and properties (1999) Biochem. J., 343, pp. 177-183; Bailey, T.L., Grundy, W.N., Classifying proteins by family using the product of correlated P-values (1999) Proceedings of the Third International Conference on Computational Molecular Biology (RECOMB99), pp. 10-14. , P. Istrail, P. Pevzner, and M. Waterman, eds. ACM, New York; Bateman, A., Bimey, E., Cerruti, L., Durbin, R., Etwiller, L., Eddy, S.R., Griffiths-Jones, S., Sonnhammer, E.L., The Pfam protein families database (2002) Nucleic Acids Res., 30, pp. 276-280; Berg, D.E., Howe, M.H., (1987) Mobile DNA, , American Society for Microbiology Press, Washington, DC; Besansky, N.J., A retrotransposable element from the mosquito Anopheles gambiae (1990) Mol. Cell. Biol., 10, pp. 863-871; Besansky, N.J., Bedell, J.A., Mukabayire, O., Q: A new retrotransposon from the mosquito Anopheles gambiae (1994) Insect Mol. Biol., 3, pp. 49-56; Burch, J.B., Davis, D.L., Haas, N.B., Chicken repeat 1 elements contain a pol-like open reading frame and belong to the non-long terminal repeat class of retrotransposons (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 8199-8203; Capili, A.D., Schultz, D.C., Rauscher, I.F., Borden, K.L., Solution structure of the PHD domain from the KAP-1 corepressor: Structural determinants for PHD, RING and LIM zinc-binding domains (2001) EMBO J., 20, pp. 165-177; Capy, P., Bazin, C., Higuet, D., Langin, T., (1998) Dynamics and Evolution of Transposable Elements, , Chapman & Hall, New York; Chaboissier, M.C., Finnegan, D., Bucheton, A., Retrotransposition of the I factor, a non-long terminal repeat retrotransposon of Drosophila, generates tandem repeats at the 3′ end (2000) Nucleic Acids Res., 28, pp. 2467-2472; Coffin, J.M., Hughes, S.H., Varmus, H.E., (1997) Retroviruses, , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York; Coscoy, L., Sanchez, D.J., Ganem, D., A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition (2001) J. Cell Biol., 155, pp. 1265-1273; Craig, N.L., Unity in transposition reactions (1995) Science, 270, pp. 253-254; Dalrymple, B.P., Cybinski, D.H., Layton, I., McSweeney, C.S., Xue, G.P., Swadling, Y.J., Lowry, J.B., Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases (1997) Microbiology, 143, pp. 2605-2614; Dawson, A., Hartswood, E., Paterson, T., Finnegan, D.J., A LINE-like transposable element in Drosophila, the I factor, encodes a protein with properties similar to those of retroviral nucleocapsids (1997) EMBO J., 16, pp. 4448-4455; Drablos, F., Petersen, S.B., Identification of conserved residues in family of esterase and lipase sequences (1997) Methods Enzymol., 284, pp. 28-61; Drew, A.C., Brindley, P.J., A retrotransposon of the non-long terminal repeat class from the human blood fluke Schistosoma mansoni. Similarities to the chicken-repeat-1-like elements of vertebrates (1997) Mol. Biol. Evol., 14, pp. 602-610; Dunphy, J.T., Linder, M.E., Signalling functions of protein palmitoylation (1998) Biochim. Biophys. Acta, 1436, pp. 245-261; Eickbush, D.G., Luan, D.D., Eickbush, T.H., Integration of Bombyx mori R2 sequences into the 28S ribosomal RNA genes of Drosophila melanogaster (2000) Mol. Cell. Biol., 20, pp. 213-223; Gibbons, R.J., Bachoo, S., Picketts, D.J., Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain (1997) Nat. Genet., 17, pp. 146-148; Gough, J., Karplus, K., Hughey, R., Chothia, C., Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure (2001) J. Mol. Biol., 313, pp. 903-919; Haas, N.B., Grabowski, J.M., North, J., Moran, J.V., Kazazian, H.H., Burch, J.B., Subfamilies of CR1 non-LTR retrotransposons have different 5′ UTR sequences but are otherwise conserved (2001) Gene, 265, pp. 175-183; Haas, N.B., Grabowski, J.M., Sivitz, A.B., Burch, J.B., Chicken repeat 1 (CR1) elements, which define an ancient family of vertebrate non-LTR retrotransposons, contain two closely spaced open reading frames (1997) Gene, 197, pp. 305-309; Herrler, G., Rott, R., Klenk, H.D., Muller, H.P., Shukla, A.K., Schauer, R., The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase (1985) EMBO J., 4, pp. 1503-1506; Ho, Y.S., Swenson, L., Derewenda, U., Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer (1997) Nature, 385, pp. 89-93; Hohjoh, H., Singer, M.F., Sequence-specific single-strand RNA binding protein encoded by the human LINE-1 retrotransposon (1997) EMBO J., 16, pp. 6034-6043; Holmes, S.E., Singer, M.F., Swergold, G.D., Studies on p40, the leucine zipper motif-containing protein encoded by the first open reading frame of an active human LINE-1 transposable element (1992) J. 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Evol., 14, pp. 1206-1217; Kapitonov, V.V., Jurka, J., Molecular paleontology of transposable elements from Arabidopsis thaliana (1999) Genetica, 107, pp. 27-37; Rolling-circle transposons in eukaryotes (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 8714-8719; Kehle, J., Beuchle, D., Treuheit, S., Christen, B., Kennison, J.A., Bienz, M., Muller, J., dMi-2, a hunchback-interacting protein that functions in polycomb repression (1998) Science, 282, pp. 1897-1900; Koipally, J., Renold, A., Kim, J., Georgopoulos, K., Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes (1999) EMBO J., 18, pp. 3090-3100; Kolosha, V.O., Martin, S.L., In vitro properties of the first ORF protein from mouse LINE-1 support its role in ribonucleoprotein particle formation during retrotransposition (1997) Proc. Natl. Acad. Sci. 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"Foley J.E., Rand C., Leutenegger C.","7402872921;7006599246;7006706489;","Inflammation and changes in cytokine levels in neurological feline infectious peritonitis",2003,"Journal of Feline Medicine and Surgery","5","6",,"313","322",,40,"10.1016/S1098-612X(03)00048-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344393519&doi=10.1016%2fS1098-612X%2803%2900048-2&partnerID=40&md5=9b946b1cf034a04c0d59df3c725b3071","Department of Medicine/Epidemiology, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Center for Campanion Animal Health, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Foley, J.E., Department of Medicine/Epidemiology, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States, Center for Campanion Animal Health, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Rand, C., Center for Campanion Animal Health, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States; Leutenegger, C., Department of Medicine/Epidemiology, Davis School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Feline infectious peritonitis (FIP) is a progressive, fatal, predominantly Arthus-type immune-mediated disease that is triggered when cats are infected with a mutant enteric coronavirus. The disease presents variably with multiple organ failure, seizures, generalized effusion, or shock. Neurological FIP is clinically and pathologically more homogeneous than systemic 'wet' or 'dry' FIP; thus, comparison of cytokine profiles from cats with neurological FIP, wet FIP, and non-FIP neurological disease may provide insight into some baseline characteristics relating to the immunopathogenesis of neurological FIP. This study characterizes inflammation and changes in cytokines in the brain tissue of FIP-affected cats. Cellular infiltrates in cats with FIP included lymphocytes, plasma cells, neutrophils, macrophages, and eosinophils. IL-1β, IL-6, IL-12, IL-18, TNF-α, macrophage inhibitory protein (MIP)-1α, and RANTES showed no upregulation in the brains of control cats, moderate upregulation in neurological FIP cats, and very high upregulation in generalized FIP cats. Transcription of IFN-γ appeared upregulated in cats with systemic FIP and slightly downregulated in neurological FIP. In most cytokines tested, variance was extremely high in generalized FIP and much less in neurological FIP. Principal components analysis was performed in order to find the least number of 'components' that would summarize the cytokine profiles in cats with neurological FIP. A large component of the variance (91.7%) was accounted for by levels of IL-6, MIP-1α, and RANTES. These findings provide new insight into the immunopathogenesis of FIP and suggest targets for immune therapy of this disease. © 2003 ESFM and AAFP. Published by Elsevier Ltd. All rights reserved.",,"cytokine; gamma interferon; interleukin 1; interleukin 12; interleukin 18; interleukin 6; macrophage migration inhibition factor; RANTES; tumor necrosis factor alpha; animal tissue; article; bacterial peritonitis; brain tissue; cat disease; cell infiltration; clinical feature; controlled study; down regulation; effusion; eosinophil; immunopathogenesis; lymphocyte; macrophage; multiple organ failure; neutrophil; nonhuman; plasma cell; principal component analysis; reverse transcription polymerase chain reaction; seizure; serology; shock; upregulation; Coronavirus; Enteric coronavirus; Felidae; Felis catus","Akira, S., Taga, T., Kishimoto, T., Interleukin-6 in biology and medicine (1993) Advances in Immunology, 54, pp. 1-78; August, J., Feline infectious peritonitis: An immune-mediated coronaviral vasculitis (1984) Veterinary Clinics of North America Small Animal Practice, 14, pp. 971-984; Boyd, N.K., Cohen, N.D., Lim, W.S., Martens, R.J., Chaffin, M.K., Ball, J.M., Temporal changes in cytokine expression of foals during the first month of life (2003) Veterinary Immunology and Immunopathology, 92, pp. 75-85; 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Saunders Ltd",1098612X,,,"14623200","English","J. Feline Med. Surg.",Article,"Final",,Scopus,2-s2.0-0344393519
"Chen H.I., Kao S.J., Wang D., Lee R.P., Su C.F.","35317001200;7202173675;7407075899;7408203465;7402819440;","Acute respiratory distress syndrome",2003,"Journal of Biomedical Science","10","6",,"588","592",,36,"10.1159/000073523","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242362727&doi=10.1159%2f000073523&partnerID=40&md5=bea931b3cdc83afec98382a5bd6f29a5","Institute of Medical Sciences, Tzu Chi University, Hualien, Taiwan; Department of Internal Medicine, Shin Kong Wu Ho-Su Memorial Hospital, Taipei, Taiwan; Department of Nursing, Tzu Chi College of Technology, Hualien, Taiwan; Institute of Medical Sciences, Department of Nursing, Hualien, Taiwan; Department of Neurosurgery, Tzu Chi Hospital and University, Hualien, Taiwan; Institute of Medical Sciences, Tzu Chi University, 701, Section 3, Chung Yan Road, Hualien, 97004, Taiwan","Chen, H.I., Institute of Medical Sciences, Tzu Chi University, Hualien, Taiwan, Institute of Medical Sciences, Tzu Chi University, 701, Section 3, Chung Yan Road, Hualien, 97004, Taiwan; Kao, S.J., Department of Internal Medicine, Shin Kong Wu Ho-Su Memorial Hospital, Taipei, Taiwan; Wang, D., Department of Nursing, Tzu Chi College of Technology, Hualien, Taiwan; Lee, R.P., Institute of Medical Sciences, Department of Nursing, Hualien, Taiwan; Su, C.F., Department of Neurosurgery, Tzu Chi Hospital and University, Hualien, Taiwan","Acute respiratory distress syndrome (ARDS) can be associated with various disorders. Among these, coronavirus infection may cause life-threatening severe acute respiratory syndrome (SARS). In this review, we present animal models and techniques for the study of ARDS, and discuss the roles and possible mechanisms of various chemical factors, including nitric oxide (NO). Our early work revealed that cerebral compression elicits severe hemorrhagic pulmonary edema (PE), leading to central sympathetic activation that results in systemic vasoconstriction. The consequence of systemic vasoconstriction is volume and pressure loading in the pulmonary circulation. Vasodilators, but not oxidant radical scavengers, are effective in the prevention of centrogenic PE. In isolated perfused lung, exogenous and endogenous NO enhances lung injury following air embolism and ischemia/reperfusion. In contrast, NO synthase (NOS) inhibitors reverse such lung injury. Although NO is important in maintaining vasodilator tone, hypoxia-induced pulmonary vasoconstriction is accompanied by an increase instead of a decrease in NO release. In animal and isolated lung studies, endotoxin produces acute lung injury that is associated with increases in cytokines and inducible NOS mRNA expression, suggesting that NO is toxic to the lung in endotoxin shock. Recently, we reported several rare cases that indicate that ARDS in patients with Japanese B encephalitis, lymphangitis with breast cancer and fat embolism is caused by different mechanisms. Our early and recent studies on ARDS and PE may provide information for clinical practice and the understanding of the pathogenesis of SARS. Copyright © 2003 National Science Council, ROC and S. Karger AG, Basel.","Acute respiratory distress syndrome; Lung injury; Nitric oxide; Pulmonary edema","cytokine; messenger RNA; nitric oxide; nitric oxide donor; nitric oxide synthase; nitric oxide synthase inhibitor; scavenger; alpha adrenergic receptor blocking agent; arginine; beta adrenergic receptor blocking agent; bretylium; dexamethasone; endotoxin; glyceryl trinitrate; inducible nitric oxide synthase; mecaprine; n(g) nitroarginine methyl ester; nitric oxide; nitroprusside sodium; phenoxybenzamine; phentolamine; respine; scavenger; thiourea derivative; unclassified drug; vasodilator agent; adult respiratory distress syndrome; air embolism; brain cortex; drug mechanism; gene expression; lung edema; lung infarction; lung injury; lung perfusion; lung pressure; lung vasoconstriction; nonhuman; priority journal; regulatory mechanism; respiratory distress syndrome; review; septic shock; sympathetic tone; vasoconstriction; vasodilatation; adult respiratory distress syndrome; animal; disease model; 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Hsu, K., Wang, D., Chang, M.L., Wu, C.P., Chen, H.I., Pulmonary edema induced by phorbol myristate acetate is attenuated by compounds that increase intracellular cAMP (1996) Res Exp Med, 196, pp. 17-28; Hsu, K., Wang, D., Wu, S.Y., Shen, C.Y., Chen, H.I., Ischemia-reperfusion lung injury attenuated by ATP-MgCl2 in rats (1994) J Appl Physiol, 76, pp. 545-552; Hsu, Y.H., Kao, S.J., Lee, R.P., Chen, H.I., Acute pulmonary oedema: Rare causes and possible mechanisms (2003) Clin Sci, 104, pp. 259-264; Hu, C.T., Chang, K.C., Wu, C.Y., Chen, H.I., Acute effects of nitric oxide blockade with L-NAME on arterial hemodynamics in the rat (1997) Br J Pharmacol, 122, pp. 1237-1243; Kao, J.S., Peng, T.C., Lee, R.P., Hsu, K., Chen, C.F., Huang, Y.K., Wang, D., Chen, H.I., Nitric oxide mediates lung injury induced by ischemia-reperfusion in rats (2003) J Biomed Sci, 10, pp. 58-64; Ksiazek, T.G., Erman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1984-1992; Lee, R.P., Wang, D., Kao, S.J., Chen, H.I., The lung is the major site that produces nitric oxide to induce acute pulmonary oedema in endotoxin shock (2001) Clin Exp Pharmacol Physiol, 28, pp. 315-320; Lee, R.P., Wang, D., Lin, N.T., Chen, H.I., Physiological and chemical indicators for early and late stages of sepsis in conscious rats (2002) J Biomed Sci, 9, pp. 613-621; Lee, R.P., Wang, D., Lin, N.T., Chou, Y.W., Chen, H.I., A modified technique for tail cuff pressure measurement in unrestrained conscious rats (2002) J Biomed Sci, 9, pp. 424-427; Moncada, S., Palmer, R.M.J., Higgs, E.A., Nitric oxide: Physiology, pathophysiology and pharmacology (1991) Pharmacol Rev, 43, pp. 109-142; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1993-2003; Shen, C.Y., Wang, D., Chang, M.L., Hsu, K., Protective effect of mepacrine on hypoxia-reoxygenation-induced acute lung injury in rats (1995) J Appl Physiol, 78, pp. 225-231; Stamler, J.S., Loh, E., Roddy, M.A., Currie, K.E., Creager, M.A., Nitric oxide regulates basal systemic and pulmonary vascular resistance in healthy humans (1994) Circulation, 89, pp. 2035-2040; Stewart, T.E., Valenza, F., Ribeiro, S.P., Wener, A.D., Volgyesi, G., Mullen, J.B., Slutsky, A.S., Increased nitric oxide in exhaled gas as an early marker of lung inflammation in a model of sepsis (1995) Am J Respir Crit Care Med, 151, pp. 713-718; Su, C.F., Hu, C.T., Chen, H.I., Effects of intracranial hypertension on steady and pulsatile hemodynamics in dogs (1999) Clin Exp Pharmacol Physiol, 26, pp. 898-902; Szabo, C., Mitchell, J.A., Thiemermann, C., Vane, J.R., Nitric oxide mediated hyporeactivity to noradrenaline precedes the induction of nitric oxide synthase in endotoxin shock (1993) Br J Pharmacol, 108, pp. 786-792; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1975-1983; Wang, D., Hsu, K., Hwang, C.P., Chen, H.I., Measurement of nitric oxide release in the isolated perfused rat lung (1995) Biochem Biophys Res Commun, 208, pp. 1016-1020; Wang, D., Li, M.H., Hsu, K., Shen, C.Y., Chen, H.I., Air embolism-induced lung injury in isolated rat lungs (1992) J Appl Physiol, 72, pp. 1235-1242; Wang, D., Wei, J., Hsu, K., Jau, J.C., Lieu, M.W., Chao, T.J., Chen, H.I., Effects of nitric oxide synthase inhibitors on systemic hypotension, cytokines and inducible nitric oxide synthase expression and lung injury following endotoxin administration in rats (1999) J Biomed Sci, 6, pp. 28-35; Wright, C.E., Rees, D.D., Moncada, S., Protective and pathological roles of nitric oxide in endotoxin shock (1992) Cardiovasc Res, 26, pp. 48-57","Chen, H.I.; Institute of Medical Sciences, Tzu Chi University, 701, Section 3, Chung Yan Road, Hualien, 97004, Taiwan; email: chenhi@mail.tcu.edu.tw",,"BioMed Central Ltd.",10217770,,JBCIE,"14576460","English","J. Biomed. Sci.",Review,"Final",,Scopus,2-s2.0-0242362727
"Hoet A.E., Nielsen P.R., Hasoksuz M., Thomas C., Wittum T.E., Saif L.J.","6602855175;7402902693;6603236044;7404413122;7004009529;7102226747;","Detection of bovine torovirus and other enteric pathogens in feces from diarrhea cases in cattle",2003,"Journal of Veterinary Diagnostic Investigation","15","3",,"205","212",,29,"10.1177/104063870301500301","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037639085&doi=10.1177%2f104063870301500301&partnerID=40&md5=773c6206de2cbea5d3b34733a7b92e28","Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH, United States; Depto. Enfermedades Transmisibles, Facultad de Ciencias Veterinarias, Universidad del Zulia, Maracaibo, Venezuela; Department of Microbiology, Veterinary Faculty, Istanbul University, Avcilar 34850, Istanbul, Turkey","Hoet, A.E., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States, Depto. Enfermedades Transmisibles, Facultad de Ciencias Veterinarias, Universidad del Zulia, Maracaibo, Venezuela; Nielsen, P.R., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Hasoksuz, M., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States, Department of Microbiology, Veterinary Faculty, Istanbul University, Avcilar 34850, Istanbul, Turkey; Thomas, C., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States; Wittum, T.E., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States, Dept. of Vet. Preventive Medicine, Ohio State University, Columbus, OH, United States; Saif, L.J., Dept. of Vet. Preventive Medicine, OH Agric. R. and D. Center, Ohio State University, Wooster, OH 44691, United States","The objectives of this study were to determine the prevalence of bovine torovirus (BoTV) in bovine fecal samples from diarrhea cases submitted to the Ohio Animal Disease Diagnostic Laboratory (ADDL) and to assess if a relationship exists between BoTV and the other enteric pathogens detected. From November 1999 to May 2001, 259 specimens from 53 calves (≤6 months old), 27 young adults (≤2 years), 125 adults (≥2 years), and 54 animals of unknown age were examined by an antigen-capture enzyme-linked immunosorbent assay (ELISA) and reverse transcriptase-polymerase chain reaction (RT-PCR) assay developed to detect BoTV. Testing for other enteric pathogens was performed by ADDL, and the results were analyzed with the BoTV data. The BoTV was detected using ELISA or RT-PCR in 9.7% (25/259) of the clinical samples, 56% (14/25) of which were from calves (P < 0.001) representing 26.4% (14/53) of the calves tested. Of the BoTV-positive calves, 71% (10/14) were less than 3 weeks of age. In 11/25 positive specimens, BoTV was the only pathogen detected among those examined. Other enteric organisms detected alone or in combination with BoTV in calf samples were rotavirus, coronavirus, Salmonella spp., Cryptosporidium spp., and Giardia spp.; but no consistent association between BoTV and these organisms was observed. In summary, BoTV was detected in fecal samples from cattle with diarrhea, principally in young calves less than 3 weeks of age. Future studies of infectious diarrhea in cattle should also include assays for this etiologic agent.",,"Animalia; Bos taurus; Bovinae; Bovine torovirus; Coronavirus; Cryptosporidium; Cryptosporidium; Giardia; Giardia; Rotavirus; Salmonella; Salmonella; Torovirus; virus RNA; aging; animal; animal disease; article; cattle; cattle disease; diarrhea; enzyme linked immunosorbent assay; feces; female; genetics; isolation and purification; male; prevalence; reverse transcription polymerase chain reaction; season; Torovirus; United States; virology; virus infection; Aging; Animals; Cattle; Cattle Diseases; Diarrhea; Enzyme-Linked Immunosorbent Assay; Feces; Female; Male; Ohio; Prevalence; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; Seasons; Torovirus; Torovirus Infections","Ali, A., Reynolds, D.L., Characterization of the stunting syndrome agent: Relatedness to known viruses (2000) Avian Dis, 44, pp. 45-50; Beards, G.M., Brown, D.W.G., Green, J., Preliminary characterization of torovirus-like particles of humans: Comparison with Berne virus of horses and Breda virus of calves (1986) J Med Virol, 20, pp. 67-78; Bredenbeek, P.J., Snijder, E.J., Den Boon, J.A., The polymerase gene of corona- and toroviruses: Evidence for an evolutionary relationship (1990) Coronaviruses and Their Diseases, pp. 307-316. , ed. Cavanagh D, Brown TDK, Plenum Press, New York, NY; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch Virol, 143, pp. 629-633; Lahm, C., What are toroviruses? (1999) Molecular Characterization of Ungulate Toroviruses, pp. 7-20. , ed. Cornelissen LAHM, Universiteit Utrecht, Utrecht, The Netherlands; De La Fuente, R., García, A., Ruiz-Santa-Quiteria, J.A., Proportional morbidity rates of enteropathogens among diarrheic dairy calves in central Spain (1998) Prev Vet Med, 36, pp. 145-152; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin Virol, 8, pp. 33-47; Duckmanton, L.M., Carman, S., Nagy, E., Detection of bovine torovirus in fecal specimens of calves with diarrhea from Ontario farms (1998) J Clin Microbiol, 36, pp. 1266-1270; Duckmanton, L.M., Luan, Bo., Devenish, J., Characterization of torovirus from human fecal specimens (1997) Virology, 239, pp. 158-168; Fagerland, J.A., Pohlenz, J.F.L., Woode, G.N., A morphological study of the replication of Breda virus (proposed family Toroviridae) in bovine intestinal cells (1986) J Gen Virol, 67, pp. 1293-1304; Frey, A., Canzio, J.D., Zurakowski, D., A statistically defined endpoint titer determination method for immunoassays (1998) J Immunol Methods, 221, pp. 35-41; García, A., Ruiz-Santa-Quiteria, J.A., Orden, J.A., Rotavirus and concurrent infections with other enteropathogens in neonatal diarrheic dairy calves in Spain (2000) Comp Immunol Microbiol Infect Dis, 23, pp. 175-183; Hoet, A.E., Cho, K.O., Chang, K.O., Enteric and nasal shedding of bovine torovirus (Breda virus) in feedlot cattle (2002) Am J Vet Res, 63, pp. 342-348; Hoet, A.E., Cho, K.O., Loerch, S.C., Enteric shedding of bovine torovirus (Breda virus) by feedlot cattle (2000) 81st Conference of Research Workers in Animal Diseases, , Chicago, IL. #77, Iowa State University Press, Ames, IA; Hoet, A.E., Kyeong-Ok, C., Saif, L.J., Comparison of ELISA and RT-PCR versus immune electron microscopy for detection of bovine torovirus (Breda virus) in calf fecal specimens J Vet Diagn Invest, 15 (2), pp. 100-106. , In press; Horzinek, M.C., Weis, M., Toroviruses (1990) Viral Diarrheas of Man and Animals, pp. 253-262. , ed. Saif LJ, Theil KW, CRC Press, Boca Raton, FL; Horzinek, M.C., Weiss, M., Ederveen, J., Toroviridae: A proposed new family of enveloped RNa viruses (1987) Ciba Foundation Symposium, pp. 162-174. , Novel diarrhoea viruses. ed. Brock G, Whelan J, John Wiley & Sons, Chichester, UK; Koopmans, M., Cremers, H., Woode, G.N., Breda virus (Toroviridae) infection and systemic antibody response in sentinel calves (1990) Am J Vet Res, 51, pp. 1443-1448; Koopmans, M., Horzinek, M.C., Toroviruses of animals and humans: A review (1994) Adv Virus Res, 43, pp. 233-273; Koopmans, M., Wuijckhuise-Sjouke, Lv., Schukken, Y.H., Association of diarrhea in cattle with torovirus infections on farms (1991) Am J Vet Res, 52, pp. 1769-1773; Kroneman, A., Cornelissen, L., Horzinek, M.C., Identification and characterization of a porcine torovirus (1998) J Virol, 72, pp. 3507-3511; Kuo, L., Harty, J.T., Erickson, L., A nested set of eight RNAs is formed in macrophages infected with lactate dehydrogenase-elevating virus (1991) J Virol, 65, pp. 5118-5123; Lamouliatte, F., Pasquier, P.Du., Rossi, F., Studies on bovine Breda virus (1987) Vet Microbiol, 15, pp. 261-278; Lucchelli, A., Lance, S.E., Bartlett, P.B., Prevalence of bovine group a rotavirus shedding among dairy calves in Ohio (1992) Am J Vet Res, 53, pp. 169-174; Pohlenz, J.F., Woode, G.N., Cheville, N.F., Morphologic lesions in the intestinal mucosa of newborn calves reproduced by unclassified virus (""Breda-virus"") (1982) Proceedings of XII World Congress of Cattle Disease, pp. 252-254. , Utrecht, the Netherlands; Pohlenz, J.F.L., Cheville, N.F., Woode, G.N., Cellular lesions in intestinal mucosa of gnotobiotic calves experimentally infected with a new unclassified bovine virus (Breda virus) (1984) Vet Pathol, 21, pp. 407-417; Radostits, O.M., Blood, D.C., Gay, C.C., Diseases of the alimentary tract (2000) Veterinary Medicine: A Textbook of the Diseases of Cattle, Sheep, Pigs, Goats and Horses, 9th Ed., pp. 234-246. , Saunders, New York, NY; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in southern Britain (1986) Vet Rec, 119, pp. 34-39; Saif, L.J., Comparative aspects of enteric viral infections (1990) Viral Diarrheas of Man and Animal, pp. 9-34. , ed. Saif LJ, Theil KW, CRC Press, Boca Raton, FL; Saif, L.J., Redman, D.R., Theil, K.W., Studies on an enteric ""Breda"" virus in calves (1981) 62nd Conference for Research Workers of Animal Diagnosis, , Abstract 236; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J Vet Diagn Invest, 8, pp. 99-105; Snijder, E.J., Ederveen, J., Spaan, W.J.M., Characterization of Berne virus genomic and messenger RNAs (1988) J Gen Virol, 69, pp. 2135-2144; Snijder, E.J., Horzinek, M.C., Toroviruses: Replication, evolution and comparison with other members of the coronaviruslike superfamily (1993) J Gen Virol, 74, pp. 2305-2316; Snijder, E.J., Horzinek, M.C., Spaan, W.J.M., The coronaviruslike superfamily (1994) Coronaviruses: Molecular Biology and Virus-host Interactions, pp. 235-244. , ed. Laude H, Vautherot JF, Plenum Press, New York, NY; Snijder, E.J., Spaan, W.J.M., The coronaviruslike superfamily (1995) The Coronaviridae, pp. 239-255. , ed. Siddell SG, Plenum Press, New York, NY; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Advances in Veterinary Science and Comparative Medicine, 29, pp. 103-179. , ed. Cornelius CE, Simpson CF, Orlando, Academic Press, FL; Woode, G.N., Etiology of enteric viral infections of calves: Pathological and clinical aspects (1982) 12th World Congress on Cattle Diseases, pp. 201-208. , Utrecht, the Netherlands; Woode, G.N., Breda and Breda-like viruses: Diagnosis, pathology and epidemiology (1987) Ciba Foundation Symposium, pp. 175-191. , Novel diarrhoea viruses. ed. Brock G, Whelan J, John Wiley & Sons, Chichester, UK; Woode, G.N., The toroviruses: Bovine (Breda virus) and equine (Berne virus) and the torovirus-like agents of humans and animals (1994) Viral Infections of the Gastrointestinal Tract, pp. 581-602. , ed. Kapikian AZ, Marcel Dekker, New York, NY; Woode, G.N., Pohlenz, J.F.L., Kelso-Gourley, N.E., Astrovirus and Breda virus infections of dome cell epithelium of bovine ileum (1984) J Clin Microbiol, 19, pp. 623-630; Woode, G.N., Reed, D.E., Runnels, P.L., Studies with an unclassified virus isolated from diarrheic calves (1982) Vet Microbiol, 7, pp. 221-240; Woode, G.N., Saif, L.J., Quesada, M., Comparative studies on three isolates of Breda virus of calves (1985) Am J Vet Res, 46, pp. 1003-1010","Hoet, A.E.; Depto. Enfermedades Transmisibles, Facultad de Ciencias Veterinarias, Universidad del Zulia, Maracaibo, Venezuela",,"American Assoc. of Veterinary Laboratory Diagnosticians",10406387,,,"12735342","English","J. Vet. Diagn. Invest.",Article,"Final",Open Access,Scopus,2-s2.0-0037639085
"Wong P.-N., Mak S.-K., Lo K.-Y., Tong G.M.W., Wong Y., Watt C.-L., Wong A.K.M.","7403980442;7102103296;7402101598;36060391100;35093426600;7005965559;7403147057;","Clinical Presentation and Outcome of Severe Acute Respiratory Syndrome in Dialysis Patients",2003,"American Journal of Kidney Diseases","42","5",,"1075","1081",,9,"10.1016/j.ajkd.2003.08.005","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142219909&doi=10.1016%2fj.ajkd.2003.08.005&partnerID=40&md5=4859239ea9504863a3a5fec312c650e3","Renal Unit, Dept. of Medicine and Geriatrics, Kwong Wah Hospital, 25 Waterloo Road, Kowloon, Hong Kong","Wong, P.-N., Renal Unit, Dept. of Medicine and Geriatrics, Kwong Wah Hospital, 25 Waterloo Road, Kowloon, Hong Kong; Mak, S.-K.; Lo, K.-Y.; Tong, G.M.W.; Wong, Y.; Watt, C.-L.; Wong, A.K.M.","There was a major outbreak of severe acute respiratory syndrome (SARS) affecting more than 300 patients occurring in a private housing estate in Hong Kong, in which an infected renal patient was suspected to be the primary source. It is unknown whether renal patients would represent a distinct group of patients who share some characteristics that could predispose them to have higher infectivity. In this context, we have encountered 4 dialysis patients contracting SARS in a minor outbreak, which involved 11 patients and 4 health care workers, in a medical ward of a regional hospital. Of these 4 dialysis patients, 1 patient was receiving hemodialysis while the other 3 patients were on continuous ambulatory peritoneal dialysis. Fever and radiological changes were their dominant presenting features. All were having positive results for SARS-associated coronavirus ribonucleic acid by reverse transcriptase-polymerase chain reaction performed on their nasopharyngeal aspirates or stool samples. It appeared that treatment with high-dose intravenous ribavirin and corticosteroids could only resolve the fever, but it could not stop the disease progression. All 4 patients developed respiratory failure requiring mechanical ventilation on days 9 through 12. At the end, all of the patients died from sudden cardiac arrest, which was associated with acute myocardial infarction in 2 cases. From this small case series, it appeared that dialysis patients might have an aggressive clinical course and poor outcome after contracting SARS. However, a large-scale study is required to further examine this issue, and further investigation into the immunologic abnormalities associated with the uremic state in this group of patients is also warranted. © 2003 by the National Kidney Foundation, Inc.","Dialysis; Outcome; Presentation; Severe acute respiratory syndrome (SARS)","antivirus agent; corticosteroid; hydrocortisone; methylprednisolone; ribavirin; acute disease; adult; aged; article; case report; chill; clinical article; clinical feature; continuous ambulatory peritoneal dialysis; Coronavirus; coughing; diabetes mellitus; dialysis; disease severity; dyspnea; female; fever; human; infection control; kidney disease; kidney failure; mortality; myalgia; respiratory tract infection; reverse transcription polymerase chain reaction; rigor; severe acute respiratory syndrome; thorax radiography; treatment outcome; virus detection; virus infection","(2003) Multicountry Outbreak-Update 34 - Unanswered Questions: A Critical Point in the Evolution of SARS, , http://www.who.int/csr/sars/archive/2003_04_19/en/; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Atypical Pneumonia, , http://www.info.gov.hk/dh/diseases/ap.htm; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Pesanti, E.L., Immunologic defects and vaccination in patients with chronic renal failure (2001) Infect Dis Clin North Am, 15, pp. 813-832; Hon, K.L., Leung, C.W., Cheng, W.T., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703","Wong, P.-N.; Renal Unit, Dept. of Medicine and Geriatrics, Kwong Wah Hospital, 25 Waterloo Road, Kowloon, Hong Kong; email: apnwong@yahoo.com",,"W.B. Saunders",02726386,,AJKDD,"14582052","English","Am. J. Kidney Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0142219909
"Pasternak A.O., Van den Born E., Spaan W.J.M., Snijder E.J.","57189016387;6506651119;7007172944;7006058325;","The stability of the duplex between sense and antisense transcription-regulating sequences is a crucial factor in arterivirus subgenomic mRNA synthesis",2003,"Journal of Virology","77","2",,"1175","1183",,39,"10.1128/JVI.77.2.1175-1183.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037223731&doi=10.1128%2fJVI.77.2.1175-1183.2003&partnerID=40&md5=a58f13ec952cf7af4495d0ee73a9bd88","Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands","Pasternak, A.O., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Van den Born, E., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Spaan, W.J.M., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; Snijder, E.J., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands, Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands","Subgenomic mRNAs of nidoviruses (arteriviruses and coronaviruses) are composed of a common leader sequence and a ""body"" part of variable size, which are derived from the 5′- and 3′-proximal part of the genome, respectively. Leader-to-body joining has been proposed to occur during minus-strand RNA synthesis and to involve transfer of the nascent RNA strand from one site in the template to another. This discontinuous step in subgenomic RNA synthesis is guided by short transcription-regulating sequences (TRSs) that are present at both these template sites (leader TRS and body TRS). Sense-antisense base pairing between the leader TRS in the plus strand and the body TRS complement in the minus strand is crucial for strand transfer. Here we show that extending the leader TRS-body TRS duplex beyond its wild-type length dramatically enhanced the subgenomic mRNA synthesis of the arterivirus Equine arteritis virus (EAV). Generally, the relative amount of a subgenomic mRNA correlated with the calculated stability of the corresponding leader TRS-body TRS duplex. In addition, various leader TRS mutations induced the generation of minor subgenomic RNA species that were not detected upon infection with wild-type EAV. The synthesis of these RNA species involved leader-body junction events at sites that bear only limited resemblance to the canonical TRS. However, with the mutant leader TRS, but not with the wild-type leader TRS, these sequences could form a duplex that was stable enough to direct subgenomic RNA synthesis, again demonstrating that the stability of the leader TRS-body TRS duplex is a crucial factor in arterivirus subgenomic mRNA synthesis.",,"genomic RNA; messenger RNA; Arterivirus; article; base pairing; calculation; controlled study; mutation; nonhuman; priority journal; RNA synthesis; species difference; transcription regulation; wild type; Antisense Elements (Genetics); Arteritis Virus, Equine; Base Sequence; DNA Probes; Genome, Viral; Mutagenesis, Site-Directed; RNA, Messenger; RNA, Viral; Sequence Homology, Nucleic Acid; Transcription, Genetic","Alonso, S., Izeta, A., Sola, I., Enjuanes, L., Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus (2002) J. Virol., 76, pp. 1293-1308; An, S., Makino, S., Characterizations of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency (1998) Virology, 243, pp. 198-207; Baric, R.S., Yount, B., Subgenomic negative-strand RNA function during mouse hepatitis virus infection (2000) J. Virol., 74, pp. 4039-4046; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Semin. Virol., 8, pp. 101-111; Budzilowicz, C.J., Wilczynski, S.P., Weiss, S.R., Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′ end of the viral mRNA leader sequence (1985) J. Virol., 53, pp. 834-840; Den Boon, J.A., Kleijnen, M.F., Spaan, W.J.M., Snijder, E.J., Equine arteritis virus subgenomic mRNA synthesis: Analysis of leader-body junctions and replicative-form RNAs (1996) J. Virol., 70, pp. 4291-4298; De Vries, A.A.F., Glaser, A.L., Raamsman, M.J.B., Rottier, P.J.M., Recombinant equine arteritis virus as an expression vector (2001) Virology, 284, pp. 259-276; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Godeny, E.K., De Vries, A.A.F., Wang, X.C., Smith, S.L., De Groot, R.J., Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: Evidence for gene duplication during arterivirus evolution (1998) J. Virol., 72, pp. 862-867; Hofmann, M.A., Chang, R.Y., Ku, S., Brian, D.A., Leader-mRNA junction sequences are unique for each subgenomic mRNA species in the bovine coronavirus and remain so throughout persistent infection (1993) Virology, 196, pp. 163-171; Hsue, B., Masters, P.S., Insertion of a new transcriptional unit into the genome of mouse hepatitis virus (1999) J. Virol., 73, pp. 6128-6135; Jaeger, J.A., Turner, D.H., Zuker, M., Improved predictions of secondary structures for RNA (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 7706-7710; Jeong, Y.S., Repass, J.F., Kim, Y.N., Hwang, S.M., Makino, S., Coronavirus transcription mediated by sequences flanking the transcription consensus sequence (1996) Virology, 217, pp. 311-322; Joo, M., Makino, S., Mutagenic analysis of the coronavirus intergenic consensus sequence (1992) J. Virol., 66, pp. 6330-6337; Joo, M., Makino, S., The effect of two closely inserted transcription consensus sequences on coronavirus transcription (1995) J. Virol., 69, pp. 272-280; Konings, D.A., Bredenbeek, P.J., Noten, J.F., Hogeweg, P., Spaan, W.J.M., Differential premature termination of transcription as a proposed mechanism for the regulation of coronavirus gene expression (1988) Nucleic Acids Res., 16, pp. 10849-10860; Krishnan, R., Chang, R.Y., Brian, D.A., Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the downstream-most initiation site (1996) Virology, 218, pp. 400-405; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Mathews, D.H., Sabina, J., Zuker, M., Turner, D.H., Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure (1999) J. Mol. Biol., 288, pp. 911-940; Meulenherg, J.J.M., De Meijer, E.J., Moormann, R.J.M., Subgenomic RNAs of Lelystad virus contain a conserved leader-body junction sequence (1993) J. Gen. Virol., 74, pp. 1697-1701; Nelsen, C.J., Murtaukh, M.P., Faaberg, K.S., Porcine reproductive and respiratory syndrome virus comparison: Divergent evolution on two continents (1999) J. Virol., 73, pp. 270-280; Ozdarendeli, A., Ku, S., Rochat, S., Williams, G.D., Senanayake, S.D., Brian, D.A., Downstream sequences influence the choice between a naturally occurring noncanonical and closely positioned upstream canonical heptameric fusion motif during bovine coronavirus subgenomic mRNA synthesis (2001) J. Virol., 75, pp. 7362-7374; Pasternak, A.O., Gultyaev, A.P., Spaan, W.J.M., Snijder, E.J., Genetic manipulation of arterivirus alternative mRNA leader-body junction sites reveals tight regulation of structural protein expression (2000) J. Virol., 74, pp. 11642-11653; Pasternak, A.O., Van den Born, E., Spaan, W.J.M., Snijder, E.J., Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis (2001) EMBO J., 20, pp. 7220-7228; Sawicki, S.G., Sawicki, D.L., Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands (1995) Adv. Exp. Med. Biol., 380, pp. 499-506; Sawicki, D.L., Wang, T., Sawicki, S.G., The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus (2001) J. Gen. Virol., 82, pp. 385-396; Shieh, C.K., Soe, L.H., Makino, S., Chang, M.F., Stohlman, S.A., Lai, M.M.C., The 5′-end sequence of the murine coronavirus genome: Implications for multiple fusion sites in leader-primed transcription (1987) Virology, 156, pp. 321-330; Snijder, E.J., Meulenberg, J.J.M., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Van der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Dinten, L.C., Den Boon, J.A., Wassenaar, A.L.M., Spaan, W.J.M., Snijder, E.J., An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 991-996; Van Marle, G., Dobbe, J.C., Gultyaev, A.P., Luytjes, W., Spaan, W.J.M., Snijder, E.J., Arterivirus discontinuous mRNA transcription is guided by base pairing between sense and antisense transcription-regulating sequences (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 12056-12061; Van Marle, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Van Marle, G., Van Dinten, L.C., Spaan, W.J.M., Luytjes, W., Snijder, E.J., Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis (1999) J. Virol., 73, pp. 5274-5281","Snijder, E.J.; Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, Netherlands; email: e.j.snijder@lumc.nl",,,0022538X,,JOVIA,"12502834","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037223731
"Bitnun A., Allen U., Heurter H., King S.M., Opavsky M.A., Ford-Jones E.L., Matlow A., Kitai I., Tellier R., Richardson S., Manson D., Babyn P., Read S.","6602414951;7007010602;6603072733;7403002365;6603134333;7004490364;7003398492;6603766890;7004847486;35380152000;7006667566;7006367819;7101661755;","Children hospitalized with severe acute respiratory syndrome-related illness in Toronto.",2003,"Pediatrics","112","4",,"","",,69,"10.1542/peds.112.4.e261","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141975396&doi=10.1542%2fpeds.112.4.e261&partnerID=40&md5=947ae182e027caeeb9cf2c69bf135046","Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada","Bitnun, A., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Allen, U., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Heurter, H., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; King, S.M., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Opavsky, M.A., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Ford-Jones, E.L., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Matlow, A., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Kitai, I., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Tellier, R., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Richardson, S., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Manson, D., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Babyn, P., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada; Read, S., Division of Infectious Diseases, Department of Paediatrics, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada","OBJECTIVE: An outbreak of severe acute respiratory syndrome (SARS) occurred in the greater Toronto area between February and June 2003. We describe the clinical, laboratory, and epidemiologic features of children who were admitted to the Hospital for Sick Children, Toronto, with a presumptive diagnosis of suspect or probable SARS. METHODS: A prospective investigational study protocol was established for the management of children with a presumptive diagnosis of suspect or probable SARS. All were ultimately classified as having probable SARS, suspect SARS, or another cause on the basis of their epidemiologic exposure, clinical and radiologic features, and results of microbiologic investigations. RESULTS: Twenty-five children were included; 10 were classified as probable SARS and 5 were classified as suspect SARS, and in 10 another cause was identified. The exposure consisted of direct contact with at least 1 adult probable SARS case in 11 children, travel from a World Health Organization-designated affected area in Asia in 9 children, and presence in a Toronto area hospital in which secondary SARS spread had occurred in 5 children. The predominant clinical manifestations of probable cases were fever, cough, and rhinorrhea. With the exception of 1 teenager, none of the children developed respiratory distress or an oxygen requirement, and all made full recoveries. Mild focal alveolar infiltrates were the predominant chest radiograph abnormality. Lymphopenia; neutropenia; thrombocytopenia; and elevated alanine aminotransferase, aspartate aminotransferase, and creatine kinase were present in some cases. Nasopharyngeal swab specimens were negative for the SARS-associated coronavirus by an in-house reverse transcriptase-polymerase chain reaction in all 25 children. CONCLUSIONS: Our results indicate that SARS is a relatively mild and nonspecific respiratory illness in previously healthy young children. The presence of fever in conjunction with a SARS exposure history should prompt one to consider SARS as a possible diagnosis in children irrespective of the presence or absence of respiratory symptoms. Reverse-transcriptase polymerase chain reaction analysis of nasopharyngeal specimens seems to be of little utility for the diagnosis of SARS during the early symptomatic phase of this illness in young children.",,"antivirus agent; clarithromycin; ribavirin; adolescent; article; Asia; Canada; child; child hospitalization; cohort analysis; disease transmission; epidemic; ethnology; female; hospital; human; infant; isolation and purification; male; preschool child; prospective study; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; statistics; travel; virology; Adolescent; Antiviral Agents; Asia; Child; Child, Hospitalized; Child, Preschool; Clarithromycin; Cohort Studies; Disease Outbreaks; Disease Transmission, Horizontal; Female; Hospitals, Pediatric; Humans; Infant; Male; Ontario; Prospective Studies; Reverse Transcriptase Polymerase Chain Reaction; Ribavirin; SARS Virus; Severe Acute Respiratory Syndrome; Travel",,"Bitnun, A.",,,10984275,,,"14523209","English","Pediatrics",Article,"Final",Open Access,Scopus,2-s2.0-0141975396
"Naqi S., Gay K., Patalla P., Mondal S., Liu R.","7003290056;6603585670;6505605784;7102825018;56317819800;","Establishment of persistent avian infectious bronchitis virus infection in antibody-free and antibody-positive chickens",2003,"Avian Diseases","47","3",,"594","601",,35,"10.1637/6087","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141683613&doi=10.1637%2f6087&partnerID=40&md5=807656adb4dae48e8ac944b6fc468024","Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Depts. of Med./Microbiol./Immunology, Emory University School of Medicine, Atlanta, GA 30303, United States","Naqi, S., Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Gay, K., Depts. of Med./Microbiol./Immunology, Emory University School of Medicine, Atlanta, GA 30303, United States; Patalla, P., Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Mondal, S., Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States; Liu, R., Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States","Avian infectious bronchitis virus (IBV) causes a highly contagious and economically significant disease in chickens. Establishment of a carrier state in IBV infection and the potential for the persistent virus to undergo mutations and recombination in chicken tissues have important consequences for disease management. Nevertheless, whether chickens can maintain persistent IBV infection in the absence of reinfection from exogenous sources or the presence of antibody in the host can modulate virus persistence remains unclear. Indeed, whether or not IBV genome can undergo genetic changes during in vivo infection has not been demonstrated experimentally. In the present study, IBV shedding and tissue persistence were monitored in individual chickens maintained under strict isolation that precluded reinfection from exogenous sources. In the first of two experiments, intranasal exposure of 6-wk-old antibody-free chickens to IBV vaccine virus resulted in intermittent shedding of the virus from both trachea and cloaca of individual birds for up to 63 days. Also, the virus was recovered from the internal organs (spleen, gonad, kidney, lung, cecal tonsil, and cloacal bursa) of six of eight birds killed at various intervals between 27 and 163 days postinoculation (DPI). In the second experiment, IBV exposure of 1-day-old maternal antibody-positive chicks led to periodic virus shedding from the trachea and cloaca in all chickens until 77 days; however, internal organs (lungs and kidneys) of only one of seven birds (killed at 175 DPI) were virus positive, suggesting that presence of antibody at the time of infection protects internal organs from IBV infection. When the lung and kidney isolates of IBV from the latter experiment were compared with the parent-vaccine virus, no changes in their antigenicity, tissue tropism, or the nucleotide sequence of the S1 glycoprotein gene were observed. These findings indicate that, unlike the mammalian coronaviruses, propensity for frequent genetic change may not be inherent in the IBV genome.","Antibody-free chickens; Antibody-positive chickens; Coronavirus; Infectious bronchitis virus; Sequence; Serotype; Spike protein gene; Virus persistence","Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Enterobacter; Gallus gallus; Mammalia","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazel, F., Fleming, J.O., Baker, S.C., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasi-species nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; Alexander, D.J., Gough, R.E., Isolation of avian infectious bronchitis virus from experimentally infected chickens (1977) Res. Vet. Sci., 23, pp. 344-347; Cavanagh, D., Davis, P.J., Coronavirus IBV: Removal of spike glycopolypeptide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells (1986) J. Gen. Virol., 67, pp. 1443-1448; Cavanagh, D., Davis, P.J., Cook, J.K.A., Li, D., Kant, A., Koch, G., Location of the amino acid differences in the S1 spike glycoprotein subunit of closely related serotypes of infectious bronchitis virus (1992) Avian Pathol., 21, pp. 33-43; Cavanagh, D., Davis, P.J., Mockett, A.P.A., Amino acid within hypervariable region 1 of avian coronavirus IBV (Massachusetts serotype) spike glycoproteins are associated with neutralization epitopes (1988) Virus Res., 11, pp. 141-150; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of Poultry, 10th Ed., pp. 511-526. , B. W. Calnek, H. J. Barnes, C. W. Beard, L. R. McDougald, and Y. M. Saif, eds. Iowa State University Press, Ames, IA; Cook, J.K.A., Duration of experimental infectious bronchitis in chickens (1968) Res. Vet. Sci., 9, pp. 506-514; El-Houadfi, M.D., Jones, R.C., Cook, J.K.A., Ambali, A.G., The isolation and characterization of six avian infectious bronchitis viruses isolated in Morocco (1986) Avian Pathol., 15, pp. 93-105; Fleming, J.O., Houtman, J.J., Alaca, H., Hinze, H.C., McKenzie, D., Aiken, J., Bleasdale, T., Baker, S., Persistence of viral RNA in the central nervous system of mice inoculated with MHV-4 (1994) Coronaviruses, pp. 327-332. , H. Laude and J. F. Vautherot, eds. Plenum Press, New York; Gelb J., Jr., Jackwood, M.W., Infectious bronchitis (1998) A Laboratory Manual for the Isolation and Identification of Avian Pathogens, 4th Ed., pp. 169-174. , D. E. Swayne, J. R. Glisson, M. W. Jackwood, J. E. Pearson, and W. M. Reed, eds. American Association of Avian Pathologists, Kennett Square, PA; Hawkes, R.A., Darbyshire, J.H., Peters, R.W., Mockett, A.P.A., Cavanagh, D., Presence of viral antigens and antibody in trachea of chickens infected with avian infectious bronchitis virus (1983) Avian Pathol., 12, pp. 331-340; Jackwood, M.W., Yousef, N.M.H., Hilt, D.A., Further development and use of a molecular serotype identification test for infectious bronchitis virus (1997) Avian Dis., 41, pp. 105-110; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Jia, W., Mondal, S.P., Naqi, S.A., Genetic and antigenic diversity in avian infectious bronchitis virus isolates of the 1940s (2002) Avian Dis., 46, pp. 437-441; Jones, R.C., Ambali, A.G., Re-excretion of an enterotropic infectious bronchitis virus by hens at point of lay after experimental infection at day old (1987) Vet. Rec., 120, pp. 617-620; Jones, R.C., Jordan, F.T.W., Persistence of virus in the tissues and development of the oviduct in the fowl following infection at day old with infectious bronchitis virus (1972) Res. Vet. Sci., 13, pp. 52-60; Karaca, K., Naqi, S.A., Palukatis, P., Lucio, B., Serological and molecular characterization of three enteric isolates of infectious bronchitis virus of chickens (1990) Avian Dis., 34, pp. 899-904; Kingham, B.E., Keeler C.L., Jr., Nix, W.A., Ladman, B.S., Gelb J., Jr., Identification of avian infectious bronchitis virus by direct automated cycle sequencing of the S-1 gene (2000) Avian Dis., 44, pp. 325-335; Lee, C., Hilt, D.A., Jackwood, M.W., Redesign of primer and application of the reverse transcriptase-polymerase chain reaction and restriction fragment length polymorphism test to the DE072 strain of infectious bronchitis virus (2000) Avian Dis., 44, pp. 650-654; Lee, C.W., Jackwood, M.W., Evidence of genetic diversity generated by recombination among avian coronavirus IBV (2000) Arch. Virol., 145, pp. 2135-2148; Naqi, S.A., A monoclonal antibody-based immunoperoxidase procedure for rapid detection of infectious bronchitis virus in infected tissues (1990) Avian Dis., 34, pp. 893-898; Naqi, S.A., Karaca, K., Bauman, B., A monoclonal antibody-based antigen capture enzyme-linked immunosorbent assay for identification of infectious bronchitis virus serotypes (1993) Avian Pathol., 22, pp. 555-564; Reed, L.J., Muench, H., A simple method for estimating fifty percent endpoints (1938) Am. J. Hyg., 27, pp. 493-497; Rowe, C.L., Baker, S.C., Nathan, M.J., Fleming, J.O., Evolution of mouse hepatitis virus: Detection and characterization of spike deletion varients during persistent infection (1997) J. Virol., 71, pp. 2959-2969; Seo, S.H., Wang, L., Smith, R., Collisson, E.W., The carboxyl-terminal 120-residue polypeptide of infectious bronchitis virus nucleocapsid induces cytotoxic T lymphocytes and protects chickens from acute infection (1997) J. Virol., 71, pp. 7889-7894; Stern, D.F., Sefton, B.M., Coronavirus proteins: Biogenesis of avian coronavirus infectious bronchitis virus (1982) J. Virol., 44, pp. 794-803; Stern, D.F., Sefton, B.M., Coronavirus multiplication: Locations of genes for virion proteins on the avian infectious bronchitis virus genome (1984) J. Virol., 50, pp. 22-29; Wang, L., Yu, Y., Collisson, E.W., Experimantal confirmation of recombination upstream of the S1 hypervariable region of infectious bronchitis virus (1997) Virus Res., 49, pp. 139-145","Naqi, S.; Dept. of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States",,"American Association of Avian Pathologists",00052086,,AVDIA,"14562886","English","Avian Dis.",Article,"Final",,Scopus,2-s2.0-0141683613
"Lai R.Q., Feng X.D., Wang Z.C., Lai H.W., Tian Y., Zhang W., Yang C.H.","7201986896;56303107200;7410047522;7201967207;57212703231;57192227197;10640121800;","Pathological and ultramicrostructural changes of tissues in a patient with severe acute respiratory syndrome",2003,"Zhonghua bing li xue za zhi Chinese journal of pathology","32","3",,"205","208",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346041794&partnerID=40&md5=aefa712c4d64b5f48a4b72b14247104b","General Hospital of Guangzhou Command, Guangzhou, 510010, China","Lai, R.Q., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Feng, X.D., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Wang, Z.C., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Lai, H.W., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Tian, Y., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Zhang, W., General Hospital of Guangzhou Command, Guangzhou, 510010, China; Yang, C.H., General Hospital of Guangzhou Command, Guangzhou, 510010, China","OBJECTIVE: To study the morphological, ultramicrostructural and pathological changes of tissues from a patient with severe acute respiratory syndrome (SARS). METHODS: One autopsy case of diagnosed SARS was investigated. Lung puncture was performed immediately after the patient died, and the autopsy was done after 12 h. The specimens from lymph nodes, spleen, small intestine, colon and bone marrow were studied by immunohistochemical technique. The antibodies used included CD20, CD45RO (UCHL-1), CD4, CD8, CD68 and CD34. RESULTS: The principal lesions of the SARS case consisted of acute lobular intrastitial pneumonia, hyaloid membranes of pulmonic alveoli and hyperplasia and shedding of alveolar epithelium of. Virus-like inclusions occasionally contained cytoplasm of the alveolar epithelium, which were positive by histochemical staining. The adjacent blood-vessels were changed by hyperplasia and enlargement. The structures of lymph nodes and spleen were damaged with lymph follicles depletion and splenic nodules atrophy. The specific changes included reduction of lymphocytes and hyperplasia of histiocytes, depletion of the follicles of small intestine and colon wall, decreased hyperplasia of the bone marrow and increased number of the megakaryocyte. Meanwhile, in the immunohistochemical study, CD(20)(+) B cells were fully expressed in lymph nodes and spleen, and the CD45RO (UCHL-1)(+) T cells were scatteredly expressed. The number of CD4(+) help T cell was markedly decreased, while the number of CD8+ poisonal T cells increased, and the ratio of the former and latter was no more than 0.5. Under the electronic microscopy observation, virus-like particles with 80 - 160 nm diameter and halo or garland envelope were found in mononuclear macrophage and cytoplasm of alveolar epithelium. CONCLUSION: The specific lesions of SARS consist of lobular intrastitial pneumonia with the formation of hyaline membranes of lung, haemorrhage, necrosis, inflammation of blood vessels and the damages of extralung lymphohemopioetic system. The damages were very similar to the pathological features of tissues infected by human immunodeficiency virus, in which numbers of T cells decreased and CD(4)(+) T cell/CD(8)(+) T cell ratio was no more than 0.5. According to the virus-like particles found in lung of the SARS case, it is considered that these virus-like particles may be a new kind of coronavirus which caused the ""atypical pneumonia"".",,"article; case report; electron microscopy; heart muscle; human; immunohistochemistry; lung; lymph node; male; middle aged; pathology; severe acute respiratory syndrome; Humans; Immunohistochemistry; Lung; Lymph Nodes; Male; Microscopy, Electron; Middle Aged; Myocardium; Severe Acute Respiratory Syndrome",,"Lai, R.Q.",,,05295807,,,"12882682","Chinese","Zhonghua Bing Li Xue Za Zhi",Article,"Final",,Scopus,2-s2.0-0346041794
"Lu P.X., Zhou B.P., Hu Y.W., Yang G.L., Yang D.G., Luo Z.Y., Chen X.C., Gong X.L., Yang G.D., Wang Z.Q., Yuan B.T.","55648158500;7401906727;56163053400;7405754750;57198915362;57209997388;55109589100;7201999122;8710357800;57210002667;7203054883;","Clinical and chest X-ray characteristics of 5 cases with severe acute respiratory syndrome in children in Shenzhen area",2003,"Zhonghua er ke za zhi. Chinese journal of pediatrics","41","9",,"645","647",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342641438&partnerID=40&md5=8062bff6db160775e3da6401f5516a66","Department of Radiology, Shenzhen East Lake Hospital, China, 518020","Lu, P.X., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Zhou, B.P., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Hu, Y.W., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Yang, G.L., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Yang, D.G., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Luo, Z.Y., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Chen, X.C., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Gong, X.L., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Yang, G.D., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Wang, Z.Q., Department of Radiology, Shenzhen East Lake Hospital, China, 518020; Yuan, B.T., Department of Radiology, Shenzhen East Lake Hospital, China, 518020","OBJECTIVE: To explore clinical and chest X-ray features of SARS in children to facilitate correct diagnosis. METHODS: Clinical manifestations and chest X-ray findings in five children suffering from SARS admitted for treatment in the hospital between February and May, 2003 in Shenzhen area were analyzed. The diagnosis was confirmed by epidemiological, clinical, laboratory and radiological examinations. Among the 5 cases, 1 was a boy and the others were girls at the age of 4 to 13 years. RESULTS: Of the 5 SARS children, 3 presented a history of close contact with SARS patients. Fever was the initiative symptom, 4 had a body temperature of over 38 degrees C with the highest being 40 degrees C; fever sustained from 4 to 7 days with an average of 5.6 days. All the 5 cases developed nonproductive cough; on auscultation, both moist and dry rales could be heard in 3 out of the 5 cases. Mean total white count of peripheral blood was (2.96 - 6.9) x 10(9)/L, and was < 5.0 x 10(9)/L in 4 cases. SARS associated coronavirus specific RNA fragment was found positive by RT-PCR in 1 case; 1 case was positive for both IgM and IgG antibodies to the virus; 1 case was positive for only IgM antibody and another 2 cases were positive for only IgG antibody. IgG and IgM antibodies to Mycoplasma pneumoniae and Chlamydia pneumoniae as well as blood culture for bacteria were all negative. Findings on chest X-ray examination: 4 cases showed presence of patchy or macular opacities with cord-like shadows in unilateral lung plates while 1 case each showed ground-glass-like opacity and migratory changes; 1 case showed interstitial changes in the lungs in the form of irregular reticular lattice and cord-like shadows. Two cases received CT scanning and macular-patchy or spotty shadows were seen all over the lung. The shortest time for absorption of foci in the lungs was 7 days while the longest was 33 days with a mean of 15 +/- 6 days. None of the cases had any signs of fibrosis in the lungs. All the 5 cases were completely cured and discharged 7 to 40 days (mean 18 +/- 11 days) after admission. CONCLUSION: Compared with adult cases with SARS, children with SARS had milder symptoms and signs. Presence of unilateral patchy shadow in lungs represented the main chest X-ray findings.",,"immunoglobulin G; immunoglobulin M; virus antibody; adolescent; article; case report; child; female; genetics; human; immunology; male; pathology; preschool child; radiography; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; thorax radiography; virology; Adolescent; Antibodies, Viral; Child; Child, Preschool; Female; Humans; Immunoglobulin G; Immunoglobulin M; Male; Radiography, Thoracic; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome",,"Lu, P.X.",,,05781310,,,"14733797","Chinese","Zhonghua Er Ke Za Zhi",Article,"Final",,Scopus,2-s2.0-2342641438
"Wang C., Pang B.S.","54935541900;7006274811;","Dynamic changes and the meanings of blood cytokines in severe acute respiratory syndrome",2003,"Zhonghua jie he he hu xi za zhi = Zhonghua jiehe he huxi zazhi = Chinese journal of tuberculosis and respiratory diseases","26","10",,"586","589",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2142741880&partnerID=40&md5=1c40cba76d2a9d8bb5df5226c6478f15","Beijing Chaoyang Hospital-Affiliate of Capital University of Medical Sciences, Beijing Institute of Respiratory Medicine, Beijing, 100020, China","Wang, C., Beijing Chaoyang Hospital-Affiliate of Capital University of Medical Sciences, Beijing Institute of Respiratory Medicine, Beijing, 100020, China; Pang, B.S., Beijing Chaoyang Hospital-Affiliate of Capital University of Medical Sciences, Beijing Institute of Respiratory Medicine, Beijing, 100020, China","OBJECTIVE: To investigate the dynamic changes observed in serum levels of interleukins (ILs), tumor necrosis factor-alpha (TNF-alpha) and transforming growth factor-beta1 (TGF-beta1) in severe acute respiratory syndrome (SARS). METHODS: Sixty-one cases of SARS were classified into the following categories according to the duration from the onset of illness to the time blood was drawn: 3-7 day group, 8-14 day group and over 14 day group. Forty-four healthy individuals served as the control. Serum levels of ILs, TNF-alpha and TGF-beta1 were measured in all cases. Serum antibodies to SARS-coronavirus (SARS-CoV) were measured only in SARS cases. RESULTS: The mean concentration of serum IL-6 in SARS patients did not differ from the control group in 3-7 day group and 8-14 day group, but became significantly higher in over 14 day group as compared to the control group, 3-7 day group and 8-14 day group (P < 0.01). The mean concentration of serum IL-8 in SARS patients did not differ from the control group in 3-7 day group, were significantly higher than the control group in 8-14 days group and in over 14 day group (P < 0.05) and significantly higher in over 14 day group than in 3-7 day group and 8-14 day group (P < 0.01). The mean concentration of IL-16 and TNF-alpha in all groups of SARS was higher than that of the control group, but it was the highest in over 14 day group (P < 0.01). SARS patients experienced higher concentration of serum IL-13 as compared to controls in 3-7 day group (P < 0.01), but it returned to normal levels in 8-14 day group and the over 14 day group. The mean concentration of serum IL-18 in SARS patients was significantly lower than that of the control group during all groups of SARS patients (P < 0.05); The mean concentration of TGF-beta1 in all groups of SARS patients was higher than that of the control group. Although TGF-beta1 in sera decreased in over 14 day group, the average was still higher than that of the control group (P < 0.01). CONCLUSIONS: Proinflammatory cytokines and TGF-beta1 were elevated during the early phase of SARS, a phenomenon which may be associated with lung infiltration and proliferation. Concurrently, the mean concentration of serum IL-13 decreased gradually and the mean concentration of serum IL-18 level in SARS patients was lower than that of the control group during the whole disease course. It suggested that the immune state of SARS was obviously abnormal. Observing the dynamic changes in blood cytokine levels can provide us with a scientific basis to assess pathogenesis and efficacy of clinical treatment of SARS.",,"cytokine; interleukin derivative; transforming growth factor beta; tumor necrosis factor alpha; adolescent; adult; aged; article; blood; female; human; immunology; male; middle aged; severe acute respiratory syndrome; Adolescent; Adult; Aged; Cytokines; Female; Humans; Interleukins; Male; Middle Aged; Severe Acute Respiratory Syndrome; Transforming Growth Factor beta; Tumor Necrosis Factor-alpha",,"Wang, C.",,,10010939,,,"14633438","Chinese","Zhonghua Jie He He Hu Xi Za Zhi",Article,"Final",,Scopus,2-s2.0-2142741880
"Pratelli A., Martella V., Pistello M., Elia G., Decaro N., Buonavoglia D., Camero M., Tempesta M., Buonavoglia C.","7004884960;7003300496;7003992117;7005135633;6701636107;7004335810;6701658830;7005599031;7005623145;","Identification of coronaviruses in dogs that segregate separately from the canine coronavirus genotype",2003,"Journal of Virological Methods","107","2",,"213","222",,27,"10.1016/S0166-0934(02)00246-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037290951&doi=10.1016%2fS0166-0934%2802%2900246-X&partnerID=40&md5=d2546db5d21a8896dadcfeffa83fc99b","Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Department of Biomedicine, Retrovirus Center/Virology Section, University of Pisa, Pisa, Italy; Department of Pathology, University of Messina, Messina, Italy","Pratelli, A., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Martella, V., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Pistello, M., Department of Biomedicine, Retrovirus Center/Virology Section, University of Pisa, Pisa, Italy; Elia, G., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Decaro, N., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Buonavoglia, D., Department of Pathology, University of Messina, Messina, Italy; Camero, M., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Tempesta, M., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; Buonavoglia, C., Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy","The genetic diversity of 16 canine coronavirus (CCoV) samples is described. Samples were obtained from pups infected naturally living in different areas. Sequence data were obtained from the M gene and pol1a and pol1b regions. The phylogenetic relationships among these sequences and sequences published previously were determined. The canine samples segregated in two separate clusters. Samples of the first cluster were intermingled with reference strains of CCoV genotype and therefore could be assigned to this genotype. The second cluster segregated separately from CCoV and feline coronavirus genotypes and therefore these samples may represent genetic outliers. The reliability of the classification results was confirmed by repeating the phylogenetic analysis with nucleotide and amino acid sequences from multiple genomic regions. © 2002 Elsevier Science B.V. All rights reserved.","Coronavirus; Dog; Genotype","amino acid sequence; article; biodiversity; cluster analysis; controlled study; Coronavirus; gene sequence; genetic variability; genome; genotype; nonhuman; nucleotide sequence; phylogeny; priority journal; publishing; reliability; sampling; virus identification; Amino Acid Sequence; Animals; Coronavirus Infections; Coronavirus, Canine; DNA-Directed RNA Polymerases; Dog Diseases; Dogs; Genotype; Molecular Sequence Data; Phylogeny; Polymerase Chain Reaction; Sequence Analysis, DNA; Variation (Genetics); Viral Matrix Proteins; Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline coronavirus","Almazan, F., Gonzales, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Appel, M.J., Cooper, B.J., Greisen, H., Scott, F., Carmichael, L.E., Canine viral enteritis. I. 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Virol., 23, pp. 41-49; De Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., Van der Ziejst, B.A.M., Spaan, W.J.M., CDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus (1987) J. Gen. Virol., 68, pp. 2639-2646; De Haan, C.A., Vennema, H., Rottier, P.J., Assembly of the coronavirus envelope: Homotypic interactions between the M proteins (2000) J. Virol., 74, pp. 4967-4978; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Dolja, V.V., Carrington, J.C., Evolution of positive-strand RNA viruses (1992) Semin. Virol., 3, pp. 315-326; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, Classification and Nomenclature of Viruses, pp. 835-849. , M.H.V. van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle, & R.B. Wickner. New York: Academic Press; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidoviridales (2000) Virus Taxonomy, Classification and Nomenclature of Viruses, pp. 827-834. , M.H.V. van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle, & R.B. Wickner. New York: Academic Press; Gebauer, F., Posthumus, W.A.P., Correa, I., Suné, C., Sánchez, C.M., Smerdou, C., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Herrewegh, A.A.P.M., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissue, and body fluid of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Hohdatsu, T., Okada, S., Koyama, H., Characterization of monoclonal antibodies against feline infectious peritonitis virus type II and antigenic relationship between feline, porcine, and canine coronavirus (1991) Arch. Virol., 117, pp. 85-95; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Horsburgh, B.C., Brierley, I., Brown, T.D., Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA (1992) J. Gen. Virol., 73, pp. 2849-2862; Jarvis, T.C., Kirkegaard, K., The polymerase in its labyrinth: Mechanisms and implications of RNA recombination (1991) Trends Genet., 7, pp. 186-191; Jia, W., Karaka, K., Parrish, C.R., Naqi, S.A., A novel variant of infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Keck, J.G., Matsushima, G.K., Makino, S., Fleming, J.O., Vannier, D.M., Stohlman, S.A., Lai, M.M.C., In vivo RNA-RNA recombination of coronavirus in mouse brain (1988) J. Virol., 62, pp. 1810-1813; Kirkegaard, K., Baltimore, D., The mechanism of RNA recombination in poliovirus (1986) Cell, 47, pp. 433-443; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Kusters, J.G., Jager, E.J., Niesters, H.G.M., Zeist, B.A.M., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M.C., Baric, R.S., Makino, S., Keck, J.G., Egbert, J., Leibowitz, J.L., Stohlman, S.A., Recombination between nonsegmented RNA genomes of murine coronaviruses (1985) J. Virol., 56, pp. 449-456; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, pp. 33-49. , S.G. Siddell. New York: Plenum Press; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronavirus (1986) J. Virol., 57, pp. 729-739; Martin, H.D., Zeidner, N.S., Concomitant cryptosporidia, coronavirus and parvovirus infection in a raccoon (Procyon lotor) (1992) J. Wildl. Dis., 28, pp. 113-115; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Canine coronavirus infection in cats; A possible role in feline infectious peritonitis (1990) Adv. Exp. Med. Biol., 276, pp. 475-479; McArdle, F., Bennett, M., Gaskell, R.M., Tennant, B., Kelly, D.F., Gaskell, C.J., Induction and enhancement of feline infectious peritonitis by canine coronavirus (1992) Am. J. Vet. Res., 53, pp. 1500-1506; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Naylor, M.J., Harrison, G.A., Monckton, R.P., McOrist, S., Lehrbach, P.R., Deane, E.M., Identification of canine coronavirus strains from feces by S gene nested PCR and molecular characterization of a new Australian isolate (2001) J. Clin. Microbiol., 39, pp. 1036-1041; Pratelli, A., Buonavoglia, D., Martella, V., Cavalli, A., Lavazza, Buonavoglia, C., Enteriti virali del cane: Risultati di un'indagine virologica (1999) Veterinaria, 13, pp. 57-63; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) J. Virol. Methods, 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) J. Virol. Methods, 84, pp. 91-94; Pratelli, A., Martella, V., Elia, G., Tempesta, M., Guarda, F., Capucchio, M.T., Carmichael, L.E., Buonavoglia, C., Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus (2001) J. Vet. Med. B, 48, pp. 385-392; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Mol. Cell Probes, 15, pp. 229-233; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Risco, C., Antón, I.M., Sune, C., Pedregosa, A.M., Martín-Alonso, J.M., Parra, F., Carrascosa, J.L., Enjuanes, L., Membrane protein molecules of transmissible gastroenteritis coronavirus also espose the carboxy-terminal region on the external surface of the virion (1995) J. Virol., 69, pp. 5269-5277; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S.G. Siddell. New York: Plenum Press; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Siddell, S.G., The coronaviridae, an introduction (1995) The Coronaviridae, pp. 1-10. , S.G. Siddell. New York: Plenum Press; Stoddart, C.A., Barlough, J.E., Baldwin, C.A., Scott, F.W., Attempted immunisation of cats against feline infectious peritonitis using canine coronavirus (1988) Res. Vet. Sci., 45, pp. 383-388; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-44; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination within the S1 gene of infectious bronchitis virus (1993) Virology, 192, pp. 710-716; Woods, R.D., Wesley, R.D., Kapke, P.A., Complement-dependent neutralization of transmissible gastroenteritis virus by monoclonal antibodies (1987) Adv. Exp. Med. Biol., 218, pp. 493-500; Yasoshima, A., Fujinami, F., Doi, K., Kojima, A., Takada, H., Okaniwa, A., Case report on mixed infection of canine parvovirus and canine coronavirus - Electron microscopy and recovery of canine coronavirus (1983) Nippon Juigaku Zasshi, 45, pp. 217-225","Pratelli, A.; Department of Animal Health, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010 Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,,01660934,,JVMED,"12505636","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0037290951
"Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.","6506900911;6602571243;57203154014;7102670281;7201657724;","Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E",2003,"Journal of Virology","77","4",,"2530","2538",,109,"10.1128/JVI.77.4.2530-2538.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037321751&doi=10.1128%2fJVI.77.4.2530-2538.2003&partnerID=40&md5=b76b4b197ea57d874736efb1f689c7a3","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Molecular Biology Program, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; INRS-Institut Armand-Frappier, Laval, Que. H7V 1B7, Canada; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 E. 9th Ave., Denver, CO 80220, United States; Department of Comparative Medicine, Johns Hopkins Univ. Sch. of Medicine, Retrovirus Laboratory, Baltimore, MD 21287, United States","Bonavia, A., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Department of Comparative Medicine, Johns Hopkins Univ. Sch. of Medicine, Retrovirus Laboratory, Baltimore, MD 21287, United States; Zelus, B.D., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Wentworth, D.E., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Talbot, P.J., INRS-Institut Armand-Frappier, Laval, Que. H7V 1B7, Canada; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Molecular Biology Program, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 E. 9th Ave., Denver, CO 80220, United States","Human coronavirus HCoV-229E uses human aminopeptidase N (hAPN) as its receptor (C. L. Yeager et al., Nature 357:420-422, 1992). To identify the receptor-binding domain of the viral spike glycoprotein (S), we expressed soluble truncated histidine-tagged S glycoproteins by using baculovirus expression vectors. Truncated S proteins purified by nickel affinity chromatography were shown to be glycosylated and to react with polyclonal anti-HCoV-229E antibodies and monoclonal antibodies to the viral S protein. A truncated protein (S547) that contains the N-terminal 547 amino acids bound to 3T3 mouse cells that express hAPN but not to mouse 3T3 cells transfected with empty vector. Binding of S547 to hAPN was blocked by an anti-hAPN monoclonal antibody that inhibits binding of virus to hAPN and blocks virus infection of human cells and was also blocked by polyclonal anti-HCoV-229E antibody. S proteins that contain the N-terminal 268 or 417 amino acids did not bind to hAPN-3T3 cells. Antibody to the region from amino acid 417 to the C terminus of S blocked binding of S547 to hAPN-3T3 cells. Thus, the data suggest that the domain of the spike protein between amino acids 417 and 547 is required for the binding of HCoV-229E to its hAPN receptor.",,"microsomal aminopeptidase; monoclonal antibody; polyclonal antibody; spike glycoprotein; unclassified drug; virus antibody; virus glycoprotein; animal cell; article; baculovirus expression system; controlled study; Coronavirus; genetic transfection; nonhuman; priority journal; protein analysis; protein domain; protein function; protein glycosylation; protein protein interaction; protein purification; receptor binding; spike; 3T3 Cells; Aminopeptidases; Animals; Baculoviridae; Binding Sites; Cells, Cultured; Coronavirus 229E, Human; Humans; Membrane Glycoproteins; Mice; Receptors, Virus; Recombinant Proteins; Spodoptera; Structure-Activity Relationship; Viral Envelope Proteins","Baker, K.A., Dutch, R.E., Lamb, R.A., Jardetzky, T.S., Structural basis for paramyxovirus-mediated membrane fusion (1999) Mol. 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Virol., 77, pp. 830-840; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor. Bgp1(b), and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Holmes, K.V.; Department of Microbiology, Campus Box B-175, Univ. of Colorado Hlth. Sci. Center, 4200 E. 9th Ave., Denver, CO 80220, United States; email: kathryn.holmes@uchsc.edu",,,0022538X,,JOVIA,"12551991","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037321751
"Thumerelle C., Deschildre A., Bouquillon C., Santos C., Sardet A., Scalbert M., Delbecque L., Debray P., Dewilde A., Turck D., Leclerc F.","55922265400;7004402827;7801357720;7201458798;7005669446;6603222425;36871680600;57213311209;7004613991;7102357517;7103287993;","Role of viruses and atypical bacteria in exacerbations of asthma in hospitalized children: A prospective study in the Nord-Pas de Calais region (France)",2003,"Pediatric Pulmonology","35","2",,"75","82",,94,"10.1002/ppul.10191","https://www.scopus.com/inward/record.uri?eid=2-s2.0-12244303678&doi=10.1002%2fppul.10191&partnerID=40&md5=23d416e1a6d4d2e55d065e721be0fcc6","Department of Pediatrics, CHU Lille, Lille, France; Department of Virology, CHU Lille, Lille, France; Department of Pediatrics, Hôpital Lens, Lens, France; Department of Pediatrics, Hôpital St.-Antoine-Lille, Lille, France; Department of Pediatrics, Hôpital Tourcoing, Tourcoing, France; Department of Pediatrics, Hôpital Valenciennes, Valenciennes, France; Secretariat de Pneumologie Infantile, Hôpital Jeanne de Flandre, CHU de Lille, 59037 Lille Cedex, France","Thumerelle, C., Department of Pediatrics, CHU Lille, Lille, France, Secretariat de Pneumologie Infantile, Hôpital Jeanne de Flandre, CHU de Lille, 59037 Lille Cedex, France; Deschildre, A., Department of Pediatrics, CHU Lille, Lille, France; Bouquillon, C., Department of Virology, CHU Lille, Lille, France; Santos, C., Department of Pediatrics, CHU Lille, Lille, France; Sardet, A., Department of Pediatrics, Hôpital Lens, Lens, France; Scalbert, M., Department of Pediatrics, Hôpital St.-Antoine-Lille, Lille, France; Delbecque, L., Department of Pediatrics, Hôpital Tourcoing, Tourcoing, France; Debray, P., Department of Pediatrics, Hôpital Valenciennes, Valenciennes, France; Dewilde, A., Department of Virology, CHU Lille, Lille, France; Turck, D., Department of Pediatrics, CHU Lille, Lille, France; Leclerc, F., Department of Pediatrics, CHU Lille, Lille, France","We studied the role of viruses and atypical bacteria in children hospitalized with exacerbated asthma by a prospective study of children with acute asthma admitted to the Department of Pediatrics in Lille, and to 15 hospitals in the Nord-Pas de Calais region, from October 1, 1998-June 30, 1999. We included children aged 2-16 years with active asthma, defined as three or more recurrent episodes of reversible wheezing. The severity of asthma and of asthmatic exacerbations was recorded. Immunofluorescence assays (IFA) on nasopharyngeal secretions (NPS), serological tests, or both, were used for detection of influenza virus, respiratory syncytial virus (RSV), adenovirus, parainfluenza virus, and coronavirus. Polymerase chain reaction (PCR) assays on NPS were used for rhinovirus and enterovirus. Serological tests for Chlamydia pneumoniaeand Mycoplasma pneumoniae were performed. A control group of asymptomatic asthmatic outpatients was examined for respiratory viruses (using IFA and PCR). Eighty-two symptomatic children (mean age, 7.9 years) were examined. Viruses were detected in 38% (enterovirus, 15.8%; rhinovirus, 12%; RSV, 7.3%). Serological tests for atypical bacteria were positive in 10% of patients (C. pneumoniae, 5%; M. pneumoniae, 5%). Among the 27 control subjects (mean age, 7.9 years), one PCR was positive for enterovirus. There was no correlation between severity of chronic asthma or asthmatic exacerbations and the diagnosis of infection. Atypical bacterial pathogen infections were linked with prolonged asthmatic symptoms. In conclusion, we confirmed the high incidence of viral infection in acute exacerbations of asthma, especially enteroviruses or rhinoviruses. Persistent clinical features were more frequently associated with atypical bacterial infections, suggesting that these infections should be investigated and treated in cases of persistent asthmatic symptoms. © 2003 Wiley-Liss, Inc.","Asthma; Children; Chlamydia pneumoniae; Gastrointestinal symptoms; Infections; Mycoplasma pneumoniae; Virus","Adenovirus; adolescent; article; asthma; bacterial infection; child; child hospitalization; Chlamydophila pneumoniae; clinical feature; controlled study; Coronavirus; disease exacerbation; disease severity; Enterovirus; female; France; human; immunofluorescence test; Influenza virus; major clinical study; male; Mycoplasma pneumoniae; Parainfluenza virus; polymerase chain reaction; priority journal; Respiratory syncytial pneumovirus; Rhinovirus; serology; virus detection; virus infection; wheezing; Adolescent; Age Factors; Asthma; Child; Child, Preschool; Chlamydophila pneumoniae; Female; France; Hospitalization; Humans; Male; Mycoplasma pneumoniae; Prospective Studies; RNA Viruses; Severity of Illness Index","Pin, I., Pilenko-McGuigan, C., Cans, C., Gousset, M., Fison, C., Epidemiologie de l'allergie respiratoire de l'enfant (1999) Arch Pediatr [Suppl], 6, pp. 6-13; Mitchell, E.A., Asthma epidemiology: Clues and puzzles (1999) Pediatr Pulmonol [Suppl], 18, pp. 31-33; Warner, J.O., Naspitz, C.K., Cropp, G.J.A., Third international pediatric consensus statement on the management of childhood asthma (1998) Pediatr Pulmonol, 25, pp. 1-17; Nicholson, K.G., Kent, J., Ireland, D.C., Respiratory viruses and exacerbation of asthma in adults (1993) Br Med J [Clin Res], 307, pp. 982-986; Pattemore, P.K., Johnston, S.L., Bardin, P.G., Viruses as precipitants of asthma symptoms. 1. Epidemiology (1992) Clin Exp Allergy, 22, pp. 325-336; Johnston, S.L., Role of viral and atypical bacterial pathogens in asthma pathogenesis (1999) Pediatr Pulmonol [Suppl], 18, pp. 141-143; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Lampe, F., Josephs, L., Symington, P., Holgate, S., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) Br Med J [Clin Res], 310, pp. 1225-1229; Cunningham, A.F., Johnston, S.L., Julious, S.A., Lampe, F.C., Ward, M.E., Chronic Chlamydia pneumoniae infection and asthma exacerbations in children (1998) Eur Respir J, 11, pp. 345-349; Guidelines on the management of asthma (1993) Thorax [Suppl], 48, pp. 1-24; Andreolletti, L., Lesay, M., Deschildre, A., Lambert, V., Dewilde, A., Wattre, P., Differential detection of rhinoviruses RNA sequences associated with classical immunofluorescence assay detection of respiratory virus antigens in nasopharyngeal swabs from infants with bronchiolitis (2000) J Med Virol, 61, pp. 341-346; Gama, R.E., Horsnell, P.R., Hughes, P.J., North, C., Bruce, C.B., Al-Nakib, W., Stanway, G., Amplification of rhinovirus specific nucleic acids from clinical samples using the polymerase chain reaction (1989) J Med Virol, 28, pp. 73-77; Johnston, S.L., Pattemore, P.K., Sanderson, G., Smith, S., Campbell, M.J., Josephs, L.K., Cunningham, A., Holgate, S.T., The relationship between upper respiratory infections with hospital admissions for asthma: A time trend analysis (1996) Am J Respir Crit Care Med, 154, pp. 654-660; Johnston, S.L., Viral infections in children with existing asthma (1996) From Genetics to Quality of Life. The Optimal Treatment and Management of Asthma, pp. 102-107. , Chanez P, Bousquet J, Michel FB, Godard P, editors. Seattle: Hogrefe and Huber Publishers; Freymuth, F., Vabret, A., Brouard, J., Toutain, F., Verdon, R., Petitjean, J., Gouarin, S., Guillois, B., Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae infections in exacerbations of asthma in children (1999) J Clin Virol, 13, pp. 131-139; Freymuth, F., Vabret, A., Gallateau-Salle, F., Ferey, J., Eugene, G., Petitjean, J., Gennetay, E., Guillois, B., Detection of respiratory syncytial virus, parainfluenzavirus 3, adenovirus and rhinovirus sequences in respiratory tract of infants by PCR and hybridization (1997) Clin Diagn Virol, 8, pp. 31-40; Johnston, S.L., Sanderson, G., Pattemore, P.K., Smith, S., Bardin, P.G., Bruce, C.B., Lambden, P.R., Holgate, S.T., Use of polymerase chain reaction for diagnosis of picornavirus infection in subjects with or without respiratory symptoms (1993) J Clin Microbiol, 31, pp. 111-117; Monto, A.S., Studies of the community and family: Acute respiratory illness and infection (1994) Epidemiol Rev, 16, pp. 351-373; Makela, M.J., Puhakka, T., Ruuskanen, O., Leinonen, M., Saikku, P., Kimpimaki, M., Blomqvist, S., Arstila, P., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Dallo, S.F., Baseman, J.B., Intracellular DNA replication and longterm survival of pathogenic mycoplasmas (2000) Microb Pathog, 29, pp. 301-309; Gendrel, D., Intracellular pathogens and asthma: Mycoplasma pneumoniae and Chlamydia pneumoniae in paediatric patients (1996) Eur Respir Rev, 38, pp. 231-234; Hahn, D.L., Intracellular pathogens and their role in asthma: Chlamydia pneumoniae in adult patients (1996) Eur Respir Rev, 38, pp. 224-230; Grayston, J.T., Campbell, L.A., Kuo, C.C., Mordhorst, C.H., Saikku, P., Thom, D.H., Wang, S.P., A new respiratory tract pathogen: Chlamydia pneumoniae strain TWAR (1990) J Infect Dis, 161, pp. 618-625; Hahn, D.L., Peeling, R.W., Dillon, E., McDonald, R., Saikku, P., Serologic markers for Chlamydia pneumoniae in asthma (2000) Ann Allergy Asthma Immunol, 84, pp. 227-233; Tomasi, T.B., Grey, H.M., Structure and function of immunoglobulin A (1972) Prog Allergy, 16, pp. 181-213; Emre, U., Roblin, P., Gelling, M., Dumornay, W., Rao, M., Hammerschlag, M.R., Schachter, J., The association of Chlamydia pneumoniae infection and reactive airway disease in children (1994) Arch Pediatr Adolesc Med, 148, pp. 727-732; Clyde, W.A., Clinical overview of typical Mycoplasma pneumoniae infections (1993) Clin Infect Dis [Suppl], 17, pp. 32-36; Mygind, N., Gwaltney, J.M., Winther, B., Owen Hendley, J., The common cold and asthma (1999) Allergy [Suppl], 54, pp. 146-159; Papadopoulos, N.G., Johnston, S.L., Rhinovirus as pathogens of lower respiratory tract (2000) Can Respir J, 7, pp. 409-414; Gern, J.E., Calhoun, W., Swenson, C., Shen, G., Busse, W.W., Rhinovirus infection preferentially increases lower responsiveness in allergic subjects (1997) Am J Respir Crit Care Med, 155, pp. 1872-1876; Come, J.M., Holgate, S.T., Mechanisms of virus induced exacerbations of asthma (1997) Thorax, 52, pp. 380-389; Welliver, R.C., Immunologic mechanisms of virus-induced wheezing and asthma (1999) J Pediatr, 135, pp. 14-20; Erb, K.J., Atopic disorders: A default pathway in the absence of infection? (1999) Immunol Today, 20, pp. 317-322; Hahn, D.L., Bukstein, D., Luksin, G., Zeitz, H., Evidence for Chlamydia pneumoniae infection in steroid-dependant asthma (1998) Ann Allergy Asthma Immunol, 80, pp. 45-49; Black, P., The use of macrolides in the treatment of asthma (1996) Eur Respir Rev, 38, pp. 240-243","Thumerelle, C.; Secretariat de Pneumologie Infantile, Hôpital Jeanne de Flandre, CHU de Lille, 59037 Lille Cedex, France; email: adeschildre@chru-lille.fr",,,87556863,,PEPUE,"12526066","English","Pediatr. Pulmonol.",Article,"Final",,Scopus,2-s2.0-12244303678
"Narayanan K., Chen C.-J., Maeda J., Makino S.","7101933409;56288577100;23135329700;7403067550;","Nucleocapsid-independent specific viral RNA packaging via viral envelope protein and viral RNA signal",2003,"Journal of Virology","77","5",,"2922","2927",,75,"10.1128/JVI.77.5.2922-2927.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037369042&doi=10.1128%2fJVI.77.5.2922-2927.2003&partnerID=40&md5=5c361b89748479e114f9e1bbfff0b130","Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan","Narayanan, K., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Chen, C.-J., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; Maeda, J., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan; Makino, S., Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States","For any of the enveloped RNA viruses studied to date, recognition of a specific RNA packaging signal by the virus's nucleocapsid (N) protein is the first step described in the process of viral RNA packaging. In the murine coronavirus a selective interaction between the viral transmembrane envelope protein M and the viral ribonucleoprotein complex, composed of N protein and viral RNA containing a short cis-acting RNA element, the packaging signal, determines the selective RNA packaging into virus particles. In this report we show that expressed coronavirus envelope protein M specifically interacted with coexpressed noncoronavirus RNA transcripts containing the short viral packaging signal in the absence of coronavirus N protein. Furthermore, this M protein-packaging signal interaction led to specific packaging of the packaging signal-containing RNA transcripts into coronavirus-like particles in the absence of N protein. These findings not only highlight a novel RNA packaging mechanism for an enveloped virus, where the specific RNA packaging can occur without the core or N protein, but also point to a new, biologically important general model of precise and selective interaction between transmembrane proteins and specific RNA elements.",,"envelope protein M; guanine nucleotide binding protein; ribonucleoprotein; unclassified drug; virus envelope protein; virus RNA; article; Coronavirus; nonhuman; priority journal; protein expression; protein protein interaction; RNA processing; RNA transcription; signal transduction; virus nucleocapsid; virus particle; Animals; Mice; Murine hepatitis virus; Nucleocapsid; Nucleocapsid Proteins; RNA, Viral; Signal Transduction; Viral Matrix Proteins; Virion; Virus Assembly","Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., Warren, G., Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus (1984) Nature, 308, pp. 751-752; Baric, R.S., Nelson, G.W., Fleming, J.O., Deans, R.J., Keck, J.G., Casteel, N., Stohlman, S.A., Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription (1988) J. 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Virol., 75, pp. 1312-1324; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., Monoclonal antibodies to the matrix (E1) glycoprotein of mouse hepatitis virus protect mice from encephalitis (1989) Virology, 168, pp. 162-167; Fosmire, J.A., Hwang, K., Makino, S., Identification and characterization of a coronavirus packaging signal (1992) J. Virol., 66, pp. 3522-3530; Fuerst, T.R., Niles, E.G., Studier, F.W., Moss, B., Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8122-8126; Gosert, R., Kanjanahaluethai, A., Egger, D., Blenz, K., Baker, S.C., RNA replication of mouse hepatitis virus takes place at double-membrane vesicles (2002) J. Virol., 76, pp. 3697-3708; Hirano, N., Fujiwara, K., Hino, S., Matumoto, M., Replication and plaque formation of mouse hepatitis virus (MHV-2) in mouse cell line DBT culture (1974) Arch. Gesamte Virusforsch., 44, pp. 298-302; Holmes, K.V., Doller, E.W., Sturman, L.S., Tunicamycin resistant glycosylation of coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein (1981) Virology, 115, pp. 334-344; Joo, M., Banerjee, S., Makino, S., Replication of murine coronavirus defective interfering RNA from negative-strand transcripts (1996) J. Virol., 70, pp. 5769-5776; Kim, K.H., Narayanan, K., Makino, S., Assembled coronavirus from complementation of two defective interfering RNAs (1997) J. Virol., 71, pp. 3922-3931; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Kuo, L., Masters, P.S., Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus (2002) J. Virol., 76, pp. 4987-4999; Lai, M.M., Baric, R.S., Brayton, P.R., Stohlman, S.A., Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus (1984) Proc. Natl. Acad. Sci. USA, 81, pp. 3626-3630; Lai, M.M., Stohlman, S.A., RNA of mouse hepatitis virus (1978) J. Virol., 26, pp. 236-242; Locker, J.K., Opstelten, D.J., Ericsson, M., Horzinek, M.C., Rottier, P.J., Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention (1995) J. Biol. Chem., 270, pp. 8815-8821; Lopez, S., Yao, J.S., Kuhn, R.J., Strauss, E.G., Strauss, J.H., Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses (1994) J. Virol., 68, pp. 1316-1323; Maeda, J., Maeda, A., Makino, S., Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells (1999) Virology, 263, pp. 265-272; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Shieh, C.K., Keck, J.G., Lai, M.M., Defective interfering particles of murine coronavirus: Mechanism of synthesis of defective viral RNAs (1988) Virology, 163, pp. 104-111; Makino, S., Taguchi, F., Hirano, N., Fujiwara, K., Analysis of genomic and intracellular viral RNAs of small plaque mutants of mouse hepatitis virus, JHM strain (1984) Virology, 139, pp. 138-151; Muriaux, D., Mirro, J., Harvin, D., Rein, A., RNA is a structural element in retrovirus particles (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 5246-5251; Narayanan, K., Maeda, A., Maeda, J., Makino, S., Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells (2000) J. Virol., 74, pp. 8127-8134; Narayanan, K., Makino, S., Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging (2001) J. Virol., 75, pp. 9059-9067; Rolls, M.M., Webster, P., Balba, N.H., Rose, J.K., Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA (1994) Cell, 79, pp. 497-506; Rottier, P.J., Horzinek, M.C., Van der Zeijst, B.A., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Simons, K., Garoff, H., The budding mechanisms of enveloped animal viruses (1980) J. Gen. Virol., 50, pp. 1-21; Spaan, W., Delius, H., Skinner, M., Armstrong, J., Rottier, P., Smeekens, S., Van der Zeijst, B.A., Siddell, S.G., Coronavirus mRNA synthesis involves fusion of non-contiguous sequences (1983) EMBO J., 2, pp. 1839-1844; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Suomalainen, M., Liljestrom, P., Garoff, H., Spike protein-nucleocapsid interactions drive the budding of alphaviruses (1992) J. Virol., 66, pp. 4737-4747; Tooze, J., Tooze, S., Warren, G., Replication of coronavirus MHV-A59 in sac-cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Van der Most, R.G., Bredenbeek, P.J., Spaan, W.J., A domain at the 3′ end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs (1991) J. Virol., 65, pp. 3219-3226; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Woo, K., Joo, M., Narayanan, K., Kim, K.H., Makino, S., Murine coronavirus packaging signal confers packaging to nonviral RNA (1997) J. Virol., 71, pp. 824-827; Yamada, Y.K., Takimoto, K., Yabe, M., Taguchi, F., Acquired fusion activity of a murine coronavirus MHV-2 variant with mutations in the proteolytic cleavage site and the signal sequence of the S protein (1997) Virology, 227, pp. 215-219; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zhao, H., Garoff, H., Role of cell surface spikes in alphavirus budding (1992) J. Virol., 66, pp. 7089-7095","Makino, S.; Department of Microbiology, University of Texas Medical Branch, Galveston, TX 77555-1019, United States; email: shmakino@utmb.edu",,,0022538X,,JOVIA,"12584316","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037369042
"Halbur P.G., Pallarés F.J., Opriessnig T., Vaughn E.M., Paul P.S.","7005935318;7003845129;6602341858;7007145803;7202714004;","Pathogenicity of three isolates of porcine respiratory coronavirus in the USA",2003,"Veterinary Record","152","12",,"358","361",,4,"10.1136/vr.152.12.358","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344838446&doi=10.1136%2fvr.152.12.358&partnerID=40&md5=6aff78dd77058adfef228a7efdcedb88","College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Facultad de Veterinaria, Universidad de Murcia, 30071 Murcia, Spain; Boehringer Ingelheim Animal Health, Ames, IA 50010, United States; University of Nebraska, Lincoln, NE 68588, United States","Halbur, P.G., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Pallarés, F.J., Facultad de Veterinaria, Universidad de Murcia, 30071 Murcia, Spain; Opriessnig, T., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Vaughn, E.M., Boehringer Ingelheim Animal Health, Ames, IA 50010, United States; Paul, P.S., University of Nebraska, Lincoln, NE 68588, United States","The pathogenicity of three isolates of porcine respiratory coronavirus (AR310, LEPP and 1894) from the USA was assessed in specific pathogen-free pigs. Pigs inoculated with 1894 developed mild respiratory disease and pigs inoculated with AR310 and LEPP developed moderate respiratory disease from fout to 10 days after they were inoculated, but all the pigs recovered fully by 14 days after inoculation. Gross and microscopic examination revealed mild (1894) to moderate (AR310 and LEPP) multifocal bronchointerstitial pneumonia from four to 10 days after inoculation. The lesions were characterised by necrotising bronchiolitis, septal infiltration with mononuclear cells, and a mixed alveolar exudate. No clinical signs or microscopic lesions were observed in cotnrol pigs that had not been inoculated.",,"animal tissue; article; bronchiolitis; bronchopneumonia; cell infiltration; controlled study; Coronavirus; disease course; disease severity; experimental infection; germfree animal; inoculation; interstitial pneumonia; lung alveolus; lung extravascular fluid; microscopy; mononuclear cell; nonhuman; respiratory tract infection; swine; United States; virus isolation; virus pathogenesis; virus pneumonia; virus strain; Animalia; Coronavirus; Porcine respiratory coronavirus; Suidae; Sus scrofa","Cox, E., Hooyberghs, J., Pensaert, M.B., Sites of replication of a porcine repiratory coronavirus related to transmissible gastroeteritis virus (1990) Research in Veterinary Science, 48, pp. 165-169; Duret, C., Brun, A., Guilmoto, H., Dauvergne, M., Isolement, identification et pathogène chez le porc d'un coronavirus apparenté au virus de la gastro-entérite transmissible (1988) Recueil De Médecine Vt́érinaire De L'Ecole D'Alfort, 164, pp. 221-226; Halbur, P.G., Paul, P.S., Frey, M.L., Landgraf, J., Eernisse, K., Meng, X.J., Lum, M.A., Rathje, J.A., Comparison of the pathogenicity of two US porcine reproductive and respiratory syndrome virus isolates with the Lelystad virus (1995) Veterinary Pathology, 32, pp. 648-660; Halbur, P.G., Paul, P.S., Meng, X.J., Lum, M.A., Andrews, J.J., Rathje, J.A., Comparative pathogenicity of nine US porcine reproductive and respiratory syndrome virus (PRRSV) isolates in a five-week-old cesarean-derived, colostrum-deprived pig model (1996) Journal of Veterinary Diagnostic Investigation, 8, pp. 11-20; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with procine respiratory coronavirus isolate AR310 (1993) Journal of Veterinary Diagnostic Investigation, 5, pp. 184-188; Hayes, J., Sestak, K., Myers, G., Kim, L., Stromberg, P., Saif, L., Dual infection of nursery pigs with porcine reproductive and respiratory syndrome virus and porcine respiratory coronavirus: Preliminary findings (1998), p. 83. , Proceedings of the 41st Annual Meeting of the American Association of Veterinary Laboratory Diagnosticians. Minneapolis, USA, October 3 to 9, 1998; Hill, H.T., Biwer, J.D., Wood, R.D., Wesley, R.D., Porcine respiratory coronavirus isolated from two US swine herds (1990), pp. 333-335. , Proceedings of the 21st Annual Meeting of the American Association of Swine Practioners. Denver, USA, March 4 to 6, 1990; Jabrane, A., Girad, C., Elazhary, Y., Pathogenicity of porcine respiratory coronavirus isolated in Quebec (1994) Canadian Veterinary Journal, 35, pp. 86-92; Kim, L., Hayes, J., Lewis, P., Parwani, A.V., Chang, K.O., Saif, L.J., Molecular characterization and pathogenesis of transmissible gastroenteristis coronavirus (TGEV) and porcine respiratory coronavirus (PRCV) field isolates co-circulating in a swine herd (2000) Archives of Virology, 145, pp. 1133-1147; Laude, H., Van Reeth, K., Pensaert, M., Porcine respiratory coronavirus: Molecular features and virus-host interactions (1993) Veterinary Research, 24, pp. 125-150; Mcgoldrick, A., Lowings, J.P., Paton, D.J., Characterization of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a (1999) Archives of Virology, 144, pp. 763-770; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathologenicity of experimental infection with 'pneumotropic' porcine respiratory coronavirus (1989) Research in Veterinary Science, 47, pp. 23-29; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Veterinary Quarterly, 8, pp. 257-261; Pensaert, M.B., Cox, E., Porcine respiratory coronavirus related to transmissible gastroenteritis virus (1989) Agri-practice, 10, pp. 17-21; Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) Journal of General Virology, 71, pp. 2599-2607; Sirinarumitr, T., Paul, P.S., Kluge, J.P., Halbur, P.G., In situ hybridization technique for the detection of swine enteric and respiratory coronaviruses, transmissible gastroenteritis virus (TGEV) and porcine respiratory coronavirus (PRCV) in formalin-fixed paraffin-embedded tissues (1996) Journal of Virological Methods, 56, pp. 149-160; Vannier, P., Disorders induced by the experimental infection of pigs with the porcine respiratory coronavirus (1990) Journal of Veterinary Medicine B, 37, pp. 177-180; Van Reeth, K., Nauwynck, H., Pensaert, M., Dual infections of feeder pigs with porcine reproductive and respiratory syndrome virus followed by porcine respiratory coronavirus or swine influenza virus: A clinical and virological study (1996) Veterinary Microbiology, 48, pp. 325-335; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) Journal of Clinical Microbiology, 32, pp. 1809-1812; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3 and 3-1 genes (1995) Journal of Virology, 69, pp. 3176-3184; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) Journal of Virology, 65, pp. 3369-3373; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) Journal of Veterinary Diagnostic Investigation, 2, pp. 312-317; Zhu, X.Z., Paul, P.S., Vaughn, E.M., Morales, A., Characterization and reactivity of monoclonal antibodies to the Miller strain of transmissible gastroenteritis virus (TGEV) of swine (1990) American Journal of Veterinary Research, 51, pp. 232-238","Halbur, P.G.; College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States",,"British Veterinary Association",00424900,,VETRA,"12678259","English","Vet. Rec.",Article,"Final",,Scopus,2-s2.0-0344838446
"Ortego J., Sola I., Almazán F., Ceriani J.E., Riquelme C., Balasch M., Plana J., Enjuanes L.","35254237800;7003336781;6603712040;6507634901;7004010730;6602693824;11539108300;7006565392;","Transmissible gastroenteritis coronavirus gene 7 is not essential but influences in vivo virus replication and virulence",2003,"Virology","308","1",,"13","22",,85,"10.1016/S0042-6822(02)00096-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037473293&doi=10.1016%2fS0042-6822%2802%2900096-X&partnerID=40&md5=80863507b116414aac179675ed920448","Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain","Ortego, J., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Sola, I., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Almazán, F., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Ceriani, J.E., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Riquelme, C., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Balasch, M., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Plana, J., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Enjuanes, L., Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Transmissible gastroenteritis coronavirus (TGEV) contains eight overlapping genes that are expressed from a 3′-coterminal nested set of leader-containing mRNAs. To facilitate the genetic manipulation of the viral genome, genes were separated by duplication of transcription regulating sequences (TRSs) and introduction of unique restriction endonuclease sites at the 5′ end of each gene using an infectious cDNA clone. The recombinant TGEV (rTGEV) replicated in cell culture with similar efficiency to the wild-type virus and stably maintained the modifications introduced into the genome. In contrast, the rTGEV replication level in the lungs and gut of infected piglets and virulence were significantly reduced. rTGEV in which gene 7 expression was abrogated (rTGEV-Δ7) were recovered from cDNA constructs, indicating that TGEV gene 7 was a nonessential gene for virus replication. Interestingly, in vivo infections with rTGEV-Δ7 showed an additional reduction in virus replication in the lung and gut, and in virulence, indicating that TGEV gene 7 influences virus pathogenesis. © 2003 Elsevier Science (USA). All rights reserved.",,"complementary DNA; messenger RNA; restriction endonuclease; animal model; animal tissue; article; cell culture; controlled study; gene duplication; gene expression; gene sequence; genetic manipulation; in vivo study; intestine; lung; molecular cloning; newborn; nonhuman; pathogenesis; priority journal; swine; Transmissible gastroenteritis virus; virogenesis; virus gene; virus infection; virus replication; virus virulence; Coronavirus; Transmissible gastroenteritis virus","Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Armstrong, J., Smeekens, S., Rottier, P., Sequence of the nucleocapsid gene from murine coronavirus MHV-A59 (1983) Nucleic Acids Res., 11, pp. 883-891; Boursnell, M.E.G., Binns, M.M., Foulds, I.J., Brown, T.D.K., Sequences of the nucleocapsid genes from two strains of avian infectious bronchitis virus (1985) J. Gen. Virol., 66, pp. 573-580; Cowley, J.A., Walker, P.J., The complete genome sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses (2002) Arch. Virol., 147, pp. 1977-1987; De Haan, C.A.M., Masters, P.S., Shen, S., Weiss, S., Rottier, P.J.M., The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host (2002) Virology, 296, pp. 177-189; De Vries, A.A.F., Glaser, A.L., Raamsman, M.J.B., De Haan, C.A.M., Sarnataro, S., Godeke, G.J., Rottier, P.J.M., Genetic manipulation of equine arteritis virus using full-length cDNA clones: Separation of overlapping genes and expression of a foreign epitope (2000) Virology, 270, pp. 84-97; Delmas, B., Gelfi, J., Sjöström, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1994) Adv. Exp. Med. Biol., 342, pp. 293-298; Denison, M.R., Sims, A.C., MHV-A59 gene 1 proteins are associated with two distinct membrane populations (2001) Adv. Exp. Med. Biol., 494, pp. 655-661; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, pp. 835-849. , M.H.V. van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carsten, M.K. Estes, S.M. Lemon, D.J. McGeoch, J. Maniloff, M.A. Mayo, C.R. Pringle, & R.B. Wickner. New York: Classification and Nomenclature of Viruses, Academic Press; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidovirales (2000) Virus Taxonomy, pp. 827-834. , M.H.V. van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carsten, M.K. Estes, S.M. Lemon, D.J. McGeoch, J. Maniloff, M.A. Mayo, C.R. Pringle, & R.B. Wickner. New York: Classification and Nomenclature of Viruses, Academic Press; Garwes, D.J., Stewart, F., Britton, P., The polypeptide of Mr 14000 of porcine transmissible gastroenteritis virus: Gene assignment and intracellular location (1989) J. Gen. Virol., 70, pp. 2495-2499; González, J.M., Penzes, Z., Almazán, F., Calvo, E., Enjuanes, L., Stabilization of a full-length infectious cDNA clone of transmissible gastroenteritis coronavirus by the insertion of an intron (2002) J. Virol., 76, pp. 4655-4661; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., Groot, P.J., The molecular genetics of feline coronavirus comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hiscox, J.A., The nucleolus - A gateway to viral infection? (2002) Arch. Virol., 147, pp. 1077-1089; Kamahora, T., Soe, L.H., Lai, M.M.C., Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus OC43 (1989) Virus Res., 12, pp. 1-9; Kennedy, M., Boedeker, N., Gibbs, P., Kania, S., Deletions in the 7a ORF of feline coronavirus associated with an epidemic of feline infectious peritonitis (2001) Vet. Microbiol., 81, pp. 227-234; Kuo, L., Masters, P.S., Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus (2002) J. Virol., 76, pp. 4987-4999; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lapps, W., Hogue, B.G., Brian, D.A., Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes (1987) Virology, 157, pp. 47-57; Mayo, M.A., A summary of taxonomic changes recently approved by ICTV (2002) Arch. Virol., 147, pp. 1655-1656; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Med. Vet. Sci., 30, pp. 190-198; Motulsky, H., Comparing two paired groups: paired t and Wilcoxon tests (1995) Intuitive Biostatistics, pp. 225-229. , Oxford Univ. Press, New York; Ortego, J., Escors, D., Laude, H., Enjuanes, L., Generation of a replication competent, propagation-deficient virus vector based on the transmissible gastroenteritis coronavirus genome (2002) J. Virol., 76, pp. 11518-11529; Penzes, Z., González, J.M., Calvo, E., Izeta, A., Smerdou, C., Mendez, A., Sánchez, C.M., Enjuanes, L., Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the Purdue virus cluster (2001) Virus Genes, 23, pp. 105-118; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis (1992) Diseases of Swine Seventh ed, pp. 362-386. , A.D. Leman, B.E. Straw, W.L. Mengeling, S. D'Allaire, & D.J. Taylor. Ames, IA: Wolfe Publishing Ltd; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Skinner, M.A., Siddell, S.G., Coding sequence of coronavirus MHV-JHM mRNA 4 (1985) J. Gen. Virol., 66, pp. 593-596; Snijder, E.J., Van Tol, H., Roos, N., Pedersen, K.W., Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex (2001) J. Gen. Virol., 82, pp. 985-994; Tung, F.Y.T., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., Brian, D.A., The 9-kDa hydrophobic protein encoded at the 3′ end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Virology, 186, pp. 676-683; Wertz, G.W., Moudy, R., Ball, L.A., Adding genes to the RNA genome of vesicular stomatitis virus: Positional effects on stability of expression (2002) J. Virol., 76, pp. 7642-7650","Enjuanes, L.; Ctro. Nac. de Biotecnología, Dept. of Molecular and Cell Biology, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,"Academic Press Inc.",00426822,,VIRLA,"12706086","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0037473293
"Haijema B.J., Volders H., Rottier P.J.M.","55893259700;6507537974;7006145490;","Switching species tropism: An effective way to manipulate the feline coronavirus genome",2003,"Journal of Virology","77","8",,"4528","4538",,89,"10.1128/JVI.77.8.4528-4538.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037384422&doi=10.1128%2fJVI.77.8.4528-4538.2003&partnerID=40&md5=d2c18eb68c8786e4f08c3b6eb35ccb64","Institute of Virology, Department of Infectious Diseases, Utrecht University, 3584 CL Utrecht, Netherlands; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","Haijema, B.J., Institute of Virology, Department of Infectious Diseases, Utrecht University, 3584 CL Utrecht, Netherlands; Volders, H., Institute of Virology, Department of Infectious Diseases, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Institute of Virology, Department of Infectious Diseases, Utrecht University, 3584 CL Utrecht, Netherlands, Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands","Feline infectious peritonitis virus (FIPV), a coronavirus, is the causative agent of an invariably lethal infection in cats. Like other coronaviruses, FIPV contains an extremely large positive-strand RNA genome of ca. 30 kb. We describe here the development and use of a reverse genetics strategy for FIPV based on targeted RNA recombination that is analogous to what has been described for the mouse hepatitis virus (MHV) (L. Kuo et al., J. Virol. 74:1393-1406, 2000). In this two-step process, we first constructed by targeted recombination a mutant of FIPV, designated mFIPV, in which the ectodomain of the spike glycoprotein was replaced by that of MHV. This switch allowed for the selection of the recombinant virus in murine cells: mFIPV grows to high titers in these cells but has lost the ability to grow in feline cells. In a second, reverse process, mFIPV was used as the recipient, and the reintroduction of the FIPV spike now allowed for selection of candidate recombinants by their regained ability to grow in feline cells. In this fashion, we reconstructed a wild-type recombinant virus (r-wtFIPV) and generated a directed mutant FIPV in which the initiation codon of the nonstructural gene 7b had been disrupted (FIPVΔ7b). The r-wtFIPV was indistinguishable from its parental virus FIPV 79-1146 not only for its growth characteristics in tissue culture but also in cats, exhibiting a highly lethal phenotype. FIPVΔ7b had lost the expression of its 7b gene but grew unimpaired in cell culture, confirming that the 7b glycoprotein is not required in vitro. We establish the second targeted RNA recombination system for coronaviruses and provide a powerful tool for the genetic engineering of the FIPV genome.",,"glycoprotein; virus protein; animal cell; animal tissue; article; cat; cat disease; controlled study; Coronavirus; fetus; gene disruption; gene expression; in vitro study; Murine hepatitis coronavirus; nonhuman; phenotype; plant growth; priority journal; RNA recombination; start codon; tissue culture; virogenesis; virus genome; virus mutant; virus recombinant; wild type; Amino Acid Sequence; Animals; Base Sequence; Cats; Cells, Cultured; Coronavirus, Feline; Feline Infectious Peritonitis; Genetic Engineering; Membrane Glycoproteins; Mice; Molecular Sequence Data; Murine hepatitis virus; Recombinant Fusion Proteins; Recombination, Genetic; RNA, Viral; Sequence Analysis, DNA; Species Specificity; Viral Envelope Proteins; Viral Nonstructural Proteins; Virulence","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., Reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) J. Virol., 75, pp. 12359-12369; Cavanagh, D., The coronavirus surface protein (1995) The Coronaviridae, pp. 73-103. , S. G. Siddell (ed.). Plenum Press, Inc., New York, N.Y; Chang, R.Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; De Groot, R.J., Andeweg, A.C., Horzinek, M.C., Spaan, W.J., Sequence analysis of the 3′ end of the feline coronavirus FIPV 79-1146 genome: Comparison with the genome of porcine coronavirus TGEV reveals large insertions (1988) Virology, 167, pp. 370-376; De Groot, R.J., Lenstra, J.A., Luytjes, W., Niesters, H.G., Horzinek, M.C., Van der Zeijst, B.A., Spaan, W.J., Sequence and structure of the coronavirus peplomer protein (1987) Adv. Exp. Med. Biol., 218, pp. 31-38; De Groot, R.J.H., Horzinek, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-309. , S. G. Siddell (ed.). Plenum Press, Inc., New York, N.Y; De Haan, C.A., De Wit, M., Kuo, L., Montalto, C., Masters, P.S., Weiss, S.R., Rottier, P.J., O-glycosylation of the mouse hepatitis coronavirus membrane protein (2002) Virus Res., 82, pp. 77-81; De Haan, C.A., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; De Haan, C.A., Smeets, M., Vernooij, F., Vennema, H., Rottier, P.J., Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein (1999) J. Virol., 73, pp. 7441-7452; Delmas, B., Laude, H., Assembly of coronavirus spike protein into trimers and its role in epitope expression (1990) J. Virol., 64, pp. 5367-5375; De Vries, A.A.F.H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Escors, D., Ortego, J., Laude, H., Enjuanes, L., The membrane M protein carboxy terminus binds to transmissible gastroenteritis coronavirus core and contributes to core stability (2001) J. Virol., 75, pp. 1312-1324; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Glaser, A.L., De Vries, A.A.F., Raamsman, M.J.B., Horzinek, M.C., Rottier, P.J.M., An infectious cDNA clone of equine arteritis virus: A tool for for future fundamental studies and vaccine development (1998) Proceedings of the 8th International Conference on Equine Infectious Diseases, pp. 166-176. , W. R. Plowright, P. D. Rossdale, and J. F. Wade (ed.), Dubai. R&W Publications, Newmarket, United Kingdom; Godeke, G.J., De Haan, C.A., Rossen, J.W., Vennema, H., Rottier, P.J., Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein (2000) J. Virol., 74, pp. 1566-1571; Herrewegh, A.A., Smeenk, I., Horzinek, M.C., Rottier, P.J., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Herrewegh, A.A., Vennema, H., Horzinek, M.C., Rottier, P.J., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631; Hsue, B., Hartshorne, T., Masters, P.S., Characterization of an essential RNA secondary structure in the 3′ untranslated region of the murine coronavirus genome (2000) J. Virol., 74, pp. 6911-6921; Hsue, B., Masters, P.S., A bulged stem-loop structure in the 3′ untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J. Virol., 71, pp. 7567-7578; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Kuo, L., Masters, P.S., Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus (2002) J. Virol., 76, pp. 4987-4999; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Semin. Virol., 7, pp. 381-388; Lavi, E., Kuo, L., Haluskey, J.A., Masters, P.S., Targeted recombination between MHV-2 and MHV-A59 to study neurotropic determinants of MHV (1998) Adv. Exp. Med. Biol., 440, pp. 543-547; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J. 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Immunol., 40, pp. 425-433; Narayanan, K., Makino, S., Cooperation of an RNA packaging signal and a viral envelope protein in coronavirus RNA packaging (2001) J. Virol., 75, pp. 9059-9067; Navas, S., Seo, S.H., Chua, M.M., Das Sarma, J., Hingley, S.T., Lavi, E., Weiss, S.R., Role of the spike protein in murine coronavirus-induced hepatitis: An in vivo study using targeted RNA recombination (2001) Adv. Exp. Med. Biol., 494, pp. 139-144; Navas, S., Seo, S.H., Chua, M.M., Sarma, J.D., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J. Virol., 75, pp. 2452-2457; Nguyen, V.P., Hogue, B.G., Protein interactions during coronavirus assembly (1997) J. Virol., 71, pp. 9278-9284; Olsen, C.W., Corapi, W.V., Ngichabe, C.K., Baines, J.D., Scott, F.W., Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages (1992) J. Virol., 66, pp. 956-965; Ontiveros, E., Kuo, L., Masters, P.S., Perlman, S., Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS (2001) Virology, 289, pp. 230-238; Opstelten, D.J., Raamsman, M.J., Wolfs, K., Horzinek, M.C., Rottier, P.J., Envelope glycoprotein interactions in coronavirus assembly (1995) J. Cell Biol., 131, pp. 339-349; Penzes, Z., Tibbles, K., Shaw, K., Britton, P., Brown, T.D., Cavanagh, D., Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus (1994) Virology, 203, pp. 286-293; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Rottier, P.J., Spaan, W.J., Horzinek, M.C., Van der Zeijst, B.A., Translation of three mouse hepatitis virus strain A59 subgenomic RNAs in Xenopus laevis oocytes (1981) J. Virol., 38, pp. 20-26; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Snijder, E.J., Den Boon, J.A., Horzinek, M.C., Spaan, W.J., Characterization of defective interfering RNAs of Berne virus (1991) J. Gen. Virol., 72, pp. 1635-1643; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Van der Most, R.G.A.S., Spaan, W.J.M., (1995) Coronavirus Replication, Transcription, and RNA Recombination, pp. 11-31. , Plenum Press, London, United Kingdom; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Vennema, H., Heijnen, L., Rottier, P.J., Horzinek, M.C., Spaan, W.J., A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal (1992) J. Virol., 66, pp. 4951-4956; Vennema, H., Rossen, J.W., Wesseling, J., Horzinek, M.C., Rottier, P.J., Genomic organization and expression of the 3′ end of the canine and feline enteric coronaviruses (1992) Virology, 191, pp. 134-140; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Yount, B., Denison, M.R., Weiss, S.R., Baric, R.S., Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59 (2002) J. Virol., 76, pp. 11065-11078","Rottier, P.J.M.; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, Netherlands; email: P.Rottier@vet.uu.nl",,,0022538X,,JOVIA,"12663759","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037384422
"Breslin J.J., Mørk I., Smith M.K., Vogel L.K., Hemmila E.M., Bonavia A., Talbot P.J., Sjöströ H., Norén O., Holmes K.V.","7004753945;6506805100;44361520000;7102142452;6507872503;6506900911;7102670281;6504277308;7006675786;7201657724;","Human coronavirus 229E: Receptor binding domain and neutralization by soluble receptor at 37°C",2003,"Journal of Virology","77","7",,"4435","4438",,59,"10.1128/JVI.77.7.4435-4438.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037377733&doi=10.1128%2fJVI.77.7.4435-4438.2003&partnerID=40&md5=b6deda2290ee28f8654539650743f7bb","Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Department of Medical Biochemistry, University of Copenhagen, Copenhagen, Denmark; INRS-Institut Armand-Frappier, University of Quebec, Laval, Que., Canada; Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Breslin, J.J., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Mørk, I., Department of Medical Biochemistry, University of Copenhagen, Copenhagen, Denmark; Smith, M.K., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Vogel, L.K., Department of Medical Biochemistry, University of Copenhagen, Copenhagen, Denmark; Hemmila, E.M., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Bonavia, A., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States; Talbot, P.J., INRS-Institut Armand-Frappier, University of Quebec, Laval, Que., Canada; Sjöströ, H., Department of Medical Biochemistry, University of Copenhagen, Copenhagen, Denmark; Norén, O., Department of Medical Biochemistry, University of Copenhagen, Copenhagen, Denmark; Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Center, Denver, CO 80262, United States, Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States","Truncated human coronavirus HCoV-229E spike glycoproteins containing amino acids 407 to 547 bound to purified, soluble virus receptor, human aminopeptidase N (hAPN). Soluble hAPN neutralized the infectivity of HCoV-229E virions at 37°C, but not 4°C. Binding of hAPN may therefore trigger conformational changes in the viral spike protein at 37°C that facilitate virus entry.",,"amino acid; aminopeptidase; virus glycoprotein; virus receptor; article; controlled study; Coronavirus; enzyme binding; nonhuman; priority journal; protein conformation; receptor binding; temperature dependence; virion; virus cell interaction; virus infectivity; Amino Acid Sequence; Animals; Antigens, CD13; Binding Sites; Cell Line; Coronavirus 229E, Human; Humans; Membrane Glycoproteins; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Receptors, Virus; Sequence Deletion; Solubility; Viral Envelope Proteins","Ashmun, R.A., Look, A.T., Metalloprotease activity of CD13/ aminopeptidase N on the surface of human myeloid cells (1990) Blood, 75, pp. 462-469; Bonavia, A., Zelus, B.D., Wentworth, D.E., Talbot, P.J., Holmes, K.V., Identification of the receptor binding domain of HCoV-229E spike glycoprotein (2003) J. 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Wright (ed.), Marcel Dekker, New York, N.Y; Godet, M., Grosclaude, J., Delmas, B., Laude, H., Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein (1994) J. Virol., 68, pp. 8008-8016; Gomez Yafal, A., Kaplan, G., Racaniello, V.R., Hogle, J.M., Characterization of poliovirus conformational alteration mediated by soluble cell receptors (1993) Virology, 197, pp. 501-505; Greve, J.M., Forte, C.P., Marlor, C.W., Meyer, A.M., Hoover-Litty, H., Wunderlich, D., McClelland, A., Mechanisms of receptor-mediated rhinovirus neutralization defined by two soluble forms of ICAM-1 (1991) J. Virol., 65, pp. 6015-6023; Hansen, A.S., Noren, O., Sjostrom, H., Werdelin, O., A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules (1993) Eur. J. 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B. C. M. Kenny (ed.), BIOS Scientific Publishers, Oxford, United Kingdom; Powell, R.M., Ward, T., Evans, D.J., Almond, J.W., Interaction between echovirus 7 and its receptor, decay-accelerating factor (CD55): Evidence for a secondary cellular factor in A-particle formation (1997) J. Virol., 71, pp. 9306-9312; Riemann, D., Kehlen, A., Langner, J., CD13 - Not just a marker in leukemia typing (1999) Immunol. Today, 20, pp. 83-88; Signoret, N., Poignard, P., Blanc, D., Sattentau, Q.J., Human and simian immunodeficiency viruses: Virus-receptor interactions (1993) Trc Ads Microbiol., 1, pp. 328-333; Sjostrom, H., Noren, O., Olsen, J., Structure and function of aminopeptidase N (2000) Cellular Peptidases in Immune Functions and Diseases 2, pp. 25-34. , J. A. S. Langner (ed.), Kluwer Academic/Plenum Publishers, New York, N.Y; Stegmann, T., Membrane fusion mechanisms: The influenza hemagglutinin paradigm and its implications for intracellular fusion (2000) Traffic, 1, pp. 598-604; Tresnan, D.B., Levis, R., Holmes, K.V., Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I (1996) J. Virol., 70, pp. 8669-8674; Vogel, L.K., Noren, O., Sjostrom, H., The apical sorting signal on human aminopeptidase N is not located in the stalk but in the catalytic head group (1992) FEBS Lett., 308, pp. 14-17; Wiley, D.C., Skehel, J.J., The structure and function of the hemagglutinin membrane glycoprotein of influenza virus (1987) Annu. Rev. Biochem., 56, pp. 365-394; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Zelus, B.D., Schickli, J.H., Blau, D.M., Weiss, S.R., Holmes, K.V., Confirmational changes in the spike glycoprotein of murine coronavirus are induced at 37°C either by soluble murine CEACAMI receptor glycoproteins or by pH 8 (2003) J. Virol., 77, pp. 830-840; Zelus, B.D., Wessner, D.R., Williams, R.K., Pensiero, M.N., Phibbs, F.T., DeSouza, M., Dveksler, G.S., Holmes, K.V., Purified, soluble recombinant mouse hepatitis virus receptor, Bgp1b, and Bgp2 murine coronavirus receptors differ in mouse hepatitis virus binding and neutralizing activities (1998) J. Virol., 72, pp. 7237-7244","Holmes, K.V.; Department of Microbiology, School of Medicine, Univ. of Colorado Hlth. Sci. Center, 4200 East 9th Ave., Denver, CO 80262, United States; email: kathryn.holmes@uchsc.edu",,,0022538X,,JOVIA,"12634402","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037377733
"Kuo L., Masters P.S.","7101601942;7006234572;","The small envelope protein E is not essential for murine coronavirus replication",2003,"Journal of Virology","77","8",,"4597","4608",,109,"10.1128/JVI.77.8.4597-4608.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037383461&doi=10.1128%2fJVI.77.8.4597-4608.2003&partnerID=40&md5=7ed1df8ab829c6534810e9d7734a92be","New York State Department of Health, University at Albany, State University of New York, Albany, NY 12201, United States; Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","Kuo, L., New York State Department of Health, University at Albany, State University of New York, Albany, NY 12201, United States; Masters, P.S., New York State Department of Health, University at Albany, State University of New York, Albany, NY 12201, United States, Department of Biomedical Sciences, University at Albany, State University of New York, Albany, NY 12201, United States, David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States","The importance of the small envelope (E) protein in the assembly of coronaviruses has been demonstrated in several studies. While its precise function is not clearly defined, E is a pivotal player in the morphogenesis of the virion envelope. Expression of the E protein alone results in its incorporation into vesicles that are released from cells, and the coexpression of the E protein with the membrane protein M leads to the assembly of coronavirus-like particles. We have previously generated E gene mutants of mouse hepatitis virus (MHV) that had marked defects in viral growth and produced virions that were aberrantly assembled in comparison to wild-type virions. We have now been able to obtain a viable MHV mutant in which the entire E gene, as well as the nonessential upstream genes 4 and 5a, has been deleted. This mutant (ΔE) was obtained by a targeted RNA recombination method that makes use of a powerful host range-based selection system. The ΔE mutant produces tiny plaques with an unusual morphology compared to plaques formed by wild-type MHV. Despite its low growth rate and low infectious titer, the ΔE mutant is genetically stable, showing no detectable phenotypic changes after several passages. The properties of this mutant provide further support for the importance of E protein in MHV replication, but surprisingly, they also show that E protein is not essential.",,"envelope protein; isoprotein; RNA; animal cell; article; gene deletion; genetic stability; growth rate; host range; morphology; mouse; Murine hepatitis coronavirus; nonhuman; phenotypic variation; priority journal; RNA recombination; viral genetics; virion; virogenesis; virus gene; virus mutant; virus plaque; virus replication; virus titration; wild type; Amino Acid Sequence; Animals; Base Sequence; Gene Deletion; Mice; Murine hepatitis virus; Plaque Assay; Recombination, Genetic; RNA, Viral; Viral Envelope Proteins; Virus Replication","Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. 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Virol., 65, pp. 5605-5608; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Masters, P.S.; David Axelrod Institute, Wadsworth Center, NYSDOH, New Scotland Ave., Albany, NY 12201-2002, United States; email: masters@wadsworth.org",,,0022538X,,JOVIA,"12663766","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037383461
"Navas S., Weiss S.R.","7003695377;57203567044;","Murine coronavirus-induced hepatitis: JHM genetic background eliminates A59 spike-determined hepatotropism",2003,"Journal of Virology","77","8",,"4972","4978",,43,"10.1128/JVI.77.8.4972-4978.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037384952&doi=10.1128%2fJVI.77.8.4972-4978.2003&partnerID=40&md5=fe6ad457b714a01b45ee426c40fcfa1b","Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Navas, S., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States","Recombinant murine coronaviruses, differing only in the spike gene and containing the strain A59 (moderately hepatotropic) and JHM (neurotropic) spike genes in the background of the JHM genome, were compared for the ability to replicate in the liver and induce hepatitis in weanling C57BL/6 mice. Interestingly, expression of the A59 spike glycoprotein within the background of the neurotropic JHM strain does not reproduce the A59 hepatotropic phenotype. Thus, the JHM genetic background plays a dominant role over the spike in the determination of hepatotropism.",,"animal cell; animal tissue; article; controlled study; Coronavirus; hepatitis; liver; mouse; nonhuman; phenotype; priority journal; protein expression; virogenesis; virus genome; virus replication; Animals; Hepatitis, Viral, Animal; Liver; Male; Membrane Glycoproteins; Mice; Mice, Inbred C57BL; Murine hepatitis virus; Recombination, Genetic; Viral Envelope Proteins; Virulence","Batts, K.P., Ludwig, J., Chronic hepatitis: An update on terminology and reporting (1995) Am. J. Surg. Pathol., 19, pp. 1409-1417; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. 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Virol., 72, pp. 9628-9636; Marten, N.W., Stohlman, S.A., Bergmann, C.C., MHV infection of the CNS: Mechanisms of immune-mediated control (2001) Viral Immunol., 14, pp. 1-18; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv. Virus Res., 53, pp. 245-264; Matthews, A.E., Weiss, S.R., Paterson, Y., Murine hepatitis virus: A model for virus-induced CNS demyelination (2002) J. Neurovirol., 8, pp. 76-85; Navas, S., Seo, S.H., Chua, M.M., Das Sarma, Y., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J. Virol., 75, pp. 2452-2457; Ning, Q.M., Liu, M., Kongkham, P., Lai, M.M., Marsden, P.A., Tseng, J., Pereira, B., Levy, G., The nucleocapsid protein of murine hepatitis virus type 3 induces transcription of the novel fgl2 prothrombinase gene (1999) J. Biol. Chem., 274, pp. 9930-9936; Ontiveros, E., Kuo, L., Masters, P.S., Perlman, S., Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS (2001) Virology, 289, pp. 230-238; Pereira, C.A., Steffan, A.M., Kirn, A., Interaction between mouse hepatitis viruses and primary cultures of Kupffer and endothelial liver cells from resistant and susceptible inbred mouse strains (1984) J. Gen. Virol., 65, pp. 1617-1620; Pereira, C.A., Steffan, A.M., Kirn, A., Kupffer and endothelial liver cell damage renders A/J mice susceptible to mouse hepatitis virus type 3 (1984) Virus Res., 1, pp. 557-563; Perlman, S., Pathogenesis of coronavirus-induced infections (1998) Coronaviruses and Arteriviruses, pp. 503-513. , L. Enjuanes, S. G. Siddell, and W. Spaan (ed.). Plenum Press, New York, N.Y; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Phillips, J.J., Chua, M.M., Rail, G., Weiss, S.R., Murine coronavirus spike glycoprotein mediates degree of viral spread, inflammation and virus-induced immunopathology in the central nervous system (2002) Virology, 301, pp. 109-120; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Taguchi, F., Kawamura, S., Fujiwara, K., Replication of mouse hepatitis viruses with high and low virulence in cultured hepatocytes (1983) Infect. Immun., 39, pp. 955-959; Tsai, J., Zelus, B.D., Holmes, K.V., Weiss, S.R., The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain (2003) J. Virol., 77, pp. 841-850; Van der Most, R.G., Heijnen, L., Spaan, W.J., De Groot, R.J., Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs (1992) Nucleic Acids Res., 20, pp. 3375-3381; Williams, R.K., Jiang, G.S., Holmes, K.V., Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 5533-5536; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.L., Lai, M.M.C., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA viral pathogenesis (1998) Virology, 242, pp. 170-183","Weiss, S.R.; Department of Microbiology, Univ. of Pennsylvania Sch. of Med., 36th St. and Hamilton Walk, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,,0022538X,,JOVIA,"12663803","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037384952
"Demirkiran O., Utku T.","6602182205;7801659456;","Severe Acute Respiratory Syndrome [Şiddetli Akut Solunum Yetersizliǧi Sendromu (SARS)]",2003,"SENDROM","15","4",,"88","95",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037669019&partnerID=40&md5=5921696427210f3a4bd27594e981ccc8","Istanbul University, Cerrahpaşa Medical Faculty, Department of Anesthesiology, Istanbul, Turkey","Demirkiran, O., Istanbul University, Cerrahpaşa Medical Faculty, Department of Anesthesiology, Istanbul, Turkey; Utku, T., Istanbul University, Cerrahpaşa Medical Faculty, Department of Anesthesiology, Istanbul, Turkey","In the fall of 2002, there were reports from Guangdong Province in southern China relating to 305 cases of highly contagious and very severe atypical pneumonia of unknown cause. The condition appeared to be particularly prevalent among healthcare workers and their household members, indeed many cases were rapidly fatal. On March 13, 2003 as the condition began to spread from China, the World Health Organization (WHO) issued a global alert about the out-break and instituted worldwide surveillance. In the late February the US Centers for Disease Control and Prevention (COC) termed this condition as ""Severe Acute Respiratory Syndrome (SARS)"" and provided clinical case definition. SARS was diagnosed in 2890 patients up to April 12, 2003. Early manifestations in these patients have included influenza-like symptoms such as fever, myalgias, headache, sore throat, dry cough, shortness of breath, or difficulty in breathing. In some cases hypoxia, pneumonia, and occasionally acute respiratory distress requiring mechanical ventilation and unfortunately death accompanied these symptoms. Laboratory findings may include thrombocytopenia and leukopenia. Coronavirus has not been proved to be the cause of SARS, but strong supportive evidence suggesting coronavirus as an etiological factor is accumulating. At least eight international laboratories have found coronavirus in blood cultures of patients with SARS. No specific treatment recommendations can be made at this time. Empiric therapy should provide antimicrobial coverage for organisms associated with any community-acquired pneumonia of unclear etiology, with agents having activity against both typical and atypical respiratory pathogens Treatment choices may be influenced by severity of the illness. Although no clinical response to combination antibiotherapy with a betalactam and a macrolide agent has been obtained, empirical treatment with a combination of a high dose corticosteroid and ribavirin promised clinical improvement.",,"antibiotic agent; beta lactam antibiotic; corticosteroid; macrolide; ribavirin; article; artificial ventilation; China; clinical feature; Coronavirus; coughing; drug megadose; dyspnea; epidemiological data; flu like syndrome; geographic distribution; human; hypoxia; leukopenia; pathogenesis; prevalence; respiratory distress; SARS coronavirus; severe acute respiratory syndrome; sore throat; thrombocytopenia; treatment outcome; virus pneumonia; world health organization","(2003) Acute Respiratory Syndrome in China-Update3: Disease Outbreak Reported, , http://www.who.int/csr/, Geneva (Mart 31, 2003); Severe cute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, p. 86; Lee, N., Hui, D.H., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348. , www.nejm.org; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348. , www.nejm.org; Gerberding, J.L., Faster.. but fast enough? Responding to the epidemic of severe acute respiratory syndrome (2003) N Engl J Med, 348. , www.nejm.org; www.who.int/csr/sarscountry/, WHO web sayfasi; Drazen, J.M., Case clusters of the severe acute respiratory syndrome (2003) N Engl J Med, 348. , www.nejm.org; Poutanen, S.M., Low, D.E., Henry, B., Identification of Severe Acute Respiratory Syndrome in Canada (2003) N Engl J Med, 348; www.cdc.gov/ncidod/sars/; Ksizazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus assosciated with severe acute respiratory syndrome (2003) N Engl J Med, 348. , www.nejm.org; Drosten, C., Günther, S., Wolfgang, P., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348. , www.nejm.org; Holmes, K.V., Coronaviruses (2001) Fields Virology, 4th Edn., pp. 1187-1203. , Knipe DM, Howley PM, eds. Philadelphia: Lippincott Williams and Wilkins; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) The Lancet, 36 T; Tsang, K.W., Ho, P.L., Ooi, G.K., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348. , www.nejm.org; www.hssgm.gov.tr, TC. Saǧlik Bakanliǧi Hudut ve Sahiller Genel Müdürlüǧü web sayfasi","Demirkiran, O.; Istanbul University, Cerrahpaşa Medical Faculty, Department of Anesthesiology, Istanbul, Turkey",,,10165134,,SENDE,,"Turkish","SENDROM",Article,"Final",,Scopus,2-s2.0-0037669019
"Nourrit F.","6602864224;","The SARS coronavirus up close [Un coronavirus à la loupe]",2003,"Biofutur",,"232",,"68","69",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038746614&partnerID=40&md5=a7cd3106ce4e872ef5dddbb644fb7e37",,"Nourrit, F.",[No abstract available],,"Coronavirus; nonhuman; pneumonia; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; short survey; virulence; virus detection; virus genome; virus identification; virus transmission; Coronavirus; SARS coronavirus","(2003) Communiqué de Presse du CDC, , http://www.cdc.gov/od/oc/media/pressrel/r030430.htm, 30 avril; Rota, P.A., (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085952v1.pdf, 1er mai; http://straitstimes.asia1.com.sg/mnt/html/webspecial/sars/0205_14.html; Catala, I., (2003) Le Quotidien du Médecin, , 29 avril; (2003) Compte-Rendu de la Téléconférence du CDC, , http://www.cdc.gov/od/oc/media/transcripts/t030424.htm, 24 avril; Premières Données Compilées par l'OMS sur la Stabilité et la Résistance du Virus du SRAS, , http://www.who.int/csr/sars/survval_2003_05_04/en/; http://www.hkupasteur.hku.hk/hkuip/SARS.html; http://www.grog.org/documents/grog_coronavirus_avant_SARS.doc",,,,02943506,,BIOFE,,"French","Biofutur",Short Survey,"Final",,Scopus,2-s2.0-0038746614
"Pratelli A., Tinelli A., Decaro N., Cirone F., Elia G., Roperto S., Tempesta M., Buonavoglia C.","7004884960;6701370203;6701636107;6602223775;7005135633;6508365316;7005599031;7005623145;","Efficacy of an inactivated canine coronavirus vaccine in pups",2003,"New Microbiologica","26","2",,"151","155",,24,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037805067&partnerID=40&md5=19aaa00d573d552a654f1b0841a8fdbf","Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Dept. of Animal Health and Pathology, Faculty of Veterinary Medicine, via F. Delfino 1, 80137, Napoli, Italy","Pratelli, A., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Tinelli, A., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Decaro, N., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Cirone, F., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Elia, G., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Roperto, S., Dept. of Animal Health and Pathology, Faculty of Veterinary Medicine, via F. Delfino 1, 80137, Napoli, Italy; Tempesta, M., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy; Buonavoglia, C., Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy","The efficacy of an inactivated CCoV vaccine (Duramune PC) was evaluated in four pups. Two dogs were maintained non-vaccinated. Ten days after the booster shot all the pups were challenged with a field CCoV strain administered by oro-nasal route. The vaccinated pups did not display clinical signs and shed the challenge-virus for 11.25 days, evaluated by virus isolation, and 13.5 days, evaluated by PCR assay. The two non vaccinated pups displayed mild diarrhoea at day post-challenge 4 and shed the challenge-virus for 14 and 15 days respectively, by virus isolation, and for 22 and 24 days respectively, by PCR assay.","Coronavirus; Efficacy; Inactivate vaccine","canine coronavirus vaccine; inactivated vaccine; unclassified drug; virus vaccine; inactivated vaccine; virus vaccine; article; controlled study; Coronavirus; diarrhea; drug efficacy; drug screening; nonhuman; polymerase chain reaction; virus infection; virus isolation; virus strain; animal; animal disease; clinical trial; dog; dog disease; immunology; isolation and purification; virus infection; Canine coronavirus; Canis familiaris; Coronavirus; Animals; Coronavirus Infections; Coronavirus, Canine; Dog Diseases; Dogs; Vaccines, Inactivated; Viral Vaccines","Carmichael, L.E., Vaccines for dogs (1997) Veterinary Vaccinology. First Edition, , Pastoret, P-P., Blancou, J., Vannier, P., Verschueren, C. Eds, Elsevier, New York (USA); De Haan, C.A., Vennema, H., Rottier, P.J., Assembly of the coronavirus envelope: Homotypic interactions between the M proteins (2000) Journal of Virology, 74, pp. 4967-4978; Elia, G., Decaro, N., Tinelli, A., Martella, V., Pratelli, A., Buonavoglia, C., Evaluation of antibody response to canine coronavirus infection in dogs by Western Blotting analysis (2002) New Microbiologica, 25, pp. 275-280; Gebauer, F., Posthumus, W.A.P., Correa, I., Suñé, C., Smerdou, C., Sánchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the formation of the antigenic sites of the S protein of transmissible gastroenteritis coronavirus (1991) Virology, 183, pp. 225-238; Keenan, K.P., Jervis, H.R., Marchwicki, R.H., Binn, L.N., Intestinal infection of neonatal dogs with canine corona virus 1-71: Studies by virologic, histologic, histochemical and immunofluorescent techniques (1976) American Journal of Veterinary Research, 37, pp. 247-256; Luytjes, W., Coronavirus gene expression: Genome organization and protein expression (1995) The Coronaviridae, , Siddell, S.G. Ed, Plenum Press, New York (USA); Marsilio, F., Pratelli, A., Elia, G., Ricci, L., Enterite da coronavirus del cane: Caratterizzazione del virus isolato (2002) Veterinaria, 2, pp. 59-62; Pratelli, A., Canine coronavirus (2000) Recent Advances in Canine Infectious Diseases, , www.ivis.org/, Carmichael, L.E. Ed, International Veterinary Information Service; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) Journal of Virological Methods, 80, pp. 11-15; Pratelli, A., Buonavoglia, D., Martella, V., Tempesta, M., Lavazza, A., Buonavoglia, C., Diagnosis of canine coronavirus infection using nested-PCR (2000) Journal of Virological Methods, 84, pp. 91-94; Pratelli, A., Martella, V., Elia, G., Tempesta, M., Guarda, F., Capucchio, M.T., Carmichael, L.E., Buonavoglia, C., Severe enteric disease in an animal shelter associated with dual infections by canine adenovirus type 1 and canine coronavirus (2001) Journal of Veterinary Medicine B, 48, pp. 385-392; Pratelli, A., Elia, G., Martella, V., Palmieri, A., Cirone, F., Tinelli, A., Corrente, M., Buonavoglia, C., Prevalence of canine coronavirus antibodies in dogs in the south of Italy (2002) Journal of Virological Methods, 102, pp. 67-71; Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., Carstens, E.B., Estes, M.K., Lemon, S.M., Maniloff, J., Wickner, R.B., Family Coronaviridae (2000) Virus Taxonomy. Classification and Nomenclature of Viruses, , Regenmortel, M.H.V., Fauquet, C.M., Bishop, D.H.L., Carstens, E.B., Estes, M.K., Lemon, S.M., Maniloff, J., Mayo, M.A., McGeoch, D.J., Pringle, C.R., and Wickner, R.B. Eds, Seventh Report of the International Committee on Taxonomy of Viruses. Academic Press, New York (USA); Tennant, B.J.R., Gaskell, M., Kelly, D.F., Carter, S.C., Gaskell, C.J., Canine coronavirus infection in dog following oronasal inoculation (1991) Research in Veterinary Science, 51, pp. 11-18; Woods, R.D., Wesley, R.D., Kapke, P.A., Complement-dependent neutralization of transmissible gastroenteritis virus by monoclonal antibodies (1987) Advances in Experimental Medicine and Biology, 218, pp. 493-500","Pratelli, A.; Dept. of Anim. Health and Well-being, Faculty of Veterinary Medicine, Strada per Casamassima km 3, 70010 Valenzano (Bari), Italy",,,11217138,,,"12737196","English","New Microbiol.",Article,"Final",,Scopus,2-s2.0-0037805067
"Wilhelmi I., Roman E., Sánchez-Fauquier A.","6701746199;7101781727;6602492925;","Viruses causing gastroenteritis",2003,"Clinical Microbiology and Infection","9","4",,"247","262",,235,"10.1046/j.1469-0691.2003.00560.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038748139&doi=10.1046%2fj.1469-0691.2003.00560.x&partnerID=40&md5=ec12d9ef818021f571a63660577f41bc","Servicio de Microbiología, Hospital Severo Ochoa, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain; Servicio de Pediatría, Hospital Severo Ochoa, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain; Centro Nacional de Microbiologia, Instituto de Salud Carlos III, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain","Wilhelmi, I., Servicio de Microbiología, Hospital Severo Ochoa, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain; Roman, E., Servicio de Pediatría, Hospital Severo Ochoa, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain; Sánchez-Fauquier, A., Centro Nacional de Microbiologia, Instituto de Salud Carlos III, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain","Acute gastroenteritis is one of the most common diseases in humans worldwide. Viruses are recognized as important causes of this disease, particularly in children. Since the Norwalk virus was identified as a cause of gastroenteritis, the number of viral agents associated with diarrheal disease in humans has steadily increased. Rotavirus is the most common cause of severe diarrhea in children under 5 years of age. Astrovirus, calicivirus and enteric adenovirus are also important etiologic agents of acute gastroenteritis. Other viruses, such as toroviruses, coronaviruses, picobirnaviruses and pestiviruses, are increasingly being identified as causative agents of diarrhea. In recent years, the availability of diagnostic tests, mainly immunoassays or molecular biology techniques, has increased our understanding of this group of viruses. The future development of a safe and highly effective vaccine against rotavirus could prevent, at least, cases of severe diarrhea and reduce mortality from this disease.","Acute diarrhea; Astroviruses; Coronaviruses; Enteric adenoviruses; Human calciviruses; Picobirnaviruses; Rotaviruses; Toroviruses; Viral gastroenteritis","plasmid DNA; Rotavirus vaccine; virus vaccine; Adenovirus; Astrovirus; Calicivirus; childhood disease; Coronavirus; dehydration; diagnostic test; diarrhea; disease severity; drug safety; enteric virus; fluid therapy; gastroenteritis; human; immunoassay; intestine intussusception; molecular biology; mortality; Norwalk gastroenteritis virus; Pestivirus; Picobirnavirus; priority journal; review; Rotavirus; Torovirus; virus identification; virus infection; Adenoviridae; Astroviridae; Caliciviridae; Coronavirus; Norwalk virus; Pestivirus; Picobirnavirus; Rotavirus; Torovirus","Glass, R.I., Kilgore, P.E., Etiology of acute viral gastroenteritis (1997) Diarrheal Disease, pp. 39-54. , Gracey M, Walker JA, eds. Nestlé Nutrition Workshop Series. Philadelphia: Lippincott-Raven; Snyder, J.D., Merson, M.H., The magnitude of the global problem of acute diarrhoeal disease: A review of active surveillance data (1982) Bull. WHO, 60, pp. 605-631; Bern, C., Glass, R.I., Impact of diarrhoeal disease worldwide (1994) Viral Infection of Gastrointestinal Tract, pp. 1-26. , Kapikian AZ, ed. New York: Marcel Dekker; Guerrant, R.I., Hughes, J.M., Lima, N.L., Crane, J., Diarrhea in developed and developing countries: Magnitude, special settings, and etiologies (1990) Rev. Infect. Dis., 12 (SUPPL. 1), pp. S41-S50; Warren, K.S., Tropical medicine or tropical health. The Health Clark lectures 1988 (1990) Rev. Infect. Dis., 12, pp. 142-156; Christensen, M.L., Rotaviruses (1999) Manual of Clinical Microbiology, pp. 999-1004. , Murray PR, Baron EJ, Pfaller MA, Tenover FC, Yolken RH, eds. Washington: ASM Press; Kapikian, A.Z., Overview of viral gastroenteritis (1996) Arch. Virol. Suppl., 12, pp. 7-19; Parashar, U.D., Bresee, J.S., Gentsch, J.R., Glass, R.I., Rotavirus (1998) Emerg. Infect. Dis., 4, pp. 561-570; Kapikian, A.Z., Wyatt, R.G., Dolin, R., Thornhill, T.S., Kalica, A.R., Chanock, R.M., Visualization by immune electron microscopy of a 27 nm particle associated with acute infectious non-bacterial gastroenteritis (1972) J. Virol., 10, pp. 1075-1081; Bishop, R.F., Davidson, G.P., Holmes, I.H., Ruck, B.J., Virus particles in epithelial cells of duodenal mucosa from children with acute non bacterial gastroenteritis (1973) Lancet, 2, pp. 1281-1283; Madeley, C.R., Cosgrove, B.P., 28 nm particles in faeces in infantile gastroenteritis (1975) Lancet, 2, pp. 451-452; Flewett, T.H., Bryden, A.S., Davies, H., Morris, C.A., Epidemic viral enteritis in a long-stay children's ward (1975) Lancet, 1, pp. 4-5; Caul, E.O.K., Paver, K., Clarke, S.K.R., Coronavirus particles in faeces from patients with gastroenteritis (1975) Lancet, 1, p. 1192; Chandra, R., Picobirnavirus, a novel group of undescribed viruses of mammals and birds: A minireview (1997) Acta. Virol., 41, pp. 59-62; Grohmann, G.S., Glass, R.I., Pereira, H.G., Monroe, S.S., Hightower, A.W., Bryan, R.T., Enteric virus and diarrhea in HIV infected patients (1993) N Engl. J. Med., 329, pp. 14-20; Ludert, J.E., Liprandi, F., Identification of viruses with bi- and trisegmented double-stranded RNA genome in faeces of children with gastroenteritis (1993) Res. Virol., 144, pp. 219-224; Yolken, R.H., Dubovi, E., Leister, F., Reid, R., Almeido-Hill, J., Santosham, M., Infantile gastroenteritis associated with excretion of pestiviruses antigens (1989) Lancet, 1, pp. 517-520; Beards, G.M., Brown, W.G., Green, J., Flewett, T.H., An enveloped virus in stools of children and adults with gastroenteritis that resembles de Breda virus of calves (1986) J. Med. Virol., 20, pp. 67-78; Jamieson, F., Wang, E.I., Bain, C., Human torovirus: A new nosocomial gastrointestinal pathogen (1998) J. Infect. Dis., 178, pp. 1263-1269; Kapikian, A.Z., Viral gastroenteritis (1997) Viral Infections of Humans: Epidemiology and Control, pp. 285-343. , Evans AS, Kaslow RA, eds. New York: Plenum Medical Book Company; Kilgore, P.E., Glass, R.I., Gastrointestinal syndromes (1997) Clinical Virology, pp. 55-67. , Richman DD, Whitley RJ, Hayden FG, eds. New York: Churchill Livingstone; Matthews, R.E.F., The classification and nomenclature of viruses: Summary of results of meetings of the International Committee on Taxonomy of Viruses in The Hague (1979) Intervirology, 11, pp. 133-135; Kapikian, A.Z., Chanock, R.M., Rotaviruses (1996) Virology, pp. 1657-1708. , Fields BN, Knipe DM, Howley PM, eds. 3rd edn. Philadelphia: Lippincott-Raven Press; Offit, P.A., Clark, H.F., Rotavirus (1995) Principles and Practice of Infectious Diseases, pp. 1448-1455. , Mandell GL, Bennet JE, Dolin R, eds. New York: Churchill Livingstone; Desselberger, U., Genome rearrangements of rotaviruses (1996) Arch. Virol. Suppl., 12, pp. 37-51; Ball, J.M., Tian, P., Zeng, C.Q.Y., Morris, A.P., Estes, M.K., Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein (1996) Science, 272, pp. 101-104; Kirkwood, C.D., Palombo, E.A., Genetic characterization of the rotavirus nonstructural protein, NSP4 (1997) Virology, 236, pp. 258-265; Estes, M.K., Cohen, J., Rotavirus gene structure and function (1989) Microbiol. Rev., 53, pp. 410-449; Rao, C.D., Gowda, K., Reddy, B.S., Sequence analysis of VP4 and VP7 genes of nontypeable strains identifies a new pair of outer capsid proteins representing novel P and G genotypes in bovine rotaviruses (2000) Virology, 276, pp. 104-113; Beards, G., Xu, L., Ballard, A., Desselberger, U., McCrae, M.A., A serotype 10 human rotavirus (1992) J. Clin. 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Withdrawal of rotavirus vaccine recommendation (1999) MMWR, 48, p. 1007. , Advisory Committee on Immunization Practices (ACIP); Intussusception among recipients of rotavirus vaccine-United States, 1998-1999 (1999) MMWR, 48, pp. 577-581. , Centers for Disease Control and Prevention; Bresee, J.S., Glass, R.I., Ivanoff, B., Gentsch, J.R., Current status and future priorities for rotavirus vaccine development, evaluation and implementation in developing countries (1999) Vaccine, 17, pp. 2207-2222; Wilhelmi, I., Mier, C., Román, E., Colomina, J., Prat, J., Sánchez-Fauquier, A., Molecular epidemiology of rotavirus in Spanish children (1999) Enferm. Infecc. Microbiol. Clin., 17, pp. 509-514; Jain, V., Das, B.K., Bhan, M.K., Glass, R.I., Gentsch, J.R., Great diversity of group A rotavirus strains and high prevalence of mixed rotavirus infection in India (2001) J. Clin. Microbiol., 39, pp. 3524-3529; Das, S., Sen, A., Uma, G., Genomic diversity of group A rotavirus strains infecting humans in eastern India (2002) J. Clin. Microbiol., 40, pp. 146-149","Wilhelmi, I.; Servicio de Microbiología, Hospital Severo Ochoa, Secc. Virus Prod. Gastroenteritis, Leganés 28911 Madrid, Spain; email: iwilhelmi@hsvo.insalud.es",,"Blackwell Publishing Ltd.",1198743X,,CMINF,"12667234","English","Clin. Microbiol. Infect.",Review,"Final",Open Access,Scopus,2-s2.0-0038748139
"Hoet A.E., Smiley J., Thomas C., Nielsen P.R., Wittum T.E., Saif L.J.","6602855175;57204251693;7404413122;7402902693;7004009529;7102226747;","Association of enteric shedding of bovine torovirus (Breda virus) and other enteropathogens with diarrhea in veal calves",2003,"American Journal of Veterinary Research","64","4",,"485","490",,22,"10.2460/ajvr.2003.64.485","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037672815&doi=10.2460%2fajvr.2003.64.485&partnerID=40&md5=97fee4a84f79bae47a419730e629f72a","Food Animal Health Research Program, Ohio Agricultural Res./Devmt. Center, The Ohio State University, Wooster, OH 44691, United States; Dept. of Veterinary Preventive Med., College of Veterinary Medicine, The Ohio State University, Columbus, OH 43210, United States; Catedra de Enfermedades Infecciosas, Facultad de Ciencias Veterinarias, La Universidad del Zulia, Maracaibo, Venezuela","Hoet, A.E., Catedra de Enfermedades Infecciosas, Facultad de Ciencias Veterinarias, La Universidad del Zulia, Maracaibo, Venezuela; Smiley, J., Food Animal Health Research Program, Ohio Agricultural Res./Devmt. Center, The Ohio State University, Wooster, OH 44691, United States; Thomas, C., Food Animal Health Research Program, Ohio Agricultural Res./Devmt. Center, The Ohio State University, Wooster, OH 44691, United States; Nielsen, P.R., Food Animal Health Research Program, Ohio Agricultural Res./Devmt. Center, The Ohio State University, Wooster, OH 44691, United States; Wittum, T.E., Dept. of Veterinary Preventive Med., College of Veterinary Medicine, The Ohio State University, Columbus, OH 43210, United States; Saif, L.J., Food Animal Health Research Program, Ohio Agricultural Res./Devmt. Center, The Ohio State University, Wooster, OH 44691, United States","Objective - To determine the prevalence, fecal shedding pattern, and association of bovine torovirus (BoTV) with diarrhea in veal calves at time of arrival and periodically throughout the first 35 days after their arrival on a veal farm. Animals - 62 veal calves. Procedure - Fecal samples collected on days 0, 4, 14, and 35 after arrival were tested for BoTV by use of ELISA and reverse transcriptase-polymerase chain reaction (RT-PCR) assay. Paired serum samples obtained from blood collected on days 0 and 35 were analyzed for BoTV antibodies with a hemagglutination inhibition assay. Fecal samples were also screened for other enteric pathogens, including rotavirus, coronavirus, and Cryptosporidium spp. Results - Fecal shedding of BoTV was detected in 15 of 62 (24%) calves by use of ELISA and RT-PCR assay, with peak shedding on day 4. A significant independent association between BoTV shedding and diarrhea was observed. In addition, calves shedding ≥ 2 enteric pathogens were more likely to have diarrhea than calves shedding ≤ 1 pathogen. Calves that were seronegative or had low antibody titers against BoTV (≤ 1:10 hemagglutination inhibition units) at arrival seroconverted to BoTV (> 4-fold increase in titer); these calves were more likely to shed virus than calves that were seropositive against BoTV at arrival. Conclusions and clinical relevance - Shedding of BoTV was strongly associated with diarrhea in neonatal veal calves during the first week after arrival at the farm. These data provide evidence that BoTV is an important pathogen of neonatal veal calves.",,"virus antibody; immunoglobulin G; virus antibody; antibody detection; article; beef cattle; cattle disease; cattle farming; controlled study; Coronavirus; Cryptosporidium; diarrhea; enzyme linked immunosorbent assay; feces analysis; hemagglutination inhibition test; intestine infection; male; nonhuman; prevalence; reverse transcription polymerase chain reaction; RNA virus infection; screening test; serodiagnosis; Torovirus; virus detection; virus diagnosis; virus shedding; animal; animal disease; blood; cattle; cattle disease; colostrum; diarrhea; feces; genetics; immunology; isolation and purification; physiology; Rotavirus; virology; virus culture; virus infection; virus shedding; Animalia; Bos taurus; Bovinae; Bovine torovirus; Breda virus; Coronavirus; Cryptosporidium; RNA viruses; Rotavirus; Torovirus; Animals; Antibodies, Viral; Cattle; Cattle Diseases; Colostrum; Coronavirus Infections; Coronavirus, Bovine; Diarrhea; Enzyme-Linked Immunosorbent Assay; Feces; Immunoglobulin G; Male; Prevalence; Reverse Transcriptase Polymerase Chain Reaction; Rotavirus; Rotavirus Infections; Torovirus; Torovirus Infections; Virus Cultivation; Virus Shedding","McDonough, S.P., Stull, C.L., Osburn, B.I., Enteric pathogens in intensively reared veal calves (1994) Am. J. Vet. Res., 55, pp. 1516-1520; de Visser, N.A., Breukink, H.J., van Zijderveld, F.G., Enteric infections in veal calves: A longitudinal study on four veal calf units (1987) Vet. Q, 9, pp. 289-296; Fallon, R.J., Harte, F.J., The occurrence of diarrhoea in calves under different management systems (1983) Ann. Rech. Vet., 14, pp. 473-478; Sargeant, J.M., Blackwell, T.E., Martin, S.W., Production practices, calf health and mortality on six white veal farms in Ontario (1994) Can. J. Vet. Res., 58, pp. 189-195; Neindre, P.L., Evaluating housing systems for veal calves (1993) J Anim. Sci., 71, pp. 1345-1354; Heath, S.E., Neonatal diarrhea in calves: Investigation of herd management practices (1992) Compend. Contin. Educ. Pract. Vet., 14, pp. 385-395; Wilson, J.B., McEwen, S.A., Clarke, C.R., A case-control study of selected pathogens including verocytotoxigenic Escherichia coli in calf diarrhea on an Ontario veal farm (1992) Can. J. Vet. Res., 56, pp. 184-188; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Aetiology of diarrhoea in young calves (1986) Vet. Rec., 119, pp. 31-34; Tzipori, S., The relative importance of enteric pathogens affecting neonates of domestic animals (1985) Adv. Vet. Sci. Comp. Med., 29, pp. 103-206; Snodgrass, D.R., Enteric viral vaccines for calves (1996) Bovine Pract., 30, pp. 40-43; Woode, G.N., Saif, L.J., Quesada, M., Comparative studies on three isolates of Breda virus of calves (1985) Am. J. Vet. Res., 46, pp. 1003-1010; Woode, G.N., Reed, D.E., Runnels, P.L., Studies with an unclassified virus isolated from diarrheic calves (1982) Vet. Microbiol., 7, pp. 221-240; Woode, G.N., Pohlenz, J.F., Gourley, N.E., Astrovirus and Breda virus infections of dome cell epithelium of bovine ileum (1984) J. Clin. Microbiol., 19, pp. 623-630; Pohlenz, J.F., Cheville, N.F., Woode, G.N., Cellular lesions in intestinal mucosa of gnotobiotic calves experimentally infected with a new unclassified bovine virus (Breda virus) (1984) Vet. Pathol., 21, pp. 407-417; Fagerland, J.A., Pohlenz, J.F., Woode, G.N., A morphological study of the replication of Breda virus (proposed family Toroviridae) in bovine intestinal cells (1986) J. Gen. Virol., 67, pp. 1293-1304; Woode, G.N., Breda and Breda-like viruses: Diagnosis, pathology and epidemiology (1987) Novel Diarrhoea Viruses, pp. 175-191. , Brock G, Whelan J, eds. Ciba Foundation Symposium. Chichester, England: John Wiley & Sons; Lamouliatte, F., du Pasquier, P., Rossi, F., Studies on bovine Breda virus (1987) Vet. Microbiol., 15, pp. 261-278; Koopmans, M., van Wuijckhuise-Sjouke, L., Schukken, Y.H., Association of diarrhea in cattle with torovirus infections on farms (1991) Am. J. Vet. Res., 52, pp. 1769-1773; Koopmans, M., Cremers, H., Woode, G.N., Breda virus (Toroviridae) infection and systemic antibody response in sentinel calves (1990) Am. J. Vet. Res., 51, pp. 1443-1448; Hoet, A.E., Chang, K.O., Saif, L.J., Comparison of ELISA and RT-PCR versus immune electron microscopy for detection of Bovine Torovirus (Breda virus) in calf fecal specimens (2002) J. Vet. Diagn. Invest., , in press; Lucchelli, A., Lance, S.E., Bartlett, P.B., Prevalence of bovine group A rotavirus shedding among dairy calves in Ohio (1992) Am. J. Vet. Res., 53, pp. 169-174; Smith, D.R., Tsunemitsu, H., Heckert, R.A., Evaluation of two antigen-ELISAs using polyclonal or monoclonal antibodies for the detection of bovine coronavirus (1996) J. Vet. Diagn. Invest., 8, pp. 99-105; Cho, K.O., Hasoksuz, M., Nielsen, P.R., Cross-protection studies between respiratory and calf diarrhea and winter dysentery coronavirus strains in calves and RT-PCR and nested PCR for their detection (2001) Arch. Virol., 146, pp. 2401-2419; Nielsen, C.K., Ward, L.A., Enhanced detection of Cryptosporidium in the acid-fast stain (1999) J. Vet. Diagn. Invest., 11, pp. 567-569; Pfeiffer, N.E., McGuire, T.C., A sodium sulfite-precipitation test for assessment of colostral immunoglobulin transfer to calves (1977) J. Am. Vet. Med. Assoc., 170, pp. 809-811; Pérez, E., Kummeling, A., Janssen, M.M., Infectious agents associated with diarrhoea of calves in the canton of Tilarán, Costa Rica (1998) Prev. Vet. Med., 33, pp. 195-205; Duckmanton, L.M., Carman, S., Nagy, E., Detection of bovine torovirus in fecal specimens of calves with diarrhea from Ontario farms (1998) J. Clin. Microbiol., 36, pp. 1266-1270; Hoet, A.E., Cho, K.O., Chang, K.O., Enteric and nasal shedding of bovine torovirus (Breda virus) in feedlot cattle (2002) Am. J. Vet. Res., 63, pp. 342-348; Cho, K.J., Hoet, A.E., Loerch, S.C., Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle (2001) Am. J. Vet. Res., 62, pp. 1436-1441; Koopmans, M., Horzinek, M.C., The pathogenesis of torovirus infections in animals and humans (1995) The Coronaviridae, pp. 403-413. , Siddell SG, ed. New York: Plenum Press; de la Fuente, R., García, A., Ruiz-Santa-Quiteria, J.A., Proportional morbidity rates of enterepathogens among diarrheic dairy calves in central Spain (1998) Prev. Vet. Med., 36, pp. 145-152; García, A., Ruiz-Santa-Quiteria, J.A., Orden, J.A., Rotavirus and concurrent infections with other enteropathogens in neonatal diarrheic dairy calves in Spain (2000) Comp. Immunol. Microbiol. Infect. Dis., 23, pp. 175-183; Reynolds, D.J., Morgan, J.H., Chanter, N., Microbiology of calf diarrhoea in Southern Britain (1986) Vet. Rec., 119, pp. 34-39","Saif, L.J.; Food Animal Health Research Program, Ohio. Agricultural Res./Devmt. Ctr., The Ohio State University, Wooster, OH 44691, United States",,,00029645,,AJVRA,"12693541","English","Am. J. Vet. Res.",Article,"Final",,Scopus,2-s2.0-0037672815
"Sola I., Alonso S., Zúñiga S., Balasch M., Plana-Durán J., Enjuanes L.","7003336781;57210695335;6603777678;6602693824;6604038063;7006565392;","Engineering the transmissible gastroenteritis virus genome as an expression vector inducing lactogenic immunity",2003,"Journal of Virology","77","7",,"4357","4369",,60,"10.1128/JVI.77.7.4357-4369.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037377719&doi=10.1128%2fJVI.77.7.4357-4369.2003&partnerID=40&md5=b41b216793f8bc49d86ecda6f1c886aa","Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain","Sola, I., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Alonso, S., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Zúñiga, S., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Balasch, M., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Plana-Durán, J., Fort-Dodge Veterinaria, Dept. of Research and Development, Girona, Spain; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","The genome of the coronavirus transmissible gastroenteritis virus (TGEV) has been engineered as an expression vector with an infectious cDNA. The vector led to the efficient (≥40 μg/106 cells) and stable (≥20 passages) expression of a heterologous gene (green fluorescent protein [GFP]), driven by the transcription-regulating sequences (TRS) of open reading frame (ORF) 3a inserted in the site previously occupied by the nonessential ORFs 3a and 3b. Expression levels driven by this TRS were higher than those of an expression cassette under the control of regulating sequences engineered with the N gene TRS. The recombinant TGEV including the GFP gene was still enteropathogenic, albeit with a 10- to 102-fold reduction in enteric tissue growth. Interestingly, a specific lactogenic immune response against the heterologous protein has been elicited in sows and their progeny. The engineering of an additional insertion site for the heterologous gene between viral genes N and 7 led to instability and to a new genetic organization of the 3′ end of the recombinant viruses. As a consequence, a major species of subgenomic mRNA was generated from a TRS with the noncanonical core sequence 5′-CUAAAA-3′. Extension of the complementarity between the TRS and sequences at the 3′ end of the viral leader was associated with transcriptional activation of noncanonical core sequences. The engineered vector led to expression levels as high as those of well-established vectors and seems very promising for the development of vaccines and, possibly, for gene therapy.",,"green fluorescent protein; article; bacterial artificial chromosome; Coronavirus; expression vector; genetic engineering; heterologous expression; immune response; immunity; nonhuman; nucleotide sequence; open reading frame; priority journal; transcription initiation; transcription regulation; Transmissible gastroenteritis virus; virus genome; Animals; Base Sequence; Cell Line; Colostrum; Cricetinae; DNA, Viral; Female; Gastroenteritis, Transmissible, of Swine; Genetic Engineering; Genetic Vectors; Genome, Viral; Green Fluorescent Proteins; Luminescent Proteins; Molecular Sequence Data; Open Reading Frames; Pregnancy; Recombinant Proteins; RNA, Messenger; RNA, Viral; Sus scrofa; Swine; Transmissible gastroenteritis virus","Agapov, E.V., Frolov, I., Lindenbach, B.D., Pragai, B.M., Schlesinger, S., Rice, C.M., Noncytopathic Sindbis virus RNA vectors for heterologous gene expression (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 12989-12994; Almazán, F., González, J.M., Pénzes, Z., Izeta, A., Calvo, E., Plana-Durán, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Alonso, S., Izeta, A., Sola, I., Enjuanes, L., Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus (2002) J. Virol., 76, pp. 1293-1308; Alonso, S., Sola, I., Teifke, J., Reimann, I., Izeta, A., Balach, M., Plana-Durán, J., Enjuanes, L., In vitro and in vivo expression of foreign genes by transmissible gastroenteritis coronavirus-derived minigenomes (2002) J. Gen. Virol., 83, pp. 567-579; An, S., Makino, S., Characterizations of coronavirus cis-acting RNA elements and the transcription step affecting its transcription efficiency (1998) Virology, 243, pp. 198-207; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Semin. Virol., 8, pp. 101-111; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: Molecular evidence for the first invertebrate nidovirus (2000) Nidoviruses, , E. Lavi, S. Weiss, and S. T. Hingley (ed.), in press. Plenum Press, New York, N.Y; Cowley, J.A., Walker, P.J., The complete genome sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses (2002) Arch. Virol., 147, pp. 1977-1987; Curtis, K.M., Yount, B., Baric, R.S., Heterologous gene expression from transmissible gastroenteritis virus replicon particles (2002) J. Virol., 76, pp. 1422-1434; De Vries, A.A.F., Glaser, A.L., Raamsman, M.J.B., Rottier, P.J.M., Recombinant equine arteritis virus as an expression vector (2001) Virology, 284, pp. 259-276; Delmas, B., Gelfi, J., Sjöström, H., Noren, O., Laude, H., Further characterization of aminopeptidase-N as a receptor for coronaviruses (1994) Adv. Exp. Med. Biol., 342, pp. 293-298; Den Boon, J.A., Kleijnen, M.F., Spaan, W.J.M., Snijder, E.J., Equine arteritis virus subgenomic mRNA synthesis: Analysis of leader-body junctions and replicative-form RNAs (1996) J. Virol., 70, pp. 4291-4298; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy: Classification and Nomenclature of Viruses, pp. 835-849. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M. Lemon, D. J. McGeoch, J. Maniloff, M. A. Mayo, C. R. Pringle, and R. B. Wickner (ed.). Academic Press, New York, N.Y; Enjuanes, L., Sola, I., Almazán, F., Ortego, J., Izeta, A., González, J.M., Alonso, S., Sánchez, C.M., Coronavirus derived expression systems (2001) J. Biotechnol., 88, pp. 183-204; Enjuanes, L., Spaan, W., Snijder, E., Cavanagh, D., Nidovirales (2000) Virus Taxonomy: Classification and Nomenclature of Viruses, pp. 827-834. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M. Lemon, D. J. McGeoch, J. Maniloff, M. A. Mayo, C. R. Pringle, and R. B. Wickner (ed.). Academic Press, New York, N.Y; Enjuanes, L., Van der Zeijst, B.A.M., Molecular basis of transmissible gastroenteritis coronavirus epidemiology (1995) The Coronaviridae, pp. 337-376. , S. G. Siddell (ed.). Plenum Press, New York, N.Y; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., Analysis of a recombinant mouse hepatitis virus expressing a foreign gene reveals a novel aspect of coronavirus transcription (1997) J. Virol., 71, pp. 5148-5160; Frolov, I., Hoffman, T.A., Prágai, B.M., Dryga, S.A., Huang, H.V., Schlesinger, S., Rice, C.M., Alphavirus-based expression vectors: Strategies and applications (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 11371-11377; González, J.M., Penzes, Z., Almazán, F., Calvo, E., Enjuanes, L., Stabilization of a full-length infectious cDNA clone of transmissible gastroenteritis coronavirus by the insertion of an intron (2002) J. Virol., 76, pp. 4655-4661; Hiscox, J.A., Mawditt, K.L., Cavanagh, D., Britton, P., Investigation of the control of coronavirus subgenomic mRNA transcription by with T7-generated negative-sense RNA transcripts (1995) J. Virol., 69, pp. 6219-6227; Hsue, B., Masters, P.S., Insertion of a new transcriptional unit into the genome of mouse hepatitis virus (1999) J. 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Microbiol., 23, pp. 147-154; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Joo, M., Makino, J.K., A system for study of coronavirus messenger RNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Makino, S., Soe, L.H., Shieh, C.K., Lai, M.C.C., Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs (1988) J. Virol., 62, pp. 3870-3873; Mason, B.B., Davis, A.R., Bhat, B.M., Ghengalvala, M., Lubeck, M.D., Zandle, G., Kostek, B., Hung, P.P., Adenovirus vaccine vectors expressing hepatitis B surface antigen: Importance of regulatory elements in the adenovirus major late intron (1990) Virology, 177, pp. 452-461; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv. Virus Res., 53, pp. 245-264; McClurkin, A.W., Norman, J.O., Studies on transmissible gastroenteritis of swine. II. Selected characteristics of a cytopathogenic virus common to five isolates from transmissible gastroenteritis (1966) Can. J. Comp. Med. Vet. Sci., 30, pp. 190-198; McGoldrick, A., Lowings, J.P., Paton, D.J., Characterisation of a recent virulent transmissible gastroenteritis virus from Britain with a deleted ORF 3a (1999) Arch. Virol., 144, pp. 763-770; Meulenberg, J.J.M., De Meijer, E.J., Moormann, R.J.M., Subgenomic RNAs of Lelystad virus contain a conserved leader body junction sequence (1993) J. Gen. Virol., 74, pp. 1697-1701; Mittal, S.K., Andrew, J.B., Prevec, L., Graham, F.L., Foreign gene expression by human adenovirus type 5-based vectors studied with firefly luciferase and bacterial β-galactosidase genes as reporters (1995) Virology, 210, pp. 226-230; Nagy, P.D., Simon, A.E., New insights into the mechanisms of RNA recombination (1997) Virology, 235, pp. 1-9; Ortego, J., Escors, D., Laude, H., Enjuanes, L., Generation of a replication-competent, propagation-deficient virus vector based on the transmissible gastroenteritis coronavirus genome (2002) J. Virol., 76, pp. 11518-11529; Ortego, J., Sola, I., Almazan, F., Ceriani, J.E., Riquelme, C., Balach, M., Plana-Durán, J., Enjuanes, L., Transmissible gastroenteritis coronavirus gene 7 is not essential but influences in vivo virus replication and virulence (2003) Virology, , in press; Penzes, Z., González, J.M., Calvo, E., Izeta, A., Smerdou, C., Mendez, A., Sánchez, C.M., Enjuanes, L., Complete genome sequence of transmissible gastroenteritis coronavirus PUR46-MAD clone and evolution of the Purdue virus cluster (2001) Virus Genes, 23, pp. 105-118; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y; Sánchez, C.M., Izeta, A., Sánchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Durán, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Sánchez, C.M., Jiménez, G., Laviada, M.D., Correa, I., Suñé, C., Bullido, M.J., Gebauer, F., Enjuanes, L., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-220; Thiel, V., Herold, J., Schelle, B., Siddell, S., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Van der Most, R.G., De Groot, R.J., Spaan, W.J.M., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Marie, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J.M., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Walsh, E.P., Baron, M.D., Anderson, J., Barrett, T., Development of a genetically marked recombinant rinderpest vaccine expressing green fluorescent protein (2000) J. Gen. Virol., 81, pp. 709-718; Walsh, E.P., Baron, M.D., Rennie, L.F., Monaghan, P., Anderson, J., Barrett, T., Recombinant rinderpest vaccines expressing membrane-anchored proteins as genetic markers: Evidence of exclusion of marker protein from the virus envelope (2000) J. Virol., 74, pp. 10165-10175; Wertz, G.W., Perepelitsa, V.P., Ball, L.A., Gene rearrangement attenuates expression and lethality of a nonsegmented negative strand RNA virus (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 3501-3506; Wesley, R.D., Cheung, A.K., Michael, D.M., Woods, R.D., Nucleotide sequence of coronavirus TGEV genomic RNA: Evidence of 3 mRNA species between the peplomer and matrix protein genes (1989) Virus Res., 13, pp. 87-100; Wesley, R.D., Wesley, I.V., Woods, R.D., Differentiation between transmissible gastroenteritis virus and porcine respiratory coronavirus with a cDNA probe (1991) J. Vet. Diagn. Investig., 3, pp. 29-32; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic analysis of porcine respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus (1991) J. Virol., 65, pp. 3369-3373; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: The transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Zhang, X., Lai, M.M.C., Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination (1994) J. Virol., 68, pp. 6626-6633","Enjuanes, L.; Department of Molecular Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; email: L.Enjuanes@cnb.uam.es",,,0022538X,,JOVIA,"12634392","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037377719
"Hohmann C.","17345793800;","The SARS pathogen is probably a coronavirus [SARS-erreger: Vermutlich ein coronavirus]",2003,"Pharmazeutische Zeitung","148","14",,"37","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037417386&partnerID=40&md5=f9335aae601d9f79188f868278ff2b59",,"Hohmann, C.",[No abstract available],,"Coronavirus; human; mortality; note; pneumonia; respiratory tract disease; severe acute respiratory syndrome; world health organization",,,,,00317136,,PZSED,,"German","Pharm. Ztg.",Note,"Final",,Scopus,2-s2.0-0037417386
"Tremblay J.-F., Rawls R.","7202646793;7004151955;","SARS exacts toll",2003,"Chemical and Engineering News","81","14",,"8","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037424975&partnerID=40&md5=17ff44f5bbbb034ae0beda104e4b50dc",,"Tremblay, J.-F.; Rawls, R.","The effect of severe acute respiratory syndrome (SARS), a highly contagious disease, on the business of chemical industries in Asia is discussed. The financial losses includes lost sales opportunities, slowdowns in joint-venture negotiations and the eroding contact with customers and partners. The agent responsible for SARS is not yet confirmed but health officials are zeroing in on a new form of coronavirus.",,"Chemical industry; Health care; Industrial economics; Sales; Contagious diseases; Pulmonary diseases",,,,,00092347,,CENEA,,"English","Chem Eng News",Note,"Final",,Scopus,2-s2.0-0037424975
"Hassler D., Schwarz T.F., Braun R.","7005853595;57206314642;57196572384;","SARS: A new paramyxovirus or coronavirus? [SARS: Ein neues paramyxovirus oder coronavirus]",2003,"Deutsche Medizinische Wochenschrift","128","15",,"786","",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037624725&partnerID=40&md5=53aa9f60b43f3f5f9f6df43f2262095c",,"Hassler, D.; Schwarz, T.F.; Braun, R.",[No abstract available],,"China; clinical feature; Coronavirus; diagnostic test; Hong Kong; human; infection control; nonhuman; Paramyxovirus; pneumonia; polymerase chain reaction; prophylaxis; respiratory tract disease; severe acute respiratory syndrome; short survey; Singapore; Viet Nam; Coronaviridae Infections; Coronavirus; Humans; Respirovirus; Respirovirus Infections; SARS Virus; Severe Acute Respiratory Syndrome",,,,,00120472,,DMWOA,"12723569","German","Dtsch. Med. Wochenschr.",Short Survey,"Final",,Scopus,2-s2.0-0037624725
"Vabret A., Mourez T., Gouarin S., Petitjean J., Freymuth F.","7003959575;8553384500;56107903900;7006379234;7103410207;","An outbreak of coronavirus OC43 respiratory infection in Normandy, France",2003,"Clinical Infectious Diseases","36","8",,"985","989",,121,"10.1086/374222","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037445549&doi=10.1086%2f374222&partnerID=40&md5=ca1e1da175a8c4f2bf44432012c0b53f","Lab. of Human and Molecular Virology, University Hospital, Caen, France; Lab. of Human and Molecular Virology, University Hospital, Av. Georges Clemenceau, 14 033 Caen, France","Vabret, A., Lab. of Human and Molecular Virology, University Hospital, Caen, France, Lab. of Human and Molecular Virology, University Hospital, Av. Georges Clemenceau, 14 033 Caen, France; Mourez, T., Lab. of Human and Molecular Virology, University Hospital, Caen, France; Gouarin, S., Lab. of Human and Molecular Virology, University Hospital, Caen, France; Petitjean, J., Lab. of Human and Molecular Virology, University Hospital, Caen, France; Freymuth, F., Lab. of Human and Molecular Virology, University Hospital, Caen, France","The 2 groups of human coronaviruses (HCoVs) represented by the prototype strains HCoV 229E and HCoV OC43 are mostly known as viruses responsible for common cold syndrome. HCoVs are difficult to detect, and epidemiological data are rare. From October 2000 through April 2001, we tested 1803 respiratory samples for HCoV by reverse-transcriptase polymerase chain reaction. From 8 February through 27 March 2001, HCoV OC43 was detected in samples obtained from 30 (6%) of 501 patients. The other viruses detected were respiratory syncytial virus (6.1%), parainfluenza virus 3 (1%), influenza virus A (7.8%), influenza virus B (7.2%), rhinovirus (6.4%), enterovirus (1%), and adenovirus (2%). Infection with HCoV OC43 was detected in patients of all age groups. The following clinical symptoms were noted: fever (in 59.8% of patients), general symptoms (in 30%), digestive problems (in 56.8%), rhinitis (in 36.6%), pharyngitis (in 30%), laryngitis (in 3.3%), otitis (in 13.3%), bronchitis (in 16.6%), bronchiolitis (in 10%), and pneumonia (in 6.6%). This study shows that an outbreak of HCoV OC43 respiratory infection was responsible for the lower respiratory tract symptoms observed in nearly one-third of patients identified by active surveillance for coronavirus infection.",,"Adenovirus; adolescent; adult; age distribution; aged; article; bronchiolitis; bronchitis; child; clinical feature; common cold; Coronavirus; Enterovirus; epidemic; fever; France; gastrointestinal disease; gene sequence; human; Influenza virus A; Influenza virus B; laryngitis; lower respiratory tract infection; major clinical study; nucleotide sequence; otitis; Parainfluenza virus 3; pharyngitis; pneumonia; priority journal; Respiratory syncytial pneumovirus; respiratory tract infection; reverse transcription polymerase chain reaction; rhinitis; Rhinovirus; virus detection; virus gene; virus infection; virus strain; classification; France; middle aged; preschool child; respiratory tract infection; virology; virus infection; Adolescent; Adult; Aged; Child; Child, Preschool; Coronavirus; Coronavirus Infections; Disease Outbreaks; France; Humans; Middle Aged; Respiratory Tract Infections","Myint, S.H., Human coronaviruses: A brief review (1994) Medical Virology, 4, pp. 35-46; El-Sahly, H.M., Atmar, R.L., Glezen, W.P., Greenberg, S.B., Spectrum of clinical illness in hospitalized patients with ""common cold"" virus infection (2000) Clin Infect Dis, 31, pp. 96-100; Falsey, A.R., Walsh, E.E., Hayden, F.G., Rhinovirus and coronavirus infection-associated hospitalizations among older adults (2002) J Infect Dis, 185, pp. 1338-1340; Monto, A.S., Lim, S.K., The Tecumseh study of respiratory illness. VI. Frequency of and relationship between outbreaks of coronavirus infection (1974) J Infect Dis, 129, pp. 271-276; McIntosh, K., Kapikian, A.Z., Turner, H.C., Hartley, J.W., Parrott, R.H., Chanock, R.M., Seroepidemiologic studies of coronavirus infection in adults and children (1970) Am J Epidemiol, 91, pp. 585-592; Macnaughton, M.R., Occurence and frequency of coronavirus infections in humans as determined by enzyme-linked immunosorbent assay (1982) Infect Immun, 38, pp. 419-423; Hamre, D., Been, M., Virologic studies of acute respiratory disease in young adults. V. Coronavirus 229E infections during six years of surveillance (1972) Am J Epidemiol, 96, pp. 94-106; Freymuth, F., Vabret, A., Galateau-Salle, F., Detection of respiratory syncytial virus, parainfluenza 3, adenovirus and rhinovirus in respiratory tract of infants by PCR and hybridization (1997) Clin Diagn Virol, 8, pp. 31-40; Freymuth, F., Vabret, A., Brouard, J., Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae infections in exacerbations of asthma in children (1999) J Clin Virol, 13, pp. 131-139; Vabret, A., Mouthon, F., Mourez, T., Gouarin, S., Petitjean, J., Freymuth E Direct diagnosis of human respiratory coronaviruses 229E and OC43 by the polymerase chain reaction (2001) J Virol Methods, 97, pp. 59-66; Myint, S.H., Johnston, S., Sanderson, G., Simpson, H., Evaluation of nested polymerrase chain methods for the detection of human coronaviruses 229E and OC43 (1994) Mol Cell Probes, 8, pp. 357-364; Kaye, H.S., Marsh, H.B., Dowdle, W.R., Seroepidemiologic survvey of coronavirus (strain OC43) related infections in a children's population (1971) Am J Epidemiol, 94, pp. 43-49; Lina, B., Valette, M., Foray, S., Surveillance of community-acquired viral infections due respiratory viruses in Rhone-Alpes (France) during winter 1994 to 1995 (1996) J Clin Microbiol, 34, pp. 3007-3011; Nokso-Koivisto, J., Kinnary, T.J., Lindahl, P., Hovi, T., Pitkäranta, A., Human picornavirus and coronavirus RNA in nasopharynx of children without concurrent respiratory symptoms (2002) J Med Virol, 66, pp. 417-420; Glezen, P.W., Greenberg, S.B., Atmar, R.L., Piedra, P.A., Couch, R.B., Impact of respiratory virus infections on persons with chronic underlying conditions (2000) JAMA, 283, pp. 499-505; Chany, C., Moscovici, O., Lebon, P., Rousset, S., Association of coronavirus infection with neonatal necrotizing enterocolitis (1982) Pediatrics, 69, pp. 209-214","Vabret, A.; Lab. of Human and Molecular Virology, University Hospital, Av. Georges Clemenceau, 14 033 Caen, France; email: vabret-a@chu-caen.fr",,,10584838,,CIDIE,"12684910","English","Clin. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0037445549
"Walgate R.","7006043615;","WHO says coronavirus causes SARS",2003,"Genome Biology","4","1", spotlight-20030417-01,"","",,,"10.1186/gb-spotlight-20030417-01","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84974687883&doi=10.1186%2fgb-spotlight-20030417-01&partnerID=40&md5=00e5d11ee07e43f2a70903a036580e9c",,"Walgate, R.",[No abstract available],,"antivirus agent; DNA; single stranded RNA; Article; Coronaviridae; diagnostic test; DNA probe; gene sequence; Hong Kong; host susceptibility; human; Human immunodeficiency virus; nonhuman; polymerase chain reaction; profit; severe acute respiratory syndrome","SARS-associated coronavirus, , http://www.bcgsc.ca/bioinfo/SARS/; SARS coronavirus sequencing, , http://www.cdc.gov/ncidod/sars/sequence.htm; http://www.nml.ca/; Walgate, R., (2003) Cause of SARS disputed, , http://www.the-scientist.com/news/20030411/04, The Scientist, April 11; Walgate, R., (2003) Latest SARS evidence, , http://www.the-scientist.com/news/20030404/03/, The Scientist, April 4; http://www.artus-biotech2.com/en/index_flash.php; Haijema, B.J., Volders, H., Rottier, P.J., Switching species tropism: an effective way to manipulate the feline coronavirus genome (2003) J Virol, 77, pp. 4528-4538; Carlo, U., http://www.timesonline.co.uk/article/0,60-642183,00.html, Dr","Walgate, R.email: walgate@scienceanalysed.com",,"BioMed Central Ltd.",14747596,,GNBLF,,"English","Genome Biol.",Article,"Final",Open Access,Scopus,2-s2.0-84974687883
"Bohannon J.","7003431358;","From bioweapons backwater to main attraction",2003,"Science","300","5618",,"414","415",,5,"10.1126/science.300.5618.414","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037453471&doi=10.1126%2fscience.300.5618.414&partnerID=40&md5=a1ceacdc19f81683bb02efdfc2e7c9c8",,"Bohannon, J.","Anthrax researchers, like experts on coronaviruses (see above story), find themselves thrust into a new environment.",,"Disease control; Research; Bioweapons; Viruses; abthrax; anthrax toxin; anthrax vaccine; antibiotic agent; bacterial DNA; bacterial protein; bacterium antibody; ciprofloxacin; DNA vaccine; unclassified drug; anthrax toxin; anthrax vaccine; antitoxin; ATXA protein, Bacillus anthracis; bacterial antigen; bacterial toxin; DNA vaccine; transactivator protein; biological weapon; virus; anthrax; antibiotic resistance; antibiotic therapy; Bacillus anthracis; bacterial genetics; biological warfare; budget; human; nonhuman; priority journal; research; short survey; terrorism; United States; vaccination; victim; animal; anthrax; bacterial gene; bacterial genome; bacterial spore; conference paper; drug effect; gene expression regulation; genetics; immunology; microbiology; pathogenicity; physiology; plasmid; serodiagnosis; Anthrax; Bacillus anthracis; Bacteria (microorganisms); Animals; Anthrax; Anthrax Vaccines; Antigens, Bacterial; Antitoxins; Bacillus anthracis; Bacterial Proteins; Bacterial Toxins; Biological Warfare; Bioterrorism; Drug Resistance, Bacterial; Gene Expression Regulation, Bacterial; Genes, Bacterial; Genome, Bacterial; Humans; Neutralization Tests; Plasmids; Spores, Bacterial; Trans-Activators; Vaccination; Vaccines, DNA",,,,,00368075,,SCIEA,"12702854","English","Science",Short Survey,"Final",,Scopus,2-s2.0-0037453471
"Peiris J.S.M., Lai S.T., Poon L.L.M., Guan Y., Yam L.Y.C., Lim W., Nicholls J., Yee W.K.S., Yan W.W., Cheung M.T., Cheng V.C.C., Chan K.H., Tsang D.N.C., Yung R.W.H., Ng T.K., Yuen K.Y.","7005486823;7402937038;7005441747;7202924055;7102764741;7202378277;7201463077;7005216073;7402221587;7201897513;23670479400;7406034307;7005609132;7005594277;7402229817;36078079100;","Coronavirus as a possible cause of severe acute respiratory syndrome",2003,"Lancet","361","9366",,"1319","1325",,1680,"10.1016/S0140-6736(03)13077-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242717589&doi=10.1016%2fS0140-6736%2803%2913077-2&partnerID=40&md5=c9a4585fd30df220046bd73c1b7880cd","Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Department of Medicine, Intensive Care and Pathology, Princess Margaret Hospital, Hong Kong, Hong Kong; Government Virus Unit, Department of Health, Hong Kong, Hong Kong; Department of Medicine and Pathology, Pamela Youde Nethersole E. Hospital, Hong Kong, Hong Kong; Department of Medicine, Kwong Wah Hospital, Hong Kong, Hong Kong; Department of Pathology, Queen Elizabeth Hospital, Hong Kong, SAR, Hong Kong; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, SAR, Hong Kong","Peiris, J.S.M., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong, Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, SAR, Hong Kong; Lai, S.T., Department of Medicine, Intensive Care and Pathology, Princess Margaret Hospital, Hong Kong, Hong Kong; Poon, L.L.M., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Yam, L.Y.C., Department of Medicine and Pathology, Pamela Youde Nethersole E. Hospital, Hong Kong, Hong Kong; Lim, W., Government Virus Unit, Department of Health, Hong Kong, Hong Kong; Nicholls, J., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Yee, W.K.S., Department of Medicine, Kwong Wah Hospital, Hong Kong, Hong Kong; Yan, W.W., Department of Medicine, Intensive Care and Pathology, Princess Margaret Hospital, Hong Kong, Hong Kong; Cheung, M.T., Department of Medicine and Pathology, Pamela Youde Nethersole E. Hospital, Hong Kong, Hong Kong; Cheng, V.C.C., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Chan, K.H., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Tsang, D.N.C., Department of Pathology, Queen Elizabeth Hospital, Hong Kong, SAR, Hong Kong; Yung, R.W.H., Department of Medicine and Pathology, Pamela Youde Nethersole E. Hospital, Hong Kong, Hong Kong; Ng, T.K., Department of Medicine, Intensive Care and Pathology, Princess Margaret Hospital, Hong Kong, Hong Kong; Yuen, K.Y., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong","Background: An outbreak of severe acute respiratory syndrome (SARS) has been reported in Hong Kong. We investigated the viral cause and clinical presentation among 50 patients. Methods: We analysed case notes and microbiological findings for 50 patients with SARS, representing more than five separate epidemiologically linked transmission clusters. We defined the clinical presentation and risk factors associated with severe disease and investigated the causal agents by chest radiography and laboratory testing of nasopharyngeal aspirates and sera samples. We compared the laboratory findings with those submitted for microbiological investigation of other diseases from patients whose identity was masked. Findings: Patients' age ranged from 23 to 74 years. Fever, chills, myalgia, and cough were the most frequent complaints. When compared with chest radiographic changes, respiratory symptoms and auscultatory findings were disproportionally mild. Patients who were household contacts of other infected people and had older age, lymphopenia, and liver dysfunction were associated with severe disease. A virus belonging to the family Coronaviridae was isolated from two patients. By use of serological and reverse-transcriptase PCR specific for this virus, 45 of 50 patients with SARS, but no controls, had evidence of infection with this virus. Interpretation: A coronavirus was isolated from patients with SARS that might be the primary agent associated with this disease. Serological and molecular tests specific for the virus permitted a definitive laboratory diagnosis to be made and allowed further investigation to define whether other cofactors play a part in disease progression.",,"adult; age; aged; article; aspiration; blood sampling; chill; clinical article; clinical feature; comparative study; Coronavirus; coughing; data analysis; disease association; disease severity; epidemiological data; female; fever; human; image analysis; laboratory test; liver dysfunction; lung auscultation; lymphocytopenia; male; medical record; microbiological examination; myalgia; nasopharynx; nucleotide sequence; pneumonia; priority journal; reverse transcription polymerase chain reaction; risk factor; serology; serum; severe acute respiratory syndrome; symptom; thorax radiography; virus infection; virus isolation; virus transmission","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, p. 86; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Chan, K.H., Maldeis, N., Pope, W., Evaluation of directigen flu A+B test for rapid diagnosis of influenza A and B virus infections (2002) J Clin Microbiol, 40, pp. 1675-1680; Wiedbrauk, D.L., Johnston, S.L.G., (1993) Manual of clinical virology, , New York: Raven Press; Fouchier, R.A., Bestebroer, T.M., Herfst, S., Van Der Kemp, L., Rimmelzwaan, G.F., Osterhaus, A.D., Detection of influenza A virus from different species by PCR amplification of conserved sequences in the matrix gene (2000) J Clin Microbiol, 38, pp. 4096-4101; Holmes, K.V., Coronaviruses (2001) Fields Virology 4th edn, pp. 1187-1203. , D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott Williams and Wilkins; El-Sahly, H.M., Atmar, R.L., Glezen, W.P., Greenberg, S.B., Spectrum of clinical illness in hospitalized patients with ""common cold"" virus infections (2000) Clin Infect Dis, 31, pp. 96-100; Fotz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; Wenzel, R.P., Hendley, J.O., Davies, J.A., Gwaltney J.M., Jr., Coronavirus infections in military recruits: Three-year study with coronavirus strains OC43 and 229E (1974) Am Rev Respir Dis, 109, pp. 621-624; Talbot, P.J., Cote, G., Arbour, N., Human coronavirus OC43 and 229E persistence in neural cell cultures and human brains Adv Exp Med Biol, , in press; McIntosh, K., Coronaviruses: A comparative review (1974) Curr Top Microbiol Immunol, 63, pp. 85-129; McIntosh, K., Kapikian, A.Z., Turner, H.C., Hartley, J.W., Parrott, R.H., Chanock, R.M., Seroepidemiologic studies of coronavirus infection in adults and children (1970) Am J Epidemiol, 91, pp. 585-592; Caul, E.O., Egglestone, S.I., Further studies on human enteric coronaviruses (1977) Arch Virol, 54, pp. 107-117; Cheung, C.Y., Poon, L.L.M., Lau, A.S.Y., Induction of proinflammatory cytokines in human macrophages by influenza A (H5N1) viruses: A mechanism for the unusual severity of human disease (2002) Lancet, 360, pp. 1831-1837; Yuen, K.Y., Chan, P.K.S., Peiris, M., Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus (1998) Lancet, 351, pp. 467-471","Peiris, J.S.M.; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, SAR, Hong Kong; email: malik@hkucc.hku.hk",,"Elsevier Limited",01406736,,LANCA,"12711465","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0242717589
"Falsey A.R., Walsh E.E.","7003365074;7202168527;","Novel coronavirus and severe acute respiratory syndrome",2003,"Lancet","361","9366",,"1312","1313",,39,"10.1016/S0140-6736(03)13084-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037454390&doi=10.1016%2fS0140-6736%2803%2913084-X&partnerID=40&md5=d53dfacf6dc4c87535ae3f46ff4a0f8d","Rochester General Hospital, Univ. Rochester Sch. of Med./Dent., Rochester, NY 1462, United States","Falsey, A.R., Rochester General Hospital, Univ. Rochester Sch. of Med./Dent., Rochester, NY 1462, United States; Walsh, E.E., Rochester General Hospital, Univ. Rochester Sch. of Med./Dent., Rochester, NY 1462, United States",[No abstract available],,"creatine kinase; glucocorticoid; liver enzyme; ribavirin; virus RNA; anamnesis; antibody blood level; antigen detection; assisted ventilation; blood sampling; bronchus secretion; clinical feature; Coronavirus; coughing; disease association; disease severity; dose time effect relation; epidemic; government; health care management; health status; Hong Kong; human; infection control; laboratory; lethality; lung auscultation; lymphocytopenia; medical research; molecular genetics; mortality; note; physician; pneumonia; priority journal; respiratory failure; reverse transcription polymerase chain reaction; sensitivity and specificity; serology; serum; severe acute respiratory syndrome; technique; thorax radiography; travel; virus culture; virus infection; virus isolation","Kass, E.H., Legionnaires' disease (1977) N Engl J Med, 297, pp. 1229-1230; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe respiratory syndrome in Canada (2003) N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030634v2, March 31; (2003) CDC lab analysis suggests new coronavirus may cause SARS, , http://www.cdc.gov/od/oc/media/pressrel/r030324.htm, March 24; (2003) CDC telebriefing transcript: CDC update on severe acute respiratory distress syndrome (SARS), , http://www.cdc.gov/od/oc/media/transcripts/t030404.htm, April 4; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030666v2, March 31; Falsey, A.R., Cunningham, C.K., Barker, W.H., Respiratory syncytial virus and Influenza A infections in the hospitalized elderly (1995) J Infect Dis, 172, pp. 389-394; Peret, T.C., Boivin, G., Li, Y., Characterization of human metapneumoviruses isolated from patients in North America (2002) J Infect Dis, 185, pp. 1660-1663; Zambon, M.C., Stockton, J.D., Clewley, J.P., Fleming, D.M., Contribution of influenza and respiratory syncytial virus to community cases of influenza-like illness: An observational study (2001) Lancet, 358, pp. 1410-1416; Nicholson, K.G., Kent, J., Hammersley, V., Cancio, E., Acute viral infections of upper respiratory tract in elderly people living in the community; Comparative, prospective, population based study of disease burden (1997) BMJ, 315, pp. 1060-1064","Falsey, A.R.; Rochester General Hospital, Univ. Rochester Sch. of Med./Dent., Rochester, NY 1462, United States; email: Ann.Falsey@viahealth.org",,"Elsevier Limited",01406736,,LANCA,"12711460","English","Lancet",Note,"Final",Open Access,Scopus,2-s2.0-0037454390
"Zambon M.","7006818684;","Severe acute respiratory syndrome revisited: Coronavirus may be responsible, but new information arrives every day",2003,"BMJ","326","7394",,"831","832",,10,"10.1136/bmj.326.7394.831","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037454361&doi=10.1136%2fbmj.326.7394.831&partnerID=40&md5=dea3194853c4bf5c343de8045d2a404b","Enteric, Respiratory and Neurological Virus Laboratory, Health Protection Agency, London NW9 5HT, United Kingdom","Zambon, M., Enteric, Respiratory and Neurological Virus Laboratory, Health Protection Agency, London NW9 5HT, United Kingdom",[No abstract available],,"Asia; Canada; Coronavirus; diagnostic test; economic aspect; editorial; Hong Kong; human; incubation time; infection control; laboratory test; Metapneumovirus; onset age; pathogenesis; pneumonia; priority journal; severe acute respiratory syndrome; Singapore; world health organization; Adult; Communicable Diseases, Emerging; Coronaviridae; Disease Outbreaks; Humans; Metapneumovirus; Paramyxoviridae Infections; Severe Acute Respiratory Syndrome","Zambon, M.C., Nicholson, K.G., Sudden acute respiratory syndrome (2003) BMJ, 326, pp. 669-670; (2003) Summary on major findings in relation to coronavirus by members of the WHO multi-centre collaborative network on SARS aetiology and diagnosis, , http://www.who.int/csr/sars/findings/en, Geneva WHO, 4 April (accessed 10Apr 2003); Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavi-rus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361. , http://image.thelancet.com/extras/03art3477web.pdf, (accessed 11 Apr 2003); Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, , http://content.nejm.org/cgi/reprint/NEJMoa030634v1.pdf, published ahead of print, 31 March 2003 (accessed 11 Apr 2003)","Zambon, M.; Enteric, Respiratory and Neurological Virus Laboratory, Health Protection Agency, London NW9 5HT, United Kingdom",,,09598138,,,"12702595","English","BMJ",Editorial,"Final",,Scopus,2-s2.0-0037454361
"Chan-Yeung M., Yu W.C.","34567622600;7403914214;","Outbreak of severe acute respiratory syndrome in Hong Kong Special Administrative Region: Case report",2003,"BMJ","326","7394",,"850","852",,102,"10.1136/bmj.326.7394.850","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037454366&doi=10.1136%2fbmj.326.7394.850&partnerID=40&md5=b45d3645bb31edf283f4dec93bf84436","Division of Respiratory and Critical Care Medicine, Queen Mary Hospital, University of Hong Kong, 4/F, Professorial Block, SAR, China; Department of Medicine, Princess Margaret Hospital, SAR, China","Chan-Yeung, M., Division of Respiratory and Critical Care Medicine, Queen Mary Hospital, University of Hong Kong, 4/F, Professorial Block, SAR, China; Yu, W.C., Department of Medicine, Princess Margaret Hospital, SAR, China","Objective: To describe the outbreak of severe acute respiratory syndrome in Hong Kong. Design: Descriptive case series. Setting: Hong Kong, Special Administrative Region, China Results: The outbreak started with a visitor from southern China on 21 February. At the hospitals where the first cases were treated the disease spread quickly among healthcare workers, and then out into the community as family members became infected. By 1 April, 685 cases had been reported with 16 deaths. Symptoms include high fever and one or more respiratory symptoms (including cough, shortness of breath, and difficulty breathing). Changes in lung tissue suggest that part of the lung damage is due to cytokines induced by the microbial agent, which has led to empirical treatment with corticosteroids, broad spectrum antiviral agent, and antibacterial cover. There is strong evidence that a novel coronavirus is the pathogen. Precautions for droplet infection should be instituted, including the wearing of masks and rigorous disinfection and hygiene procedures. On 27 March the Department of Health announced drastic measures, including vigorous contact tracing and examination, quarantine of contacts in their homes, and closure of all schools and universities. Conclusion: The rapidity of the spread of the disease and the morbidity indicate that the agent responsible is highly infectious and virulent. Strict infection control measures for droplet and contact transmission by healthcare workers, a vigilant healthcare profession, and public education are essential for disease prevention. © 2003, BMJ Publishing Group Ltd. All rights reserved.",,"antiinfective agent; antivirus agent; corticosteroid; hydrocortisone; levofloxacin; macrolide; methylprednisolone; ribavirin; adult respiratory distress syndrome; article; case report; clinical feature; Coronavirus; corticosteroid therapy; drug indication; empiricism; epidemic; histopathology; Hong Kong; human; human tissue; infection control; mortality; open lung biopsy; pneumonia; priority journal; reverse transcription polymerase chain reaction; severe acute respiratory syndrome; virus culture; virus infection; virus pathogenesis; virus transmission; Communicable Diseases, Emerging; Cross Infection; Disease Outbreaks; Disease Transmission, Patient-to-Professional; Hong Kong; Humans; Laboratory Techniques and Procedures; Severe Acute Respiratory Syndrome","Severe acute respiratory syndrome (SARS) (2003), http://www.who.int/csr/2003_03_12/en, March 12th; Atypical pneumonia http://www.info.gov.hk/info/infection-c.htm, (accessed 7 Apr 2003); Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , http://content.nejm.org/cgi/reprint/NEJMoa030666v2.pdf, Apr 1 [epub ahead of print] (accessed 7 Apr 2003); Periris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrom (2003) Lancet, , http://image.thelancet.com/extras/03art3477web.pdf, Online 8 Apr; Severe acute respiratory syndrome: clinical guidelines http://www.ha.org.hk/hesd/nsapi/?MIval=ha_view_template&group=PRS&Area=CGL, (revised 27 Mar 2003) (accessed 7 Apr 2003); Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong N Engl J Med, 3003. , http://www.nejm.org/, 7 Apr; Severe acute respiratory syndrome (SARS): information for clinicians http://www.cdc.gov/ncidod/sars/clinicians.htm, (accessed 7 Apr 2003)","Chan-Yeung, M.; Division of Respiratory and Critical Care Medicine, Queen Mary Hospital, University of Hong Kong, 4/F, Professorial Block, SAR, China",,,09598138,,,"12702616","English","BMJ",Article,"Final",Open Access,Scopus,2-s2.0-0037454366
"Tao S., Yang R., Li Z., Zhang Z., Zhou Y., Zhang Q., Zhu P., Du J., Zhao C., Ma Q., Ren L., Wang C., Jiang D., Liu Y., Yang H., Rong L., An S., Li Z., Wang J., Cheng Y., Liu O., Zheng Z., Zuo H., Shan Q., Ruan L., Lu Z., Hong T., Cheng J.","14919746100;8731276000;57191704370;55721686500;8856367700;7406718867;55420602100;7402575083;57199830709;7402815613;7202371986;55766678000;57198894088;7410220196;56100731700;57206381605;7203025534;55548780300;56147682700;7404914368;57198317318;57198507914;7005708907;7007145032;7006832508;7404769102;41961152900;26643191200;","Fabrication and application of SARS coronavirus gene chips for preliminary clinical sample testing",2003,"Qinghua Daxue Xuebao/Journal of Tsinghua University","43","5",,"715","720",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041317229&partnerID=40&md5=5bd33dc94cf7aa17d5f76f41955c9dd2","Lab. of Biomembrane, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China; Capital Biochip Corp., Beijing 100084, China; No. 302 Hospital of PLA, Beijing 100039, China; Jiuxianqiao Hospital, Tsinghua Univ., Beijing 100016, China; Yuquanlu Hospital, Tsinghua Univ., Beijing 100039, China","Tao, S., Lab. of Biomembrane, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Yang, R., Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Li, Z., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Zhang, Z., Lab. of Biomembrane, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Zhou, Y., Lab. of Biomembrane, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Zhang, Q., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Zhu, P., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Du, J., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Zhao, C., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Ma, Q., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Ren, L., Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Wang, C., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Jiang, D., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Liu, Y., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Yang, H., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Rong, L., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; An, S., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Li, Z., Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China; Wang, J., Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Cheng, Y., No. 302 Hospital of PLA, Beijing 100039, China; Liu, O., Jiuxianqiao Hospital, Tsinghua Univ., Beijing 100016, China; Zheng, Z., Yuquanlu Hospital, Tsinghua Univ., Beijing 100039, China; Zuo, H., Yuquanlu Hospital, Tsinghua Univ., Beijing 100039, China; Shan, Q., Jiuxianqiao Hospital, Tsinghua Univ., Beijing 100016, China; Ruan, L., Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Lu, Z., No. 302 Hospital of PLA, Beijing 100039, China; Hong, T., Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; Cheng, J., Lab. of Biomembrane, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China, Natl. Res. Ctr. for Biochip Technol., Beijing 100084, China, Capital Biochip Corp., Beijing 100084, China","A gene chip-based analytical system was developed for potential early detection of severe acute respiratory syndrome (SARS) coronavirus presented in the collected clinical samples. SARS coronavirus RNAs were extracted from both sputum and whole blood. The cDNAs were then produced through reverse-transcription process followed by nested PCR to generate sufficient amount of amplicons with expected sizes. The amplicons were allowed to hybridize against the SARS coronavirus-specific DNA probes immobilized on the glass substrate for confirming the presence of the SARS coronavirus in the collected clinical samples. Two sputum samples and two whole blood samples were tested with the gene chips and the results indicate that the SARS coronavirus exists in all four samples.","Clinical sample; Gene chip; SARS coronavirus","Centrifugation; DNA; Genes; Laser diagnostics; Respiratory system; RNA; Sampling; Testing; Coronavirus; Gene chip; Severe acute respiratory syndrome; Viruses","Marra, M.A., Jones, S.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus http://www.sciencemag.org/scienceexpress/recent.shtml; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome http://www.sciencemag.org/scienceexpress/recent.shtml","Wang, J.; Inst. of Viral Disease Control, Chinese Ctr. for Disease Control, Beijing 100052, China; email: wangjw28@vip.sina.com",,,10000054,,QDXKE,,"Chinese","Qinghua Daxue Xuebao",Article,"Final",,Scopus,2-s2.0-0041317229
"Hackney K., Cavanagh D., Kaiser P., Britton P.","6505821852;26642890500;57195190507;57203302770;","In vitro and in ovo expression of chicken gamma interferon by a defective RNA of avian coronavirus infectious bronchitis virus",2003,"Journal of Virology","77","10",,"5694","5702",,16,"10.1128/JVI.77.10.5694-5702.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038033072&doi=10.1128%2fJVI.77.10.5694-5702.2003&partnerID=40&md5=9da9e825b650bb1e28e488b49f6144f7","Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","Hackney, K., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Kaiser, P., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; Britton, P., Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom, Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom","Coronavirus defective RNAs (D-RNAs) have been used for site-directed mutagenesis of coronavirus genomes and for expression of heterologous genes. D-RNA CD-61 derived from the avian coronavirus infectious bronchitis virus (IBV) was used as an RNA vector for the expression of chicken gamma interferon (chIFN-γ). D-RNAs expressing chIFN-γ were shown to be capable of rescue, replication, and packaging into virions in a helper virus-dependent system following electroporation of in vitro-derived T7 RNA transcripts into IBV-infected cells. Secreted chIFN-γ, under the control of an IBV transcription-associated sequence derived from gene 5 of the Beaudette strain, was expressed from two different positions within CD-61 and shown to be biologically active. In addition, following infection of 10-day-old chicken embryos with IBV containing D-RNAs expressing chIFN-γ, the allantoic fluid was shown to contain biologically active chIFN-γ, demonstrating that IBV D-RNAs can express heterologous genes in vivo.",,"CD61 antigen; gamma interferon; virus RNA; virus vector; amnion fluid; animal cell; animal model; article; Avian infectious bronchitis virus; chicken; controlled study; electroporation; embryo; gene expression; gene sequence; heterologous expression; in vitro study; mutagenesis; nonhuman; priority journal; protein expression; protein secretion; virus genome; virus infection; virus replication; virus strain; virus transcription; Animals; Cells, Cultured; Chick Embryo; Chickens; Defective Viruses; DNA-Binding Proteins; Eggs; Gene Expression Regulation, Viral; Genetic Vectors; Infectious bronchitis virus; Interferon Type II; Retroviridae Proteins; RNA, Viral; Trans-Activators; Virion; Virus Assembly; Virus Replication","Alonso, S., Izeta, A., Sola, I., Enjuanes, L., Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus (2002) J. 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Immunopathol., 74, pp. 137-144; Lawson, S., Rothwell, L., Lambrecht, B., Howes, K., Venugopal, K., Kaiser, P., Turkey and chicken interferon-γ, which share high sequence identity, are biologically cross-reactive (2001) Dev. Comp. Immunol., 25, pp. 69-82; Liao, C.L., Zhang, X., Lai, M.M., Coronavirus defective-interfering RNA as an expression vector: The generation of a pseudorecombinant mouse hepatitis virus expressing hemagglutinin-esterase (1995) Virology., 208, pp. 319-327; Lillehoj, H.S., Choi, K.D., Recombinant chicken interferon-γ mediated inhibition of Eimeria tenella development in vitro and reduction of oocyst production and body weight loss following Eimeria acervulina challenge infection (1998) Avian Dis., 42, pp. 307-314; Lin, Y.J., Lai, M.M., Deletion mapping of a mouse hepatitis virus defective interfering RNA reveals the requirement of an internal and discontiguous sequence for replication (1993) J. 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Dis., 184, pp. 1423-1430; Min, W., Lillehoj, H.S., Burnside, J., Weining, K.C., Staeheli, P., Zhu, J.J., Adjuvant effects of IL-1β, IL-2, IL-8, IL-15, IFN-α, IFN-γ, TGF-β4 and lymphotactin on DNA vaccination against Eimeria acervulina (2001) Vaccine, 20, pp. 267-274; Otsuki, K., Maeda, J., Yamamoto, H., Tsubokura, M., Studies on avian infectious bronchitis virus (IBV). III. Interferon induction by and sensitivity to interferon of IBV (1979) Arch. 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Virol., 81, pp. 791-801; Yilma, T., Owens, S., Fennie, E.H., Anderson, K.P., Enhancement of primary and secondary immune responses by interferon-γ (1989) Adv. Exp. Med. Biol., 251, pp. 145-152; Zhang, X., Hinton, D.R., Cua, D.J., Stohlman, S.A., Lai, M.M., Expression of interferon-γ by a coronavirus defective-interfering RNA vector and its effect on viral replication, spread, and pathogenicity (1997) Virology, 233, pp. 327-338; Zhang, X., Hinton, D.R., Park, S., Parra, B., Liao, C.L., Lai, M.M., Stohlman, S.A., Expression of hemagglutinin/esterase by a mouse hepatitis virus coronavirus defective-interfering RNA alters viral pathogenesis (1998) Virology, 242, pp. 170-183","Britton, P.; Division of Molecular Biology, Institute for Animal Health, Compton Laboratory, Newbury, Berkshire RG20 7NN, United Kingdom; email: paul.britton@bbsrc.ac.uk",,,0022538X,,JOVIA,"12719562","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0038033072
"Nilges K., Höhn H., Pilch H., Neukirch C., Freitag K., Talbot P.J., Maeurer M.J.","6507885740;7005564164;35556789600;6603734795;7004804085;7102670281;7004422039;","Human papillomavirus type 16 E7 peptide-directed CD8+ T cells from patients with cervical cancer are cross-reactive with the coronavirus NS2 protein",2003,"Journal of Virology","77","9",,"5464","5474",,54,"10.1128/JVI.77.9.5464-5474.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344080581&doi=10.1128%2fJVI.77.9.5464-5474.2003&partnerID=40&md5=2f0161dbdcc0728fb955d56071ff3c8c","Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; Department of Gynecology, Johannes Gutenberg University, Mainz, Germany; Human Health Research Center, INRS-Institut Armand Frappier, University of Quebec, Laval, Que., Canada","Nilges, K., Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; Höhn, H., Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; Pilch, H., Department of Gynecology, Johannes Gutenberg University, Mainz, Germany; Neukirch, C., Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; Freitag, K., Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; Talbot, P.J., Human Health Research Center, INRS-Institut Armand Frappier, University of Quebec, Laval, Que., Canada; Maeurer, M.J., Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany","Human papillomavirus type 16 (HPV16) E6 and E7 oncoproteins are required for cellular transformation and represent candidate targets for HPV-specific and major histocompatibility complex class I-restricted CD8+-T-cell responses in patients with cervical cancer. Recent evidence suggests that cross-reactivity represents the inherent nature of the T-cell repertoire. We identified HLA-A2 binding HPV16 E7 variant peptides from human bacterial, or viral origin which are able to drive CD8+-T-cell responses directed against wild-type HPV16 E7 amino acid 11 to 19/20 (E711-19/20) epitope YMLDLQPET(T) in vitro. CD8+ T cells reacting to the HLA-A2-presented peptide from HPV16 E711-19(20) recognized also the HLA-A2 binding peptide TMLDIQPED (amino acids 52 to 60) from the human coronavirus OC43 NS2 gene product. Establishment of coronavirus NS2-specific, HLA-A2-restricted CD8+-T-cell clones and ex vivo analysis of HPV16 E7 specific T cells obtained by HLA-A2 tetramer-guided sorting from PBL or tumor-infiltrating lymphocytes obtained from patients with cervical cancer showed that cross-reactivity with HPV16 E711-19(20) and coronavirus NS252-60 represents a common feature of this antiviral immune response defined by cytokine production. Zero of 10 patients with carcinoma in situ neoplasia and 3 of 18 patients with cervical cancer showed ≥0.1% HPV16 E7-reactive T cells in CD8+ peripheral blood lymphocytes. In vivo priming with HPV16 was confirmed in patients with cervical cancer or preinvasive HPV16-positive lesions using HLA-A2 tetramer complexes loaded with the E6-derived epitope KLPQLCTEL. In contrast, we could not detect E6-reactive T cells in healthy individuals. These data imply that the measurement of the HPV16 E711-19(20) CD8+-T-cell response may reflect cross-reactivity with a common pathogen and that variant peptides may be employed to drive an effective cellular immune response against HPV.",,"epitope; gene product; HLA A2 antigen; lysylleucylprolylglutaminylleucylcysteinylthreonylglutamylleucine; peptide derivative; protein NS2; tetramer; threonylmethionylleucylaspartylisoleucylglutaminylprolylglutamylaspartic acid; tyrosylmethionylleucylaspartylleucylglutaminylprolylglutamylthreonine; unclassified drug; virus protein; article; cancer patient; carcinoma in situ; cellular immunity; clinical article; controlled study; Coronavirus; cross reaction; cytokine production; female; human; human cell; immune response; in vivo study; lymphocyte clone; measurement; nucleotide sequence; peripheral lymphocyte; priority journal; T lymphocyte; tumor associated leukocyte; uterine cervix cancer; Wart virus; Amino Acid Sequence; CD8-Positive T-Lymphocytes; Coronavirus; Cross Reactions; Epitopes, T-Lymphocyte; Female; HLA-A2 Antigen; Humans; Lymphocyte Activation; Molecular Sequence Data; Oncogene Proteins, Viral; Papillomaviridae; Papillomavirus Infections; Peptides; Tumor Virus Infections; Uterine Cervical Neoplasms; Viral Nonstructural Proteins","Adams, M., Borysiewicz, L., Fiander, A., Man, S., Jasani, B., Navabi, H., Lipetz, C., Mason, M., Clinical studies of human papilloma vaccines in pre-invasive and invasive cancer (2001) Vaccine, 19, pp. 2549-2556; Al-Saleh, W., Giannini, S.L., Jacobs, N., Moutschen, M., Doyen, J., Boniver, J., Delvenne, P., Correlation of T-helper secretory differentiation and types of antigen-presenting cells in squamous intraepithelial lesions of the uterine cervix (1998) J. Pathol, 184, pp. 283-290; Bakker, A.B., Schreurs, M.W., Tafazzul, G., De Boer, A.J., Kawakami, Y., Adema, G.J., Figdor, C.G., Identification of a novel peptide derived from the melanocyte-specific gp100 antigen as the dominant epitope recognized by an HLA-A2.1-restricted anti-melanoma CTL line (1995) Int. J. Cancer, 62, pp. 97-102; Bartholomew, J.S., Stacey, S.N., Coles, B., Burt, D.J., Arrand, J.R., Stern, P.L., Identification of a naturally processed HLA A0201-restricted viral peptide from cells expressing human papillomavirus type 16 E6 oncoprotein (1994) Eur. J. 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USA, 92, pp. 5042-5046; Misko, I.S., Cross, S.M., Khanna, R., Elliott, S.L., Schmidt, C., Pye, S.J., Silins, S.L., Crossreactive recognition of viral, self, and bacterial peptide ligands by human class I-restricted cytotoxic T lymphocyte clonotypes: Implications for molecular mimicry in autoimmune disease (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 2279-2284; Mohagheghpour, N., Gammon, D., Kawamura, L.M., Van Vollenhoven, A., Benike, C.J., Engleman, E.G., CTL response to Mycobacterium tuberculosis: Identification of an immunogenic epitope in the 19-kDa lipoprotein (1998) J. Immunol., 161, pp. 2400-2406; Pilch, H., Hohn, H., Freitag, K., Neukirch, C., Necker, A., Haddad, P., Tanner, B., Maeurer, M.J., Improved assessment of T-cell receptor (TCR) VB repertoire in clinical specimens: Combination of TCR-CDR3 spectratyping with flow cytometry-based TCR VB frequency analysis (2002) Clin. Diagn. Lab. Immunol., 9, pp. 257-266; Puisieux, I., Even, J., Pannetier, C., Jotereau, F., Favrot, M., Kourilsky, P., Oligoclonality of tumor-infiltrating lymphocytes from human melanomas (1994) J. Immunol., 153, pp. 2807-2818; Ressing, M.E., Sette, A., Brandt, R.M., Ruppert, J., Wentworth, P.A., Hartman, M., Oseroff, C., Kast, W.M., Human CTL epitopes encoded by human papillomavirus type 16 E6 and E7 identified through in vivo and in vitro immunogenicity studies of HLAA*0201-binding peptides (1995) J. Immunol., 154, pp. 5934-5943; Ressing, M.E., Van Driel, W.J., Brandt, R.M., Kenter, G.G., De Jong, J.H., Bauknecht, T., Fleuren, G.J., Melief, C.J., Detection of T helper responses, but not of human papillomavirus-specific cytotoxic T lymphocyte responses, after peptide vaccination of patients with cervical carcinoma (2000) J. Immunother., 23, pp. 255-266; Ressing, M.E., Van Driel, W.J., Celis, E., Sette, A., Brandt, M.P., Hartman, M., Anholts, J.D., Melief, C.J., Occasional memory cytotoxic T-cell responses of patients with human papillomavirus type 16-positive cervical lesions against a human leukocyte antigen-A *0201-restricted E7-encoded epitope (1996) Cancer Res., 56, pp. 582-588; Rudolf, M.P., Man, S., Melief, C.J., Sette, A., Kast, W.M., Human T-cell responses to HLA-A-restricted high binding affinity peptides of human papillomavirus type 18 proteins E6 and E7 (2001) Clin. Cancer Res., 7, pp. 788s-795s; Seedorf, K., Krammer, G., Durst, M., Suhai, S., Rowekamp, W.G., Human papillomavirus type 16 DNA sequence (1985) Virology, 145, pp. 181-185; Selin, L.K., Nahill, S.R., Welsh, R.M., Cross-reactivities in memory cytotoxic T lymphocyte recognition of heterologous viruses (1994) J. Exp. Med., 179, pp. 1933-1943; Selin, L.K., Varga, S.M., Wong, I.C., Welsh, R.M., Protective heterologous antiviral immunity and enhanced immunopathogenesis mediated by memory T cell populations (1998) J. Exp. Med., 188, pp. 1705-1715; Smith, D.K., Dudani, R., Pedras-Vasconcelos, J.A., Chapdelaine, Y., Van Faassen, H., Sad, S., Cross-reactive antigen is required to prevent erosion of established T cell memory and tumor immunity: A heterologous bacterial model of attrition (2002) J. Immunol., 169, pp. 1197-1206; Song, Y.S., Kee, S.H., Kim, J.W., Park, N.H., Kang, S.B., Chang, W.H., Lee, H.P., Major sequence variants in E7 gene of human papillomavirus type 16 from cervical cancerous and noncancerous lesions of Korean women (1997) Gynecol. Oncol., 66, pp. 275-281; Thomson, C.T., Kalergis, A.M., Sacchettini, J.C., Nathenson, S.G., A structural difference limited to one residue of the antigenic peptide can profoundly alter the biological outcome of the TCR-peptide/MHC class I interaction (2001) J. Immunol., 166, pp. 3994-3997; Tjandrawan, T., Martin, D.M., Maeurer, M.J., Castelli, C., Lotze, M.T., Storkus, W.J., Autologous human dendriphages pulsed with synthetic or natural tumor peptides elicit tumor-specific CTLs in vitro (1998) J. Immunother., 21, pp. 149-157; Traversari, C., Van der Bruggen, P., Luescher, I.F., Lurquin, C., Chomez, P., Van Pel, A., De Plaen, E., Boon, T., A nonapeptide encoded by human gene MAGE-1 is recognized on HLA-A1 by cytolytic T lymphocytes directed against tumor antigen MZ2-E (1992) J. Exp. Med., 176, pp. 1453-1457; Varga, S.M., Wang, X., Welsh, R.M., Braciale, T.J., Immunopathology in rsv infection is mediated by a discrete oligoclonal subset of antigen-specific cd4(+) t cells (2001) Immunity, 15, pp. 637-646; Wei, C.H., Yagita, H., Masucci, M.G., Levitsky, V., Different programs of activation-induced cell death are triggered in mature activated CTL by immunogenic and partially agonistic peptide ligands (2001) J. Immunol., 166, pp. 989-995; Yang, H.Y., Dundon, P.L., Nahill, S.R., Welsh, R.M., Virus induced polyclonal cytotoxic T lymphocyte stimulation (1989) J. Immunol., 142, pp. 1710-1718; Youde, S.J., Dunbar, P.R., Evans, E.M., Fiander, A.N., Borysiewicz, L.K., Cerundolo, V., Man, S., Use of fluorogenic histocompatibility leukocyte antigen-A*0201/HPV 16 E7 peptide complexes to isolate rare human cytotoxic T-lymphocyte-recognizing endogenous human papillomavirus antigens (2000) Cancer Res., 60, pp. 365-371; Zeh H.J. III, Leder, G.H., Lotze, M.T., Salter, R.D., Tector, M., Stuber, G., Modrow, S., Storkus, W.J., Flow-cytometric determination of peptide-class I complex formation. Identification of p53 peptides that bind to HLA-A2 (1994) Hum. Immunol., 39, pp. 79-86","Maeurer, M.J.; Dept. of Medical Microbiology, University of Mainz, Hochhaus Augustusplatz, 55101 Mainz, Germany; email: maeurer@mail.uni-mainz.de",,,0022538X,,JOVIA,"12692247","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0344080581
"Ison M.G., Hayden F.G., Kaiser L., Corey L., Boeckh M.","6701366871;7103233446;57203230856;57188630168;7005979598;","Rhinovirus infections in hematopoietic stem cell transplant recipients with pneumonia",2003,"Clinical Infectious Diseases","36","9",,"1139","1143",,104,"10.1086/374340","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037542600&doi=10.1086%2f374340&partnerID=40&md5=7f5d3a7dec320ef4f884fb9027ef204c","Div. of Infect. Dis./Intl. Health, University of Virginia, Charlottesville, VA, United States; Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, University of Washington, Seattle, WA, United States; Department of Medicine, University of Washington, Seattle, WA, United States; Department of Laboratory Medicine, University of Washington, Seattle, WA, United States; Division of Infectious Diseases, University Hospital of Geneva, Geneva, Switzerland; Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, PO Box 19024, Seattle, WA, United States","Ison, M.G., Div. of Infect. Dis./Intl. Health, University of Virginia, Charlottesville, VA, United States; Hayden, F.G., Div. of Infect. Dis./Intl. Health, University of Virginia, Charlottesville, VA, United States; Kaiser, L., Division of Infectious Diseases, University Hospital of Geneva, Geneva, Switzerland; Corey, L., Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, University of Washington, Seattle, WA, United States, Department of Medicine, University of Washington, Seattle, WA, United States, Department of Laboratory Medicine, University of Washington, Seattle, WA, United States; Boeckh, M., Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, University of Washington, Seattle, WA, United States, Department of Medicine, University of Washington, Seattle, WA, United States, Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, PO Box 19024, Seattle, WA, United States","Little is known about the impact of human rhinovirus (HRV) and coronavirus infections in hematopoietic stem cell transplant (HSCT) recipients. We tested bronchoalveolar lavage (BAL) samples obtained from HSCT recipients with acute pulmonary infiltrates for HRV (n = 122) and coronavirus (n = 46) by reverse-transcriptase polymerase chain reaction. HRV RNA was detected in 6 (8%) of 77 patients, and coronavirus RNA was detected in 0 of 46 of BAL samples from HSCT recipients. The fatality rate in HRV-infected patients was high (83%), but all patients had significant coinfections, and the overall mortality rate was not different from that of patients who were negative for HRV in BAL samples. These results suggest that HRV may be a cause of lower respiratory tract infections in HSCT recipients and that its detection in BAL samples is associated with frequent copathogens. Whether the poor prognosis is due to HRV or the copathogen is not clear.",,"virus RNA; adolescent; adult; article; Coronavirus; fatality; female; hematopoietic stem cell transplantation; human; lower respiratory tract infection; lung infiltrate; lung lavage; major clinical study; male; mortality; pathogenesis; pneumonia; priority journal; prognosis; reverse transcription polymerase chain reaction; Rhinovirus; virus infection; virus isolation; Adolescent; Adult; Female; Hematopoietic Stem Cell Transplantation; Humans; Male; Middle Aged; Picornaviridae Infections; Pneumonia; Rhinovirus","Gwaltney J.M., Jr., Heinz, B.A., Rhinovirus (2002) Clinical Virology, pp. 995-1018. , Hayden FG, ed. Washington, DC: American Society for Microbiology Press; Arruda, E., Pitkaranta, A., Witek T.J., Jr., Doyle, C.A., Hayden, F.G., Frequency and natural history of rhinovirus infections in adults during autumn (1997) J Clin Microbiol, 35, pp. 2864-2868; Gonzalez, Y., Martino, R., Badell, I., Pulmonary enterovirus infections in stem cell transplant recipients (1999) Bone Marrow Transplant, 23, pp. 511-513; Bowden, R.A., Respiratory virus infections after marrow transplant: The Fred Hutchinson Cancer Research Center experience (1997) Am J Med, 102, pp. 27-30; Crooks, B.N., Taylor, C.E., Turner, A.J., Respiratory viral infections in primary immune deficiencies: Significance and relevance to clinical outcome in a single BMT unit (2000) Bone Marrow Transplant, 26, pp. 1097-1102; Monto, A.S., Fendrick, A.M., Sarnes, M.W., Respiratory illness caused by picornavirus infection: A review of clinical outcomes (2001) Clin Ther, 23, pp. 1615-1627; Rabella, N., Rodriguez, P., Labeaga, R., Conventional respiratory viruses recovered from immunocompromised patients: Clinical considerations (1999) Clin Infect Dis, 28, pp. 1043-1048; Papadopoulos, N.G., Sanderson, G., Hunter, J., Johnston, S.L., Rhinoviruses replicate effectively at lower airway temperatures (1999) J Med Virol, 58, pp. 100-104; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Connolly M.G., Jr., Baughman, R.P., Dohn, M.N., Linnemann C.C., Jr., Recovery of viruses other than cytomegalovirus from bronchoalveolar lavage fluid (1994) Chest, 105, pp. 1775-1781; Halperin, S.A., Eggleston, P.A., Hendley, J.O., Suratt, P.M., Groschel, D.H., Gwaltney J.M., Jr., Pathogenesis of lower respiratory tract symptoms in experimental rhinovirus infection (1983) Am Rev Respir Dis, 128, pp. 806-810; Papadopoulos, N.G., Bates, P.J., Bardin, P.G., Rhinoviruses infect the lower airways (2000) J Infect Dis, 181, pp. 1875-1884; Mosser, A.G., Brockman-Schneider, R., Amineva, S., Similar frequency of rhinovirus-infectible cells in upper and lower airway epithelium (2002) J Infect Dis, 185, pp. 734-743; Falsey, A.R., Walsh, E.E., Hayden, F.G., Rhinovirus and coronavirus infection-associated hospitalizations among older adults (2002) J Infect Dis, 185, pp. 1338-1341; Malcolm, E., Arruda, E., Hayden, F.G., Kaiser, L., Clinical features of patients with acute respiratory illness and rhinovirus in their bronchoalveolar lavages (2001) J Clin Virol, 21, pp. 9-16; El-Sahly, H.M., Atmar, R.L., Glezen, W.P., Greenberg, S.B., Spectrum of clinical illness in hospitalized patients with ""common cold"" virus infections (2000) Clin Infect Dis, 31, pp. 96-100; Imakita, M., Shiraki, K., Yutani, C., Ishibashi-Ueda, H., Pneumonia caused by rhinovirus (2000) Clin Infect Dis, 30, pp. 611-612; Papadopoulos, N.G., Bates, P.J., Bardin, P.G., Rhinoviruses infect the lower airways (2000) J Infect Dis, 181, pp. 1875-1884; Ghosh, S., Champlin, R., Couch, R., Rhinovirus infections in myelosuppressed adult blood and marrow transplant recipients (1999) Clin Infect Dis, 29, pp. 528-532; Folz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; Nichols, W.G., Corey, L., Gooley, T., Davis, C., Boeckh, M., Parainfluenza virus infections after hematopoietic stem cell transplantation: Risk factors, response to antiviral therapy, and effect on transplant outcome (2001) Blood, 98, pp. 573-578; Crippa, F., Holmberg, L., Carter, R.A., Infectious complications after autologous CD34-selected peripheral blood stem cell transplantation (2002) Biol Blood Marrow Transplant, 8, pp. 281-289; Arruda, E., Hayden, F.G., Detection of human rhinovirus RNA in nasal washings by PCR (1993) Mol Cell Probes, 7, pp. 373-379; Pitkaranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR (1997) J Clin Microbiol, 35, pp. 1791-1793; Pitkaranta, A., Virolainen, A., Jero, J., Arruda, E., Hayden, F.G., Detection of rhinovirus, respiratory syncytial virus, and coronavirus infections in acute otitis media by reverse transcriptase polymerase chain reaction (1998) Pediatrics, 102, pp. 291-295; Arruda, E., Crump, C.E., Rollins, B.S., Ohlin, A., Hayden, F.G., Comparative susceptibilities of human embryonic fibroblasts and HeLa cells for isolation of human rhinoviruses (1996) J Clin Microbiol, 34, pp. 1277-1279; Ison, M.G., Hayden, F.G., Viral infections in immunocompromised patients: What's new with respiratory viruses? (2002) Curr Opin Infect Dis, 15, pp. 355-367; Marr, K.A., Carter, R.A., Boeckh, M., Martin, P., Corey, L., Invasive aspergillosis in allogeneic stem cell transplant recipients: Changes in epidemiology and risk factors (2002) Blood, 100, pp. 4358-4366; Gern, J.E., Joseph, B., Galagan, D.M., Borcherding, W.R., Dick, E.C., Rhinovirus inhibits antigen-specific T cell proliferation through an intercellular adhesion molecule-1-dependent mechanism (1996) J Infect Dis, 174, pp. 1143-1150; Schmidt, G.M., Horak, D.A., Niland, J.C., Duncan, S.R., Forman, S.J., Zaia, J.A., A randomized, controlled trial of prophylactic ganciclovir for cytomegalovirus pulmonary infection in recipients of allogeneic bone marrow transplants: The City of Hope-Stanford-Syntex CMV Study Group (1991) N Engl J Med, 324, pp. 1005-1011; Slavin, M.A., Gooley, T.A., Bowden, R.A., Prediction of cytomegalovirus pneumonia after marrow transplantation from cellular characteristics and cytomegalovirus culture of bronchoalveolar lavage fluid (1994) Transplantation, 58, pp. 915-919; Rotbart, H.A., Webster, A.D., Treatment of potentially life-threatening enterovirus infections with pleconaril (2001) Clin Infect Dis, 32, pp. 228-235","Boeckh, M.; Program in Infectious Diseases, Fred Hutchinson Cancer Res. Center, PO Box 19024, Seattle, WA, United States; email: mboeckh@fhcrc.org",,,10584838,,CIDIE,"12715308","English","Clin. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0037542600
"Kökoǧlu Ö.F., Köksal N., Çetinkaya A.","9838781300;55854278100;6603014450;","Severe acute respiratory syndrome (SARS) [Şiddetli ani solunum yetersizliǧi sendromu (SARS)]",2003,"SENDROM","15","5",,"18","28",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038374529&partnerID=40&md5=b4a32823bb3ceff464d7c0dada6a15e9","KSU Medical Faculty, Department of Infection Diseases, Kahramanmaraş, Turkey","Kökoǧlu, Ö.F., KSU Medical Faculty, Department of Infection Diseases, Kahramanmaraş, Turkey; Köksal, N., KSU Medical Faculty, Department of Infection Diseases, Kahramanmaraş, Turkey; Çetinkaya, A., KSU Medical Faculty, Department of Infection Diseases, Kahramanmaraş, Turkey","The rapid worldwide spread of the coronavirus that causes severe acute respiratory syndrome (SARS) has led to 30 countries reporting cases as of May 6, 2003. The evolution, spread, and persistence of infectious diseases are facilitated by the mobility of contemporary society, for example through air travel, the continued growth in the world population, and the steady rise in the number of densely populated urban areas, especially in Asia. World Health Organization (WHO) took a pivotal role in the investigation of the outbreak, with the development of a case definition for SARS. A global network of 11 leading laboratories in 10 countries was established to collaborate in the search for the causative organism and daily updates were provided on the WHO website. After an incubation period of 2-7 days, the illness begins with a prodrome of fever (>38°C) sometimes associated with chills, rigors and other symptoms such as headache, malaise and myalgia. After 3-7 days of prodromal symptoms, a respiratory phase begins with onset of dry, nonproductive cough or dyspnea, which may progress to hypoxia. Between 10% and 20% of patients have required mechanical ventilation. The primary radiologic appearance of SARS is air-space shadowing determined on CT to be sub-pleural focal consolidation with air bronchograms and ground-glass opacities predominantly affecting the lower lobes. The initial radiographic appearance, however, may be normal. Pathological studies of patients who died with SARS show diffuse alveolar damage in the lung as the most notable feature, a finding consistent with the severe respiratory illness seen in some patients with SARS. The family Coronaviridae includes the genus coronavirus and torovirus. They are enveloped RNA viruses that cause disease in human beings and animals. The previously known human coronaviruses, types 229E and OC43 are a major cause of the common cold. Phylogenetically, human pneumonia-associated coronavirus (SARS-CoV) was not closely related to any known human or animal coronavirus or torovirus. The sequence of the complete genome of SARS-CoV was determined, and the initial characterization of the viral genome is presented in this report. The genome of SARS-CoV is 29,727 nucleotides in length, has 11 open reading frames, and the genome organization is similar to that of other coronaviruses. Phylogenetic analyses and sequence comparisons showed that SARS-CoV is not closely related to any of the previously characterized coronaviruses. SARS can be transmitted through close contact with patients, particularly by family members and health care workers. In Canada, the 11 reported cases occurred in people who had recently travelled to Hong Kong or who had close contact with family members who had recently travelled there or with health care workers who cared for patients with SARS.",,"artificial ventilation; aviation; Canada; chill; computer assisted tomography; Coronavirus; coughing; disease transmission; dyspnea; epidemic; fever; headache; health care personnel; Hong Kong; hypoxia; incubation time; malaise; myalgia; open reading frame; phylogeny; radiodiagnosis; review; rigor; RNA virus; sequence analysis; severe acute respiratory syndrome; Torovirus; virus genome; virus pneumonia; world health organization","Hui, D.N., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Yung, M.Y., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , Apr 14; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition, Geneva: World Health Organization; Peiris, J., Lai, S., Poon, L., Guan, Y., Yam, L., Lim, W., Nicholls, J., Yuen, K., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), p. 1319. , Apr 19; (2003) Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_05_06/en/, Geneva; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, , Apr 10; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/, Atlanta; (2003) First Data on Stability and Resistance of SARS Coronavirus Complied by Members of WHO Laboratory Network, , http://www.who.int/csr/sars/survival_2003_05_04/en/index.html, Geneva; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel corona-virus associated with severe acute respiratory synd (2003) N Engl J Med, , Apr 30; Updated interim surveillance case definition for severe acute respiratory syndro-me (SARS) - United States, April 29 (2003) Morbidity and Mortality Weekly Report (MMWR), 52. , April 29, 2003; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Chan, P.K.S., Chu, W.C.W., Kwan, Y.W., Li, A.M., Fok, T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children THE LANCET, , http://image.thelancet.com/extras/03let4127web.pdf; Fotz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; Wenzel, R.P., Hendley, J.O., Davies, J.A., Gwaltney J.M., Jr., Coronavirus infections in military recruits: Three-year study with coronavirus strains OC43 and 229E (1974) Am Rev Respir Dis, 109, pp. 621-624; Talbot, P.J., Cote, G., Arbour, N., Human coronavirus OC43 and 229E persistence in neural cell cultures and human brains Adv Exp Med Biol (Baskida); (2003) Severe Acute Respiratory Syndrome (SARS): Laboratory Diagnostic Tests, , http://www.who.int/csr/sars/diagnostictests/en/, Geneva; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Characterization of A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome, , www.sciencexpress.org/1May2003/Page2/10.1126/science, 1085952; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , Apr 11; Ahuja, A.T., Wong, J.K.T., Griffith, J.F., Antonio, G.E., Radiological Appearances of Recent Cases of Atypical Pneumonia in Hong Kong, , http://www.droid.cuhk.edu.hk; Ventilation with lower tidal volumes as compared with traditional tidal volumes for acute lung injury and the acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1301-1308; Seto, W.H., Tsang, D., Yung, R.W.H., Ching, T.Y., Ng, T.K., Ho, M., Ho, L.M., Peiris, J.S.M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) The Lancet, 361, pp. 1519-1520","Kökoǧlu, Ö.F.; KSU Medical Faculty, Department of Infection Diseases, Kahramanmaraş, Turkey",,,10165134,,SENDE,,"Turkish","SENDROM",Review,"Final",,Scopus,2-s2.0-0038374529
"Koley T.K.","57200009123;","Severe acute respiratory syndrome: A preliminary review",2003,"Journal of the Indian Medical Association","101","5",,"308","310",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141998454&partnerID=40&md5=8da6a4157ec10223e75f7c4ac4d4be9b","Hindu Rao Hospital, Delhi 110007, India","Koley, T.K., Hindu Rao Hospital, Delhi 110007, India","Severe acute respiratory syndrome (SARS) is a new disease of unknown aetiology and probably a new strain of coronavirus is thought to be responsible for the disease. After oginating from south-east China it has spread to several countries across the world. Patients of SARS suffer from fever with cough and dyspnoea. The virus spreads by droplet to nearby contacts and has high tendency to spread to the healthcare providers. Since the aetiology is not yet clear exact treatment is not yet defined and hence prevention is of utmost importance.","Coronavirus; Droplet spread; Human metapneumovirus; Severe acute respiratory syndrome (SARS)","antibiotic agent; azithromycin; cephalosporin derivative; clarithromycin; oseltamivir; quinoline derived antiinfective agent; ribavirin; steroid; China; Coronavirus; coughing; dyspnea; face mask; fever; hand washing; health care personnel; hospital hygiene; human; infection prevention; nebulization; respiratory tract disease; review; severe acute respiratory syndrome; strain identification; virus transmission; Anti-Infective Agents; Coronavirus; Disease Transmission, Horizontal; Humans; Severe Acute Respiratory Syndrome; Universal Precautions","http://www.cdc.gov/mmwr/preview/mmwrhtm1/mm5211a5.htm; http://www.who.int/csr/sarscountry/20030407/enhttp://www.who.int/csr/ sarscountry/20030326/en; Sapatnekar, S.M., Severe acute respiratory syndrome - Global alert (2003) J Assoc Physicians India, 51, pp. 343-344; http://www/cdc.gov/mmwr; (2003) Case Definition for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en, Geneva: WHO; www.who.int/en/; Sizun, J., Yu, M.W.N., Tablot, P.J., Survival of human coronavirus 229E and OC43 in suspension after drying on surfaces: A possible source of hospital acquired infections (2000) J Hosp Infect, 46, pp. 55-60; http://www.hc-sc.gc.ca/pphb-dgspsp/publication/ccdr-rmtc/03vo129/prev/ dr-sars0325.html; Zambon, M., Nicholson, K.G., Severe acute respiratory syndrome - May be a rehearsal for the next influenza pandemic (2003) BMJ, 326, pp. 669-670; Keneath, W.T., Pak, L.H., Gaik, C.O., (2003) A Cluster of Cases of Severe Acute Respiratory Syndrome in Hong Kong, , www.nejm.org, 31st March","Koley, T.K.; Hindu Rao Hospital, Delhi 110007, India",,,00195847,,JIMAA,"14575220","English","J. Indian Med. Assoc.",Review,"Final",,Scopus,2-s2.0-0141998454
"Gu J.","57198406969;","What is coronavirus?",2003,"Chinese Medical Journal","116","5",,"776","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038171303&partnerID=40&md5=2a29934d7ab2c0bcaaab292fe9037a8a",,"Gu, J.",[No abstract available],,"messenger RNA; nucleic acid; structural protein; virus protein; virus RNA; Coronavirus; electron microscopy; epidemic; genetic code; nonhuman; note; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; virion; virus envelope; virus genome; virus nucleocapsid; virus particle; world health organization",,,,,03666999,,CMDJA,,"English","Chin. Med. J.",Note,"Final",,Scopus,2-s2.0-0038171303
"Bhaskar G., Lodha R., Kabra S.K.","55313594100;7007019609;36488033400;","Severe acute respiratory syndrome (SARS)",2003,"Indian Journal of Pediatrics","70","5",,"401","405",,2,"10.1007/BF02723614","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037498566&doi=10.1007%2fBF02723614&partnerID=40&md5=490f5a5856d6108a2cacba1a3b49b579","Dept. of Pediatrics, AIIMS, New Delhi-110029, India","Bhaskar, G., Dept. of Pediatrics, AIIMS, New Delhi-110029, India; Lodha, R., Dept. of Pediatrics, AIIMS, New Delhi-110029, India; Kabra, S.K., Dept. of Pediatrics, AIIMS, New Delhi-110029, India","Several cases of life threatening respiratory disease with no identifiable cause were reported from Guangdong Province, China; these were soon followed by reports from many other countries. The disease was named as severe acute respiratory syndrome (SARS). A novel coronavirus, isolated from the respiratory secretions of patients, has been implicated in the causation of SARS. The modes of transmission include droplet spread, close contact, and Fomites; shedding of virus from respiratory tract is the primary mode of transmission. SARS clinically presents with high-grade fever, chills and rigors, myalgia, headache, cough with or without sputum production, dyspnea, and dizziness. Chest radiographs reveal unilateral or bilateral, predominantly peripheral, areas of consolidation progressing with in a short time of bilateral patchy consolidation. Preliminary reports suggest a milder illness in young children. The case definition of probable SARS cases, laboratory investigations and precautions for prevention of spread are discussed.","Children; Diagnosis; SARS","antibiotic agent; antivirus agent; cephalosporin derivative; clarithromycin; levofloxacin; ribavirin; steroid; article; bronchus secretion; child; chill; China; clinical feature; close person contact; Coronavirus; coughing; diagnostic value; disease severity; disease transmission; droplet spread; dyspnea; fever; fomes; headache; human; human relation; infection prevention; influenza; insect; laboratory diagnosis; myalgia; nose congestion; respiratory tract disease; rigor; SARS coronavirus; severe acute respiratory syndrome; sputum examination; thorax radiography; vertigo; virus infection; virus isolation; virus shedding; virus transmission","Cummulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_05_03/en/; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with Severe Acute Respiratory Syndrome (2003) N Engl J Med, 348, pp. 1947-1958; Drosten, C., Günther, S., Preiser, W., Van der Werf, S., Brodt, H., Becker, S., (2003) Identification of a Novel Coronavirus in Patients With Severe Acute Respiratory Syndrome, , www.nejm.org, Article published, on April 10; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., (2003) Identification of Severe Acute Respiratory Syndrome in Canada, , www.nejm.org, Article published, on March 31; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., (2003) A Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong, , www.nejm.org, Article published, on April 7; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., (2003) A Cluster of Cases of Severe Acute Respiratory Syndrome in Hong Kong, , www.nejm.org, Article published, on March 31; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Chan, P.K.S., Chu, W.C.W., Kwan, Y.W., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, , http://image.thelancet.com/extras/03let4127web.pdf, Published online April 29; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Prospective study of the clinical progression and viral load of SARS associated coronavirus pneumonia in a community outbreak Lancet, , http://www.who.int/csr/sars/prospectivestudy/en/index.html; Severe Acute Respiratory Syndrome: Updated Interim Care Definition, , http://www.cdc.gov/ncidod/sars/casedefinition.htm; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/; Management of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/management/en/; WHO Hospital Discharge and Follow-Up Policy for Patients Diagnosed With Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/discharge/en/; Hospital Infection Control Guidance for Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/infectioncontrol/en/; Updated Interim Domestic Infection Control Guidance in the Health Care and Community Setting for Patients With Suspected SARS, , http://www.cdc.gov/ncidod/sars/infectioncontrol.htm","Kabra, S.K.; Dept. of Pediatrics, AIIMS, New Delhi-110029, India; email: skkabra@hotmail.com",,"The Indian Journal of Pediatrics",00195456,,IJPEA,"12841401","English","Indian J. Pediatr.",Article,"Final",Open Access,Scopus,2-s2.0-0037498566
"Rahav G.","35482389900;","Severe Acute Respiratory Syndrome (SARS)",2003,"Harefuah","142","5",,"322","323+400",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038684431&partnerID=40&md5=25a940bd2125c2b12bb8733b80f72216","Chaim Sheba Medical Center, Tel Hashomer, Israel","Rahav, G., Chaim Sheba Medical Center, Tel Hashomer, Israel","On November 2002, 305 cases of atypical pneumonia appeared in southern China. In February 2003, cases were reported in Hong Kong and from there the disease spread to many other countries, mainly, China, Hong Kong, Singapore, Vietnam and Toronto in Canada. The syndrome was defined as Severe Acute Respiratory Syndrome SARS), and a person is suspected of having SARS if he/she became ill after November 1 2002, has a fever exceeding 38°C, has symptoms of a respiratory disease and was in a risk area or in close contact with a SARS patient within ten days prior the appearance of symptoms. The World Health Organization has received reports of 4,836 cases, of which 293 persons have died. Most were family members or medical staff treating the patient, persons who came into close and prolonged contact with the patient. The estimated incubation period is two days to one week. Symptoms of the disease include fever, shortness of breath and cough. Ten percent of patients afflicted with SARS require artificial breathing. The mortality rate is 6-7%. A novel coronavirus is associated with this outbreak, and the evidence indicates that this virus has an etiologic role in SARS. Infection is transmitted from person to person through direct or close contact with airborne droplets or personal objects of an infected person. Patients must be isolated and treated by contact and airborne isolation. Treatment consists of support care and artificial respiration when required. The use of anti-viral medications has not yet proven effective.","ARS; Corona; Epidemic; Pneumonia; Virus","antivirus agent; artificial ventilation; Canada; China; disease transmission; epidemic; epidemiological data; Hong Kong; human; mortality; severe acute respiratory syndrome; short survey; Singapore; symptomatology; Viet Nam; virus pneumonia; world health organization; Canada; China; Humans; Respiration, Artificial; SARS Virus; Severe Acute Respiratory Syndrome; Vietnam; World Health Organization","(2003) Acute Respiratory Syndrome in China - Update 3: Disease Outbreak Reported, , http://www.who.int/csr/sars/csr/don/2003_2_20/en, Geneva: World Health Organization; (2003) Severe Acute Respiratory Syndrome - Press Briefing, , http://www.who.int/csr/sars/csr/press/2003_4_1/en/print.html, Geneva: World Health Organization; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/case-definition/en, Geneva: World Health Organization; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/, Atlanta: Center for Disease Control and Prevention; (2003) Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/, Geneva: World Health Organization; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel Coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1947-1958; Drosten, C., Gunther, S., Preiser, W., Identification of a novel Coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , April 27 electronic publication; (2003) CDC Lab Sequences Genome of New Coronavirus, , CDC Media Relations. April 14; (2003) Canadian Scientists Cast Doubt on Cause of SARS, , ProMEDmail. 22 Apr; Hong, T., SARS: Detection of chlamydia-like and coronavirus-like agents in 7 fatal cases (2003) National Med J China, 83, pp. 632-636; Update: Outbreak of serve acute respiratory syndrome worldwide (2003) 2003 MMWR, 52, pp. 241-248","Rahav, G.; Chaim Sheba Medical Center, Tel Hashomer, Israel",,,00177768,,HAREA,"12803049","Hebrew","Harefuah",Short Survey,"Final",,Scopus,2-s2.0-0038684431
"Franco-Paredes C., Kuri-Morales P., Alvarez-Lucas C., Palacios-Zavala E., Nava-Frías M., Betancourt-Cravioto M., Santos-Preciado J.I., Tapia-Conyer R.","7003449834;6701453496;6603480604;6505540514;7801550424;12795674000;7005233243;7006147351;","Severe Acute Respiratory Syndrome: A global view of the epidemic [Síndrome Agudo Respiratorio Severo: Un panorama mundial de la epidemia]",2003,"Salud Publica de Mexico","45","3",,"211","220",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038167321&partnerID=40&md5=3a16d3c1f1f2196a77265065529666e0","Ctro. Nac. Salud Inf./Adol., Departamento de Salud, México, DF, Mexico; Direccion General de Epidemiologia, Departamento de Salud, México, DF, Mexico; Departamento de Salud, México, DF, Mexico; Ctro. Nac. Salud Inf./Adol., Consejo Nacional de Vacunacion, Francisco P. Miranda 177, 01600 México, DF, Mexico","Franco-Paredes, C., Ctro. Nac. Salud Inf./Adol., Departamento de Salud, México, DF, Mexico; Kuri-Morales, P., Direccion General de Epidemiologia, Departamento de Salud, México, DF, Mexico; Alvarez-Lucas, C., Direccion General de Epidemiologia, Departamento de Salud, México, DF, Mexico; Palacios-Zavala, E., Direccion General de Epidemiologia, Departamento de Salud, México, DF, Mexico; Nava-Frías, M., Ctro. Nac. Salud Inf./Adol., Departamento de Salud, México, DF, Mexico; Betancourt-Cravioto, M., Direccion General de Epidemiologia, Departamento de Salud, México, DF, Mexico; Santos-Preciado, J.I., Ctro. Nac. Salud Inf./Adol., Departamento de Salud, México, DF, Mexico, Ctro. Nac. Salud Inf./Adol., Consejo Nacional de Vacunacion, Francisco P. Miranda 177, 01600 México, DF, Mexico; Tapia-Conyer, R., Departamento de Salud, México, DF, Mexico","In early February 2003, the World Health Organization (WHO) began receiving reports of patients with a syndrome characterized by an atypical pneumonia with rapid progression to respiratory failure without an identified cause despite extensive diagnostic workups. Most of these reports pointed out that the outbreak started in Southern China, specifically in the Guandong Province. The initial outbreak in South East Asia has already spread to other Regions in Asia, Europe, North and South America, and South Africa. Many of these cases can be linked through chains of transmission to an index case from the Guandong Province who visited Hong Kong. Although the exact mode of transmission has not been clearly established, the etiology of this syndrome has already been identified. A novel Coronavirus has been identified by electron microscopy and molecular assays in multiple laboratories from respiratory specimens throughout the world. The syndrome has been defined as SARS (Severe Acute Respiratory Syndrome) by WHO, and is characterized by an incubation period between I and 10 days (average 5 days) and by a febrile phase that usually lasts approximately 3 days. During the respiratory phase that begins around day 3, patients start developing a dry cough,shortness of breath and hypoxemia. Mechanical ventilatory support is required in about 10 to 40% of cases and the case-fatality rate ranges between 3 and 16%. The laboratory findings in SARS cases include leukopenia, thrombocytopenia, and a rise in transaminases and lactic dehydrogenase levels. Treatment of SARS includes supportive measures and the empiric use of ribavirin. Respiratory isolation, use of respiratory masks, and compulsory hand hygiene constitute the principal preventive measures. The confirmation of a case can be performed at reference laboratories by serologic and molecular assays. From the onset of this epidemic Mexico established a surveillance system as well as clinical guidelines and recommendations for the identification, prevention of secondary spread, and medical management of suspicious and probable cases by health care personnel.","Coronavirus; Pneumonia, atypical; Respiratory insufficiency; Severe acute respiratory syndrome","aminotransferase; lactate dehydrogenase; ribavirin; acute respiratory tract disease; artificial ventilation; Asia; China; Coronavirus; coughing; disease course; dyspnea; electron microscopy; epidemic; Europe; face mask; fatality; fever; hand; health care personnel; Hong Kong; human; hypoxemia; incubation time; laboratory test; leukopenia; North America; patient care; personal hygiene; practice guideline; prophylaxis; respiratory failure; review; serology; severe acute respiratory syndrome; South Africa; South America; thrombocytopenia; virus pneumonia; virus transmission; world health organization; Canada; China; Disease Outbreaks; Hong Kong; Humans; Severe Acute Respiratory Syndrome; United States; World Health","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Drazen, J.M., Case clusters of the severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 6-7. , http://www.nejm.com(10.1056/NEJMe030062), versión electrónica (marzo 31 de 2003); CDC update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (13), pp. 269-272; Gerberding, J.L., Faster...but fast enough? Responding to the epidemic of severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 2030-2031. , http://www.nejm.com(10.1056/NEJMe030067), versión electrónica (abril 12 de 2003); CDC update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 529 (12), pp. 241-248; Beijing doctor alleges SARS cases cover-up in China (2003) Lancet, 361 (9366), p. 1357; Kahn, J., China discovers medical secrecy is expensive (2003) New York Times, , April 17; Falsey, A.R., Walsh, E.E., Novel Coronavirus and severe acute respiratory syndrome (2003) Lancet, 36 (9366), pp. 1312-1313. , http://image.thelancet.com/extras/03cm+8/neb.port, versión electrónica (abril 8 de 2003); (2003) Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome, , http://www.who.int/esr/sarscountry/2003_04_03/en/, 3 de abril; http://www.who.int/csr/sars/en/, Severe acute respiratory syndrome Homepage; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348 (20), pp. 1995-2005. , http://www.nejm.com(10.1056/NEJMoa030634), versión electrónica (marzo 31 de 2003); Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chang-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348 (20), pp. 1977-1985. , http://www.nejm.org(10.1056/NEJMoa030666), versión electrónica (marzo 31 de 2003); Preliminary clinical description of severe acute respiratory syndrome (2003) MMWR Morb Mortal Wkly Rep, 52 (12), pp. 255-256; Pearson, H., Mystery virus slow to yield its identity as patient numbers rise (2003) Nature, 422 (364), pp. 423-424. , http://www.nature.com(doi.10.1038/42324), versión electrónica, (marzo 27 de 2003); Bolvin, G., Abed, Y., Pelletier, G., Virological features and clinical manifestations associated with human metaneumovirus: A new Paramyxovirus responsible for acute respiratory-tract infections in all age groups (2002) J Infect Dis, 186, pp. 1330-1334; Stockton, J., Stephenson, I., Fleming, D., Zambon, M., Human metapneumovirus as a cause of community-acquired respiratory illness (2002) Emerg Infect Dis, 8 (9), p. 84; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., A novel Coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 1953-1966. , http://www.nejm.com(10.1056/NEJMoa030781), versión electrónica (abril 10 de 2003); Drosten, C., Gunther, C., Preiser, W., Van der Werf, S., Hans-Reinhard, B., Becker, S., Identification of a novel Coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 1967-1976. , http://www.nejm.com(10.10S6/NEJMoa030747/NEJMoa030747v2.pdf), versión electrónica, (abril 16 de 2003); Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325. , http://image.thelancet.com/extras/03art3477web.pdf, versión electrónica (abril 8 de 2003); Fouchler, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Bernadette, G., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423 (240), pp. 333-340. , http://www.nature.com(doi:10.1038/423240a), versión electrónica (mayo 15 de 2003); NaaNes, M., (2003) U.S. Immunization News. LSU Professor Hopes to Develop Vaccine Against SARS, , http://www.theadvocate.com, Baton Rouge Advocate. Versión electrónica (abril 24); (2003) Severe Acute Respiratory Syndrome (SARS)-Multi-Country Outbreak-Update 30. Status of Diagnostic Tests, Significance of ""Super Spreaders"", Situation in China, , http://www.who.int/csr/don2003_04_15/en/, Versión electrónica (abril 15); Update. Severe acute respiratory syndrome. United States, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (15), pp. 332-336; Global update on SARS cases (2003) Lancet, 361 (9366), p. 1289; Diagnosis/Evaluation of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/diagnosis.htm; Masur, H., Ezequiel, E., Lane, C.H., Severe acute respiratory syndrome. Providing care in the face of uncertainty (2003) JAMA, 289 (21), pp. 10-12; Cyranoski, D., Abbot, A., Apartment complex holds clues to pandemic potential of SARS (2003) Nature, pp. 3-4. , http://www.nature.com(doi:10.1038/423003a), versión electrónica (mayo 1 de 2003); (2003) Update. Severe Acute Respiratory Syndrome: United States, 52 (20), pp. 466-468. , May 21; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289 (21), pp. 1-8; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766. , http://image.thelancet.com/extras/03art4453web.pdf, version electrónica (mayo 17 de 2003); Hon, K.L., Leung, C.W., Cheng, W.T., Chan, P.K., Chu, W.C., Kwan, Y.W., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703. , http://image.thelancet.com/extras/03let4127web.pdf, version electrónica (abril 29 de 2003); Ordan, O., Rotem, R., Jaspers, I., Fiescher, E., Stress-responsive JNK mitogen-activated protein kinase mediates aspirin-induced suppression of B 16 melanoma acellular proliferation (2003) Br J Pharmacol, 138, pp. 1156-1162; McGilvray, I.D., Lu, Z., Dackiw, A.P., Marshall, J.C., Kapus, A., Murine hepatitis virus strain-3 induces the macrophage prothrombinase fgl-2 through p38 mitogen-activated protein-kinase activation (1998) J Biol Chem, 273 (48), pp. 1156-1162; Anand, K.Z., Washwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main-proteinase (3Clpro) structure: Basis for design of anti-SARS drugs (2003) Science, , http://www.sciencemag.org(doi.1126/science.1084658), versión electrónica (13 de mayo de 2003); Nicholss, J.M., Poon, L.L.M., Lu, K.C., Wai, F.N., Loung, C.Y., Hui, P.K., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778. , http://image.thelancet.com/extras/03art4347web.pdf, versión electrónica (16 de mayo de 2003); Ho, W., Guidelines on management of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1313-1314. , http://mage.thelancet.com/extras/03cmt89web.pdf, versión electrónica (8 de abril de 2003); Sing Tao, L.I.T., Buckley, T.A., Yap, F.H.Y., Sung, J.J.Y., Joynt, G.M., Severe acute respiratory syndrome (SARS) Infection Control (2003) Lancet, 361, pp. 1386-1387; (2003) Updated Interim Domestic Infection Control Guidance in the Health Care and Community Settings for Patients with Suspected SARS, , http://www.cdc.gov/sars, Versión electrónica (April 25); Cluster of severe acute respiratory syndrome cases among protected health care workers - Toronto, April 2003 (2003) Canada Communicable Disease Report, , http://www.hc-sc.gc.ca/pphb-dgspsp/publicat/ccdr-rmtc/03vol29/prev/dr- sars0515.html, versión electronica (18 de abril); Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of SARS in Hong Kong (2003) N Engl J Med, 348 (20), pp. 1986-1994. , http://www.nejm.com(10.1056)/NEJMoa030685), versión electrónica (16 de abril de 2003)","Santos-Preciado, J.I.; Ctro. Nac. Salud Inf./Adol., Consejo Nacional de Vacunacion, Francisco P. Miranda 177, 01600 México, DF, Mexico; email: jisantos@supernet.com.mx",,,00363634,,SPMXA,"12870423","Spanish","Salud Publica Mex.",Review,"Final",,Scopus,2-s2.0-0038167321
[No author name available],[No author id available],"Erratum: Outbreak of Severe Acute Respiratory (SARS) and Coronavirus Testing-United States, 2003 (Journal of the American Medical Association 52:14 (301))",2003,"Journal of the American Medical Association","289","17",,"2206","",,,"10.1001/jama.289.17.2206-a","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345023556&doi=10.1001%2fjama.289.17.2206-a&partnerID=40&md5=a9d23777779656b200f7f7510cf07f82",,"",[No abstract available],,"erratum; error; priority journal",,,,,00987484,,JAMAA,,"English","J. Am. Med. Assoc.",Erratum,"Final",Open Access,Scopus,2-s2.0-0345023556
"Feldt T., Oette M., Kroidl A., Göbels K., Richter J., Häussinger D.","6603715062;6602554073;57189487636;6602907508;55573636800;35376932100;","Severe acute respiratory syndrome (SARS) [SARS - Die fakten: Übertragungswege, diagnostik und umgang mit verdachtsfällen]",2003,"MMW-Fortschritte der Medizin","145","19",,"36","40",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037566812&partnerID=40&md5=2b8a9d546a305e62a0a70ddcc08d00f7","Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany","Feldt, T., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; Oette, M., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; Kroidl, A., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; Göbels, K., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; Richter, J., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; Häussinger, D., Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany","Severe Acute Respiratory Syndrome (SARS) is a new infectious disease that, in the short period between 1 February and 24 April 2003, has been diagnosed in more than 4000 patients. Its origin was traced to Guandong, a province in southeast China. The culprit organism was identified as a new coronavirus. The clinical presentation is unspecific and includes fever, respiratory symptoms, lymphopenia and pulmonary infiltrates on X-ray. Essential steps to prevent further dissemination of the virus are rapid identification, and treatment in an isolation unit. Despite all the international efforts and the rapid progress in the investigation of SARS coordinated by the World Health Organization (WHO), the epidemic has not yet been brought under control.","Clinical presentation; Coronavirus; Severe acute respiratory syndrome","China; clinical feature; Coronavirus; epidemic; fever; human; lung infiltrate; lymphocytopenia; respiratory tract infection; review; severe acute respiratory syndrome; symptomatology; thorax radiography; virus inhibition; world health organization; article; cause of death; cross-sectional study; differential diagnosis; disease transmission; dose response; drug administration; drug combination; electron microscopy; epidemic; infection control; intravenous drug administration; mortality; patient care; SARS coronavirus; severe acute respiratory syndrome; statistics; ultrastructure; hydrocortisone; ribavirin; Cause of Death; Cross-Sectional Studies; Diagnosis, Differential; Disease Outbreaks; Dose-Response Relationship, Drug; Drug Administration Schedule; Drug Therapy, Combination; Humans; Hydrocortisone; Infusions, Intravenous; Microscopy, Electron; Patient Isolation; Quarantine; Ribavirin; SARS Virus; Severe Acute Respiratory Syndrome",,"Oette, M.; Klin. fur Gastroenterologie, H./I., Universitatsklinikum Dusseldorf, Moorenstr. 5, D-40225 Düsseldorf, Germany; email: oette@med.uni-duesseldorf.de",,,14383276,,MFMEF,"12813976","German","MMW-Fortschr. Med.",Review,"Final",,Scopus,2-s2.0-0037566812
"Wang F.S., Zhou X.Z.","57199198552;9746028300;","Characterization of severe acute respiratory syndrome outbreak and identification of novel coronavirus",2003,"Zhonghua yi xue za zhi","83","9",,"705","707",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4444261229&partnerID=40&md5=ed4b77319e0887bbb92f0c8b2a372e6f",,"Wang, F.S.; Zhou, X.Z.",[No abstract available],,"China; editorial; epidemic; human; isolation and purification; SARS coronavirus; severe acute respiratory syndrome; virology; China; Disease Outbreaks; Humans; SARS Virus; Severe Acute Respiratory Syndrome",,"Wang, F.S.",,,03762491,,,"12913999","Chinese","Zhonghua Yi Xue Za Zhi",Editorial,"Final",,Scopus,2-s2.0-4444261229
"Ksiazek T.G., Erdman D., Goldsmith C.S., Zaki S.R., Peret T., Emery S., Tong S., Urbani C., Comer J.A., Lim W., Rollin P.E., Dowell S.F., Ling A.-E., Humphrey C.D., Shieh W.-J., Guarner J., Paddock C.D., Roca P., Fields B., DeRisi J., Yang J.-Y., Cox N., Hughes J.M., LeDuc J.W., Bellini W.J., Anderson L.J.","7101963789;7005380414;7102705107;7101848151;6602425443;7005789549;55783951400;7006097862;7103319132;7202378277;7101827480;7004419871;7102194546;7102630659;7102282113;7004588460;7006678201;7005448365;7101759332;7004334309;8080350000;57203054779;56750630700;7102688922;7005204113;55512739900;","A novel coronavirus associated with severe acute respiratory syndrome",2003,"New England Journal of Medicine","348","20",,"1953","1966",,2187,"10.1056/NEJMoa030781","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038076030&doi=10.1056%2fNEJMoa030781&partnerID=40&md5=2e8bd9c9f717f561e64a8a2e1d01627d","Special Pathogens Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Influenza Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Division of Bacterial Diseases, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Division of Rickettsial Diseases, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Office of the Director, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; World Health Organization, Hanoi, Viet Nam; Government Virus Unit, Queen Mary Hospital, Hong Kong, Hong Kong; Intl. Emerging Infect. Dis. Program, Bangkok, Thailand; Department of Pathology, Singapore General Hospital, Singapore, Singapore; Univ. of California, San Francisco, San Francisco, CA, United States; Center for Disease Control, Department of Health, Taipei, Taiwan","Ksiazek, T.G., Special Pathogens Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Erdman, D., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Goldsmith, C.S., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Zaki, S.R., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Peret, T., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Emery, S., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Tong, S., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Urbani, C., World Health Organization, Hanoi, Viet Nam; Comer, J.A., Special Pathogens Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Lim, W., Government Virus Unit, Queen Mary Hospital, Hong Kong, Hong Kong; Rollin, P.E., Special Pathogens Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Dowell, S.F., Intl. Emerging Infect. Dis. Program, Bangkok, Thailand; Ling, A.-E., Department of Pathology, Singapore General Hospital, Singapore, Singapore; Humphrey, C.D., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Shieh, W.-J., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Guarner, J., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Paddock, C.D., Infect. Disease Pathology Activity, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Roca, P., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Fields, B., Division of Bacterial Diseases, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; DeRisi, J., Univ. of California, San Francisco, San Francisco, CA, United States; Yang, J.-Y., Center for Disease Control, Department of Health, Taipei, Taiwan; Cox, N., Influenza Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Hughes, J.M., Office of the Director, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; LeDuc, J.W., Division of Rickettsial Diseases, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Bellini, W.J., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States; Anderson, L.J., Respiratory and Enteric Virus Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States","BACKGROUND: A worldwide outbreak of severe acute respiratory syndrome (SARS) has been associated with exposures originating from a single ill health care worker from Guangdong Province, China. We conducted studies to identify the etiologic agent of this outbreak. METHODS: We received clinical specimens from patients in seven countries and tested them, using virus-isolation techniques, electron-microscopical and histologic studies, and molecular and serologic assays, in an attempt to identify a wide range of potential pathogens. RESULTS: None of the previously described respiratory pathogens were consistently identified. However, a novel coronavirus was isolated from patients who met the case definition of SARS. Cytopathological features were noted in Vero E6 cells inoculated with a throatswab specimen. Electron-microscopical examination revealed ultrastructural features characteristic of coronaviruses. Immunohistochemical and immunofluorescence staining revealed reactivity with group I coronavirus polyclonal antibodies. Consensus coronavirus primers designed to amplify a fragment of the polymerase gene by reverse transcription-polymerase chain reaction (RT-PCR) were used to obtain a sequence that clearly identified the isolate as a unique coronavirus only distantly related to previously sequenced coronaviruses. With specific diagnostic RT-PCR primers we identified several identical nucleotide sequences in 12 patients from several locations, a finding consistent with a point-source outbreak. Indirect fluorescence antibody tests and enzyme-linked immunosorbent assays made with the new isolate have been used to demonstrate a virus-specific serologic response. This virus may never before have circulated in the U.S. population. CONCLUSIONS: A novel coronavirus is associated with this outbreak, and the evidence indicates that this virus has an etiologic role in SARS. Because of the death of Dr. Carlo Urbani, we propose that our first isolate be named the Urbani strain of SARS-associated coronavirus.",,"virus RNA; adult; article; cell ultrastructure; clinical article; Coronavirus; cytopathology; electron microscopy; enzyme linked immunosorbent assay; epidemic; female; gene amplification; gene sequence; geographic distribution; histopathology; human; immunofluorescence; immunohistochemistry; inoculation; male; nonhuman; nucleotide sequence; open reading frame; priority journal; reverse transcription polymerase chain reaction; sequence analysis; serology; severe acute respiratory syndrome; throat culture; United States; Vero cell; virus gene; virus isolation; virus pneumonia; Adult; Animals; Bronchoalveolar Lavage Fluid; Cell Line; Disease Outbreaks; Female; Humans; Lung; Male; Microscopy, Electron; Middle Aged; Oropharynx; Phylogeny; Polymerase Chain Reaction; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome","(2003) Acute Respiratory Syndrome in China - Update 3: Disease Outbreak Reported, , Geneva: World Health Organization, February; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-248; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1975-1983; Lee, N., Hui, D., Wu, A., A major out-break of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1984-1992; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1993-2003; Wulff, H., Lange, J.V., Indirect immunofluorescence for the diagnosis of Lassa fever infection (1975) Bull World Health Organization, 52, pp. 429-436; Ksiazek, T.G., West, C.P., Rollin, P.E., Jahrling, P.B., Peters, C.J., ELISA for the detection of antibodies to Ebola viruses (1999) J Infect Dis, 179 (SUPPL. 1), pp. S192-S198; Zaki, S., Greer, P.W., Coffield, L.M., Hantavirus pulmonary syndrome: Pathogenesis of an emerging infectious disease (1995) Am J Pathol, 146, pp. 552-579; Falsey, A.R., Erdman, D., Anderson, L.J., Walsh, E.E., Human metapneumovirus infections in young and elderly adults (2003) J Infect Dis, 87, pp. 785-790; Wang, D., Coscoy, L., Zylberberg, M., Microarray-based detection and genotyping of viral pathogens (2002) Proc Natl Acad Sci U S A, 99, pp. 15687-15692; Bohlander, S.K., Espinosa R. III, Le Beau, M.M., Rowley, J.D., Diaz, M.O., A method for the rapid sequence-independent amplification of microdissected chromosomal material (1992) Genomics, 13, pp. 1322-1324; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res, 22, pp. 4673-4680; Swofford, D.L., (1999) PAUP 4.0: Phylogenetic Analysis Using Parsimony (And Other Methods), , Sunderland, Mass.: Sinauer; Becker, W.B., McIntosh, K., Dees, J.H., Chanock, R.M., Morphogenesis of avian infectious bronchitis virus and a related human virus (strain 229E) (1967) J Virol, 1, pp. 1019-1027; Oshiro, L.S., Schieble, J.H., Lennette, E.H., Electron microscopic studies of coronavirus (1971) J Gen Virol, 12, pp. 161-168; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J Gen Virol, 79, pp. 715-718; Smolinski, M.S., Hamburg, M.A., Lederberg, J., (2003) Microbial Threats to Health: Emergence, Detection, and Response, , Washington, D.C.: National Academy Press; McIntosh, K., Kapikian, A.Z., Hardison, K.A., Hartley, J.W., Chanock, R.M., Antigenic relationships among the coronaviruses of man and between human and animal coronaviruses (1969) J Immunol, 102, pp. 1109-1118; Bradburne, A.F., Antigenic relationships amongst coronaviruses (1970) Arch Gesamte Virusforsch, 31, pp. 352-364; Bradburne, A.F., Somerset, B.A., Coronavirus antibody titres in sera of healthy adults and experimentally infected volunteers (1972) J Hyg (Lond), 70, pp. 235-244; Hazelton, P.R., Gelderblom, H.R., Electron microscopy for rapid diagnosis of infectious agents in emergent situations (2003) Emerg Infect Dis, 9, pp. 294-303; Johnson, K.M., Lange, J.V., Webb, P.A., Murphy, F.A., Isolation and partial characterisation of a new virus causing acute haemorrhagic fever in Zaire (1977) Lancet, 1, pp. 569-571; Chua, K.B., Bellini, W.J., Pota, P.A., Nipah virus: A recently emergent deadly paramyxovirus (2000) Science, 288, pp. 1432-1435; Murray, K., Selleck, P., Hooper, P., A morbillivirus that caused fatal disease in horses and humans (1995) Science, 268, pp. 94-97; Hofmann, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell culture (1988) J Clin Microbiol, 26, pp. 2235-2239; Bruckova, M., McIntosh, K., Kapikian, A.Z., Chanock, R.M., The adaption of two human coronavirus strains (OC38 and OC43) to growth in cell monolayers (1970) Proc Soc Exp Biol Med, 135, pp. 431-435; Patterson, S., Macnaughton, M.R., Replication of human respiratory coronavirus strain 229E in human macrophages (1982) J Gen Virol, 60, pp. 307-314; Luby, J.P., Clinton, R., Kurtz, S., Adaptation of human enteric coronavirus to growth in cell lines (1999) J Clin Virol, 12, pp. 43-51; Lavi, E., Wang, Q., Weiss, S.R., Gonatas, N.K., Syncytia formation induced by coronavirus infection is associated with fragmentation and rearrangement of the Golgi apparatus (1996) Virology, 221, pp. 325-334; Kusanagi, K., Kuwahara, H., Katoh, T., Isolation and serial propagation of porcine epidemic diarrhea virus in cell cultures and partial characterization of the isolate (1992) J Vet Med Sci, 54, pp. 313-318; Jacobse-Geels, H.E., Horzinek, M.C., Expression of feline infectious peritonitis coronavirus antigens on the surface of feline macrophage-like cells (1983) J Gen Virol, 64, pp. 1859-1866; Wong, K.T., Shieh, W.-J., Kumar, S., Nipah virus infection: Pathology and pathogenesis of an emerging paramyxoviral zoonosis (2002) Am J Pathol, 161, pp. 2153-2167; Guarner, J., Shieh, W.J., Dawson, J., Immunohistochemical and in situ hybridization studies of influenza A virus infection in human lungs (2000) Am J Clin Pathol, 114, pp. 227-233","Ksiazek, T.G.; Special Pathogens Branch, Natl. Center for Infectious Diseases, Centers for Dis. Control/Prevention, Atlanta, GA, United States",,,00284793,,NEJMA,"12690092","English","New Engl. J. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0038076030
"Drosten C., Günther S., Preiser W., Van der Werf S., Brodt H.-R., Becker S., Rabenau H., Panning M., Kolesnikova L., Fouchier R.A.M., Berger A., Burguière A.-M., Cinatl J., Eickmann M., Escriou N., Grywna K., Kramme S., Manuguerra J.-C., Müller S., Rickerts V., Stürmer M., Vieth S., Klenk H.-D., Osterhaus A.D.M.E., Schmitz H., Doerr H.W.","7003813990;7102978849;7004338253;7005851162;7003657741;55446677800;7004984201;6602216657;7005230287;7006060466;7402970321;6602262335;35247582600;55913596100;6603606703;6504374660;6507533537;7003610543;55457154400;6603369104;6603811497;6602565962;24432172000;55533604400;7203078610;7102740671;","Identification of a novel coronavirus in patients with severe acute respiratory syndrome",2003,"New England Journal of Medicine","348","20",,"1967","1976",,2039,"10.1056/NEJMoa030747","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038523806&doi=10.1056%2fNEJMoa030747&partnerID=40&md5=fcc25c6478d80cc7453f6f106569e7de","Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Medical Clinic III, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Institute of Virology, Philipps University, Marburg, Germany; Pasteur Institute, Molec. Genet. of Resp. Tract Viruses, National Influenza Center, Paris, France; Institute of Virology, Erasmus University, Rotterdam, Netherlands; Department of Virology, Bernhard Nocht Inst. for Trop. Med., Bernhard-Nocht Str. 74, 20359 Hamburg, Germany","Drosten, C., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany, Department of Virology, Bernhard Nocht Inst. for Trop. Med., Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; Günther, S., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Preiser, W., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Van der Werf, S., Pasteur Institute, Molec. Genet. of Resp. Tract Viruses, National Influenza Center, Paris, France; Brodt, H.-R., Medical Clinic III, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Becker, S., Institute of Virology, Philipps University, Marburg, Germany; Rabenau, H., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Panning, M., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Kolesnikova, L., Institute of Virology, Philipps University, Marburg, Germany; Fouchier, R.A.M., Institute of Virology, Erasmus University, Rotterdam, Netherlands; Berger, A., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Burguière, A.-M., Pasteur Institute, Molec. Genet. of Resp. Tract Viruses, National Influenza Center, Paris, France; Cinatl, J., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Eickmann, M., Institute of Virology, Philipps University, Marburg, Germany; Escriou, N., Pasteur Institute, Molec. Genet. of Resp. Tract Viruses, National Influenza Center, Paris, France; Grywna, K., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Kramme, S., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Manuguerra, J.-C., Pasteur Institute, Molec. Genet. of Resp. Tract Viruses, National Influenza Center, Paris, France; Müller, S., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Rickerts, V., Medical Clinic III, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Stürmer, M., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany; Vieth, S., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Klenk, H.-D., Institute of Virology, Philipps University, Marburg, Germany; Osterhaus, A.D.M.E., Institute of Virology, Erasmus University, Rotterdam, Netherlands; Schmitz, H., Bernhard Nocht Inst. for Trop. Med., Natl. Ref. Ctr. Trop. Infect. Dis., Hamburg, Germany; Doerr, H.W., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt am Main, Germany","BACKGROUND: The severe acute respiratory syndrome (SARS) has recently been identified as a new clinical entity. SARS is thought to be caused by an unknown infectious agent. METHODS: Clinical specimens from patients with SARS were searched for unknown viruses with the use of cell cultures and molecular techniques. RESULTS: A novel coronavirus was identified in patients with SARS. The virus was isolated in cell culture, and a sequence 300 nucleotides in length was obtained by a polymerase-chain-reaction (PCR)-based random-amplification procedure. Genetic characterization indicated that the virus is only distantly related to known coronaviruses (identical in 50 to 60 percent of the nucleotide sequence). On the basis of the obtained sequence, conventional and real-time PCR assays for specific and sensitive detection of the novel virus were established. Virus was detected in a variety of clinical specimens from patients with SARS but not in controls. High concentrations of viral RNA of up to 100 million molecules per milliliter were found in sputum. Viral RNA was also detected at extremely low concentrations in plasma during the acute phase and in feces during the late convalescent phase. Infected patients showed seroconversion on the Vero cells in which the virus was isolated. CONCLUSIONS: The novel coronavirus might have a role in causing SARS.",,"virus RNA; article; blood analysis; cell culture; controlled study; feces analysis; gene amplification; genetic analysis; human; human cell; major clinical study; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; RNA extraction; sequence analysis; sequence homology; seroconversion; severe acute respiratory syndrome; sputum analysis; Vero cell; virus gene; virus identification; virus isolation; virus pneumonia; Adult; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus; Disease Outbreaks; DNA, Viral; Female; Humans; Male; Molecular Sequence Data; Phylogeny; Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sequence Homology, Nucleic Acid; Severe Acute Respiratory Syndrome; Sputum","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Acute respiratory syndrome China, Hong Kong Special Administrative Region of China, and Viet Nam (2003) Wkly Epidemiol Rec, 78, pp. 73-74; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1975-1983; (2003) Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_04_04/en/, Geneva: World Health Organization; Drosten, C., Göttig, S., Schilling, S., Rapid detection and quantification of RNA of Ebola and Marburg viruses, Lassa virus, Crimean-Congo hemorrhagic fever virus, Rift Valley fever virus, dengue virus, and yellow fever virus by real-time reverse transcription-PCR (2002) J Clin Microbiol, 40, pp. 2323-2330; Felsenstein, J., (2000) PHYLIP (Phylogeny Inference Package), Version 3.57c, , http://evolution.genetics.washington.edu/phylip.html, Washington, D.C.: Department of Genetics, University of Washington; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Pes, 60, pp. 181-189; Günther, S., Emmerich, P., Laue, T., Imported lassa fever in Germany: Molecular characterization of a new Lassa virus strain (2000) Emerg Infect Dis, 6, pp. 466-476; Makela, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Cossart, Y., TTV a common virus, but pathogenic? (1998) Lancet, 352, p. 164; Kew, M.C., Kassianides, C., HGV: Hepatitis G virus or harmless G virus? (1996) Lancet, 348 (SUPPL. 2), pp. sII10; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1993-2003; Cho, K.O., Hoet, A.E., Loerch, S.C., Wittum, T.E., Saif, L.J., Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle (2001) Am J Vet Res, 62, pp. 1436-1441","Drosten, C.; Department of Virology, Bernhard Nocht Inst. for Trop. Med., Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; email: drosten@bni-hamburg.de",,,00284793,,NEJMA,"12690091","English","New Engl. J. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0038523806
"Sedlak B.J.","7003676763;","Biofirms intensifying efforts to combat SARS",2003,"Genetic Engineering News","23","10",,"1+48","49",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038044609&partnerID=40&md5=f5f1eb32f5500c21161e18d88fbc8e97",,"Sedlak, B.J.","With the gene sequence of the coronavirus responsible for severe acute respiratory syndrome determined, companies pursue various research avenues to identify effective preventive and therapeutic compounds.",,"anthrax vaccine; SARS coronavirus vaccine; unclassified drug; virus vaccine; acute respiratory tract disease; anthrax; article; biotechnology; Coronavirus; diagnostic test; drug efficacy; drug safety; drug screening; food and drug administration; gene mapping; gene sequence; human; immunotherapy; investment; nonhuman; SARS coronavirus; severe acute respiratory syndrome; Vero cell; virus genome; Anthrax; Coronavirus; SARS coronavirus",,,,"Mary Ann Liebert Inc.",02706377,,GENND,,"English","Genet. Eng. News",Article,"Final",,Scopus,2-s2.0-0038044609
"Holmes K.V.","7201657724;","SARS-associated coronavirus",2003,"New England Journal of Medicine","348","20",,"1948","1951",,181,"10.1056/NEJMp030078","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038326554&doi=10.1056%2fNEJMp030078&partnerID=40&md5=7dc74750f50da226b1d1e9ead1dbf02d","Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States","Holmes, K.V., Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States",[No abstract available],,"inactivated vaccine; messenger RNA; proteinase inhibitor; RNA directed DNA polymerase; virulence factor; virus glycoprotein; virus RNA; virus vaccine; common cold; convalescence; Coronavirus; drug targeting; gene deletion; gene insertion; genetic code; host pathogen interaction; human; immune response; infection control; infection risk; nonhuman; nucleotide sequence; priority journal; protein binding; review; serology; severe acute respiratory syndrome; virus genome; virus identification; virus morphology; virus nucleocapsid; virus pathogenesis; virus pneumonia; virus replication; Animal Diseases; Animals; Coronavirus; Disease Outbreaks; Genome, Viral; Humans; Mutation; SARS Virus; Severe Acute Respiratory Syndrome; Viral Vaccines; Virion; Virulence","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325","Holmes, K.V.; Univ. of Colorado Hlth. Sci. Center, Denver, CO, United States",,,00284793,,NEJMA,"12748314","English","New Engl. J. Med.",Review,"Final",Open Access,Scopus,2-s2.0-0038326554
"Poutanen S.M., Low D.E., Henry B., Finkelstein S., Rose D., Green K., Tellier R., Draker R., Adachi D., Ayers M., Chan A.K., Skowronski D.M., Salit I., Simor A.E., Slutsky A.S., Doyle P.W., Krajden M., Petric M., Brunham R.C., McGeer A.J.","6603932528;56870843600;7102689992;36122858400;16239941600;7402278221;7004847486;6506467065;56349416900;7006091897;37121626600;7004017482;7006508256;7102427049;35227997700;7202241662;7004178160;16216941800;7007047752;7006664445;","Identification of severe acute respiratory syndrome in Canada",2003,"New England Journal of Medicine","348","20",,"1995","2005",,866,"10.1056/NEJMoa030634","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0013165966&doi=10.1056%2fNEJMoa030634&partnerID=40&md5=0f29b2d64012c79e4b797bd0421a119c","Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada; Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada; Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada; Department of Medicine, Interdept. Div. of Critical Care, University of Toronto, Toronto, Ont., Canada; City of Toronto Pub. Hlth. Dept., Toronto, Ont., Canada; Scarborough Hospital, Toronto, Ont., Canada; Hospital for Sick Children, Toronto, Ont., Canada; Epidemiology Services, Brit. Columbia Ctr. for Dis. Control, Vancouver, BC, Canada; Laboratory Services, Brit. Columbia Ctr. for Dis. Control, Vancouver, BC, Canada; University Health Network, Toronto, Ont., Canada; S./Women's Coll. Hlth. Sci. Ctr., Toronto, Ont., Canada; St. Michael's Hospital, Toronto, Ont., Canada; Department of Laboratory Medicine, Vancouver Hosp./Hlth. Sci. Centre, University of British Columbia, Vancouver, BC, Canada; University of British Columbia, Center for Disease Control, Vancouver, BC, Canada","Poutanen, S.M., Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada, Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada; Low, D.E., Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada, Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada, Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada; Henry, B., City of Toronto Pub. Hlth. Dept., Toronto, Ont., Canada; Finkelstein, S., Scarborough Hospital, Toronto, Ont., Canada; Rose, D., Scarborough Hospital, Toronto, Ont., Canada; Green, K., Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada; Tellier, R., Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada, Hospital for Sick Children, Toronto, Ont., Canada; Draker, R., Hospital for Sick Children, Toronto, Ont., Canada; Adachi, D., Hospital for Sick Children, Toronto, Ont., Canada; Ayers, M., Hospital for Sick Children, Toronto, Ont., Canada; Chan, A.K., Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada; Skowronski, D.M., Epidemiology Services, Brit. Columbia Ctr. for Dis. Control, Vancouver, BC, Canada; Salit, I., Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada, University Health Network, Toronto, Ont., Canada; Simor, A.E., Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada, Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada, S./Women's Coll. Hlth. Sci. Ctr., Toronto, Ont., Canada; Slutsky, A.S., Department of Medicine, Interdept. Div. of Critical Care, University of Toronto, Toronto, Ont., Canada, St. Michael's Hospital, Toronto, Ont., Canada; Doyle, P.W., Department of Laboratory Medicine, Vancouver Hosp./Hlth. Sci. Centre, University of British Columbia, Vancouver, BC, Canada; Krajden, M., Laboratory Services, Brit. Columbia Ctr. for Dis. Control, Vancouver, BC, Canada; Petric, M., Laboratory Services, Brit. Columbia Ctr. for Dis. Control, Vancouver, BC, Canada; Brunham, R.C., University of British Columbia, Center for Disease Control, Vancouver, BC, Canada; McGeer, A.J., Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada, Department of Laboratory Medicine, University of Toronto, Toronto, Ont., Canada, Department of Medicine, Division of Infectious Diseases, University of Toronto, Toronto, Ont., Canada","BACKGROUND: Severe acute respiratory syndrome (SARS) is a condition of unknown cause that has recently been recognized in patients in Asia, North America, and Europe. This report summarizes the initial epidemiologic findings, clinical description, and diagnostic findings that followed the identification of SARS in Canada. METHODS: SARS was first identified in Canada in early March 2003. We collected epidemiologic, clinical, and diagnostic data from each of the first 10 cases prospectively as they were identified. Specimens from all cases were sent to local, provincial, national, and international laboratories for studies to identify an etiologic agent. RESULTS: The patients ranged from 24 to 78 years old; 60 percent were men. Transmission occurred only after close contact. The most common presenting symptoms were fever (in 100 percent of cases) and malaise (in 70 percent), followed by nonproductive cough (in 100 percent) and dyspnea (in 80 percent) associated with infiltrates on chest radiography (in 100 percent). Lymphopenia (in 89 percent of those for whom data were available), elevated lactate dehydrogenase levels (in 80 percent), elevated aspartate aminotransferase levels (in 78 percent), and elevated creatinine kinase levels (in 56 percent) were common. Empirical therapy most commonly included antibiotics, oseltamivir, and intravenous ribavirin. Mechanical ventilation was required in five patients. Three patients died, and five have had clinical improvement. The results of laboratory investigations were negative or not clinically significant except for the amplification of human metapneumovirus from respiratory specimens from five of nine patients and the isolation and amplification of a novel coronavirus from five of nine patients. In four cases both pathogens were isolated. CONCLUSIONS: SARS is a condition associated with substantial morbidity and mortality. It appears to be of viral origin, with patterns suggesting droplet or contact transmission. The role of human metapneumovirus, a novel coronavirus, or both requires further investigation.",,"antibiotic agent; aspartate aminotransferase; creatine kinase; lactate dehydrogenase; oseltamivir; ribavirin; adult; aged; article; artificial ventilation; Canada; cell infiltration; clinical article; clinical feature; Coronavirus; coughing; diagnostic test; disease course; disease transmission; dyspnea; epidemic; epidemiological data; female; fever; histopathology; human; human tissue; malaise; male; Metapneumovirus; mortality; priority journal; severe acute respiratory syndrome; thorax radiography; virus gene; virus isolation; virus pneumonia; Adult; Aged; Canada; Chronology; Contact Tracing; Cough; Disease Outbreaks; Disease Progression; Dyspnea; Family Health; Female; Fever; Humans; Lung; Male; Middle Aged; Pedigree; Severe Acute Respiratory Syndrome","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-248; Borio, L., Inglesby, T., Peters, C.J., Hemorrhagic fever viruses as biological weapons: Medical and public health management (2002) JAMA, 287, pp. 2391-2405; Peret, T.C., Boivin, G., Li, Y., Characterization of human metapneumoviruses isolated from patients in North America (2002) J Infect Dis, 185, pp. 1660-1663; Heymann, D.L., Rodier, G.R., Hot spots in a wired world: WHO surveillance of emerging and re-emerging infectious diseases (2001) Lancet Infect Dis, 1, pp. 345-353; Van den Hoogen, B.G., De Jong, J.C., Groen, J., A newly discovered human pneumovirus isolated from young children with respiratory tract disease (2001) Nat Med, 7, pp. 719-724; Boivin, G., Abed, Y., Pelletier, G., Virological features and clinical manifestations associated with human metapneumovirus: A new paramyxovirus responsible for acute respiratory-tract infections in all age groups (2002) J Infect Dis, 186, pp. 1330-1334; Stockton, J., Stephenson, I., Fleming, D., Zambon, M., Human metapneumovirus as a cause of community-acquired respiratory illness (2002) Emerg Infect Dis, 8, pp. 897-901; Nissen, M.D., Siebert, D.J., Mackay, I.M., Sloots, T.P., Withers, S.J., Evidence of human metapneumovirus in Australian children (2002) Med J Aust, 176, p. 188; Vabret, A., Brouard, J., Petitjean, J., Eugene-Ruellan, G., Freymuth, F., Infections à coronavirus humains: Importance et diagnostic (1998) Presse Med, 27, pp. 1813-1817; Truyen, U., Parrish, C.R., Harder, T.C., Kaaden, O.R., There is nothing permanent except change: The emergence of new virus diseases (1995) Vet Microbiol, 43, pp. 103-122; Falsey, A.R., McCann, R.M., Hall, W.J., The ""common cold"" in frail older persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J Am Geriatr Soc, 45, pp. 706-711; Farr, B.M., Bartlett, C.L., Wadsworth, J., Miller, D.L., Risk factors for community-acquired pneumonia diagnosed upon hospital admission (2000) Respir Med, 94, pp. 954-963; Greensill, J., McNamara, P.S., Dove, W., Flanagan, B., Smyth, R.L., Hart, C.A., Human metapneumovirus in severe respiratory syncytial virus bronchiolitis (2003) Emerg Infect Dis, 9, pp. 372-375; Crotty, S., Maag, D., Arnold, J.J., The broad-spectrum antiviral ribonucleoside ribavirin is an RNA virus mutagen (2000) Nat Med, 6, pp. 1375-1379. , Erratum, Nat Med 2001;7: 255; Smith, D.W., Frankel, L.R., Mathers, L.H., Tang, A.T.S., Ariagno, R.L., Prober, C.G., A controlled trial ofaerosolized ribavirin in infants receiving mechanical ventilation for severe respiratory syncytial virus infection (1991) N Engl J Med, 325, pp. 24-29; Weiss, R.C., Oostrom-Ram, T., Inhibitory effects of ribavirin alone or combined with human alfa interferon on feline infectious peritonitis virus replication in vitro (1989) Vet Microbiol, 20, pp. 255-265; Sidwell, R.W., Huffman, J.H., Call, E.W., Warren, R.P., Radov, L.A., Murray, R.J., Inhibition of murine hepatitis virus infections by the immunomodulator 2,3,5,6,7,8-hexahydro-2-phenyl-8,8-dimethoxy-imidazo[1,2a]pyridine (PR-879-317A) (1987) Antimicrob Agents Chemother, 31, pp. 1130-1134; Bernard, G.R., Artigas, A., Brigham, K.L., The American-European Consensus Conference on ARDS: Definitions, mechanisms, relevant outcomes, and clinical trial coordination (1994) Am J Respir Crit Care Med, 149, pp. 818-824; Ware, L.B., Matthay, M.A., The acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1334-1349; Ventilation with lower tidal volumes as compared with traditional tidal volumes for acute lung injury and the acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1301-1308; Slutsky, A.S., Tremblay, L.N., Multiple system organ failure: Is mechanical ventilation a contributing factor? (1998) Am J Respir Crit Care Med, 157, pp. 1721-1725; Imai, Y., Parodo, J., Kajikawa, O., Injurious mechanical ventilation and end-organ epithelial cell apoptosis and organ dysfunction in an experimental model (2003) JAMA, 289, pp. 2104-2120","Poutanen, S.M.; Toronto Medical Laboratories, Mount Sinai Hospital, Department of Microbiology, 600 University Ave., Toronto, Ont. M5G 1X5, Canada",,,00284793,,NEJMA,"12671061","English","New Engl. J. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0013165966
"Rickerts V., Wolf T., Rottmann C., Preiser W., Drosten C., Jakobi V., Leong H.N., Brodt H.R.","6603369104;56425194000;7801369991;7004338253;7003813990;56802466800;7005127973;7003657741;","Clinical presentation and management of the severe acute respiratory syndrome (SARS) [Klinik und behandlung des schweren akuten respiratorischen syndroms]",2003,"Deutsche Medizinische Wochenschrift","128","20",,"1109","1114",,11,"10.1055/s-2003-39253","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038276072&doi=10.1055%2fs-2003-39253&partnerID=40&md5=8bf0c5c50742604092e5e662ebd9a8e2","Medizinische Klinik III/Infektiologie, Universitätsklinik Frankfurt, Germany; Institut für Virologie, Universitätsklinik Frankfurt, Germany; Institut für diagnostische und interventionelle Radiologie, Universitätsklinik Frankfurt, Germany; Bernhard Nocht Institut für Tropenmedizin, Hamburg, Germany; Singapore General Hospital, Department of Internal Medicine, Germany","Rickerts, V., Medizinische Klinik III/Infektiologie, Universitätsklinik Frankfurt, Germany; Wolf, T., Medizinische Klinik III/Infektiologie, Universitätsklinik Frankfurt, Germany; Rottmann, C., Medizinische Klinik III/Infektiologie, Universitätsklinik Frankfurt, Germany; Preiser, W., Institut für Virologie, Universitätsklinik Frankfurt, Germany; Drosten, C., Bernhard Nocht Institut für Tropenmedizin, Hamburg, Germany; Jakobi, V., Institut für diagnostische und interventionelle Radiologie, Universitätsklinik Frankfurt, Germany; Leong, H.N., Singapore General Hospital, Department of Internal Medicine, Germany; Brodt, H.R., Medizinische Klinik III/Infektiologie, Universitätsklinik Frankfurt, Germany","Background and objective: In February 2003, a newly emerged infectious disease was described, the etiology of which was initially unknown. It is referred to under the term SARS. In the beginning, it spread in some regions South-East Asia. Import infections appeared in many other parts of the world. Based on the first cases in Germany, this report illustrates the clinical appearance, the diagnostic results and the management of this new disease. Patients and methods: We analysed the data of two patients with SARS and one suspected patient. The results of radiological, laboratory, micobiological and physical examinations were abstracted and compared with the data obtained in other regions. Results: Two of the three patients under our care developed SARS disease. This is characterised by fever of sudden onset lasting for more than 5 days, rapidly changing consolidations in chest x-ray not affected by antimicrobial therapy, leuco-, lympho- as well as thrombopenia with a compromised pulmonary function later in the course. Close contacts with SAPS patients does not regularly result in full development of the disease. Secretion of a coronavirus could be detected in respiratory samples during the febrile phase and in feces for a longer time. It is still an open question whether bedrest and antibiotic prophylaxis by themselves or an additional administration of ribavirin and corticosteroids can improve the outcome. Conclusion: SARS is a new and highly contagious lung disease. It is crucial to be able to recognize the clinical appearance and the diagnostic features of this disease at an early stage, in order to prevent a further dissemination of the disease.",,"antibiotic agent; corticosteroid; doxycycline; erythromycin; imipenem; levofloxacin; oseltamivir; paracetamol; ribavirin; antiinfective agent; antibiotic therapy; article; bed rest; case report; clinical examination; clinical feature; Coronavirus; disease course; feces; fever; human; infection control; laboratory diagnosis; leukopenia; lung function; lymphocytopenia; microbiology; pneumonia; prophylaxis; sampling; severe acute respiratory syndrome; thorax radiography; thrombocytopenia; treatment outcome; virus detection; virus transmission; adult; computer assisted tomography; coughing; differential diagnosis; drug combination; ethnology; female; fever; Germany; headache; isolation and purification; lung lavage; male; middle aged; patient care; pregnancy; pregnancy complication; severe acute respiratory syndrome; Singapore; sputum; travel; virology; Adult; Anti-Infective Agents; Bed Rest; Bronchoalveolar Lavage Fluid; Coronavirus; Cough; Diagnosis, Differential; Drug Therapy, Combination; Female; Fever; Germany; Headache; Humans; Male; Middle Aged; Patient Isolation; Pregnancy; Pregnancy Complications, Infectious; Radiography, Thoracic; Severe Acute Respiratory Syndrome; Singapore; Sputum; Tomography, X-Ray Computed; Travel","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 12, pp. 81-88; WHO recommends measures for persons undertaking international travel from areas affected by severe acute respiratory syndrome (2003) Wkly Epidemiol Rec, 14, pp. 97-99; Acute respiratory syndrome China, Hong Kong Special Administrative Region of China, and Viet Nam (2003) Wkly Epidemiol Rec, 11, pp. 73-74; WHO multicentre collaborative networks for severe acute respiratory syndrome (SARS) diagnosis (2003) Wkly Epidemiol Rec, 15, pp. 121-122; Drosten, C., Günther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) NEJM 2003, , http://www.nejm.org/earlyrelease/sars.asp; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) NEJM 2003, , http://www.nejm.org/earlyrelease/sars.asp; Tsang, K.W., Ho, P.L., Ooi, G.C., A Cluster of cases of severe accute respiratory syndrome in Hong Kong (2003) NEJM 2003, , http://www.nejm.org/earlyrelease/sars.asp; Seto, W.H., Tsang, D., Yung, R.W.H., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520","Brodt, H.R.; Med. Klinik III/Infektiologie, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany; email: reinhard@brodt.net",,,00120472,,DMWOA,"12748900","German","Dtsch. Med. Wochenschr.",Article,"Final",,Scopus,2-s2.0-0038276072
"Stöhr K.","7004827453;","A multicentre collaboration to investigate the cause of severe acute respiratory syndrome",2003,"Lancet","361","9370",,"1730","1733",,125,"10.1016/S0140-6736(03)13376-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037509844&doi=10.1016%2fS0140-6736%2803%2913376-4&partnerID=40&md5=a7de513a2d3e5d47beb428d5caf75c52","Communicable Diseases, World Health Organization, CH-1211 Geneva 27, Switzerland","Stöhr, K., Communicable Diseases, World Health Organization, CH-1211 Geneva 27, Switzerland","Severe acute respiratory syndrome is a new disease in human beings, first recognised in late February, 2003, in Hanoi, Vietnam. The severity of the disease, combined with its rapid spread along international air-travel routes, prompted WHO to set up a network of scientists from 11 laboratories around the world to try to identify the causal agent and develop a diagnostic test. The network unites laboratories with different methods and capacities to rapidly fulfil all postulates for establishing a virus as the cause of a disease. Results are shared in real time via a secure website, on which microscopy pictures, protocols for testing, and PCR primer sequences are also posted. Findings are discussed in daily teleconferences. Progress is further facilitated through sharing between laboratories of samples and test materials. The network has identified a new coronavirus, consistently detected in samples of SARS patients from several countries, and conclusively named it as the causative agent of SARS; the strain is unlike any other known member of the genus Coronavirus. Three diagnostic tests are now available, but all have limitations.",,"acute respiratory tract disease; aviation; Coronavirus; diagnostic test; disease severity; electron microscopy; enzyme linked immunosorbent assay; human; image analysis; information processing; Internet; laboratory; polymerase chain reaction; priority journal; review; severe acute respiratory syndrome; telecommunication; virus pneumonia; virus strain; world health organization","Acute respiratory syndrome China, Hong Kong Special Administrative Region of China, and Viet Nam (2003) Wkly Epidemiol Rec, 78, pp. 73-74; Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/en/; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Outbreak of severe acute respiratory syndrome: Worldwide, 2003 (2003) Morb Mortal Wkly Rep, 52, pp. 226-228; http://www.who.int/csr/sars/guidelines/en/, Severe acute respiratory syndrome (SARS): WHO guidelines/recommendations/descriptions; Situation Updates: Severe Acute Respiratory Syndrome, , http://www.who.int/csr/sarsarchive/en/; Lee, N., Hui, D., Wu, A., A Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong, , http://content.nejm.org/cgi/reprint/NEJMoa030685v2.pdf; World Health Organization Issues Emergency Travel Advisory, , http://www.who.int/csr/sarsarchive/2003_03_15/en/; WHO Collaborative Multi-centre Research Project on Severe Acute Rspiratory Syndrome (SARS) Diagnosis, , http://www.who.int/csr/sars/project/en/; Acute respiratory syndrome, China (2003) Wkly Epidemiol Rec, 78, p. 41; Acute Respiratory Syndrome in China: Update 2, , http://www.who.int/csr/don/2003_02_14/en/; Influenza A(H5N1), Hong Kong, Special Administrative Region of China (2003) Wkly Epidemiol Rec, 78, pp. 49-50; WHO Issues a Global Alert About Cases of Atypical Pneumonia: Cases of Severe Respiratory Illness may Spread to Hospital Staff, , http://www.who.int/csr/sarsarchive/2003_03_12/en/; Claas, E.C.J., Osterhaus, A.D.M.E., Van Beek, R., Human influena A H5N2 virus related to a highly pathogenic avian influenza virus (1998) Lancet, 351, pp. 472-477; Chua, K.B., Bellini, W.J., Rota, P.A., Nipah virus: A recently emergent deadly paramyxovirus (2000) Science, 288, pp. 1432-1435; Goh, K.J., Tan, C.T., Chew, N.K., Clinical features of Nipah virus encephalitis among pig farmers in Malaysia (2000) N Engl J Med, 342, pp. 1229-1235; McCormack, J.G., Allworth, A.M., Emerging viral infections in Australia (2002) Med J Aust, 177, pp. 45-49; Wells, R.M., Young, J., Williams, R.J., Hantavirus transmission in the United States (1997) Emerg Infect Dis, 3, pp. 361-365; Feng, P., Escherichia coli serotype O157:H7: Novel vehicles of infection and emergence of phenotypic variants (1995) Emerg Infect Dis, 1, pp. 47-52; Almond, J., Patttison, J., Human BSE (1997) Nature, 389, pp. 437-438; Gubler, D.J., Human arbovirus infections worldwide (2001) Ann N Y Acad Sci, 951, pp. 13-24; Petersen, L.R., Toehrig, J.T., West Nile virus: A reemerging global pathogen (2001) Emerg Infect Dis, 7, pp. 611-614; Meningococcal disease, serogroup W135, Burkina Faso (2002) Wkly Epidemiol Rec, 77, pp. 152-155; Arthropod-borne and rodent-borne viral diseases: Report of a WHO Scientific Group (1985) World Health Organ Tech Rep Ser, 719, pp. 1-116; Outbreak of Ebola haemorrhagic fever, Uganda, August 2000-January 2001 (2001) Wkly Epidemiol Rec, 76, pp. 41-48; Report of an international commission: Ebola haemorrhagic fever in Zaire, 1976 (1978) Bull World Health Organ, 56, pp. 271-293; Heymann, D.L., Barakamfitiye, D., Szczeniowski, M., Ebola hemorrhagic fever: Lessons from Kikwit, Democratic Republic of the Congo (1999) J Infect Dis, 179 (SUPPL. 1), pp. 283-S286; Rivers, T.M., Viruses and Koch's postulates (1937) J Bacteriol, 33, pp. 1-12; Van den Hoogen, B.G., De Jong, J.C., Groen, J., A newly discovered human pneumovirus isolated from young children with respiratory tract disease (2001) Nat Med, 7, pp. 719-724; Enserink, M., Vogel, G., Deferring competition, global net closes in on SARS (2003) Science, 300, pp. 224-225; Ksiazek, T.G., Erdman, D., Goldsmith, C., A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome, , http://content.nejm.org/cgi/reprint/NEJMoa030781v3.pdf; Drosten, C., Günther, S., Preiser, W., Identification of a Novel Coronavirus in Patients with Severe Acute Respiratory Syndrome, , http://content.nejm.org/cgi/reprint/NEJMoa030747v2.pdf; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325","Stöhr, K.; Communicable Diseases, World Health Organization, CH-1211 Geneva 27, Switzerland; email: SARSetiology@who.int",,"Elsevier Limited",01406736,,LANCA,"12767752","English","Lancet",Review,"Final",Open Access,Scopus,2-s2.0-0037509844
"Yarnell A.","7004130265;","In search of SARS therapeutics",2003,"Chemical and Engineering News","81","20",,"13","",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038628858&partnerID=40&md5=4430285fbf53a1f0c508ac7adb28fbce",,"Yarnell, A.","A study is performed on search of SARS therapeutics. Many viruses, including the coronavirus that causes SARS, rely on protein-cleaving enzyme called main proteinase to activate replication. It is reported that X-ray study of enzyme from related viruses suggests drug design strategy.",,"Biochemistry; Crystal structure; Enzymes; Viruses; Drug design; Diseases",,,,,00092347,,CENEA,,"English","Chem Eng News",Note,"Final",,Scopus,2-s2.0-0038628858
"Ruan Y., Wei C.L., Ee L.A., Vega V.B., Thoreau H., Yun S.T.S., Chia J.-M., Ng P., Chiu K.P., Lim L., Tao Z., Peng C.K., Ean L.O.L., Lee N.M., Sin L.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.","7103091069;7401658175;6603085939;7003826492;6506053008;24173964900;35261438500;7201376967;7202988047;7401517149;36892096000;57199068132;6505539970;7402721983;57190075276;7201477950;7004336104;7006838132;7201512253;7202240109;","Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection",2003,"Lancet","361","9371",,"1779","1785",,326,"10.1016/S0140-6736(03)13414-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037686664&doi=10.1016%2fS0140-6736%2803%2913414-9&partnerID=40&md5=6daf8114bcec5cd66a02077649cab5bf","Genome Institute of Singapore, Singapore, Singapore; Virology Section, Department of Pathology, Singapore General Hospital, Singapore, Singapore; Department of Microbiology, Electron Microscopy Unit, National University of Singapore, Singapore, Singapore; Tan Tock Seng Hospital, Singapore, Singapore; Singapore Science Park II, 1 Science Park Road 05-01, Singapore 117528, Singapore","Ruan, Y., Genome Institute of Singapore, Singapore, Singapore; Wei, C.L., Genome Institute of Singapore, Singapore, Singapore; Ee, L.A., Virology Section, Department of Pathology, Singapore General Hospital, Singapore, Singapore; Vega, V.B., Genome Institute of Singapore, Singapore, Singapore; Thoreau, H., Genome Institute of Singapore, Singapore, Singapore; Yun, S.T.S., Virology Section, Department of Pathology, Singapore General Hospital, Singapore, Singapore; Chia, J.-M., Genome Institute of Singapore, Singapore, Singapore; Ng, P., Genome Institute of Singapore, Singapore, Singapore; Chiu, K.P., Genome Institute of Singapore, Singapore, Singapore; Lim, L., Genome Institute of Singapore, Singapore, Singapore; Tao, Z., Genome Institute of Singapore, Singapore, Singapore; Peng, C.K., Virology Section, Department of Pathology, Singapore General Hospital, Singapore, Singapore; Ean, L.O.L., Virology Section, Department of Pathology, Singapore General Hospital, Singapore, Singapore; Lee, N.M., Department of Microbiology, Electron Microscopy Unit, National University of Singapore, Singapore, Singapore; Sin, L.Y., Tan Tock Seng Hospital, Singapore, Singapore; Ng, L.F.P., Genome Institute of Singapore, Singapore, Singapore; Ren, E.C., Genome Institute of Singapore, Singapore, Singapore; Stanton, L.W., Genome Institute of Singapore, Singapore, Singapore; Long, P.M., Genome Institute of Singapore, Singapore, Singapore; Liu, E.T., Genome Institute of Singapore, Singapore, Singapore, Singapore Science Park II, 1 Science Park Road 05-01, Singapore 117528, Singapore","Background: The cause of severe acute respiratory syndrome (SARS) has been identified as a new coronavirus. Whole genome sequence analysis of various isolates might provide an indication of potential strain differences of this new virus. Moreover, mutation analysis will help to develop effective vaccines. Methods: We sequenced the entire SARS viral genome of cultured isolates from the index case (SIN2500) presenting in Singapore, from three primary contacts (SIN2774, SIN2748, and SIN2677), and one secondary contact (SIN2679). These sequences were compared with the isolates from Canada (TOR2), Hong Kong (CUHK-W1 and HKU39849), Hanoi (URBANI), Guangzhou (GZ01), and Beijing (BJ01, BJ02, BJ03, BJ04). Findings: We identified 129 sequence variations among the 14 isolates, with 16 recurrent variant sequences. Common variant sequences at four loci define two distinct genotypes of the SARS virus. One genotype was linked with infections originating in Hotel M in Hong Kong, the second contained isolates from Hong Kong, Guangzhou, and Beijing with no association with Hotel M (p<0.0001). Moreover, other common sequence variants further distinguished the geographical origins of the isolates, especially between Singapore and Beijing. Interpretation: Despite the recent onset of the SARS epidemic, genetic signatures are emerging that partition the worldwide SARS viral isolates into groups on the basis of contact source history and geography. These signatures can be used to trace sources of infection. In addition, a common variant associated with a non-conservative aminoacid change in the S1 region of the spike protein, suggests that immunological pressures might be starting to influence the evolution of the SARS virus in human populations.",,"article; Coronavirus; epidemic; gene sequence; genotype; geography; human; immunology; nonhuman; nucleotide sequence; priority journal; SARS coronavirus; virus isolation; virus mutation","Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_04_24/en/; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , published online April 10, 10.1056/NEJMoa030781; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, , published online April 10, DOI: 10.1056/NEJMoa030747; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J Virol, 74, pp. 1393-1406; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J Virol, 73, pp. 7607-7618; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J Virol, 73, pp. 7752-7760; Bergmann, C.C., Yao, Q., Lin, M., Stohlman, S.A., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response (1996) J Gen Virol, 77, pp. 315-325; Gomez, N., Carrillo, C., Salinas, J., Parra, F., Borca M., V., Escribano, J.M., Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants (1998) Virology, 249, pp. 352-358; Jackwood, M.W., Hilt, D.A., Production and immunogenicity of multiple antigenic peptide (MAP) constructs derived from the S1 glycoprotein of infectious bronchitis virus (IBV) (1995) Adv Exp Med Biol, 308, pp. 213-219; Ndifuna, A., Waters A., K., Zhou, M., Collison, E.W., Recombinant nucleocapsid protein is potentially an inexpensive, effective serodiagnostic reagent for IBV (1998) J Virol Methods, 70, pp. 37-44; Callenbaut, P., Enjuanes, L., Pensaert, M., An adenovirus recombinant expression the spike glycoprotein of porcine respiratory coronavirus is immunogenic in swine (1998) J Gen Virol, 77, pp. 309-313; Homberger, F.R., Nucleotide sequence comparison of the membrane protein genes of three enterotropic strains of mouse hepatitis virus (1994) Virus Res, 31, pp. 49-56; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-88. , http://www.who.int/wer/pdf/2003/wer7812.pdf; Update: Outbreak of severe acute respiratory syndrome, worldwide (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 269-272. , http://www.cdc.gov/mmwr/preview/mmwrhtml/mm5212a1.htm; http://www.who.int/cdsdiagnostics; http://www.bcgsc.bc.ca; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL-W - Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res, 22, pp. 4673-4680; Gish, W., WU-BLAST (1996-2003), , http://blast.wustl.edu; Swofford, D.L., (2003) PAUP. Phylogenetic Analysis Using Parsimony (and Other Methods). Version 4, , Sunderland, Massachusetts: Sinauer Associates; Marra, M.A., Jones, S.J.M., Astell, C.R., (2003) The Genome Sequence of the SARS-Associated Coronavirus, , http://www.sciencemag.org/cgi/rapidpdf/1085953v1.pdf, Published online May 1; Rowe, C.L., Fleming, J.O., Nathan, M.J., Sgro, J.Y., Palmenberg, A.C., Baker, S.C., Generation of coronavirus spike deletion variants by high-frequency recombination at regions of predicted RNA secondary structure (1997) J Virol, 71, pp. 6183-6190; Lee, C.W., Jackwood, M.W., Origin and evolution of Georgia 98 (GA98), a new serotype of avian infectious bronchitis virus (2001) Virus Res, 80, pp. 33-39; Bush, R.M., Smith, C.B., Cox, N.J., Fitch, W.M., Effects of passage history and sampling bias on phylogenetic reconstruction of human influenza A evolution (2000) Proc Natl Acad Sci USA, 97, pp. 6974-6980. , BLAST The basic local alignment search tool is a system for searching similar sequences against all available sequence databases irrespective of whether the query is DNA or protein sequences. The BLAST programs consist of blastn","Liu, E.T.; Singapore Science Park II, 1 Science Park Road 05-01, Singapore 117528, Singapore; email: gisliue@nus.edu.sg",,"Elsevier Limited",01406736,,LANCA,"12781537","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0037686664
"Peiris J.S.M., Chu C.M., Cheng V.C.C., Chan K.S., Hung I.F.N., Poon L.L.M., Law K.I., Tang B.S.F., Hon T.Y.W., Chan C.S., Chan K.H., Ng J.S.C., Zheng B.J., Ng W.L., Lai R.W.M., Guan Y., Yuen K.Y.","7005486823;7404345558;23670479400;15924732400;7006103457;7005441747;7202563012;8908243000;6603902566;25939333400;35338760600;57206039289;7201780588;7401613401;57203977175;7202924055;36078079100;","Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study",2003,"Lancet","361","9371",,"1767","1772",,985,"10.1016/S0140-6736(03)13412-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038362701&doi=10.1016%2fS0140-6736%2803%2913412-5&partnerID=40&md5=5b622a3e8cc718d02268a839611cc7fa","Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong","Peiris, J.S.M., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Chu, C.M., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Cheng, V.C.C., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Chan, K.S., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Hung, I.F.N., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Poon, L.L.M., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Law, K.I., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Tang, B.S.F., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Hon, T.Y.W., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Chan, C.S., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Chan, K.H., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Ng, J.S.C., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Zheng, B.J., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Ng, W.L., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Lai, R.W.M., Dept. Med., Intensive Care, R., United Christian Hospital, Hong Kong, Hong Kong; Guan, Y., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., Depts. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong, Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong","Background: We investigated the temporal progression of the clinical, radiological, and virological changes in a community outbreak of severe acute respiratory syndrome (SARS). Methods: We followed up 75 patients for 3 weeks managed with a standard treatment protocol of ribavirin and corticosteroids, and assessed the pattern of clinical disease, viral load, risk factors for poor clinical outcome, and the usefulness of virological diagnostic methods. Findings: Fever and pneumonia initially improved but 64 (85%) patients developed recurrent fever after a mean of 8.9 (SD 3.1) days, 55 (73%) had watery diarrhoea after 7.5 (2.3) days, 60 (80%) had radiological worsening after 7.4 (2.2) days, and respiratory symptoms worsened in 34 (45%) after 8.6 (3.0) days. In 34 (45%) patients, improvement of initial pulmonary lesions was associated with appearance of new radiological lesions at other sites. Nine (12%) patients developed spontaneous pneumomediastinum and 15 (20%) developed acute respiratory distress syndrome (ARDS) in week 3. Quantitative reverse-transcriptase (RT) PCR of nasopharyngeal aspirates in 14 patients (four with ARDS) showed peak viral load at day 10, and at day 15 a load lower than at admission. Age and chronic hepatitis B virus infection treated with lamivudine were independent significant risk factors for progression to ARDS (p=0.001). SARS-associated coronavirus in faeces was seen on RT-PCR in 65 (97%) of 67 patients at day 14. The mean time to seroconversion was 20 days. Interpretation: The consistent clinical progression, shifting radiological infiltrates, and an inverted V viral-load profile suggest that worsening in week 2 is unrelated to uncontrolled viral replication but may be related to immunopathological damage.",,"amoxicillin plus clavulanic acid; azithromycin; corticosteroid; hydrocortisone; lamivudine; levofloxacin; meprednisone; prednisolone; ribavirin; adult; article; aspiration; clinical feature; clinical trial; Coronavirus; diagnostic procedure; disease association; disease course; epidemic; female; fever; follow up; hepatitis B; hospital admission; human; immunopathology; lung injury; major clinical study; male; patient care; pneumomediastinum; pneumonia; priority journal; prospective study; quantitative analysis; radiological procedures; recurrent disease; respiratory distress; respiratory tract disease; respiratory tract infection; reverse transcription polymerase chain reaction; risk factor; seroconversion; severe acute respiratory syndrome; treatment outcome; Verner Morrison syndrome; virus load; virus replication","Severe Acute Respiratory Syndrome (SARS): Multi-country Outbreak - Update 34, , http://www.who.int/csr/don/2003_04_19/en/; SARS Coronavirus Sequencing, , http://www.cdc.gov/ncidod/sars/sequence.htm; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome, , http://content.nejm.org/cgi/reprint/NEJMoa030781v3.pdf; Poutanen, S.M., Low, D.E., Henry, B., Identification of Severe Acute Respiratory Syndrome in Canada, , http://content.nejm.org/cgi/reprint/NEJMoa030634v3.pdf; Lee, N., Hui, D., Wu, A., A Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong, , http://content.nejm.org/cgi/reprint/NEJMoa030685v2.pdf; Tsang, K.W., Ho, P.L., Ooi, G.C., A Cluster of Cases of Severe Acute Respiratory Syndrome in Hong Kong, , http://content.nejm.org/cgi/reprint/NEJMoa030666v3.pdf; Atypical Pneumonia, , http://www.info.gov.hk/dh/ap.htm; Ho, W., Guideline on management of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1313-1315; HA Guidelines on Severe Acute Respiratory Syndrome, , http://www.ha.org.hk/sars/guidelines/index.html; Bernard, G.R., Artigas, A., Brigham, K.L., The American-European consensus conference on ARDS: Definitions, mechanisms, relevant outcomes, and clinical trial coordination (1994) Am J Respir Crit Care Med, 149, pp. 818-824; Knaus, W.A., Draper, E.A., Wagner, D.P., APACHE II: A severity of disease classification system (1985) Crit Care Med, 13, pp. 818-829; Poon, L.L.M., Wong, O.K., Luk, W., Rapid Diagnosis of a Coronavirus Associated with Severe Acute Respiratory Syndrome (SARS), , http://www.clinchem.org/cgi/content/full/49/4/DC1; Majeski, E.I., Harley, R.A., Bellum, S.C., Differential role for T cells in the development of fibrotic lesions associated with reovirus 1/L-induced bronchiolitis obliterans organizing pneumonia versus acute respiratory distress syndrome (2003) Am J Respir Cell Mol Biol, 28, pp. 208-217; Ning, Q., Brown, D., Parodo, J., Ribavirin inhibits viral-induced macrophage production of TNF, IL-1, the procoagulant fgl2 prothrombinase and preserves Th1 cytokine production but inhibits Th2 cytokine response (1998) J Immunol, 160, pp. 3487-3493; Turner, R.B., Felton, A., Kosak, K., Prevention of experimental coronavirus colds with intranasal alpha-2b interferon (1986) J Infect Dis, 154, pp. 443-447; Olliff, J.F., Williams, M.P., Radiological appearances of cytomegalovirus infections (1989) Clin Radiol, 40, pp. 463-467; Tutor, J.D., Montgomery, V.L., Eid, N.S., A case of influenza bronchiolitis complicated by pneumomediastinum and subcutaneous emphysema (1995) Pediatr Pulmonol, 19, pp. 393-395","Yuen, K.Y.; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong; email: kyyuen@hkucc.hku.hk",,"Elsevier Limited",01406736,,LANCA,"12781535","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0038362701
"Ruan Y.J., Wei C.L., Ling A.E.","7103091069;7401658175;36853163800;","Erratum: Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (Lancet (2003) 361 (1779-1785))",2003,"Lancet","361","9371",,"1832","",,2,"10.1016/S0140-6736(03)13442-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038778375&doi=10.1016%2fS0140-6736%2803%2913442-3&partnerID=40&md5=bf85fc7b3d60f37c02c7e0abaed66015",,"Ruan, Y.J.; Wei, C.L.; Ling, A.E.",[No abstract available],,"erratum; error; priority journal",,,,"Elsevier Limited",01406736,,LANCA,,"English","Lancet",Erratum,"Final",,Scopus,2-s2.0-0038778375
"Brown E.G., Tetro J.A.","7404130404;6508339233;","Comparative analysis of the SARS coronavirus genome: A good start to a long journey",2003,"Lancet","361","9371",,"1756","1757",,15,"10.1016/S0140-6736(03)13444-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038101477&doi=10.1016%2fS0140-6736%2803%2913444-7&partnerID=40&md5=cb7858cf02437608fa0d65cb06cb2e3a","Dept. Biochem., Microbiol./Immunol., Faculty of Medicine, University of Ottawa, Ottawa, Ont. K1H 8M5, Canada","Brown, E.G., Dept. Biochem., Microbiol./Immunol., Faculty of Medicine, University of Ottawa, Ottawa, Ont. K1H 8M5, Canada; Tetro, J.A., Dept. Biochem., Microbiol./Immunol., Faculty of Medicine, University of Ottawa, Ottawa, Ont. K1H 8M5, Canada",[No abstract available],,"amino acid; glycoprotein; virus RNA; Canada; cell assay; China; clinical feature; Coronavirus; genetic analysis; genetic conservation; genetic stability; genetic variability; human; immunity; medical literature; molecular biology; mutation; myalgia; nonhuman; note; open reading frame; pneumonia; priority journal; respiratory tract infection; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; sore throat; Vero cell; viral genetics; virus examination; virus genome; virus transmission; water contamination; zoonosis","Luk, J., Gross, P., Thompson, W.W., Observations on mortality during the 1918 influenza pandemic (2001) Clin Infect Dis, 33, pp. 1375-1378; (2003) Hospital Infection Control Guidance for Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/infectioncontrol/en/, April 24; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; (2003) Update 31: Coronavirus Never before Seen in Humans is the Cause of SARS, , http://www.who.int/csr/sarsarchive/2003_04_16/en/, April 16; Lai, M.M.C., Holmes, K.V., Coronaviridae: The viruses and their replication (2001) Fields virology 4th edn, pp. 1163-1186. , D.M. Knipe, & P.M. Howley. London: Lippincott Williams & Wilkins; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030747v2; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085952v1.pdf; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085953v1.pdf; Bush, R.M., Smith, C.B., Cox, N.J., Fitch, W.M., Effects of passage history and sampling bias on phylogenetic reconstruction of human influenza A evolution (2000) Proc Natl Acad Sci USA, 97, pp. 6974-6980; Ewald, P.W., The evolution of virulence and emerging diseases (1998) J Urban Health, 75, pp. 480-491; Brown, E.G., Liu, H., Kit, L.C., Baird, S., Nesrallah, M., Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: Identification of functional themes (2001) Proc Natl Acad Sci USA, 98, pp. 6883-6888; Seo, S.H., Hoffmann, E., Webster, R.G., Lethal H5N1 influenza viruses escape host anti-viral cytokine responses (2002) Nat Med, 8, pp. 950-954; Fields, B.N., AIDS: Time to turn to basic science (1994) Nature, 369, pp. 95-96","Brown, E.G.; Dept. Biochem., Microbiol./Immunol., Faculty of Medicine, University of Ottawa, Ottawa, Ont. K1H 8M5, Canada; email: ebrown@uottawa.ca",,"Elsevier Limited",01406736,,LANCA,"12781529","English","Lancet",Note,"Final",Open Access,Scopus,2-s2.0-0038101477
"Nicholls J.M., Poon L.L.M., Lee K.C., Ng W.F., Lai S.T., Leung C.Y., Chu C.M., Hui P.K., Mak K.L., Lim W., Yan K.W., Chan K.H., Tsang N.C., Guan Y., Yuen K.Y., Peiris J.S.M.","7201463077;7005441747;7501503975;7401613384;7402937038;55586287700;7404345558;57210687265;35735787500;7202378277;7102869279;7406034307;7005609132;7202924055;36078079100;7005486823;","Lung pathology of fatal severe acute respiratory syndrome",2003,"Lancet","361","9371",,"1773","1778",,477,"10.1016/S0140-6736(03)13413-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038024612&doi=10.1016%2fS0140-6736%2803%2913413-7&partnerID=40&md5=39223c0c984e687c0e05444db3f3592d","Department of Pathology, University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Department of Pathology and Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Department of Pathology, Yan Chai Hospital, Kowloon, Hong Kong; Department of Pathology, United Christian Hospital, Kowloon, Hong Kong; Department of Medicine, United Christian Hospital, Kowloon, Hong Kong; Government Virus Unit, Kowloon, Hong Kong; Department of Pathology, Queen Elizabeth Hospital, Kowloon, Hong Kong; Department of Microbiology, Queen Elizabeth Hospital, Kowloon, Hong Kong; Department of Microbiology, University of Hong Kong, Pok Fu Lam, Hong Kong, Hong Kong","Nicholls, J.M., Department of Pathology, University of Hong Kong, Hong Kong, Hong Kong; Poon, L.L.M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Lee, K.C., Department of Pathology and Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Ng, W.F., Department of Pathology, Yan Chai Hospital, Kowloon, Hong Kong; Lai, S.T., Department of Pathology and Medicine, Princess Margaret Hospital, Kowloon, Hong Kong; Leung, C.Y., Department of Pathology, United Christian Hospital, Kowloon, Hong Kong; Chu, C.M., Department of Medicine, United Christian Hospital, Kowloon, Hong Kong; Hui, P.K.; Mak, K.L.; Lim, W., Government Virus Unit, Kowloon, Hong Kong; Yan, K.W., Department of Pathology, Queen Elizabeth Hospital, Kowloon, Hong Kong; Chan, K.H., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Tsang, N.C., Department of Microbiology, Queen Elizabeth Hospital, Kowloon, Hong Kong; Guan, Y., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong, Department of Microbiology, University of Hong Kong, Pok Fu Lam, Hong Kong, Hong Kong","Background: Severe acute respiratory syndrome (SARS) is a novel infectious disease with global impact. A virus from the family Coronaviridae has been identified as the cause, but the pathogenesis is still unclear. Methods: Post-mortem tissue samples from six patients who died from SARS in February and March, 2003, and an open lung biopsy from one of these patients were studied by histology and virology. Only one full autopsy was done. Evidence of infection with the SARS-associated coronavirus (SARS-CoV) and human metapneumovirus was sought by reverse-transcriptase PCR and serology. Pathological samples were examined by light and electron microscopy and immunohistochemistry. Findings: All six patients had serological evidence of recent infection with SARS-CoV. Diffuse alveolar damage was common but not universal. Morphological changes identified were bronchial epithelial denudation, loss of cilia, and squamous metaplasia. Secondary bacterial pneumonia was present in one case. A giant-cell infiltrate was seen in four patients, with a pronounced increase in macrophages in the alveoli and the interstitium of the lung. Haemophagocytosis was present in two patients. The alveolar pneumocytes also showed cytomegaly with granular amphophilic cytoplasm. The patient for whom full autopsy was done had atrophy of the white pulp of the spleen. Electron microscopy revealed viral particles in the cytoplasm of epithelial cells corresponding to coronavirus. Interpretation: SARS is associated with epithelial-cell proliferation and an increase in macrophages in the lung. The presence of haemophagocytosis supports the contention that cytokine dysregulation may account, at least partly, for the severity of the clinical disease. The case definition of SARS should acknowledge the range of lung pathology associated with this disease.",,"cytokine; adult; aged; article; autopsy; bacterial pneumonia; bronchus mucosa; cadaver; cell assay; cell count; cell infiltration; cell proliferation; clinical article; Coronavirus; cytomegaly; cytoplasm; disease association; disease severity; electron microscopy; epithelium cell; erythrophagocytosis; fatality; female; giant cell; histology; human; human tissue; immunohistochemistry; lung alveolus; lung alveolus cell; lung biopsy; lung disease; lung injury; lung interstitium; macrophage; male; Metapneumovirus; microbiological examination; priority journal; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; spleen disease; squamous cell metaplasia; structure analysis; virology; virus infection; virus particle","Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome. (SARS), , http://www.who.int/csr/sarscountry/2003_04_05/en; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong N Engl J Med, , in press; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Severe acute respiratory syndrome (SARS) is associated with a coronavirus (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome N Engl J Med, , in press; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada N Engl J Med, , in press; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Fouchier, R.A., Bestebroer, T.M., Herfst, S., Van Der Kemp, L., Rimmelzwaan, G.F., Osterhaus, A.D., Detection of influenza A virus from different species by PCR amplification of conserved sequences in the matrix gene (2000) J Clin Microbiol, 38, pp. 4096-4101; Mitchell, S., O'Neill, H.J., Ong, G.M., Clinical assessment of a generic DNA amplification assay for the identification of respiratory adenovirus infections (2003) J Clin Virol, 26, pp. 331-338; Myers, J.C., Colby, T.V., Yousem, S.A., Common pathways and patterns of injury (1994) Pulmonary pathology 2nd edn, pp. 57-77. , D.H. Dail, & S.P. Hammar. New York: Springer-Verlag; Bellingan, G.J., The pulmonary physician in critical care: 6, the pathogenesis of ALI/ARDS (2002) Thorax, 57, pp. 540-546; Kim, E.A., Lee, K.S., Primack, S.L., Viral pneumonias in adults: Radiologic and pathologic findings (2002) Radiographics, 22, pp. 137-S149; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong N Engl J Med, , in press; Transmissible Gastroenteritis, , http://www.oie.int/eng/normes/mmanual/A_00085.htm; Corse, E., Machamer, C.E., The cytoplasmic tail of infectious bronchitis virus E protein directs Golgi targeting (2002) J Virol, 76, pp. 1273-1284; Garantziotis, S., Howell, D.N., McAdams, H.P., Davis, R.D., Henshaw, N.G., Palmer, S.M., Influenza pneumonia in lung transplant recipients: Clinical features and association with bronchiolitis obliterans syndrome (2001) Chest, 119, pp. 1277-1280; Halbur, P.G., Paul, P.S., Frey, M.L., Comparison of the pathogenicity of two US porcine reproductive and respiratory syndrome virus isolates with that of the Lelystad virus (1995) Vet Pathol, 32, pp. 648-660; Halbur, P.G., Paul, P.S., Vaughn, E.M., Andrews, J.J., Experimental reproduction of pneumonia in gnotobiotic pigs with porcine respiratory coronavirus isolate AR310 (1993) J Vet Diagn Invest, 5, pp. 184-188; Pensaert, M.B., Transmissible gastroentertitis virus (respiritory variant) (1989) Virus infection of porcines, pp. 154-165. , M.B. Pensaert. Amsterdam: Elsevier Science Publishers; To, K.F., Chan, P.K., Chan, K.F., Pathology of fatal human infection associated with avian influenza A H5N1 virus (2001) J Med Virol, 63, pp. 242-246; Fisman, D.N., Hemophagocytic syndromes and infection (2000) Emerg Infect Dis, 6, pp. 60-68; Yuen, K.Y., Chan, P.K.S., Peiris, M., Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus (1998) Lancet, 351, pp. 467-471; Cheung, C.Y., Poon, L.L.M., Lau, A.S.Y., Induction of proinflammatory cytokines in human macrophages by influenza A (H5N1) viruses: A mechanism for the unusual severity of human disease (2002) Lancet, 360, pp. 1831-1837; Collins, A.R., Human macrophages are susceptible to coronavirus OC43 (1998) Adv Exp Med Biol, 440, pp. 635-639; Lai, K.N., Leung, J.C., Metz, C.N., Lai, F.M., Bucala, R., Lan, H.Y., Role for macrophage migration inhibitory factor in acute respiratory distress syndrome (2003) J Pathol, 199, pp. 496-508; Halbur, P.G., Pallarés, F.J., Opriessnig, T., Vaughn, E.M., Paul, P.S., Pathogenicity of three isolates of porcine respiratory coronavirus in the USA (2003) Vet Rec, 152, pp. 358-361; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/","Peiris, J.S.M.; Department of Microbiology, University of Hong Kong, Pok Fu Lam, Hong Kong, Hong Kong; email: malik@hkucc.hku.hk",,"Elsevier Limited",01406736,,LANCA,"12781536","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0038024612
"Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A., Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y., Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R., Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S., Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M., Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K., Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R., Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A., Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S., Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M., Skowronski D.M., Upton C., Roper R.L.","55553154800;55732380600;57206715216;7402085535;6701511300;6506267972;6603469190;7003795883;7102357255;36901169300;7003718735;7102479331;7402382685;6506328805;7102837839;14007254600;56155388900;7101994011;57209550015;6602629764;7102461235;56597396300;35351155100;9246643900;6602540218;55396130300;7405755430;7102012709;6701413300;7003508990;6602480468;7005784446;7103336339;6602131094;57200253688;7003412968;8635430300;7006769609;6601989221;57216090579;6602386764;57194562205;7202115850;36610540200;57189174119;35187394200;7006946434;6603000295;6701743502;7103350166;6507252656;55738012500;7202917118;7007047752;7004178160;16216941800;7004017482;7004783828;35243331600;","The genome sequence of the SARS-associated coronavirus",2003,"Science","300","5624",,"1399","1404",,1370,"10.1126/science.1085953","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038823524&doi=10.1126%2fscience.1085953&partnerID=40&md5=f7c518fa68688c8112eb121dc4d0f359","Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Brit. Columbia Ctr. for Dis. Control, Univ. Brit. Columbia Ctr. Dis. Ctrl., 655 West 12th Avenue, Vancouver, BC V5Z 4R4, Canada; Department of Biochemistry, University of Victoria, STN CSC, Post Office Box 3055, Victoria, BC V8W 3P6, Canada","Marra, M.A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Jones, S.J.M., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Astell, C.R., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Holt, R.A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Brooks-Wilson, A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Butterfield, Y.S.N., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Khattra, J., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Asano, J.K., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Barber, S.A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Chan, S.Y., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Cloutier, A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Coughlin, S.M., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Freeman, D., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Girn, N., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Griffith, O.L., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Leach, S.R., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Mayo, M., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; McDonald, H., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Montgomery, S.B., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Pandoh, P.K., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Petrescu, A.S., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Robertson, A.G., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Schein, J.E., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Siddiqui, A., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Smailus, D.E., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Stott, J.M., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Yang, G.S., Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; Plummer, F., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Andonov, A., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Artsob, H., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Bastien, N., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Bernard, K., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Booth, T.F., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Bowness, D., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Czub, M., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Drebot, M., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Fernando, L., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Flick, R., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Garbutt, M., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Gray, M., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Grolla, A., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Jones, S., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Feldmann, H., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Meyers, A., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Kabani, A., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Li, Y., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Normand, S., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Stroher, U., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Tipples, G.A., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Tyler, S., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Vogrig, R., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Ward, D., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Watson, B., National Microbiology Laboratory, 1015 Arlington Street, Winnipeg, Man. R3E 3R2, Canada; Brunham, R.C., Brit. Columbia Ctr. for Dis. Control, Univ. Brit. Columbia Ctr. Dis. Ctrl., 655 West 12th Avenue, Vancouver, BC V5Z 4R4, Canada; Krajden, M., Brit. Columbia Ctr. for Dis. Control, Univ. Brit. Columbia Ctr. Dis. Ctrl., 655 West 12th Avenue, Vancouver, BC V5Z 4R4, Canada; Petric, M., Brit. Columbia Ctr. for Dis. Control, Univ. Brit. Columbia Ctr. Dis. Ctrl., 655 West 12th Avenue, Vancouver, BC V5Z 4R4, Canada; Skowronski, D.M., Brit. Columbia Ctr. for Dis. Control, Univ. Brit. Columbia Ctr. Dis. Ctrl., 655 West 12th Avenue, Vancouver, BC V5Z 4R4, Canada; Upton, C., Department of Biochemistry, University of Victoria, STN CSC, Post Office Box 3055, Victoria, BC V8W 3P6, Canada; Roper, R.L., Department of Biochemistry, University of Victoria, STN CSC, Post Office Box 3055, Victoria, BC V8W 3P6, Canada","We sequenced the 29,751-base genome of the severe acute respiratory syndrome (SARS)-associated coronavirus known as the Tor2 isolate. The genome sequence reveals that this coronavirus is only moderately related to other known coronaviruses, including two human coronaviruses, HCoV-OC43 and HCoV-229E. Phylogenetic analysis of the predicted viral proteins indicates that the virus does not closely resemble any of the three previously known groups of coronaviruses. The genome sequence will aid in the diagnosis of SARS virus infection in humans and potential animal hosts (using polymerase chain reaction and immunological tests), in the development of antivirals (including neutralizing antibodies), and in the identification of putative epitopes for vaccine development.",,"Antibodies; Genes; Immunology; Pulmonary diseases; Vaccines; Genome sequence; Viruses; complementary DNA; gene product; membrane protein; RNA directed RNA polymerase; spike glycoprotein; unclassified drug; virus glycoprotein; virus protein; virus RNA; genetics; virus; amino acid sequence; article; base pairing; Coronavirus; genome; nonhuman; nucleotide sequence; open reading frame; phylogeny; polymerase chain reaction; priority journal; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; virus genome; virus infection; virus isolation; virus particle; 3' Untranslated Regions; 5' Untranslated Regions; Animals; Base Sequence; Conserved Sequence; Coronavirus; DNA, Complementary; Frameshifting, Ribosomal; Genome, Viral; Humans; Membrane Glycoproteins; Nucleocapsid Proteins; Open Reading Frames; Phylogeny; Regulatory Sequences, Nucleic Acid; RNA Replicase; RNA, Viral; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome; Viral Envelope Proteins; Viral Matrix Proteins; Viral Proteins; Animalia; Coronavirus; RNA viruses; SARS coronavirus","Donnelly, C.A., (2003) Lancet, , http://image.thelancet.com/extras/03art4453web.pdf, published online 7 May; Peiris, J.S.M., (2003) Lancet, , http://image.thelancet.com/extras/03art3477web.pdf, published online 8 April; Ksiazek, T.G., (2003) N. Engl. J. Med., , published online 10 April (10.1056/NEJMoa030781); Munch, R., (2003) Microbes Infect., 5, p. 69; Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., (2001) Fields Virology, , Lippincott Williams & Wilkins, Philadelphia, ed. 4; Lai, M.M.C., Cavanagh, D., (1997) Adv. Virus Res., 48, p. 1; Sawicki, S.G., Sawicki, D.L., (1998) Adv. Exp. Med. Biol., 440, p. 215; Sawicki, D.L., (2001) J. Gen. Virol., 82, p. 386; Sawicki, S.G., Sawicki, D.L., (1990) J. Virol., 64, p. 1050; Schaad, M., Baric, R.S.J., (1994) J. Virol., 68, p. 8169; Sethna, P.B., (1989) Proc. Natl. Acad. Sci. U.S.A., 86, p. 5626; Myint, S.H., (1995) The Coronaviridae, pp. 389-401. , S. G. Siddell, Ed. Plenum, New York; Enjuanes, L., (2000) Virus Taxonomy. Classification and Nomenclature of Viruses, pp. 835-849. , M. H. V. van Regenmortel et al., Eds. Academic Press, New York; note; Poutanen, S.M., (2003) N. Engl. J. Med., , published online 31 March (10.1056/NEJMoa030634); Rota, P.A., (2003) Science, 300, p. 1394. , published online 1 May 2003 (10.1126/science.1085952); Jonassen, C.M., Jonassen, T.O., Grinde, B., (1998) J. Gen. Virol., 79, p. 715; Lapps, W., Hogue, B.G., Brian, D.A., (1987) Virology, 157, p. 47; Krishnan, R., Chang, R.Y., Brian, D.A., (1996) Virology, 218, p. 400; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, p. 853; Nielsen, H., Engelbrecht, J., Brunak, S., Von Heijne, G., (1997) Protein Eng., 10, p. 1; Sonnhammer, E.L., Von Heijne, G., Krogh, A., (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol., 6, p. 175; Tsai, J.C., Zelus, B.D., Holmes, K.V., Weiss, S.R., (2003) J. Virol., 77, p. 841; Altschul, S.F., (1997) Nucleic Acids Res., 25, p. 3389; Pearson, W.R., Lipman, D.J., (1988) Proc. Natl. Acad. Sci. U.S.A., 85, p. 2444; Bateman, A., (2002) Nucleic Acids Res., 30, p. 276; Hofman, K., Stoffel, W., (1993) Biol. Chem. Hoppe-Seyler, 374, p. 166; Aipweiler, R., (2001) Nucleic Acids Res., 29, p. 37; Zdobnov, E.M., Apweiler, R., (2001) Bioinformatics, 17, p. 847; Ortego, J., (2002) J. Virol., 76, p. 11518; Kuo, L., (2002) Annual Meeting of the American Society for Virology, , paper presented, Lexington, KY, 20 to 24 July; note; Thompson, J.D., Higgins, D.G., Gibson, T.J., (1994) Nucleic Acids Res., 22, p. 4673; Felsenstein, J., (1993) PHYLIP (Phylogeny Inference Package) Version 3.5c; note","Marra, M.A.; Brit. Columbia Cancer Agency (BCCA), Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC V5Z 4E6, Canada; email: mmarra@bccgsc.ca",,,00368075,,SCIEA,"12730501","English","Science",Article,"Final",Open Access,Scopus,2-s2.0-0038823524
"Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R., Icenogle J.P., Peñaranda S., Bankamp B., Maher K., Chen M.-H., Tong S., Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D., Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S., Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R., Günther S., Osterhaus A.D.H.E., Drosten C., Pallansch M.A., Anderson L.J., Bellini W.J.","7005808979;7003793073;35452262100;7101713301;57189162110;7003937598;6603440800;6602349036;7005575079;55602090900;57214433240;6602551546;8924653800;6508253305;7004334309;57198482438;16403747800;7005380414;6602425443;7201834936;7101963789;7101827480;35499296900;6507669856;7101996910;6602905875;6603928696;6506504516;7006060466;7102978849;55533604400;7003813990;56943590300;55512739900;7005204113;","Characterization of a novel coronavirus associated with severe acute respiratory syndrome",2003,"Science","300","5624",,"1394","1399",,1579,"10.1126/science.1085952","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037561920&doi=10.1126%2fscience.1085952&partnerID=40&md5=3d4885c1d9106729bd1190254d4912d7","Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Department of Biochemistry, Univ. of California-San Francisco, San Francisco, CA 94143, United States; Department of Virology, Erasmus University, Rotterdam, 3000 DR, Netherlands; Department of Virology, Bernhard Nocht Inst. for Trop. Med., 20359 Hamburg, Germany","Rota, P.A., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Oberste, M.S., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Monroe, S.S., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Nix, W.A., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Campagnoli, R., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Icenogle, J.P., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Peñaranda, S., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Bankamp, B., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Maher, K., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Chen, M.-H., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Tong, S., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Tamin, A., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Lowe, L., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Frace, M., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; DeRisi, J.L., Department of Biochemistry, Univ. of California-San Francisco, San Francisco, CA 94143, United States; Chen, Q., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Wang, D., Department of Biochemistry, Univ. of California-San Francisco, San Francisco, CA 94143, United States; Erdman, D.D., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Peret, T.C.T., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Burns, C., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Ksiazek, T.G., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Rollin, P.E., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Sanchez, A., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Liffick, S., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Holloway, B., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Limor, J., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; McCaustland, K., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Olsen-Rasmussen, M., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Fouchier, R., Department of Virology, Erasmus University, Rotterdam, 3000 DR, Netherlands; Günther, S., Department of Virology, Bernhard Nocht Inst. for Trop. Med., 20359 Hamburg, Germany; Osterhaus, A.D.H.E., Department of Virology, Erasmus University, Rotterdam, 3000 DR, Netherlands; Drosten, C., Department of Virology, Bernhard Nocht Inst. for Trop. Med., 20359 Hamburg, Germany; Pallansch, M.A., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Anderson, L.J., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; Bellini, W.J., Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States","In March 2003, a novel coronavirus (SARS-CoV) was discovered in association with cases of severe acute respiratory syndrome (SARS). The sequence of the complete genome of SARS-CoV was determined, and the initial characterization of the viral genome is presented in this report. The genome of SARS-CoV is 29,727 nucleotides in length and has 11 open reading frames, and its genome organization is similar to that of other coronaviruses. Phylogenetic analyses and sequence comparisons showed that SARS-CoV is not closely related to any of the previously characterized coronaviruses.",,"Composition; Genes; Pulmonary diseases; Severe acute respiratory syndrome (SARS); Viruses; gene product; membrane protein; proteinase; RNA directed DNA polymerase; RNA directed RNA polymerase; structural protein; unclassified drug; virus E protein; virus glycoprotein; virus M protein; virus N protein; virus protein; virus RNA; virus S protein; disease; medicine; amino acid sequence; article; Coronavirus; genome; human; major clinical study; nonhuman; nucleotide sequence; open reading frame; phylogeny; priority journal; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; strain difference; Urbani strain of SARS coronavirus; virus genome; virus infection; Amino Acid Sequence; Conserved Sequence; Coronavirus; DNA, Complementary; Endopeptidases; Genome, Viral; Humans; Membrane Glycoproteins; Molecular Sequence Data; Nucleocapsid Proteins; Open Reading Frames; Phylogeny; Polyproteins; Regulatory Sequences, Nucleic Acid; RNA Replicase; RNA, Messenger; RNA, Viral; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome; Transcription, Genetic; Viral Envelope Proteins; Viral Matrix Proteins; Viral Proteins; Coronavirus; RNA viruses; SARS coronavirus","Poutanen, S.M., (2003) N. Engl. J. Med., , http://nejm.org/earlyrelease/sars.asp#4-2, 17 April; Lee, N., (2003) N. Engl. J. Med., , http://nejm.org/earlyrelease/sars.asp#4-2, 17 April; Tsang, K.W., (2003) N. Engl. J. Med., , http://nejm.org/earlyrelease/sars.asp#4-2, 17 April; (2003) Morb. Mortal. Wkly. Rep., 52, pp. 3S7; Ksiazek, S.T.G., (2003) N. Engl. J. Med., 348, p. 1947; Peiris, J.S., (2003) Lancet, 361, p. 1319; Drosten, C., (2003) N. Engl. J. Med., , http;//nejm.org/earlyrelease/sars.asp#4-2, 17 April; Lai, M.M.C., Holmes, K.V., (2001) Fields Virology, , D. M. Knipe, P. M. Howley, Eds. Lippincott Williams & Wilkins, New York, ed. 4, chap. 35; Enjuanes, L., (2000) Virus Taxonomy, pp. 835-849. , M. H. V. van Regenmortal et al., Eds. Academic Press, New York; Holmes, K.V., (2001) Fields Virology, , D. M. Knipe, P. M. Howley, Eds. Lippincott Williams & Wilkins, New York, ed. 4, chap. 36; note; note; Sawicki, G.S., Sawicki, D.L., (1998) Adv. Exp. Med. Biol., 440, p. 215; note; Liu, D.X., Inglis, S.C., (1992) J. Virol., 66, p. 6143; Thiel, V., Siddell, S.G., (1994) J. Gen. Virol., 75, p. 3041; Rota, P., data not shown; Lote, K.S., (1999) J. Virol., 73, p. 152; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, p. 853; Siddell, S.G., (1995) The Coronaviridae, , Plenum, New York; Escors, D., Ortego, J., Laude, H., Enjuanes, L., (2001) J. Virol., 75, p. 1312; Garoff, H., Hewson, R., Opstelten, D.-J.E., (1998) Microbiol. Mol. Biol. Rev., 62, p. 1171; Sanchez, C.M., (1999) J. Virol., 73, p. 7607; Leparc-Goffart, I., (1998) J. Virol., 72, p. 9628; note; note; De Haan, C.A.M., (2002) Virus Res., 82, p. 77; De Haan, C.A.M., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J.M., (1998) J. Virol., 72, p. 6838; note; Marra, M.A., (2003) Science, 300, p. 1399. , published online 1 May 2003 (10.1126.science.1085953); note","Rota, P.A.; Natl. Center for Infectious Diseases, Centers for Dis. Ctrl./Prevention, Atlanta, CA 30333, United States; email: prota@cdc.gov",,,00368075,,SCIEA,"12730500","English","Science",Article,"Final",Open Access,Scopus,2-s2.0-0037561920
"Holmes K.V., Enjuanes L.","7201657724;7006565392;","The SARS coronavirus: A postgenomic era",2003,"Science","300","5624",,"1377","1378",,82,"10.1126/science.1086418","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038103690&doi=10.1126%2fscience.1086418&partnerID=40&md5=c66be51a8e9d3e796cfa8de24ae68655","Department of Microbiology, Univ. of Colorado Hlth. Sci. Ctr., Denver, CO 80262, United States; Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC Campus Univ. Autonoma, Madrid, Spain","Holmes, K.V., Department of Microbiology, Univ. of Colorado Hlth. Sci. Ctr., Denver, CO 80262, United States; Enjuanes, L., Department of Molecular Biology, Centro Nacional de Biotecnologia, CSIC Campus Univ. Autonoma, Madrid, Spain",[No abstract available],,"complementary DNA; envelope protein; gene product; membrane protein; messenger RNA; proteinase; RNA directed RNA polymerase; virus glycoprotein; virus protein; virus RNA; antivirus agent; virus antigen; virus vaccine; disease; medicine; amino acid sequence; Coronavirus; genome; nonhuman; nucleotide sequence; open reading frame; priority journal; respiratory tract infection; reverse transcription polymerase chain reaction; review; SARS coronavirus; severe acute respiratory syndrome; virion; virus genome; virus infection; virus isolation; virus morphology; virus virulence; animal; chemistry; classification; Coronavirus; DNA sequence; drug design; genetic transcription; genetics; human; immunology; molecular evolution; note; phylogeny; physiology; regulatory sequence; SARS coronavirus; severe acute respiratory syndrome; virology; Coronavirus; RNA viruses; SARS coronavirus; Amino Acid Sequence; Animals; Antigens, Viral; Antiviral Agents; Base Sequence; Coronavirus; Drug Design; Evolution, Molecular; Genome, Viral; Humans; Open Reading Frames; Phylogeny; Regulatory Sequences, Nucleic Acid; RNA, Messenger; RNA, Viral; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome; Transcription, Genetic; Viral Proteins; Viral Vaccines","Marra, M.A., (2003) Science, 300, p. 1399. , published online 1 May 2003 (10.1126/science. 1085953); Rota, P.A., (2003) Science, 300, p. 1394. , published online 1 May 2003 (10.1126/science. 1085952); Ruan, Y.J., Lancet, 361. , published online 17 May 2003; Lai, M.M.C., Holmes, K.V., (2001) Fields Virology, 1, pp. 1163-1185. , D. Knipe et al., Eds. Lippincott-Williams and Wilkins, Philadelphia; Anand, K., (2003) Science, , 13 May 10.1126/science. 1085658; Masters, P.S., (1999) Adv. Virus. Res., 53, p. 245; Thiel, V., (2001) J. Gen. Virol., 82, p. 1273; Casais, R., (2001) J. Virol., 75, p. 12359; Almazan, F., (2000) Proc. Natl. Acad. Sci. U.S.A., 97, p. 5516; Yount, B., (2002) J. Virol., 76, p. 11065; Enjuanes, L., (2001) J. Biotechnol., 88, p. 183; Ortego, J., (2002) J. Virol., 76, p. 11518; Sola, I., (2003) J. Virol., 77, p. 4357","Holmes, K.V.; Department of Microbiology, Univ. of Colorado Hlth. Sci. Ctr., Denver, CO 80262, United States; email: kathryn.holmes@UCHSC.edu",,,00368075,,SCIEA,"12775826","English","Science",Review,"Final",,Scopus,2-s2.0-0038103690
"Zhang W.-G., Li J.-Q., Zhou H.-M.","54394758100;54393744700;57207400290;","Genomic characterization of SARS coronavirus: A novel member of coronavirus",2003,"Acta Genetica Sinica","30","6",,"501","508",,5,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037773611&partnerID=40&md5=694a7f05914a10aff8c25f662a8344c4",,"Zhang, W.-G.; Li, J.-Q.; Zhou, H.-M.","In March 2003, SARS-CoV, a novel coronavirus which has been proved to be a pathogen causing Severe Acute Respiratory Syndrome (SARS). The complete genome of SARS-CoV has been sequenced by international collaboration including China. In the present study, the genome sequences were collected from NCBI and genomic characterization was analyzed. SARS-CoV has a genome of 28-30 kb including 11 ORFs (Open Reading Frames), which is consistent with that of coronavirus family, and its genome organization is similar to those of other coronaviruses as well. SARS-CoV evolutionally closes to other coronavirus in their corresponding proteins, such as spike protein, small membrane protein and nucleocapsid protein. In some regions of the genome, the genomic sequence of SARS-CoV was significantly different from that of other coronavirus, and has a self-conservative genomic sequence. Moreover, its encoding protein sequences were greatly different from those of other coronavirus. The analysis indicated that SARS-CoV has lower redundancy, that is, it has a high variation possibility. It may not be a variant of other coronaviruses but a novel coronavirus, which existed independently in nature and was not recognized by human being before, although SARS-CoV is morphologically similar to other coronavirus and belongs to coronavirus family. The sequences of its genes and encoding proteins are substantially different from those of other coronavirus.","Genomic characterization; Redundancy analysis; SARS-CoV","membrane protein; nucleocapsid protein; protein; spike protein; unclassified drug; virus protein; acute respiratory failure; amino acid sequence; article; China; Coronavirus; evolution; gene sequence; genetic variability; nonhuman; nucleotide sequence; open reading frame; redundancy analysis; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; unindexed sequence; virus genome; virus morphology; Coronavirus; SARS coronavirus; SARS CoV","Cheng, J.-H., Contribution of the most neighboring analysis (1982) Advance in Biochemistry and Biophysics, 6, pp. 7-10; De Qin, E., Zhu, Q., Yu, M., Fan, B., Chang, G., A complete sequence and comparative analysis of SARS-associated virus(Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Paul, A., Rota, M., Steven, O., Stephan, S., Monroe, W., Allan, N., Ray, C., Characterization of a Novel Coronavirus Associated with Severe Acute Respiratory Syndrome, , http://www.sciencexpress.org; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooks-Wilson, A., The Genome Sequence of the SARS-Associated Coronavirus, , http://www.sciencexpress.org; http://www.who.int; http://ww.ncbi.nlm.nih.gov; Ministry of Health, , http://ww.moh.gov.cn, P.R. China; National Laboratory of Molecular and Biomolecular Electronic, , http://www.lmbe.seu.edu.on; http://cmbi.bjmu.edu.cn; Chen, Y.-J., Gao, G., Bao, Y.-M., Wu, J.-M., Cai, T., Ye, Z.-Q., Gu, X.-C., Luo, J.-C., Initial analysis of complete genome sequences of SARS coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 493-500",,,"Science Press",03794172,,ICHPC,"12939793","Chinese","Acta Genet. Sin.",Article,"Final",,Scopus,2-s2.0-0037773611
"Ye X., Meng X., Dong J.-B., Liang M., Hu F., Chen H.-Z.","8121561400;57214788077;13906780400;22997810400;55187144300;8121561600;","Current research on SARS coronavirus vaccine",2003,"Progress in Biochemistry and Biophysics","30","3",,"331","334",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041328245&partnerID=40&md5=8dbf882558e5f74e7ac84dd45e1ea094","Department of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China; Shanghai Sunway Biotech., Shanghai 201206, China; Department of Biochemistry, School of Pharmacy, Fudan University, Shanghai 200032, China; Liver Cancer Institute, Zhong Shan Hospital, Fudan University, Shanghai 200032, China","Ye, X., Department of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China, Shanghai Sunway Biotech., Shanghai 201206, China; Meng, X., Department of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China, Shanghai Sunway Biotech., Shanghai 201206, China; Dong, J.-B., Department of Biochemistry, School of Pharmacy, Fudan University, Shanghai 200032, China; Liang, M., Shanghai Sunway Biotech., Shanghai 201206, China, Liver Cancer Institute, Zhong Shan Hospital, Fudan University, Shanghai 200032, China; Hu, F., Shanghai Sunway Biotech., Shanghai 201206, China; Chen, H.-Z., Department of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China","A novel coronavirus has been identified to be associated with the newly outbreak of severe acute respiratory syndrome (SARS). To date 12 whole genome sequences from various samples are available in public-domain database. Spike protein of coronavirus is considered to be the major antigen and contains many potential antigenicity domains. The relatively low mutation rate in spike protein provides high opportunity for effective vaccine development. Since inactivated or attenuated coronavirus holds some potential limitations and risks to prepare and to inoculate, the current best hope for protection is to combine a protein vaccine (i. e., a purified SARS coronavirus spike protein) with a ""vectored"" vaccine, consisting of a plasmid or a harmless virus, such as recombinant adenovirus which has been genetically engineered to produce coronavirus spike protein.","Coronavirus; SARS; Spike protein; Vaccine","spike protein; unclassified drug; virus protein; virus vaccine; adenovirus vector; amino acid substitution; antigenicity; article; controlled study; Coronavirus; gene sequence; genetic engineering; mutation rate; nonhuman; plasmid; pneumonia; severe acute respiratory syndrome; virus strain; Adenoviridae; Coronavirus; SARS coronavirus","Enserink, M., Vogel, G., Infectious diseases: Deferring competition, global net closes in on SARS (2003) Science, 300 (5617), pp. 224-225; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, , http://content.nejm.org/cgi/reprint/NEJMoa030634v3.pdf; Qin, E.D., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of strain (BJ01) of the SARS-associated virus (2003) Chin Sci Bull, 48 (10), pp. 941-948; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe actue respiratory syndrome (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085952v1.pdf; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085953v1.pdf; Singh, H., Raghava, G.P.S., ProPred: Prediction of HLA-DR binding sites (2001) Bioinformatics, 17 (12), pp. 1236-1237; Walgate, R., SARS Vaccine Race: US and European Groups Moving Forward, but WHO Would Rather Put SARS ""Back in the Box"", , http://www.biomedcentral.com/news/20030502/03; Tuboly, T., Nagy, E., Construction and characterization of recombinant porcine adenovirus serotype 5 expressing the transmissible gastroenteritis virus spike gene (2001) J Gen Virol, 82 (1 PART), pp. 183-190; Hussain, K.A., Storz, J., Kousoulas, K.G., Comparison of bovine coronavirus (BCV) antigens: Monoclonal antibodies to the spike glycoprotein distinguish between vaccine and wild-type strains (1991) Virology, 183 (1), pp. 442-445; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to the S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Res, 61 (2), pp. 145-152; Jia, W., Karaca, K., Parrish, C.R., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch Virol, 140 (2), pp. 259-271; Corpet, F., Multiple sequence alignment with hierarchical clustering (1988) Nucleic Acids Res, 16 (22), pp. 10881-10890; Altman, L.K., Grad, Y.D., Study of SARS Genome Shows No Big Mutations, , http://www.nytimes.com/2003/05/09/science/sciencespecial/09INFE.html; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) The Lancet, , http://image.thelancet.com/extras/03art4454web.pdf; Chattergoon, M., Boyer, J., Weiner, D.B., Genetic immunization: A new era in vaccines and immune therapeutics (1997) FASEB J, 11 (10), pp. 753-763; Tuettenberg, A., Jonuleit, H., Tuting, T., Priming of T cells with Ad-transduced DC followed by expansion with peptide-pulsed DC significantly enhances the induction of tumor-specific CD8+ T cells: Implications for an efficient vaccination strategy (2003) Gene Ther, 10 (3), pp. 243-250; Vordermeier, H.M., Lowrie, D.B., Hewinson, R.G., Improved immunogenicity of DNA vaccination with mycobacterial HSP65 against bovine tuberculosis by protein boosting (2003) Vet Microbiol, 93 (4), pp. 349-359; Bernt, K., Liang, M., Ye, X., A new type of adenovirus vector that utilizes homologous recombination to achieve tumor-specific replication (2002) J Virol, 76 (21), pp. 10994-11002; Srivastava, I.K., Liu, M.A., Gene vaccines (2003) Ann Intern Med, 138 (7), pp. 550-559; Bragonzi, A., Conese, M., Non-viral approach toward gene therapy of cystic fibrosis lung disease (2002) Curr Gene Ther, 2 (3), pp. 295-305; Griesenbach, U., Ferrari, S., Geddes, D.M., Gene therapy progress and prospects: Cystic fibrosis (2002) Gene Ther, 9 (20), pp. 1344-1350; Torres, J.M., Sanchez, C., Sune, C., Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein (1995) Virology, 213 (2), pp. 503-516; Torres, J.M., Alonso, C., Ortega, A., Tropism of human adenovirus type 5-based vectors in swine and their ability to protect against transmissible gastroenteritis coronavirus (1996) J Virol, 70 (6), pp. 3770-3780; Callebaut, P., Enjuanes, L., Pensaert, M., An adenovirus recombinant expressing the spike glycoprotein of porcine respiratory coronavirus is immunogenic in swine (1996) J Gen Virol, 77 (2 PART), pp. 309-313","Chen, H.-Z.; Department of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China; email: yaoli@shsmu.edu.cn",,,10003282,,,,"Chinese","Prog. Biochem. Biophys.",Article,"Final",,Scopus,2-s2.0-0041328245
"Raman S., Bouma P., Williams G.D., Brian D.A.","7201483869;7003730370;7406083594;7006460232;","Stem-loop III in the 5′ untranslated region is a cis-acting element in bovine coronavirus defective interfering RNA replication",2003,"Journal of Virology","77","12",,"6720","6730",,46,"10.1128/JVI.77.12.6720-6730.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037942817&doi=10.1128%2fJVI.77.12.6720-6730.2003&partnerID=40&md5=a6ce2605b5c527cb8a76af3fd0c2d921","Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Preventive Medicine Department, Uniformed Serv. Univ. of Hlth. Sci., Bethesda, MD 20814, United States","Raman, S., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States; Bouma, P., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States, Preventive Medicine Department, Uniformed Serv. Univ. of Hlth. Sci., Bethesda, MD 20814, United States; Williams, G.D., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States; Brian, D.A., Department of Microbiology, University of Tennessee, College of Veterinary Medicine, Knoxville, TN 37996-0845, United States, Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","Higher-order structures in the 5′ untranslated region (UTR) of plus-strand RNA viruses are known in many cases to function as cis-acting elements in RNA translation, replication, or transcription. Here we describe evidence supporting the structure and a cis-acting function in defective interfering (DI) RNA replication of stem-loop III, the third of four predicted higher-order structures mapping within the 210-nucleotide (nt) 5′ UTR of the 32-kb bovine coronavirus (BCoV) genome. Stem-loop III maps at nt 97 through 116, has a calculated free energy of -9.1 kcal/mol in the positive strand and -3.0 kcal/mol in the negative strand, and has associated with it beginning at nt 100 an open reading frame (ORF) potentially encoding an 8-amino-acid peptide. Stem-loop III is presumed to function in the positive strand, but its strand of action has not been established. Stem-loop III (i) shows phylogenetic conservation among group 2 coronaviruses and appears to have a homolog in coronavirus groups 1 and 3, (ii) has in all coronaviruses for which sequence is known a closely associated short, AUG-initiated intra-5′ UTR ORF, (iii) is supported by enzyme structure-probing evidence in BCoV RNA, (iv) must maintain stem integrity for DI RNA replication in BCoV DI RNA, and (v) shows a positive correlation between maintenance of the short ORF and maximal DI RNA accumulation in BCoV DI RNA. These results indicate that stem-loop III in the BCoV 5′ UTR is a cis-acting element for DI RNA replication and that its associated intra-5′ UTR ORF may function to enhance replication. It is postullated that these two elements function similarly in the virus genome.",,"cis acting element; defective interfering RNA; peptide; unclassified drug; virus RNA; 5' untranslated region; article; Coronavirus; energy transfer; enzyme structure probing; evolutionary homology; gene mapping; genetic conservation; human; human cell; molecular probe; nonhuman; nucleotide sequence; open reading frame; phylogeny; priority journal; RNA replication; RNA sequence; RNA structure; sequence analysis; stem loop iii; virus genome; 5' Untranslated Regions; Amino Acid Sequence; Animals; Base Sequence; Cattle; Coronavirus, Bovine; Defective Viruses; Enhancer Elements (Genetics); Genome, Viral; Humans; Mice; Molecular Sequence Data; RNA Interference; RNA, Viral; Virus Replication","Baric, R.S., Shieh, C.-K., Stohlman, S.A., Lai, M.M.C., Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription (1987) Virology, 156, pp. 342-354; Baric, R.S., Yount, B., Subgenomic negative-strand RNAs function during mouse hepatitis virus infection (2000) J. 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Virol., 69, pp. 3744-3751; Van der Most, R.G., Spaan, W.J.M., Coronavirus replication, transcription, and RNA recombination (1995) The Coronaviridae, pp. 11-31. , S. G Siddell (ed.). Plenum Press, New York. N.Y; Varani, G., Exceptionally stable nucleic acid hairpins (1995) Annu. Rev. Biophys. Biomol. Struct., 24, pp. 379-404; Williams, G.D., Chang, R.-Y., Brian, D.A., A phylogenetically conserved hairpin-type 3′ untranslated region pseudoknot functions in coronavirus RNA replication (1999) J. Virol., 73, pp. 8349-8355; Zuker, M., Mathews, D.H., Turner, D.H., Algorithms and thermodynamics for RNA secondary structure prediction: A practical guide in RNA biochemistry and biotechnology (1999) NATO ASI Series, pp. 11-43. , J. Barciszewski and B. F. C. Clark (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,,0022538X,,JOVIA,"12767992","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037942817
"Shi D.-H., Zhou H.-J., Wang B.-B., Gu Y.-H., Wang Y.-F.","7402052218;57198957030;55729740600;55439301400;35305984800;","Multiple sequence alignment of the M protein in SARS-associated and other known coronaviruses",2003,"Journal of Shanghai University","7","2",,"118","123",,,"10.1007/s11741-003-0078-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84867995417&doi=10.1007%2fs11741-003-0078-8&partnerID=40&md5=3542c94a372cde84a5d8f0d3cdf6b56a","Department of Mathematics, Shanghai University, Shanghai 200436, China","Shi, D.-H., Department of Mathematics, Shanghai University, Shanghai 200436, China; Zhou, H.-J., Department of Mathematics, Shanghai University, Shanghai 200436, China; Wang, B.-B., Department of Mathematics, Shanghai University, Shanghai 200436, China; Gu, Y.-H., Department of Mathematics, Shanghai University, Shanghai 200436, China; Wang, Y.-F., Department of Mathematics, Shanghai University, Shanghai 200436, China","In this paper, we report a multiple sequence alignment result on the basis of 10 amino acid sequences of the M protein, which come from different coronaviruses (4 SARS-associated and 6 others known). The alignment model was based on the profile HMM (Hidden Markov Model), and the model training was implemented through the SAHMM (Self-Adapting Hidden Markov Model) software developed by the authors. © 2003 Shanghai University.","corona virus; M (Membrane or Matrix) protein; multiple sequence alignment, profile HMM; SARS (Severe Acute Respiratory Syndrome)",,"Ksiazek, T.G., A novel coronavirus associated with Severe Acute Respiratory Syndrome (2003) The New England Journal of Medicine, , April 10; E'De, Q., A complete sequence and comparative analysis of a SARS-associated virus (isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948. , 10.1360/03wc0186; Durbin, S., (1998) Biological Sequence Analysis: Probabilistic Models of Proteins and Nucleic Acids, , Cambridge University Press London 0929.92010; Schwarz, G., Estimating the dimension of a model (1978) Annuals of Statistics, 6, pp. 461-464. , 0379.62005","Shi, D.-H.; Department of Mathematics, Shanghai University, Shanghai 200436, China; email: shidh2001@263.net",,,10076417,,JSUNF,,"English","J Shanghai Univ",Article,"Final",Open Access,Scopus,2-s2.0-84867995417
"Zhang Y., Xu J.-Y., Deng W., Zhang N., Cai L., Zhao Y., Bu D.-B., Chen R.-S.","36072041800;12777322100;57199965934;56965752900;34767949400;56510664100;7003550200;8587708000;","siRNA designs to the crucial proteins of SARS coronavirus",2003,"Progress in Biochemistry and Biophysics","30","3",,"335","338",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042830820&partnerID=40&md5=edf85c91a8c6296b357b90c1cb97e353","Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China","Zhang, Y., Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Xu, J.-Y., Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Deng, W., Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Zhang, N., Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Cai, L., Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Zhao, Y., Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Bu, D.-B., Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Chen, R.-S., Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, Key Lab. of Intelligent Info. Proc., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China, Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China","RNA interference (RNAi) is the process of sequence-specific, post-transcriptional gene silencing in animals and plants, initiated by double-stranded RNA (dsRNA) that is homologous in sequence to the silenced gene. In mammal cells, small interfering RNA (siRNA) duplexes can induce RNAi potently, which may provide a new approach to the therapeutics of certain diseases. Focusing on the five genes which coding five crucial proteins of SARS coronavirus(SARS-CoV) respectively, 348 siRNA candidate targets were obtained following bioinformatic methods. In theory, potent siRNA duplexes specifically suppress expression of their corresponding SARS-CoV target gene, while have no influence on the normal expression of human gene. It would lay a foundation for the further experimental researches on the siRNA-like drug design for the SARS-CoV.","Bioinformatics; RNA interference (RNAi); SARS coronavirus (SARS-CoV); Small interfering RNA (siRNA)","envelope protein; membrane protein; nucleocapsid protein; RNA; RNA polymerase; spike protein; unclassified drug; virus protein; article; bioinformatics; controlled study; Coronavirus; drug design; gene sequence; gene silencing; nonhuman; pneumonia; RNA sequence; sequence homology; severe acute respiratory syndrome; silencer gene; Animalia; Coronavirus; Mammalia; SARS coronavirus","Kontoyiannis, D.P., Pasqualini, R., Arap, W., Aminopeptidase N inhibitors and SARS (2003) Lancet, 361 (9368), p. 1558; Anand, K., Ziebuhr, J., Wadhwani, P., (2003) Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs, , http://www.sciencemag.org/cgi/rapidpdf/1085658vl; Hammond, S.M., Caudy, A.A., Hannon, G.J., Post-transcriptional gene silencing by double-stranded RNA (2001) Nat Rev Genet, 2 (2), pp. 110-119; Elbashir, S.M., Harborth, J., Lendeckel, W., Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells (2001) Nature, 411 (6836), pp. 494-498; Caplen, N.J., Parrish, S., Imani, F., Specific inhibition of gene expression by small double-stranded RNAs in invertebrate and vertebrate systems (2001) Proc Natl Acad Sci USA, 98 (17), pp. 9742-9747; Jacque, J.M., Triques, K., Stevenson, M., Modulation of HIV-1 replication by RNA interference (2002) Nature, 418 (6896), pp. 435-438; Wilson, J.A., Jayasena, S., Khvorova, A., RNA interference blocks gene expression and RNA synthesis from hepatitis C replicons propagated in human liver cells (2003) Proc Natl Acad Sci USA, 100 (5), pp. 2783-2788; Marra, M.A., Jones, S.J., Astell, C.R., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Qin, E., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Elbashir, S.M., Martinez, J., Patkaniowska, A., Functional anatomy of siRNAs for mediating efficient RNAi in Drosophila melanogaster embryo lysate (2001) Embo J, 20 (23), pp. 6877-6888; Altschul, S.F., Madden, T.L., Schaffer, A.A., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res, 25 (17), pp. 3389-3402; Novina, C.D., Murray, M.F., Dykxhoorn, D.M., siRNA-directed inhibition of HIV-1 infection (2002) Nat Med, 8 (7), pp. 681-686","Chen, R.-S.; Bioinformatics Laboratory, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; email: crs@sun5.ibp.ac.cn",,,10003282,,,,"English","Prog. Biochem. Biophys.",Article,"Final",,Scopus,2-s2.0-0042830820
"Chen Y.-J., Gao G., Bao Y.-M., Lopez R., Wu J.-M., Cai T., Ye Z.-Q., Gu X.-C., Luo J.-C.","7601429679;35751410900;7202213519;7401491151;55713817900;55626331800;7401957064;7403204103;7404183061;","Initial analysis of complete genome sequences of SARS coronavirus",2003,"Acta Genetica Sinica","30","6",,"493","500",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038787989&partnerID=40&md5=f7c55fe99db897a20d1de68a12fe5a27","College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; European Bioinformatics Institute, Hinxton CB101 SD, United Kingdom","Chen, Y.-J., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Gao, G., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Bao, Y.-M.; Lopez, R., European Bioinformatics Institute, Hinxton CB101 SD, United Kingdom; Wu, J.-M., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Cai, T., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Ye, Z.-Q., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Gu, X.-C., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; Luo, J.-C., College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China","Multiple sequence alignment among 12 complete SARS coronavirus (SARS-CoV) sequences reveals that the major parts of 29708 b of the genomes have 99.82% identical bases. Forty two nucleotide mismatches were found in addition to the five and six gaps in two genomes. Among them, 28 mismatches result in changes of amino acid in the encoded proteins. Analysis of the changes implies possible effect on the Spike and Membrane protein of the virus, while most of the other changes seem not very significant to alter the structure and function of the proteins. These results have been released on the anti-sars web site maintained by the Centre of Bioinformatics, Peking University (antisars.cbi.pku.edu.cn) and may be of help for further experimental study.","Bioinformatics; Multiple sequence alignment; SARS coronavirus; Sequence analysis","membrane protein; protein; signal peptide; spike protein; unclassified drug; virus protein; alpha helix; amino acid sequence; article; base mispairing; base pairing; bioinformatics; China; Coronavirus; gene sequence; image analysis; Internet; multiple sequence alignment; nonhuman; nuclear localization signal; nucleotide sequence; protein conformation; protein function; protein localization; protein secondary structure; protein structure; respiratory distress; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; structure activity relation; virus genome; Amino Acid Sequence; Coronavirus; Genome, Viral; Molecular Sequence Data; SARS Virus; Sequence Alignment; Sequence Homology, Amino Acid; Viral Proteins; Coronavirus; SARS coronavirus","Sanger, F., Air, G.M., Barrell, B.G., Brown, N.L., Coulson, A.R., Fiddes, C.A., Hutchison, C.A., Smith, M., Nucliotide sequence of bacteriophage phi X174 DNA (1977) Nature, 265, pp. 687-695; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J Gen Virol, 82 (PART 6), pp. 1273-1281; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv Virus Res, 48, pp. 1-100; Siddell, S.G., The small-membrane protein The Coronaviridae, pp. 181-189. , S. G. Siddell (ed.). Plenum Press, New York, N. Y; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J Virol, 68, pp. 6523-6534; Krijnse-Locker, J., Ericsson, M., Rottier, P.J., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J Cell Biol, 124, pp. 55-70; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucl Acids Res, 22, pp. 4673-4680; Sonnhammer, E.L., Von Heijne, G., Krogh, A., A hidden Markov model for predicting transmembrane helices in protein sequences (1998) Proc Int Conf Intell Syst Mol Biol, 6, pp. 175-182; McGuffin, L.J., Bryson, K., Jones, D.T., The PSIPRED protein structure prediction server (2000) Bioinformatics, 16 (4), pp. 404-405; Eddy, S.R., Multiple alignment using hidden Markov models (1995) Proc Int Conf Intell Syst Mol Biol, 3, pp. 114-120; Nakai, K., Horton, P., PSORT: A program for detecting the sorting signals of proteins and predicting their subcellular localization (1999) Trends Biochem Sci, 24, pp. 34-35; Bateman, A., Birney, E., Cerruti, L., Durbin, R., Etwiller, L., Eddy, S.R., Griffiths-Jones, S., Sonnhammer, E.L., The Pfam protein families database (2002) Nucl Acids Res, 30, pp. 276-280; Krueger, D.K., Kelly, S.M., Lewicki, D.N., Ruffolo, R., Gallagher, T.M., Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion (2001) J Virol, 75, pp. 2792-2802; Das Sarma, J., Fu, L., Tsai, J.C., Weiss, S.R., Lavi, E., Demyelination determinants map to the spike glycoprotein gene of coronavirus mouse hepatitis virus (2000) J Virol, 74, pp. 9206-9213; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J Virol, 72, pp. 9628-9636; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J Virol, 73, pp. 7607-7618; Navas, S., Seo, S.H., Chua, M.M., Sarma, J.D., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J Virol, 75, pp. 2452-2457; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acid of the murine coronavirus spike protein (1994) J Virol, 68, pp. 5403-5410; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J Virol, 8, pp. 6523-6534; Krijnse-Locker, J., Ericsson, M., Rottier, P.J., Griffiths, G., Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step (1994) J Cell Biol, 124, pp. 55-70; Ruan, Y.J., Wei, C.L., Ee, L.A., Vega B. V, Thoreau, H., Yun, S.T.S., Chia, J.M., Liu, E.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) The Lancet?, , Published online 9 May; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, , Published online 13 May; De Qin, E., Zhu, Q., Ya, M., A complete sequence and comparative analysis of SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48, pp. 941-948; Zhang, W.-G., Li, J.-Q., Zhou, H.-M., Genomic characterization of SARS coronavirus: A novel member of coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 501-508","Chen, Y.-J.; College of Life Sciences, Natl. Lab. of Protein Engineering, Peking University, Beijing 100871, China; email: luojc@pku.edu.cn",,,03794172,,ICHPC,"12939792","Chinese; English","Acta Genet. Sin.",Article,"Final",,Scopus,2-s2.0-0038787989
"Meng X., Hu F., Qiu Q.-H., Ye X., Liang M., Chen H.-Z.","57214788077;55187144300;57198354047;8121561400;22997810400;8121561600;","Strategy for siRNA based gene therapy of SARS",2003,"Chinese Pharmacological Bulletin","19","7",,"723","726",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042161799&partnerID=40&md5=6649f7836ca1c84fc7fe972a0d5eda70","Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China; Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China","Meng, X., Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China, Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China; Hu, F., Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China; Qiu, Q.-H., Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China, Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China; Ye, X., Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China, Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China; Liang, M., Shanghai Sunway Biotech Co., Ltd., Shanghai 201206, China; Chen, H.-Z., Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China","A newly discovered member of the coronavirus family has been considered to be the cause of severe acute respiratory syndrome (SARS). There are no effective drugs for cure and prevention of this syndrome at this moment. Based on the known genomic sequences of coronavirus, the authors oropose here a plasmid vector expressed siRNA strategy for SARS gene therapy. Aerosol delivery of plasmid DNA to the lungs offers the possibility for direct application of gene preparations to pulmonary surfaces, especially in conjunction with polyethyleneimine (PEI, a polycationic polymer). The complexes of PEI-DNA may result in a specific high level of pulmonary transfection and resolve the two key difficulties of SiRNA both in delivering and targeting. This strategy might show great potential for SARS gene therapy.","Aerosol delivery; Coronavirus; PEI; Severe acute respiratory syndrome (SARS); SiRNA","plasmid DNA; plasmid vector; polycation; polyethyleneimine; polymer; recombinant RNA; aerosol; article; Coronavirus; drug targeting; gene sequence; gene targeting; genetic transfection; human; lung; nonviral gene delivery system; nonviral gene therapy; severe acute respiratory syndrome; virus gene; virus pneumonia","Chinese source; Soe, L.H., Shieh, C.K., Makino, S., Murine coronavirus 5′-end genomic RNA sequence reveals mechanism of leader-primed transcription (1987) Adv Exp Med Biol, 218, pp. 73-81; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) The Lancet, 361, pp. 1779-1785; Anand, K., Ziebuhr, J., Wadhwani, P., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, , epub ahead of print May; Kontoyiannis, D.P., Pasqualini, R., Arap, W., Aminopeptidase N inhibitors and SARS (2003) The Lancet, 361, p. 1558; Abbas-Terki, T., Blanco-Bose, W., Deglon, N., Lentiviral-mediated RNA interference (2002) Hum Gene Ther, 13, pp. 2197-2201; Barton, G.M., Medzhitov, R., Retroviral delivery of small interfering RNA into primary cells (2002) Proc Natl Acad Sci USA, 99, pp. 14943-14945; Xia, H., Mao, Q., Paulson, H.L., Davidson, B.L., siRNA-mediated gene silencing in vitro and in vivo (2002) Nat Biotechnol, 20, pp. 1006-1010; Shen, C., Buck, A.K., Liu, X., Gene silencing by adenovirus-delivered siRNA (2003) FEBS Lett, 539 (1-3), pp. 111-114; Lewis, D.L., Hagstrom, J.E., Loomis, A.G., Efficient delivery of siRNA for inhibition of gene expression in postnatal mice (2002) Nat Genet, 32, pp. 107-108; Herweijer, H., Wolff, J.A., Progress and prospects: Naked DNA gene transfer and therapy (2003) Gene Ther, 10, pp. 453-458; McCaffrey, A.P., Nakai, H., Pandey, K., Inhibition of hepatitis B virus in mice by RNA interference (2003) Nat Biotechnol, p. 12; McCaffrey, A.P., Meuse, L., Pham, T.T., RNA interference in adult mice (2002) Nature, 418, pp. 38-39; Song, E., Lee, S.K., Wang, J., RNA interference targeting Fas protects mice from fulminant hepatitis (2003) Nat Med, 9, pp. 347-351; Zhang, G., Budker, V., Wolff, J.A., High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA (1999) Hum Gene Ther, 10, pp. 1735-1737; Gautam, A., Waldrep, J.C., Densmore, C.L., Aerosol gene therapy (2003) Mol Biotechnol, 23, pp. 51-60; Boussif, O., Lezoualc'h, F., Zanta, M.A., A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: Polyethylenimine (1995) Proc Natl Acad Sci USA, 92, pp. 7297-7301; Kichler, A., Leborgne, C., Coeytaux, E., Danos, O., Polyethylenimine-mediated gene delivery: A mechanistic study (2001) J Gene Med, 3, pp. 135-144; Densmore, C.L., Orson, F.M., Xu, B., Aerosol delivery of robust polyethyleneimine-DNA complexes for gene therapy and genetic immunization (2000) Mol Ther, 1, pp. 180-188; Gautam, A., Densmore, C.L., Xu, B., Waldrep, J.C., Enhanced gene expression in mouse lung after PEI-DNA aerosol delivery (2000) Mol Ther, 2, pp. 63-70; Gautam, A., Densmore, C.L., Golunski, E., Transgene expression in mouse airway epithelium by aerosol gene therapy with PEI-DNA complexes (2001) Mol Ther, 3, pp. 551-556; Trubetskoy, V.S., Wong, S.C., Subbotin, V., Recharging cationic DNA complexes with highly charged polyanions for in vitro and in vivo gene delivery (2003) Gene Ther, 10, pp. 261-267; Elbashir, S.M., Harborth, J., Lendeckel, W., Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells (2001) Nature, 411, pp. 494-498","Meng, X.; Dept. of Pharmacology, Shanghai Second Medical University, Shanghai 200025, China; email: xmeng00@hotmail.com",,"Publication Centre of Anhui Medical University",10011978,,ZYTOE,,"Chinese","Chin. Pharmacol. Bull.",Article,"Final",,Scopus,2-s2.0-0042161799
"Shen X., Xue J.-H., Yu C.-Y., Luo H.-B., Qin L., Yu X.-J., Chen J., Chen L.-L., Xiong B., Yue L.-D., Cai J.-H., Shen J.-H., Luo X.-M., Chen K.-X., Shi T.-L., Li Y.-X., Hu G.-X., Jiang H.-L.","7402721498;36829897400;7404977287;55454058600;55245249200;57196944646;55717786100;57139000400;57206173804;7101974838;7403153214;7404929839;7402871196;26643583800;7202756564;35227517800;7401490443;34868049700;","Small envelope protein E of SARS: Cloning, expression, purification, CD determination, and bioinformatics analysis",2003,"Acta Pharmacologica Sinica","24","6",,"505","511+620",,30,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-12444316030&partnerID=40&md5=57417d3d42cb4d0feb52be196aaedee7","Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shanghai Health Digit Limited, Shanghai 200233, China; Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China; Bioinformation Center, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Inst. of Biochem. and Cell Biology, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China","Shen, X., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Xue, J.-H., Shanghai Health Digit Limited, Shanghai 200233, China; Yu, C.-Y., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, H.-B., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Qin, L., Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China; Yu, X.-J., Bioinformation Center, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Chen, J., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Chen, L.-L., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Xiong, B., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Yue, L.-D., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Cai, J.-H., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shen, J.-H., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, X.-M., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Chen, K.-X., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shi, T.-L., Bioinformation Center, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Li, Y.-X., Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China, Bioinformation Center, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Hu, G.-X., Inst. of Biochem. and Cell Biology, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Jiang, H.-L., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China","AIM: To obtain the pure sample of SARS small envelope E protein (SARS E protein), study its properties and analyze its possible functions. METHODS: The plasmid of SARS E protein was constructed by the polymerase chain reaction (PCR), and the protein was expressed in the E coli strain. The secondary structure feature of the protein was determined by circular dichroism (CD) technique. The possible functions of this protein were annotated by bioinformatics methods, and its possible three-dimensional model was constructed by molecular modeling. RESULTS: The pure sample of SARS E protein was obtained. The secondary structure feature derived from CD determination is similar to that from the secondary structure prediction. Bioinformatics analysis indicated that the key residues of SARS E protein were much conserved compared to the E proteins of other coronaviruses. In particular, the primary amino acid sequence of SARS E protein is much more similar to that of murine hepatitis virus (MHV) and other mammal coronaviruses. The transmembrane (TM) segment of the SARS E protein is relatively more conserved in the whole protein than other regions. CONCLUSION: The success of expressing the SARS E protein is a good starting point for investigating the structure and functions of this protein and SARS coronavirus itself as well. The SARS E protein may fold in water solution in a similar way as it in membrane-water mixed environment. It is possible that β-sheet I of the SARS E protein interacts with the membrane surface via hydrogen bonding, this β-sheet may uncoil to a random structure in water solution.","Bioinformatics; Circular dichroism spectroscopy; Gene expression; Severe acute respiratory syndrome (SARS); Small envelope protein","envelope protein e; membrane protein; unclassified drug; virus protein; water; amino acid sequence; article; bacterial strain; beta sheet; bioinformatics; circular dichroism; Coronavirus; Escherichia coli; gene expression; Hepatitis virus; hydrogen bond; molecular cloning; molecular model; nonhuman; nucleotide sequence; plasmid; polymerase chain reaction; protein analysis; protein expression; protein folding; protein function; protein purification; protein secondary structure; SARS coronavirus; severe acute respiratory syndrome; virus infection; Circular Dichroism; Computational Biology; Coronavirus 229E, Human; Coronavirus, Bovine; Coronavirus, Canine; Humans; Models, Molecular; Murine hepatitis virus; Protein Conformation; Protein Structure, Secondary; SARS Virus; Sequence Alignment; Sequence Homology, Amino Acid; Severe Acute Respiratory Syndrome; Viral Envelope Proteins","Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science (Sciencexpress), , May 1; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., The genome sequence of the SARS-associated coronavirus (2003) Science (Sciencexpress), , May 1; Siddell, S.G., The coronaviridae: An introduction (1995) The Coronaviridae, pp. 1-10. , Siddell SG, editor. New York: Plenum Press; Tung, F.Y., Abraham, S., Sethna, M., Hung, S.L., Sethna, P., Hogue, B.G., The 9-kDa hydrophobic protein encoded at the 3'end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated (1992) Viroolgy, 186, pp. 676-683; Maeda, J., Repass, J.R., Maeda, A., Makino, S., Membrane topology of coronavirus E protein (2001) Virology, 281, pp. 163-169; Bos, E.C.W., Luytjes, W., Van der Meulen, H., Koerten, H.K., Spaan, W.J.M., The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus (1996) Virology, 218, pp. 52-60; Vennema, H., Godeke, G.J., Rossen, J.W.A., Voorhout, M.F., Horzinek, M.C., Opstelten, D.J.E., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J, 15, pp. 2020-2028; (2000) Sybyl [Molecular Modeling Package], Version 6.8, , St. Louis (MO): Tripos Associates; Kirpatrick, S., Gelatt, C.D., Vecchi, M.P., Optimization by simulated annealing (1983) Science, 220, pp. 671-680; Cornell, W.D., Cieplak, P., Bayly, C.I., Gould, I.R., Merz, K.M., A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (1995) J Am Chem Soc, 117, pp. 5179-5197; Tieleman, D.P., Berendsen, H.J.C., Sansom, M.S.P., An alamethicin channel in a lipid bilayer: Molecular dynamics simulations (1999) Biophys J, 76, pp. 1757-1769; Godet, M., Haridon, R.L., Vautherot, J.F., Laude, H., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virion (1992) Virol, 188, pp. 666-675; Kuo, L., Masters, P.S., The small envelope protein E is not essential for murine coronavirus replication (2003) J Virol, 77, pp. 4597-4608; An, S.W., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis Inducer J (1999) Virol, 73, pp. 7853-7859; Raamsman, J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J Virol, 74, pp. 2333-2342; Anderson, A.M., Melin, L., Bean, A., Pettersson, R.F., A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein (1997) J Virol, 71, pp. 4717-4727","Shen, X.; Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China",,,16714083,,CYLPD,"12791175","English","Acta Pharmacol. Sin.",Article,"Final",,Scopus,2-s2.0-12444316030
"Rentz E.J.","6602407502;","Viral pathogens and severe acute respiratory syndrome: Oligodynamic Ag + for direct immune intervention",2003,"Journal of Nutritional and Environmental Medicine","13","2",,"109","118",,20,"10.1080/13590840310001594061","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141638733&doi=10.1080%2f13590840310001594061&partnerID=40&md5=b560448d9748ba96bbf57d1b0d33d5d6","Physical Medicine Services, 3939 Hollywood Blvd, Hollywood, FL, United States","Rentz, E.J., Physical Medicine Services, 3939 Hollywood Blvd, Hollywood, FL, United States","This retrospective study of silver-based therapeutics briefly reviews their history, and then explores the modern application of charged silver particles, especially as an antiviral agent. The recent outbreak of severe acute respiratory syndrome (SARS) suggests this is timely. Medical literature shows that a variety of viruses have been successfully treated with silver-based drugs. However, 'silver salts' and/or inferior silver preparations lack the bio-availability, active silver content and safety needed to be effective. State-of-the-art, electrolytically produced 'oligodynamic' Ag +, however, offers distinct advantages and versatility of use over older and cruder formulations. Possessing much smaller, subnanometer-sized particles, greater electrical potential and lower concentrations, it is more bio-available than other formulations. Efficacy against the SARS-related coronavirus, for example, may be enhanced when nebulized Ag+ is inhaled. This should achieve swift reduction of viral loads, especially in the early stages. Moreover, there is no known toxicity for Oligodynamic Ag + in humans. The only known mechanism of resistance also appears to play no role notwithstanding the mutability of the coronavirus. Therefore no functional barrier to the virotoxic effects of oligodynamic Ag+ may be expected regardless of the rapidity or variety of mutations.","Antiviral spectrum; Biocompatibility; Capsid; NASA-commissioned studies; Oligodynamic Ag+ pharmacokinetics; Oligodynamic colloidal silver; Protein-based viral envelope; SARS-related coronavirus; Silver speciation; Viral resistance","collargol; oligodynamic silver ion; silver derivative; silver nitrate; sulfadiazine silver; unclassified drug; adsorption; antibiotic resistance; antimicrobial activity; antiviral activity; colloid; Coronavirus; dissociation constant; drug formulation; drug research; electricity; history of medicine; human; nonhuman; particle size; priority journal; respiratory tract infection; review; severe acute respiratory syndrome; upper respiratory tract infection; virus infection; virus resistance; Apus apus; Coronavirus; RNA viruses","Bechhold, H., (1919) Colloids in Biology and Medicine, pp. 364-376. , New York: D. van Nostrand; Clayton, G.D., Clayton, F.E., (1981) Patty's Industrial Hygiene and Toxicology, 3rd Rev. 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New York: Reinhold; Voigt, J., Das Kolloide Silver (1929) Leopzig, pp. 12ff; Crocker, J.C., Grier, D.G., Interactions and dynamics in charge-stabilized colloid (1998) MRS Bull, 23, pp. 24-31; Vukovic, V.V., Nedeljkovic, J.M., Surface modification of nanometer-scale silver particles by imidazole (1993) Langmuir, 9 (4), p. 980; Zhu, X., (2003) Ag+ Concentration Determination of Argentyn 23, , Miami: Department of Marine Biology, University of Miami; Dasmahapatra, R., The Important Dots to Know about the Coronavirus Family, , http://www.stanford.edu/group/virus/corona/virushome.html; Zhang, Z.-Y., Zinc inhibition of renin and the protease from human immunodeficiency virus type 1 (1991) Biochemistry, 30 (36), p. 8719; Cliver, D.O., Foell, W.K., Goepfert, J.M., Biocidal effects of silver (1971) Contract NAS 9-9300 Final Technical Report, pp. 4-1. , University of Wisconsin, Accession Number N71 24436, NASA CR Number CR-114978, February; Milder, US Patent no. 5,322,520, 21 June 1994; Liboff, (1989), US Patent no. 4,818,697, 4 April; Hink, J., Jansen, E., Are superoxide and/or hydrogen peroxide responsible for some of the beneficial effects of hyperbaric oxygen therapy? (2001) Med Hypotheses, 57 (6), pp. 764-769; Baugh, M.A., HIV: Reactive oxygen species, enveloped viruses and hyperbaric oxygen (2000) Med Hypotheses, 55 (3), pp. 232-238; Van Den Blink, B., Van Der Kleij, A.J., Versteeg, H.H., Peppelenbosch, M.P., Immunomodulatory effect of oxygen and pressure (2002) Comp Biochem Physiol A Mol Integr Physiol, 132 (1), pp. 193-197; Patrick, T.R., Manning, G.T., Oforsagd, P.A., Trapp, W.G., The correction of severe hypoxemia in adult respiratory distress syndrome with hyperbaric oxygenation (OHP) (1970) Chest, 58 (5), pp. 483-490; Reillo, M.R., Hyperbaric oxygen therapy for the treatment of debilitating fatigue associated with HIV/AIDS (1993) J Assoc Nurses AIDS Care, 4 (3), pp. 33-38; Rogatskii, G.G., Effect of hyperbaric oxygenation on the corticosterone content of the blood in experimental acute respiratory distress syndrome (1989) Biull Eksp Biol Med, 107 (5), pp. 545-547; Lustbader, D., Fein, A., Other modalities of oxygen therapy: Hyperbaric oxygen, nitric oxide, and ECMO (2000) Respir Care Clin North Am, 6 (4), pp. 659-674","Rentz, E.J.; Physical Medicine Services, 3939 Hollywood Blvd, Hollywood, FL, United States",,,13590847,,JNEMF,,"English","J. Nutr. Environ. Med.",Review,"Final",Open Access,Scopus,2-s2.0-0141638733
"Nakajima N., Asahi-Ozaki Y., Nagata N., Sato Y., Dizon F., Paladin F.J., Olveda R.M., Odagiri T., Tashiro M., Sata T.","7402488141;6507132678;11839905700;7410374839;6506926370;6603790170;6701313494;36057355100;7201482415;7202653089;","SARS coronavirus-infected cells in lung detected by new in situ hybridization technique",2003,"Japanese Journal of Infectious Diseases","56","3",,"139","141",,29,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141519172&partnerID=40&md5=83f37e0ee887626b1f7bea07b10991e6","Research Institute for Tropical Med., Muntiniupa City, Philippines; Department of Virology III, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan","Nakajima, N., Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Asahi-Ozaki, Y., Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Nagata, N., Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Sato, Y., Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Dizon, F., Research Institute for Tropical Med., Muntiniupa City, Philippines; Paladin, F.J., Research Institute for Tropical Med., Muntiniupa City, Philippines; Olveda, R.M., Research Institute for Tropical Med., Muntiniupa City, Philippines; Odagiri, T., Department of Virology III, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Tashiro, M., Department of Virology III, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; Sata, T., Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan",[No abstract available],,"CD68 antigen; virus antibody; virus antigen; adult; article; autopsy; case report; Coronavirus; female; fluorescence analysis; gene sequence; genetic analysis; histopathology; human; human tissue; immunohistochemistry; in situ hybridization; oligonucleotide probe; pathogenesis; reverse transcription polymerase chain reaction; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; virus detection; virus isolation; virus pneumonia; virus replication; Female; Humans; In Situ Hybridization; Lung; Middle Aged; RNA, Viral; SARS Virus","Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Ng, W.F., Leung, C.Y., Chu, C.M., Hui, P.K., Peiris, J.S.M., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Nakajima, N., Ionescu, P., Sata, Y., Hashimoto, M., Kuroita, T., Takahashi, H., Yoshikura, H., Sata, T., In situ hybridization AT-tailing with catalyzed signal amplification for sensitive and specific in situ detection of human immunodeficiency virus-1 mRNA in formalin-fixed and paraffin-embedded tissues (2003) Am. J. Pathol., 162, pp. 381-389","Sata, T.; Department of Pathology, National Inst. of Infectious Dis., Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan; email: tsata@nih.go.jp",,,13446304,,JJIDF,"12944688","English","Jpn. J. Infect. Dis.",Article,"Final",,Scopus,2-s2.0-0141519172
"Poon L.L.M., Wong O.K., Luk W., Yuen K.Y., Peiris J.S.M., Guan Y.","7005441747;56672516300;57213310994;36078079100;7005486823;7202924055;","Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS)",2003,"Clinical Chemistry","49","6",,"953","955",,99,"10.1373/49.6.953","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038697628&doi=10.1373%2f49.6.953&partnerID=40&md5=d7fed569163722a058a7954848a8811e","Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong","Poon, L.L.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Wong, O.K., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Luk, W., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Guan, Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong",[No abstract available],,"adult; aged; antibody titer; article; clinical article; clinical feature; controlled study; Coronavirus; coughing; diagnostic procedure; female; gene mutation; human; lung infiltrate; male; monitoring; nucleotide sequence; pneumonia; polymerase chain reaction; respiratory tract disease; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; Adult; Aged; Female; Humans; Male; Middle Aged; Reproducibility of Results; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sensitivity and Specificity; Severe Acute Respiratory Syndrome; Virology; Coronavirus; SARS coronavirus","Acute respiratory syndrome (2003) Wkly Epidemiol Rec, 78, pp. 73-74; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; (2003) Severe Acute Respiratory Syndrome (SARS) - Multi-Country Outbreak - Update 15, , http://www.who.int/csr/don/2003_03_31/en; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., A coronavirus is associated with severe acute respiratory syndrome (SARS) (2003) Lancet, , http://www.thelancet.com/journal/vol361/iss9365/ full/llan.361.9365.early_online_publication.25296.1, Published online April 8, 2003; McIntosh, K., Coronaviruses: A comparative review (1974) Curr Top Microbiol Immunol, 63, pp. 85-112; Hruskova, J., Heinz, F., Svandova, E., Pennigerova, S., Antibodies to human coronaviruses 229E and 0C43 in the population of C. R. (1990) Acta Virol, 34, pp. 346-352; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morbid Mortal Wkly Rep, 52, pp. 269-272; Lipsky, R.H., Mazzanti, C.M., Rudolph, J.G., Xu, K., Vyas, G., Bozak, D., DNA melting analysis for detection of single nucleotide polymorphisms (2001) Clin Chem, 47, pp. 635-644; Drosten, C., Günther, S., Preiser, W., Van Der Werf, S., Brodt, H., Becker, S., Identification of a novel coronavirus in Patients with severe acute respiratory syndrome (2003) N Engl J Med, , http://content.nejm.org/cgi/content/abstract/ NEJMoaQ30747v2, published online April 10, 2003","Poon, L.L.M.; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; email: llmpoon@hkucc.hku.hk",,,00099147,,CLCHA,"12765993","English","Clin. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0038697628
"McIntosh K.","35248570900;","The SARS coronavirus: Rapid diagnostics in the limelight",2003,"Clinical Chemistry","49","6",,"845","846",,11,"10.1373/49.6.845","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038021279&doi=10.1373%2f49.6.845&partnerID=40&md5=7256d3f96e763917ec9af8895aecd256","Department of Pediatrics, Children's Hospital, Harvard Medical School, Boston, MA 02115, United States","McIntosh, K., Department of Pediatrics, Children's Hospital, Harvard Medical School, Boston, MA 02115, United States",[No abstract available],,"immunoglobulin M antibody; virus RNA; antibody detection; Coronavirus; developing country; diagnostic accuracy; early diagnosis; editorial; human; nonhuman; polymerase chain reaction; respiratory tract disease; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; technology; virus diagnosis; Humans; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome; Virology; Coronavirus; SARS coronavirus","Updated Interim U.S. Case Definition of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/casedefinition.htm; Pooh, L.L.M., Wong, O.K., Luk, W., Yuen, K.Y., Peiris, J.S.M., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, p. 49. , Published online April 18, 2003; Pieris, P.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Lim, W., Nicholls, J., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, p. 361. , http://image.thelancet.com/extras/03art3477web.pdf, Published online April 8, 2003; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, p. 348. , http://content.nejm.org/cgi/reprint/NEJMoa030781v3.pdf, Published online April 10, 2003; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.-R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, p. 348. , http://content.nejm.org/cgi/content/abstract/ NEJMoa030747v2, Published online April 10, 2003; Outbreak of severe acute respiratory syndrome - Worldwide (2003) MMWR Morb Mprtal Wkly Rep, 52, pp. 226-228; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc Soc Exp Biol Med, 121, pp. 190-193; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common-cold virus in organ cultures (1965) Br Med J, 1, pp. 1467-1470; McIntosh, K., Dees, J.H., Becker, W.B., Kapikian, A.Z., Chanock, R.M., Recovery in tracheal organ cultures of novel viruses from patients with respiratory disease (1967) Proc Natl Acad Sci U S A, 57, pp. 933-940; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, p. 348. , http://content.nejm.org/cgi/reprint/NEJMoa030634v3.pdf, Published online March 31, 2003; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, p. 348. , http://content.nejm.org/cgi/reprint/NEJMoa030666v3.pdf, Published online March 31, 2003; Bradburne, A.F., Bynoe, M.L., Tyrrell, D.A.J., Effects of a ""new"" human respiratory virus in volunteers (1967) Br Med J, 3, pp. 767-769","McIntosh, K.; Department of Pediatrics, Children's Hospital, Harvard Medical School, Boston, MA 02115, United States",,,00099147,,CLCHA,"12765977","English","Clin. Chem.",Editorial,"Final",Open Access,Scopus,2-s2.0-0038021279
[No author name available],[No author id available],"Does SARS coronavirus originate from animals?",2003,"Chinese Medical Journal","116","6",,"826","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037560102&partnerID=40&md5=ae7e82e3a8c6d619043233bf106a52d8",,"",[No abstract available],,"amino acid sequence; cat; Coronavirus; disease carrier; gene mapping; genetic code; human; nonhuman; note; reverse transcription polymerase chain reaction; SARS coronavirus; sequence homology; serology; severe acute respiratory syndrome; virus isolation; virus pneumonia; Animals; Carnivora; SARS Virus",,,,,03666999,,CMDJA,"12959142","English","Chin. Med. J.",Note,"Final",,Scopus,2-s2.0-0037560102
"Guery B., Alfandari S., Leroy O., Georges H., D'Escrivan T., Kipnis E., Mouton Y., Yazdanpanah Y.","20834455400;56220476800;25954361600;35916487000;14621455000;55919191300;7102933618;7004429065;","Severe acute respiratory syndrome [Syndrome respiratoire aigu sévère]",2003,"Medecine et Maladies Infectieuses","33","6",,"281","286",,,"10.1016/S0399-077X(03)00200-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037804100&doi=10.1016%2fS0399-077X%2803%2900200-2&partnerID=40&md5=e50bcabfd05c10837d296210a96a4b82","Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Serv. Regl. de Malad. Infect./Trop., CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France","Guery, B., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Alfandari, S., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Leroy, O., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Georges, H., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; D'Escrivan, T., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Kipnis, E., Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Mouton, Y., Serv. Regl. de Malad. Infect./Trop., CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; Yazdanpanah, Y., Serv. Regl. de Malad. Infect./Trop., CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France","In the Fall of 2002 a report from Guangdong Province in China showed the occurrence of an outbreak of atypical pneumonia. This outbreak rapidly progressed from China to Hong Kong, Singapore, Toronto, and the USA, to more than 25 countries worldwide and almost 3500 cases to date in april 2003. The clinical features associate a fever with mild respiratory symptoms which can progress to a typical acute respiratory distress syndrome requiring intensive care unit admission. Enteric forms with diarrhea were recently described in Hong Kong. The medical community responded very rapidly and united in front of this major health crisis. In a couple weeks, the agent, a new Coronavirus was isolated, therapeutic guidelines were proposed and measures to limit the outbreak diffusion were started worldwide. We summarize here the history of the outbreak, the clinical, laboratory and radiological features of SARS. April 2003 therapeutic guidelines are also reported. © 2003 Publié par Éditions scientifiques et médicales Elsevier SAS.","Coronavirus; Pneumonia; SARS","Canada; China; clinical feature; Coronavirus; diarrhea; disease activity; disease association; disease course; disease severity; disease transmission; epidemic; fever; Hong Kong; hospital admission; human; incidence; infection rate; intensive care; laboratory test; pneumonia; practice guideline; radiography; respiratory distress syndrome; respiratory tract infection; review; severe acute respiratory syndrome; Singapore; United States; virus isolation","Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52 (11), pp. 226-228; Preliminary clinical description of severe acute respiratory syndrome (2003) MMWR Morb Mortal Wkly Rep, 52 (12), pp. 255-256; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, , sous presse; Peiris, J., Mai, S., Poon, L., Guan, Y., Yam, L., Nicholls, J., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, p. 361. , Online April 8; Drosten, C., Gunther, S., Preiser, W., Van Der, W.S., Brodt, H.R., Becker, S., Identification of a novel Coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , sous presse; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., A novel Coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, , sous presse; Hofmann, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell culture (1988) J Clin Microbiol, 26 (11), pp. 2235-2239; Treanor, J., Falsey, A., Respiratory viral infections in the elderly (1999) Antiviral Res, 44 (2), pp. 79-102; Gagneur, A., Legrand, M.C., Picard, B., Baron, R., Talbot, P.J., De Parscau, L., Nosocomial infections due to human coronaviruses in the newborn (2002) Arch Pediatr, 9 (1), pp. 61-69; Sizun, J., Soupre, D., Legrand, M.C., Giroux, J.D., Rubio, S., Cauvin, J.M., Neonatal nosocomial respiratory infection with Coronavirus: A prospective study in a neonatal intensive care unit (1995) Acta Paediatr, 84 (6), pp. 617-620; Folz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115 (3), pp. 901-905; Fukutomi, T., Tsunemitsu, H., Akashi, H., Detection of bovine coronaviruses from adult cows with epizootic diarrhea and their antigenic and biological diversities (1999) Arch Virol, 144 (5), pp. 997-1006; Perlman, S., Pathogenesis of Coronavirus-induced infections. Review of pathological and immunological aspects (1998) Adv Exp Med Biol, 440, pp. 503-513; Haring, J., Perlman, S., Mouse hepatitis virus (2001) Curr Opin Microbiol, 4 (4), pp. 462-466; Musher, D.M., How contagious are common respiratory tract infections? (2003) N Engl J Med, 348 (13), pp. 1256-1266; Moser, M.R., Bender, T.R., Margolis, H.S., Noble, G.R., Kendal, A.P., Ritter, D.G., An outbreak of influenza aboard a commercial airliner (1979) Am J Epidemiol, 110 (1), pp. 1-6; Earhart, K.C., Beadle, C., Miller, L.K., Pruss, M.W., Gray, G.C., Ledbetter, E.K., Outbreak of influenza in highly vaccinated crew of U.S. Navy ship (2001) Emerg Infect Dis, 7 (3), pp. 463-465; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , sous presse; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , sous presse; Harpold, L.M., Legendre, A.M., Kennedy, M.A., Plummer, P.J., Millsaps, K., Rohrbach, B., Fecal shedding of feline Coronavirus in adult cats and kittens in an Abyssinian cattery (1999) JAmVetMedAssoc, 215 (7), pp. 948-951; Borio, L., Inglesby, T., Peters, C.J., Schmaljohn, A.L., Hughes, J.M., Jahrling, P.B., Hemorrhagic fever viruses as biological weapons: Medical and public health management (2002) JAMA, 287 (18), pp. 2391-2405","Guery, B.; Reanimation Med./Malad. Infectieuses, CH de Tourcoing, 135, rue Président-Coty, 59208 Tourcoing, France; email: bguery@invivo.ed",,"Elsevier Masson SAS",0399077X,,MMAIB,,"French","Med. Mal. Infect.",Review,"Final",,Scopus,2-s2.0-0037804100
"Nassiri R.","15132766400;","Severe acute respiratory syndrome",2003,"Medical Science Monitor","9","6",,"ED25","ED27",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038506832&partnerID=40&md5=51d9055828914a06bee953f7d2e269cb",,"Nassiri, R.","The mysterious severe acute respiratory syndrome (SARS) that has originated from the southern Chinese province of Guangdong appears to be a major public health threat and medical challenge. Laboratory studies of SARS patients in a number of countries identified the etiologic agent being a novel member of coronaviridae. High RNA concentrations of this virus in sputum make it as a highly infectious agent. Low concentrations of viral genome are also detectable in feces. Coronaviruses are ubiquitos. They cause disease in many animals including pigs, cattle, dogs, cats, and chickens. These viruses have been associated with upper respiratory infections and sometimes pneumonia in humans. SARS presents with fever, cough, malaise, dyspnea, and hypoxemia. Chest radiographs from affected regions are associated with progressive airway disease. Clinical laboratory features of SARS include lymphopenia, thrombocytopenia, and elevated lactate dehydrogenase levels. Currently, there is no FDA approved pharmacologic treatment for SARS. To date, no convincing clinical data is available for treatment of SARS with ribavirin. While there are some controversies about the use of systemic corticosteroids, Martin et al, in this issue of MSM, present their views on the use of pentoxyfylline (PTX) as a potential agent to be considered for SARS treatment. Finally, our analytical approach to the risks of SARS will certainly enable us to handle its pandemic spread.",,"corticosteroid; lactate dehydrogenase; pentoxifylline; ribavirin; virus RNA; animal disease; Chinese; clinical feature; Coronavirus; coughing; dyspnea; feces analysis; fever; human; hypoxemia; infection risk; laboratory test; lymphocytopenia; malaise; nonhuman; respiratory tract disease; review; SARS coronavirus; severe acute respiratory syndrome; sputum analysis; thorax radiography; thrombocytopenia; virus genome; virus pneumonia","Peiris, J.S.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) The Lancet, p. 8; Update: Outbreak of severe acute respiratory syndrome - Worldwide 2003 (2003) MMWR, 52 (12), pp. 241-248; Drosten, C., Identification of a novel coronavirus in patients in patients with severe acute respiratory syndrome (2003) N Eng J Med, p. 10; Ksiazck, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Eng J Med, p. 10; Oba, Y., The use of corticosteroids in SARS (2003) N Eng J Med, p. 15; Wenzel, R., Edmond, M., Managing SARS amidst uncertainty (2003) N Eng J Med, p. 15",,,"MSI Medical Science International Publishing",12341010,,MSMOF,"12824956","English","Med. Sci. Monit.",Review,"Final",,Scopus,2-s2.0-0038506832
"Xiong B., Gui C.-S., Xu X.-Y., Luo C., Chen J., Luo H.-B., Chen L.-L., Li G.-W., Sun T., Yu C.-Y., Yue L.-D., Duan W.-H., Shen J.-K., Qin L., Shi T.-L., Li Y.-X., Chen K.-X., Luo X.-M., Shen X., Shen J.-H., Jiang H.-L.","57206173804;7006382172;55706274200;26324947200;55717786100;55454058600;57139000400;55713849700;7402923095;7404977287;7101974838;7102917795;7404930878;55245249200;57206934420;35227517800;26643583800;7402871196;7402721498;7404929839;34868049700;","A 3D model of SARS_CoV 3CL proteinase and its inhibitors design by virtual screening",2003,"Acta Pharmacologica Sinica","24","6",,"497","504+619",,82,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-12444278968&partnerID=40&md5=c526e5eb06e25b00a190447c8cb34932","Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China; Inst. of Biochem. and Cell Biology, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai, 200031, China","Xiong, B., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Gui, C.-S., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Xu, X.-Y., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, C., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Chen, J., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, H.-B., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Chen, L.-L., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Li, G.-W., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Sun, T., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Yu, C.-Y., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Yue, L.-D., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Duan, W.-H., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shen, J.-K., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Qin, L., Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China; Shi, T.-L., Inst. of Biochem. and Cell Biology, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai, 200031, China; Li, Y.-X., Shanghai Ctr. for Bioinfo. Technol., Shanghai 201203, China, Inst. of Biochem. and Cell Biology, Shanghai Inst. for Biol. Sciences, Chinese Academy of Sciences, Shanghai, 200031, China; Chen, K.-X., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Luo, X.-M., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shen, X., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Shen, J.-H., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China; Jiang, H.-L., Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China","AIM: To constructed a three-dimensional (3D) model for the 3C like (3CL) proteinase of SARS coronavirus (SARS_CoV), and to design inhibitors of the 3CL proteinase based on the 3D model. METHODS: Bioinformatics analyses were performed to search the homologous proteins of the SARS_CoV 3CL proteinase from the GenBank and PDB database. A 3D model of the proteinase was constructed by using homology modeling technique. Targeting to the 3D model and its X-ray crystal structure of the main proteinase (Mpro) of transmissible gastroenteritis virus (TGEV), virtual screening was performed employing molecular docking method to identify possible 3CL proteinase inhibitors from small molecular databases. RESULTS: Sequence alignment indicated that the SARS_CoV 3CL proteinase was extremely homologous to TGEV Mpro, especially the substrate-binding pocket (active site). Accordingly, a 3D model for the SARS_CoV 3CL proteinase was constructed based on the crystal structure of TGEV Mpro. The 3D model adopts a similar fold of the TGEV Mpro, its structure and binding pocket feature are almost as same as that of TGEV Mpro. The tested virtual screening indicated that 73 available proteinase inhibitors in the MDDR database might dock into both the binding pockets of the TGEV Mpro and the SARS_CoV 3CL proteinase. CONCLUSIONS: Either the 3D model of the SARS_CoV 3CL proteinase or the X-ray crystal structure of the TGEV Mpro may be used as a starting point for design anti-SARS drugs. Screening the known proteinase inhibitors may be an appreciated shortcut to discover anti-SARS drugs.","3CL proteinase; Bioinformatics; Inhibitors; Molecular modeling; Severe acute respiratory syndrome (SARS); Virtual screening","antivirus agent; proteinase; proteinase inhibitor; article; bioinformatics; Coronavirus; crystal structure; data base; drug design; drug screening; enzyme active site; GenBank; molecular model; nonhuman; nucleotide sequence; protein targeting; SARS coronavirus; structure analysis; Transmissible gastroenteritis virus; X ray crystallography; Computational Biology; Crystallography, X-Ray; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Drug Design; Humans; Models, Molecular; Molecular Structure; Protein Conformation; SARS Virus; Sequence Alignment; Sequence Homology, Amino Acid; Severe Acute Respiratory Syndrome; Structural Homology, Protein; Transmissible gastroenteritis virus","Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science (Sciencexpress), , May 1; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., The genome sequence of the SARS-associated coronavirus (2003) Science (Sciencexpress), , May 1; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra αhelical domain (2002) EMBO J, 21, pp. 3213-3224; (2000) InsightII [Molecular Modeling Package], Version, , Calif (USA): Molecular Simulations Inc; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res, 22, pp. 4673-4680; Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints (1993) J Mol Biol, 234, pp. 779-815; Cornell, W.D., Cieplak, D.P., Bayly, C.I., Gould, I.R., Merz, K.M., Ferguson, D.M., A Second generation force field for the simulation of proteins, nucleic acids, and organic molecules (1995) J Am Chem Soc, 117, pp. 5179-5197; Bowie, J.U., Luthy, R., Eisenberg, D., A method to identify protein sequences that fold into a known three-dimensional structure (1991) Science, 253, pp. 164-170; (2000) Sybyl [Molecular Modeling Package], Version 6.8, , St Louis (MO): Tripos Associates; Muegge, I., Rarey, M., Small molecule docking and scoring (2001) Reviews in Computational Chemistry, 17, pp. 1-60. , Lipkowitz KB, Boyd DB, editors. New York: John Wiley & Sons; Ewing, T., Kuntz, I.D., Critical evaluation of search algorithms for automated molecular docking and database screening (1997) J Comput Chem, 18, pp. 1175-1189; Kuntz, I.D., Structure-based strategies for drug design and discovery (1992) Science, 257, pp. 1078-1082; Gasteiger, J., Marsili, M., Iterative partial equalization of orbital electronegativity-A rapid access to atomic charges (1980) Tetrahedron, 36, pp. 3219-3228; Marsili, M., Gasteriger, J., p charge distribution from molecular topology and p orbital electronegativity (1980) Croat Chem Acta, 53, pp. 601-614; Purcell, W.P., Singer, J.A., Brief review and table of semiempirical parameters used in the Hückel molecular orbital method (1967) J Chem Eng Data, 12, pp. 235-246; Clark, R.D., Strizhev, A., Leonard, J.M., Blake, J.F., Matthew, J.B., Consensus scoring for ligand/protein interactions (2002) J Mol Graph Model, 20, pp. 281-295; Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Automated docking using Lamarckian genetic algorithm and empirical binding free energy function (1998) J Comput Chem, 19, pp. 1639-1662; Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J., Basic local alignment search tool (1990) J Mol Biol, 215, pp. 403-410","Jiang, H.-L.; Drug Discovery and Design Center, Stt. Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai 201203, China",,,16714083,,CYLPD,"12791174","English","Acta Pharmacol. Sin.",Article,"Final",,Scopus,2-s2.0-12444278968
"Bermejo Martín J.F., Jiménez J.L., Muńoz-Fernández M.A.","35274537000;56220681700;25931106800;","Pentoxifylline and severe acute respiratory syndrome (SARS): A drug to be considered",2003,"Medical Science Monitor","9","6",,"SR29","SR34",,30,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037830323&partnerID=40&md5=1cd07f8c804b97a787453664dbe95b10","Immunobiología Molecular, Hospital Gregorio Maranon, Madrid, Spain; Immunobiología Molecular, Hospital Gregorio Maranon, C / Doctor Esquerdo 46, Madrid, 28007, Spain","Bermejo Martín, J.F., Immunobiología Molecular, Hospital Gregorio Maranon, Madrid, Spain; Jiménez, J.L., Immunobiología Molecular, Hospital Gregorio Maranon, Madrid, Spain; Muńoz-Fernández, M.A., Immunobiología Molecular, Hospital Gregorio Maranon, Madrid, Spain, Immunobiología Molecular, Hospital Gregorio Maranon, C / Doctor Esquerdo 46, Madrid, 28007, Spain","The recent outbreak of Severe Acute Respiratory Syndrome (SARS) as a new viral disease is causing a great concern for health authorities and general population. Very little is known about the infectious agent (a coronavirus) and its etiopathogeny, having no specific treatment yet. Proinflammatory cytokines released by stimulated macrophages in the alveoli could have a prominent role in pathogenesis of SARS. Current treatment of SARS with antiviral agents such as ribavirin and corticosteroids have not achieved very satisfactory results. Corticosteroids exert an antiinflammatory effect and are indicated for the treatment of respiratory distress, but, in the other hand, they exert an immunosupresor effect on humoral and cellular arms of Immune System. Based on previous reports and on our own experience in HIV, we propose here pentoxifylline (PTX), a drug commonly used in vascular indications, as a possible treatment for SARS due to its interesting properties. PTX would feature a possible antiviral activity along with a well-known cytokine-modulating activity not as immunosupresant as that of the corticoids, down-regulating proinflammatory cytokines but leaving functional the rest of the immune response. Other effects of PTX are discused, as bronchodilation. Conclusions: The antiinflammatory, antiviral, immunomodulatory and bronchodilatory effects of PTX, along with its low cost and toxicity, make it a promising drug to be considered for SARS treatment, alone or as an adjuvant therapy in combination with other drugs. The classical antiviral approach as single treatment for viral diseases should be reviewed in this occasion; immunomodulatory therapies could play an important role in SARS therapy.","Antiviral; Bronchodilation; Immunomodulation; Inflammation; Pentoxifylline; SARS","antiinflammatory agent; antivirus agent; bronchodilating agent; corticosteroid; cytokine; dexamethasone; immunosuppressive agent; pentoxifylline; phosphodiesterase IV inhibitor; prednisone; ribavirin; rolipram; adjuvant therapy; antiviral activity; article; asthma; bronchodilatation; cell stimulation; cellular immunity; clinical trial; Coronavirus; cytokine release; down regulation; drug absorption; drug cost; drug elimination; drug formulation; drug indication; drug mechanism; drug transformation; headache; human; Human immunodeficiency virus; humoral immunity; immune response; immunosuppressive treatment; leishmaniasis; lung alveolitis; lung alveolus; lung infection; macrophage; nausea; nonhuman; pathogenesis; respiratory distress; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; stomach acid secretion; stomach disease; treatment contraindication; treatment indication; vertigo; virus pneumonia; vomiting; Antiviral Agents; Humans; Intestinal Absorption; Models, Biological; Pentoxifylline; Pneumocystis Infections; SARS Virus; Severe Acute Respiratory Syndrome; Vasodilator Agents","Nicholls, J.M., Poon, L.L.M., Lee, C.K., Lung pathology of fatal severe acute respiratory syndrome (2003) The Lancet, 36, p. 9370. , http://image.thelancet.com/extras/03art4347web.pdf; Amvros'eva, T.V., Votiakov, V.I., Andreeva, O.T., New properties of trental as an inhibitor of viral activity with a wide range of activity (1993) Vopr Virusol, 38, pp. 230-233; Vasil'ev, V.S., Pron'ko, N.V., Use of trental in combined treatment of viral hepatitis (1990) Klin Med, 68 (3), pp. 68-70; Navarro, J., Punzon, M.C., Pizarro, A., Pentoxifylline inhibits acute HIV-1 replication in human T cells by a mechanism not involving inhibition of tumour necrosis factor synthesis or nuclear factor-kappa B activation (1996) AIDS, 10 (5), pp. 469-475; Navarro, J., Punzon, M.C., Jimenez, J.L., Inhibition of phosphodiesterase type IV suppresses human immunodeficiency virus type I replication and cytokine production in primary T cells: Involvement of NF-kappaB and NFAT (1998) J Virol, 72, pp. 4712-4720; Biswas, D.K., Dezube, B.J., Ahlers, C.M., Pardee, A.B., Pentoxifylline inhibits HIV-1 LTR-driven gene expression by blocking NF-kappa B action (1993) J Acquir Immune Defic Syndr, 6 (7), pp. 778-786; Clerici, M., Piconi, S., Balotta, C., Pentoxifylline improves cell-mediated immunity and reduces human immunodeficiency virus (HIV) plasma viremia in asymptomatic HIV-seropositive persons (1997) J Infect Dis, 17, pp. 1210-1215; Staak, K., Prosch, S., Stein, J., Pentoxifylline promotes replication of human cytomegalovirus ill vivo and in vitro (1997) Blood, 89, pp. 3682-3690; Shirabe, S., Nakamura, T., Tsujino, A., Successful application of pentoxifylline in the treatment of HTLV-I associated myelopathy (1997) J Neurol Sci, 151 (1), pp. 97-101; Alarcón-Guzmán, T., Alarcón-Avilés, T., Treatment of Tropical Spastic Paraparesis with Pentoxifylline: Pilot Study, , http://www.medicosecuador.com/revecautneurol/vol11_n1-2_2002/tratamiento_de_ la.htm, Article in Spanish; Fujimoto, T., Nakamura, T., Furuya, T., Relationship between the clinical efficacy of pentoxifylline treatment and elevation of serum T helper type P cytokine levels in patients with human T-lymphotropic virus type 1-associated myelopathy (1999) K Intern Med, 38 (9), pp. 717-721; Entzian, P., Bitter-Suermann, S., Burdon, D., Differences in the anti-inflammatory effects of theophylline and pentoxifylline: Important for the development of asthma therapy? (1998) Allergy, 53 (8), pp. 749-754; Kuznetsova, V.K., Zhdanov, V.F., Yakovleva, N.G., Kuzubova, N.A., Dynamics of airflow limitation in bronchial asthmatic patients after trental therapy (1997) Pulmonology, p. 7. , http://www.pulmonology.ru/sum-97-4.htm; Vassallo, R., Standing, J.E., Andrew, H.L., Isolated pneumocystis carinii cell wall glucan provokes lower respiratory tract inflammatory responses (2000) The J of Immunology, 164, pp. 3755-3763; Entzian, P., Gerlach, C., Gerdes, J., Pentoxifylline inhibits experimental bleomycin-induced fibrosing alveolitis (1997) Pneumologie, 51 (4), pp. 375-380; Ardizzoia, A., Lissoni, P., Tancini, G., Respiratory distress syndrome in patients with advanced cancer treated with pentoxifylline: A randomized study (1993) Support Care Cancer, 1 (6), pp. 313-313; Korber, M., Kamp, S., Kothe, H., Pentoxifylline inhibits secretion of O2- and TNF-alpha by alveolar macrophages in patients with sarcoidosis (1995) Immun Infekt, 23 (3), pp. 107-110; Balibrea, J.L., Arias-Diaz, J., Garcia, C., Vara, E., Effect of pentoxifylline and somatostatin on tumor necrosis factor production by human pulmonary macrophages (1994) Circ Shock, 43 (2), pp. 51-56; Lessa, H.A., Machado, P., Lima, F., Successful treatment of refractory mucosal leishmaniasis with pentoxifylline plus antimony (2000) Am J Trop Med Hyg, 65 (9), pp. 87-89; Giembycz, M.A., Development status of second generation PDE4 inhibitors for asthma and COPD: The story so far (2002) Monaldi Arch Chest Dis, 57, pp. 48-64; Williams, B.R.G., Sen, G.C., A viral on/off switch for interferon (2003) Science, 300, pp. 1100-1101; Vazquez Garcia, M.J., Vargas Camano, M.E., Olalde Carmona, R., Use of pentoxifylline in pediatric patients with grade IV (OMS) lupus nephropathy who have received multiple treatments (2000) Rev Alerg Mex, 47 (3), pp. 109-114; Streppel, M., Wittekindt, C., Von Wedel, H., Progressive hearing loss in hearing impaired children: Immediate results of antiphlogistic-rheologic infusion therapy (2001) Int J Pediatr Otorhinolaryngol, 57 (2), pp. 129-136","Muńoz-Fernández, M.A.; Immunobiología Molecular, Hospital Gregorio Maranon, C / Doctor Esquerdo 46, Madrid, 28007, Spain; email: mmunoz@cbm.uam.es",,,12341010,,MSMOF,"12824965","English","Med. Sci. Monit.",Article,"Final",,Scopus,2-s2.0-0037830323
"Erles K., Toomey C., Brooks H.W., Brownlie J.","6602971504;6603812108;7102230646;7005541438;","Detection of a group 2 coronavirus in dogs with canine infectious respiratory disease",2003,"Virology","310","2",,"216","223",,113,"10.1016/S0042-6822(03)00160-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037482847&doi=10.1016%2fS0042-6822%2803%2900160-0&partnerID=40&md5=eb5dc88f9bafd6e57231d443c62e62db","Dept. of Pathol./Infectious Diseases, Royal Veterinary College, London, United Kingdom; Royal Veterinary College, Dept. of Pathol./Infectious Diseases, Hawkshead Lane, North Mymms, Hatfield, AL9 7TA, United Kingdom","Erles, K., Dept. of Pathol./Infectious Diseases, Royal Veterinary College, London, United Kingdom, Royal Veterinary College, Dept. of Pathol./Infectious Diseases, Hawkshead Lane, North Mymms, Hatfield, AL9 7TA, United Kingdom; Toomey, C., Dept. of Pathol./Infectious Diseases, Royal Veterinary College, London, United Kingdom; Brooks, H.W., Dept. of Pathol./Infectious Diseases, Royal Veterinary College, London, United Kingdom; Brownlie, J., Dept. of Pathol./Infectious Diseases, Royal Veterinary College, London, United Kingdom","An investigation into the causes of canine infectious respiratory disease was carried out in a large rehoming kennel. Tissue samples taken from the respiratory tract of diseased dogs were tested for the presence of coronaviruses using RT-PCR with conserved primers for the polymerase gene. Sequence analysis of four positive samples showed the presence of a coronavirus with high similarity to both bovine and human coronavirus (strain OC43) in their polymerase and spike genes, whereas there was a low similarity to comparable genes in the enteric canine coronavirus. This canine respiratory coronavirus (CRCV) was detected by RT-PCR in 32/119 tracheal and 20/119 lung samples, with the highest prevalence being detected in dogs with mild clinical symptoms. Serological analysis showed that the presence of antibodies against CRCV on the day of entry into the kennel decreased the risk of developing respiratory disease. © 2003 Elsevier Science (USA). All rights reserved.","Canine respiratory disease; Coronavirus; Kennel cough","animal model; article; cattle; clinical feature; comparative study; controlled study; Coronavirus; dog; enteric virus; gene; lung; nonhuman; nucleotide sequence; prevalence; priority journal; respiratory tract disease; reverse transcription polymerase chain reaction; risk factor; sample; sequence analysis; spike; structural gene; symptom; tissue slice; virus detection; animal; animal disease; blood; dog disease; genetics; isolation and purification; molecular genetics; phylogeny; respiratory tract infection; trachea; virology; virus infection; Bovinae; Canine coronavirus; Canine respiratory coronavirus; Canis familiaris; Coronavirus; complementary DNA; membrane protein; spike glycoprotein, coronavirus; virus antibody; virus envelope protein; virus hemagglutinin; Animals; Antibodies, Viral; Conserved Sequence; Coronavirus Infections; Coronavirus, Canine; DNA, Complementary; Dog Diseases; Dogs; Genes, pol; Hemagglutinins, Viral; Lung; Membrane Glycoproteins; Molecular Sequence Data; Phylogeny; Respiratory Tract Infections; Reverse Transcriptase Polymerase Chain Reaction; Trachea; Viral Envelope Proteins","Appel, M., Binn, L.N., Canine infectious tracheobronchitis short review: Kennel cough (1987) Virus Infections of Carnivores First Ed., pp. 201-211. , Appel, M. (Ed.), Elsevier Science Publishers, Amsterdam; Appel, M., Percy, D.H., SV-5-like parainfiuenza virus in dogs (1970) J. Am. Vet. Med. Assoc., 156, pp. 1778-1781; Bemis, D.A., Carmichael, L.E., Appel, M.J., Naturally occurring respiratory disease in a kennel caused by Bordetella bronchiseptica (1977) Cornell Vet., 67, pp. 282-293; Bemis, D.A., Greisen, H.A., Appel, M.J., Pathogenesis of canine bordetellosis (1977) J. Infect. Dis., 135, pp. 753-762; Binn, L.N., Alford, J.P., Marchwicki, R.H., Keefe, T.J., Beattie, R.J., Wall, H.G., Studies of respiratory disease in random-source laboratory dogs: Viral infections in unconditioned dogs (1979) Lab. Anim. Sci., 29, pp. 48-52; Binn, L.N., Eddy, G.A., Lazar, E.C., Helms, J., Muruane, T., Viruses recovered from laboratory dogs with respiratory disease (1967) Proc. Soc. Exp. Biol. Med., 126, pp. 140-145; Chilvers, M.A., McKean, M., Rutman, A., Myint, B.S., Silverman, M., O'Callaghan, C., The effects of coronavirus on human nasal ciliated respiratory epithelium (2001) Eur. Respir. J., 18, pp. 965-970; Ditchfield, J., Macpherson, L.W., Zbitnew, A., Association of a canine adenovirus (Toronto A 26/61) with an outbreak of laryngotracheitis (""kennel cough"") (1962) Can. Vet. J., 3, pp. 238-247; Felsenstein, J., PHYLIP-Phylogeny Inference Package (Version 3.2c) (1989) Cladistics, 5, pp. 164-166; Ignjatovic, J., Sapats, S., Avian infectious bronchitis virus (2000) Rev. Sci. Tech., 19, pp. 493-508; Karpas, A., King, N.W., Garcia, F.G., Calvo, F., Cross, R.E., Canine tracheobronchitis: Isolation and characterization of the agent with experimental reproduction of the disease (1968) Proc. Soc. Exp. Biol. Med., 127, pp. 45-52; Keil, D.J., Fenwick, B., Role of Bordetella bronchiseptica in infectious tracheobronchitis in dogs (1998) J. Am. Vet. Med. Assoc., 15, pp. 200-207; Lou, T.Y., Wenner, H.A., Natural and experimental infection of dogs with reovirus, type 1: Pathogenicity of the strain for other animals (1963) Am. J. Hyg., 77, pp. 293-304; Mäikelä, M.J., Puhakka, T., Ruuskanen, O., Leinonen, M., Saikku, P., Kimpimaki, M., Blomqvist, S., Arstila, P., Viruses and bacteria in the etiology of the common cold (1998) J. Clin. Microbiol., 36, pp. 539-542; Page, R.D.M., Treeview: An application to display phylogenetic trees on personal computers (1996) Comput. Appl. Biosci., 12, pp. 357-358; Pearson, W.R., Rapid and sensitive sequence comparison with FASTP and FASTA (1990) Methods Enzymol., 183, pp. 63-98; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Q., 8, pp. 257-261; Randolph, J.F., Moise, N.S., Scarlett, J.M., Shin, S.J., Blue, J.T., Bookbinder, P.R., Prevalence of mycoplasmal and ureaplasmal recovery from tracheobronchial lavages and prevalence of mycoplasmal recovery from pharyngeal swab specimens in dogs with or without pulmonary disease (1993) Am. J. Vet. Res., 54, pp. 387-391; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res., 60, pp. 181-189; Storz, J., Purdy, C.W., Lin, X., Burrell, M., Truax, R.E., Briggs, R.E., Frank, G.H., Loan, R.W., Isolation of respiratory bovine coronavirus, other cytocidal viruses, and Pasteurella spp. from cattle involved in two natural outbreaks of shipping fever (2000) J. Am. Vet. Med. Assoc., 216, pp. 1599-1604; Tennant, B.J., Gaskell, R.M., Jones, R.C., Gaskell, C.J., Studies on the epizootiology of canine coronavirus (1993) Vet. Rec., 132, pp. 7-11; Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Res., 25, pp. 4876-4882","Erles, K.; Royal Veterinary College, Dept. of Pathol./Infectious Diseases, Hawkshead Lane, North Mymms, Hatfield, AL9 7TA, United Kingdom; email: kerles@rvc.ac.uk",,"Academic Press Inc.",00426822,,VIRLA,"12781709","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0037482847
"Pratelli A., Martella V., Decaro N., Tinelli A., Camero M., Cirone F., Elia G., Cavalli A., Corrente M., Greco G., Buonavoglia D., Gentile M., Tempesta M., Buonavoglia C.","7004884960;7003300496;6701636107;6701370203;6701658830;6602223775;7005135633;7101898079;55021372100;7101640307;7004335810;35555538300;7005599031;7005623145;","Genetic diversity of a canine coronavirus detected in pups with diarrhoea in Italy",2003,"Journal of Virological Methods","110","1",,"9","17",,66,"10.1016/S0166-0934(03)00081-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037904573&doi=10.1016%2fS0166-0934%2803%2900081-8&partnerID=40&md5=3051062e18f8c7b964d696fe9baa77c2","Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Dept. of Veterinary Public Health, Polo Universitario dell'Annunziata, Fac. of Vet. Medicine of Messina, Messina, Italy; Service of Medical Genetic, I.R.C.C.S. 'Saverio de Bellis', Castellana Grotte, Bari, Italy","Pratelli, A., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Martella, V., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Decaro, N., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Tinelli, A., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Camero, M., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Cirone, F., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Elia, G., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Cavalli, A., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Corrente, M., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Greco, G., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Buonavoglia, D., Dept. of Veterinary Public Health, Polo Universitario dell'Annunziata, Fac. of Vet. Medicine of Messina, Messina, Italy; Gentile, M., Service of Medical Genetic, I.R.C.C.S. 'Saverio de Bellis', Castellana Grotte, Bari, Italy; Tempesta, M., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; Buonavoglia, C., Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy","The sequence of the S gene of a field canine coronavirus (CCoV), strain Elmo/02, revealed low nucleotide (61%) and amino acid (54%) identity to reference CCoV strains. The highest correlation (77% nt and 81.7% aa) was found with feline coronavirus type I. A PCR assay for the S gene of strain Elmo/02 detected analogous CCoVs of different geographic origin, all which exhibited at least 92-96% nucleotide identity to each other and to strain Elmo/02. The evident genetic divergence between the reference CCoV strains and the newly identified Elmo/02-like CCoVs strongly suggests that a novel genotype of CCoV is widespread in the dog population. © 2003 Elsevier Science B.V. All rights reserved.","Coronavirus; Diversity; Dog; Genotype","amino acid sequence; article; Coronavirus; correlation analysis; diarrhea; dog disease; gene sequence; genetic variability; geographic distribution; Italy; nonhuman; nucleotide sequence; polymerase chain reaction; priority journal; sequence homology; strain difference; virus detection; virus gene; virus strain; Canine coronavirus; Canis familiaris; Coronavirus; Felidae; Feline coronavirus","Buonavoglia, C., Marsilio, F., Cavalli, A., Tiscar, P.G., L'infezione da coronavirus del cane: Indagine sulla presenza del virus in Italia (1994) Not. Farm. Vet. Nr. 2/94, ed., , SCIVAC; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, Classification and Nomenclature of Viruses, pp. 835-849. , M.H.V. van Regenmortel, C.M. Fauquet, D.H.L. Bishop, E.B. Carstens, M.K. Estes, S.M. Lemon, J. Maniloff, M.A. Mayo, D.J. McGeoch, C.R. Pringle, & R.B. Wickner. New York: Academic Press; Hall, T.A., BIOEDIT: A user-friendly biological sequence alignment and analysis program for Windows 95/98/NT (1999) Nucl. Acids Symp. Ser., 41, pp. 95-98; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Hingley, S.T., Leparc-Goffart, I., Weiss, R.S., The spike protein of murine coronavirus mouse hepatitis virus strain A59 is not cleaved in primary glial cells and primary hepatocytes (1998) J. Virol., 72, pp. 1606-1609; Horsburgh, B.C., Brown, T.D.K., Cloning, sequencing and expression of the S protein gene from two geographically distinct strains of canine coronavirus (1995) Virus Res., 39, pp. 63-74; Jacobs, L., De Groot, R., Van der Zeijst, B.A.M., Horzinek, M.C., Spaan, W., The nucleotide sequence of the peplomer gene of porcine transmissible gastroenteritis virus (TGEV): Comparison with the sequence of the peplomer protein of feline infectious peritonitis virus (FIPV) (1987) Virus Res., 8, pp. 363-371; Kocherhans, R., Bridgen, A., Ackermann, M., Tobler, K., Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence (2001) Virus Genes, 23, pp. 137-144; Kumar, S., Tamura, K., Jakobsen, I.B., Nei, M., MEGA2: Molecular evolutionary genetics analysis software (2001) Bioinformatics, 17, pp. 1244-1245; Lai, M.M.C., Holmes, K.V., Coronaviridae: The viruses and their replication (2001) Fields Virology, 1, pp. 1163-1185. , D.M. Knipe, P.M. Howley, D.E. Griffin, R.A. Lamb, M.A. Martin, B. Roizman, Strais S.E. Philadelphia: Lippincott Williams and Wilkins; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Pedersen, N.C., Black, J.W., Boyle, J.F., Evermann, J.F., McKeiman, A.J., Ott, R.L., Pathogenic differences between various feline coronavirus isolates (1984) Molecular Biology and Pathogenesis of Coronaviruses, pp. 365-380. , P.J.M. Rottier, B.A.M. van der Zeijst, W.J.M. Spaan, & M.C. Horzinek. New York: Plenum Press; Pratelli, A., Tempesta, M., Greco, G., Martella, V., Buonavoglia, C., Development of a nested PCR for the detection of canine coronavirus (1999) J. Virol. Meth., 80, pp. 11-15; Pratelli, A., Martella, V., Elia, G., Decaro, N., Aliberti, A., Buonavoglia, D., Tempesta, M., Buonavoglia, C., Variation of the sequence in the gene encoding for transmembrane protein M of canine coronavirus (CCV) (2001) Mol. Cell. Probes, 15, pp. 229-233; Pratelli, A., Tinelli, A., Decaro, N., Camero, M., Elia, G., Gentile, A., Buonavoglia, C., PCR assay for the detection and the identification of atypical canine coronavirus in dogs (2002) J. Virol. Meth., 106, pp. 209-213; Pratelli, A., Elia, G., Martella, V., Tinelli, A., Decaro, N., Marsilio, F., Buonavoglia, D., Buonavoglia, C., M gene evolution of canine coronavirus in naturally infected dogs (2002) Vet. Rec., 151, pp. 758-761; Pratelli, A., Martella, V., Pistello, M., Elia, G., Decaro, N., Buonavoglia, D., Camero, M., Buonavoglia, C., Identification of coronaviruses in dogs that segregate separately from the canine coronavirus genotype (2003) J. Virol. Meth., 107, pp. 213-222; Raamsman, M.J.B., Locker, J.K., De Hooge, A., De Vries, A.A.F., Griffiths, G., Vennema, H., Rottier, P.J.M., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Rose, T.M., Schultz, E.R., Henikoff, J.G., Pietrokovski, S., McCallum, C.M., Henikoff, S., Consensus-degenerate hybrid oligonucleotide primers for amplification of distantly related sequences (1998) NAR, 26, pp. 1628-1635; Rottier, P.J.M., The coronavirus membrane protein (1995) The Coronaviridae, pp. 115-139. , S.G. Siddell. New York: Plenum Press; Swofford, D.L., (1998) PAUP*, phylogenetic analysis using parsimony (*and other methods), version 4.0b8, , Sinauer, Sunderland, Mass; Vaughn, E.M., Halbur, P.G., Paul, P.S., Three new isolates of porcine respiratory coronavirus with various pathogenicities and spike (S) gene deletions (1994) J. Clin. Microbiol., 32, pp. 1809-1812; Wesley, R.D., The S gene of canine coronavirus, strain UCD-1, is more closely related to S gene of transmissible gastroenteritis virus than to that of feline infectious peritonitis virus (1999) Virus Res., 61, pp. 145-152; Wesseling, J.G., Vennema, H., Godeke, G., Horzinek, M.C., Rottier, P.J.M., Nucleotide sequence and expression of the spike (S) gene of canine coronavirus and comparison with the S proteins of feline and porcine coronaviruses (1994) J. Gen. Virol., 75, pp. 1789-1794","Pratelli, A.; Dept. of Anim. Health and Well-being, Fac. of Veterinary Medicine of Bari, S.p. per Casamassima km 3, 70010, Valenzano, Bari, Italy; email: a.pratelli@veterinaria.uniba.it",,"Elsevier",01660934,,JVMED,"12757915","English","J. Virol. Methods",Article,"Final",Open Access,Scopus,2-s2.0-0037904573
"Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.","56371191700;7003783935;6602347373;6601999548;7006843618;","Coronavirus main proteinase (3CLpro) Structure: Basis for design of anti-SARS drugs",2003,"Science","300","5626",,"1763","1767",,525,"10.1126/science.1085658","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038120984&doi=10.1126%2fscience.1085658&partnerID=40&md5=0f85cec8d1f102a7b58867729162df73","Institute of Biochemistry, University of Lübeck, D-23538 Lübeck, Germany; Institute of Molecular Biotechnology, D-07745 Jena, Germany; Institute of Virology and Immunology, University of Würzburg, D-97078 Würzburg, Germany; Institute of Molecular Biology, University of Jena, D-07745 Jena, Germany; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany","Anand, K., Institute of Biochemistry, University of Lübeck, D-23538 Lübeck, Germany, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, D-97078 Würzburg, Germany; Wadhwani, P., Institute of Molecular Biology, University of Jena, D-07745 Jena, Germany; Mesters, J.R., Institute of Biochemistry, University of Lübeck, D-23538 Lübeck, Germany, Institute of Molecular Biotechnology, D-07745 Jena, Germany; Hilgenfeld, R., Institute of Biochemistry, University of Lübeck, D-23538 Lübeck, Germany, Institute of Molecular Biotechnology, D-07745 Jena, Germany, Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany","A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] Mpro and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.",,"Crystal structure; Pulmonary diseases; Viruses; Severe acute respiratory syndrome (SARS); Enzymes; proteinase; virus protein; drug development; respiratory disease; virus; article; binding site; Coronavirus; crystal structure; enzyme active site; enzyme structure; molecular interaction; molecular model; nonhuman; porcine coronavirus; priority journal; Rhinovirus; SARS coronavirus; severe acute respiratory syndrome; Transmissible gastroenteritis virus; virus replication; virus strain; Amino Acid Chloromethyl Ketones; Amino Acid Sequence; Antiviral Agents; Binding Sites; Catalytic Domain; Coronavirus 229E, Human; Crystallization; Crystallography, X-Ray; Cysteine Endopeptidases; Cysteine Proteinase Inhibitors; Dimerization; Drug Design; Humans; Isoxazoles; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Pyrrolidinones; Recombinant Proteins; SARS Virus; Sequence Alignment; Sequence Homology, Amino Acid; Severe Acute Respiratory Syndrome; Transmissible gastroenteritis virus; Coronavirus; human coronavirus; Human coronavirus 229E; Rhinovirus; SARS coronavirus; SARS CoV; Suidae; Transmissible gastroenteritis virus","Myint, S.H., (1995) The Coronavirdae, p. 389. , S. G. Siddell, Ed. (Plenum, New York); Drosten, C., (2003) N. Engl. J. Med., 348, p. 1967; Ksiazek, T.G., (2003) N. Engl. J. Med, 348, p. 1953; Lee, N., (2003) N. Engl. J. Med., 348, p. 1986; Herold, J., Raabe, T., Schelle-Prinz, B., Siddell, S.G., (1993) Virology, 195, p. 680; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., (2001) J. Virol., 75, p. 6676; Ziebuhr, J., Herold, J., Siddell, S.G., (1995) J. Virol., 69, p. 4331; Anand, K., (2002) EMBO J., 21, p. 3213; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, p. 853; Hegyi, A., Ziebuhr, J., (2002) J. Gen. Virol., 83, p. 595; Marra, M., (2003) Science, 300, p. 1399. , www.bcgsc.ca/bioinfo/SARS/, 10.1126/science.1085953; Rota, P.A., (2003) Science, 300, p. 1394. , 10.1126science.1085952; Matthews, D.A., (1999) Proc. Natl. Acad. Sci. U.S.A., 96, p. 11000; note; Ziebuhr, J., Heusipp, G., Siddeli, S.G., (1997) J. Virol., 71, p. 3992; note; Siddell, S.G., (1995) The Coronavirdie, p. 1. , S. G. Siddell, Ed. (Plenum, New York); note; note; Hegyi, A., Friebe, A., Gorbalenya, A.E., Ziebuhr, J., (2002) J. Gen. Virol., 83, p. 581; note; Kräussch, H.G., Wimmer, E., (1988) Annu. Rev. Biochem., 57, p. 701; Ryan, M.D., Flint, M., (1997) J. Gen. Virol., 78, p. 699; note","Hilgenfeld, R.; Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany; email: hilgenfeld@biochem.uni-luebeck.de",,,00368075,,SCIEA,"12746549","English","Science",Article,"Final",Open Access,Scopus,2-s2.0-0038120984
"Von Grotthuss M., Wyrwicz L.S., Rychlewski L.","57207893268;6602585943;7005730168;","mRNA Cap-1 methyltransferase in the SARS genome",2003,"Cell","113","6",,"701","702",,81,"10.1016/S0092-8674(03)00424-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038681984&doi=10.1016%2fS0092-8674%2803%2900424-0&partnerID=40&md5=403e1d5370ca4834f9fb99b3978480c6","BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland","Von Grotthuss, M., BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland; Wyrwicz, L.S., BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland; Rychlewski, L., BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland","The 3D jury system has predicted the methyltransferase fold for the nsp13 protein of the SARS coronavirus. Based on the conservation of a characteristic tetrad of residues, the mRNA cap-1 methyltransferase function has been assigned to this protein, which has potential implications for antiviral therapy.",,"messenger RNA; protein nsp13; RNA methyltransferase; unclassified drug; virus protein; article; carboxy terminal sequence; Coronavirus; nonhuman; nucleotide sequence; priority journal; protein function; protein structure; RNA capping; RNA methylation; SARS coronavirus; severe acute respiratory syndrome; three dimensional imaging; virus inhibition; virus pneumonia; virus replication; Coronavirus; RNA viruses; SARS coronavirus","Bach, C., Cramer, A., Scholtissek, C., (1995) J. Gen. Virol., 76, pp. 1025-1032; Bray, M., Raymond, J.L., Geisbert, T., Baker, R.O., (2002) Antiviral Res., 55, pp. 151-159; Bujnicki, J.M., Rychlewski, L., (2001) Genome Biol., 2. , RESEARCH0038; De Clercq, E., (1998) Nucleosides Nucleotides, 17, pp. 625-634; Feder, M., Pas, J., Wyrwicz, L.S., Bujnicki, J.M., (2003) Gene, 302, pp. 129-138; Ginalski, K., Elofsson, A., Fischer, D., Rychlewski, L., (2003) Bioinformatics, 19, pp. 1015-1018; Latner, D.R., Thompson, J.M., Gershon, P.D., Storrs, C., Condit, R.C., (2002) Virology, 301, pp. 64-80; Marchler-Bauer, A., Anderson, J.B., DeWeese-Scott, C., Fedorova, N.D., Geer, L.Y., He, S., Hurwitz, D.I., Lanczycki, C.J., (2003) Nucleic Acids Res., 31, pp. 383-387; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Chan, S.Y., (2003) Science, , 10.11261/science.1085953, in press. Published online May 1 2003; Reinisch, K.M., Nibert, M.L., Harrison, S.C., (2000) Nature, 404, pp. 960-967; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Chen, M.H., Science, in press (2003) Published online, MAY 1, p. 2003. , 10.11261science1055952; Vlot, A.C., Menard, A., Bol, J.F., (2002) J. Virol., 76, pp. 11321-11328; Woyciniuk, P., Linder, M., Scholtissek, C., (1995) Virus Res., 35, pp. 91-99; Wu, X., Guarino, L.A., (2003) J. Virol., 77, pp. 3430-3440","Rychlewski, L.; BioInfoBank Institute, Limanowskiego 24A, 60-744 Poznan, Poland; email: leszek@bioinfo.pl",,"Cell Press",00928674,,CELLB,"12809601","English","Cell",Article,"Final",Open Access,Scopus,2-s2.0-0038681984
"Cinatl J., Morgenstern B., Bauer G., Chandra P., Rabenau H., Doerr H.W.","57216110934;7005523214;55425118700;7202774450;7004984201;7102740671;","Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus",2003,"Lancet","361","9374",,"2045","2046",,441,"10.1016/S0140-6736(03)13615-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038047657&doi=10.1016%2fS0140-6736%2803%2913615-X&partnerID=40&md5=5643588dff721deb23b151f75e141d59","Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany","Cinatl, J., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; Morgenstern, B., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; Bauer, G., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; Chandra, P., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; Rabenau, H., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; Doerr, H.W., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany","The outbreak of SARS warrants the search for antiviral compounds to treat the disease. At present, no specific treatment has been identified for SARS-associated coronavirus infection. We assessed the antiviral potential of ribavirin, 6-azauridine, pyrazofurin, mycophenolic acid, and glycyrrhizin against two clinical isolates of coronavirus (FFM-1 and FFM-2) from patients with SARS admitted to the clinical centre of Frankfurt University, Germany. Of all the compounds, glycyrrhizin was the most active in inhibiting replication of the SARS-associated virus. Our findings suggest that glycyrrhizin should be assessed for treatment of SARS.",,"azauridine; Glycyrrhiza extract; glycyrrhizic acid; mycophenolic acid; pirazofurin; ribavirin; animal cell; antiviral activity; article; concentration response; controlled study; Coronavirus; drug effect; drug efficacy; drug potency; hypertension; hypokalemia; nonhuman; pneumonia; priority journal; SARS coronavirus; severe acute respiratory syndrome; Vero cell; virus adsorption; virus inhibition; virus isolation; virus replication","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med., 348, pp. 1976-1976; Crance, J.M., Scaramozzino, N., Jouan, A., Garin, D., Interferon, ribavirin, 6-azauridine, and glycyrrhizin: Antiviral compounds active against pathogenic flaviviruses (2003) Antiviral Res, 58, pp. 73-79; Jeong, H.G., Kim, J.Y., Induction of inducible nitric oxide synthase expression by 18β-glycyrrhetinic acid in macrophages (2002) FEBS Lett, 513, pp. 208-212; Lin, Y.L., Huang, Y.L., Ma, S.H., Inhibition of Japanese encephalitis virus infection by nitric oxide: Antiviral effect of nitric oxide on RNA virus replication (1997) J Virol, 71, pp. 5227-5235; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 1-9","Cinatl, J.; Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Str 40, D-60596 Frankfurt, Germany; email: cinatl@em.uni-frankfurt.de",,"Elsevier Limited",01406736,,LANCA,"12814717","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0038047657
"Chew F.T., Ong S.Y., Hew C.L.","7102665290;7202336783;55665116900;","Severe acute respiratory syndrome coronavirus and viral mimicry [1]",2003,"Lancet","361","9374",,"2081","",,,"10.1016/S0140-6736(03)13652-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038516447&doi=10.1016%2fS0140-6736%2803%2913652-5&partnerID=40&md5=69f975a4e7b47d14f52bad07bd8d2061","Department of Biological Sciences, National University of Singapore, Science Drive 4, Singapore 117543, Singapore","Chew, F.T., Department of Biological Sciences, National University of Singapore, Science Drive 4, Singapore 117543, Singapore; Ong, S.Y., Department of Biological Sciences, National University of Singapore, Science Drive 4, Singapore 117543, Singapore; Hew, C.L., Department of Biological Sciences, National University of Singapore, Science Drive 4, Singapore 117543, Singapore",[No abstract available],,"complement receptor; Fc receptor; immunoglobulin G; myelin; myelin basic protein; virus antibody; virus protein; antibody specificity; antigen binding; autoimmune disease; cellular immunity; complement system; complex formation; Coronavirus; cross reaction; disease course; endocytosis; Feline panleukopenia virus; host cell; immune response; letter; macrophage; molecular evolution; molecular mimicry; monocyte; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; pathogenesis; priority journal; protein expression; regulatory mechanism; SARS coronavirus; severe acute respiratory syndrome; stereospecificity; T lymphocyte; Transmissible gastroenteritis virus; virus infectivity; virus particle","Oleszak, E.L., Perlman, S., Leibowitz, J.L., MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity (1992) Virology, 186, pp. 122-132; Vennema, H., De Groot, R.J., Harbour, D.A., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J Virol, 64, pp. 1407-1409; Talbot, P.J., Paquette, J.S., Ciurli, C., Antel, J.P., Ouellet, F., Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis (1996) Ann Neurol, 39, pp. 233-240; Burks, J.S., DeVald, B.L., Jankovsky, L.D., Gerdes, J.C., Two coronaviruses isolated from central nervous system tissue of two multiple sclerosis patients (1980) Science, 209, pp. 933-934","Chew, F.T.; Department of Biological Sciences, National University of Singapore, Science Drive 4, Singapore 117543, Singapore; email: dbscft@nus.edu.sg",,"Elsevier Limited",01406736,,LANCA,"12814734","English","Lancet",Letter,"Final",Open Access,Scopus,2-s2.0-0038516447
"Nie Q.-H., Luo X.-D., Hui W.-L.","7005041783;7402867392;8295822300;","Advances in clinical diagnosis and treatment of severe acute respiratory syndrome",2003,"World Journal of Gastroenterology","9","6",,"1139","1143",,23,"10.3748/wjg.v9.i6.1139","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037714984&doi=10.3748%2fwjg.v9.i6.1139&partnerID=40&md5=0a068770eeacf657740a2b090822916b","Chinese PLA Ctr. Diagnosis/Treatment, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; Department of Epidemiology, Chinese People's Armed Police Force, Tianjin 300162, China; Xiao Tang Shan Hospital, Beijing, China","Nie, Q.-H., Chinese PLA Ctr. Diagnosis/Treatment, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China, Xiao Tang Shan Hospital, Beijing, China; Luo, X.-D., Chinese PLA Ctr. Diagnosis/Treatment, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; Hui, W.-L., Department of Epidemiology, Chinese People's Armed Police Force, Tianjin 300162, China","It has been proved that severe acute respiratory syndrome (SARS) is caused by SARS-associated coronavirus, a novel coronavirus. SARS originated in Guangdong Province, the People's Republic of China at the end of 2002. At present, it has spread to more than 33 countries or regions all over the world and affected 8 360 people and killed 764 by May 31, 2003. Identification of the SARS causative agent and development of a diagnostic test are important. Detecting disease in its early stage, understanding its pathways of transmission and implementing specific prevention measures for the disease are dependent upon swift progress. Due to the efforts of the WHO-led network of laboratories testing for SARS, tests for the novel coronavirus have been developed with unprecedented speed. The genome sequence reveals that this coronavirus is only moderately related to other known coronaviruses. WHO established the definitions of suspected and confirmed and probable cases. But the laboratory tests and definitions are limited. Until now, the primary measures included isolation, ribavirin and corticosteroid therapy, mechanical ventilation, etc. Other therapies such as convalescent plasma are being explored. It is necessary to find more effective therapy. There still are many problems to be solved in the course of conquering SARS.",,"amoxicillin plus clavulanic acid; antiinfective agent; clarithromycin; corticosteroid; glucocorticoid; lactate dehydrogenase; levofloxacin; methylprednisolone; polypeptide; prednisolone; ribavirin; clinical examination; clinical feature; convalescence; Coronavirus; coughing; disease classification; disease transmission; dose time effect relation; drug dose regimen; dyspnea; human; laboratory test; lactate dehydrogenase blood level; lung ventilation; molecular dynamics; myalgia; nonhuman; oxygen saturation; plasma transfusion; pneumonia; review; severe acute respiratory syndrome; thorax radiography; virus isolation","Reilley, B., Van Herp, M., Sermand, D., Dentico, N., SARS, Carlo Urbani (2003) N Engl J Med, 348, pp. 1951-1952; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emmery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Falsey, A.R., Walsh, E.E., Novel coronavirus and severe acute respiratory syndrome (2003) Lancet, 361, pp. 1312-1313; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Severe acute respiratory syndrome (SARS) and coronavirus testing-United States, 2003 (2003) Minor Morb Mortal Wkly Rep, 52, pp. 297-302; From the Centers for Disease Control and Prevention. Severe Acute Respiratory Syndrome (SARS) and coronavirus testing-United States, 2003 (2003) JAMA, 289, pp. 2203-2206; Update 31 - Coronavirus never before seen in humans is the cause of SARS http://www.who.int/csr/sarsarchive/2003_04_16/en; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Walmsley, S.L., Detsky, A.S., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, , [epub ahead of print]; Zhong, N.S., The clinical diagnosis and treatment of SARS at present (2003) Zhong Guoyi Xuelun Tanbao, 4, p. 29; Chan-Yeung, M., Yu, W.C., Outbreak of severe acute respiratory syndrome in Hong Kong special administrative region: Case report (2003) BMJ, 326, pp. 850-852; SARS: Laboratory diagnostic tests (2003), http://www.who.int/csr/sars/diagnostictests/en, 29 April; Wong, K.T., Antonio, G.E., Hui, D.S., Lee, N., Yuen, E.H., Wu, A., Leung, C.B., Ahuja, A.T., Severe acute respiratory syndrome: Radiographic appearances and pattern of progression in 138 patients (2003) Radiology, , [epub ahead of print]; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Dye, C., Gay, N., Modeling the SARS Epidemic (2003) Science, , [epub adead of print]; Lipsitch, M., Cohen, T., Cooper, B., Robins, J.M., Ma, S., James, L., Gopalakrishna, G., Murray, M., Transmission dynamics and control of severe acute respiratory syndrome (2003) Science, , [epub ahead of print]; Riley, S., Fraser, C., Donnelly, C.A., Ghani, A.C., Abu-Raddad, L.J., Hedley, A.J., Leung, G.M., Anderson, R.M., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, , [epub ahead of print]; Lipsitch, M., Cohen, T., Cooper, B., Robins, J.M., Ma, S., James, L., Gopalakrishna, G., Murray, M., Transmission dynamics and control of severe acute respiratory syndrome (2003) Science, , [epub ahead of print]; Fisher, D.A., Chew, M.H., Lim, Y.T., Tambyah, P.A., Preventing local transmission of SARS: Lessons from Singapore (2003) Med J Aust, 178, pp. 555-558; Stohr, K., A multicentre collaboration to investigate the cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1730-1733; PCR primers for SARS developed by WHO Network Laboratories (2003), http://www.who.int/csr/sars/primers/en, 17 April; Case definitions for surveillance of severe acute respiratory syndrome SARS http://www.who.int/csr/sars/casedefinition/en; Updated interim U.S. case definition of severe acute respiratory syndrome (SARS) (2003), http://www.cdc.gov/ncidod/sars/diagnosis.htm, May 23; 10:00 PM; So, L.K., Lau, A.C., Yam, L.Y., Cheung, T.M., Poon, E., Yung, R.W., Yuen, K.Y., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Ventilation with lower tidal volumes as compared with traditional tidal volumes for acute lung injury and the acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1301-1308; Allegra, L., Blasi, F., Problems and perspectives in the treatment of respiratory infections caused by atypical pathogens (2001) Pulm Pharmacol Ther, 14, pp. 21-27; Atabai, K., Matthay, M.A., The pulmonary physician in critical care. 5: Acute lung injury and the acute respiratory distress syndrome: Definitions and epidemiology (2002) Thorax, 57, pp. 452-458; Ventilation with lower tidal volumes as compared with traditional tidal volumes for acute lung injury and the acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1301-1308; Cordingley, J.J., Keogh, B.F., The pulmonary physician in critical care. 8: Ventilatory management of ALI/ARDS (2002) Thorax, 57, pp. 729-734; Wong, V.W.S., Dai, D., Wu, A.K.L., Sung, J.J.Y., Treatment of severe acute respiratory syndrome with convalescent plasma H K MJ, , http://www.hkmj.org.hk/hkmj/update/SARS/cr1606.htm; WHO recommendations on SARS and blood safety http://www.who.int/csr/sars/guidelines/bloodsafety/en; Moller, J.C., Schaible, T., Roll, C., Schiffmann, J.H., Bindl, L., Schrod, L., Reiss, I., Gortner, L., Treatment with bovine surfactant in severe acute respiratory distress syndrome in children: A randomized multicentre study (2003) Intensive Care Med, 29, pp. 437-446","Nie, Q.-H.; Chinese PLA Ctr. Diagnosis/Treatment, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; email: nieqinghe@hotmail.com",,"WJG Press",10079327,,WJGAF,"12800213","English","World J. Gastroenterol.",Review,"Final",Open Access,Scopus,2-s2.0-0037714984
"Gillissen A., Ruf B.R.","7005037956;7005835956;","Severe acute respiratory syndrome (SARS) [Das schwere akute atemwegssyndrom (SARS)]",2003,"Medizinische Klinik","98","6",,"319","325",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038113407&partnerID=40&md5=9735d5929d2fc08a38dff3848fb0e7da","Robert-Koch-Klinik, Klinikum St. Georg, Leipzig, Germany; II. Medizinische Klinik, Klinikum St. Georg, Leipzig, Germany; Robert-Koch-Klinik, Klinikum St. Georg, Nikolai-Rumjanzew-Straße 100, 04207 Leipzig, Germany","Gillissen, A., Robert-Koch-Klinik, Klinikum St. Georg, Leipzig, Germany, Robert-Koch-Klinik, Klinikum St. Georg, Nikolai-Rumjanzew-Straße 100, 04207 Leipzig, Germany; Ruf, B.R., II. Medizinische Klinik, Klinikum St. Georg, Leipzig, Germany","Severe acute respiratory syndrome (SAKS) is a viral disease, observed primarily in Southern China in November 2002, with variable flu-like symptoms and pneumonia, in approx. 5% leading to death from respiratory distress syndrome (RDS). The disease was spread over more than 30 states all over the globe by SARS-virus-infected travelers. WHO and CDC received first information about a new syndrome by the end of February 2003, after the first cases outside the Republic of China had been observed. A case in Hanoi, Vietnam, led to the first precise information about the new disease entity to WHO, by Dr. Carlo Urbani, a co-worker of WHO/Doctors without Borders, who had been called by local colleagues to assist in the management of a patient with an unknown severe disease by the end of February 2003. Dr. Urbani died from SARS, as did many other health care workers. In the meantime, more than 7,000 cases have been observed worldwide, predominantly in China and Hong Kong, but also in Taiwan, Canada, Singapore, and the USA, and many other countries, and more than 600 of these patients died from RDS. Since the beginning of March 2003, when WHO and CDC started their activities, in close collaboration with a group of international experts, including the Bernhard-Nocht-Institute in Hamburg and the Department of Virology in Frankfurt/Main, a previously impossible success in the disclosure of the disease was achieved. Within only 8 weeks of research it was possible to describe the infectious agent, a genetically modified coronavirus, including the genetic sequence, to establish specific diagnostic PCR methods and to find possible mechanisms for promising therapeutic approaches. In addition, intensifying classical quarantine and hospital hygiene measures, it was possible to limit SARS in many countries to sporadic cases, and to reduce the disease in countries such as Canada and Vietnam. This review article summarizes important information about many issues of SARS (May 15th, 2003).","Adult respiratory distress syndrome; ARDS; Coronavirus; SARS; Severe acute respiratory syndrome","Canada; cause of death; China; clinical feature; clinical research; Coronavirus; flu like syndrome; gene sequence; history of medicine; Hong Kong; human; infection control; infection rate; international cooperation; nonhuman; polymerase chain reaction; respiratory distress syndrome; review; SARS coronavirus; severe acute respiratory syndrome; Singapore; Taiwan; treatment planning; United States; Viet Nam; virus diagnosis; virus gene; virus pneumonia; virus transmission; world health organization; Canada; Centers for Disease Control and Prevention (U.S.); China; Hong Kong; Humans; Research; Respiratory Distress Syndrome, Adult; Severe Acute Respiratory Syndrome; Singapore; Taiwan; United States; World Health Organization; Coronavirus; SARS coronavirus","Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis of design of anti-SARS drugs (2003) Scienceexpress, , www.sciencexpress.org; Benitez, M.A., Beijing doctor alleges SARS cases cover up in China (2003) Lancet, 391, p. 1357; Preliminary clinical description of severe acute respiratory syndrome (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 255-256; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, L.J., Anderson, K.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, , http://image.thelancet.com/extras/03art4453web.pdf; Drosten, C., Günther, S., Preiser, W., Van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Enserink, M., Vogel, G., Infectious diseases: Deferring competition, global nets closes on SARS (2003) Science, 300, pp. 224-225; Gillissen, A., Höffken, G., Early therapy with neuraminidase inhibitor oseltamivir maximizes its efficacy in influenza treatment (2002) Med Microbiol Immunol (Berl), 191, pp. 165-168; Ho, W., Guideline on management of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1313-1315; Höffken, G., Gillissen, A., Efficacy and safety of zanamivir in patients with influenza - Impact of age, severity of infections and specific risk factors (2002) Med Microbiol Immunol (Berl), 191, pp. 169-173; Holmes, K.V., SARS-associated coronavirus (2003) N Engl J Med, 348, pp. 1948-1951; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peter, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J.Y., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Nguyen-van-Tam, J., Textbook of influenza (1998) Textbook of Influenza, pp. 181-206. , Nicholson KG, Hay AJ, eds. Oxford: Blackwell Science; Nicolaou, S., Al-Nakshabandi, N.A., Muller, N.L., SARS: Imaging of severe acute respiratory syndrome (2003) AJR Am J Roentgenol, 180, pp. 1247-1249; Oba, Y., Lee, N., Sung, J., The use of corticosteroids in SARS (2003) N Engl J Med, 348, pp. 2034-2035; Peiris, J.S., Lai, S.T., Poon, L.T., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Reilley, B., Van Herp, M., Sermand, D., Dentico, N., SARS and Carlo Urbani (2003) N Engl J Med, 348, pp. 1951-1952; Ruan, Y., Wei, C.L., Ee, L.A., Vega, V.B., Thoreau, H., Yun, S.T.S., Chia, J.-M., Liu, E.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, , http://image.thelancet.com/extras/03art4454web.pdf; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Wutzler, P., Kossow, K.-D., Lode, H., Ruf, B., Scholz, H., Vogel, G.E., Antivirale therapie und prophylaxe der influenza (2003) Chemother J, 12, pp. 1-3; Yang, W., Severe acute respiratory syndrome (SARS): Infection control (2003) Lancet, 361, pp. 1386-1387","Gillissen, A.; Robert-Koch-Klinik, Klinikum St. Georg, Nikolai-Rumjanzew-Straße 100, 04207 Leipzig, Germany; email: adrian.gillissen@sanktgeorg.de",,,07235003,,MEKLA,"12811416","German","Med. Klin.",Review,"Final",,Scopus,2-s2.0-0038113407
"Shen S., Wen Z.L., Liu D.X.","7403431806;55630978700;8972667300;","Emergence of a coronavirus infectious bronchitis virus mutant with a truncated 3b gene: Functional characterization of the 3b protein in pathogenesis and replication",2003,"Virology","311","1",,"16","27",,42,"10.1016/S0042-6822(03)00117-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038384949&doi=10.1016%2fS0042-6822%2803%2900117-X&partnerID=40&md5=8f7721b7d38eb75226098bf5a905057a","Inst. of Molecular and Cell Biology, National University of Singapore, Singapore 117604, Singapore; School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore","Shen, S., Inst. of Molecular and Cell Biology, National University of Singapore, Singapore 117604, Singapore; Wen, Z.L., Inst. of Molecular and Cell Biology, National University of Singapore, Singapore 117604, Singapore; Liu, D.X., School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore","The subgenomic RNA 3 of IBV has been shown to be a tricistronic mRNA, encoding three products in IBV-infected cells. To explore if the least expressed ORF, ORF 3b, which encodes a nonstructural protein, is evolutionarily conserved and functionally indispensable for viral propagation in cultured cells, the Beaudette strain of IBV was propagated in chicken embryonated eggs for three passages and then adapted to a monkey kidney cell line, Vero. The 3b gene of passage 3 in embryonated eggs and passages 7, 15, 20, 25, 30, 35 50, and 65 in Vero cells were amplified by reverse transcription-polymerase chain reaction and sequenced. The results showed that viral RNA extracted from passages 35, 50, and 65 contained a single A insertion in a 6A stretch of the 3b gene between nucleotides 24075 and 24080, whereas the early passages carried the normal 3b gene. This insertion resulted in a frameshift event and therefore, if expressed, a C-terminally truncated protein. We showed that the frameshifting product, cloned in a plasmid, was expressed in vitro and in cells transfected with the mutant construct. The normal product of the 3b gene is 64 amino acids long, whereas the frameshifting product is 34 amino acids long with only 17 homogeneous amino acid residues at the N-terminal half. Immunofluorescent studies revealed that the normal 3b protein was localized to the nucleus and the truncated product showed a ""free"" distribution pattern, indicating that the C-terminal portion of 3b was responsible for its nuclear localization. Comparison of the complete genome sequences (27.6 kb) of isolates p20c22 and p36c12 (from passages 20 and 36, respectively) revealed that p36c12 contains three amino acid substitutions, two in the 195-kDa protein (encoded by gene 1) and one in the S protein, in addition to the frameshifting 3b product. Further characterization of the two isolates demonstrated that p36c12 showed growth advantage over p20c22 in both Vero cells and chicken embryos and was more virulent in chicken embryos than p20c22. These results suggest that the 3b gene product is not essential for the replication of IBV. © 2003 Elsevier Science (USA). All rights reserved.",,"amino acid; vitronectin; amino terminal sequence; animal cell; article; Avian infectious bronchitis virus; bronchitis; carboxy terminal sequence; cell culture; comparative study; Coronavirus; frameshift mutation; gene construct; genetic transfection; in vitro study; molecular cloning; nonhuman; nuclear localization signal; nucleotide sequence; pathogenesis; plasmid; priority journal; protein analysis; protein expression; Vero cell; virus isolation; virus replication; Avian infectious bronchitis virus; Coronavirus; Gallus gallus; insertion sequences","Borden, K.L., Campbell Dwyer, E.J., Salvato, M.S., An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm (1998) J. 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Virol., 67 (7), pp. 1435-1442; Cavanagh, D., Brian, D.A., Brinton, M.A., Eujuanes, L., Homles, K.V., Horzinek, M.C., Lai, M.M.C., Talbot, P.J., Nidovirales: A new ordor comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Cavanagh, D., A nomenclature for avian coronavirus isolates and the question of species status (2001) Avian Pathol., 30, pp. 109-115; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathol., 30, pp. 365-378; Cavanagh, D., Mawditt, K., Welchman Dde., B., Britton, P., Gough, R.E., Coronaviruses from pheasants (Phasianus colchicus) are genetically closely related to coronaviruses of domestic fowl (infectious bronchitis virus) and turkeys (2002) Avian Pathol., 31, pp. 81-93; Chen, H., Wurm, T., Britton, P., Brooks, G., Hiscox, J.A., Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell (2002) J. 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Virol., 64, pp. 4784-4791; Shen, S., Burke, B., Desselberger, U., Rearrangement of the VP6 gene of a group A rotavirus in combination with a point mutation affecting trimer stability (1994) J. Virol., 68, pp. 1682-1688; Shen, S., McKee, T.A., Wang, Z.D., Desselberger, U., Liu, D.X., Sequence analysis and in vitro expression of genes 6 and 11 of an ovine group B rotavirus isolates, Kb63: Evidence for a non-defective, C-terminally truncated NSP1 and a phosphorylated NSP5 (1999) J. Gen. Virol., 80, pp. 2077-2085; Shen, S., Kwang, J., Liu, W., Liu, D.X., Determination of the complete nucleotide sequence of a vaccine strain of porcine reproductive and respiratory syndrome virus and identification of the Nsp2 gene with a unique insertion (2000) Arch. Virol., 145, pp. 871-883; Taguchi, F., The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding (1995) J. Virol., 69, pp. 7260-7263; Thiel, V., Siddell, S.G., Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5 (1994) J. Gen. Virol., 75, pp. 3042-3046; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes (1996) EMBO J., 15, pp. 2020-2028; Weiss, S.R., Zoltick, P.W., Leibowitz, J.L., The ns 4 gene of mouse hepatitis virus (MHV), strain A 59 contains two ORFs and thus differs from ns 4 of the JHM and S strains (1993) Arch. Virol., 129, pp. 301-309; Wesley, R.D., Woods, R.D., Cheung, A.K., Genetic basis for the pathogenesis of transmissible gastroenteritis virus (1990) J. Virol., 64, pp. 4761-4766; Wurm, T., Chen, H., Hodgson, T., Britton, P., Brooks, G., Hiscox, J.A., Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division (2001) J. Virol., 75, pp. 9345-9356; Xu, H.Y., Lim, K.P., Shen, S., Liu, D.X., Further identification and characterization of novel intermediate and mature cleavage products released from the ORF 1b region of the avian coronavirus infectious bronchitis virus 1a/1b polyprotein (2001) Virology, 288, pp. 212-222; Yokomori, K., Banner, L.R., Lai, M.M., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Yokomori, K., Lai, M.M., Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins ns4 and ns5a are not essential for murine coronavirus replication (1991) J. Virol., 65, pp. 5605-5608; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Zheng, P., Guo, Y., Niu, Q., Levy, D.E., Dyck, J.A., Lu, S., Sheiman, L.A., Liu, Y., Proto-oncogene PML controls genes devoted to MHC class I antigen presentation (1998) Nature, 396, pp. 373-376","Liu, D.X.; School of Biological Sciences, Nanyang Technological University, 1 Nanyang Walk, Block 5, Singapore 637616, Singapore; email: dxliu@ntu.edu.sg",,"Academic Press Inc.",00426822,,VIRLA,"12832199","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0038384949
"Zhang X., Li H., Zheng K., Chen Q.-X., Wan Z.-Y., Huang J.-C., Zhong H.-J., Zhou H.-Q., Huang P., Znang W.-L., Diao L.-M., Chen J.-D., Zhang Q.-F., Cui J.-M., Huang X.-J., Znahg J.-Q.","35224294000;56986831800;25937079000;7406336372;7101835882;56965768400;23026499100;7404742143;7403658890;6504366769;23988528000;57206953374;8279516600;7401811280;7410248097;6505543119;","Isolation, identification and the variance of a coronavirus from a imputting SARS case",2003,"Chinese Journal of Microbiology and Immunology","23","6",,"409","413",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042065165&partnerID=40&md5=ef3108a5fa864c02f7ca438a2024f31c","Ctr. Dis. Ctrl./Prev. Guangdong P., Guangzhou 510300, China","Zhang, X., Ctr. Dis. Ctrl./Prev. Guangdong P., Guangzhou 510300, China; Li, H.; Zheng, K.; Chen, Q.-X.; Wan, Z.-Y.; Huang, J.-C.; Zhong, H.-J.; Zhou, H.-Q.; Huang, P.; Znang, W.-L.; Diao, L.-M.; Chen, J.-D.; Zhang, Q.-F.; Cui, J.-M.; Huang, X.-J.; Znahg, J.-Q.","Objective: The microbial pathogen of a Severe Acute Respiratory Syndrome (SARS) case from Hongkong was isolated, identified and the variance of SARS association-coronavirus was also studied, so as to lay the foundation for the diagnosis, prevention and treatment of the SARS. Methods: The throat swab from the patient with SARS was inoculated into cell cultures. The isolate was identified by morphology, serology, RT-PCR amplification and partial sequence analysis. Results: A coronavirus (F69) was isolated from the SARS patient. A large quantity of coronavirus-like particles could be observed in the infected cells and supernatants under transmission electron microscope (TEM). Serological assay indicated that the isolated virus was clearly associated with current SARS epidemics. 1635bp of S segments of SARS association-coronaviruses was amplified by RT-PCR and sequenced, sequence analysis showed that the homology of the amplified S fragments to the previously known coronaviruses (HKU, US Urbani and TOR2)was 100%. Compared with GZ01, CUHK and BJ01, there were two nucleotide substitutions in the S protein of F69. Conclusion: There are differences between F69 and coronavirus in Guangzhou. The isolated coronavirus was possibly the key causative agent of SARS.","Atypical pneumonia; Coronavirus; Isolation; S gene; Sequence analysis","virus protein; vitronectin; article; case report; cell culture; Coronavirus; epidemic; gene amplification; Hong Kong; human; human tissue; morphology; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; sequence analysis; serology; severe acute respiratory syndrome; supernatant; throat culture; transmission electron microscopy; virus identification; virus isolation; virus particle","Cumulative Number of Reported Cases (SARS), , http://www.who.int/csr/sarscountry/2003-05-10; SARS Case Fatality Ratio, Incubation Period, , http://www.who.int/csr/sars/2003-05-06; Drosten, C., Günther, S., Preiser, W., Identification of a novel Coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , www.nejm.org, Low-1-low-10 (April 10); Chinese source; Chinese source; Regenmortel, V., (2001) Virus Taxonomy. 7th Ed., , Academic Press; Popova, R., Zhang, X., The spike but not the hemagglutinin/esterase protein of bovine coronavirus is necessary and sufficient for viral infection (2002) Virology, 294, pp. 222-236; Fields, B.N., Knipe, D.M., Howley, P.M., (2001) Virology, , 4th de, Lippincott Williams & Wilkins press, New York","Zhang, X.; Ctr. Dis. Ctrl./Prev. Guangdong P., Guangzhou 510300, China; email: zhangxinhui16@163.com",,,02545101,,ZWMZD,,"Chinese","Chin. J. Microbiol. Immunol.",Article,"Final",,Scopus,2-s2.0-0042065165
"Wu X., Cheng G., Di B., Yin A., He Y., Wang M., Zhou X., He L., Luo K., Du L.","7407060805;57199921434;6602190900;57206130835;7404942268;7406685232;56168504100;27168813800;57205920401;57199308688;","Establishment of a fluorescent polymerase chain reaction method for the detection of the SARS-associated coronavirus and its clinical application",2003,"Chinese Medical Journal","116","7",,"988","990",,9,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042061056&partnerID=40&md5=3798713b39886f0b06e42d6a681db3a3","Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China","Wu, X., Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; Cheng, G., DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China; Di, B., Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; Yin, A., DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China; He, Y., DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China; Wang, M., Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; Zhou, X., DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China; He, L., Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; Luo, K., DA AN Gene Co. LTD., Zhong Shan University, Guangzhou 510089, China; Du, L., Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China","Objective. To establish a fluorescent polymerase chain reaction (F-PCR) method for detecting the coronavirus related to severe acute respiratory syndrome (SARS) and to evaluate its value for clinical application. Methods. The primers and the fluorescence-labeled probe were designed and synthesized according to the published sequence of the SARS-associated coronavirus genes. A F-PCR diagnosis kit for detecting the coronavirus was developed, and 115 clinical nasopharyngeal gargling liquid samples were tested. Results. The sequence of PCR amplified products completely matched the related sequence of the SARS-associated coronavirus genome. Forty-nine out of 67 samples from identified SARS patients and 8 of 18 samples from persons having close contact with SARS patients showed positive results. All 30 samples from healthy controls were negative. Conclusion. The F-PCR method established may be a rapid, accurate and efficient way for screening and for the early diagnosis of SARS patients.","Coronavirus; Nasopharyngeal gargling liquid; Polymerase chain reaction; Severe acute respiratory syndrome","article; controlled study; Coronavirus; diagnostic accuracy; diagnostic kit; diagnostic procedure; diagnostic value; early diagnosis; fluorescence analysis; gargle; gene amplification; gene sequence; genome analysis; human; liquid; molecular probe; nasopharynx; nonhuman; nucleotide sequence; polymerase chain reaction; respiratory tract infection; sampling; SARS coronavirus; screening test; sequence analysis; severe acute respiratory syndrome; virus detection; virus genome; Fluorescence; Humans; Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Livak, K.J., Flood, S.J.A., Marmaro, J., Oligonucleotides with fluorescent dyes at opposite ends provide a quenched probe system useful for detecting PCR product and nucleic acid hybridization (1995) PCR Methods Appl., 4, pp. 357-362; Chen, S., Yee, A., Griffiths, M., The evaluation of a fluorogenic polymerase chain reaction assay for the detection of Salmonella species in food commodities (1997) Int. J. Food. Microbiol., 35, pp. 239-250","Wu, X.; Guangzhou Ctr. for Dis. Ctrl./Prev., Guangzhou 510080, China; email: tom.wu@tom.com",,,03666999,,CMDJA,"12890368","English","Chin. Med. J.",Article,"Final",,Scopus,2-s2.0-0042061056
"Kanjanahaluethai A., Jukneliene D., Baker S.C.","6603130302;6507875957;7403307881;","Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2",2003,"Journal of Virology","77","13",,"7376","7382",,26,"10.1128/JVI.77.13.7376-7382.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037791748&doi=10.1128%2fJVI.77.13.7376-7382.2003&partnerID=40&md5=504a423e9af577ec5b3492a4aad607fc","Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, Maywood, IL, United States; Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand; Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, 2160 S. First Ave., Maywood, IL 60153, United States","Kanjanahaluethai, A., Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, Maywood, IL, United States, Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand; Jukneliene, D., Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, Maywood, IL, United States; Baker, S.C., Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, Maywood, IL, United States, Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, 2160 S. First Ave., Maywood, IL 60153, United States","The replicase polyprotein of murine coronavirus is extensively processed by three proteinases, two papainlike proteinases (PLPs), termed PLP1 and PLP2, and a picornavirus 3C-like proteinase (3CLpro). Previously, we established a trans-cleavage assay and showed that PLP2 cleaves the replicase polyprotein between p210 and membrane protein 1 (MP1) (A. Kanjanahaluethai and S. C. Baker, J. Virol. 74:7911-79, 2000). Here, we report the results of our studies identifying and characterizing this cleavage site. To determine the approximate position of the cleavage site, we expressed constructs that extended various distances upstream from the previously defined C-terminal end of MP1. We found that the construct extending from the putative PLP2 cleavage site at glycine 2840-alanine 2841 was most similar in size to the processed MP1 replicase product generated in a trans-cleavage assay. To determine which amino acids are critical for PLP2 recognition and processing, we generated 14 constructs with amino acid substitutions upstream and downstream of the putative cleavage site and assessed the effects of the mutations in the PLP2 trans-cleavage assay. We found that substitutions at phenylalanine 2835, glycine 2839, or glycine 2840 resulted in a reduction in cleavage of MP1. Finally, to unequivocally identify this cleavage site, we isolated radiolabeled MP1 protein and determined the position of [35S] methionine residues released by Edman degradation reaction. We found that the aminoterminal residue of MP1 corresponds to alanine 2841. Therefore, murine coronavirus PLP2 cleaves the replicase polyprotein between glycine 2840, and alanine 2841, and the critical determinants for PLP2 recognition and processing occupy the P6, P2, and P1 positions of the cleavage site. This study is the first report of the identification and characterization of a cleavage site recognized by murine coronavirus PLP2 activity.",,"alanine; amino acid; BCR ABL protein; glycine; membrane protein; papain like proteinase 1; papain like proteinase 2; phenylalanine; proteinase; RNA directed RNA polymerase; unclassified drug; amino acid substitution; amino terminal sequence; article; carboxy terminal sequence; Coronavirus; enzyme activity; human; human cell; isotope labeling; molecular recognition; mutation; nonhuman; Picornavirus; priority journal; protein degradation; protein processing; Amino Acid Sequence; Base Sequence; Binding Sites; Coronaviridae; DNA Primers; Hela Cells; Humans; Mutagenesis, Site-Directed; Open Reading Frames; Papain; Viral Proteins","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain (2002) EMBO J., 21, pp. 3213-3224; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. Virol., 63, pp. 3693-3699; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M., Identification of the catalytic sites of a papainlike cysteine proteinase of murine coronavirus (1993) J. Virol., 67, pp. 6056-6063; Berry, D.M., Cruickshank, J.G., Chu, H.P., Wells, R.J.H., The structure of infectious bronchitis virus (1964) Virology, 23, pp. 403-407; Bonilla, P.J., Gorbalenya, A.E., Weiss, S.R., Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains (1994) Virology, 198, pp. 736-740; Bonilla, P.J., Hughes, S.A., Weiss, S.R., Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59 (1997) J. Virol., 71, pp. 900-909; Brierley, I., Boursnell, M.E., Binns, M.M., Bilimoria, B., Blok, V.C., Brown, T.D., Inglis, S.C., An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV (1987) EMBO J., 6, pp. 3779-3785; Casals, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., Reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) J. 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Identification of rubiand aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses (1991) FEBS Lett., 288, pp. 201-205; Gosert, R., Kanjanahaluethai, A., Egger, D., Bienz, K., Baker, S.C., RNA replication of mouse hepatitis virus takes place at double-membrane vesicles (2002) J. Virol., 76, pp. 3697-3708; Herold, J., Gorbalenya, A.E., Thiel, V., Schelle, B., Siddell, S.G., Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate (1998) J. Virol., 72, pp. 910-918; Herold, J., Siddell, S.G., Gorbalenya, A.E., A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold (1999) J. Biol. Chem., 274, pp. 14918-14925; Holmes, K.V., Coronaviruses (2001) Fields Virology, 1, pp. 1187-1203. , D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa; Hughes, S.A., Bonilla, P.J., Weiss, S.R., Identification of the murine coronavirus p28 cleavage site (1995) J. Virol., 69, pp. 809-813; Kanjanahaluethai, A., Baker, S.C., Identification of mouse hepatitis virus papain-like proteinase 2 activity (2000) J. Virol., 74, pp. 7911-7921; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lai, M.M.C., Holmes, K.V., Coronaviridae: The viruses and their replication (2001) Fields Virology, 1, pp. 1163-1185. , D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa; Lee, H.J., Shieh, C.K., Gorbalenya, A.E., Koonin, E.V., La Monica, N., Tuler, J., Bagdzhadzhyan, A., Lai, M.M., The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase (1991) Virology, 180, pp. 567-582; Lim, K.P., Liu, D.X., Characterization of the two overlapping papain-like proteinase domains encoded in gene 1 of the coronavirus infectious bronchitis virus and determination of the C-terminal cleavage site of an 87-kDa protein (1998) Virology, 245, pp. 303-312; Lim, K.P., Ng, L.F., Liu, D.X., Identification of a novel cleavage activity of the first papain-like proteinase domain encoded by open reading frame la of the coronavirus avian infectious bronchitis virus and characterization of the cleavage products (2000) J. Virol., 74, pp. 1674-1685; Lu, X., Lu, Y., Denison, M.R., Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59 (1996) Virology, 222, pp. 375-382; Lu, X.T., Sims, A.C., Denison, M.R., Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro (1998) J. Virol., 72, pp. 2265-2271; Lu, Y., Denison, M.R., Determinants of mouse hepatitis virus 3C-like proteinase activity (1997) Virology, 230, pp. 335-342; Lu, Y., Lu, X., Denison, M.R., Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59 (1995) J. Virol., 69, pp. 3554-3559; Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes (1987) J. Biol. Chem., 262, pp. 10035-10038; Pedersen, K.W., Van der Meer, Y., Roos, N., Snijder, E.J., Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex (1999) J. Virol., 73, pp. 2016-2026; Pinon, J.D., Mayreddy, R.R., Turner, J.D., Khan, F.S., Bonilla, P.J., Weiss, S.R., Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes (1997) Virology, 230, pp. 309-322; Pinon, J.D., Teng, H., Weiss, S.R., Further requirements for cleavage by the murine coronavirus 3C-like proteinase: Identification of a cleavage site within ORF1b (1999) Virology, 263, pp. 471-484; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, I.C., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med. [Online], , www.nejm.org, 31 March, posting date; Schiller, J.J., Kanjanahaluethai, A., Baker, S.C., Processing of the coronavirus MHV-JHM polymerase polyprotein: Identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a (1998) Virology, 242, pp. 288-302; Shi, S.T., Schiller, J.J., Kanjanahjaluethai, A., Baker, S.C., Oh, J.W., Lai, M.M., Colocalization and membrane association of murine hepatitis virus gene 1 products and de novo-synthesized viral RNA in infected cells (1999) J. Virol., 73, pp. 5957-5969; Snijder, E.J., Meulenberg, J.J., The molecular biology of arteriviruses (1998) J. Gen. Virol., 79, pp. 961-979; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Yount, B., Denison, M.R., Weiss, S.R., Baric, R.S., Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59 (2002) J. Virol., 76, pp. 11065-11078; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Ziebuhr, J., Thiel, V., Gorbalenya, A.E., The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond (2001) J. Biol. Chem., 276, pp. 33220-33232","Baker, S.C.; Department of Microbiology, Stritch School of Medicine, Loyola University of Chicago, 2160 S. First Ave., Maywood, IL 60153, United States; email: sbaker1@lumc.edu",,,0022538X,,JOVIA,"12805436","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0037791748
"Escors D., Izeta A., Capiscol C., Enjuanes L.","6507259181;6602523425;6507897822;7006565392;","Transmissible gastroenteritis coronavirus packaging signal is located at the 5′ end of the virus genome",2003,"Journal of Virology","77","14",,"7890","7902",,34,"10.1128/JVI.77.14.7890-7902.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038758951&doi=10.1128%2fJVI.77.14.7890-7902.2003&partnerID=40&md5=806b021baaf2cd558af18bc03833ddf2","Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","Escors, D., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Izeta, A., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Capiscol, C., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain; Enjuanes, L., Dept. of Molecular and Cell Biology, Centro Nacional de Biotecnologia, Campus Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain","To locate the transmissible gastroenteritis coronavirus (TGEV) packaging signal, the incorporation of TGEV subgenomic mRNAs (sgmRNAs) into virions was first addressed. TGEV virions were purified by three different techniques, including an immunopurification using an M protein-specific monoclonal antibody. Detection of sgmRNAs in virions by specific reverse transcription-PCRs (RT-PCRs) was related to the purity of virus preparations. Interestingly, virus mRNAs were detected in partially purified virus but not in virus immunopurified using stringent conditions. Analyses by quantitative RT-PCR confirmed that virus mRNAs were not present in highly purified preparations. Lack of sgmRNA encapsidation was probably due to the absence of a packaging signal (ψ) within these mRNAs. This information plus that from the encapsidation of a collection of TGEV-derived minigenomes suggested that ψ is located at the 5′ end of the genome. To confirm that this was the case, a set of minigenomes was expressed that included an expression cassette for an mRNA including the β-glucuronidase gene (GUS) plus variable sequence fragments from the 5′ end of the virus genome potentially including ψ. Insertion of the first 649 nucleotides (nt) of the TGEV genome led to the specific encapsidation of the mRNA, indicating that a ψ was located within this region which was absent from all of the other virus mRNAs. The presence of this packaging signal was further confirmed by showing the expression and rescue of the MRNA including the first 649 nt of the TGEV genome under control of the cytomegalovirus promoter in TGEV-infected cells. This mRNA was successfully amplified and encapsidated, indicating that the first 649 nt of TGEV genome also contained the 5′ cis-acting replication signals. The encapsidation efficiency of this mRNA was about 30-fold higher than the genome encapsidation efficiency, as estimated by quantitative RT-PCR. In contrast, viral mRNAs presented significantly lower encapsidation efficiencies (about 100-fold) than those of the virus genome, strongly suggesting that TGEV mRNAs in fact lacked an alternative TGEV ψ.",,"beta glucuronidase; messenger RNA; virus nucleoprotein; animal cell; article; carboxy terminal sequence; Coronavirus; DNA packaging; gastroenteritis; gene location; nonhuman; priority journal; promoter region; reverse transcription polymerase chain reaction; tissue specificity; virus capsid; virus detection; virus expression; virus genome; virus purification; virus replication; virus transmission; 5' Untranslated Regions; Animals; Base Sequence; Capsid; Cell Line; Genome, Viral; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; RNA, Viral; Signal Transduction; Swine; Transmissible gastroenteritis virus; Virion; Virus Assembly; Virus Replication","Adkins, B., Hunter, T., Identification of a packaged cellular mRNA in virions of Rous sarcoma virus (1981) J. 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"Signorini S., Vonesch N., Di Renzi S., Tomao P., Pera A., Palmi S.","7004590604;6603283337;7801627151;15836153400;35613023200;6602134196;","SARS and occupational risk [SARS e rischio occupazionale]",2003,"Giornale Italiano di Medicina del Lavoro ed Ergonomia","25","SUPPL. 3",,"254","255",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1042267331&partnerID=40&md5=b404ee98348c3e9b182cd4175fd6eef9","ISPESL, Dipartimento Medicina del Lavoro, Italy","Signorini, S., ISPESL, Dipartimento Medicina del Lavoro, Italy; Vonesch, N., ISPESL, Dipartimento Medicina del Lavoro, Italy; Di Renzi, S., ISPESL, Dipartimento Medicina del Lavoro, Italy; Tomao, P., ISPESL, Dipartimento Medicina del Lavoro, Italy; Pera, A., ISPESL, Dipartimento Medicina del Lavoro, Italy; Palmi, S., ISPESL, Dipartimento Medicina del Lavoro, Italy","SARS is an infectious disease caused by a previously unrecognized human coronavirus, called SARS-associated coronavirus (SARS-CoV). Current information indicates that most transmission is via respiratory droplets coming from a person who is symptomatic with SARS (""close contact""). The aim of our study is to evidence the critical role of the family physician, the first health-care worker who cares with suspected/probable SARS patients, underlying the importance of the correct use and management of the personal protective equipment.","Occupational risk; SARS","conference paper; general practitioner; Hong Kong; human; occupational hazard; protective equipment; SARS coronavirus; severe acute respiratory syndrome; Taiwan; Thailand; United States; Viet Nam; virus transmission; Disease Transmission, Patient-to-Professional; Humans; Occupational Diseases; Risk Factors; Severe Acute Respiratory Syndrome","(2003) CDC - MMWR, 52 (12), pp. 241-248; (2003) CDC - MMWR, 52 (19), pp. 433-436; Seto, (2003) Lancet, 361 (9368), pp. 1519-1520","ISPESL, Dipartimento Medicina del LavoroItaly",,,15927830,,GIMLB,"14979174","Italian","G. Ital. Med. Lav. Ergon.",Conference Paper,"Final",,Scopus,2-s2.0-1042267331
"Kaaden O.-R., Essbauer S., Wilhelm S.","7005855283;55941679000;26321611200;","SARS: State of art on epidemiology and aetiology with special regard to environmental resistance of corona-viruses [SARS: Gegenwärtiger stand der epidemiologie und ätiologie unter besonderer berücksichtigung der tenazität von coronaviren]",2003,"Tierarztliche Umschau","58","7",,"339","342",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041877716&partnerID=40&md5=694b8995ed52cdb5f6a3cd127c9b7394","Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, München, Germany; Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, Veterinärstr. 13, 80539 München, Germany","Kaaden, O.-R., Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, München, Germany, Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, Veterinärstr. 13, 80539 München, Germany; Essbauer, S., Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, München, Germany; Wilhelm, S., Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, München, Germany","Severe acute respiratory syndrome SARS was first described in the Guandong area in China in November 2002 as a atypical pneumonia. Since then it spread worldwide to 31 countries with hot spots in China, Asia and Canada. A total of 8.200 individuals was until 26 May affected and about 720 fatalities confirmed. The transmission occurred by a close person-to-person contact via infected droplets and aerosols. The aetiological agent was identified as a novel human coronavirus related to but not identical with any other formerly known human or animal coronavirus. SARS virus could by transmitted to maccace monkeys inducing similar clinical symptoms.",,"airborne infection; article; Asia; Canada; China; communicable disease; Coronavirus; fatality; human; nonhuman; pathogenesis; Pneumovirinae; SARS coronavirus; severe acute respiratory syndrome; virus pneumonia; virus resistance; virus transmission; Animalia; Coronavirus; Pneumovirinae; SARS coronavirus",,"Kaaden, O.-R.; Inst. Med. Mikrobiol., I., Ludwig-Maximilians-Univ. Munchen, Veterinärstr. 13, 80539 München, Germany; email: o.kaaden@lrz.uni-muenchen.de",,,00493864,,,,"German","Tierarztl. Umsch.",Article,"Final",,Scopus,2-s2.0-0041877716
"Sampathkumar P., Temesgen Z., Smith T.F., Thompson R.L.","6603742479;6603577394;7405496656;7406366909;","SARS: Epidemiology, clinical presentation, management, and infection control measures",2003,"Mayo Clinic Proceedings","78","7",,"882","890",,45,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038170225&partnerID=40&md5=8ce210538356b329fd5bdd8a18ee2ee4","Div. of Infect. Dis. and Int. Med., Mayo Clinic, Rochester, MN, United States; Dept. of Lab. Medicine and Pathology, Mayo Clinic, Rochester, MN, United States; Division of Infectious Diseases, Mayo Clinic, 200 First St Sw, Rochester, MN 55905, United States","Sampathkumar, P., Div. of Infect. Dis. and Int. Med., Mayo Clinic, Rochester, MN, United States, Division of Infectious Diseases, Mayo Clinic, 200 First St Sw, Rochester, MN 55905, United States; Temesgen, Z., Div. of Infect. Dis. and Int. Med., Mayo Clinic, Rochester, MN, United States; Smith, T.F., Dept. of Lab. Medicine and Pathology, Mayo Clinic, Rochester, MN, United States; Thompson, R.L., Div. of Infect. Dis. and Int. Med., Mayo Clinic, Rochester, MN, United States","Severe acute respiratory syndrome (SARS) is a recently recognized febrile respiratory illness that first appeared in southern China in November 2002, has since spread to several countries, and has resulted in more than 8000 cases and more than 750 deaths. The disease has been etiologically linked to a novel coronavirus that has been named the SARS-associated coronavirus. It appears to be spread primarily by large droplet transmission. There is no specific therapy, and management consists of supportive care. This article snmmarizes currently available information regarding the epidemiology, clinical features, etiologic agent, and modes of transmission of the disease, as well as infection control measures appropriate to contain SARS.",,"antibiotic agent; corticosteroid; macrolide; methylprednisolone; quinoline derived antiinfective agent; ribavirin; airborne infection; antibiotic therapy; China; clinical feature; Coronavirus; corticosteroid therapy; diagnostic procedure; electrolyte disturbance; epidemic; exposure; fever; hemolytic anemia; hospital care; human; hypokalemia; hypomagnesemia; infection control; morbidity; mortality; outpatient care; respiratory tract disease; SARS coronavirus; screening; severe acute respiratory syndrome; short survey; side effect; virus transmission","Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , www.who.int/csr/sarscountry/2003_04_23/en; Preliminary clinical description of severe acute respiratory syndrome (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 255-256; Updated Interim U.S. Case Definition of Severe Acute Respiratory Syndrome (SARS), , www.cdc.gov/ncidod/sars/casedefinition.htm; Updated interim surveillance case definition for severe acute respiratory syndrome (SARS) - United States, April 29, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 391-393; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Hsu, L.-Y., Lee, C.-C., Green, J.A., Severe Acute Respiratory Syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis [Serial Online], , www.cdc.gov/ncidod/EID/vol9no6/03-0264.htm, June; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809. , http://jama.ama-assn.org/cgi/search?fulltext=greater+toronto+area; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet [Serial Online], , http://image.thelancet.com/extras/03art4432web.pdf, May; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet [Serial Online], , http://image.thelancet.com/extras/03let4127web.pdf, April; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peiris, J.S.M., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science Mag [Serial Online], 300, pp. 1399-1404. , www.sciencemag.org/cgi/content/abstract/1085953v1; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science Mag [Serial Online], 300, pp. 1394-1399. , www.sciencemag.org/cgi/content/abstract/1085952v1; First Data on Stability and Resistance of SARS Coronavirus Compiled by Members of WHO Laboratory Network, , www.who.int/csr/sars/survival_2003_05_04/en/; Severe acute respiratory syndrome - Singapore, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 405-411; Guidelines for Collection of Specimens from Potential Cases of SARS, , www.cdc.gov/ncidod/sars/specimen_collection_sars2.htm; Interim Laboratory Biosafety Guidelines for Handling and Processing Specimens Associated with Severe Acute Respiratory Syndrome (SARS), , www.cdc.gov/ncidod/sars/sarslabguide.htm; So, L.K., Lau, A.C., Yam, L.Y., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617","Sampathkumar, P.; Division of Infectious Diseases, Mayo Clinic, 200 First St Sw, Rochester, MN 55905, United States; email: sampathkumar.priya@mayo.edu",,"Elsevier Ltd",00256196,,MACPA,,"English","Mayo Clin. Proc.",Short Survey,"Final",,Scopus,2-s2.0-0038170225
"Nicastri E., Petrosillo N., Macrì G., Ippolito G.","7004355827;7004966952;6701807694;7102706668;","SARS: The first transmissible disease of 21st century [Severe Acute Respiratory Syndrome: La prima malattia trasmissibile del nuovo secolo]",2003,"Recenti Progressi in Medicina","94","7-8",,"295","303",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041474826&partnerID=40&md5=334188e411b97c5f18b30814f7575183","II Divisione, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, Roma, Italy; Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, II Divisione, Via Portuense, 292, 00149 Roma, Italy","Nicastri, E., II Divisione, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, Roma, Italy; Petrosillo, N., II Divisione, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, Roma, Italy, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, II Divisione, Via Portuense, 292, 00149 Roma, Italy; Macrì, G., II Divisione, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, Roma, Italy; Ippolito, G., II Divisione, Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, Roma, Italy","The Severe Acute Respiratory Syndrome (SARS) is the first severe and easily transmissible disease to emerge in the 21st century. It is caused by the infection with a coronavirus, a single strand RNA capsulated virus, recently found in a small mammalian, the masked palm civet. It is likely to represent the source of human infection. The first cases of SARS have been reported in the Chinese province of Guangdong and, since then, probable cases have been reported world wide. The clinical picture is characterized by nonspecific symptoms such as fever, cough or dyspnea in patients affected by air-space opacities (unifocal involvement in the 54.6% of cases) or distress respiratory syndrome and linked to a recent exposure to a SARS case or to a travel/residence in an affected area. The empirical therapy is based on broad-spectrum antibiotics, steroids and ribavirin, but susceptibility testing have failed to demonstrate direct anti-viral activity of ribavirin against SARS-related coronavirus in vitro. The exposure to respiratory droplets and the contact with biologic fluids (respiratory and gastrointestinal secretions) represent the most efficient transmission modality of the SARS-related coronavirus. Hand hygiene is the most simple and cost effective measure of infection control to prevent contagion, and the use of airborne, contact and droplet precaution is strictly recommended to all health care workers taking care of such patients. The spread of SARS, to less developed country with limited resource for public health programs, represent the emerging alarming threat in the new global scenario.","Antibiotics; Coronavirus; Infectious diseases; Ribavirin; Severe acute respiratory syndrome; Steroids","antibiotic agent; ribavirin; steroid; antibiotic therapy; antiviral activity; China; Coronavirus; coughing; developing country; disease transmission; dyspnea; epidemic; fever; human; hygiene; infection control; mammal; masked palm civet; respiratory distress syndrome; review; SARS coronavirus; severe acute respiratory syndrome; symptomatology; travel; virus pneumonia; Adult; Aged; Algorithms; Antiviral Agents; China; Hong Kong; Humans; Middle Aged; Ribavirin; Severe Acute Respiratory Syndrome; Time Factors; Travel; World Health; World Health Organization","Petersdorf, R.G., Adams, R.D., Braunwald, R., Isselbacher, K.J., Martin, J.B., Wilson, J.D., (1983) Harrison's Principles of Internal Medicine. 10th Ed., , New York: McGraw-Hill; Krause, R.M., (1998) Emerging Infections. Biomedical Research Reports, , New York: Academic Press; Fauci, A., Infectious diseases: Considerations for the 21 st century (2001) Clin Infect Dis, 32, pp. 675-685; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of Severe Acute Respiratory Syndrome in Hong Kong (2003) New Eng Journal Med, 348, pp. 1986-1994. , http://content.nejm.ora/cgi/reprint/NEJMoa030666v3.pdf; Lee, N., Hui, D.A., Wu, A., Major outbreak of Severe Acute Respiratory Syndrome in Hong Kong (2003) New Engl Journal Med, 348, pp. 1977-1985. , http://content.nejm.org/cgi/reprint/NEJMoa030685v1.pdf; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325. , http://image.thelancet.com/extras/03art3477web.pf; Cumulative Number of Reported Probable SARS World-wide, , http://www.who.int/csr/sars/counhv/2008_05_26/en/, Geneva; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, , http://image.thelancet.com/extras/031et4127web.pdf; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with Severe Acute Respiratory Syndrome (2003) New Engl Journal Med, 348, pp. 1953-1966. , http://content.nejm.org/cgi/content/abstract/NEJMoa030781v3; Update: Outbreak of severe acute respiratory syndrome-worldwide, 2003 (2003) MMWR, 52, pp. 241-248; Riley, S., Fraser, C., Donnelly, C.A., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of Public Health interventions (2003) Science, , www.sciencemag.org/cai/content/full/1086478/DC1; Lipsitch, M., Cohen, T., Cooper, B., Transmission dynamics and control of Severe Acute Respiratory Syndrome (2003) Science, , www.sciencemag.org/cgi/content/full/1086616/DC1; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/, Geneva; Ho, W., Guideline on management of severe acute respiratory syndrome (SARS) (2003) Lancet, 361 (9366), pp. 1313-1315. , http://pdf.thelancet.com/pdfdownload?uid=llan.361.9366. editorial_and_review.25371.1&x=x.pdf; Severe Acute Respiratory Syndrome (SARS). Updated Interim Case Definition, , http://www.cdc.gov/ncidod/sars/casedefinition.htm, Atlanta; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289. , http://jama.amaassn.org/cgi/reprint/289.21.JOC30885v1.pdf; Coronavirus Never Before Seen in Humans is the Cause of SARS, , http://www.who.int/mediacentre/releases/2003/pr31/en/, Geneva; Marra, M.A., Jones, S.J., Astell, C.R., The Genome sequence of the SARS-associated coronavirus (2003) Science, , http://www.sciencemag.org/cgi/rapidpdf/1085953v1; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origine of infection (2003) Lancet, 361, pp. 1779-1785. , http://image.thelancet.com/extras/03art4454web.pdf; Brown, K.G., Tetro, J.A., Comparative analysis of the SARS coronavirus genome: A good start to a long journey (2003) Lancet, 361, pp. 1757-1758. , http://pdf.thelancet.com/pdfdownload?uid=llan.361.9371. editorial_andreview.25845.1&x=x.pdf; (2003) PCR Primers for SARS Developed by WHO Network Laboratories, , http://www.who.int/csr/sars/primers/en/, Geneva, April 17; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, , www.sciencemag.org/cgi/content/full/1085658/DC1; Zambon, M., Severe acute respiratory syndrome revisited (2003) BMJ, 326, pp. 831-832; Comments on the Reported Isolation of Viruses Related to the SARS Coronavirus in Wild Animale in Southern China, , http://www.who.int/csr/don/2003_05_23b/en/, Geneva; Nicholls, J.M., Poon, L.M.L., Lee, K.C., Lung pathology of fatal severe acute respiratory sindrome Lancet, 361 (9371), pp. 1773-1778. , http://pdf.thelancet.com/pdfdownload?uid=llan.361.9371. original_research.25764.1&x=x.pdf; To, K.F., Chan, P.K., Chan, K.F., Pathology of fatal human infection associated with avian influenza A H5N1 virus (2001) J Med Virol, 63, pp. 242-246; Main Findings of an Investigation into the Outbreak of Severe Acute Respiratory Syndrome at Amoy Gardens, , http://www.info.gov.hk/info/an/ndf/amoy_e.pdf; Wong, K.T., Antonio, G.E., Hui, D.S., Severe Acute Respiratory Syndrome: Radiographic appearances and pattern of progression in 138 patients (2003) Radiology, , http://radiology.rsnajnls.org/cgi/content/full/2282030593v1; Radiological Appearances of Recent Cases of Atypical Pneumonia in Hong Kong, , http://www.droid.cuhk.edu.hk/web/atypical_pneumoni/ atypical_pneurnonia.htm#img_find; Chan-Yeung, M., Yu, W.C., Outbreak of severe acute respiratory syndrome in Hong Kong Special Administrative Region: Case report (2003) BMJ, 326, pp. 850-852; (2003) Health Canada Management of Severe Acute Respiratory Syndrome (SARS) in Adults: Interim Guidance for Health Care Providers, , http://www.hc-sc.gc.ca/pphb-dgspsp/sars-sras/pdf/ sars-clin-guide-05-01-03c_e.pdf, May 1; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinante of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766. , http://image.thelancet.com/extras/03art4453web.pdf; Bartlett, J.G., Dowell, S.F., Mandell, L.A., File T.M., Jr., Musher, D.M., Fine, M.J., Practice guidelines for the management of community-acquired pneumonia in adulte (2000) Clin Infect Dis, 31, pp. 347-382. , http://www.journals.uchicago.edu/CID/journal/issues/ v31n2/000441/000441.web.pdf, Infectious Diseases Society of America; Tao Li, T.S., Buckley, T.A., Yap, F.H.Y., Sung, J.J.Y., Joynt, G.M., Severe acute respiratory syndrome (SARS): Infection control (2003) Lancet, 361, p. 1386; Data on In-flight Transmission Updated, , http://www.who.int/csr/don/2003_05_22/en/, Geneva; Seto, W.H., Tsang, D., Yung, R.W., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361 (9368), pp. 1519-1520. , http://pdf.thelancet.com/pdfdownload?uid=llan.361.9368. original_research.25515.1&x=x.pdf; The Lancet Editorial. Will SARS hurt the world's poor? (2003) Lancet, 361 (9368), p. 1485; (2003) World BankWorld Development Indicators","Petrosillo, N.; Ist. Naz. per le Malat. Infet. IRCCS, Lazzaro Spallanzani, II Divisione, Via Portuense, 292, 00149 Roma, Italy; email: nicastri@tiscali.it",,,00341193,,RPMDA,"12868234","Italian","Recenti Prog. Med.",Review,"Final",,Scopus,2-s2.0-0041474826
"Thomas P.A.","7404888984;","Severe acute respiratory syndrome",2003,"Indian Journal of Medical Microbiology","21","3",,"152","160",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346264923&partnerID=40&md5=e36b227de93b28a7142236149e2a453d","Institute of Ophthalmology, Joseph Eye Hospital, Tiruchirapalli 620 001, India","Thomas, P.A., Institute of Ophthalmology, Joseph Eye Hospital, Tiruchirapalli 620 001, India","Severe acute respiratory syndrome (SARS) is a form of atypical pneumonia that apparently originated in Guangdong Province of the People's Republic of China in late 2002. This first came to the world's attention in late February 2003, and has since spread worldwide. As of June 23rd 2003, the disease had been reported from 32 countries or regions globally, affecting 8459 people; 805 individuals (9.5 % of the total affected) have died of the disease. A novel coronavirus, the SARS-associated coronavirus (SARS-CoV) has been found in various specimens taken from patients with SARS. Although there has been rapid development of tests to detect SARS Co-V, these tests presently have certain limitations. Definitions of suspected, confirmed and probable cases have been formulated. Measures currently used for the management of patients with SARS include isolation, ribavirin, corticosteroid therapy and mechanical ventilation. Unfortunately, almost 10 % of affected patients succumb to their illness, underlying the need for developing more effective therapy. It remains to be seen how long it will take to bring this epidemic under control.","China; Coronavirus; Epidemic; SARS","amoxicillin plus clavulanic acid; clarithromycin; corticosteroid; esterase inhibitor; levofloxacin; methylprednisolone; oxygen; protein antibody; proteinase inhibitor; receptor antibody; ribavirin; virus vaccine; artificial ventilation; China; diagnostic test; drug efficacy; drug mechanism; drug synthesis; drug use; epidemic; geographic distribution; human; hypoxemia; infection control; mortality; nonhuman; oxygen therapy; patient care; patient coding; review; SARS coronavirus; severe acute respiratory syndrome; virus pneumonia","Hoey, J., Severe acute respiratory syndrome (2003) CMAJ, 168 (8), p. 1013; US Centers for Disease Control and Prevention. Updated interim surveillance case definition for severe acute respiratory syndrome (SARS) - United States, April 29, 2003 (2003) MMWR, 52 (17), pp. 391-393; Wenzel, R.P., Edmond, M.B., Managing SARS amidst uncertainty (2003) N. Engl. J. Med., 348 (20), pp. 1947-1948; World Health Organization SARS website. Update 86: Hong Kong removed from list of areas with local transmission (2003), http://www.who.int/csr/don/2003_06_23/en/, 23 June; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major out break of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348 (20), pp. Surg1-Surg9; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348 (20), pp. 1977-1985; Nie, Q.-H., Luo, X.-D., Hui, W.-L., Advances in clinical diagnosis and treatment of severe acute respiratory syndrome (2003) World J. Gastroenterol., 9 (6), pp. 1139-1143; World Health Organization SARS website. Cumulative number of reported probable cases of SARS http://www.who.int /csr /sars /country/2003-06-23/en/; Brooks, G.F., Jawetz, E., Butel, J.S., Melnick, J.L., Ornston, L.N., Adelberg, E.A., (1992) Jawetz, Melnick and Adelberg's Medical Microbiology, , 19th ed. (Appleton and Lange, Norwalk); Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348 (20), pp. 1948-1951; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325. , (9366); Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emerg, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1967-1976; Fouchier, R.A., Kuiken, T., Schutten, M., van Amerongen, G., van Doomum, G.J., van den Hoogen, B.G., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240. , (6937); Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , (5624); Ruan, Y.J., Wei, C.L., Ec, A.L., Vega, V.B., Thorean, H., Su, S.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1756-1757. , (9371); Wong, R.S.M., Severe acute respiratory syndrome in a doctor working at the Prince of Wales Hospital (2003) Hong Kong Med. J., 9 (3), pp. 202-205; Zhang, J.Z., Severe acute respiratory syndrome and its lesions in the digestive system (2003) World J. Gastroenterol., 9 (6), pp. 1135-1138; Wong, K.T., Antonio, G.E., Hui, D.S., Lee, N., Yuen, E.H., Wu, A., Severe acute respiratory syndrome: Radiographic appearances and pattern of progression in 138 patients (2003) Radiology, , (e pub. ahead of publication); Antonio, G.E., Wong, K.T., Hui, D.S., Wu, A., Lee, N., Yuen, E.H., Thin section CT in patients with severe acute respiratory syndrome following hospital discharge: Preliminary experience (2003) Radiology, , June 12 (epub. ahead of print); Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772. , (9371); World Health Organization SARS website. PCR primers for SARS developed by WHO Network Laboratories (2003), http://www.who.int/csr/sars/primers/en, 17 April; Nicholls, J.M., Poon, L.L., Lee, K.C., Ng, W.F., Lai, S.T., Leung, C.Y., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778. , (9371); So, L.K., Lau, A.C., Yam, L.Y., Cheung, T.M., Poon, E., Yung, R.W., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Dwosh, H.A., Hong, H.H.L., Austgarden, D., Herman, S., Schabas, R., Identification and containment of an outbreak of SARS in a community hospital (2003) CMAJ, 168, p. 1415","Thomas, P.A.; Institute of Ophthalmology, Joseph Eye Hospital, Tiruchirapalli 620 001, India",,,02550857,,IJMME,,"English","Indian J. Med. Microbiol.",Review,"Final",,Scopus,2-s2.0-0346264923
"Luo Y., Jiang L., Ao X., Lu Z., Liu H.-D., Xu Y., Ao Y., Ren Q., Lu C., Xu H.-M., Zhang X.","55712644500;57198538205;6701683197;57198843848;26652430300;8070507500;14061741600;36114825700;7404805666;8404851100;20336388600;","Genomic variations in the locus for aminopeptidase N: A putative cellular receptor for SARS-CoV spike glycoprotein",2003,"Acta Genetica Sinica","30","7",,"687","692",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042315221&partnerID=40&md5=438bf8c3c49305756a982ee331613f3c","Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Department of Medical Genetics, Institute of Basic Medical Sciences, Peking Union Medical College, Beijing 100005, China","Luo, Y., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Jiang, L., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Ao, X., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Lu, Z., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Liu, H.-D., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Xu, Y., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Ao, Y., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Ren, Q., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Lu, C., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Xu, H.-M., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; Zhang, X., Research Center for Medical Genomics, China Medical University, Shenyang 110001, China, Department of Medical Genetics, Institute of Basic Medical Sciences, Peking Union Medical College, Beijing 100005, China","Aminopeptidase N has been identified as the cellular receptor for human coronavirus HCoV-229E and was a putative receptor for the spike glycoprotein encoded by the SARS-associated coronavirus (SARS-CoV). We report here identification of 9 single nucleotide polymorphisms (SNPs) in ANPEP, encoding human aminopeptidase N, in Chinese. All ANPEP exons and their flanking intronic sequences were amplified from unrelated normal individuals by polymerase chain reaction (PCR) and screened using denaturing high-performance liquid chromatography (DHPLC). Nine SNPs were revealed after direct sequencing of PCR amplified fragments which showed changes of DHPLC chromatogram. Four of these polymorphisms, T321M(962C > T), S651L(1952C > T), S752N(2255G > A) and G764R(2290G > A), were non-synonymous; the remaining exonic synonymous and intronic ones were T795T(2385 > T), IVS7 + 17G > A,IVS14-16A > G,IVS17 + 12C > G and IVS17 + 44C > T. Our data may be useful for studies to investigate the role of host genetic factors in SARS pathogenesis, especially for identifying SARS-susceptible and/or anti-SARS alleles.","Aminopeptidase N; DHPLC; SARS-CoV; SNP","microsomal aminopeptidase; spike glycoprotein; unclassified drug; virus glycoprotein; allele; article; Chinese; chromatography; Coronavirus; exon; gene locus; gene sequence; genetic variability; heredity; high performance liquid chromatography; host susceptibility; human; intron; nonhuman; pathogenesis; polymerase chain reaction; respiratory tract disease; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; single nucleotide polymorphism; Animals; Antigens, CD13; Chromatography, High Pressure Liquid; Humans; Membrane Glycoproteins; Polymerase Chain Reaction; Receptors, Virus; SARS Virus; Sequence Analysis, DNA; Variation (Genetics); Viral Envelope Proteins; Coronavirus; SARS coronavirus","Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Qin, E.-D., Zhu, Q.-Y., Yu, M., Fan, B.-C., Chang, G.-H., Si, B.-Y., Yang, B.-A., Yang, H.-M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJO1) (2003) Chinese Science Bulletin, 48, pp. 941-948; Ruan, Y.J., Wei, C.L., Ee, A.L., Vega B. V, Thoreau, H., Su, S.T., Chia, J.M., Liu, E.T., Com parative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361 (9371), pp. 1779-1785; Chen, Y.-J., Gao, G., Bao, Y.-M., Lopez, R., Wu, J.-M., Cai, T., Ye, Z.-Q., Luo, J.-C., Initial analysis of complete genome sequences of SARS coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 493-500; Zhang, W.-G., Li, J.-Q., Zhou, H.-M., Genomic characterization of SARS coronavirus: A novel member of coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 501-508; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357 (6377), pp. 420-422; Yu, X.-J., Luo, C., Lin, J.-C., Hao, P., He, Y.-Y., Guo, Z.-M., Qin, L., Li, Y.-X., Putative hAPN receptor binding sites in SARS-CoV spike protein (2003) Acta Pharmacol Sin, 24 (6), pp. 481-488; Hill, A.V., The genomics and genetics of human infectious disease susceptibility genes (2001) Ann Rev Genomics Hum Genet, 2, pp. 373-400; Hogan, C.M., Hammer, S.M., Host determinants in HIV infection and disease. Part 2: Genetic factors and implications for antiretroviral therapeuties (2001) Ann Intern Med, 134, pp. 978-996","Luo, Y.; Research Center for Medical Genomics, China Medical University, Shenyang 110001, China; email: luoyangjj@sina.com",,,03794172,,ICHPC,"14579541","Chinese","Acta Genet. Sin.",Article,"Final",,Scopus,2-s2.0-0042315221
"Kullberg B.J., Voss A.","7006279060;55636322092;","Severe acute respiratory syndrome: Lessons and uncertainties",2003,"Netherlands Journal of Medicine","61","7",,"235","237",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242367235&partnerID=40&md5=2c5f2ec1ed72deb6faf2ba047e666266","Department of Medicine, University Medical Centre St Radboud, Nijmegen, Netherlands; Department of Medical Microbiology, University Medical Centre St Radboud, Nijmegen, Netherlands; Nijmegen University, Centre for Infectious Diseases, University Medical Centre St Radboud, Nijmegen, Netherlands","Kullberg, B.J., Department of Medicine, University Medical Centre St Radboud, Nijmegen, Netherlands, Nijmegen University, Centre for Infectious Diseases, University Medical Centre St Radboud, Nijmegen, Netherlands; Voss, A., Department of Medical Microbiology, University Medical Centre St Radboud, Nijmegen, Netherlands, Nijmegen University, Centre for Infectious Diseases, University Medical Centre St Radboud, Nijmegen, Netherlands","The outbreak of severe acute respiratory syndrome (SARS) has produced scientific and epidemiological discoveries with unprecedented speed, and this information has been spread instantaneously to the global health community through the internet. Within a few weeks, the coronavirus associated with SARS (SARS-CoV) was identified and sequenced. The source of the outbreak and the exact modes of transmission are still subjects of research. Important lessons can be learned from the SARS outbreak about both the scientific and the public health approach to emerging pathogens. © 2003 Van Zuiden Communications B.V. All rights reserved.",,"corticosteroid; ribavirin; epidemic; epidemiological data; geographic distribution; human; Internet; medical information; medical research; public health; review; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; virus identification; virus transmission; virus virulence; disease transmission; epidemic; international cooperation; severe acute respiratory syndrome; Disease Outbreaks; Humans; International Cooperation; Internet; Severe Acute Respiratory Syndrome","Acute respiratory syndrome in China -update 3: Disease outbreak reported (2003), http://www.who.int/csr/don/2003_2_20/en, Geneva: World Health Organization, 2003. Accessed April 22, at; Cumulative number of reported cases of severe acute respiratory syndrome (SARS) (2003), http://www.who.int/csr/sarscountry/2003_06_9/en/, Geneva: World Health Organization, 2003. Accessed June 9, at; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 15, p. 240; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1975-1983; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1993-2003; Vonderen, M.G.A., van Bos, J.C., Prins, J.M., Wertheim-Van Dillen, P., Speelman, P., Ribavirin in the treatment of severe acute respiratory syndrome (SARS) (2003) Neth. J. Med., 61, pp. 238-241","Kullberg, B.J.; Department of Medicine, University Medical Centre St Radboud, Nijmegen, Netherlands; email: b.kullberg@aig.umcn.nl",,,03002977,,NJNEE,"14567519","English","Neth. J. Med.",Review,"Final",,Scopus,2-s2.0-0242367235
"Vabret A.","7003959575;","Coronavirus: A successful emergence [Coronavirus: Une émergence réussie]",2003,"Virologie","7","4",,"237","241",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141702295&partnerID=40&md5=f9b64e1761e4a641ad293d8e36443df1","Laboratoire de Virologie, CHU, avenue Georges-Clemenceau, 14000 Caen, France","Vabret, A., Laboratoire de Virologie, CHU, avenue Georges-Clemenceau, 14000 Caen, France",[No abstract available],,"Coronavirus; Ebola virus; editorial; Human rhinovirus; Influenza virus; Kaposi sarcoma; mortality; nonhuman; opportunistic infection; respiratory distress; Respiratory syncytial pneumovirus; SARS coronavirus; seroconversion; severe acute respiratory syndrome; virus envelope; virus genome; virus transmission; Coronavirus; Ebola virus; Human rhinovirus sp.; Influenza virus; Pneumovirus; Respiratory syncytial virus; Rhinovirus; SARS coronavirus","Serink, M., Infectious diseases. Calling all coronavirologists (2003) Science, 300, pp. 413-414; Chastel, C., Emergences vitales chez l'homme et réussite émergentielle (2000) Virologie, 4, pp. 273-279; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, , May 1 (publication électronique); Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 1-9; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CL pro) structure: Basis for design of anti-SARS drugs (2003) Science, , May 13 (publication électronique); Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Eng J Med, 348, pp. 1967-1976; Fouchier, R.A.M., Kuiken, T., Schulten, M., Koch's postulates fullfilled for SARS virus (2003) Nature, 423, p. 240; Beaudette, F.R., Hudson, C.B., Cultivation of the virus of infectious bronchitis (1937) J Am Vet Med Assoc, 90, p. 51; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin: Isolation and biologic properties of the virus (1949) J Exp Med, 90, p. 181; Tyrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common cold virus in organ culture (1967) J Gen Virol, 1, p. 175; Hamre, D., Procknow, J.J., A new virus isolated from the human respiratory tract (1966) Proc Soc Exp Biol Med, 121, p. 190; Mc Intosh, K., Becker, W.B., Chanock, R.M., Growth in suckling mouse brain of « IBV-like » viruses from patients with upper respiratory tract disease (1967) Proc Natl Acad Sci USA, 58, p. 2268; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch Virol, 142, pp. 629-633; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) J Virol, 70, pp. 4773-4777; Almazan, F., Gonzalez, J.M., Penzes, Z., Engineering the largest RNA virus genome as an infectious bacterial artifical chromosome (2000) Proc Natl Acad Sci USA, 97, pp. 5516-5521; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet Q, 8, pp. 257-261; De Groot, R.J., Horzinek, M.C., (1995) The Coronaviridae, pp. 293-315. , Würzburg: Siddell SG, eds; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol, 5, pp. 9-12; Vabret, A., Brouard, J., Petitjean, J., Eugène-Ruelland, G., Freymuth, F., Infections à coronavirus humains: Importance et diagnostic (1998) Press Med, 27, pp. 1813-1817; Vabret, A., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., An outbreak of coronlviriis OC43 respiratory infection in Normandy, France (2003) Clin Infect Dis, 36, pp. 985-989; Arbour, N., Day, Yuen, K.Y.R., Newcombe, J.I.A., Talbot, J.P., Neuroinvasion by human respiratory coronavirus (2000) J Virol, 74, pp. 8913-8921; Holmes, K.V., SARS-associated coronavirus (2003) N Engl J Med, 348, pp. 1948-1951; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, p. 1767. , and members of the HKU/UCH SARS Study Group; Kontoyiannis, D.P., Pasqualini, R., Arap, W., Aminopeptidase N inhibitors and SARS (2003) Lancet, 361, p. 1558","Vabret, A.; Laboratoire de Virologie, CHU, avenue Georges-Clemenceau, 14000 Caen, France; email: vabret-a@chu-caen.fr",,,12678694,,VIROF,,"French","Virologie",Editorial,"Final",,Scopus,2-s2.0-0141702295
"Shah A., Lone R., Wani T.","35478078400;8439178100;6602168711;","SARS virus: A novel coronavirus",2003,"JK Practitioner","10","3",,"182","184",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041932475&partnerID=40&md5=d9986597c18782a0c0fe967e44bdad1c","Dept. of Pathology and Microbiology, SKIMS, Soura, Srinagar 190011, Kashmir, India","Shah, A., Dept. of Pathology and Microbiology, SKIMS, Soura, Srinagar 190011, Kashmir, India; Lone, R., Dept. of Pathology and Microbiology, SKIMS, Soura, Srinagar 190011, Kashmir, India; Wani, T., Dept. of Pathology and Microbiology, SKIMS, Soura, Srinagar 190011, Kashmir, India",[No abstract available],,"clinical feature; Coronavirus; diagnostic accuracy; fatality; histopathology; human; immunohistochemistry; nonhuman; practice guideline; prevalence; respiratory tract disease; review; sampling; SARS coronavirus; serology; severe acute respiratory syndrome; symptomatology; viral genetics; virus morphology","Almeida, J.D., Tyrell, D.J., The morphology of three previously uncharacterized human respiratory viruses that grow in organ culture (1967) J Gen Virol, 1, pp. 175-178; Bradbarne, A.F., Tyrell, D.J., Coronaviruses of man (1971) Prog. Med Virol, 13, pp. 373-403; Tyrell, D.A., Bynoe, M.L., Cultivation of a novel type of common cold virus in organ culture (1965) A Prog Med J, 1, pp. 1467-1470; Hamre, D., Kindig, D.A., Mann, J., Growth and intracellular development of a new respiratory virus (1967) J Virol, 1, pp. 810-816; Hamre, D., Procknow, J.J., A new virus isolated from the respiratory tract (1966) Proc Soc Exp Biol Med, 121, pp. 191-193; McIntosh, K., Becker, W.B., Channock, R.M., Growth in suckling mouse brain of ""1BV- like"" viruses from patients with upper respiratory tract diseases (1967) Proc Natl Acad Sci, 58, pp. 2268-2273; Siddell, S.G., Snyder, E.J., Coronaviruses, toraviruses and arteroviruses in collier Leds (1998) Topley and Wilson Microbiology and Microbial Infections London Edward Acnold, 1, pp. 463-484; Wage, H., Sidelell, S., Ter Menlers, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbial Immunol, 99, pp. 165-200; MacNaughton, M.R., Davies, H.A., Nermut, M.V., Ribonucleo protein like structures from coronaviruses particles (1978) J Gen Virol, 39, pp. 545-549; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoprotein and interaction with the viral nucleocapsid (1980) A F. J Virol, 30, pp. 449-462; Griffiths, G., Rottier, P.J.M., Cell biology of viruses that assemble along the biosynthetic pathway (1992) Semen Cell Biol, 3, pp. 367-381; Oslero, L.S., Coronaviruses (1973) Ultrastructure of Animal Viruses and Bacteriophages, pp. 331-343. , in Dalton AJ, Hagnenae F eds; An atlas New York, Academic Press; Tooze, J., Tooze, S.A., Infection of AtT20 musine pituitary tumor cells by mouse hepatitis virus strain A59; Virus budding is restricted to the golgi region (1985) Eur J Cell Biol, 37, pp. 203-212; Machamer, C.E., Grim, M.G., Esquela, A., Retention of a Cis Golgi protein requires polar residue on face of a predicted alpha-helix in the transmembrane domain (1993) Mol Biol Cell, 4, pp. 695-704; Machemer, C.E., Mantone, S.A., Rose, J.K., The E1 glycoprotein of an avain corona virus is targeted to cis Golgi complex (1990) Proc Natl Acad Sci USA, 87, pp. 6944-6948; Machamer, C.E., Rose, J.K., A specific transmembrane domain of a coronavirus E1 glycoprotein (1987) J Cell Biol, 105, pp. 1205-1214; Godet, M., E Harridon, R., Vautherot, J.F., TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions (1992) Virology, 188, pp. 666-675; Vennema, H., Godeke, G.J., Rossen, J.W.A., Nucleocapsid independent assembly of coronavirus like particles by coexpression of viral envelop protein genes (1996) EMBO J, 15, pp. 2020-2028; Yu, X., Bi, W., Weiss, S.R., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023; Lomniczi, B., Biological properties of avian coronavirus RNA (1977) J Gen Virol, 36, pp. 531-533; Schochetman, B., Stevens, R.H., Simpson, R.W., Presence of infectious polyadenylated RNA in the coronavirus avian bronchitis (1977) Virology, 77, pp. 772-782; Steinhauher, D.A., Holland, J.J., Direct method for quantitation of extreme polymerase error frequencies at selected single base sites in viral RNA (1986) J Virol, 57, pp. 219-228; Lepare-Geofart, I., Hingley, S.T., Chua, M.M., Altered pathogenesis of murine coronavirus MHV-A59 is associated with a Q159L aminoacid substitution in the spike protein (1997) Virology, 239, pp. 1-10; Barie, R.S., Schaad, M.C., Establishing a genetic recombination map for murine coronavirus strain A59 complimentation groups (1990) Virology, 177, pp. 646-654; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Mobiol Rev, 56, pp. 61-69; Banner, L.R., Keck, J.G., Lai, M.M., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Acute respiratory syndrome (2003) Wkly Epidemiol Rec, 78, pp. 73-74; Hoffman, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell cultures (1988) J Clin Microbial, 26, pp. 2235-2239; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , http://www.nejm.org/cgi/content, Published in April 10, 2003; Holmes, K.V., Coronaviruses Fields Virology 4th ed, , in David MK, Peter MH, Drane EG; Lippincott Williams and Wilkins; Severe acute respiratory syndrome. Updated interim case fatality associated with SARS http://www.cdc.gov/sars/casedefinition.htm, Accessed 8th May 2003; Cumulative number of reported cases (SARS) from 1st November to 14th May 2003 http://www.who.int/cst/sarscountry/2003, Accessed 14th May 2003; Preliminary clinical description of SARS (2003) MMWR Morb Wkly Rep, 52, pp. 255-256; Guidelines for collection and handling of specimen for investigation of potential cases of SARS http://www.nicd.org/guidelines, Accessed 8th May 2003; Severe acute respiratory syndrome. Updated interim case definition http://www.cdc.gov/sars/casedefinition.htm, Accessed 8th May 2003; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, , http://www.nejm.org/cgi/content, Published in April 10, 2003; Leo, L.M., On, K.W., Winsie, L., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome http://www.clinchem.org, Accessed 8th May 2003; Ksaizi, T.G., West, C.P., Pollin, P.E., ELISA for detection of antibodies to Ebola viruses (1999) J Infect Dis, 179, pp. 192-198","Shah, A.; Dept. of Pathology and Microbiology, SKIMS, Soura, Srinagar 190011, Kashmir, India",,,09718834,,JKPRF,,"English","JK Pract.",Review,"Final",,Scopus,2-s2.0-0041932475
"Poon L.L.M., Wong O.K., Chan K.H., Luk W., Yuen K.Y., Peiris J.S.M., Guan Y.","7005441747;56672516300;7406034307;57213310994;36078079100;7005486823;7202924055;","Erratum: Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (International Journal of Laboratory Medicine and Molecular Diagnostics (2003) 49 (953-5)",2003,"Clinical Chemistry","49","7",,"1234","",,1,"10.1373/49.7.1234","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038271920&doi=10.1373%2f49.7.1234&partnerID=40&md5=14769ed6e9c6458936f92c52264cb48d","Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, Queen Mary Hospital, Hong Kong, Hong Kong","Poon, L.L.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Wong, O.K., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Chan, K.H., Department of Microbiology, Queen Mary Hospital, Hong Kong, Hong Kong; Luk, W., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong",[No abstract available],,"erratum; error; Coronavirus",,"Poon, L.L.M.; Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong",,,00099147,,CLCHA,,"English","Clin. Chem.",Erratum,"Final",Open Access,Scopus,2-s2.0-0038271920
"Oxford J.S., Bossuyt S., Lambkin R.","7102877671;6602078073;6601996658;","A new infectious disease challenge: Urbani severe acute respiratory syndrome (SARS) associated coronavirus",2003,"Immunology","109","3",,"326","328",,13,"10.1046/j.1365-2567.2003.01684.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038127076&doi=10.1046%2fj.1365-2567.2003.01684.x&partnerID=40&md5=2e824deb7bb2e6c1beef5de5cd699869","Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, London, United Kingdom; Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, 327 Mile End Road, London, E1 4NS, United Kingdom","Oxford, J.S., Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, London, United Kingdom, Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, 327 Mile End Road, London, E1 4NS, United Kingdom; Bossuyt, S., Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, London, United Kingdom; Lambkin, R., Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, London, United Kingdom",[No abstract available],,"esterase; matrix protein; nucleoprotein; proteinase; RNA directed RNA polymerase; spike protein; unclassified drug; virus hemagglutinin; virus protein; community acquired pneumonia; Coronavirus; disease transmission; epidemic; Hong Kong; human; infection control; Influenza virus; Influenza virus A; nonhuman; pneumonia; priority journal; respiratory tract infection; review; SARS coronavirus; severe acute respiratory syndrome; vaccination; virus detection; virus infection; Asia, Southeastern; Communicable Diseases, Emerging; Disease Outbreaks; Humans; SARS Virus; Severe Acute Respiratory Syndrome; Viral Vaccines","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Oxford, J.S., Influenza A pandemics of the 20th century with special reference to 1918: Virology, pathology and epidemiology (2000) Rev Med Virol, 10, pp. 119-133; Scholtissek, C., Stech, J., Krauss, S., Webster, R.G., Cooperation between the hemagglutinin of avian viruses and the matrix protein of human influenza A viruses (2002) J Virol, 76, pp. 1781-1786; Oxford, J.S., Sefton, A., Jackson, R., Innes, W., Daniels, R.S., Johnson, N.P., World War I may have allowed the emergence of 'Spanish' influenza (2002) Lancet Infect Dis, 2, pp. 111-114; Yuen, K.Y., Chan, P.K., Peiris, M., Tsang, D.N., Que, T.L., Shortridge, K.F., Cheung, P.T., Cheng, A.F., Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus (1998) Lancet, 351, pp. 467-471; Hampson, A.W., Influenza virus antigens and 'Antigenic Drift' (2002) Influenza, pp. 49-85. , Potter GW, ed. Amsterdam: Elsevier; Tyrrell, D.A.J., Bynoe, M.L., Cultivation of a novel type of common cold virus in organ culture (1965) Br Med J, 1, pp. 1467-1470; Siddell, S., Myint, S., Coronaviruses (1995) Viral and Other Infections of the Human Respiratory Tract, , Myint SH, Taylor-Robinson D, eds. Dordrecht: Kluwer Academic Publishers; Severe Acute Respiratory Syndrome (SARS) and coronavirus testing (2003) MMWR, 52, pp. 14-15; Ruan, Y.J., Comparative full length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins and infection (2003) Lancet, , in press; MacNaughton, M.R., Hasony, H.J., Madge, M.H., Reed, S.E., Antibody to virus components in volunteers experimentally infected with human coronavirus 229E group viruses (1981) Infect Immun, 31, pp. 845-849; Fleming, J.O., Shubin, R.A., Sussman, M.A., Casteel, N., Stohlman, S.A., Monoclonal antibodies to the matrix (E1) glycoprotein of mouse hepatitis virus protect mice from encephalitis (1989) Virology, 168, pp. 162-167; Deregt, D., Babiuk, L.A., Monoclonal antibodies to bovine coronavirus, characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins (1987) Virology, 161, pp. 410-420; Sidwell, R.W., Ribavirin. Review of a broad-spectrum antiviral agent (1985) Viral Chemotherapy, pp. 49-97. , Shugar D, ed. Oxford: Pergamon Press","Oxford, J.S.; Retroscreen Virology Ltd., Qu. Mary's Sch. of Med./Dentistry, 327 Mile End Road, London, E1 4NS, United Kingdom; email: j.s.oxford@retroscreen.com",,,00192805,,IMMUA,"12807475","English","Immunology",Review,"Final",Open Access,Scopus,2-s2.0-0038127076
"Tan D.Y.L., Kaw G.J.L., Tsou I.Y.Y., Wansaicheong G.K.-L., Green J.A., Tai D.Y.H., Chee T.S.G.","7202902032;6602550492;56631588100;6603327791;57199008049;7005049004;7004196781;","Radiographic features of a case of severe acute respiratory syndrome with fatal outcome",2003,"Annals of the Academy of Medicine Singapore","32","4",,"542","546",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141670424&partnerID=40&md5=d7b70b2ff9f879fbf389396bf1e20894","Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore; Department of Infectious Diseases, Tan Tock Seng Hospital, Singapore, Singapore; Department of General Medicine, Tan Tock Seng Hospital, Singapore, Singapore; Department of Diagnostic Radiology, Tan Tock Seng Hospital, 11 Jalan Tan Tock Seng, Singapore 308433, Singapore","Tan, D.Y.L., Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore, Department of Diagnostic Radiology, Tan Tock Seng Hospital, 11 Jalan Tan Tock Seng, Singapore 308433, Singapore; Kaw, G.J.L., Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore; Tsou, I.Y.Y., Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore; Wansaicheong, G.K.-L., Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore; Green, J.A., Department of Infectious Diseases, Tan Tock Seng Hospital, Singapore, Singapore; Tai, D.Y.H., Department of General Medicine, Tan Tock Seng Hospital, Singapore, Singapore; Chee, T.S.G., Department of Diagnostic Radiology, Tan Tock Seng Hospital, Singapore, Singapore","Introduction: Severe acute respiratory syndrome (SARS) is a new form of atypical pneumonia caused by a coronavirus. We present the clinical course and chest radiographic findings of a case of SARS with fatal outcome. Clinical Picture: A 39-year-old Chinese male presented with fever, sore throat and non-productive cough. During his illness, serial chest radiographs showed increasingly severe air-space shadowing in both lungs. Treatment and Outcome: The patient was treated with supplemental oxygen, levofloxacin, oseltamivir, ribavirin and methylprednisolone. As his condition worsened, he required ventilatory and inotropic support. He later developed a myocardial infarct and coagulopathy, and succumbed to his illness. Conclusion: The reported case mortality of SARS is about 9% worldwide. In Singapore, the mortality is 15.5%. Acute respiratory distress syndrome (ARDS) is believed to be a contributory factor to our patient's demise. We report this case to show the radiographic changes of ARDS in a patient with SARS.","Acute respiratory distress syndrome; Air-space shadowing; Atypical pneumonia; Coronavirus; Thoracic radiography","levofloxacin; methylprednisolone; oseltamivir; oxygen; ribavirin; adult; adult respiratory distress syndrome; article; blood clotting disorder; case report; clinical feature; Coronavirus; coughing; disease course; disease severity; fever; heart infarction; human; lung ventilation; male; mortality; oxygen therapy; pneumonia; radiodiagnosis; respiratory tract infection; risk factor; severe acute respiratory syndrome; sore throat; thorax radiography; treatment planning; Adult; Combined Modality Therapy; Disease Progression; Fatal Outcome; Humans; Male; Multiple Organ Failure; Radiography, Thoracic; Severe Acute Respiratory Syndrome; Severity of Illness Index; Singapore","Acute Respiratory Syndrome in Hong Kong Special Administrative Region of China/Vietnam, , http://www.who.int/csr/don/2003_03_12/en; Severe Acute Respiratory Syndrome (SARS): Multi-Country Outbreak, , http://www.who.int/csr/don/2003_03_15/en/; Cumulative Number of Reported Probable Cases of SARS, , http://www.who.int/csr/sars/country/2003_07_11/en/; (2003) SARS Update. 9 July 2003, , http://app.moh.gov.sg/new/new02.asp?id=1&mid=7800; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/; Matar, L.D., McAdams, H.P., Palmer, S.M., Howell, D.N., Henshaw, N.G., Davis, R.D., Respiratory viral infections in lung transplant recipients: Radiologic findings with clinical correlation (1999) Radiology, 213, pp. 735-742; Zahradnik, J.M., Adenovirus pneumonia (1987) Semin Respir Infect, 2, pp. 104-111; Ruben, F.L., Nguyen, M.L., Viral pneumonitis (1991) Clin Chest Med, 12, pp. 223-235; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Ware, L.B., Matthay, M.A., The acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1334-1349; Hansell, D.M., Peters, A.M., Pulmonary vascular diseases and pulmonary oedema (2000) Imaging of Diseases of the Chest. 3rd Ed., pp. 405-465. , Armstrong P, Wilson A G, Dee P, Hansell D M, editors. London: Mosby; Updated Interim US Case Definition of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/casedefinition.htm; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Tyrrell, D.A., Bynoe, M.L., Cultivation of viruses from a high proportion of patients with colds (1966) Lancet, 1, pp. 76-77; Ijaz, M.K., Brunner, A.H., Sattar, S.A., Nair, R.C., Johnson-Lussenburg, C.M., Survival characteristics of airborne human coronavirus 229E (1985) J Gen Virol, 66, pp. 2743-2748; Sizun, J., Yu, M.W., Talbot, P.J., Survival of human coronaviruses 229E and OC43 in suspension and after drying on surfaces: A possible source of hospital-acquired infections (2000) J Hosp Infect, 46, pp. 55-60","Tan, D.Y.L.; Department of Diagnostic Radiology, Tan Tock Seng Hospital, 11 Jalan Tan Tock Seng, Singapore 308433, Singapore; email: diana_tan@ttsh.com.sg",,,03044602,,AAMSC,"12968561","English","Ann. Acad. Med. Singapore",Article,"Final",,Scopus,2-s2.0-0141670424
"Calza L., Manfredi R., Verucchi G., Chiodo F.","7102251828;7101890204;57200377343;7102064002;","SARS: A novel emergency for the world health [SARS: Una nuova emergenza sanitaria mondiale]",2003,"Recenti Progressi in Medicina","94","7-8",,"284","294",,7,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042977579&partnerID=40&md5=589dcc825f9b9ed08c444721bf143180","Dipto. Med. Clin. Specialistica/S., Universita Alma Mater Studiorum, Policlinico S. Orsola, Bologna, Italy; Universita Alma Mater Studiorum, Policlinico S. Orsola, Dipto. Med. Clin. Specialistica/S., Via G. Massarenti, 11, 40138 Bologna, Italy","Calza, L., Dipto. Med. Clin. Specialistica/S., Universita Alma Mater Studiorum, Policlinico S. Orsola, Bologna, Italy, Universita Alma Mater Studiorum, Policlinico S. Orsola, Dipto. Med. Clin. Specialistica/S., Via G. Massarenti, 11, 40138 Bologna, Italy; Manfredi, R., Dipto. Med. Clin. Specialistica/S., Universita Alma Mater Studiorum, Policlinico S. Orsola, Bologna, Italy; Verucchi, G., Dipto. Med. Clin. Specialistica/S., Universita Alma Mater Studiorum, Policlinico S. Orsola, Bologna, Italy; Chiodo, F., Dipto. Med. Clin. Specialistica/S., Universita Alma Mater Studiorum, Policlinico S. Orsola, Bologna, Italy","The Severe Acute Respiratory Syndrome (SARS) is a new life-threatening respiratory disease which has its origins in Guangdong province, China, where the earliest known cases were identified in November 2002. Since then, probable cases of SARS have been reported in 30 countries and the current cumulative number of cases is 8,240, with 745 deaths and a global fatality rate of 9%. The most frequently involved areas include China, Hong Kong, Singapore, Canada, Vietnam and Philippines. Most cases of SARS to date have occurred in young adults and this disease appears to spread most commonly by close person-to-person contact, involving exposure to infectious droplets and body fluids. This transmission pattern generally involves household members, health care workers and international travellers, while a large and sudden cluster of almost simultaneous cases in an housing estate of Hong Kong has raised the possibility of transmission from an environmental source. The most common presenting symptoms are fever, malaise, non-productive cough and dyspnea, associated with pulmonary interstitial infiltrates on chest radiography. A novel coronavirus is associated with this outbreak, and the laboratory evidences indicate that this virus has an etiologic role in SARS, but the role of other concurrent viral agents (such as metapneumovirus) identified in these patients requires further investigation.","Antibiotics; Coronavirus; Electron microscopy; Molecular analysis; Respiratory failure; Ribavirin; Severe acute respiratory syndrome","ribavirin; Canada; China; Coronavirus; coughing; disease transmission; dyspnea; electron microscopy; epidemic; fatality; fever; health care personnel; Hong Kong; human; lung infiltrate; malaise; Metapneumovirus; Philippines; review; SARS coronavirus; severe acute respiratory syndrome; Singapore; symptomatology; thorax radiography; travel; Viet Nam; virus pneumonia; Adult; Antiviral Agents; Canada; China; Disease Outbreaks; Emergencies; Hong Kong; Humans; Ribavirin; Severe Acute Respiratory Syndrome; Singapore; Taiwan; World Health","Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mort Wkly Rep, 52, pp. 241-248; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348. , in corso di stampa; Lee, N., Hui, D.H., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348. , in corso di stampa; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348. , in corso di stampa; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289. , in corso di stampa; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, , May 1 (in corso di stampa); Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, , May 1 (in corso di stampa); Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1947-1958; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348. , in corso di stampa; Falsey, A.R., McCann, R.M., Hall, W.J., The ""common cold"" in frail order persons: Impact of rhinovirus and coronavirus in a senior daycare center (1997) J Am Geriatr Soc, 45, pp. 706-711; Farr, B.M., Bartlett, C.L., Wadsworth, J., Miller, D.L., Risk factors for community-acquired pneumonia diagnosed upon hospital admission (2000) Respir Med, 94, pp. 954-963; Greensill, J., McNamara, P.S., Dove, W., Flanagan, B., Smyth, R.I., Hart, C.A., Human metapneumovirus in severe respiratory syncytial virus bronchiolitis (2003) Emerg Infect Dis, 9, pp. 372-375; Chua, K.B., Bellini, W.J., Rota, P.A., Nipah virus: A recently emergent deadly paramyxovirus (2000) Science, 288, pp. 1432-1435; Murray, K., Selleck, P., Hooper, P., A morbillivirus that caused fatal disease in horses and humans (1995) Science, 268, pp. 94-97; Smith, D.W., Frankel, L.R., Mathers, L.H., Tang, A.T.S., Ariagno, R.I., Prober, C.G., A controlled trial of aerosolized ribavirin in infants receiving mechanical ventilation for severe respiratory syncytial virus infection (1991) N Engl J Med, 325, pp. 24-29; Sidwell, R.W., Huffman, J.H., Call, E.W., Warren, R.P., Radov, L.A., Murray, R.J., Inhibition of murine hepatitis virus infections by the immunomodulator 2,3,5,6,7,8-hexahydro-2-phenyl-8,8-dimethoxy-imidazo[1,2a]pyridine (PR-879-317A) (1987) Antimicrob Agents Chemother, 31, pp. 1130-1134; Bernard, G.R., Artigas, A., Brigham, K.L., The American-European Consensus Conference on ARDS: Definitions, mechanisms, relevant outcomes, and clinical trial coordination (1994) Am J Respir Crit Care Med, 149, pp. 818-824; Oshiro, L.S., Schieble, J.H., Lennette, E.H., Electron microscopic studies of coronavirus (1971) J Gen Virol, 12, pp. 161-168; Hofmann, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell culture (1988) J Clin Microbiol, 26, pp. 2235-2239; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J Gen Virol, 79, pp. 715-718; Ware, L.B., Matthay, M.A., The acute respiratory distress syndrome (2000) N Engl J Med, 342, pp. 1334-1349; Cho, K.O., Hoet, A.E., Loerch, S.C., Wittum, T.E., Saif, L.J., Evaluation of concurrent shedding of bovine coronavirus via the respiratory tract and enteric route in feedlot cattle (2001) Am J Vet Res, 62, pp. 1436-1441; Boivin, G., Abed, Y., Pelletier, G., Virological features and clinical manifestations associated with human metapneumovirus: A new paramyxovirus responsible for acute respiratory-tract infections in all age groups (2002) J Infect Dis, 186, pp. 1330-1334; Stockton, J., Stephenson, I., Fleming, D., Zambon, M., Human metapneumovirus as a cause of community-acquired respiratory illness (2002) Emerg Infect Dis, 8, pp. 897-901; Nissen, M.D., Siebert, D.J., Mackay, I.M., Sloots, T.P., Withers, S.J., Evidence of human metapneumovirus in Australian children (2002) Med J Aust, 176, p. 188","Calza, L.; Universita Alma Mater Studiorum, Policlinico S. Orsola, Dipto. Med. Clin. Specialistica/S., Via G. Massarenti, 11, 40138 Bologna, Italy; email: calza@med.unibo.it",,,00341193,,RPMDA,"12868233","Italian","Recenti Prog. Med.",Review,"Final",,Scopus,2-s2.0-0042977579
"Ding Y., Wang H., Shen H., Li Z., Geng J., Han H., Cai J., Li X., Kang W., Weng D., Lu Y., Wu D., He L., Yao K.","7404137178;57196429736;35084245300;7409076066;57212700356;8440811700;56517361800;55924516600;36852704100;7005125455;7405480785;57211677067;57211831750;57214495127;","The clinical pathology of severe acute respiratory syndrome (SARS): A report from China",2003,"Journal of Pathology","200","3",,"282","289",,167,"10.1002/path.1440","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038349053&doi=10.1002%2fpath.1440&partnerID=40&md5=78e5b1150b819fc302592e46307562d8","Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China","Ding, Y., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Wang, H., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Shen, H., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Li, Z., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Geng, J., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Han, H., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Cai, J., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Li, X., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Kang, W., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Weng, D., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Lu, Y., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Wu, D., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; He, L., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; Yao, K., Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China","In order to investigate the clinical pathology of severe acute respiratory syndrome (SARS), the autopsies of three patients who died from SARS in Nan Fang Hospital Guangdong, China were studied retrospectively. Routine haematoxylin and eosin (H&E) staining was used to study all of the tissues from the three cases. The lung tissue specimens were studied further with Macchiavello staining, viral inclusion body staining, reticulin staining, PAS staining, immunohistochemistry, ultrathin sectioning and staining, light microscopy, and transmission electron microscopy. The first symptom was hyperpyrexia in all three cases, followed by progressive dyspnoea and lung field shadowing. The pulmonary lesions included bilateral extensive consolidation, localized haemorrhage and necrosis, desquamative pulmonary alveolitis and bronchitis, proliferation and desquamation of alveolar epithelial cells, exudation of protein and monocytes, lymphocytes and plasma cells in alveoli, hyaline membrane formation, and viral inclusion bodies in alveolar epithelial cells. There was also massive necrosis of splenic lymphoid tissue and localized necrosis in lymph nodes. Systemic vasculitis included oedema, localized fibrinoid necrosis, and infiltration of monocytes, lymphocytes, and plasma cells into vessel walls in the heart, lung, liver, kidney, adrenal gland, and the stroma of striated muscles. Thrombosis was present in small veins. Systemic toxic changes included degeneration and necrosis of the parenchyma cells in the lung, liver, kidney, heart, and adrenal gland. Electron microscopy demonstrated clusters of viral particles, consistent with coronavirus, in lung tissue. SARS is a systemic disease that injures many organs. The lungs, immune organs, and systemic small vessels are the main targets of virus attack, so that extensive consolidation of the lung, diffuse alveolar damage with hyaline membrane formation, respiratory distress, and decreased immune function are the main causes of death. Copyright © 2003 John Wiley & Sons, Ltd.",,"eosin; hematoxylin; reticulin; adrenal disease; adult; article; autopsy; bronchitis; case report; cell infiltration; controlled study; Coronavirus; desquamation; dyspnea; edema; female; fever; heart muscle necrosis; histopathology; human; human tissue; hyaline membrane disease; kidney necrosis; liver necrosis; lung alveolitis; lung alveolus epithelium; lung extravascular fluid; lung hemorrhage; lung parenchyma; lymphadenopathy; male; microthrombus; monocyte; plasma cell; priority journal; severe acute respiratory syndrome; spleen disease; staining; symptom; systemic vasculitis; tissue necrosis; transmission electron microscopy; virus detection; virus inclusion; virus pneumonia; Adrenal Glands; Adult; Bone Marrow; Brain; Female; Humans; Immunohistochemistry; Kidney; Liver; Lung; Lymph Nodes; Male; Microscopy, Electron; Middle Aged; Myocardium; Retrospective Studies; Severe Acute Respiratory Syndrome; Spleen","Update: Outbreak of severe acute respiratory syndrome-worldwide (2003) Morb. Mortal Wkly. Rep., 52 (11), pp. 241-248; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1-9. , (published at www.nejm.org. [31 March 2003]); Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1-11. , (published at www.nejm.org. [31 March 2003]); Thomas, G., Ksiazek, D., Erdman, D., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Luby, J.P., Clinton, R., Kurtz, S., Adaptation of human enteric coronavirus to growth in cell lines (1999) J. Clin. Virol., 12, pp. 43-51; Yeager, C.L., Ashmun, R.A., Williams, R.K., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422","Ding, Y.; Department of Pathology, Nan Fang Hospital, First Military Medical University, Guangzhou, Guangdong Province 510515, China; email: dyq@fimmu.com",,,00223417,,JPTLA,"12845623","English","J. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0038349053
"Mckean M.C., Hewitt C., Lambert P.C., Myint St., Silverman M.","7004143832;7202923866;7402303348;35479862600;7403299029;","An adult model of exclusive viral wheeze: Inflammation in the upper and lower respiratory tracts",2003,"Clinical and Experimental Allergy","33","7",,"912","920",,11,"10.1046/j.1365-2222.2003.01715.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038162242&doi=10.1046%2fj.1365-2222.2003.01715.x&partnerID=40&md5=1b5ec87828722da4510ad56e92f99c6b","Dept. of Respiratory Paediatrics, Royal Victoria Infirmary, Newcastle upon Type, United Kingdom; Dept. of Microbiology and Immunology, University of Leicester, Leicester, United Kingdom; Dept. of Epidemiol./Publich Health, University of Leicester, Leicester, United Kingdom; Institute for Long Health, University of Leicester, Leicester, United Kingdom; Anti-Infection Therapy Unit, Glaxo-Smith-Kline, Harlow, Essex, United Kingdom; Department of Child Health, University of Leicester, Leicester, United Kingdom; Dept. of Respiratory Paediatrics, Royal Victoria Infirmary, Queen Victoria Road, Newcastle upon Tyne NEI 4LP, United Kingdom","Mckean, M.C., Dept. of Respiratory Paediatrics, Royal Victoria Infirmary, Newcastle upon Type, United Kingdom, Dept. of Respiratory Paediatrics, Royal Victoria Infirmary, Queen Victoria Road, Newcastle upon Tyne NEI 4LP, United Kingdom; Hewitt, C., Dept. of Microbiology and Immunology, University of Leicester, Leicester, United Kingdom, Institute for Long Health, University of Leicester, Leicester, United Kingdom; Lambert, P.C., Dept. of Epidemiol./Publich Health, University of Leicester, Leicester, United Kingdom; Myint, St., Institute for Long Health, University of Leicester, Leicester, United Kingdom, Anti-Infection Therapy Unit, Glaxo-Smith-Kline, Harlow, Essex, United Kingdom; Silverman, M., Institute for Long Health, University of Leicester, Leicester, United Kingdom, Department of Child Health, University of Leicester, Leicester, United Kingdom","Background: We have previously reported an experimental infection of young adults with a history of episodic and exclusive viral wheeze (EVW) using human coronavirus, in which 16 of 24 with EVW (15 atopic) and 11 of 19 healthy controls (seven atopic) developed a symptomatic cold with evidence of infection, but only those with EVW developed lower respiratory tract symptoms and increased airway responsiveness. Objective: The aim of this study was to compare the EVW and control groups from this study for inflammatory changes occurring in the upper and lower respiratory tracts during the experimental infection, in particular, to determine whether eosinophil-driven inflammation was associated with EVW. Methods: Nasal lavage and induced sputum were collected prior to inoculation (day 0) and 2, 4 and 17 days later. Differential cell counts were performed and supernatant was assayed for IL-8, IL-5, IFN-γ, and eosinophilic cationic protein (ECP). Results: There was no difference between the two groups in any measurement at baseline. In both groups, during colds the volume of nasal secretion increased as did leucocyte counts in both upper and lower respiratory tracts. A modest increase in nasal neutrophil count was seen in both EVW and control groups with symptomatic colds on day 2 (median (quartile) difference from baseline 5.4 (0.0, 11.0) and 1.8 ( - 1.1, 2.2) × 104/mL of secretions, respectively). The change in nasal neutrophil counts in all subjects correlated with nasal symptom scores. A significant relative increase in sputum differential neutrophil count was seen on day 4 in the EVW group with a cold but not in controls (mean difference (95% confidence interval) 20.4 (9.6, 31.1)% and 3.1 (- 8.2, 14.5)%, respectively, P&lt;0.01); however, this increase did not correlate with lower respiratory tract symptom scores. IL-8 increased in both the upper and lower respiratory tracts in both EVW and control subjects with colds, the largest change being seen on day 4 in the sputum of those with EVW (mean difference from baseline (95% confidence interval) 2.5 (0.55-4.46) ng/mL). Only modest changes were seen in IFN-γ and no changes were seen in IL-5 or ECP. Norte of the results was influenced by the atopic status of the subjects in either group. Conclusions: EVW wheeze is characterized by neutrophilic inflammation in both the upper and lower respiratory tracts without eosinophilia (even in atopic subjects). IL-8 is likely to be an important chemokine in this process. Symptoms and airway responsiveness were correlated with change in neutrophils.","Common cold; Exclusive viral wheeze; Human coronavirus; Neutrophil","eosinophil cationic protein; gamma interferon; interleukin 5; interleukin 8; adult; article; clinical article; common cold; controlled study; Coronavirus; exclusive viral wheeze; female; human; human tissue; lavage; leukocyte count; leukocyte differential count; lower respiratory tract; male; neutrophil; nose secretion; priority journal; respiratory tract inflammation; sputum; upper respiratory tract; wheezing; Common Cold; Enzyme-Linked Immunosorbent Assay; Eosinophils; Forced Expiratory Volume; Humans; Inflammation; Interleukin-8; Nose; Respiratory Sounds; Respiratory Tract Infections; Sputum","Martinez, F.D., Wright, A.L., Taussig, L.M., Asthma and wheezing in the first six years of life (1995) N Engl J M, 332, pp. 133-138; Stevenson, E.C., Turner, G., Heaney, L.G., Bronchoalveolar lavage findings suggest two different forms of childhood asthma (1997) Clin Exp Allergy, 27, pp. 1027-1035; Godden, D.J., Ross, S., Abdalla, M., Outcome of wheeze in childhood. Symptoms and pulmonary function 25 years later (1994) Am J Respir Crit Care Med, 149, pp. 106-112; Mckean, M.C., Leech, M., Lambert, P.L., Hewitt, C., Myint, S., Silverman, M., A model of viral wheeze in non-asthmatic adults: Symptoms and physiology (2001) Europ Respir J, 18, pp. 23-32; Fahy, J.V., Kwong Woo, K., Liu, J., Boushey, H.A., Respiratory pathophysiologic responses: Prominent neutrophilic inflammation in sputum from subjects with asthma exacerbation (1995) J Allergy Clin Immunol, 95, pp. 843-852; Pizzichini, M.M.M., Pizzichini, E., Efthimiadis, A., Asthma and natural colds- Inflammatory indices in induced sputum: A feasibility study (1998) Am J Respir Crit Care Med, 158, pp. 1178-1184; Fraenkel, D.J., Bardin, P.G., Sanderson, G., Lampe, F., Johnston, S.L., Holgate, S.T., Lower airways inflammation during rhinovirus colds in normal and in asthmatic subjects (1995) Europ Arch Oto-Rhino-Laryngol, 151 S, pp. 879-886; Grunberg, K., Smits, H.H., Timmers, M.C., Experimental rhinovirus 16 infection: Effects on cell differentials and soluble markers in sputum in asthmatic subjects (1997) Am J Respir Crit Care Med, 156, pp. 609-616; Fleming, H.E., Little, F.F., Schnurr, D., Rhinovirus-16 colds in healthy and in asthmatic subjects: Similar changes in upper and lower airways (1999) Am J Respir Crit Care Med, 160, pp. 100-108; Grunberg, K., Sharon, R.F., Sont, J.K., Rhinovirus-induced airway inflammation in asthma: Effect of treatment with inhaled corticosteroids before and during experimental infection (2001) Am J Respir Crit Care Med, 15 (164), pp. 1816-1822; Turner, R.B., The role of neutrophils in the pathogenesis of rhinovirus infections (1990) Ped Infectious Dis J, 9, pp. 832-835; Noah, T.L., Henderson, F.W., Wortman, I.A., Nasal cytokine production in viral acute upper respiratory infection of childhood (1995) J Infect Dis, 171, pp. 584-592; Noah, T.L., Henderson, F.W., Henry, M.M., Peden, D.B., Devlin, R.B., Nasal lavage cytokines in normal, allergic, and asthmatic schoolage children (1995) Am J Respir Crit Care Med, 152, pp. 1290-1296; Teran, L.M., Johnston, S.L., Schroder, J., Church, M.K., Holgate, S.T., Role of nasal interleukin-8 in neutrophil recruitment and activation in children with virus-induced asthma (1997) Am J Respir Crit Care Med, 155, pp. 1362-1366; Greiff, L., Andersson, M., Svensson, C., Linden, M., Myint, S., Persson, C.G.A., Allergen challenge-induced acute exudation of IL-8, ECP and alpha2- macroglobulin in human rhinovirus-induced common colds (1999) Europ Respir J, 13, pp. 41-47; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; McIntosh, K., Chao, R.K., Krause, H.E., Wasil, R., Mocega, H.E., Mufson, M.A., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Siddell, S., Myint, S., Coronaviruses (1996) Viral and Other Infections of the Human Respiratory Tract, , Myint S, Taylor-Robinsob D, eds. London: Chapman & Hall; Balfour-Lynn, I.M., Valman, B., Silverman, M., Webster, A.D.B., Nasal IgA response in wheezy infants (1993) Arch Dis Child, 68, pp. 472-476; Pizzichini, E., Pizzichini, M.M.M., Efthimiadis, A., Indices of airway inflammation in induced sputum: Reproducibility and validity of cell and fluid-phase measurements (1996) Am J Respir Crit Care Med, 154, pp. 308-317; Von Mutius, E., Is asthma really linked to atopy? (2001) Clin Exp Allergy, 31, pp. 1651-1652; Kuehni, C.E., Davis, A., Brooke, A.M., Silverman, M., Are all wheezing disorders in very young (preschool) children increasing in prevalence? (2001) Lancet, 357, pp. 1821-1825; Myint, S., Siddell, S., Tyrrell, D., Detection of human coronavirus 229E in nasal washings using RNA: RNA hybridisation (1989) J Med Virol, 29, pp. 70-73; Chilvers, M.A., Mckean, M.C., Rutman, A., Myint, S., Silverman, M., O'Callaghan, C., The effects of coronavirus on human nasal ciliated respiratory epithelium (2001) Europ Respir J, 18, pp. 965-970; Bardin, P.G., Fraenkel, D.J., Sanderson, G., Dorward, M., Lau, L.C., Johnston, S.L., Amplified rhinovirus colds in atopic subjects (1994) Clin Exp Allergy, 24, pp. 457-464; Callow, K.A., Tyrrell, D.A., Shaw, R.J., Fitzharris, P., Wardlaw, A.J., Kay, A.B., Influence of atopy on the clinical manifestations of coronavirus infection in adult volunteers (1988) Clin Exp Allergy, 18, pp. 119-129; Holz, O., Richter, K., Jorres, R.A., Speckin, P., Mucke, M., Magnussen, H., Changes in sputum composition between two inductions performed on consecutive days (1998) Thorax, 53, pp. 83-86; Pavord, I.D., Sputum induction to assess airway inflammation: Is it an inflammatory stimulus? (1998) Thorax, 53, pp. 79-80; Simpson, J.L., Gibson, P.G., Ward, P.A., Optimisation of sputum-processing methods for the measurement of interleukin-5: Effects of protease inhibition (2002) Respirology, 7, pp. 111-116; Hauser, R., Garcia-Closas, M., Kelsey, K.T., Christiani, D.C., Variability of nasal lavage polymorphonuclear leukocyte counts in unexposed subjects: Its potential utility for epidemiology (1994) Arch Environ Health, 49, pp. 267-272; Everard, M.L., Swarbrick, A., Wrightham, M., McIntyre, J., Dunkley, C., James, P.D., Analysis of cells obtained by bronchial lavage of infants with respiratory syncytial virus infection (1994) Arch Dis Child, 71, pp. 428-432; Gern, J.E., Galagan, D.M., Jarjour, N.N., Dick, E.C., Busse, W.W., Detection of rhinovirus RNA in lower airway cells during experimentally induced infection (1997) Am J Respir Crit Care Med, 155, pp. 1159-1161; Papadopoulos, N.G., Sanderson, G., Hunter, J., Johnston, S.L., Rhinoviruses replicate effectively at lower airway temperatures (1999) J Med Virol, 58, pp. 100-104; Papadopoulos, N.G., Bates, P.J., Bardin, P.G., Rhinoviruses infect the lower airways (2000) J Inf Dis, 181, pp. 1875-1884; Fontanari, P., Zattara-Hartmann, M., Burnet, H., Jammes, Y., Nasal eupnoeic inhalation of cold, dry air increases airway resistance in asthmatic patients (1997) Europ Respir J, 10, pp. 2250-2254","Mckean, M.C.; Dept. of Respiratory Paediatrics, Royal Victoria Infirmary, Queen Victoria Road, Newcastle upon Tyne NEI 4LP, United Kingdom; email: Michael.Mckean@nuth.northy.nhs.uk",,,09547894,,CLEAE,"12859447","English","Clin. Exp. Allergy",Article,"Final",,Scopus,2-s2.0-0038162242
"Tsui S.K.W., Chim S.S.C., Lo Y.M.D.","7004961364;6701728226;7401935391;","Coronavirus genomic-sequence variations and the epidemiology of the severe acute respiratory syndrome [1]",2003,"New England Journal of Medicine","349","2",,"187","188",,55,"10.1056/NEJM200307103490216","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037775607&doi=10.1056%2fNEJM200307103490216&partnerID=40&md5=e7ba30f895f30575dc68bc09f2e8a444","Chinese University of Hong Kong, Shatin, New Territories, Hong Kong","Tsui, S.K.W., Chinese University of Hong Kong, Shatin, New Territories, Hong Kong; Chim, S.S.C., Chinese University of Hong Kong, Shatin, New Territories, Hong Kong; Lo, Y.M.D., Chinese University of Hong Kong, Shatin, New Territories, Hong Kong",[No abstract available],,"glycoprotein; nucleotide; membrane protein; spike glycoprotein, coronavirus; virus envelope protein; adult; amino acid sequence; China; clinical article; Coronavirus; disease severity; epidemic; female; gene; gene sequence; genome; Hong Kong; human; letter; nucleotide sequence; pneumonia; priority journal; SARS coronavirus; severe acute respiratory distress syndrome; strain identification; teaching hospital; virus isolation; virus strain; classification; DNA sequence; genetics; Hong Kong; isolation and purification; molecular genetics; nucleotide sequence; SARS coronavirus; severe acute respiratory syndrome; virology; virus genome; Base Sequence; Female; Genome, Viral; Hong Kong; Humans; Membrane Glycoproteins; Molecular Sequence Data; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome; Viral Envelope Proteins","Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peiris, J.S., Lai, S.T., Poon, L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-246; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985","Tsui, S.K.W.; Chinese University of Hong Kong, Shatin, New Territories, Hong Kong; email: loym@cuhk.edu.hk",,,00284793,,NEJMA,"12853594","English","New Engl. J. Med.",Letter,"Final",,Scopus,2-s2.0-0037775607
"Lin-Liu J.","6602640011;","A microbiologist on the front lines",2003,"Chronicle of Higher Education","49","45",,"A35","A36",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041767387&partnerID=40&md5=52d434321b64723e0a93ab625f502e9a",,"Lin-Liu, J.","An account of the efforts of a Honk Kong University microbiologist, Yuen Kwok-Yung, in fighting severe acute respiratory syndrome (SARS) is reported. Dr. Yuen's team was the first to trace the disease to a type of virus known as Coronavirus. His team also provided the evidences that wild animals consumed as food in southern China might be the source behind SARS. The drug combinations offered by this team was later adopted by Toronto physicians.",,"Antibiotics; Disease control; Education; Health care; Pulmonary diseases; Societies and institutions; Viruses; Infections; Microbiology",,,,"Allen Press Inc.",00095982,,,,"English","Chron High Educ",Review,"Final",,Scopus,2-s2.0-0041767387
"Corse E., Machamer C.E.","36957600500;7004585797;","The cytoplasmic tails of infectious bronchitis virus E and M proteins mediate their interaction",2003,"Virology","312","1",,"25","34",,72,"10.1016/S0042-6822(03)00175-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042167579&doi=10.1016%2fS0042-6822%2803%2900175-2&partnerID=40&md5=b5fc721469ea92b14bc94f527041a348","Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, United States","Corse, E., Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, United States; Machamer, C.E., Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, United States","Virus-like particle (VLP) formation by the coronavirus E and M proteins suggests that interactions between these proteins play a critical role in coronavirus assembly. We studied interactions between the infectious bronchitis virus (IBV) E and M proteins using in vivo crosslinking and VLP assembly assays. We show that IBV E and M can be crosslinked to each other in IBV-infected and transfected cells, indicating that they interact. The cytoplasmic tails of both proteins are important for this interaction. We also examined the ability of the mutant and chimeric E and M proteins to form VLPs. IBV M proteins that are missing portions of their cytoplasmic tails or transmembrane regions were not able to support VLP formation, regardless of their ability to be crosslinked to IBV E. Interactions between the E and M proteins and the membrane bilayer are likely to play an important role in VLP formation and virus budding. © 2003 Elsevier Science (USA). All rights reserved.","Coronavirus; Enveloped virus assembly; Infectious bronchitis virus; Virus-like particle","protein e; protein m; unclassified drug; virus protein; animal cell; article; Avian infectious bronchitis virus; chimera; Coronavirus; cross linking; cytoplasm; genetic transfection; nonhuman; priority journal; protein interaction; virus morphology; virus particle; Avian infectious bronchitis virus; Coronavirus","Barr, F.A., Nakamura, N., Warren, G., Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae (1998) EMBO J., 17, pp. 3258-3268; Baudoux, P., Carrat, C., Besnardeau, L., Charley, B., Laude, H., Coronavirus pseudoparticles formed with recombinant M and E proteins induce alpha interferon synthesis by leukocytes (1998) J. Virol., 72, pp. 8636-8643; Corse, E., Machamer, C.E., Infectious bronchitis virus E protein is targeted to the Golgi complex and directs release of virus-like particles (2000) J. Virol., 74, pp. 4319-4326; Corse, E., Machamer, C.E., Infectious bronchitis virus envelope protein targeting: Implications for virus assembly (2001) Adv Exp. Med. Biol., 494, pp. 571-576; Corse, E., Machamer, C.E., The cytoplasmic tail of infectious bronchitis virus E protein directs Golgi targeting (2002) J. Virol., 76, pp. 1273-1284; De Haan, C.A., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; De Haan, C.A., Vennema, H., Rottier, P.J., Assembly of the coronavirus envelope: Homotypic interactions between the M proteins (2000) J. Virol., 74, pp. 4967-4978; Dubois-Dalcq, M., Holmes, K.V., Rentier, B. 1984. Assembly of Enveloped RNA Viruses. Kingsbury, D.W. (Ed.) Springer-Verlag, Wien New York; Elroy-Stein, O., Moss, B., Cytoplasmic expression system based on constitutive synthesis of bacteriophage T7 RNA polymerase in mammalian cells (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6743-6747; Fischer, F., Stegen, C.F., Masters, P.S., Samsonoff, W.A., Analysis of constructed E gene mutants of mouse hepatitis virus confirms a pivotal role for E protein in coronavirus assembly (1998) J. Virol., 72, pp. 7885-7894; Fuerst, T.R., Giles, E.G., Studier, F.W., Moss, B., Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase (1986) Proc. Nat. Acad Sci., 83, pp. 8122-8126; Garoff, H., Hewson, R., Opstelten, D.J., Virus maturation by budding (1998) Microbiol. Mol. Biol. Rev., 62, pp. 1171-1190; Godeke, G.J., De Haan, C.A., Rossen, J.W., Vennema, H., Rottier, P.J., Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein (2000) J. Virol., 74, pp. 1566-1571; Griffiths, G., Rottier, P., Cell biology of viruses that assemble along the biosynthetic pathway (1992) Semin. Cell. Biol., 3, pp. 367-381; Hung, T., Chou, Z.Y., Zhao, T.X., Xia, S.M., Hang, C.S., Morphology and morphogenesis of viruses of hemorrhagic fever with renal syndrome (HFRS). I. Some peculiar aspects of the morphogenesis of various strains of HFRS virus (1985) Intervirology, 23, pp. 97-108; Klumperman, J., Locker, J.K., Meijer, A., Horzinek, M.C., Geuze, H.J., Rottier, P.J., Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding (1994) J. Virol., 68, pp. 6523-6534; Lim, K.P., Liu, D.X., The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins (2001) J. Biol. Chem., 276, pp. 17515-17523; Liu, D.X., Inglis, S.C., Association of the infectious bronchitis virus 3c protein with the virion envelope (1991) Virology, 185, pp. 911-917; Machamer, C.E., Grim, M.G., Esquela, A., Chung, S.W., Rolls, M., Ryan, K., Swift, A.M., Retention of a cis Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain (1993) Mol. Biol. Cell, 4, pp. 695-704; Machamer, C.E., Mentone, S.A., Rose, J.K., Farquhar, M.G., The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 6944-6948; Machamer, C.E., Rose, J.K., A specific transmembrane domain of a coronavirus E1 glycoprotein is required for its retention in the Golgi region (1987) J. Cell Biol., 105, pp. 1205-1214; Mackenzie, J.M., Westaway, E.G., Assembly and maturation of the flavivirus kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively (2001) J. Virol., 75, pp. 10787-10799; Maeda, J., Maeda, A., Makino, S., Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells (1999) Virology, 263, pp. 265-272; Pettersson, R.F., Protein localization and virus assembly at intracellular membranes (1991) Curr. Top. Microbiol. Immunol., 170, pp. 67-106; Seemann, J., Jokitalo, E., Pypaert, M., Warren, G., Matrix proteins can generate the higher order architecture of the Golgi apparatus (2000) Nature, 407, pp. 1022-1026; Seemann, J., Jokitalo, E.J., Warren, G., The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo (2000) Mol. Biol. Cell, 11, pp. 635-645; Stern, D.F., Burgess, L., Sefton, B.M., Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus (1982) J. Virol., 42, pp. 208-219; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Swift, A.M., Machamer, C.E., A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein (1991) J. Cell Biol., 115, pp. 19-30; Vennema, H., Godeke, G.J., Rossen, J.W., Voorhout, W.F., Horzinek, M.C., Opstelten, D.J., Rottier, P.J., Nucleocapsid-independent assembly of coronavirus-like particles by co- expression of viral envelope protein genes (1996) EMBO, J15, pp. 2020-2028; Weisz, O.A., Machamer, C.E., Use of recombinant vaccinia virus vectors for cell biology (1994) Methods Cell Biol., 43, pp. 137-159; Weisz, O.A., Swift, A.M., Machamer, C.E., Oligomerization of a membrane protein correlates with its retention in the Golgi complex (1993) J. Cell Biol., 122, pp. 1185-1196","Machamer, C.E.; Department of Cell Biology, Johns Hopkins Univ. Sch. of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, United States; email: machamer@jhmi.edu",,"Academic Press Inc.",00426822,,VIRLA,"12890618","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0042167579
"Chen L.-L., Ou H.-Y., Zhang R., Zhang C.-T.","35226293800;7005561046;7404865123;55566455000;","ZCURVE_CoV: A new system to recognize protein coding genes in coronavirus genomes, and its applications in analyzing SARS-CoV genomes",2003,"Biochemical and Biophysical Research Communications","307","2",,"382","388",,28,"10.1016/S0006-291X(03)01192-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038690315&doi=10.1016%2fS0006-291X%2803%2901192-6&partnerID=40&md5=ffdcac1abf2937c885e9b4c446d0c366","Department of Physics, Tianjin University, Tianjin 300072, China; Department of Biology, Shandong University of Technology, Zibo 255049, China; Dept. of Epidemiol./Biostatistics, Tianjin Cancer Inst. and Hospital, Tianjin 300060, China","Chen, L.-L., Department of Physics, Tianjin University, Tianjin 300072, China, Department of Biology, Shandong University of Technology, Zibo 255049, China; Ou, H.-Y., Department of Physics, Tianjin University, Tianjin 300072, China; Zhang, R., Dept. of Epidemiol./Biostatistics, Tianjin Cancer Inst. and Hospital, Tianjin 300060, China; Zhang, C.-T., Department of Physics, Tianjin University, Tianjin 300072, China","A new system to recognize protein coding genes in the coronavirus genomes, specially suitable for the SARS-CoV genomes, has been proposed in this paper. Compared with some existing systems, the new program package has the merits of simplicity, high accuracy, reliability, and quickness. The system ZCURVE_CoV has been run for each of the 11 newly sequenced SARS-CoV genomes. Consequently, six genomes not annotated previously have been annotated, and some problems of previous annotations in the remaining five genomes have been pointed out and discussed. In addition to the polyprotein chain ORFs 1a and 1b and the four genes coding for the major structural proteins, spike (S), small envelop (E), membrane (M), and nuleocaspid (N), respectively, ZCURVE_CoV also predicts 5-6 putative proteins in length between 39 and 274 amino acids with unknown functions. Some single nucleotide mutations within these putative coding sequences have been detected and their biological implications are discussed. A web service is provided, by which a user can obtain the annotated result immediately by pasting the SARS-CoV genome sequences into the input window on the web site (http://tubic.tju.edu.cn/sars/). The software ZCURVE_CoV can also be downloaded freely from the web address mentioned above and run in computers under the platforms of Windows or Linux. © 2003 Elsevier Inc. All rights reserved.","Coronavirus; Gene-finding; Genome; Mutation; SARS-CoV; Severe acute respiratory syndrome","amino acid; nucleotide; polyprotein; protein; structural protein; accuracy; article; Avian infectious bronchitis virus; computer program; Coronavirus; gene sequence; genetic code; genome analysis; intermethod comparison; membrane; Murine hepatitis coronavirus; mutation; nonhuman; nucleotide sequence; open reading frame; prediction; priority journal; protein analysis; protein function; reliability; SARS coronavirus; Transmissible gastroenteritis virus; virus envelope; virus genome; virus nucleocapsid; Coronavirus","Peiris, J.S., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Tsang, K.W., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Lee, N., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Poutanen, S.M., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1398; Marra, M.A., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Qin, E'd., A complete sequence and comparative analysis of strain (BJ01) of the SARS-associated virus (2003) Chinese Sci. Bull., 48, pp. 941-948; Besemer, J., Borodovsky, M., Heuristic approach to deriving models for gene finding (1999) Nucleic Acids Res., 27, pp. 3911-3920; Salzberg, S.L., Delcher, A.L., Kasif, S., White, O., Microbial gene identification using interpolated Markov models (1998) Nucleic Acids Res., 26, pp. 544-548; Guo, F.B., Ou, H.Y., Zhang, C.-T., ZCURVE: A new system for recognizing protein coding genes in bacterial and archaeal genomes (2003) Nucleic Acids Res., 31, pp. 1780-1789; Zhang, C.-T., Zhang, R., Analysis of distribution of bases in the coding sequences by a diagrammatic technique (1991) Nucleic Acids Res., 19, pp. 6313-6317; Zhang, C.-T., Wang, J., Recognition of protein coding genes in the yeast genome at better than 95% accuracy based on the Z curve (2000) Nucleic Acids Res., 28, pp. 2804-2814; Jenkins, G.M., Holmes, E.C., The extent of codon usage bias in human RNA viruses and its evolutionary origin (2003) Virus Res., 92, pp. 1-7; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22, pp. 4673-4680","Zhang, C.-T.; Department of Physics, Tianjin University, Tianjin 300072, China; email: ctzhang@tju.edu.cn",,"Academic Press Inc.",0006291X,,BBRCA,"12859968","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-0038690315
"Kuiken T., Fouchier R.A.M., Schutten M., Rimmelzwaan G.F., Van Amerongen G., Van Riel D., Laman J.D., De Jong T., Van Doornum G., Lim W., Ling A.E., Chan P.K.S., Tam J.S., Zambon M.C., Gopal R., Drosten C., Van Der Werf S., Escriou N., Manuguerra J.-C., Stöhr K., Peiris J.S.M., Osterhaus A.D.M.E.","26643529400;7006060466;7004005251;7005416180;7004695265;6602932722;21635097100;7201837394;7005445921;7202378277;7102194546;32067487100;24788939600;7006818684;7102284995;7003813990;7005851162;6603606703;7003610543;55942879600;7005486823;55533604400;","Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome",2003,"Lancet","362","9380",,"263","270",,545,"10.1016/S0140-6736(03)13967-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042198682&doi=10.1016%2fS0140-6736%2803%2913967-0&partnerID=40&md5=1effcdd67284120fbaa9c4deed7846d9","Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Department of Immunology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Department of Pathology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Government Virus Unit, Public Health Laboratory Centre, Shek Kip Mei, Kowloon, Hong Kong; Department of Pathology, Singapore General Hospital, Singapore, Singapore; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Kong Kong, Hong Kong; Enteric Resp./Neurol. Virus Lab., Health Protection Agency, London, United Kingdom; Department of Virology, Bernhard-Nocht Inst. for Trop. Med., Hamburg, Germany; U. Genet. Molec. Virus Respiratoires, Institut Pasteur, Paris, France; SARS Aetiology Study Group, WHO, Geneva, Switzerland; Dept. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong","Kuiken, T., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Fouchier, R.A.M., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Schutten, M., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Rimmelzwaan, G.F., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Van Amerongen, G., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Van Riel, D., Department of Immunology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Laman, J.D., Department of Immunology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; De Jong, T., Department of Pathology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Van Doornum, G., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; Lim, W., Government Virus Unit, Public Health Laboratory Centre, Shek Kip Mei, Kowloon, Hong Kong; Ling, A.E., Department of Pathology, Singapore General Hospital, Singapore, Singapore; Chan, P.K.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Kong Kong, Hong Kong; Tam, J.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Kong Kong, Hong Kong; Zambon, M.C., Enteric Resp./Neurol. Virus Lab., Health Protection Agency, London, United Kingdom; Gopal, R., Enteric Resp./Neurol. Virus Lab., Health Protection Agency, London, United Kingdom; Drosten, C., Department of Virology, Bernhard-Nocht Inst. for Trop. Med., Hamburg, Germany; Van Der Werf, S., U. Genet. Molec. Virus Respiratoires, Institut Pasteur, Paris, France; Escriou, N., U. Genet. Molec. Virus Respiratoires, Institut Pasteur, Paris, France; Manuguerra, J.-C., U. Genet. Molec. Virus Respiratoires, Institut Pasteur, Paris, France; Stöhr, K., SARS Aetiology Study Group, WHO, Geneva, Switzerland; Peiris, J.S.M., Dept. of Microbiology and Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Osterhaus, A.D.M.E., Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands","Background: The worldwide outbreak of severe acute respiratory syndrome (SARS) is associated with a newly discovered coronavirus, SARS-associated coronavirus (SARS-CoV). We did clinical and experimental studies to assess the role of this virus in the cause of SARS. Methods: We tested clinical and postmortem samples from 436 SARS patients in six countries for infection with SARS-CoV, human metapneumovirus, and other respiratory pathogens. We infected four cynomolgus macaques (Macaca fascicularis) with SARS-CoV in an attempt to replicate SARS and did necropsies on day 6 after infection. Findings: SARS-CoV infection was diagnosed in 329 (75%) of 436 patients fitting the case definition of SARS; human metapneumovirus was diagnosed in 41 (12%) of 335, and other respiratory pathogens were diagnosed only sporadically. SARS-CoV was, therefore, the most likely causal agent of SARS. The four SARS-CoV-infected macaques excreted SARS-CoV from nose, mouth, and pharynx from 2 days after infection. Three of four macaques developed diffuse alveolar damage, similar to that in SARS patients, and characterised by epithelial necrosis, serosanguineous exudate, formation of hyaline membranes, type 2 pneumocyte hyperplasia, and the presence of syncytia. SARS-CoV was detected in pneumonic areas by virus isolation and RT-PCR, and was localised to alveolar epithelial cells and syncytia by immunohistochemistry and transmission electron microscopy. Interpretation: Replication in SARS-CoV-infected macaques of pneumonia similar to that in human beings with SARS, combined with the high prevalence of SARS-CoV infection in SARS patients, fulfill the criteria required to prove that SARS-CoV is the primary cause of SARS.",,"animal cell; animal tissue; article; autopsy; cell hyperplasia; clinical article; clinical feature; controlled study; Coronavirus; fetus; human; human cell; hyaline membrane disease; immunohistochemistry; lung alveolus; lung alveolus cell type 2; lung alveolus epithelium; lung extravascular fluid; lung injury; Macaca; Metapneumovirus; microbiological examination; mouth; necrosis; nonhuman; nose; pharynx; prevalence; priority journal; Respiratory syncytial pneumovirus; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; transmission electron microscopy; virus infection; virus isolation; virus pneumonia; virus replication","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/country/2003_07_03; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Pneumonia-China (Guangdong), , http://www.promedmail.org/pls/askus/ f?p=2400:1202:400889022850976471::NO:: F2400_P1202_CHECK_DISPLAY,F2400_P1202_PUB_MAIL_ID:X,20691; Pneumonia-China (Guangdong), , http://www.promedmail.org/pls/askus/ f?p=2400:1202:400889022850976471::NO:: F2400_P1202_CHECK_DISPLAY,F2400_P1202_PUB_MAIL_ID:X,20755; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Peiris, J.S., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Peiris, J.S.M., Tang, W.H., Chan, K.H., Children with respiratory disease associated with metapneumovirus in Hong Kong (2003) Emerg Infect Dis, 9, pp. 628-633; PCR Primers for SARS Developed by WHO Network Laboratories, , http://www.who.int/csr/sars/primers/en/; Stephensen, C.B., Casebolt, D.B., Gangopadhyay, N.N., Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay (1999) Virus Res, 60, pp. 181-189; Peret, T.C.T., Boivin, G., Li, Y., Characterization of human metapneumoviruses isolated from patients in North America (2002) J Infect Dis, 185, pp. 1660-1663; Chan, P.K.S., Tam, J.S., Lam, C.W., Detection of human metapneumovirus from patients with severe acute respiratory syndrome: A methodological evaluation Emerg Infect Dis, , in press; Fouchier, R.A., Bestebroer, T.M., Herfst, S., Van Der, K.L., Rimmelzwaan, G.F., Osterhaus, A.D., Detection of influenza A viruses from different species by PCR amplification of conserved sequences in the matrix gene (2000) J Clin Microbiol, 38, pp. 4096-4101; Lai, M.M.C., Holmes, K.V., Coronaviridae: The viruses and their replication (1999) Fields virology, pp. 1163-1185. , D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott Williams and Wilkins; Claas, H.C., Melchers, W.J.G., De Bruijn, I.H., Detection of Chlamydia trachomatis in clinical specimens by the polymerase chain reaction (1990) Eur J Clin Microbiol Infect Dis, 9, pp. 864-868; Reischl, U., Lehn, N., Simnacher, U., Marre, R., Essig, A., Rapid and standardised detection of Chlamydia pneumoniae using LightCycler real-time fluorescence PCR (2003) Eur J Clin Microbiol Infect Dis, 22, pp. 54-57; Mahy, B.W.J., (1997) A dictionary of virology 2nd edn, , San Diego: Academic Press; Van den Hoogen, B.G., De Jong, J.C., A newly discovered human metapneumovirus isolated from young children with respiratory tract disease (2001) Nat Medicine, 7, pp. 719-724; Bhatt, P.N., Jacoby, R.O., Experimental infection of adult axenic rats with Parker's rat coronavirus (1977) Arch Virol, 54, pp. 345-352; O'Toole, D., Brown, I., Bridges, A., Cartwright, S.F., Pathogenicity of experimental infection with 'pneumotropic' porcine coronavirus (1989) Res Vet Sci, 47, pp. 23-29; Myers, J.L., Colby, T.V., Yousem, S.A., Common pathways and patterns of injury (1993) Pulmonary pathology, pp. 57-77. , D.H. Dail, & S.P. Hammar. New York: Springer-Verlag; Dungworth, D.L., The respiratory system (1993) Pathology of domestic animals, 2, pp. 539-699. , K.V.F. Jubb, P.C. Kennedy, & N. Palmer. San Diego: Academic Press; Jabrane, A., Girard, C., Elazhary, Y., Pathogenicity of porcine respiratory coronavirus isolated in Québec (1994) Can Vet J, 35, pp. 86-92; Schneider-Schaulies, S., Ter Meulen, V., Measles virus and immunomodulation: Molecular bases and perspectives (2002) Expert Rev Mol Med, , http://expertreviews.org/02004696h.htm","Kuiken, T.; Departments of Virology, Erasmus Medical Centre, PO Box 1738, 3000 DR Rotterdam, Netherlands; email: t.kuiken@erasmusmc.nl",,"Elsevier Limited",01406736,,LANCA,"12892955","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0042198682
[No author name available],[No author id available],"Coronavirus is cause of SARS",2003,"Pharmaceutical Journal","271","7259",,"108","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-85076942885&partnerID=40&md5=2150631e2039e3dc903858ccd19dd522",,"",[No abstract available],,"autopsy; clinical examination; Coronavirus; Internet; nonhuman; note; pneumonia; publication; sample; SARS coronavirus; severe acute respiratory syndrome",,,,"Pharmaceutical Press",00316873,,PHJOA,,"English","Pharm. J.",Note,"Final",,Scopus,2-s2.0-85076942885
"Cinatl J., Morgenstern B., Bauer G., Chandra P., Rabenau H., Doerr H.W.","57216110934;7005523214;55425118700;7202774450;7004984201;7102740671;","Treatment of SARS with human interferons",2003,"Lancet","362","9380",,"293","294",,213,"10.1016/S0140-6736(03)13973-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0043200981&doi=10.1016%2fS0140-6736%2803%2913973-6&partnerID=40&md5=405a8701042601ff0e532bf59bdf236d","Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany","Cinatl, J., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; Morgenstern, B., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; Bauer, G., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; Chandra, P., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; Rabenau, H., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; Doerr, H.W., Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany","Effective antiviral agents are needed to treat severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infection. We assessed the antiviral potential of recombinant interferons against two clinical isolates of SARS-CoV - FFM-1, from Frankfurt patients, and Hong Kong - replicated in Vero and Caco2 cells. Interferon β was five to ten times more effective in Caco2 cells. Interferon α effectively inhibited SARS-CoV replication, but with a selectivity index 50-90 times lower than that for interferon β. Interferon γ was slightly better than interferon α in Vero cell cultures, but was completely ineffective in Caco2 cell cultures. Interferon β could be useful alone or in combination with other antiviral drugs for the treatment of SARS.",,"alpha interferon; antivirus agent; beta interferon; gamma interferon; recombinant interferon; animal cell; article; cell strain CACO 2; controlled study; Coronavirus; drug efficacy; drug potency; drug selectivity; drug sensitivity; Hong Kong; human; human cell; nonhuman; priority journal; SARS coronavirus; severe acute respiratory syndrome; United States; Vero cell; virus isolation; virus pneumonia; virus replication","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Cinatl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H., Doerr, H.W., Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus (2003) Lancet, 361, pp. 2045-2046; Garcia, S., Crance, J.M., Billecocq, A., Quantitative real-time PCR detection of Rift Valley fever virus and its application to evaluation of antiviral compounds (2001) J Clin Microbiol., 39, pp. 4456-4461; Der, S.D., Zhou, A., Williams, B.R., Silverman, R.H., Identification of genes differentially regulated by interferon alpha, beta, or gamma using oligonucleotide arrays (1998) Proc Natl Acad Sci USA., 95, pp. 15623-15628; Pitkaranta, A., Nokso-Koivisto, J., Jantti, V., Takala, A., Kilpi, T., Hovi, T., Lowered yields of virus-induced interferon production in leukocyte cultures and risk of recurrent respiratory infections in children (1999) J Clin Virol, 14, pp. 199-205","Cinatl, J.; Institute of Medical Virology, Frankfurt University Medical School, Paul-Ehrlich Strasse 40, D-60596 Frankfurt, Germany; email: cinatl@em.uni-frankfurt.de",,"Elsevier Limited",01406736,,LANCA,"12892961","English","Lancet",Article,"Final",,Scopus,2-s2.0-0043200981
"Gelinck L.B.S., Van Steenbergen J.E., Van Dissel J.T.","6506814919;6701669160;7006432720;","Severe acute respiratory syndrome (SARS): Epidemiology, clinical signs, diagnosis and prevention ['Severe acute respiratory syndrome' (SARS): Epidemiologie, kliniek, diagnostiek en preventie]",2003,"Nederlands Tijdschrift voor Geneeskunde","147","30",,"1449","1454",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041323315&partnerID=40&md5=a61e11f1b0e6d563a5aa1723ecebfcb1","Leids Universitair Medisch Centrum, Afd. Infectieziekten, Postbus 9600, 2300 RC Leiden, Netherlands","Gelinck, L.B.S., Leids Universitair Medisch Centrum, Afd. Infectieziekten, Postbus 9600, 2300 RC Leiden, Netherlands; Van Steenbergen, J.E., Leids Universitair Medisch Centrum, Afd. Infectieziekten, Postbus 9600, 2300 RC Leiden, Netherlands; Van Dissel, J.T., Leids Universitair Medisch Centrum, Afd. Infectieziekten, Postbus 9600, 2300 RC Leiden, Netherlands","Severe acute respiratory syndrome (SARS) is caused by a recently identified Coronavirus (SARS-CoV). - The clinical symptoms are non-specific and during the first few days in particular, are not clinically distinguishable from those of many other viral or bacterial infections. The majority of infected patients develop pneumonia within a week of the first symptoms appearing. - Since November 2002 the virus has spread from South China to almost 30 other countries, where about 8500 infected individuals have been registered; about 800 people have already died from the disease (9.5%). - The number of infected persons includes a noticeably high percentage of health workers. This fact underlines the importance of good infection prevention measures for each patient contact. - The implementation of hygienic measures requires attention, because the infection of personnel in Toronto hospitals still occurred after the virus and transmission routes were known. - It appears that transmission can be prevented with relatively simple precautions, as long as these are consistently implemented. Early recognition and isolation of a possible source are an essential part of this. - SARS is a group A notifiable disease (report if suspected). - In the Netherlands the general practitioner has a prominent role in assessing and treating individuals who are infected or might be infected with SARS-CoV. A protocol and a detailed action plan are available. - In addition to this hospitals should be prepared for the initial reception of a patient with SARS, who presents directly to the outpatients' clinic or Casualty Department.",,"bacterial infection; Canada; China; Coronavirus; health care personnel; hospital infection; human; infection prevention; Netherlands; pneumonia; review; SARS coronavirus; severe acute respiratory syndrome; symptomatology; virus infection; virus transmission; Cross Infection; Disease Transmission, Patient-to-Professional; Humans; Hygiene; Infection Control; Netherlands; Pneumonia, Viral; SARS Virus; Severe Acute Respiratory Syndrome","Zaaijer, H.L., 'Severe acute respiratory syndrome' (SARS) in perspectief (2003) Ned Tijdschr Geneeskd, 147, pp. 846-848; Acute respiratory syndrome, China (2003) Weekly Epidemiol Rec, 78, p. 41; Rosling, L., Rosling, M., Pneumonia causes panic in Guangdong province (2003) BMJ, 326, p. 416; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-248; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Severe acute respiratory syndrome - Singapore, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 405-411; Enserink, M., Infectious diseases. Clues to the animal origins of SARS (2003) Science, 300, p. 1351; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F., Poon, L.L., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Epidemiological determinants of spread of causal agent of severe acute repiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Seto, W.H., Tsang, D., Yung, R.W.H., Ching, T.Y., Ng, T.K., Ho, M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520","Van Dissel, J.T.; Leids Universitair Medisch Centrum, Afd. Infectieziekten, Postbus 9600, 2300 RC Leiden, Netherlands; email: j.t.van_dissel@lumc.nl",,,00282162,,NETJA,"12908346","Dutch","Ned. Tijdschr. Geneeskd.",Review,"Final",,Scopus,2-s2.0-0041323315
"Li G., Chen X., Xu A.","56153486100;57192470203;56221325600;","Profile of specific antibodies to the SARS-associated coronavirus [6]",2003,"New England Journal of Medicine","349","5",,"508","509",,96,"10.1056/NEJM200307313490520","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042343795&doi=10.1056%2fNEJM200307313490520&partnerID=40&md5=4ed6d36437c15b2f3c7fcce42cb3cd3d","Sun Yat Sen University, Guangzhou 510275, China","Li, G., Sun Yat Sen University, Guangzhou 510275, China; Chen, X., Sun Yat Sen University, Guangzhou 510275, China; Xu, A., Sun Yat Sen University, Guangzhou 510275, China",[No abstract available],,"immunoglobulin G antibody; immunoglobulin M antibody; virus antibody; immunoglobulin G; immunoglobulin M; antibody response; Coronavirus; enzyme linked immunosorbent assay; human; humoral immunity; letter; priority journal; severe acute respiratory syndrome; virus pneumonia; immunology; metabolism; SARS coronavirus; severe acute respiratory syndrome; Humans; Immunoglobulin G; Immunoglobulin M; SARS Virus; Severe Acute Respiratory Syndrome","Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Poutanen, S.M., Low, D.E., Henry, B., Identification ofsevere acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Kawai, H., Feinstone, S.M., Acute viral hepatitis (2000) Mandell, Douglas, and Bennett's Principles and Practice of Infectious Diseases. 5th Ed., 1, pp. 1279-1297. , Mandell GL, Bennett JE, Dolin R, eds. Philadelphia: Churchill Livingstone","Li, G.; Sun Yat Sen University, Guangzhou 510275, China; email: ligangzh@pub.guangzhou.gd.cn",,,00284793,,NEJMA,"12890855","English","New Engl. J. Med.",Letter,"Final",Open Access,Scopus,2-s2.0-0042343795
"Zhang R., Guo Z., Lu J., Meng J., Zhou C., Zhan X., Huang B., Yu X., Huang M., Pan X., Ling W., Chen X., Wan Z., Zheng H., Yan X., Wang Y., Ran Y., Liu X., Ma J., Wang C., Zhang B.","12778550800;8886262500;8079348400;57199969920;57199738428;26027386800;57207403629;7404114135;57198803382;56236622900;14054110400;8079349300;8066291500;7403441204;8066291300;35277747300;8355638400;57192258269;36488230200;55766565500;7406908703;","Inhibiting severe acute respiratory syndrome-associated coronavirus by small interfering RNA",2003,"Chinese Medical Journal","116","8",,"1262","1264",,26,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041829054&partnerID=40&md5=71c8e5f0308a5b467137b923e63c7b90","Sun Yat-Sen University, Guangzhou 510089, China; Ctr. Disease Control and Prevention, Guangzhou 510300, China; Jinan University, Guangzhou 510632, China; Maxim Biotech. Inc., San Francisco, CA 94080, United States; The Quartermaster University of PLA, Changchun 130062, China; Med. Sch. of Univ. of Massachussetts, Worcester, MA 01605, United States","Zhang, R., Sun Yat-Sen University, Guangzhou 510089, China; Guo, Z., Sun Yat-Sen University, Guangzhou 510089, China; Lu, J., Sun Yat-Sen University, Guangzhou 510089, China; Meng, J., Sun Yat-Sen University, Guangzhou 510089, China; Zhou, C., Sun Yat-Sen University, Guangzhou 510089, China; Zhan, X., Sun Yat-Sen University, Guangzhou 510089, China; Huang, B., Sun Yat-Sen University, Guangzhou 510089, China; Yu, X., Sun Yat-Sen University, Guangzhou 510089, China; Huang, M., Sun Yat-Sen University, Guangzhou 510089, China; Pan, X., Sun Yat-Sen University, Guangzhou 510089, China; Ling, W., Sun Yat-Sen University, Guangzhou 510089, China; Chen, X., Sun Yat-Sen University, Guangzhou 510089, China; Wan, Z., Ctr. Disease Control and Prevention, Guangzhou 510300, China; Zheng, H., Ctr. Disease Control and Prevention, Guangzhou 510300, China; Yan, X., Ctr. Disease Control and Prevention, Guangzhou 510300, China; Wang, Y., Jinan University, Guangzhou 510632, China; Ran, Y., Jinan University, Guangzhou 510632, China; Liu, X., Jinan University, Guangzhou 510632, China; Ma, J., Maxim Biotech. Inc., San Francisco, CA 94080, United States; Wang, C., The Quartermaster University of PLA, Changchun 130062, China; Zhang, B., Med. Sch. of Univ. of Massachussetts, Worcester, MA 01605, United States","Objective. To evaluate the effectiveness of small interfering RNA (siRNA) on inhibiting severe acute respiratory syndrome (SARS)-associated coronavirus replication, and to lay bases for the future clinical application of siRNA for the treatment of viral infectious diseases. Methods. Vero-E6 cells was transfected with siRNA before SARS virus infection, and the effectiveness of siRNA interference was evaluated by observing the cytopathic effect (CPE) on Vero-E6 cells. Results. Five pairs of siRNA showed ability to reduce CPE dose dependently, and two of them had the best effect. Conclusion. siRNA may be effective in inhibiting SARS-associated coronavirus replication.","Coronavirus; Cytopathic effect; Severe acute respiratory syndrome; Small interfering RNA; Viral","RNA; animal cell; article; controlled study; Coronavirus; cytopathogenic effect; gene silencing; genetic transfection; nonhuman; RNA transcription; SARS coronavirus; Vero cell; virus infection; virus inhibition; virus replication; Animals; Cercopithecus aethiops; RNA, Small Interfering; SARS Virus; Transfection; Vero Cells; Virus Replication","Tuschl, T., RNA interference and small interfering RNAs (2001) Chembiochem., 2, pp. 239-245; Yang, D., Buchholz, F., Huang, Z., Short RNA duplexes produced by hydrolysis with Escherichia coli RNase III mediate effective RNA interference in mammalian cells (2002) Proc. Natl. Acad Sci. U. S. A., 99, pp. 9942-9947; Xiao, F.Q., Dong, S.A., Irvin, S.Y., Inhibiting HIV-1 infection in human T cells by lentiviral-mediated delivery of small interfering RNA against CCR5 (2003) Proc. Natl. Acad Sci. U. S. A., 100, pp. 183-188; Hamasaki, K., Nakao, K., Matsumoto, K., Short interfering RNA-directed inhibition of hepatitis B virus replication (2003) FEBS Lett., 543, pp. 51-54; Randall, G., Grakoui, A., Rice, C.M., Clearance of replicating hepatitis C virus replicon RNAs in cell culture by small interfering RNAs (2003) Proc. Natl. Acad Sci. U. S. A., 100, pp. 235-240; Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Holen, T., Amarzguioui, M., Wiiger, M.T., Positional effects of short interfering RNAs targeting the human coagulation trigger tissue factor (2002) Nucleic Acids Res., 30, pp. 1757-1766; Song, E., Lee, S.K., Wang, J., RNA interference targeting Fas protects mice from fulminant hepatitis (2003) Nat. Med., 9, pp. 347-351","Lu, J.; Sun Yat-Sen University, Guangzhou 510089, China; email: jiahailu@yahoo.com",,,03666999,,CMDJA,"12935424","English","Chin. Med. J.",Article,"Final",,Scopus,2-s2.0-0041829054
"Bosch B.J., Van der Zee R., De Haan C.A.M., Rottier P.J.M.","7003681993;35460297700;7003682643;7006145490;","The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex",2003,"Journal of Virology","77","16",,"8801","8811",,395,"10.1128/JVI.77.16.8801-8811.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042208243&doi=10.1128%2fJVI.77.16.8801-8811.2003&partnerID=40&md5=27830b5c828e82d9e7fbfeb84f5ab408","Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Immunology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands","Bosch, B.J., Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Van der Zee, R., Immunology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; De Haan, C.A.M., Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Virology Division, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands","Coronavirus entry is mediated by the viral spike (S) glycoprotein. The 180-kDa oligomeric S protein of the murine coronavirus mouse hepatitis virus strain A59 is posttranslationally cleaved into an S1 receptor binding unit and an S2 membrane fusion unit. The latter is thought to contain an internal fusion peptide and has two 4,3 hydrophobic (heptad) repeat regions designated HR1 and HR2. HR2 is located close to the membrane anchor, and HR1 is some 170 amino acids (aa) upstream of it. Heptad repeat (HR) regions are found in fusion proteins of many different viruses and form an important characteristic of class I viral fusion proteins. We investigated the role of these regions in coronavirus membrane fusion. Peptides HR1 (96 aa) and HR2 (39 aa), corresponding to the HR1 and HR2 regions, were produced in Escherichia coli. When mixed together, the two peptides were found to assemble into an extremely stable oligomeric complex. Both on their own and within the complex, the peptides were highly alpha helical. Electron microscopic analysis of the complex revealed a rod-like structure ∼14.5 nm in length. Limited proteolysis in combination with mass spectrometry indicated that HR1 and HR2 occur in the complex in an antiparallel fashion. In the native protein, such a conformation would bring the proposed fusion peptide, located in the N-terminal domain of HR1, and the transmembrane anchor into close proximity. Using biological assays, the HR2 peptide was shown to be a potent inhibitor of virus entry into the cell, as well as of cell-cell fusion. Both biochemical and functional data show that the coronavirus spike protein is a class I viral fusion protein.",,"hybrid protein; virus protein; vitronectin; article; controlled study; Coronavirus; electron microscopy; fusion gene; human; human cell; mass spectrometry; membrane fusion; nucleotide repeat; priority journal; protein assembly; protein binding; protein conformation; protein degradation; virus strain; Amino Acid Sequence; Base Sequence; Circular Dichroism; Coronavirus; DNA Primers; Membrane Fusion; Membrane Glycoproteins; Microscopy, Electron; Molecular Sequence Data; Sequence Homology, Amino Acid; Viral Envelope Proteins","Baker, K.A., Dutch, R.E., Lamb, R.A., Jardetzky, T.S., Structural basis for paramyxovirus-mediated membrane fusion (1999) Mol. 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Biol., 126, pp. 131-144; Yao, Q., Compans, R.W., Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection (1996) Virology, 223, pp. 103-112; Yoo, D.W., Parker, M.D., Babiuk, L.A., The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells (1991) Virology, 180, pp. 395-399; Young, J.K., Hicks, R.P., Wright, G.E., Morrison, T.G., Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling (1997) Virology, 238, pp. 291-304; Zhao, X., Singh, M., Malashkevich, V.N., Kim, P.S., Structural characterization of the human respiratory syncytial virus fusion protein core (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 14172-14177","Rottier, P.J.M.; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands; email: p.rottier@vet.uu.nl",,,0022538X,,JOVIA,"12885899","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0042208243
"Chan H.L.Y., Tsui S.K.W., Sung J.J.Y.","25722700100;7004961364;35405352400;","Coronavirus in severe acute respiratory syndrome (SARS)",2003,"Trends in Molecular Medicine","9","8",,"323","325",,21,"10.1016/S1471-4914(03)00135-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042427332&doi=10.1016%2fS1471-4914%2803%2900135-7&partnerID=40&md5=a3571b2d1a0414ba5e97b7abc16ae089","Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, 9/F Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong; Department of Biochemistry, Chinese University of Hong Kong, Mong Man Wai Building, Shatin, Hong Kong","Chan, H.L.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, 9/F Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong; Tsui, S.K.W., Department of Biochemistry, Chinese University of Hong Kong, Mong Man Wai Building, Shatin, Hong Kong; Sung, J.J.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, 9/F Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong","Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Future research on the molecular virology of SARS-CoV will be important in the understanding of the epidemiology and the natural history of SARS. This will also facilitate the development of sensitive and accurate diagnostic tests, as well as vaccination and other therapeutics to combat SARS.",,"Coronavirus; diagnostic test; disease course; molecular biology; review; severe acute respiratory syndrome; vaccination; virus pneumonia; Coronavirus","Lee, N., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) New Engl. J. Med., 348, pp. 1986-1994; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) New Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) New Engl. J. Med., 348, pp. 1967-1976; Peiris, J.S.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ruan, Y.J., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Anand, K., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Philips, J.J., Murine coronavirus spike glycoprotein medicates degree of viral spread, inflammation and virus-induced immunopathology in the central nervous system (2002) Virology, 301, pp. 109-120; Gallagher, T.M., Buchmeier, M.J., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Tsai, J.C., The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain (2003) J. Virol., 77, pp. 841-850; Bonavia, A., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Peiris, J.S.M., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Kilby, J.M., Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry (1998) Nat. Med., 4, pp. 1302-1307","Sung, J.J.Y.; Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, 9/F Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong; email: joesung@cuhk.edu.hk",,"Elsevier Ltd",14714914,,TMMRC,"12928031","English","Trends Mol. Med.",Short Survey,"Final",Open Access,Scopus,2-s2.0-0042427332
"De Haan C.A.M., De Wit M., Kuo L., Montalto-Morrison C., Haagmans B.L., Weiss S.R., Masters P.S., Rottier P.J.M.","7003682643;7102191667;7101601942;6506323924;6701371301;57203567044;7006234572;7006145490;","The glycosylation status of the murine hepatitis coronavirus M protein affects the interferogenic capacity of the virus in vitro and its ability to replicate in the liver but not the brain",2003,"Virology","312","2",,"395","406",,37,"10.1016/S0042-6822(03)00235-6","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042062360&doi=10.1016%2fS0042-6822%2803%2900235-6&partnerID=40&md5=4adc020e3dbd844daebfb2643af15774","Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Dept. of Vacc. Technol./Immunology, Intervet International BV, 5830 AA Boxmeer, Netherlands; Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Institute of Virology, Erasmus MC, 3015 GE Rotterdam, Netherlands; Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584 CL Utrecht, Netherlands","De Haan, C.A.M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584 CL Utrecht, Netherlands; De Wit, M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Dept. of Vacc. Technol./Immunology, Intervet International BV, 5830 AA Boxmeer, Netherlands; Kuo, L., Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Montalto-Morrison, C., Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Haagmans, B.L., Institute of Virology, Erasmus MC, 3015 GE Rotterdam, Netherlands; Weiss, S.R., Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Masters, P.S., Wadsworth Center, New York State Department of Health, Albany, NY 12201, United States; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands","The coronavirus M protein, the most abundant coronaviral envelope component, is invariably glycosylated, which provides the virion with a diffuse, hydrophilic cover on its outer surface. Remarkably, while the group 1 and group 3 coronaviruses all have M proteins with N-linked sugars, the M proteins of the group 2 coronaviruses [e.g., mouse hepatitis virus (MHV)] are O-glycosylated. The conservation of the N- and O-glycosylation motifs suggests that each of these types of carbohydrate modifications is beneficial to their respective virus. Since glycosylation of the M protein is not required for virus assembly, the oligosaccharides are likely to be involved in the virus-host interaction. In order to investigate the role of the M protein glycosylation in the host, two genetically modified MHVs were generated by using targeted RNA recombination. The recombinant viruses carried M proteins that were either N-glycosylated or not glycosylated at all, and these were compared with the parental, O-glycosylated, virus. The M protein glycosylation state did not influence the tissue culture growth characteristics of the recombinant viruses. However, it affected their interferogenic capacity as measured using fixed, virus-infected cells. Viruses containing M proteins with N-linked sugars induced type I interferons to higher levels than viruses carrying M proteins with O-linked sugars. MHV with unglycosylated M proteins appeared to be a poor interferon inducer. In mice, the recombinant viruses differed in their ability to replicate in the liver, but not in the brain, whereas their in vivo interferogenic capacity did not appear to be affected by their glycosylation status. Strikingly, their abilities to replicate in the liver correlated with their in vitro interferogenic capacity. This apparent correlation might be explained by the functioning of lectins, such as the mannose receptor, which are abundantly expressed in the liver but also play a role in the induction of interferon-α by dendritic cells. © 2003 Elsevier Science (USA). All rights reserved.",,"alpha interferon; carbohydrate; hepatitis coronavirus m protein; mannose receptor; oligosaccharide; unclassified drug; virus protein; animal cell; animal experiment; animal tissue; article; bioaccumulation; controlled study; correlation analysis; dendritic cell; liver; mouse; nonhuman; priority journal; protein expression; protein glycosylation; protein induction; protein motif; RNA recombination; tissue culture; virus assembly; virus cell interaction; virus recombinant; virus replication; virus virulence; Coronavirus; Murinae; Murine hepatitis virus","Alexander, S., Elder, J.H., Carbohydrate dramatically influences immune reactivity of antisera to viral glycoprotein antigens (1984) Science, 226, pp. 1328-1330; Aurisicchio, L., Delmastro, P., Salucci, V., Paz, O.G., Rovere, P., Ciliberto, G., La Monica, N., Palombo, F., Liver-specific alpha 2 interferon gene expression results in protection from induced hepatitis (2000) J. 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Virol., 66, pp. 743-749; Lee, S.J., Evers, S., Roeder, D., Parlow, A.F., Risteli, J., Risteli, L., Lee, Y.C., Nussenzweig, M.C., Mannose receptor-mediated regulation of serum glycoprotein homeostasis (2002) Science, 295, pp. 1898-1901; Masters, P.S., Reverse genetics of the largest RNA viruses (1999) Adv. Virus Res., 53, pp. 245-264; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. 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Virol., 64, pp. 339-346; Yamada, Y.K., Yabe, M., Ohtsuki, T., Taguchi, F., Unique N-linked glycosylation of murine coronavirus MHV-2 membrane protein at the conserved O-linked glycosylation site (2000) Virus Res., 66, pp. 149-154","De Haan, C.A.M.; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584 CL Utrecht, Netherlands; email: x.haan@vet.uu.nl",,"Academic Press Inc.",00426822,,VIRLA,"12919744","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0042062360
"Hooks J.J., Wang Y., Detrick B.","7006661655;56802808200;7003911483;","The critical role of IFN-γ in experimental coronavirus retinopathy",2003,"Investigative Ophthalmology and Visual Science","44","8",,"3402","3408",,17,"10.1167/iovs.02-1106","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041342105&doi=10.1167%2fiovs.02-1106&partnerID=40&md5=ca24e7bba3066fcdb2f0725c113f7ef3","Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States; Department of Pathology, Johns Hopkins Medical Institutions, Baltimore, MD, United States; Immunology and Virology Section, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, United States","Hooks, J.J., Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States, Immunology and Virology Section, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, United States; Wang, Y., Laboratory of Immunology, National Eye Institute, Bethesda, MD, United States; Detrick, B., Department of Pathology, Johns Hopkins Medical Institutions, Baltimore, MD, United States","PURPOSE. Experimental coronavirus retinopathy (ECOR) is an animal model of progressive retinal disease that is first manifest as an acute retinal inflammation followed by chronic, immune-associated retinal degeneration in genetically susceptible, BALB/c mice. In retinal degeneration-resistant CD-1 mice, only the acute infection is seen. In the present study, interferon (IFN)-γ production during ECOR was studied and its role evaluated in the clearance of infectious virus from the retina. METHODS. BALB/c, CD-1, and IFN-γ deficient (IFN-γ gko) mice were inoculated with the JHM strain of murine coronavirus by the intravitreal route. Mouse eyes were evaluated for infiltrating cells and major histocompatibility complex (MHC) expression by immunocytochemical staining. Isolated retinas were analyzed for IFN-γ mRNA by RT-PCR, and sera were evaluated for IFN-γ protein by ELISA assays. RESULTS. Virus infection in BALB/c mice was associated with an increase in the incidence and levels of systemic IFN-γ. Moreover, IFN-γ mRNA was detected within the retinas of infected animals during the acute phase of the disease but was not detected in normal or mock-injected animals. IFN-γ mRNA was detected at the time of T-cell infiltration, and earlier studies have shown that this is temporally related to granzyme B gene expression and the clearance of infectious virus from the retina. Retinal IFN-γ mRNA was also associated with the upregulation of MHC class I and II molecules within the retina. When this infection occurred in IFN-γ gko mice, the virus was unchecked, and the infection led to death. CONCLUSIONS. These studies indicate that generation of IFN-γ by cells infiltrating the retina is an essential part of an immune mechanism responsible for noncytolytic clearance of infectious virus from the retina.",,"gamma interferon; granzyme B; major histocompatibility antigen; messenger RNA; acute disease; animal cell; animal experiment; animal model; animal tissue; antigen expression; article; cause of death; cell infiltration; controlled study; Coronavirus; cytokine production; enzyme linked immunosorbent assay; gene control; gene expression; immune response; lymphocytic infiltration; major histocompatibility complex; mouse; nonhuman; priority journal; retina degeneration; retinopathy; reverse transcription polymerase chain reaction; upregulation; Animals; Coronavirus; Coronavirus Infections; Disease Models, Animal; Enzyme-Linked Immunosorbent Assay; Eye Infections, Viral; Fluorescent Antibody Technique, Indirect; Gene Expression; Histocompatibility Antigens Class I; Histocompatibility Antigens Class II; Interferon Type II; Mice; Mice, Inbred BALB C; Microscopy, Fluorescence; Monocytes; Retinal Diseases; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; T-Lymphocytes","Vilcek, J., Sen, G.C., Interferons and other cytokines (1996) Virology, 1, pp. 375-399. , Fields BN, Knipe DM, Howley PM, eds. Philadelphia: Lippincott-Raven; Muller, U., Steinhoff, U., Reis, L.F., Functional role of type I and type II interferons in antiviral defense (1994) Science, 264, pp. 1918-1921; Kundig, T.M., Hengartner, H., Zinkernagel, R.M., T cell-dependent IFN-gamma exerts an antiviral effect in the central nervous system but not in peripheral solid organs (1993) J Immunol, 150, pp. 2316-2321; Parra, B., Hinton, D.R., Marten, N.W., IFN-gamma is required for viral clearance from central nervous system oligodendroglia (1999) J Immunol, 162, pp. 1641-1647; Bouley, D.M., Kanangat, S., Wire, W., Rouse, B.T., Characterization of herpes simplex virus type-1 infection and herpetic stromal keratitis development in IFN-gamma knockout mice (1995) J Immunol, 155, pp. 3964-3971; Geiger, K., Howes, E., Gallina, M., Huang, X.J., Travis, G.H., Sarvetnick, N., Transgenic mice expressing IFN-gamma in the retina develop inflammation of the eye and photoreceptor loss (1994) Invest Ophthalmol Vis Sci, 35, pp. 2667-2681; Geiger, K., Howes, E.L., Sarvetnick, N., Ectopic expression of gamma interferon in the eye protects transgenic mice from intraocular herpes simplex virus type 1 infections (1994) J Virol, 68, pp. 5556-5567; Levy, D.E., Garcia-Sastre, A., The virus battles: IFN induction of the antiviral state and mechanisms of viral evasion (2001) Cytokine Growth Factor Rev, 12, pp. 143-156; Detrick, B., Hooks, J.J., Cytokines in human immunology (1997) Handbook of Human Immunology, pp. 233-266. , Leffell M, Donnenberg AD, Rose NR eds. Boca Raton, FL: CRC Press; Guidotti, L.G., Chisari, F.V., Cytokine-mediated control of viral infections (2000) Virology, 273, pp. 221-227; Guidotti, L.G., Rochford, R., Chung, J., Shapiro, M., Purcell, R., Chisari, F.V., Viral clearance without destruction of infected cells during acute HBV infection (1999) Science, 284, pp. 825-829; Binder, G.K., Griffin, D.E., Interferon-gamma-mediated site-specific clearance of alphavirus from CNS neurons (2001) Science, 293, pp. 303-306; Hooks, J.J., Percopo, C., Wang, Y., Detrick, B., Retina and retinal pigment epithelial cell autoantibodies are produced during murine coronavirus retinopathy (1993) J Immunol, 151, pp. 3381-3389; Robbins, S.G., Detrick, B., Hooks, J.J., Retinopathy following intravitreal injection of mice with MHV strain JHM (1990) Adv Exp Med Biol, 276, pp. 519-524; Robbins, S.G., Detrick, B., Hooks, J.J., Ocular tropisms of murine coronavirus (strain JHM) after inoculation by various routes (1991) Invest Ophthalmol Vis Sci, 32, pp. 1883-1893; Wang, Y., Burnier, M., Detrick, B., Hooks, J.J., Genetic predisposition to coronavirus-induced retinal disease (1996) Invest Ophthalmol Vis Sci, 37, pp. 250-254; Komurasaki, Y., Nagineni, C.N., Wang, Y., Hooks, J.J., Virus RNA persists within the retina in coronavirus-induced retinopathy (1996) Virology, 222, pp. 446-450; Wang, Y., Detrick, B., Hooks, J.J., Coronavirus (JHM) replication within the retina: Analysis of cell tropism in mouse retinal cell cultures (1993) Virology, 193, pp. 124-137; Wang, Y., Detrick, B., Yu, Z.X., Zhang, J., Chesky, L., Hooks, J.J., The role of apoptosis within the retina of coronavirus-infected mice (2000) Invest Ophthalmol Vis Sci, 41, pp. 3011-3018; Vinores, S., Wang, Y., Vinores, M.A., Blood-retinal barrier breakdown in experimental coronavirus retinopathy: Association with viral antigen, inflammation, and VEGF in sensitive and resistant strains (2001) J Neuroimmunol, 119, pp. 175-182; Percopo, C.M., Hooks, J.J., Shinohara, T., Caspi, R., Detrick, B., Cytokine-mediated activation of a neuronal retinal resident cell provokes antigen presentation (1990) J Immunol, 145, pp. 4101-4107; Marten, N.W., Stohlman, S.A., Bergmann, C.C., MHV infection of the CNS: Mechanisms of immune-mediated control (2001) Viral Immunol, 14, pp. 1-18; Lin, M.T., Stohlman, S.A., Hinton, D.R., Mouse hepatitis virus is cleared from the central nervous systems of mice lacking perforin-mediated cytolysis (1997) J Virol, 71, pp. 383-391; Parra, B., Hinton, D.R., Lin, M.T., Cua, D.J., Stohlman, S.A., Kinetics of cytokine mRNA expression in the central nervous system following lethal and nonlethal coronavirus-induced acute encephalomyelitis (1997) Virology, 233, pp. 260-270; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J Virol, 68, pp. 5483-5495; Haring, J.S., Pewe, L.L., Perlman, S., High-magnitude, virus-specific CD4 T-cell response in the central nervous system of coronavirus-infected mice (2001) J Virol, 75, pp. 3043-3047; Schijns, V.E., Wierda, C.M., Van Hoeij, M., Horzinek, M.C., Exacerbated viral hepatitis in IFN-gamma receptor-deficient mice is not suppressed by IL-12 (1996) J Immunol, 157, pp. 815-821; Vollstedt, S., Franchini, M., Alber, G., Ackermann, M., Suter, M., Interleukin-12- and gamma interferon-dependent innate immunity are essential and sufficient for long-term survival of passively immunized mice infected with herpes simplex virus type 1 (2001) J Virol, 75, pp. 9596-9600; Hooks, J.J., Chan, C.C., Detrick, B., Identification of the lymphokines, interferon-gamma and interleukin-2, in inflammatory eye diseases (1988) Invest Ophthalmol Vis Sci, 29, pp. 1444-1451; Egwuagu, C.E., Sztein, J., Mahdi, R.M., IFN-gamma increases the severity and accelerates the onset of experimental autoimmune uveitis in transgenic rats (1999) J Immunol, 162, pp. 510-517; Ciurea, A., Klenerman, P., Hunziker, L., Persistence of lymphocytic choriomeningitis virus at very low levels in immune mice (1999) Proc Natl Acad Sci USA, 96, pp. 11964-11969; Rehermann, B., Ferrari, C., Pasquinelli, C., Chisari, F.V., The hepatitis B virus persists for decades after patients' recovery from acute viral hepatitis despite active maintenance of a cytotoxic T-lymphocyte response (1996) Nat Med, 2, pp. 1104-1108","Hooks, J.J.; Immunology and Virology Section, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, United States; email: jjhooks@helix.nih.gov",,,01460404,,IOVSD,"12882788","English","Invest. Ophthalmol. Vis. Sci.",Article,"Final",Open Access,Scopus,2-s2.0-0041342105
"Kumar D., Tellier R., Draker R., Levy G., Humar A.","7402293996;7004847486;6506467065;35391580500;57205215365;","Severe acute respiratory syndrome (SARS) in a liver transplant recipient and guidelines for donor SARS screening",2003,"American Journal of Transplantation","3","8",,"977","981",,34,"10.1034/j.1600-6143.2003.00197.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042490790&doi=10.1034%2fj.1600-6143.2003.00197.x&partnerID=40&md5=c8812a4acf62d4a06bd45d4389971f2f","Infect. Dis./Multi-Organ Transplant, University Health Network, University of Toronto, Toronto, Ont., Canada; Research Institute, Division of Microbiology, Hospital for Sick Children, Toronto, Ont., Canada","Kumar, D., Infect. Dis./Multi-Organ Transplant, University Health Network, University of Toronto, Toronto, Ont., Canada; Tellier, R., Research Institute, Division of Microbiology, Hospital for Sick Children, Toronto, Ont., Canada; Draker, R., Research Institute, Division of Microbiology, Hospital for Sick Children, Toronto, Ont., Canada; Levy, G., Infect. Dis./Multi-Organ Transplant, University Health Network, University of Toronto, Toronto, Ont., Canada; Humar, A., Infect. Dis./Multi-Organ Transplant, University Health Network, University of Toronto, Toronto, Ont., Canada","Severe acute respiratory syndrome (SARS) is a recently described infectious entity with salient features of fever, headache and malaise, with rapid progression to pneumonitis. The etiology of SARS is likely a novel coronavirus. During the winter of 2003, an outbreak of SARS involving several hospitals occurred in Toronto, Canada. We describe a patient post liver transplant who contracted SARS and died during the outbreak, with subsequent infection of family and several health-care workers. A novel coronavirus was detected in respiratory specimens by PCR. Due to the potential severity of SARS in transplant recipients and the large number of cases of SARS in the community, in order to avoid transmission of SARS from a donor, we developed guidelines for SARS screening of organ donors. A screening tool based on potential hospital SARS exposure, clinical symptoms, and epidemiological exposure was used to stratify donors as high, intermediate or low risk for SARS. As SARS spreads throughout the world, it may become an increasingly significant problem for transplant patients and programs.","Coronavirus; Donor screening; Severe acute respiratory syndrome","aged; article; case report; clinical feature; Coronavirus; disease course; epidemic; fever; headache; health program; human; liver transplantation; malaise; male; nucleotide sequence; organ donor; pneumonia; polymerase chain reaction; practice guideline; respiratory distress syndrome; SARS coronavirus; screening; severe acute respiratory syndrome; virus transmission; winter; Aged; Base Sequence; Contact Tracing; DNA Primers; Humans; Liver Transplantation; Male; Practice Guidelines; Severe Acute Respiratory Syndrome; Tissue Donors","Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_04-10/en/; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome Lancet, , http://www.thelancet.com/journal/vol361/iss9365/full/Ilan.361.9365.early_ online_publication.25296.1; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronaviruses associated with severe acute respiratory syndrome N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030781v1; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa03O747v1; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa03O634v1; Tellier, R., Bukh, J., Emerson, S.U., Purcell, R.H., Amplification of the full-length hepatitis A virus genome by long reverse transcription-PCR and transcription of infectious RNA directly from the amplicon (1996) Proc Natl Acad Sci, 93, pp. 4370-4373; Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/en; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong N Engl J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030685v1; Whimbey, E.E., Englund, J.A., Community respiratory virus infections in transplant recipients (1998) Transplant Infections, pp. 295-308. , Bowden RA, Ljungman P, Paya CV, eds. Philadelphia, NY: Lippincott-Raven Publishers","Kumar, D.; Infect. Dis./Multi-Organ Transplant, University Health Network, University of Toronto, Toronto, Ont., Canada; email: Deepali.kumar@uhn.on.ca",,,16006135,,AJTMB,"12859532","English","Am. J. Transplant.",Article,"Final",Open Access,Scopus,2-s2.0-0042490790
"Zhao X., Han J., Ning Y., Meng A., Chen Y.","37080000600;57199892040;7102383410;7006106872;55972143800;","Bioinformatic analysis of putative gene products encoded in SARS HCoV genome",2003,"Tsinghua Science and Technology","8","4",,"389","394",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344036183&partnerID=40&md5=25f5acf55233bf7e79befa93b5649603","Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Dana Farber Cancer Inst., Harvard Univ., Boston, MA 02115, United States","Zhao, X., Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Han, J., Dana Farber Cancer Inst., Harvard Univ., Boston, MA 02115, United States; Ning, Y., Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Meng, A., Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; Chen, Y., Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China","The cause of severe acute respiratory syndrome (SARS) has been identified as a new coronavirus named as SARS-HCoV. Using bioinformatic methods, we have performed a detailed domain search. In addition to the viral structure proteins, we have found that several putative polypeptides share sequence similarity to known domains or proteins. This study may provide a basis for future studies on the infection and replication process of this notorious virus.","Bioinfomatics; Genome analysis; Human coronavirus; Severe acute respiratory syndrome (SARS)","Analysis; Genes; Polypeptides; Proteins; Respiratory therapy; Structure (composition); Bioinfomatics; Bioinformatic analysis; Genome analysis; Human coronavirus; Severe acute respiratory syndrome; Viruses","Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, , 1085953; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, , 1085952; Altschul, S.F., Madden, T.L., Schaffer, A.A., Gapped BLAST and PSI-BLAST. A new generation of protein database search programs (1997) Nucleic Acids Res., 25, pp. 3389-3402; Mulder, N.J., Apweiler, R., Attwood, T.K., The InterPro Database, 2003 brings increased coverage and new features (2003) Nucleic Acids Res., 31, pp. 315-318; Martzen, M.R., McCraith, S.M., Spinelli, S.L., A biochemical genomics approach for identifying genes by the activity of their products (1999) Science, 286, pp. 1153-1155; Virtanen, T., Lipocalin allergens (2001) Allergy, 56 (SUPPL. 67), pp. 48-51; Saraste, M., Sibbald, P.R., Wittinghofer, A., The P-loop - A common motif in ATP- and GTP-binding proteins (1990) Trends Biochem. Sci., 15, pp. 430-434; Bugl, H., Fauman, E.B., Staker, B.L., RNA methylation under heat shock control (2000) Mol. Cell, 6, pp. 349-360; Bonavia, A., Zelus, B.D., Wentworth, D.E., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Lu, Y., Chen, Y., Spike protein homology between the SARS-associated virus and murine hepatitis virus implies existence of a putative receptor-binding region (2003) Chinese Sci. Bull., , in press","Chen, Y.; Lab. of Membrane Biotechnology, Dept. of Biol. Sci., Tsinghua Univ., Beijing 100084, China; email: ygchen@tsinghua.edu.cn",,,10070214,,TSTEF,,"English","Tsinghua Sci. Tech.",Article,"Final",,Scopus,2-s2.0-0344036183
"Chen T.-G., Wu S.-F., Wan P., Du C.-J., Li J.-Q., Li D., Wei G.-Z., Li B., Wang Z.-S., Xue X.-F., Zhu Y.-P., He F.-C.","55745056300;12239213700;7103181983;7202172575;55720527700;36068588000;7402847996;26643217800;57207121224;14822822500;9248689600;7201951930;","Gene prediction and function research of SARS-CoV(BJ01)",2003,"Acta Genetica Sinica","30","8",,"773","780",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744226530&partnerID=40&md5=d3f61037e267ae3990ff1868cf813832","Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China","Chen, T.-G., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Wu, S.-F., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Wan, P., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Du, C.-J., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Li, J.-Q., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Li, D., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Wei, G.-Z., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Li, B., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Wang, Z.-S., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Xue, X.-F., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; Zhu, Y.-P., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; He, F.-C., Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China","Through reading the articles, this study points out the shortage of gene prediction and function research about SARS-CoV, and predict it again for developing effective drugs and future vaccines. Using twelve gene prediction methods to predict coronavirus known genes, we select four better methods including Heuristic models, Gene Identification, ZCURVE _ CoV and ORF FINDER to predict SARS-CoV(BJ01), and use ATGpr for analyzing probability of initiation codon and Kozak rule, search transcription regulating sequence(TRS) in order to improve the accuracy of predicted genes. Twenty-one probable new genes with more than 50 amino acids have been obtained excluding 13 ORFs which are similar to the genes of NCBI and relative articles. For predicted proteins, we use ProtParam to analyse physical and chemical features; SignalP to analyse signal peptide; BLAST, FASTA to search similar sequences; TMPred, TMHMM, PFAM and HMMTOP to analyse domain and motif in order to improve reliability of gene function prediction. At the same time, we separate the 21 ORFs into four classes using codition of four gene prediction methods, match score, match expection and match length between predicted gene and Coronavirus known gene. In the end, we discuss the results and analyse the reasons.","Gene function; Gene prediction; SARS-CoV","amino acid; signal peptide; article; codon; Coronavirus; gene function; gene identification; genetic analysis; genetic transcription; medical research; nucleotide sequence; open reading frame; protein domain; protein motif; respiratory tract infection; SARS coronavirus; sequence analysis; severe acute respiratory syndrome; Computational Biology; Genes, Viral; Open Reading Frames; Reproducibility of Results; SARS Virus; Coronavirus; SARS coronavirus","http://www.who.int/csr/sars/country/2003_06_05/en/; http://database.cpst.net.cn/popul/special/sars/artic/30517133107.html; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) The New England Journal of Medicine, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) The New England Journal of Medicine, 348, pp. 1947-1958; Avendano, M., Derkach, P., Swan, S., Clinical course and management of SARS in health care workers in Toronto: A case series (2003) CMAJ, 168 (13), pp. 1649-1660; Qin, L., Xiong, B., Luo, C., Guo, Z.-M., Hao, P., Su, J., Nan, P., Li, Y.-X., Identification of probable genomic packaging signal sequence from SARS-CoV genome by bioinformatics analysis (2003) Acta Pharmacol Sin, 24 (6), pp. 489-496; Fukami-Kobayashi, K., Saito, N., How to make good use of CLUSTALW (2002) Tanpakushitsu Kakusan Koso, 47 (9), pp. 1237-1239; Zhang, W.-G., Li, J.-Q., Zhou, H.-M., Genomic characterization of SARS Coronavirus: A novel member of coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 501-508; Chen, Y.-J., Gao, G., Bao, Y.-M., Lopez, R., Wu, J.-M., Cai, T., Ye, Z.-Q., Luo, J.-C., Initial analysis of complete genome sequences of SARS Coronavirus (2003) Acta Genetica Sinica, 30 (6), pp. 493-500; Li, W.-J., Liu, T., Epitope analysis of SARS-CoV (2003) Med J Chinese PLA (Supplement), 28, pp. s7-s8; http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NC_004718; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-Associated coronavirus (2003) Sciencexpress, , www.sciencexpress.org/science,1085953:Page1/10.1126/1,2003; Qin, E., Zhu, Q., Yu, M., Fan, B., Chang, G., Si, B., Yang, B., Yang, R., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Ruan, Y.J., Wei, C.L., Ee, L.A., Vega, V.B., Thoreau, H., Yun, S.T.S., Chia, J.-M., Liu, E.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) The Lancet, pp. 1-7. , http://image.thelancet.com/extras/03art4454web.pdf, Published online; http://www.ncbi.nlm.nih.gov/gorf/gorf.html; He, F.-C., (2003) SARS - Severe Acute Respiratory Syndrome, pp. 52-71. , www.sciencep.com; Chen, L.L., Ou, H.Y., Zhang, R., Zhang, C.T., ZCURVE _ CoV: A new system to recognize protein coding genes in coronavirus genomes, and its applications in analyzing SARS-CoV genomes (2003) Biochem Biophys Res Commun, 307, pp. 382-388; Salamov, A.A., Nishikawa, T., Swindells, M.B., Assessing protein coding region integrity in cDNA sequencing projects (1998) Bioinformatics, 14, pp. 384-390; Kozak, M., An analysis of 5′ noncoding sequences from 699 vertebrate messenger RNAs (1987) Nucleic Acids Research, 15, pp. 8125-8132; Ikai, A., Extraction of the apo B cluster from human low density lipoprotein with Tween 80 (1980) J Biochem (Tokyo), 88 (5), pp. 1349-1357; http://www.cbs.dtu.dk/services/SignalP/; http://fasta.bioch.virginia.edu/; http://www.ch.embnet.org/software/TMPRED_form.html; http://www.cbs.dtu.dk/services/TMHMM/; http://www.sanger.ac.uk/Software/Pfam/search.shtml; http://www.enzim.hu/hmmtop1.1/doc/help.html#format","Chen, T.-G.; Laboratory of Systems Biology, Beijing Inst. of Radiation Medicine, Beijing 100850, China; email: chentg@hupo.org.cn",,,03794172,,ICHPC,"14682248","Chinese","Acta Genet. Sin.",Article,"Final",,Scopus,2-s2.0-10744226530
"Drosten C., Preiser W., Günther S., Schmitz H., Doerr H.W.","7003813990;7004338253;7102978849;7203078610;7102740671;","Severe acute respiratory syndrome: Identification of the etiological agent",2003,"Trends in Molecular Medicine","9","8",,"325","327",,77,"10.1016/S1471-4914(03)00133-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042427333&doi=10.1016%2fS1471-4914%2803%2900133-3&partnerID=40&md5=f100c5ac4437a36f4b427826b5fe0972","Department of Virology, Bernhard-Nocht Inst. Trop. Medicine, Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; Institute of Medical Virology, University of Frankfurt/Main, Paul-Ehrlich Str. 40, 60596 Frankfurt/Main, Germany","Drosten, C., Department of Virology, Bernhard-Nocht Inst. Trop. Medicine, Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; Preiser, W., Institute of Medical Virology, University of Frankfurt/Main, Paul-Ehrlich Str. 40, 60596 Frankfurt/Main, Germany; Günther, S., Department of Virology, Bernhard-Nocht Inst. Trop. Medicine, Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; Schmitz, H., Department of Virology, Bernhard-Nocht Inst. Trop. Medicine, Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; Doerr, H.W., Institute of Medical Virology, University of Frankfurt/Main, Paul-Ehrlich Str. 40, 60596 Frankfurt/Main, Germany","The severe acute respiratory syndrome (SARS) emerged in late 2002 in southern China and rapidly spread to countries around the globe. Three research groups within a World Health Organization (WHO)-coordinated network have independently and simultaneously shown that a novel coronavirus is linked to SARS. A fourth group has completed the Koch's postulates by infecting monkeys with the agent. Sequencing of the complete genome was achieved only weeks after the first isolate of the virus became available.",,"China; Coronavirus; gene sequence; laboratory diagnosis; review; severe acute respiratory syndrome; virus isolation; virus pneumonia; world health organization; Coronavirus","Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol. Rec., 78, pp. 81-83; Donnelly, C.A., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Stohr, K., A multicentre collaboration to investigate the cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1730-1733; Fouchier, R.A., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) New Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) New Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Identification of severe acute respiratory syndrome in Canada (2003) New Engl. J. Med., 348, pp. 1995-2005; Ruan, Y.J., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Luytjes, W., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Chang, Y., Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma (1994) Science, 266, pp. 1865-1869; Choo, Q.L., Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome (1989) Science, 244, pp. 359-362","Drosten, C.; Department of Virology, Bernhard-Nocht Inst. Trop. Medicine, Bernhard-Nocht Str. 74, 20359 Hamburg, Germany; email: drosten@bni-hamburg.de",,"Elsevier Ltd",14714914,,TMMRC,"12928032","English","Trends Mol. Med.",Short Survey,"Final",Open Access,Scopus,2-s2.0-0042427333
"Tsai J.C., De Groot L., Pinon J.D., Iacono K.T., Phillips J.J., Seo S.-H., Lavi E., Weiss S.R.","7403610594;7005626336;35870444000;57193216473;7404582468;7202469910;7006986911;57203567044;","Amino acid substitutions within the heptad repeat domain 1 of murine coronavirus spike protein restrict viral antigen spread in the central nervous system",2003,"Virology","312","2",,"369","380",,19,"10.1016/S0042-6822(03)00248-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0043064024&doi=10.1016%2fS0042-6822%2803%2900248-4&partnerID=40&md5=e6984230f51f85cb4a0176230252d2d0","Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Dept. of Pathol./Laboratory Medicine, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, Philadelphia, PA 19104-6076, United States","Tsai, J.C., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; De Groot, L., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Pinon, J.D., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Iacono, K.T., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Phillips, J.J., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Seo, S.-H., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Lavi, E., Dept. of Pathol./Laboratory Medicine, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States; Weiss, S.R., Department of Microbiology, Univ. of PA School of Medicine, Philadelphia, PA 19104-6076, United States, Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, Philadelphia, PA 19104-6076, United States","Targeted recombination was carried out to select mouse hepatitis viruses (MHVs) in a defined genetic background, containing an MHV-JHM spike gene encoding either three heptad repeat 1 (HR1) substitutions (Q1067H, Q1094H, and L1114R) or L1114R alone. The recombinant virus, which expresses spike with the three substitutions, was nonfusogenic at neutral pH. Its replication was significantly inhibited by lysosomotropic agents, and it was highly neuroattenuated in vivo. In contrast, the recombinant expressing spike with L1114R alone mediated cell-to-cell fusion at neutral pH and replicated efficiently despite the presence of lysosomotropic agents; however, it still caused only subclinical morbidity and no mortality in animals. Thus, both recombinant viruses were highly attenuated and expressed viral antigen which was restricted to the olfactory bulbs and was markedly absent from other regions of the brains at 5 days postinfection. These data demonstrate that amino acid substitutions, in particular L1114R, within HR1 of the JHM spike reduced the ability of MHV to spread in the central nervous system. Furthermore, the requirements for low pH for fusion and viral entry are not prerequisites for the highly attenuated phenotype. © 2003 Elsevier Science (USA). All rights reserved.","CNS infection; MHV spike; Murine coronavirus; Viral fusion; Viral pathogenesis","protein; spike protein; unclassified drug; virus antigen; amino acid substitution; animal cell; animal experiment; animal model; animal tissue; antigen expression; article; cell adhesion; central nervous system; controlled study; Coronavirus; genetic code; male; mouse; nonhuman; olfactory bulb; pH; priority journal; protein domain; tandem repeat; virus gene; virus recombinant; virus replication; Animalia; Coronavirus; Murinae; Murine hepatitis virus","Barnett, E.M., Cassell, M.D., Perlman, S., Two neurotropic viruses, herpes simplex virus type 1 and mouse hepatitis virus, spread along different neural pathways from the main olfactory bulb (1993) Neuroscience, 57, pp. 1007-1125; Carr, C.M., Chaudhry, C., Kim, P.S., Influenza hemagglutinin is spring-loaded by a metastable native conformation (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 14306-14313; Dalziel, R.G., Lampert, P.W., Talbot, P.J., Buchmeier, M.J., Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence (1986) J. Virol., 59, pp. 463-471; DeGroot, R.J., Luytjes, W., Horzinek, M.C., Van der Zeijst, B.A.M., Spaan, W.J.M., Lenstra, J.A., Evidence for a coiled-coil structure in the spike proteins of coronaviruses (1987) J. Mol. Biol., 196, pp. 963-966; Dveksler, G.S., Pensiero, M.N., Cardellichio, C.B., Williams, R.K., Jiang, G.S., Holmes, K.V., Dieffenbach, C.W., Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV (1991) J. Virol., 65, pp. 6881-6891; Frana, M.F., Behnke, J.N., Sturman, S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Gallagher, T.M., Buchmeier, M.J., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Gallagher, T.M., Escarmis, C., Buchmeier, M.J., Alteration of pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein (1991) J. Virol., 65, pp. 1916-1928; Hsue, B., Masters, P.S., An essential secondary structure in the 3′ untranslated region of the mouse hepatitis virus genome (1998) Adv. Exp. Med. Biol., 440, pp. 297-302; Krueger, D.K., Kelly, S.M., Lewicki, D.N., Ruffolo, R., Gallagher, T.M., Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion (2001) J. Virol., 75, pp. 2792-2802; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 5403-5410; Kuo, L., Godeke, G.J., Raamsman, M.J., Masters, P.S., Rottier, P.J., Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier (2000) J. Virol., 74, pp. 1393-1406; Lavi, E., Gilden, D.H., Wroblewska, Z., Rorke, L.B., Weiss, S.R., Experimental demyelination produced by the A59 strain of mouse hepatitis virus (1984) Neurology, 34, pp. 597-603; Lavi, E., Murray, E.M., Makino, S., Stohlman, S.A., Lai, M.M.C., Weiss, S.R., Determinants of coronavirus MHV pathogenesis are localized to 3′ portions of the genome as determined by ribonucleic acid-ribonucleic acid recombination (1990) Lab. Investig., 62, pp. 570-578; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Jiang, X., Lavi, E., Weiss, S.R., Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein (1997) Virology, 239, pp. 1-10; Leparc-Goffart, I., Hingley, S.T., Chua, M.M., Phillips, J., Lavi, E., Weiss, S.R., Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism (1998) J. Virol., 72, pp. 9628-9636; Lewicki, D.N., Gallagher, T.M., Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors (2002) J. Biol. Chem., 277, pp. 19727-19734; Luo, Z., Matthews, A.M., Weiss, S.R., Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion (1999) J. Virol., 73, pp. 8152-8159; Luo, Z., Weiss, S.R., Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein (1998) Virology, 244, pp. 483-494; Matsuyama, S., Taguchi, F., Receptor-induced conformational changes of murine coronavirus spike protein (2002) J. Virol., 76, pp. 11819-11826; Matsuyama, S., Taguchi, F., Communication between S1N330 and a region in S2 of murine coronavirus spike protein is important for virus entry into cells expressing CEACAM1b receptor (2002) Virology, 295, pp. 160-171; Nash, T.C., Buchmeier, M.J., Entry of mouse hepatitis virus into cells by endosomal and nonendosomal pathways (1997) Virology, 233, pp. 1-8; Navas, S., Seo, S.H., Chua, M.M., Sarma, J.D., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J. Virol., 75, pp. 2452-2457; Ontiveros, E., Kuo, L., Masters, P.S., Perlman, S., Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS (2001) Virology, 289, pp. 230-238; Parker, S.E., Gallagher, T.M., Buchmeier, M.J., Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoproteins of several strains of murine hepatitis virus (1989) Virology, 173, pp. 664-673; Pearce, B.D., Hobbs, M.V., McGraw, T.S., Buchmeier, M.J., Cytokine induction during T-cell-mediated clearance of mouse hepatitis virus from neurons in vivo (1994) J. Virol., 68, pp. 5483-5495; Phillips, J.J., Chua, M., Rall, G.F., Weiss, S.R., Murine coronavirus spike glycoprotein mediates degree of viral spread, inflammation and virus-induced immunopathology in the central nervous system (2002) Virology, 301, pp. 109-120; Phillips, J.J., Chua, M., Seo, S.H., Weiss, S.R., Multiple regions of the murine coronavirus spike glycoprotein influence neurovirulence (2001) J. Neurovirol., 7, pp. 421-431; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Reed, L.J., Muench, H., A simple method of estimating fifty percent points (1938) Am. J. Hyg., 27, pp. 493-497; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) J. Virol., 71, pp. 9024-9031; Singh, M., Berger, B., Kim, P.S., LearnCoil-VMF: Computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins (1999) J. Mol. Biol., 290, pp. 1031-1041; Taguchi, F., Matsuyama, S., Soluble receptor potentiates receptor-independent infection by murine coronavirus (2002) J. Virol., 76, pp. 950-958; Tsai, J.C., Weiss, S.R., In vitro properties and pathogenesis of A59/MHV4 chimeric mouse hepatitis viruses (2001) Adv. Exp. Med. Biol., 494, pp. 169-172; Tsai, J.C., Zelus, B.D., Holmes, K.V., Weiss, S.R., The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain (2003) J. Virol., 77, pp. 841-850; Wang, F.I., Fleming, J.O., Lai, M.M., Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropathogenicity (1992) Virology, 186, pp. 742-749; White, J., Membrane fusion (1992) Science, 258, pp. 917-924; Zelus, B.D., Schickli, J.H., Blau, D.M., Weiss, S.R., Holmes, K.V., Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37°C by soluble murine CEACAM1 receptor glycoproteins or by pH 8 (2003) J. Virol., 77, pp. 830-840","Weiss, S.R.; Department of Microbiology, 203A Johnson Pavilion, University of Pennsylvania, Philadelphia, PA 19104-6076, United States; email: weisssr@mail.med.upenn.edu",,"Academic Press Inc.",00426822,,VIRLA,"12919742","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0043064024
"Glass W.G., Lane T.E.","7004536096;24722465300;","Functional analysis of the CC chemokine receptor 5 (CCR5) on virus-specific CD8+ T cells following coronavirus infection of the central nervous system",2003,"Virology","312","2",,"407","414",,36,"10.1016/S0042-6822(03)00237-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042062356&doi=10.1016%2fS0042-6822%2803%2900237-X&partnerID=40&md5=bf8c98015a4c6f833162c93e703a6e8d","Dept. of Molec. Biol./Biochemistry, University of California, Irvine, CA 92697-3900, United States; Dept. of Molec. Biol./Biochemistry, 3205 McGaugh Hall, University of California, Irvine, CA 92697-3900, United States","Glass, W.G., Dept. of Molec. Biol./Biochemistry, University of California, Irvine, CA 92697-3900, United States; Lane, T.E., Dept. of Molec. Biol./Biochemistry, University of California, Irvine, CA 92697-3900, United States, Dept. of Molec. Biol./Biochemistry, 3205 McGaugh Hall, University of California, Irvine, CA 92697-3900, United States","Intracranial infection of C57BL/6 mice with mouse hepatitis virus (MHV) results in an acute encephalomyelitis followed by a demyelinating disease similar in pathology to the human disease multiple sclerosis (MS). T cells participate in both defense and disease progression following MHV infection. Expression of chemokine receptors on activated T cells is important in allowing these cells to traffic into and accumulate within the central nervous system (CNS) of MHV-infected mice. The present study evaluated the contributions of CCR5 to the activation and trafficking of virus-specific CD8+ T cells into the MHV-infected CNS mice. Comparable numbers of virus-specific CD8+ T cells derived from immunized CCR5+/+ or CCR5-/- mice were present within the CNS of MHV-infected RAG1-/- mice following adoptive transfer, indicating that CCR5 is not required for trafficking of these cells into the CNS. RAG1-/- recipients of CCR5-/--derived CD8+ T cells exhibited a modest, yet significant (P ≤ 0.05), reduction in viral burden within the brain which correlated with increased CTL activity and IFN-γ expression. Histological analysis of RAG1-/- recipients of either CCR5+/+or CCR5-/--derived CD8+ T cells revealed only focal areas of demyelination with no significant differences in white matter destruction. These data indicate that CCR5 signaling on CD8+ T cells modulates antiviral activities but is not essential for entry into the CNS. © 2003 Elsevier Science (USA). All rights reserved.","Chemokine receptors; Chemokines; Neuroinflammation; T cell; Virus","CD8 antigen; chemokine receptor CCR5; gamma interferon; animal experiment; animal tissue; antigen specificity; article; cell activity; central nervous system infection; controlled study; correlation analysis; cytotoxic lymphocyte; demyelination; histology; mouse; multiple sclerosis; Murine hepatitis coronavirus; nonhuman; priority journal; protein analysis; protein expression; protein function; T lymphocyte; virus infection; Coronavirus; Murine hepatitis virus","Brodie, S.J., Patterson, B.K., Lewinsohn, D.A., Diem, K., Spach, D., Greenberg, P.D., Riddell, S.R., Corey, L., HIV-specific cytotoxic T lymphocytes traffic to lymph nodes and localize at sites of HIV replication and cell death (2000) J. Clin. Invest., 105, pp. 1407-1417; Castro, R.F., Perlman, S., CD8+ T-cell epitopes within the surface glycoprotein of a neurotropic coronavirus and correlation with pathogenicity (1995) J. Virol., 69, pp. 8127-8131; Chen, B.P., Kuziel, W.A., Lane, T.E., Lack of CCR2 results in increased mortality and impaired leukocyte activation and trafficking following infection of the central nervous system with a neurotropic coronavirus (2001) J. Immunol., 167, pp. 4585-4592; Fukada, K., Sobao, Y., Tomiyama, H., Oka, S., Takiguchi, M., Functional expression of the chemokine receptor CCR5 on virus epitope-specific memory and effector CD8+ T cells (2002) J. Immunol., 168, pp. 2225-2232; Glass, W.G., Lane, T.E., Functional expression of chemokine receptor CCR5 on CD4(+) T cells during virus-induced central nervous system disease (2003) J. Virol., 77, pp. 191-198; Glass, W.G., Liu, M.T., Kuziel, W.A., Lane, T.E., Reduced macrophage infiltration and demyelination in mice lacking the chemokine receptor CCR5 following infection with a neurotropic coronavirus (2001) Virology, 288, pp. 8-17; Hirano, N., Murakami, T., Fujiwara, K., Matsumoto, M., Utility of mouse cell line DBT for propagation and assay of mouse hepatitis virus (1978) Jpn. J. Exp. Med., 48, pp. 71-75; Houtman, J.J., Fleming, J.O., Pathogenesis of mouse hepatitis virus-induced demyelination (1996) J. Neurovirol., 2, pp. 361-376; Lane, T.E., Asensio, V.C., Yu, N., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., Dynamic regulation of alpha- and beta-chemokine expression in the central nervous system during mouse hepatitis virus-induced demyelinating disease (1998) J. Immunol., 160, pp. 970-978; Lane, T.E., Buchmeier, M.J., Murine coronavirus infection: A paradigm for virus-induced demyelinating disease (1997) Trends Microbiol., 5, pp. 9-14; Lane, T.E., Liu, M.T., Chen, B.P., Asensio, V.C., Samawi, R.M., Paoletti, A.D., Campbell, I.L., Buchmeier, M.J., A central role for CD4(+) T cells and RANTES in virus-induced central nervous system inflammation and demyelination (2000) J. Virol., 74, pp. 1415-1424; Liu, M.T., Armstrong, D., Hamilton, T.A., Lane, T.E., Expression of Mig (monokine induced by interferon-gamma) is important in T lymphocyte recruitment and host defense following viral infection of the central nervous system (2001) J. Immunol., 166, pp. 1790-1795; Liu, M.T., Chen, B.P., Oertel, P., Buchmeier, M.J., Armstrong, D., Hamilton, T.A., Lane, T.E., The T cell chemoattractant IFN-inducible protein 10 is essential in host defense against viral-induced neurologic disease (2000) J. Immunol., 165, pp. 2327-2330; Liu, M.T., Chen, B.P., Oertel, P., Buchmeier, M.J., Hamilton, T.A., Armstrong, D.A., Lane, T.E., The CXC chemokines IP-10 and Mig are essential in host defense following infection with a neurotropic coronavirus (2001) Adv. Exp. Med. Biol., 494, pp. 323-327; Marten, N.W., Stohlman, S.A., Bergmann, C.C., MHV infection of the CNS: Mechanisms of immune-mediated control (2001) Viral Immunol., 14, pp. 1-18; Nansen, A., Christensen, J.P., Andreasen, S.O., Bartholdy, C., Christensen, J.E., Thomsen, A.R., The role of CC chemokine receptor 5 in antiviral immunity (2002) Blood, 99, pp. 1237-1245; Pewe, L., Haring, J., Perlman, S., CD4 T-cell-mediated demyelination is increased in the absence of gamma interferon in mice infected with mouse hepatitis virus (2002) J. Virol., 76, pp. 7329-7333; Pewe, L., Perlman, S., Cutting edge: CD8 T cell-mediated demyelination is IFN-gamma dependent in mice infected with a neurotropic coronavirus (2002) J. Immunol., 168, pp. 1547-1551; Stohlman, S.A., Bergmann, C.C., Lin, M.T., Cua, D.J., Hinton, D.R., CTL effector function within the central nervous system requires CD4+ T cells (1998) J. Immunol., 160, pp. 2896-2904; Williamson, J.S., Stohlman, S.A., Effective clearance of mouse hepatitis virus from the central nervous system requires both CD4+ and CD8+ T cells (1990) J. Virol., 64, pp. 4589-4592; Wu, G.F., Dandekar, A.A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286; Wu, G.F., Perlman, S., Macrophage infiltration, but not apoptosis, is correlated with immune-mediated demyelination following murine infection with a neurotropic coronavirus (1999) J. Virol., 73, pp. 8771-8780","Lane, T.E.; Dept. of Molec. Biol./Biochemistry, 3205 McGaugh Hall, University of California, Irvine, CA 92697-3900, United States; email: tlane@uci.edu",,"Academic Press Inc.",00426822,,VIRLA,"12919745","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0042062356
"Ferreira H.L., Pilz D., Mesquita L.G., Cardoso T.","12241195400;7006221152;57197288633;8344789200;","Infectious bronchitis virus replication in the chicken embryo related cell line",2003,"Avian Pathology","32","4",,"413","417",,5,"10.1080/0307945031000121167","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141836728&doi=10.1080%2f0307945031000121167&partnerID=40&md5=85a8ff9e61dfcf6b63268a0a57b8a13e","Curso de Medicina Veterinaria, Faculdade de Odontologia, UNESP - Araçatuba, Säo Paulo, Brazil; Universidade Estadual de Londrina, Paraná, Brazil; Depto. de Apoio, Prod. e Saude Anim., Curso de Medicina Veterinária, Rua Clóvis Pestana 793, 16.050-680 Araçatuba, SP, Brazil","Ferreira, H.L., Curso de Medicina Veterinaria, Faculdade de Odontologia, UNESP - Araçatuba, Säo Paulo, Brazil; Pilz, D., Universidade Estadual de Londrina, Paraná, Brazil; Mesquita, L.G., Curso de Medicina Veterinaria, Faculdade de Odontologia, UNESP - Araçatuba, Säo Paulo, Brazil; Cardoso, T., Curso de Medicina Veterinaria, Faculdade de Odontologia, UNESP - Araçatuba, Säo Paulo, Brazil, Depto. de Apoio, Prod. e Saude Anim., Curso de Medicina Veterinária, Rua Clóvis Pestana 793, 16.050-680 Araçatuba, SP, Brazil","The susceptibility of the chicken embryo related (CER) cell line to infectious bronchitis virus (IBV M41) was characterized after five consecutive passages in CER cells. Virus replication was monitored by cytopathic effect observation, electron microscopy, indirect immunofluorescence, and reverse transcription polymerase chain reaction (RT-PCR). At 96 h post-infection (p.i.), the cytopathic effect was graded 75% by cell fusion, rounding up of cells and monolayer detachment, and the electron microscopy image characterized by coronavirus morphology. Cytoplasmic fluorescence was readily observed by from 24 h p.i. onwards, and at all times the respective viral RNA from IBV-infected monolayers was demonstrated by RT-PCR. Extra-cellular virus was measured by virus titration performed on chicken kidney cells and embryonated chicken eggs, and respective titres ranged from 4.0 to 6.0 log10 EID 50/ml on embryonated chicken eggs, and from 2.0 to 6.0 log 10 TCID50/ml on both CER cells and chicken kidney cells studied from 24 to 120 h p.i. These results confirmed that the M41 strain replicated well in the CER cell line.",,"Animals; Cell Line; Chick Embryo; Infectious bronchitis virus; Virus Cultivation; Virus Replication; Aves; Avian infectious bronchitis virus; Coronavirus; Gallus gallus","Brenner, S., Horne, R.W., A negative staining method for high resolution electron microscopy (1959) Biochemistry and Biophysics Acta, 34, pp. 103-110; Bronzoni, R.V.M., Pinto, A.A., Montassier, H.J., Detection of infectious bronchitis virus in experimentally infected chickens by an antigen-competitive ELISA (2001) Avian Pathology, 30, pp. 67-71; Bussereau, F., Flamand, A., Pese-Part, D., Reproducible plaquing system for rabies in CER cells (1982) Journal of Virological Methods, 4, pp. 277-282; Capua, I., Minta, Z., Karpinska, E., Mawditt, K., Britton, P., Cavanagh, D., Gough, R.E., Co-circulation of four types of infectious bronchitis virus (793/B, 624/1, B1648 and Massachusetts) (1999) Avian Pathology, 28, pp. 587-593; Cardoso, T.C., Mouro De Sousa, R.L., Oliveira, C., Stringhini, G., Pinto, A.A., A liquid phase blocking ELISA for the detection of antibodies against infectious bronchitis virus (1999) Brazilian Journal of Medical and Biological Research, 32, pp. 747-752; Cardoso, T.C., Rahal, P., Pilz, D., Teixeira, M.C., Arns, C.W., Replication of classical infectious bursal disease virus in the chicken embryo related cell line (2000) Avian Pathology, 29, pp. 213-217; Cavanagh, D., Innovation and discovery: The application of nucleic-based technology to avian virus detection and characterization (2001) Avian Pathology, 30, pp. 581-598; Cavanagh, D., Naqi, S.A., Infectious bronchitis (1997) Diseases of Poultry, 10th Edn, pp. 511-526. , B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald & Y.M. 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Geneva: World Health Organization","Cardoso, T.; Depto. de Apoio, Prod. e Saude Anim., Curso de Medicina Veterinária, Rua Clóvis Pestana 793, 16.050-680 Araçatuba, SP, Brazil; email: tcardoso@fmva.unesp.br",,,03079457,,AVPAD,"17585465","English","Avian Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0141836728
"Chen H., Schifferli D.M.","55743114500;7004526277;","Construction, characterization, and immunogenicity of an attenuated Salmonella enterica serovar typhimurium pgtE vaccine expressing fimbriae with integrated viral epitopes from the spiC promoter",2003,"Infection and Immunity","71","8",,"4664","4673",,30,"10.1128/IAI.71.8.4664-4673.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042265010&doi=10.1128%2fIAI.71.8.4664-4673.2003&partnerID=40&md5=5f6fff649891928119dc58b0ddc7f883","Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., Philadelphia, PA 19104, United States; Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., 3800 Spruce St., Philadelphia, PA 19104, United States","Chen, H., Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., Philadelphia, PA 19104, United States; Schifferli, D.M., Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., Philadelphia, PA 19104, United States, Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., 3800 Spruce St., Philadelphia, PA 19104, United States","Transmissible gastroenteritis virus (TGEV) is a porcine coronavirus that causes diarrhea, leading to near 100% mortality in neonatal piglets with corresponding devastating economic consequences. For the protection of neonatal and older animals, oral live vaccines present the attractive property of inducing desired mucosal immune responses, including colostral antibodies in sows - an effective means to passively protect suckling piglets. Newly attenuated Salmonella vaccine constructs expressing TGEV S protein epitopes were studied and evaluated for improved humoral immune response to TGEV. The macrophage-inducible Salmonella ssaH and spiC/ssaB promoters were compared for their ability to express the TGEV C and A epitopes in the context of the heterologous 987P fimbriae on Salmonella vaccines. Compared to the ssaH promoter, the Salmonella cya crp vector elicited significantly higher levels of mucosal and systemic antibodies in orally immunized mice when the chimeric fimbriae were expressed from the spiC promoter. The Salmonella spiC promoter construct induced the highest level of chimeric fimbriae after being taken up by the J774A.1 macrophagelike cells. The Salmonella cya crp vaccine vector was shown to incorporate into 987P partially degraded chimeric subunits lacking the TGEV epitopes. In contrast, its isogenic pgtE mutant produced fimbriae consisting exclusively of intact chimeric subunits. Mice immunized orally with the Salmonella pgtE vaccine expressing chimeric fimbriae from the spiC promoter elicited significantly higher systemic and mucosal antibody titers against the TGEV epitopes compared to the parental vaccine. This study indicates that the Salmonella cya crp pgtE vector and the spiC promoter can be used successfully to improve immune responses toward heterologous antigens.",,"chimeric protein; epitope; salmonellosis vaccine; virus antigen; adolescent; animal cell; antibody titer; article; bacterial gene; expression vector; female; fimbria; gene expression; humoral immunity; immunogenicity; macrophage; mouse; mucosal immunity; nonhuman; pgtE gene; priority journal; promoter region; Salmonella cya crp pgtE vector; Salmonella enterica; spiC gene; ssaB gene; ssaH gene; swine disease; Transmissible gastroenteritis virus; vaccine production; Adhesins, Escherichia coli; Amino Acid Sequence; Animals; Antibodies, Viral; Antigens, Bacterial; Antigens, Viral; Bacterial Proteins; Base Sequence; DNA, Bacterial; Endopeptidases; Epitopes; Female; Fimbriae Proteins; Fimbriae, Bacterial; Gastroenteritis, Transmissible, of Swine; Genes, Bacterial; Immunization, Secondary; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Mutation; Promoter Regions (Genetics); Recombinant Fusion Proteins; Salmonella typhimurium; Salmonella Vaccines; Transmissible gastroenteritis virus; Vaccines, Attenuated; Viral Vaccines","Alexeyev, M.F., Shokolenko, I.N., Croughan, T.P., Improved antibiotic-resistance gene cassettes and omega elements for Escherichia coli vector construction and in vitro deletion/insertion mutagenesis (1995) Gene, 160, pp. 63-67; Attridge, S.R., Davies, R., LaBrooy, J.T., Oral delivery of foreign antigens by attenuated Salmonella: Consequences of prior exposure to the vector strain (1997) Vaccine, 15, pp. 155-162; Bao, J.X., Clements, J.D., Prior immunologic experience potentiates the subsequent antibody response when Salmonella strains are used as vaccine carriers (1991) Infect. 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Chem., 39, p. 2021","Schifferli, D.M.; Department of Pathobiology, Univ. Pennsylvania Sch. of Vet. Med., 3800 Spruce St., Philadelphia, PA 19104, United States; email: dmschiff@vet.upenn.edu",,,00199567,,INFIB,"12874347","English","Infect. Immun.",Article,"Final",Open Access,Scopus,2-s2.0-0042265010
"Zhao Z., Zhang F., Xu M., Huang K., Zhong W., Cai W., Yin Z., Huang S., Deng Z., Wei M., Xiong J., Hawkey P.M.","57211422606;10640508100;56390237300;7403188599;7402328819;57198996745;57199668702;23987718700;55449477300;7202184597;57199829863;7005320725;","Description and clinical treatment of an early outbreak of severe acute respiratory syndrome (SARS) in Guangzhou, PR China",2003,"Journal of Medical Microbiology","52","8",,"715","720",,159,"10.1099/jmm.0.05320-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042354620&doi=10.1099%2fjmm.0.05320-0&partnerID=40&md5=3cd3ed255d1441d85166a28cf2ed6436","Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China; Eighth Munic. People's Hosp. G., 627 Dongfeng Dong Road, Guangzhou, 510180, China; Second Affil. Hosp. Guangzhou M., 250 Changgang Dong Road, Guangzhou, 510655, China; Guangzhou Red-Cross Hospital, 396 Tongfu Zhong Road, Guangzhou, 510220, China; Sixth Munic. People's Hosp. G., 19 Yuanchu Xijie, Tianhe Guangzhou, 510260, China; Division of Immunity and Infection, Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom","Zhao, Z., Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China; Zhang, F., Eighth Munic. People's Hosp. G., 627 Dongfeng Dong Road, Guangzhou, 510180, China; Xu, M., Eighth Munic. People's Hosp. G., 627 Dongfeng Dong Road, Guangzhou, 510180, China; Huang, K., Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China; Zhong, W., Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China; Cai, W., Eighth Munic. People's Hosp. G., 627 Dongfeng Dong Road, Guangzhou, 510180, China; Yin, Z., Eighth Munic. People's Hosp. G., 627 Dongfeng Dong Road, Guangzhou, 510180, China; Huang, S., Second Affil. Hosp. Guangzhou M., 250 Changgang Dong Road, Guangzhou, 510655, China; Deng, Z., Guangzhou Red-Cross Hospital, 396 Tongfu Zhong Road, Guangzhou, 510220, China; Wei, M., Sixth Munic. People's Hosp. G., 19 Yuanchu Xijie, Tianhe Guangzhou, 510260, China; Xiong, J., Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China, Division of Immunity and Infection, Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom; Hawkey, P.M., Division of Immunity and Infection, Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom","Severe acute respiratory syndrome (SARS), now known to be caused by a coronavirus, probably originated in Guangdong province in southern China in late 2002. The first major outbreak occurred in Guangzhou, the capital of Guangdong, between January and March 2003. This study reviews the clinical presentation, laboratory findings and response to four different treatment protocols. Case notes and laboratory findings were analysed and outcome measures were collected prospectively. The SARS outbreak in Guangdong province and the outbreak in Guangzhou associated with hospitals in the city are described, documenting clinical and laboratory features in a cohort of 190 patients randomly allocated to four treatment regimens. Patients were infected by close contact in either family or health-care settings, particularly following procedures likely to generate aerosols of respiratory secretions (e.g. administration of nebulized drugs and bronchoscopy). The earliest symptom was a high fever followed, in most patients, by dyspnoea, cough and myalgia, with 24% of patients complaining of diarrhoea. The most frequent chest X-ray changes were patchy consolidation with progression to bilateral bronchopneumonia over 5-10 days. Thirty-six cases developed adult respiratory distress syndrome (ARDS), of whom 11 died. There was no response to antibiotics. The best response (no deaths) was seen in the group of 60 patients receiving early high-dose steroids and nasal CPAP (continuous airway positive pressure) ventilation; the other three treatment groups had significant mortality. Cross-infection to medical and nursing staff was completely prevented in one hospital by rigid adherence to barrier precautions during contact with infected patients. The use of rapid case identification and quarantine has controlled the outbreak in Guangzhou, in which more than 350 patients have been infected. Early administration of high-dose steroids and CPAP ventilation appears to offer the best supportive treatment with a reduced mortality compared with other treatment regimens.",,"azithromycin; levofloxacin; methylprednisolone; prednisolone; quinoline derived antiinfective agent; recombinant alpha interferon; ribavirin; steroid; sulperazon; adult; aerosol; article; bronchopneumonia; China; clinical article; clinical feature; controlled study; Coronavirus; coughing; cross infection; diarrhea; dyspnea; early diagnosis; epidemic; female; histopathology; human; intermethod comparison; laboratory diagnosis; lower respiratory tract infection; male; medical staff; mortality; myalgia; nonhuman; oxygen therapy; positive end expiratory pressure; priority journal; SARS coronavirus; severe acute respiratory syndrome; thorax radiography; treatment outcome; virus identification; virus pneumonia; Adult; Anti-Infective Agents; Anti-Inflammatory Agents; Antiviral Agents; China; Disease Outbreaks; Female; Humans; Interferon-alpha; Male; Methylprednisolone; Middle Aged; Quarantine; SARS Virus; Severe Acute Respiratory Syndrome; Treatment Outcome","Bernard, G.R., Artigas, A., Brigham, K.L., Report of the American-European consensus conference on ARDS: Definitions, mechanisms, relevant outcomes and clinical trial coordination (1994) Intensive Care Med, 20, pp. 225-232. , The Consensus Committee; Chan, P.K., Outbreak of avian influenza A (H5N1) virus infection in Hong Kong in 1997 (2002) Clin Infect Dis, 34 (2 SUPPL.), pp. S58-S64; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966. , SARS Working Group; Lee, S.J., Lee, M.G., Jeon, M.J., Jung, K.S., Lee, H.K., Kishimoto, T., Atypical pathogens in adult patients admitted with community-acquired pneumonia in Korea (2002) Jpn J Infect Dis, 55, pp. 157-159; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peers, S.H., Flower, R.J., The role of lipocortin in corticosteroid actions (1990) Am Rev Respir Dis, 141, pp. S18-S21; Peiris, J.S.M., Lai, S.T., Pooh, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Saikku, P., Atypical respiratory pathogens (1991) Clin Microbiol Infect, 3, pp. 599-604; Tsang, K.M., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Acute respiratory syndrome. China, Hong Kong Special Administrative Region of China, and Viet Nam (2003) Wkly Epidemiol Rec, 78, pp. 73-74; (2003) Severe Acute Respiratory Syndrome - Press Briefing, , http://www.who.int/csr/sars/2003_04_16/en/, 16 April 2003; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinitions; Williams, T.J., Yarwood, H., Effect of glucocorticosteroids on microvascular permeability (1990) Am Rev Respir Dis, 141, pp. S39-S43; Yuen, K.Y., Chan, P.K.S., Peiris, M., Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus (1998) Lancet, 351, pp. 467-471","Zhao, Z.; Depts. of Resp. Dis./Lab. Medicine, First Munic. People's Hosp. G., 1 Panfu Road, Guangzhou, China; email: zhaozw1963@yahoo.com.cn",,,00222615,,JMMIA,"12867568","English","J. Med. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0042354620
"Çetinkaya Şardan Y.","6506154318;","Severe acute respiratory syndrome (SARS) [Aǧir akut solunum yetmezliǧi sendromu (SARS)]",2003,"Anestezi Dergisi","11","2",,"99","104",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041314033&partnerID=40&md5=2165d3169f77e57edb60ebdafb987aa3","Hacettepe Universitesi Tip Fakultesi, Ic Hastaliklari Anabilim Dali, Infeksiyon Hastaliklari Unitesi, Hacettepe, Turkey","Çetinkaya Şardan, Y., Hacettepe Universitesi Tip Fakultesi, Ic Hastaliklari Anabilim Dali, Infeksiyon Hastaliklari Unitesi, Hacettepe, Turkey","The severe acute respiratory syndrome (SARS) has recently been identified as a new clinical entity. Patients present with fever, dry cough, dyspnea, headache, and hypoxemia. Typical laboratory findings are lymphopenia and mildly elevated aminotransferase levels. Death may result from progressive respiratory failure due to alveolar damage. SARS appears to be caused by an unknown infectious agent that is transmitted from human to human. and a novel coronavirus has recently been identified in patients with SARS. The SARS epidemic started in Asia, with the majority of cases occurring in China and the Asia-Pacific region. The epidemic has spread from Asia to other continents through international travel. Early recognition, prompt isolation, and appropriate supportive therapy are the keys in combating this deadly infection.","Outbreak; Severe acute respiratory syndrome","aminotransferase; aminotransferase blood level; article; Asia; cause of death; China; clinical feature; Coronavirus; coughing; dyspnea; early diagnosis; fever; headache; human; hypoxemia; infection control; laboratory diagnosis; lung alveolus; lymphocytopenia; Pacific Ocean; patient care; respiratory failure; severe acute respiratory syndrome; travel; virus pneumonia; virus transmission","Fleischauer, A.T., (2003) MMWR, 52, pp. 226-228. , and the CDC SARS Investigating Team; (2003) MMWR, , Dispatch 52/April 29; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome N. Engl. J. Med., , http://content.nejm.org/cgi/reprint/NEJMoa030781v3.pdf, Available at; Droosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome N. Eng. J. Med., , http://content.nejm.org/cgi/reprint/NEJMoa030747v2.pdf, Available at; (2003) MMWR, 52, pp. 255-256; htpp://www.who.int/csr/sarscountry/2003_04_30/en/print.html; Lee, N., Hu, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., , Apr 14 (epub ahead of print); htpp://www.cdc.gov/ncidod/sars/ic-closecontacts.htm; htpp://www.who.int/csr/sars/infectioncontrol/en/print.html","Çetinkaya Şardan, Y.; Hacettepe Universitesi Tip Fakultesi, Ic Hastaliklari Anabilim Dali, Infeksiyon Hastaliklari Ünitesi, Ankara, Turkey; email: ycetinka@hacettepe.edu.tr",,,13000578,,ADNEC,,"Turkish","Anestezi Derg.",Article,"Final",,Scopus,2-s2.0-0041314033
"Leng Q., Bentwich Z.","56208422400;7005510294;","A novel coronavirus and SARS [3]",2003,"New England Journal of Medicine","349","7",,"709","",,15,"10.1056/NEJMc031427","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0348198434&doi=10.1056%2fNEJMc031427&partnerID=40&md5=ebdb81ad550da6dfe5bbaeed4c30d2b1","Weizmann Institute of Science, Rehovot 76100, Israel; Rosetta Genomics, Rehovot 76701, Israel","Leng, Q., Weizmann Institute of Science, Rehovot 76100, Israel; Bentwich, Z., Rosetta Genomics, Rehovot 76701, Israel",[No abstract available],,"antigen recognition; Coronavirus; cross reaction; human; immunity; letter; open reading frame; priority journal; respiratory tract infection; severe acute respiratory syndrome; T lymphocyte; virus neutralization; virus strain; animal; Coronavirus; immunology; note; SARS coronavirus; virus vaccine; Animals; Coronavirus; Cross Reactions; Humans; SARS Virus; Viral Vaccines","Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Kotwal, G.J., Poxviral mimicry of complement and chemokine system components: What's the end game? (2000) Immunol Today, 21, pp. 242-248; Leng, Q., Bentwich, Z., Beyond self and nonself: Fuzzy recognition of the immune system (2002) Scand J Immunol, 56, pp. 224-232","Leng, Q.; Weizmann Institute of Science, Rehovot 76100, Israel; email: qibin_leng@yahoo.com",,,00284793,,NEJMA,"12917313","English","New Engl. J. Med.",Letter,"Final",,Scopus,2-s2.0-0348198434
"Chou K.-C., Wei D.-Q., Zhong W.-Z.","7201905167;7202909038;57214690924;","Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS",2003,"Biochemical and Biophysical Research Communications","308","1",,"148","151",,336,"10.1016/S0006-291X(03)01342-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041848237&doi=10.1016%2fS0006-291X%2803%2901342-1&partnerID=40&md5=c95bec18117487378331f006cb4e1aa1","Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States; Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China","Chou, K.-C., Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States, Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China; Wei, D.-Q., Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China; Zhong, W.-Z., Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States, Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China","In order to stimulate the development of drugs against severe acute respiratory syndrome (SARS), based on the atomic coordinates of the SARS coronavirus main proteinase determined recently [Science 13 (May) (2003) (online)], studies of docking KZ7088 (a derivative of AG7088) and the AVLQSGFR octapeptide to the enzyme were conducted. It has been observed that both the above compounds interact with the active site of the SARS enzyme through six hydrogen bonds. Also, a clear definition of the binding pocket for KZ7088 has been presented. These findings may provide a solid basis for subsite analysis and mutagenesis relative to rational design of highly selective inhibitors for therapeutic application. Meanwhile, the idea of how to develop inhibitors of the SARS enzyme based on the knowledge of its own peptide substrates (the so-called ""distorted key"" approach) was also briefly elucidated. © 2003 Elsevier Inc. All rights reserved.","""Distorted key"" mechanism; AG7088; Binding pocket; Coronavirus proteinase; KZ7088; Octapeptide substrate; SARS","antivirus agent; kz 7088; octapeptide; proteinase; rupintrivir; unclassified drug; virus protein; article; Coronavirus; drug binding; drug design; drug research; hydrogen bond; mutagenesis; priority journal; protein binding; severe acute respiratory syndrome; virus pneumonia; Coronavirus; SARS coronavirus","Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Science, , www.scienceexpress.org; Schechter, I., Berger, A., (1967) Biochem. Biophys. Res. Commun., 27, pp. 157-162; Miller, M., Schneider, J., Sathyanarayana, B.K., Toth, M.V., Marshall, G.R., Clawson, L., Selk, L., Wlodawer, A., (1989) Science, 246, pp. 1149-1152; Chou, K.C., (1993) J. Biol. Chem., 268, pp. 16938-16948; Chou, K.C., (1996) Anal. Biochem., 233, pp. 1-14; Chou, K.C., Watenpaugh, K.D., Heinrikson, R.L., (1999) Biochem. Biophys. Res. Commun., 259, pp. 420-428; Tarricone, C., Dhavan, R., Peng, J., Areces, L.B., Tsai, L.H., Musacchio, A., (2001) Mol. Cell, 8, pp. 657-669; Chou, K.C., Tomasselli, A.G., Heinrikson, R.L., (2000) FEBS Lett., 470, pp. 249-256; Zhang, J., Luan, C.H., Chou, K.C., Johnson, G.V.W., (2002) Proteins, 48, pp. 447-453; Chou, K.C., Howe, W.J., (2002) Biochem. Biophys. Res. Commun., 292, pp. 702-708","Chou, K.-C.; Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States; email: kchou@chartermi.net",,"Academic Press Inc.",0006291X,,BBRCA,"12890493","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-0041848237
"Vijgen L., Van Bleyenbergh P., Keyaerts E., Moës E., Demedts M., Lagrou K., Peetermans W., Van Ranst M.","6602556791;6507797308;6603305291;6507575511;7103151782;19134962000;7006201816;7005113740;","SARS (severe acute respiratory syndrome): A novel pulmonary disease [SARS (""severe acute respiratory syndrome""): Een nieuwe virale longaandoening]",2003,"Tijdschrift voor Geneeskunde","59","16-17",,"971","977",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042324755&partnerID=40&md5=671af198568f13cbae089cb1e7ab2724","Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium","Vijgen, L., Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium; Van Bleyenbergh, P.; Keyaerts, E., Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium; Moës, E., Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium; Demedts, M.; Lagrou, K.; Peetermans, W.; Van Ranst, M., Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium","Severe acute respiratory syndrome (SARS) is a novel infectious disease that first emerged at the end of November 2002 in the Chinese province Guangdong. This atypical pneumonia began to spread to different countries all over the world during February and March 2003. The World Health Organization (WHO) issued a global alert on March 15, 2003 in an attempt to prevent further spread of this disease. The most common symptoms include high fever, malaise, a nonproductive cough and dyspnea. Approximately two weeks after the WHO global alert on SARS, a novel coronavirus had been identified as its cause. Phylogenetic analysis of the SARS coronavirus (SARS-CoV) genome demonstrated that this new type coronavirus is not closely related to any of the known coronaviruses. A possible animal origin for the SARS-CoV is supposed, since a genetically closely related coronavirus has been identified in civet cats. Until now (July 11, 2003), the cumulative number of SARS cases amounts to 8437, including 813 deaths. At this moment the epidemic seems to be under control. Taiwan was the last country which WHO declared free of SARS on July 5, 2003.",,"clinical feature; Coronavirus; geographic distribution; human; incidence; respiratory tract infection; review; severe acute respiratory syndrome; virus infection; virus transmission; world health organization","(2003) Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars, Geneva: World Health Organization; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Arbour, N., Day, R., Newcombe, J., Talbot, P.J., Neuroinvasion by human respiratory coronaviruses (2000) J Virol, 74, pp. 8913-8921; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Luby, J.P., Clinton, R., Kurtz, S., Adaptation of human enteric coronavirus to growth in cell lines (1999) J Clin Virol, 12, pp. 43-51; Marra, M.A., Jones, S.J., Astell, C.R., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Cyranoski, D., Abbott, A., Virus detectives seek source of SARS in China's wild animals (2003) Nature, 423, p. 467; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809","Van Ranst, M.; Lab. Klin. en Epidemiol. Virologie, Rega Instituut, K.U.Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium; email: marc.vanranst@uz.kuleuven.ac.be",,,0371683X,,TGEKB,,"Dutch","Tijdschr. Geneeskd.",Review,"Final",,Scopus,2-s2.0-0042324755
"Nie Q.-H., Lou X.-D., Zhang J.-Z., Su Q.","7005041783;36750338200;9939370800;7201716073;","Current status of severe acute repiratory syndrome in China",2003,"World Journal of Gastroenterology","9","8",,"1635","1645",,21,"10.3748/wjg.v9.i8.1635","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041426375&doi=10.3748%2fwjg.v9.i8.1635&partnerID=40&md5=54429b037f670846bb2dcb04f82fdcd9","Chinese PLA Ctr. Diagn./Treatm., Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; Department of Pathology, Beijing 306 Hospital, Beijing 100101, China; Department of Pathology, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China","Nie, Q.-H., Chinese PLA Ctr. Diagn./Treatm., Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; Lou, X.-D., Chinese PLA Ctr. Diagn./Treatm., Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; Zhang, J.-Z., Department of Pathology, Beijing 306 Hospital, Beijing 100101, China; Su, Q., Department of Pathology, Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China","Severe acute respiratory syndrome (SARS), also called infectious atypical pneumonia, is an emerging infectious disease caused by a novel variant of coronavirus (SARS-associated coronavirus, SARS-CoV). It is mainly characterized by pulmonary infection with a high infectivity and fatality. SARS is swept across almost all the continents of the globe, and has currently involved 33 countries and regions, including the mainland China, Hong Kong, Taiwan, North America and Europe. On June 30, 2003, an acumulative total reached 8450 cases with 810 deaths. SARS epidemic was very rampant in March, April and May 2003 in the mainland of China and Hong Kong. Chinese scientists and healthcare workers cooperated closely with other scientists from all over the world to fight the disease. On April 16, 2003, World Health Organization (WHO) formally declared that SARS-CoV was an etiological agent of SARS. Currently, there is no specific and effective therapy and prevention method for SARS. The main treatments include corticosteroid therapy, anti-viral agents, anti-infection, mechanical ventilation and isolation. This disease can be prevented and controlled, and it is also curable. Under the endeavor of the Chinese Government, medical staffs and other related professionals, SARS has been under control in China, and Chinese scientists have also made a great contribution to SARS research. Other studies in developing new detection assays and therapies, and discovering new drugs and vaccines are in progress. In this paper, we briefly review the current status of SARS in China.",,"acetylsalicylic acid; amoxicillin plus clavulanic acid; antibiotic agent; antiinfective agent; antipyretic analgesic agent; antivirus agent; beta lactam antibiotic; clarithromycin; corticosteroid; dddc as 001; dipeptide derivative; expectorant agent; glucocorticoid; herbaceous agent; immunomodulating agent; jieduwan; levofloxacin; lung surfactant; macrolide; methylprednisolone; prednisolone; proteinase inhibitor; quinoline derived antiinfective agent; ribavirin; sivelestat; tetracycline derivative; thymosin; unclassified drug; unindexed drug; vaccine; vancomycin; virus antibody; artificial ventilation; assay; China; clinical feature; clinical protocol; clinical trial; Coronavirus; differential diagnosis; drug pulse therapy; enzyme linked immunosorbent assay; epidemic; Europe; fatality; fever; government; health care personnel; Hong Kong; human; immunofluorescence test; infection control; intensive care; laboratory test; medical research; medical staff; microscopy; nonhuman; North America; pathogenesis; pathology; pneumonia; population; prediction; respiratory tract infection; reverse transcription polymerase chain reaction; review; Reye syndrome; SARS coronavirus; severe acute respiratory syndrome; statistical analysis; Taiwan; transmission electron microscopy; virus infectivity; virus isolation; virus transmission; world health organization","Cumulative number of reported cases of severe acute respiratory syndrome (SARS) http://www.who.int/csr/sarsarchive/2003-03-31/en, March 31, 2003; Weekly epidemiological record. 14 March 2003, 78th year http://www.who.int/wer/pdf/2003/wer7811.pdf, / 14 March 2003; Kamps, B.S., Kamps-Hoffman, 1. Timeline. SARS Reference (First Edition), , http://sarsreference.com/index.htm, May 8,2003; Reilley, B., Van Herp, M., Sermand, D., Dentico, N., SARS and Carlo Urbani (2003) N Engl J Med, 348, pp. 1951-1952; Coronavirus never before seen in humans is the cause of SARS http://www.who.int/csr/sarsarchive/2003-04-16/en/, 16 April 2003; Luo, H.M., Yu, H.J., Ni, D.X., Yin, W.W., Gao, L.D., Mo, J.J., Yang, W.Z., Li, L.M., Etiology of infectious SARS and live survey (2003) Zhonghua Liuxing Bingxue Zazhi, 24, pp. 336-339; He, J.F., Peng, G.W., Zheng, H.Z., Luo, H.M., Liang, W.J., Li, L.H., Guo, R.L., Deng, Z.H., An epidemiological study on the index cases of severe acute respiratory syndrome occurred in different cities among Guangdong province (2003) Zhonghua Liuxing Bingxue Zazhi, 24, pp. 347-349; Lu, H.Y., Huo, N., Xu, X.Y., Wang, G.F., Li, J.P., Wang, G.Q., Li, H.C., Nie, L.G., The epidemiologic characteristics of 80 patients with severe acute respiratory syndrome (SARS) (2003) Beijing Daxue Xuebao (Yixueban), 35 S, pp. 8-11; Wang, M., Du, L., Zhou, R.H., Di, B., Liu, Y.F., Qing, P.Z., Wu, X.W., Li, Z.R., Study on the epidemiology and measures for control on severe acute respiratory syndrome in Guangzhou city (2003) Zhonghua Liuxing Bingxue Zazhi, 24, pp. 353-355; Liu, Z.J., Sheng, Z., He, X., Huang, R.G., Teng, R.M., Ning, F., Li, X.M., Lin, C.Y., An epidemiological analysis on a input SARS case (2003) Zhonghua Liuxing Bingxue Zazhi, 4, pp. 358-359; Zhonghua, Y., Zhonghua, Y.Y., Zhonghua, Y.G.X., Summary of academic seminar between two shores on control SARS (2003) Zhonghua Yixue Zazhi, 83, pp. 708-712; Liu, B., Establishment of model of SARS space statistics in University of Science and Technology of China http://wwww.gmd.com.cn.gmw.defaulta.htm, 2003.06.16; Hong, T., Wang, J.W., Sun, Y.L., Duan, S.M., Chen, L.B., Qu, J.G., Ni, A.P., Ruan, L., Chlamydia-like and coronavirus-like agents found in dead cases of atypical pneumonia by electron microscopy (2003) Zhonghua Yixue Zazhi, 83, pp. 632-636; Zhu, Q.Y., Qin, E.D., Wang, C.E., The isolation and identification of a novel coronavirus from patient of severe acute respiratory syndrome (2003) Zhongguo Gongcheng Shengwu Zazhi, 23, pp. 106-112; Fan, B.C., Jiang, T., Yu, M., Deng, Y.Q., Peng, W.M., Chang, G.H., Shi, B.Y., Qing, E.D., Determination and analysis of 3′ untranslated regions of 4 strains of SARS coronavirus isolated in China (2003) Zhongguo Shengwu Huaxue Yu Fenzi Shengwu Xuebao, 19, pp. 273-277; http://www.washprofile.org/chinese/sars-pathogen-042503.cfm, 2003.04.25; Ding, Y.Q., Preliminary discussion of etiology and pathogenesis of acute respiratory syndrome (2003) Jiefangjun Yixue Zazhi, 28, pp. 475-476; Zhao, J.M., Zhou, G.D., Sun, Y.L., Wang, S.S., Yang, J.F., Mao, Y.L., Pan, D., Chen, J.M., Pathological and etiological findings in a dead case of severe acute respiratory syndrome of China (2003) Jiefangjun Yixue Zazhi, 28, pp. 379-382; Wang, C.E., Qin, E.D., Gan, Y.H., Li, Y.C., Wu, X.H., Cao, J.T., Yu, M., Zhu, Q.Y., Pathological observation on suckling mice and vero E6 cells inoculated with SARS samples (2003) Jiefangjun Yixue Zazhi, 28, pp. 383-384; Lai, H.W., Lai, R.Q., Yang, C.H., Feng, X.D., Wang, Z.C., Pathology and ultrastructure in one infectious SARS case (2003) Jiefangjun Yixue Zazhi, 28 S, pp. S34-S35; Ji, X.L., Tong, Y., Shen, M.S., Mechanisms of lung injury in severe acute respiratory syndrome (SARS): Histopathological analysis (2003) Zhonghua Weishengwuxue He Mianyixue Zazhi, 23, pp. 321-324; Zhang, F.C., Yin, Z.B., Tang, X.P., Min, X., Liu, J.X., Chen, Y.Q., Wang, J., Lei, C.L., Clinical analysis of 260 cases with severe acute respiratory syndrome in Guangzhou areas (2003) Zhonghua Chuanranbing Zazhi, 21, pp. 84-86; Peng, J., Hou, J.L., Guo, Y.B., Feng, X.R., Chen, J.J., Liu, D.L., Zhu, Y.F., Chen, Y.P., Clinical characteristics of the severe acute respiratory syndrome in Guangzhou (2003) Zhonghua Chuanranbing Zazhi, 21, pp. 89-92; Zhao, Z.W., Zhang, F.C., Xu, M., Huang, K., Zhong, W.N., Cai, W.P., Yin, Z.B., Wei, M., Clinical analysis of 190 cases outbreak with atypical pneumonia in Guangzhou in spring (2003) Zhonghua Yixue Zazhi, 83, pp. 713-718; Huo, N., Lu, H.Y., Xu, X.Y., Wang, G.F., Li, H.C., Wan, G.Q., Li, J.P., Zhuang, H., Clinical characteristics and outcome of 45 early stage patients with SARS (2003) Beijing Daxue Xuebao (Yixueban), 35 S, pp. 19-22; 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Chinese PLA Ctr. Diagn./Treatm., Tangdu Hospital, Fourth Military Medical University, Xi'an 710038, Shaanxi Province, China; email: nieqinghe@hotmail.com",,"WJG Press",10079327,,WJGAF,"12918094","English","World J. Gastroenterol.",Review,"Final",Open Access,Scopus,2-s2.0-0041426375
"Paul P.S., Halbur P., Janke B., Joo H., Nawagitgul P., Singh J., Sorden S.","7202714004;7005935318;7003826275;7101853740;6507783692;57197384506;7003697171;","Exogenous porcine viruses",2003,"Current Topics in Microbiology and Immunology","278",,,"125","183",,22,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042164566&partnerID=40&md5=0845bff24c1bfe5a7f9f22ed35ca4aef","Dept. of Vet. and Biomed. Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; College of Veterinary Medicine, University of Minnesota, Saint Paul, MN 55108, United States; Faculty of Veterinary Medicine, Kasetsart University, Kasetsart, Thailand","Paul, P.S., Dept. of Vet. and Biomed. Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; Halbur, P., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Janke, B., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Joo, H., College of Veterinary Medicine, University of Minnesota, Saint Paul, MN 55108, United States; Nawagitgul, P., Faculty of Veterinary Medicine, Kasetsart University, Kasetsart, Thailand; Singh, J., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States; Sorden, S., College of Veterinary Medicine, Iowa State University, Ames, IA 50011, United States","Porcine organs, cells and tissues provide a viable source of transplants in humans, though there is some concern of public health risk from adaptation of swine infectious agents in humans. Limited information is available on the public health risk of many exogenous swine viruses, and reliable and rapid diagnostic tests are available for only a few of these. The ability of several porcine viruses to cause transplacental fetal infection (parvoviruses, circoviruses, and arteriviruses), emergence or recognition of several new porcine viruses during the last two decades (porcine circovirus, arterivirus, paramyxoviruses, herpesviruses, and porcine respiratory coronavirus) and the immunosuppressed state of the transplant recipients increases the xenozoonoses risk of humans to porcine viruses through transplantation. Much of this risk can be eliminated with vigilance and sustained monitoring along with a better understanding of pathogenesis and development of better diagnostic tests. In this review we present information on selected exogenous viruses, highlighting their characteristics, pathogenesis of viral infections in swine, methods for their detection, and the potential xenozoonoses risk they present. Emphasis has been given in this review to swine influenza virus, paramyxovirus (Nipah virus, Menagle virus, LaPiedad paramyxovirus, porcine paramyxovirus), arterivirus (porcine reproductive and respiratory syndrome virus) and circovirus as either they represent new swine viruses or present the greatest risk. We have also presented information on porcine parvovirus, Japanese encephalitis virus, encephalomyocarditis virus, herpesviruses (pseudorabies virus, porcine lymphotropic herpesvirus, porcine cytomegalovirus), coronaviruses (TGEV, PRCV, HEV, PEDV) and adenovirus. The potential of swine viruses to infect humans needs to be assessed in vitro and in vivo and rapid and more reliable diagnostic methods need to be developed to assure safe supply of porcine tissues and cells for xenotransplantation.",,"Adenovirus; Arterivirus; Circoviridae; Coronavirus; Cytomegalovirus; diagnostic test; Encephalomyocarditis virus; eradication therapy; Herpes virus; immune deficiency; infection risk; Influenza virus; intrauterine infection; Japanese encephalitis virus; Menagle virus; Nipah virus; nonhuman; Orthomyxovirus; Paramyxovirus; Parvovirus; priority journal; Pseudorabies herpetovirus; recipient; reliability; review; risk assessment; swine disease; virus infection; virus pathogenesis; xenograft; xenotransplantation; zoonosis; Animals; Arterivirus Infections; Circoviridae Infections; Herpesviridae Infections; Humans; Orthomyxoviridae Infections; Respirovirus Infections; Swine; Swine Diseases; Transplantation, Heterologous; Virus Diseases; Zoonoses; Adenoviridae; Arterivirus; Circoviridae; Circovirus; Coronavirus; Cytomegalovirus; Encephalomyocarditis virus; Herpesviridae; Influenza virus; Japanese encephalitis virus; Nipah virus; Orthomyxoviridae; Paramyxoviridae; Parvovirus; Porcine circovirus; Porcine cytomegalovirus; Porcine parvovirus; Porcine reproductive and respiratory syndrome virus; Porcine respiratory coronavirus; Suid herpesvirus 1; Suidae; Sus scrofa; Swine influenza virus","Acland, H.M., Littlejohns, I.R., Encephalomyocarditis virus infection of pigs. 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Widen, B.F., Lowings, J.P., Belak, S., Banks, M., Development of a PCR system for porcine cytomegalovirus detection and determination of the putative partial sequence of its DNA polymerase gene (1999) Epidemiol Infect, 123, pp. 177-180; Wills, R.W., Zimmerman, J.J., Yoon, K.J., Swenson, S.L., McGinley, M.J., Hill, H.T., Platt, K.B., Nelson, E.A., Porcine reproductive and respiratory syndrome virus: A persistent infection (1997) Vet Microbiol, 55, pp. 231-240; Wong, S.C., Ooi, M.H., Wong, M.N.L., Tio, P.H., Solomon, T., Cardosa, M.J., Late presentation of Nipah virus encephalitis and kinetics of the humoral immune response (2001) J Neurol Neurosurg Psychiatry, 71, pp. 552-554; Yoon, I.J., Joo, H.S., Christianson, W.T., Kim, H.S., Collins, J.E., Morrison, R.B., Dial, G.D., An indirect fluorescent antibody test for the detection of antibody to swine infertility and respiratory syndrome virus in swine sera (1992) J Vet Diagn Invest, 4, pp. 144-147; Yoon, K.J., Wu, L.L., Zimmerman, J.J., Hill, H.T., Platt, K.B., Antibody-dependent enhancement (ADE) of porcine reproductive and respiratory syndrome virus (PRRSV) infection in pigs (1996) Viral Immunol, 9, pp. 51-63","Paul, P.S.; Dept. of Vet. and Biomed. Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; email: ppaul2@unl.edu",,,0070217X,,CTMIA,"12934944","English","Curr. Top. Microbiol. Immunol.",Review,"Final",,Scopus,2-s2.0-0042164566
"Wood L., Liu E.","57211581274;7202240109;","Questions about comparative genomics of SARS coronavirus isolates [3] (multiple letters)",2003,"Lancet","362","9383",,"578","579",,3,"10.1016/S0140-6736(03)14130-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041656382&doi=10.1016%2fS0140-6736%2803%2914130-X&partnerID=40&md5=96246265d94c57329ec808ba39014b1e","Hoover Institution, Stanford University, Stanford, CA 94305, United States; Genome Institute of Singapore, 1 Science Park Road 05-01, Singapore 117528, Singapore","Wood, L., Hoover Institution, Stanford University, Stanford, CA 94305, United States; Liu, E., Genome Institute of Singapore, 1 Science Park Road 05-01, Singapore 117528, Singapore",[No abstract available],,"RNA polymerase; comparative genomic hybridization; Coronavirus; epidemic; genetic drift; genetic similarity; health survey; letter; microsatellite instability; morphological trait; nonhuman; priority journal; respiratory tract infection; RNA gene; severe acute respiratory distress syndrome; single nucleotide polymorphism; viremia; virus isolation; virus load; virus mutation; virus pneumonia",,"Wood, L.; Hoover Institution, Stanford University, Stanford, CA 94305, United States; email: lowellwood@attbi.com",,"Elsevier Limited",01406736,,LANCA,"12932399","English","Lancet",Letter,"Final",Open Access,Scopus,2-s2.0-0041656382
"Mølbak K., Samuelsson S., Fomsgaard A.","55232729700;7005919452;7005971896;","Severe Acute Respiratory Syndrome (SARS) [Svær Akut Respiratorisk Syndrom - SARS]",2003,"Ugeskrift for Laeger","165","35",,"3311","3314",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141906388&partnerID=40&md5=933b6042959d92256ab47f9d2712cc6b","Epidemiologisk Afdeling, Statens Serum Institut, Artillerivej 5, DK-2300 København S, Denmark","Mølbak, K., Epidemiologisk Afdeling, Statens Serum Institut, Artillerivej 5, DK-2300 København S, Denmark; Samuelsson, S.; Fomsgaard, A.","Severe Acute Respiratory Syndrome (SARS) is an acute respiratory illness caused by SARS coronavirus. This virus was possibly transmitted from an animal reservoir to humans, and from February 2003, the epidemic was spread internationally by further person-to-person transmission. The SARS epidemic was managed by well-known principles of infection control, including prompt diagnosis, isolation of patients, and quarantine of contacts. The successful control of the outbreak is a remarkable international achievement, though much about SARS remains poorly understood.",,"Canada; disease transmission; electron microscopy; epidemic; Hong Kong; human; infection control; nonhuman; practice guideline; respiratory tract infection; reverse transcription polymerase chain reaction; review; SARS coronavirus; severe acute respiratory syndrome; Singapore; Viet Nam; virus detection; virus infection; virus transmission; world health organization; animal; article; disease carrier; epidemic; health; patient care; severe acute respiratory syndrome; Animals; Communicable Disease Control; Disease Outbreaks; Disease Reservoirs; Humans; Patient Isolation; Severe Acute Respiratory Syndrome; World Health","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Kuiken, T., Fouchier, R.A.M., Schutten, M., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel corona-virus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Dye, C., Gay, N., Modeling the SARS epidemic (2003) Science, 3000, pp. 1884-1885; Update: Outbreak of Severe Acute Respiratory Syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-248; Severe Acute Respiratory Syndrome - Singapore, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 405-411; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Rainer, T.H., Cameron, P.A., Smith, D., Evaluation of WHO criteria for identifying patients with severe acute respiratory syndrome out of hospital: Prospective observational study (2003) BMJ, 326, pp. 1354-1358; Seto, W.H., Tsang, D., Yung, R.W., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520","Mølbak, K.; Epidemiologisk Afdeling, Statens Serum Institut, Artillerivej 5, DK-2300 København S, Denmark",,,00415782,,UGLAA,"14531368","Danish","Ugeskr. Laeg.",Review,"Final",,Scopus,2-s2.0-0141906388
"Snijder E.J., Bredenbeek P.J., Dobbe J.C., Thiel V., Ziebuhr J., Poon L.L.M., Guan Y., Rozanov M., Spaan W.J.M., Gorbalenya A.E.","7006058325;6603901441;6602684547;35238592100;7003783935;7005441747;7202924055;7003761371;7007172944;7005626044;","Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage",2003,"Journal of Molecular Biology","331","5",,"991","1004",,694,"10.1016/S0022-2836(03)00865-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042164218&doi=10.1016%2fS0022-2836%2803%2900865-9&partnerID=40&md5=26c8c236a6b6617ca2c9ddabc79fa32b","Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands; Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Natl. Ctr. for Biotech. Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, United States","Snijder, E.J., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands; Bredenbeek, P.J., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands; Dobbe, J.C., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands; Thiel, V., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Poon, L.L.M., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., Dept. of Microbiology and Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Rozanov, M., Natl. Ctr. for Biotech. Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, United States; Spaan, W.J.M., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands; Gorbalenya, A.E., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Albinusdreef 2, 2300 RC Leiden, Netherlands","The genome organization and expression strategy of the newly identified severe acute respiratory syndrome coronavirus (SARS-CoV) were predicted using recently published genome sequences. Fourteen putative open reading frames were identified, 12 of which were predicted to be expressed from a nested set of eight subgenomic mRNAs. The synthesis of these mRNAs in SARS-CoV-infected cells was confirmed experimentally. The 4382- and 7073 amino acid residue SARS-CoV replicase polyproteins are predicted to be cleaved into 16 subunits by two viral proteinases (bringing the total number of SARS-CoV proteins to 28). A phylogenetic analysis of the replicase gene, using a distantly related torovirus as an outgroup, demonstrated that, despite a number of unique features, SARS-CoV is most closely related to group 2 coronaviruses. Distant homologs of cellular RNA processing enzymes were identified in group 2 coronaviruses, with four of them being conserved in SARS-CoV. These newly recognized viral enzymes place the mechanism of coronavirus RNA synthesis in a completely new perspective. Furthermore, together with previously described viral enzymes, they will be important targets for the design of antiviral strategies aimed at controlling the further spread of SARS-CoV. © 2003 Elsevier Ltd. All rights reserved.","Genome organization; Nidovirus; Replicase; RNA processing; Subgenomic mRNA synthesis","amino acid; messenger RNA; proteome; virus enzyme; article; controlled study; Coronavirus; gene sequence; genome analysis; nonhuman; nucleotide sequence; open reading frame; phylogeny; priority journal; protein expression; RNA processing; RNA synthesis; SARS coronavirus; sequence analysis; sequence homology; Torovirus; virus genome; Coronavirus; SARS coronavirus; Torovirus","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. 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"Thiel V., Karl N., Schelle B., Disterer P., Klagge I., Siddell S.G.","35238592100;7004162467;6602866326;6507497319;6507717840;7005260816;","Multigene RNA vector based on coronavirus transcription",2003,"Journal of Virology","77","18",,"9790","9798",,32,"10.1128/JVI.77.18.9790-9798.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141459024&doi=10.1128%2fJVI.77.18.9790-9798.2003&partnerID=40&md5=c0ef74b864bb882b670d525074d7c6cb","Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Dept. of Pathology and Microbiology, School of Medical Sciences, University of Bristol, Bristol, United Kingdom; Cantonal Hospital, St. Gallen Research Department, 9007 St. Gallen, Switzerland","Thiel, V., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany, Cantonal Hospital, St. Gallen Research Department, 9007 St. Gallen, Switzerland; Karl, N., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Schelle, B., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Disterer, P., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Klagge, I., Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany; Siddell, S.G., Dept. of Pathology and Microbiology, School of Medical Sciences, University of Bristol, Bristol, United Kingdom","Coronavirus genomes are the largest known autonomously replicating RNAs with a size of ca. 30 kb. They are of positive polarity and are translated to produce the viral proteins needed for the assembly of an active replicase-transcriptase complex. In addition to replicating the genomic RNA, a key feature of this complex is a unique transcription process that results in the synthesis of a nested set of six to eight subgenomic mRNAs. These subgenomic mRNAs are produced in constant but nonequimolar amounts and, in general, each is translated to produce a single protein. To take advantage of these features, we have developed a multigene expression vector based on human coronavirus 229E. We have constructed a prototype RNA vector containing the 5′ and 3′ ends of the human coronavirus genome, the entire human coronavirus replicase gene, and three reporter genes (i.e., the chloramphenicol acetyltransferase [CAT] gene, the firefly luciferase [LUC] gene, and the green fluorescent protein [GFP] gene). Each reporter gene is located downstream of a human coronavirus transcription-associated sequence, which is required for the synthesis of individual subgenomic mRNAs. The transfection of vector RNA and human coronavirus nucleocapsid protein mRNA into BHK-21 cells resulted in the expression of the CAT, LUC, and GFP reporter proteins. Sequence analysis confirmed the synthesis of coronavirus-specific mRNAs encoding CAT, LUC, and GFP. In addition, we have shown that human coronavirus-based vector RNA can be packaged into virus-like particles that, in turn, can be used to transduce immature and mature human dendritic cells. In summary, we describe a new class of eukaryotic, multigene expression vectors that are based on the human coronavirus 229E and have the ability to transduce human dendritic cells.",,"chloramphenicol acetyltransferase; green fluorescent protein; luciferase; virus RNA; article; Coronavirus; dendritic cell; expression vector; genetic transduction; human; human cell; multigene family; priority journal; reporter gene; virus transcription; Animals; Coronavirus; Cricetinae; Dendritic Cells; Genetic Vectors; Humans; Immunotherapy; Multigene Family; RNA, Viral; Transcription, Genetic; Transduction, Genetic; Transfection; Virus Assembly","Alonso, S., Izeta, A., Sola, I., Enjuanes, L., Transcription regulatory sequences and mRNA expression levels in the coronavirus transmissible gastroenteritis virus (2002) J. 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Virol., 76, pp. 11065-11078; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pplab (1999) J. Virol., 73, pp. 177-185; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Zitvogel, L., Mayordomo, J.I., Tjandrawan, T., DeLeo, A.B., Clarke, M.R., Lotze, M.T., Storkus, W.J., Therapy of murine tumors with tumor peptide-pulsed dendritic cells: Dependence on T cells, B7 costimulation, and T helper cell 1-associated cytokines (1996) J. Exp. Med., 183, pp. 87-97","Thiel, V.; Cantonal Hospital, St. Gallen Research Department, 9007 St. Gallen, Switzerland; email: volker.thiel@kssg.ch",,,0022538X,,JOVIA,"12941887","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141459024
"Thiel V., Ivanov K.A., Putics Á., Hertzig T., Schelle B., Bayer S., Weißbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E., Ziebuhr J.","35238592100;7202972316;6504659310;6506047745;6602866326;7005617717;6701793349;7006058325;7004984201;7102740671;7005626044;7003783935;","Mechanisms and enzymes involved in SARS coronavirus genome expression",2003,"Journal of General Virology","84","9",,"2305","2315",,402,"10.1099/vir.0.19424-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042377358&doi=10.1099%2fvir.0.19424-0&partnerID=40&md5=1e0295927c84244a78bb17cf2d1d4f0e","Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, Netherlands; Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt/Main, Germany; Research Department, Cantonal Hospital, St. Gallen, Switzerland","Thiel, V., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany, Research Department, Cantonal Hospital, St. Gallen, Switzerland; Ivanov, K.A., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Putics, Á., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Hertzig, T., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Schelle, B., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Bayer, S., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Weißbrich, B., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; Snijder, E.J., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, Netherlands; Rabenau, H., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt/Main, Germany; Doerr, H.W., Institute of Medical Virology, Johann Wolfgang Goethe University, Frankfurt/Main, Germany; Gorbalenya, A.E., Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, Netherlands; Ziebuhr, J., Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany","A novel coronavirus is the causative agent of the current epidemic of severe acute respiratory syndrome (SARS). Coronaviruses are exceptionally large RNA viruses and employ complex regulatory mechanisms to express their genomes. Here, we determined the sequence of SARS coronavirus (SARS-CoV), isolate Frankfurt 1, and characterized key RNA elements and protein functions involved in viral genome expression. Important regulatory mechanisms, such as the (discontinuous) synthesis of eight subgenomic mRNAs, ribosomal frameshiffing and post-translational proteolytic processing, were addressed. Activities of three SARS coronavirus enzymes, the helicase and two cysteine proteinases, which are known to be critically involved in replication, transcription and/or post-translational polyprotein processing, were characterized. The availability of recombinant forms of key replicative enzymes of SARS coronavirus should pave the way for high-throughput screening approaches to identify candidate inhibitors in compound libraries.",,"cysteine proteinase; helicase; messenger RNA; recombinant enzyme; virus enzyme; virus protein; controlled study; Coronavirus; enzyme activity; gene expression; gene sequence; messenger RNA synthesis; nonhuman; nucleotide sequence; priority journal; protein function; protein processing; regulatory mechanism; review; ribosomal frameshifting; RNA virus; SARS coronavirus; sequence analysis; virus genome; virus isolation; virus replication; virus transcription; Amino Acid Sequence; Catalytic Domain; Cysteine Endopeptidases; Frameshifting, Ribosomal; Gene Expression Regulation, Viral; Genome, Viral; Molecular Sequence Data; Nucleic Acid Conformation; Papain; Protein Biosynthesis; RNA Helicases; RNA, Messenger; SARS Virus; Sequence Alignment; Viral Proteins; Coronavirus; RNA viruses; SARS coronavirus","Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain (2002) EMBO J., 21, pp. 3213-3224; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Baker, S.C., Shieh, C.K., Soe, L.H., Chang, M.F., Vannier, D.M., Lai, M.M., Identification of a domain required for autoproteolytic cleavage of murine coronavirus gene A polyprotein (1989) J. 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Biol., 494, pp. 1-17; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis (1989) Nucleic Acids Res., 17, pp. 4847-4861; Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes (1989) Nucleic Acids Res., 17, pp. 4713-4730; Gorbalenya, A.E., Koonin, E.V., Lai, M.M., Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses (1991) FEBS Lett., 288, pp. 201-205; Hegyi, A., Ziebuhr, J., Conservation of substrate specificities among coronavirus main proteases (2002) J. Gen. 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Biol., 380, pp. 413-421; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , 56 other authors; Pasternak, A.O., van den Born, E., Spaan, W.J., Snijder, E.J., Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis (2001) EMBO J., 20, pp. 7220-7228; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772. , 14 other authors; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325. , 13 other authors; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , 32 other authors; Ruan, Y.J., Wei, C.L., Ee, A.L., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785. , 17 other authors; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. 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Virol., 82, pp. 1273-1281; van Dinten, L.C., van Tol, H., Gorbalenya, A.E., Snijder, E.J., The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis (2000) J. Virol., 74, pp. 5213-5223; van Vliet, A.L., Smits, S.L., Rottier, P.J., de Groot, R.J., Discontinuous and non-discontinuous subgenomic RNA transcription in a nidovirus (2002) EMBO J., 21, pp. 6571-6580; Walker, J.E., Saraste, M., Runswick, M.J., Gay, N.J., Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold (1982) EMBO J., 1, pp. 945-951; Yao, Z., Jones, D.H., Grose, C., Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction (1992) PCR Methods Appl., 1, pp. 205-207; Ziebuhr, J., Siddell, S.G., Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab (1999) J. Virol., 73, pp. 177-185; Ziebuhr, J., Herold, J., Siddell, S.G., Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity (1995) J. Virol., 69, pp. 4331-4338; Ziebuhr, J., Heusipp, G., Siddell, S.G., Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase (1997) J. Virol., 71, pp. 3992-3997; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Ziebuhr, J., Thiel, V., Gorbalenya, A.E., The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond (2001) J. Biol. Chem., 276, pp. 33220-33232","Ziebuhr, J.; Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany; email: j.ziebuhr@mail.uni-wuerzburg.de",,,00221317,,JGVIA,"12917450","English","J. Gen. Virol.",Review,"Final",Open Access,Scopus,2-s2.0-0042377358
"Li L.J., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J., Zhang Y., Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M., Yao J., Lu Q., Yao P., Bo X., Wo. J., Wang S., Hu S.","55540790300;55719831500;7405478487;12807848700;56113825700;57039481000;7404684724;10642404600;7601312081;57215040094;39762433000;55950727800;8408053100;23480635300;8850502100;26659612100;9248348300;23489549300;7102625493;7005391024;23500565900;56092645000;8938269000;","Severe acute respiratory syndrome-associated coronavirus genotype and its characterization",2003,"Chinese Medical Journal","116","9",,"1288","1292",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744228841&partnerID=40&md5=341d4d4dd6629e99d6f3dbd858194c0e","Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Infect. Dis. Key Lab. Hlth. Ministry, First Affiliated Hospital, Zhejiang University, Hangzhou 310003, China; Hangzhou Genomics Institute, J.D. Watson Genomics Science Inst., Zhejiang University, Hangzhou 310000, China; Beijing Institute of Radiation Med., Academy of Military Medical Science, Beijing 100850, China","Li, L.J., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Wang, Z., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Lu, Y., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Bao, Q., Hangzhou Genomics Institute, J.D. Watson Genomics Science Inst., Zhejiang University, Hangzhou 310000, China; Chen, S., Beijing Institute of Radiation Med., Academy of Military Medical Science, Beijing 100850, China; Wu, N., Infect. Dis. Key Lab. Hlth. Ministry, First Affiliated Hospital, Zhejiang University, Hangzhou 310003, China; Cheng, S., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Weng, J., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Zhang, Y., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Yan, J., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Mei, L., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Wang, X., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Zhu, H., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Yu, Y., Hangzhou Genomics Institute, J.D. Watson Genomics Science Inst., Zhejiang University, Hangzhou 310000, China; Zhang, M., Beijing Institute of Radiation Med., Academy of Military Medical Science, Beijing 100850, China; Li, M., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Yao, J., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Lu, Q., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Yao, P., Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; Bo, X.; Wo., J., Infect. Dis. Key Lab. Hlth. Ministry, First Affiliated Hospital, Zhejiang University, Hangzhou 310003, China; Wang, S., Beijing Institute of Radiation Med., Academy of Military Medical Science, Beijing 100850, China; Hu, S., Hangzhou Genomics Institute, J.D. Watson Genomics Science Inst., Zhejiang University, Hangzhou 310000, China","Objective. To study the severe acute respiratory syndrome (SARS)-associated coronavirus genotype and its characteristics. Methods. A SARS-associated coronavirus isolate, named ZJ01 was obtained from throat swab samples taken from a patient in Hangzhou, Zhejing province. The complete genome sequence of ZJ01 consisted of 29 715 bp (GenBank accession: AY297028, version: gi: 30910859). Seventeen SARS-associated coronavirus genome sequences in GenBank were compared to analyze the common sequence variations and the probability of co-occurrence of multiple polymorphisms or mutations. Phylogenetic analysis of those sequences was done. Results. By bioinformatics processing and analysis, the 5 loci nucleotides at ZJ01 genome were found being T, T, G, T and T, respectively. Compared with other SARS-associated coronavirus genomes in the GenBank database, an A/G mutation was detected besides the other 4 mutation loci (C: G: C: C/T: T: T: T) involved in this genetic signature. Therefore a new definition was put forward according to the 5 mutation loci. SARS-associated coronavirus strains would be grouped into two genotypes (C: G: A: C: C/T: T: G: T: T), and abbreviated as SARS coronavirus C genotype and T genotype. On the basis of this new definition, the ZJ01 isolate belongs to SARS-associated coronavirus T genotype, first discovered and reported in mainland China. Phylogenetic analysis of the spike protein gene fragments of these SARS-associated coronavirus strains showed that the GZ01 isolate was phylogenetically distinct from other isolates, and compared with groups F1 and F2 of the T genotype, the isolates of BJ01 and CUHK-W1 were more closely related to the GZ01 isolate. It was interesting to find that two (A/G and C/T) of the five mutation loci occurred in the spike protein gene, which caused changes of Asp to Gly and Thr to lle in the protein, respectively. Conclusion. Attention should be paid to whether these genotype and mutation patterns are related to the virus's biological activities, epidemic characteristics and host clinical symptoms.","Coronavirus; Genotype; Phylogeny; Polymorphism; Severe acute respiratory syndrome","adenine; aspartic acid; cytosine; glycine; guanine; nucleotide; threonine; thymine; adult; article; base pairing; bioinformatics; case report; China; clinical feature; Coronavirus; epidemic; GenBank; gene locus; gene mutation; gene sequence; genetic database; genetic polymorphism; genetic variability; genome analysis; genotype; human; mutational analysis; nonhuman; nucleotide sequence; phylogeny; SARS coronavirus; severe acute respiratory syndrome; strain difference; throat culture; virus isolation; virus pneumonia; Genotype; Humans; Middle Aged; Mutation; SARS Virus","Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Qin, K., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate RJ01) (2003) Chin. Science Bull., 48, pp. 941-948; Enserink, M., Vogel, G., Infectious diseases. Deferring competition, global net closes in on SARS (2003) Science, 300, pp. 224-225; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Zanella, A., Lavazza, A., Marchi, R., Avian infectious bronchitis: Characterization of new isolates from Italy (2003) Avian Dis., 47, pp. 180-185; Pei, J., Briles, W.E., Collisson, E.W., Memory T cells protect chicks from acute infectious bronchitis virus infection (2003) Virology, 306, pp. 376-384; Ladman, B.S., Pope, C.R., Ziegler, A.F., Protection of chickens after live and inactivated virus vaccination against challenge with nephropathogenic infectious bronchitis virus PA/Wolgemuth/98 (2002) Avian Dis., 46, pp. 938-944; Miguel, B., Pharr, G.T., Wang, C., The role of feline aminopeptidase N as a receptor for infectious bronchitis virus (2002) Arch. Virol., 147, pp. 2047-2056; Oliver, M.A., Marsh, J.A., In vivo thymulin treatments enhance avian lung natural killer cell cytotoxicity in response to infectious bronchitis virus (2003) Int. Immunopharmacol., 3, pp. 107-113; Pratelli, A., Martella, V., Decaro, N., Genetic diversity of a canine coronavirus detected in pups with diarrhoea in Italy (2003) J. Virol. Methods, 110, pp. 9-17; Hoet, A.E., Nielsen, P.R., Hasoksuz, M., Detection of bovine torovirus and other enteric pathogens in feces from diarrhea cases in cattle (2003) J. Vet. Diagn. Invest., 15, pp. 205-212; Chang, S.H., Bae, J.L., Kang, T.J., Identification of the epitope region capable of inducing neutralizing antibodies against the porcine epidemic diarrhea virus (2002) Mol. Cells, 14, pp. 295-299; Navas, S., Weiss, S.R., Murine coronavirus-induced hepatitis: JHM genetic background eliminates A59 spike-determined hepatotropism (2003) J. Virol., 77, pp. 4972-4978; Bonavia, A., Zelus, B.D., Wentworth, D.E., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Schikora, B.M., Shih, L.M., Hietala, S.K., Genetic diversity of avian infectious bronchitis virus California variants isolated between 1988 and 2001 based on the S1 subunit of the spike glycoprotein (2003) Arch. Virol., 148, pp. 115-136; Tsai, J.C., Zelus, B.D., Holmes, K.V., The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain (2003) J. Virol., 77, pp. 841-850; Wang, X., Schnitzlein, W.M., Tripathy, D.N., Construction and immunogenicity studies of recombinant fowl poxvirus containing the S1 gene of Massachusetts 41 strain of infectious bronchitis virus (2002) Avian Dis., 46, pp. 831-838; Ruan, Y.J., Wei, C.L., Ee, A.L., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Phillips, J.J., Chua, M.M., Lavi, E., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovinulence (1999) J. Virol., 73, pp. 7752-7760; Bergmann, C.C., Yao, Q., Lin, M., The JHM strain of mouse hepatitis virus induces a spike protein-specific Db-restricted cytotoxic T cell response (1996) J. Gen. Virol., 77, pp. 315-325; Gomez, N., Carrillo, C., Salinas, J., Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants (1998) Virology, 249, pp. 352-358; Jackwood, M.W., Hilt, D.A., Production and immunogenicity of' multiple antigenic peptide (MAP) constructs derived from the S1 glycoprotein of infectious bronchitis virus (IBV) (1995) Adv. Exp. Med. Biol., 308, pp. 213-219; Ndifuna, A., Waters, A.K., Zhou, M., Recombinant nucleocapsid protein is potentially an inexpensive, effective serodiagnostic reagent for IBV (1998) J. Virol. Methods, 70, pp. 37-44; Callenbaut, P., Enjuanes, L., Pensaert, M., An adenovirus recombinant expressing the spike glycoprotein of porcine respiratory coronavirus is immunogenic in swine (1998) J. Gen. Virol., 77, pp. 309-313","Wang, Z.; Zhejiang Prov. Ctr. Dis. Prevention, Hangzhou 310009, China; email: wzg188@sina.com.cn",,,03666999,,CMDJA,"14527350","English","Chin. Med. J.",Article,"Final",,Scopus,2-s2.0-10744228841
"Rest J.S., Mindell D.P.","7005900421;7003464307;","SARS associated coronavirus has a recombinant polymerase and coronaviruses have a history of host-shifting",2003,"Infection, Genetics and Evolution","3","3",,"219","225",,66,"10.1016/j.meegid.2003.08.001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141716995&doi=10.1016%2fj.meegid.2003.08.001&partnerID=40&md5=5f77546626929c03f6df037b60aedea5","Dept. of Ecology/Evolutionary Biol., Museum of Zoology, University of Michigan, 1109 Geddes Avenue, Ann Arbor, MI 48109-1079, United States","Rest, J.S., Dept. of Ecology/Evolutionary Biol., Museum of Zoology, University of Michigan, 1109 Geddes Avenue, Ann Arbor, MI 48109-1079, United States; Mindell, D.P., Dept. of Ecology/Evolutionary Biol., Museum of Zoology, University of Michigan, 1109 Geddes Avenue, Ann Arbor, MI 48109-1079, United States","The sudden appearance and potential lethality of severe acute respiratory syndrome associated coronavirus (SARS-CoV) in humans has focused attention on understanding its origins. Here, we assess phylogenetic relationships for the SARS-CoV lineage as well as the history of host-species shifts for SARS-CoV and other coronaviruses. We used a Bayesian phylogenetic inference approach with sliding window analyses of three SARS-CoV proteins: RNA dependent RNA polymerase (RDRP), nucleocapsid (N) and spike (S). Conservation of RDRP allowed us to use a set of Arteriviridae taxa to root the Coronaviridae phylogeny. We found strong evidence for a recombination breakpoint within SARS-CoV RDRP, based on different, well supported trees for a 5′ fragment (supporting SARS-CoV as sister to a clade including all other coronaviruses) and a 3′ fragment (supporting SARS-CoV as sister to group three avian coronaviruses). These different topologies are statistically significant: the optimal 5′ tree could be rejected \ for the 3′ region, and the optimal 3′ tree could be rejected for the 5′ region. We did not find statistical evidence for recombination in analyses of N and S, as there is little signal to differentiate among alternative trees. Comparison of phylogenetic trees for 11 known host-species and 36 coronaviruses, representing coronavirus groups 1-3 and SARS-CoV, based on N showed statistical incongruence indicating multiple host-species shifts for coronaviruses. Inference of host-species associations is highly sensitive to sampling and must be considered cautiously. However, current sampling suggests host-species shifts between mouse and rat, chicken and turkey, mammals and manx shearwater, and humans and other mammals. The sister relationship between avian coronaviruses and the 3′ RDRP fragment of SARS-CoV suggests an additional host-species shift. Demonstration of recombination in the SARS-CoV lineage indicates its potential for rapid unpredictable change, a potentially important challenge for public health management and for drug and vaccine development. © 2003 Elsevier B.V. All rights reserved.","Coronavirus; Host-shift; Phylogeny; Recombination; RNA-dependent RNA polymerase; SARS-CoV Nidovirales; Severe acute respiratory syndrome","nucleocapsid protein; RNA directed RNA polymerase; virus protein; 3' untranslated region; 5' untranslated region; Arterivirus; article; Bayes theorem; chicken; cladistics; controlled study; Coronavirus; genetic recombination; host; mammal; mouse; nonhuman; phylogeny; priority journal; protein analysis; rat; SARS coronavirus; turkey (bird); virus nucleocapsid; Animals; Bayes Theorem; Coronavirus; Host-Parasite Relations; Humans; Membrane Glycoproteins; Nucleocapsid; Phylogeny; Recombination, Genetic; RNA Replicase; SARS Virus; Viral Envelope Proteins; Arteriviridae; Aves; Coronaviridae; Coronavirus; Gallus gallus; Mammalia; Nidovirales; Puffinus auricularis; Puffinus puffinus","Bateman, A., Birney, E., Cerruti, L., Durbin, R., Etwiller, L., Eddy, S.R., Griffiths-Jones, S., Sonnhammer, E.L., The Pfam protein families database (2002) Nucleic Acids Res., 30, pp. 276-280; de Haan, C.A., Volders, H., Koetzner, C.A., Masters, P.S., Rottier, P.J., Coronaviruses maintain viability despite dramatic rearrangements of the strictly conserved genome organization (2002) J. Virol., 76, pp. 12491-12502; Decimo, D., Philippe, H., Hadchouel, M., Tardieu, M., Meunier-Rotival, M., The gene encoding the nucleocapsid protein: Sequence analysis in murine hepatitis virus type 3 and evolution in Coronaviridae (1993) Arch. Virol., 130, pp. 279-288; Desdevises, Y., Morand, S., Jousson, O., Legendre, P., Coevolution between Lamellodiscus (Monogenea: Diplectanidae) and Sparidae (Teleostei): The study of a complex host-parasite system (2002) Evolution, 56, pp. 2459-2471; Dimmic, M.W., Rest, J.S., Mindell, D.P., Goldstein, R.A., rtREV: An amino acid substitution matrix for inference of retrovirus and reverse transcriptase phylogeny (2002) J. Mol. E, 55, pp. 65-73; Eddy, S.R., Profile hidden Markov models (1998) Bioinformatics, 14, pp. 755-763; Huelsenbeck, J.P., Ronquist, F., MRBAYES: Bayesian inference of phylogenetic trees (2001) Bioinformatics, 17, pp. 754-755; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J. Gen. Virol., 79, pp. 715-718; Keeling, P.J., Palmer, J.D., Lateral transfer at the gene and subgenic levels in the evolution of eukaryotic enolase (2001) Proc. Natl. Acad. Sci. U.S.A., 98, pp. 10745-10750; Kirkwood, J.K., Cunningham, A.A., Hawkey, C., Howlett, J., Perrins, C.M., Hematology of fledgling Manx shearwaters (Puffinus puffinus) with and without 'puffinosis' (1995) J. Wildl. Dis., 31, pp. 96-98; Lai, M.M., Coronavirus: Organization, replication and expression of genome (1990) Annu. Rev. Microbiol., 44, pp. 303-333; Lai, M.M.C., Recombination in large RNA viruses: Coronaviruses (1996) Semin. Virol., 7, pp. 381-388; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Mau, B., Newton, M.A., Larget, B., Bayesian phylogenetic inference via Markov chain Monte Carlo methods (1999) Biometrics, 55, pp. 1-12; Morris, A., Marsden, M., Halcrow, K., Hughes, E.S., Brettle, R.P., Bell, J.E., Simmonds, P., Mosaic structure of the human immunodeficiency virus type 1 genome infecting lymphoid cells and the brain: Evidence for frequent in vivo recombination events in the evolution of regional populations (1999) J. Virol., 73, pp. 8720-8731; Murphy, W.J., Eizirik, E., O'Brien, S.J., Madsen, O., Scally, M., Douady, C.J., Teeling, E., Springer, M.S., Resolution of the early placental mammal radiation using Bayesian phylogenetics (2001) Science, 294, pp. 2348-2351; Rest, J.S., Mindell, D.P., Retroids in archaea: Phylogeny and lateral origins (2003) Mol. Biol. E, 20, pp. 1134-1142; Ronquist, F., TreeFitter (2000), http://www.ebc.uu.se/systzoo/research/treefitter/treefitter.html, Ver. 1.0. Software avialable via Uppsala University, Uppsala, Sweden; Ronquist, F., Liljeblad, J., Evolution of the gall wasp-host plant association (2001) Evolution, 55, pp. 2503-2522; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Salminen, M.O., Carr, J.K., Burke, D.S., McCutchan, F.E., Identification of breakpoints in intergenotypic recombinants of HIV type 1 by bootscanning (1995) AIDS Res. Hum. Retroviruses, 11, pp. 1423-1425; Shimodaira, H., An approximately unbiased test of phylogenetic tree selection (2002) Syst. Biol., 51, pp. 492-508; Shimodaira, H., Hasegawa, M., CONSEL: For assessing the confidence of phylogenetic tree selection (2001) Bioinformatics, 17, pp. 1246-1247; Siddell, S.G., The Coronaviridae: An introduction (1995) The Coronaviridae: an Introduction, pp. 1-10. , Siddell, S.G. (Ed.), Plenum Press, New York, NY; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-112; Wang, L., Junker, D., Collisson, E.W., Evidence of natural recombination with the S1 gene of infectious-bronchitis virus (1993) Virology, 192, pp. 710-716; Yang, Z.H., PAML: A program package for phylogenetic analysis by maximum likelihood (1997) Comput. Appl. Biosci., 13, pp. 555-556; Yang, Z.H., Rannala, B., Bayesian phylogenetic inference using DNA sequences: A Markov Chain Monte Carlo method (1997) Mol. Biol. E, 14, pp. 717-724","Mindell, D.P.; Dept. of Ecology/Evolutionary Biol., Museum of Zoology, University of Michigan, 1109 Geddes Avenue, Ann Arbor, MI 48109-1079, United States; email: mindell@umich.edu",,,15671348,,IGENC,"14522185","English","Infec. Genet. Evol.",Article,"Final",Open Access,Scopus,2-s2.0-0141716995
"Duan S.-M., Zhao X.-S., Wen R.-F., Huang J.-J., Pi G.-H., Zhang S.-X., Han J., Bi S.-L., Ruan L., Dong X.-P.","57215374665;57199993418;7005522832;57199288119;6602438655;56099098200;9237586300;7101633642;7006832508;24605193200;","Stability of SARS Coronavirus in Human Specimens and Environment and Its Sensitivity to Heating and UV Irradiation",2003,"Biomedical and Environmental Sciences","16","3",,"246","255",,49,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242361262&partnerID=40&md5=296cf621b2376cffaa45814fc7fcc89f","Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China","Duan, S.-M., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Zhao, X.-S., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Wen, R.-F., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Huang, J.-J., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Pi, G.-H., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Zhang, S.-X., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Han, J., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Bi, S.-L., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Ruan, L., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; Dong, X.-P., Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China","Objective: The causal agent for SARS is considered as a novel coronavirus that has never been described both in human and animals previously. The stability of SARS coronavirus in human specimens and in environments was studied. Methods: Using a SARS coronavirus strain CoV-P9, which was isolated from pharyngeal swab of a probable SARS case in Beijing, its stability in mimic human specimens and in mimic environment including surfaces of commonly used materials or in household conditions, as well as its resistances to temperature and UV irradiation were analyzed. A total of 106 TCID50 viruses were placed in each tested condition, and changes of the viral infectivity in samples after treatments were measured by evaluating cytopathic effect (CPE) in cell line Vero-E6 at 48 h after infectionn. Results: The results showed that SARS coronavirus in the testing condition could survive in serum, 1:20 diluted sputum and feces for at least 96 h, whereas it could remain alive in urine for at least 72 h with a low level of infectivity. The survival abilities on the surfaces of eight different materials and in water were quite comparable, revealing reduction of infectivity after 72 to 96 h exposure. Viruses stayed stable at 4°C, at room temperature (20°C) and at 37°C for at least 2 h without remarkable change in the infectious ability in cells, but were converted to be non-infectious after 90-, 60- and 30-min exposure at 56°C, at 67°C and at 75°C, respectively. Irradiation of UV for 60 min on the virus in culture medium resulted in the destruction of viral infectivity at an undetectable level. Conclusion: The survival ability of SARS coronavirus in human specimens and in environments seems to be relatively strong. Heating and UV irradiation can efficiently eliminate the viral infectivity.","Coronavirus; Environment; Severe acute respiratory syndrome; Specimen; Stability","article; China; controlled study; Coronavirus; evaluation; heating; human; human cell; nonhuman; SARS coronavirus; severe acute respiratory syndrome; sputum examination; temperature; throat culture; ultraviolet irradiation; virus isolation; virus pneumonia; virus strain; virus survival; Environment; Heat; Humans; Pharynx; SARS Virus; Survival Analysis; Ultraviolet Rays; Animalia; Coronavirus; SARS coronavirus","Cumulative Numbers of Reported Probable Cases of SARS, , http://www.who.int/csr/sars/country/2003_05_31/en; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Group, S.S., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Barthold, S.W., De Souza, M.S., Smith, A.L., Susceptibility of laboratory mice to intranasal and contact infection with coronaviruses of other species (1990) Lab. Anim. Sci., 40, pp. 481-485; Kiss, I., Ros, C., Kecskemeti, S., Tanyi, J., Klingeborn, S.B., Belak, S., Observations on the quasispecies composition of three animal pathogenic RNA viruses (1999) Acta Vet Hung, 47, pp. 471-480; Tyrrell, D.A.J., Rhinoviruses and coronaviruses - Virological aspects of their role in causing colds in human (1983) Eur. J. Respir. Dis., 128, p. 232; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Seto, W.H., Tsang, D., Yung, R.W., Ching, T.Y., Ng, T.K., Ho, M., Ho, L.M., Peiris, J.S., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Cyranoski, D., Abbott, A., Apartment complex holds clues to pandemic potential of SARS (2003) Nature, 423, pp. 3-4; Duan, S.M., Zhao, X.S., Wen, R.F., Li, D.X., Hong, T., Bi, S.L., Wang, J.W., Ruan, L., Isolations and preliminary identifications of SARS coronaviruses from various specimens of SARS patients (2003) Chinese J. Virol., 19, pp. 96-98. , In Chinese","Dong, X.-P.; Inst. Viral Dis. Contr. and Prev., Chinese Ctr. Dis. Contr. and Prev., Ying-Xin Rd. 100, Beijing 100052, China; email: dongxp@public.fhnet.cn.net",,,08953988,,,"14631830","English","Biomed. Environ. Sci.",Article,"Final",,Scopus,2-s2.0-0242361262
"Taguchi F., Qing L., Shimizu M.","7103209890;7006166225;22945496700;","Antiviral activity of povidone-iodine products against murine coronavirus",2003,"Japanese Journal of Chemotherapy","51","9",,"583","585",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141927427&partnerID=40&md5=b2536d81f68080e37df1895783df811a","National Institute of Neuroscience, Natl. Center of Neurology/Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo, Japan; Pharmaceutical Research Center, Meiji Seika Kaisha Ltd., Japan; Natl. Inst. of Infectious Diseases, 4-7 Gakuen, Musashi-Murayama, Tokyo, Japan","Taguchi, F., National Institute of Neuroscience, Natl. Center of Neurology/Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo, Japan, Natl. Inst. of Infectious Diseases, 4-7 Gakuen, Musashi-Murayama, Tokyo, Japan; Qing, L., National Institute of Neuroscience, Natl. Center of Neurology/Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo, Japan, Natl. Inst. of Infectious Diseases, 4-7 Gakuen, Musashi-Murayama, Tokyo, Japan; Shimizu, M., Pharmaceutical Research Center, Meiji Seika Kaisha Ltd., Japan","We studied the in vitro antiviral activity of commercially available povidone-iodine (PVP-I) products against murine hepatitis virus (MHV) A-59 strain, a murine coronavirus. All commercial products, i.e., PVP-I solution, PVP-I garle, PVP-I scrub, PVP-I palm, and PVP-I throat spray, decreased viral infectivity titer beyond 4 logs within 5 seconds at concentrations of 0.1% to 5% of PVP-I. These results demonstrate the strong antiviral activity fo PVP-I products against murine coronavirus.",,"povidone iodine; aerosol; antiviral activity; article; concentration response; controlled study; Coronavirus; gargle; in vitro study; Murine hepatitis coronavirus; nonhuman; virus infectivity; virus strain","(2003), 77, pp. 303-309. , Japanese source; http://idsc.nih.go.jp/others/urgentdesinfect04a.html, Japanese source; (1999), 14, pp. 142-147. , Japanese source; Shimizu, M., Okuzumi, K., Yoneyama, A., In vitro antiseptic susceptibility of clinical isolates from nosocomial infections (2002) Dermatology, 204 (SUPPL. 1), pp. 21-27; (1998), 26, pp. 371-386. , Japanese source; Saknimit, M., Inatsuku, I., Sugiyama, Y., Virucidal efficacy of physio-chemical treatments against coronavirus and parvovirus of laboratory animals (1988) Exp. Anim., 37, pp. 341-345; Kumanishi, T., Brain tumors induced with Rous sarcoma virus, Schmidt-Ruppin strain. 1. Induction of brain tumors in adult mice with Rous chicken sarcoma cells (1967) Jpn. J. Exp. Med., 37, pp. 461-474; Taguchi, F., Matsuyama, S., Soluble receptor potentiates receptor-independent infection by murine coronavirus (2002) J. Virol., 76, pp. 950-958; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , May 30; (5624); Hsu, Y.C., Nomura, S., Krusse, C.W., Some bactericidal and virucidal properties of iodine not affecting infectious RNA and DNA (1965) Am. J. Epidemiol., 82, pp. 317-328","Taguchi, F.; National Institute of Neuroscience, Natl. Center of Neurology/Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo, Japan",,,13407007,,NKRZE,,"Japanese; English","Jpn. J. Chemother.",Article,"Final",,Scopus,2-s2.0-0141927427
"Knudsen T.B., Kledal T.N., Andersen O., Eugen-Olsen J., Kristiansen T.B.","35478677300;6603019879;35499773400;7004032906;7006008013;","Severe acute respiratory syndrome - A new coronavirus from the Chinese dragon's lair",2003,"Scandinavian Journal of Immunology","58","3",,"277","284",,10,"10.1046/j.1365-3083.2003.01302.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041410010&doi=10.1046%2fj.1365-3083.2003.01302.x&partnerID=40&md5=64e1e352324122e2bd50f8485eb4a920","Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark; Clinical Research Unit, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark; Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Kettegaards allé 30, Copenhagen 1650, Denmark","Knudsen, T.B., Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark, Clinical Research Unit, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark, Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Kettegaards allé 30, Copenhagen 1650, Denmark; Kledal, T.N., Clinical Research Unit, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark; Andersen, O., Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark; Eugen-Olsen, J., Clinical Research Unit, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark; Kristiansen, T.B., Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark, Clinical Research Unit, Copenhagen Univ. Hospitals Hvidovre, Copenhagen, Denmark","The recent identification of a novel clinical entity, the severe acute respiratory syndrome (SARS), the rapid subsequent spread and case fatality rates of 14-15% have prompted a massive international collaborative investigation facilitated by a network of laboratories established by the World Health Organization (WHO). As SARS has the potential of becoming the first pandemic of the new millennium, a global warning by the WHO was issued on 12 March 2003. The disease, which is believed to have its origin in the Chinese Guangdong province, spread from Hong Kong via international airports to its current worldwide distribution. The concerted efforts of a globally united scientific community have led to the independent isolation and identification of a novel coronavirus from SARS patients by several groups. The extraordinarily rapid isolation of a causative agent of this newly emerged infectious disease constitutes an unprecedented scientific achievement. The main scope of the article is to provide the clinician with an overview of the natural history, epidemiology and clinical characteristics of SARS. On the basis of the recently published viral genome and structural features common to the members of the coronavirus family, a model for host cell-virus interaction and possible targets for antiviral drugs are presented. The epidemiological consequences of introducing a novel pathogen in a previously unexposed population and the origin and evolution of a new and more pathogenic strain of coronavirus are discussed.",,"antivirus agent; ribavirin; adult respiratory distress syndrome; anamnesis; Chinese; clinical feature; Coronavirus; diarrhea; epidemic; fever; human; pathogenesis; physician; population; priority journal; publication; review; severe acute respiratory syndrome; virus pneumonia; virus strain; China; Disease Outbreaks; Humans; SARS Virus; Severe Acute Respiratory Syndrome; Travel; World Health Organization","Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet (Online), , May 7; Situation Updates - Severe Acute Respiratory Syndrome (SARS) Update 52, , http://www.who.int; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto Area (2003) JAMA, 289, pp. 2801-2809; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Prospective Study of the Clinical Progression and Viral Load of SARS Associated Coronavirus Pneumonia in a Community Outbreak, , http://www.who.int; Situation Updates - Severe Acute Respiratory Syndrome (SARS) Update 49, , http://www.who.int; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Finkelstein, S., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Situation Updates - Severe Acute Respiratory Syndrome (SARS) Update 64, , http://www.who.int; Situation Updates - Severe Acute Respiratory Syndrome (SARS) Update 47, , http://www.who.int; Epler, G.R., Bronchiolitis obliterans organizing pneumonia (2001) Arch Intern Med, 161, pp. 158-216; Nicolaou, S., Al-Nakshabandi, N.A., Müller, N.L., SARS: Imaging of Severe Acute Respiratory Syndrome (2003) Am J Roentgenol, 180, pp. 1247-1249; http://www.afip.org/departments/Pulmonary/SARS/pathogen1b.html; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361. , epub ahead of print; Fields, B.N., Knipe, D.M., Howley, P.M., (1990) Fields Virology, 2nd Edn., pp. 841-861. , Raven Press; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Delmas, B., Gelfi, J., L'Haridon, R., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Pasqualini, R., Koivunen, E., Kain, R., Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis (2000) Cancer Res, 60, pp. 722-727; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3Clpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Saif, L.J., Wesley, R., Transmissible gastroenteritis virus (1999) Diseases of Swine, 8th Edn., pp. 295-325. , Straw BE, Allaire S, Mengeling WL, Taylor DJ, eds. Ames, Iowa: Iowa State University Press; Macnaughton, M.R., Hasony, H.J., Madge, M.H., Reed, S.E., Antibody to virus components in volunteers experimentally infected with human coronavirus 229E group viruses (1981) Infect Immun, 31, pp. 845-849; Reed, S.E., The behaviour of recent isolates of human respiratory coronavirus in vitro and in volunteers: Evidence of heterogeneity among 229E-related strains (1984) J Med Virol, 13, pp. 179-192; Cavallaro, J.J., Monto, A.S., Community-wide outbreak of infection with a 229E-like coronavirus in Tecumseh, Michigan (1970) J Infect Dis, 122, pp. 272-279; Falsey, A.R., Walsh, E.E., Hayden, F.G., Rhinovirus and coronavirus infection-associated hospitalization among older adults (2002) J Infect Dis, 185, pp. 1338-1341; Riski, H., Hovi, T., Coronavirus infections of man associated with diseases other than the common cold (1980) J Med Virol, 6, pp. 259-265; El-Sahly, H.M., Atmar, R.L., Glezen, W.P., Greenberg, S.B., Spectrum of clinical illness in hospitalized patients with 'common cold' virus infections (2000) Clin Infect Dis, 31, pp. 96-100; McIntosh, K., Chao Krause, R.K., Wasil, H.E., Mocega, R., Mufson, H.E., Coronavirus infection in acute lower respiratory tract disease in infant (1974) J Infect Dis, 130, pp. 502-507; Hon, L.E., Leung Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Chadda, K., Annane, D.K., The use of corticosteroids in severe sepsis and acute respiratory distress syndrome (2002) Ann Med, 34, pp. 582-589; Meduri, G.U., Tolley, E.A., Chrousos, G.P., Stentz, F., Prolonged methylprednisolone treatment suppresses systemic inflammation in patients with unresolving acute respiratory distress syndrome: Evidence for inadequate endogenous glucocorticoid secretion and inflammation-induced immune cell resistance to glucocorticoids (2002) Am J Respir Crit Care Med, 165, pp. 983-991","Knudsen, T.B.; Department of Infectious Diseases, Copenhagen Univ. Hospitals Hvidovre, Kettegaards allé 30, Copenhagen 1650, Denmark; email: linda.troels@get2net.dk",,,03009475,,SJIMA,"12950672","English","Scand. J. Immunol.",Review,"Final",Open Access,Scopus,2-s2.0-0041410010
"Chan P.K.S., Tam J.S., Lam C.-W., Chan E., Wu A., Li C.-K., Buckley T.A., Ng K.-C., Joynt G.M., Cheng F.W.T., To K.-F., Lee N., Hui D.S.C., Cheung J.L.K., Chu I., Liu E., Chung S.S.C., Sung J.J.Y.","32067487100;24788939600;34570692600;56413975200;7402998681;15122650100;7101745369;7403178624;7005588815;7202811097;7101911940;55503117200;7101862411;7202072287;37001476000;36920139800;7404293373;35405352400;","Human metapneumovirus detection in patients with severe acute respiratory syndrome",2003,"Emerging Infectious Diseases","9","9",,"1058","1063",,100,"10.3201/eid0909.030304","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042818007&doi=10.3201%2feid0909.030304&partnerID=40&md5=095fc992d28048cd3e05a6accd0a82c3","Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, New Territories, Hong Kong","Chan, P.K.S., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong, Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, New Territories, Hong Kong; Tam, J.S., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Lam, C.-W., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chan, E., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Wu, A., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Li, C.-K., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Buckley, T.A., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Ng, K.-C., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Joynt, G.M., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Cheng, F.W.T., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; To, K.-F., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Lee, N., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Hui, D.S.C., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Cheung, J.L.K., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chu, I., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Liu, E., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chung, S.S.C., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Sung, J.J.Y., Faculty of Medicine, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong","We used a combination approach of conventional virus isolation and molecular techniques to detect human metapneumovirus (HMPV) in patients with severe acute respiratory syndrome (SARS). Of the 48 study patients, 25 (52.1%) were infected with HMPV; 6 of these 25 patients were also infected with coronavirus, and another 5 patients (10.4%) were infected with coronavirus alone. Using this combination approach, we found that human laryngeal carcinoma (HEp-2) cells were superior to rhesus monkey kidney (LLC-MK2) cells commonly used in previous studies for isolation of HMPV. These widely available HEp-2 cells should be included in conjunction with a molecular method for cell culture followup to detect HMPV, particularly in patients with SARS.",,"adult; aged; antibody detection; article; cancer cell culture; clinical article; controlled study; Coronavirus; electron microscopy; epidemiological data; female; follow up; HEp 2 cell; human; human cell; human tissue; larynx carcinoma; male; Metapneumovirus; molecular genetics; pneumonia; reproducibility; reverse transcription polymerase chain reaction; sequence analysis; severe acute respiratory syndrome; virus detection; virus isolation","Van den Hoogen, B.G., De Jong, J.C., Groen, J., Kuiken, T., De Groot, R., Fouchier, R.A., A newly discovered human pneumovirus isolated from young children with respiratory tract disease (2001) Nat Med, 7, pp. 719-724; Jartti, T., Van den Hoogen, B., Garofalo, R.P., Osterhaus, A.D., Ruuskanen, O., Metapneumovirus and acute wheezing in children (2002) Lancet, 360, pp. 1393-1394; Nissen, M.D., Mackay, I.M., Withers, S.J., Siebert, D.J., Sloots, T.P., Evidence of human metapneumovirus in Australian children (2002) Med J Aust, 176, p. 188; Freymuth, F., Vabret, A., Legrand, L., Eterradossi, N., Lafay-Delaire, F., Brouard, J., Presence of the new human metapneumovirus in French children with bronchiolitis (2003) Pediatr Infect Dis J, 22, pp. 92-94; Stockton, J., Stephenson, I., Fleming, D., Zambon, M., Human metapneumovirus as a cause of community-acquired respiratory illness (2002) Emerg Infect Dis, 8, pp. 897-901; Peret, T.C., Boivin, G., Li, Y., Couillard, M., Humphrey, C., Osterhaus, A.D., Characterization of human metapneumoviruses isolated from patients in North America (2002) J Infect Dis, 185, pp. 1660-1663; Boivin, G., Abed, Y., Pelletier, G., Ruel, L., Moisan, D., Cote, S., Virological features and clinical manifestations associated with human metapneumovirus: A new paramyxovirus responsible for acute respiratory-tract infections in all age groups (2002) J Infect Dis, 186, pp. 1330-1334; Osterhaus, A., Fouchier, R., Human metapneumovirus in the community (2003) Lancet, 361, pp. 890-891; Falsey, A.R., Erdman, D., Anderson, L.J., Walsh, E.E., Human metapneumovirus infections in young and elderly adults (2003) J Infect Dis, 187, pp. 785-790; Greensill, J., McNamara, P.S., Dove, W., Flanagan, B., Smyth, R.L., Hart, C.A., Human metapneumovirus in severe respiratory syncytial virus bronchiolitis (2003) Emerg Infect Dis, 9, pp. 372-375; Van den Hoogen, B.G., Bestebroer, T.M., Osterhaus, A.D., Fouchier, R.A., Analysis of the genomic sequence of a human metapneumovirus (2002) Virology, 295, pp. 119-132; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; PCR Primers for SARS Developed by WHO Network Laboratories, , http://www.who.int/csr/sars/primers/en/; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2003; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1947-1958","Chan, P.K.S.; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, New Territories, Hong Kong; email: paulkschan@cuhk.edu.hk",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14519240","English","Emerg. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0042818007
"Hsueh P.-R., Hsiao C.-H., Yeh S.-H., Wang W.-K., Chen P.-J., Wang J.-T., Chang S.-C., Kao C.-L., Yang P.-C., Chen D.-S., Lee Y.-T., Teng C.-M., Ho H.-N., Chang M.-F.","7103390478;7202806734;7402085693;10938812100;7408354514;7701320048;57201855866;7403683230;7403932080;36066251200;19735178500;35549844300;7401465336;7404504288;","Microbiologic characteristics, serologic responses, and clinical manifestations in severe acute respiratory syndrome, Taiwan",2003,"Emerging Infectious Diseases","9","9",,"1163","1167",,52,"10.3201/eid0909.030367","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84983719141&doi=10.3201%2feid0909.030367&partnerID=40&md5=faa7f1a4a695b353807878b8abd43b7d","National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; National Health Research Institute, Taipei, Taiwan; Natl. Taiwan Univ. Coll. of Medicine, No 7 Chung-Shan South Road, Taipei, Taiwan","Hsueh, P.-R., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Hsiao, C.-H., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Yeh, S.-H., National Health Research Institute, Taipei, Taiwan; Wang, W.-K., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Chen, P.-J., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Wang, J.-T., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Chang, S.-C., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan; Kao, C.-L., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan, Natl. Taiwan Univ. Coll. of Medicine, No 7 Chung-Shan South Road, Taipei, Taiwan; Yang, P.-C., National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, Taipei, Taiwan, Natl. Taiwan Univ. Coll. of Medicine, No 7 Chung-Shan South Road, Taipei, Taiwan; Chen, D.-S.; Lee, Y.-T.; Teng, C.-M.; Ho, H.-N.; Chang, M.-F.","The genome of one Taiwanese severe acute respiratory syndrome-associated coronavirus (SARS-CoV) strain (TW1) was 29,729 nt in length. Viral RNA may persist for some time in patients who seroconvert, and some patients may lack an antibody response (immunoglobulin G) to SARS-CoV >21 days after illness onset. An upsurge of antibody response was associated with the aggravation of respiratory failure.",,"corticosteroid; immunoglobulin; immunoglobulin G; methylprednisolone; nucleic acid; ribavirin; virus RNA; adult; adult respiratory distress syndrome; antibiotic therapy; antibody response; antibody titer; article; artificial ventilation; clinical article; complement fixation test; Coronavirus; cytopathogenic effect; diarrhea; enzyme linked immunosorbent assay; erythrophagocytosis; female; fever; human; malaise; male; myalgia; nucleotide sequence; pancytopenia; respiratory failure; reverse transcription polymerase chain reaction; rigor; SARS coronavirus; seroconversion; severe acute respiratory syndrome; syndrome delineation; Taiwan; Vero cell; virus genome; virus pneumonia; virus strain","Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Chan, P.K.S., Chu, W.C.W., Kwan, Y.W., Clinical presentations and outcome of severe respiratory distress syndrome in children (2003) Lancet, , http//image.thelancet.com/extras/031et4127web, April 29; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; (2003) World Health Organization: Case Definition for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en, Geneva: 1 May; Updated Interim U.S. Surveillance Case Definition for Severe Acute Respiratory Syndrome (SARS)-United States, , http://www.cdc.gov/od/oc/media/pressrel/r030430.htm; Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.im/csr/sarscountry/2003_05_16/en; (2003) SARS Coronavirus Sequencing, , http://www.cdc.gov.ncidod/sars/sequence.htm; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, , http://image/thelancet.com/extras/03art4432web.pdf, May 9; Sewell, W.A.C., Jolles, S., Immunomodulatory action of intravenous immunoglobulin (2002) Immunology, 107, pp. 387-393; Rota, P.A., Oberste, M.S., Monroe, S., Allan Nix, W., Campagnoli, R., Icenogle, J.P., Characterization of a novel coronavirus associated with severe acute respiratory syndrome Science, , www.sciencexpress.org/1May2003/Page1/10.126/science.1085952; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooke-Wilson, A., Butterfield, Y.S.N., The genome sequence of the SARS-associated coronavirus Science, , www.sciencexpress.org/1May2003/Page1/10.1126/science.1085953","Kao, C.-L.; Natl. Taiwan Univ. Coll. of Medicine, No 7 Chung-Shan South Road, Taipei, Taiwan; email: clkao@ha.mc.ntu.edu.tw",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14519257","English","Emerg. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-84983719141
"Tsang K.W., Mok T.Y., Wong P.C., Ooi G.C.","7201555024;8706357200;7403979916;16239781100;","Severe acute respiratory syndrome (SARS) in Hong Kong",2003,"Respirology","8","3",,"259","265",,13,"10.1046/j.1440-1843.2003.00486.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141513797&doi=10.1046%2fj.1440-1843.2003.00486.x&partnerID=40&md5=606b96fd32f9f27cae8b43a62b68d8ca","University Department of Medicine, University of Hong Kong, Queen Mary Hospital, Hong Kong SAR, China; Univ. Dept. of Diagnostic Radiology, University of Hong Kong, Queen Mary Hospital, Hong Kong SAR, China; Kowloon Hospital, Hong Kong SAR, China; Div. of Resp. and Critical Care Med., University Department of Medicine, Queen Mary Hospital, Pokfulam, Hong Kong SAR, China","Tsang, K.W., University Department of Medicine, University of Hong Kong, Queen Mary Hospital, Hong Kong SAR, China, Div. of Resp. and Critical Care Med., University Department of Medicine, Queen Mary Hospital, Pokfulam, Hong Kong SAR, China; Mok, T.Y., Kowloon Hospital, Hong Kong SAR, China; Wong, P.C., University Department of Medicine, University of Hong Kong, Queen Mary Hospital, Hong Kong SAR, China; Ooi, G.C., Univ. Dept. of Diagnostic Radiology, University of Hong Kong, Queen Mary Hospital, Hong Kong SAR, China","Severe acute respiratory syndrome (SARS) is a recently recognized and highly contagious pneumonic illness, caused by a novel coronavirus. While developments in diagnostic, clinical and other aspects of SARS research are well underway, there is still great difficulty for frontline clinicians as validated rapid diagnostic tests or effective treatment regimens are lacking. This article attempts to summarize some of the recent developments in this newly recognized condition from the Asia Pacific perspective.","Corticosteroids; Diagnosis; Management; Ribavirin; Severe acute respiratory syndrome","antibiotic agent; cephalosporin derivative; corticosteroid; hydrocortisone; macrolide; methylprednisolone; prednisolone; ribavirin; chill; Coronavirus; diagnostic value; diarrhea; dyspnea; epidemiological data; fever; headache; hemolytic anemia; Hong Kong; human; malaise; myalgia; patient care; pneumonia; priority journal; prognosis; pulsatile drug release; respiratory failure; reverse transcription polymerase chain reaction; review; rhinorrhea; severe acute respiratory syndrome; sneezing; sore throat; treatment indication; virus pathogenesis; Antiviral Agents; Diagnosis, Differential; Disease Outbreaks; Hong Kong; Humans; Infection Control; Patient Isolation; Ribavirin; Severe Acute Respiratory Syndrome","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; http://www.who.int/csr/sars/country/2003_05_26/en/; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Hsu, L.Y., Lee, C.C., Green, J.A., Severe Acute Respiratory Syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg. Infect. Dis., 9, pp. 713-717; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Muller, N.L., Staples, C.A., Miller, R.R., Bronchiolitis obliterans organizing pneumonia: CT features in 14 patients (1990) Am. J. Roentgenol., 154, pp. 983-987; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto Area (2003) JAMA, 289, pp. 2801-2809; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/, Revised 1 May; (2003) Severe Acute Respiratory Syndrome (SARS). Diagnosis/Evaluation, , http://www.cdc.gov/ncidod/sars/diagnosis.htm, 23 May; (2003) Severe Acute Respiratory Syndrome (SARS). Diagnosis and Reporting, , http://www.ha.org.hk/sars/ps/information/diagnosis_n_report.htm, Updated 22 April; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarsarchive/2003_05_05/en/, Revised 1 May; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Wong, K.T., Antonio, G.E., Hui, D.S., Thin-section CT of severe acute respiratory syndrome: Evaluation of 74 patients exposed to or with the disease (2003) Radiology, , http://radiology.rsnajnls.org/cgi/content/full/2283030541v1, 8 May [epub ahead of print]; Lee, K.S., Kullnig, P., Hartman, T.E., Muller, N.L., Cryptogenic organizing pneumonia: CT findings in 43 patients (1994) Am. J. Roentgenol., 162, pp. 543-546; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Primack, S.L., Hartman, T.E., Ikezoe, J., Akira, M., Sakatani, M., Muller, N.L., Acute interstitial pneumonia: Radiographic and CT findings in nine patients (1993) Radiology, 188, pp. 817-820; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; (2003) Severe Acute Respiratory Syndrome (SARS). Treatment, , http://www.cdc.gov/ncidod/sars/treatment.htm, 25 March; (2003) Severe Acute Respiratory Syndrome (SARS). Management, , http://www.who.int/csr/sars/management/en/, Revised 11 April; Oba, Y., The use of corticosteroids in SARS (2003) N. Engl. J. Med., 348, pp. 2034-2035; Cyranoski, D., Critics slam treatment for SARS as ineffective and perhaps dangerous (2003) Nature, 423, p. 4; Wenzel, R.P., Edmond, M.B., Managing SARS amidst uncertainty (2003) N. Engl. J. Med., 348, pp. 1947-1948; So, L.K.Y., Lau, A.C.W., Yam, L.Y.C., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617","Tsang, K.W.; Div. of Resp. and Critical Care Med., University Department of Medicine, Queen Mary Hospital, Pokfulam, Hong Kong SAR, China; email: kwttsang@hku.hk",,,13237799,,RSPIF,"14528875","English","Respirology",Review,"Final",Open Access,Scopus,2-s2.0-0141513797
"Mills R.M.","7403035491;","The pros and cons of vaccinating the dog population against canine coronavirus and one of the serovars of Leptospira interrogans.",2003,"Australian veterinary journal","81","9",,"531","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3843102874&partnerID=40&md5=c9ed2eea537817068258bb03878053ec",,"Mills, R.M.",[No abstract available],,"bacterial vaccine; virus vaccine; animal; animal disease; Coronavirus; dog; dog disease; immunology; Leptospira interrogans; leptospirosis; letter; risk factor; vaccination; virus infection; Animals; Bacterial Vaccines; Coronavirus; Coronavirus Infections; Dog Diseases; Dogs; Leptospira interrogans; Leptospirosis; Risk Factors; Vaccination; Viral Vaccines",,"Mills, R.M.",,,00050423,,,"15086088","English","Aust Vet J",Letter,"Final",,Scopus,2-s2.0-3843102874
"Campanacci V., Egloff M.-P., Longhi S., Ferron F., Rancurel C., Salomoni A., Durousseau C., Tocque F., Brémond N., Dobbe J.C., Snijder E.J., Canard B., Cambillau C.","6602896947;7003979084;57203069695;8526522800;6508283580;6603711254;6507734832;6504728589;56711842000;6602684547;7006058325;7003995150;7006765066;","Structural genomics of the SARS coronavirus: Cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein",2003,"Acta Crystallographica - Section D Biological Crystallography","59","9",,"1628","1631",,29,"10.1107/S0907444903016779","https://www.scopus.com/inward/record.uri?eid=2-s2.0-12444276645&doi=10.1107%2fS0907444903016779&partnerID=40&md5=913da85824f7830f4454b863c9755907","Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, Netherlands","Campanacci, V., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Egloff, M.-P., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Longhi, S., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Ferron, F., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Rancurel, C., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Salomoni, A., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Durousseau, C., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Tocque, F., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Brémond, N., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Dobbe, J.C., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, Netherlands; Snijder, E.J., Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, Netherlands; Canard, B., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; Cambillau, C., Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France","A SARS-CoV whole genome approach has been develop aimed a determining the crystal structure of all of its proteins or domains. Here, the cloning E. coli expression, purification, and crystallization of the SARS-CoV Nsp9 protein, the first SARS-CoV protein to be crystallized, are reported.",,"Amino Acid Sequence; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Genomics; RNA-Binding Proteins; SARS Virus; Sequence Alignment; Viral Nonstructural Proteins; Viral Proteins; Coronavirus; RNA viruses; SARS coronavirus","Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., (2003) Science, 300, pp. 1763-1767; Bost, A.G., Carnahan, R.H., Lu, X.T., Denison, M.R., (2000) J. Virol., 74, pp. 3379-3387; (1994) Acta Cryst., D50, pp. 760-763. , Collaborative Computational Project, Number 4; Corpet, F., (1988) Nucleic Acids Res., 16, pp. 10881-10890; Cuff, J.A., Clamp, M.E., Siddiqui, A.S., Finlay, M., Barton, G.J., (1998) Bioinformatics, 14, pp. 892-893; De Francesco, R., Tomei, L., Altamura, S., Summa, V., Migliaccio, G., (2003) Antivir. Res., 58, pp. 1-16; Doublié, S., (1997) Methods Enzymol., 276, pp. 523-530; Drosten, C., (2003) N. Engl. J. Med., 348, pp. 1967-1976; Fischer, D., (2000) Pac. Symp. Biocomput., 5, pp. 119-130; Gong, C., Shuman, S., (2002) J. Biol. Chem., 277, pp. 15317-15324; Grotzinger, C., Heusipp, G., Ziebuhr, J., Harms, U., Suss, J., Siddell, S.G., (1996) Virology, 222, pp. 227-235; Hendrickson, W.A., (1991) Science, 254, pp. 51-58; Kelley, L.A., MacCallum, R.M., Sternberg, M.J., (2000) J. Mol. Biol., 299, pp. 499-520; Koren, G., King, S., Knowles, S., Phillips, E., (2003) CMAJ, 168, pp. 1289-1292; Ksiazek, T.G., (2003) N. Engl. J. Med., 348, pp. 1953-1966; Lai, M.M.C., Holmes, K.V., (2001) Fields Virology, 4th Ed., pp. 1163-1185. , edited by D. M. Knipe & P. M. Howley. Philadelphia: Lippincott Williams & Wilkins; Lartigue, A., Rivière, S., Brossut, R., Tegoni, M., Cambillau, C., (2003) Acta Cryst., D59, pp. 916-918; McGuffin, L.J., Bryson, K., Jones, D.T., (2000) Bioinformatics, 16, pp. 404-405; Matthews, B.W., (1968) J. Mol. Biol., 33, pp. 491-497; Otwinowski, Z., Minor, W., (1997) Methods Enzymol., 276, pp. 307-326; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., (2003) Lancet, 361, pp. 1319-1325; Rost, B., (1996) Methods Enzymol., 266, pp. 525-539; Snijder, E.J., Bredenbeek, P.J., Dobbe, J.C., Thiel, V., Ziebuhr, J., Poon, L.L.M., Guan, Y., Gorbalenya, A.E., (2003), In the press; Sulzenbacher, G., (2002) Acta Cryst., D58, pp. 2109-2115; Vincentelli, R., Bignon, C., Gruez, A., Sulzenbacher, G., Canaan, S., Tegoni, M., Campanacci, V., Cambillau, C., (2003) Acc. Chem. Res., 36, pp. 165-172","Canard, B.; Arch./Fonction Macromolec. B., UMR 6098 CNRS, Universites Aix-Marseille I and II, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France; email: canard@afmb.cnrs-mrs.fr",,,09074449,,ABCRE,"12925794","English","Acta Crystallogr. Sect. D Biol. Crystallogr.",Article,"Final",Open Access,Scopus,2-s2.0-12444276645
"Wesley R.D., Lager K.M.","7103154080;26643487900;","Increased litter survival rates, reduced clinical illness and better lactogenic immunity against TGEV in gilts that were primed as neonates with porcine respiratory coronavirus (PRCV)",2003,"Veterinary Microbiology","95","3",,"175","186",,15,"10.1016/S0378-1135(03)00150-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142043901&doi=10.1016%2fS0378-1135%2803%2900150-0&partnerID=40&md5=89c3d22d4a0f36d769600095f4ef83f1","Virus/Prion Dis. Livestock Res. U., National Animal Disease Center, USDA, P.O. Box 70, Ames, IA 50010, United States","Wesley, R.D., Virus/Prion Dis. Livestock Res. U., National Animal Disease Center, USDA, P.O. Box 70, Ames, IA 50010, United States; Lager, K.M., Virus/Prion Dis. Livestock Res. U., National Animal Disease Center, USDA, P.O. Box 70, Ames, IA 50010, United States","Establishing immunological memory in female piglets at a young age with PRCV was effective in inducing a secondary immune response to a limiting dose of virulent TGEV given orally 13-18 days prior to farrowing. Subsequently, because of passive antibody transfer, the offspring of these primed gilts were more efficient in surviving a lethal TGEV challenge. An average survival rate of 89% occurred in 6 litters of piglets from primed gilts that were boosted with 2.8×106 plaque forming units (PFU) of TGEV whereas 76% of the piglets survived in three litters that suckled primed gilts boosted with 3.0×105PFU of TGEV. Non-primed gilts given identical pre-farrowing doses of TGEV had litter survival rates of 63 and 55%, respectively. Moreover, both groups of litters from primed gilts suffered less clinical illness (as measured by the extent of weight loss post-challenge) than control litters. Priming of the piglets as neonates and boosting the pregnant gilts produced an anamnestic systemic immune response and correspondingly higher milk titers in the primed gilts compared to control animals. Thus, priming piglets with PRCV was beneficial in providing resistance to TGEV and could be incorporated into a vaccine strategy that yields better protection against TGEV. © 2003 Elsevier B.V. All rights reserved.","Immunologic memory; Lactogenic immunity; Porcine respiratory coronavirus (PRCV); TGEV","animal experiment; article; controlled study; Coronavirus; disease course; female; immunological memory; milk; newborn; nonhuman; passive immunization; plaque forming cell; Porcine respiratory coronavirus; pregnancy; progeny; secondary immune response; suckling; survival rate; swine; Transmissible gastroenteritis virus; virus immunity; virus plaque; virus titration; virus virulence; weight reduction; Animalia; Coronavirus; Porcine respiratory coronavirus; Suidae; Transmissible gastroenteritis virus","Britton, P., Mawditt, K.L., Page, K.W., The cloning and sequencing of the virion protein genes from a British isolate of porcine respiratory coronavirus: Comparison with transmissible gastroenteritis virus genes (1991) Virus Res., 21, pp. 181-198; Cox, E., Pensaert, M.B., Callebaut, P., Intestinal protection against challenge with transmissible gastroenteritis virus of pigs immune after infection with the porcine respiratory coronavirus (1993) Vaccine, 11, pp. 267-272; Haelterman, E.O., Lactogenic immunity to transmissible gastroenteritis of swine (1965) J. Am. Vet. Med. Assoc., 147, p. 1661; Hooper, B.E., Haelterman, E.O., Concepts of pathogenesis and passive immunity in transmissible gastroenteritis of swine (1966) J. Am. Vet. Med. Assoc., 149, pp. 1580-1586; Kim, L., Hayes, J., Lewis, P., Parwani, A.V., Chang, K.O., Saif, L.J., Molecular characterization and pathogenesis of transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCV) field isolates co-circulating in a swine herd (2000) Arch. Virol., 145, pp. 1133-1147; Krempl, C., Schultze, B., Laude, H., Herrier, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J. Virol., 71, pp. 3285-3287; Lanza, I., Shoup, D.I., Saif, L.J., Lactogenic immunity and milk antibody isotypes to transmissible gastroenteritis virus in sows exposed to porcine respiratory coronavirus during pregnancy (1995) Am. J. Vet. Res., 56, pp. 739-748; Moon, H.W., Mechanisms in the pathogenesis of diarrhea: A review (1978) J. Am. Vet. Med. Assoc., 172, pp. 443-448; Moon, H.W., Kemeny, L.J., Lambert, G., Stark, S.L., Booth, G.D., Age dependent resistance to transmissible gastroenteritis virus of swine. III. Effects of epithelial cell kinetics on coronavirus production and on atrophy of intestinal villi (1975) Vet. Pathol., 12, pp. 434-445; Paton, D.J., Saif, L.J., Levings, R.L., Transmissible gastroenteritis (1996) OIE Manual of Standards for Diagnostic Tests and Vaccines, 3rd Ed., pp. 488-495. , Office International des Epizooties, Paris, France, Chapter 3.5.5; Pensaert, M., Callebaut, P., Vergote, J., Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis (1986) Vet. Quart., 8, pp. 257-261; Rao, J.N.K., Scott, A.J., A simple method for the analysis of clustered binary data (1992) Biometics, 48, pp. 577-588; Roth, J.A., The immune system (1999) Diseases of Swine, 8th Ed., pp. 799-820. , Straw, B.E., D'Allaire, S., et al. (Eds.). Iowa State University Press, Ames, IA; Saif, L.J., Bohl, E.H., Passive immunity to transmissible gastroenteritis virus: Intramammary viral inoculation of sows (1983) Ann. NY Acad. Sci., 409, pp. 708-723; Saif, L.J., Wesley, R.D., Transmissible gastroenteritis and porcine respiratory coronavirus (1999) Diseases of Swine, 8th Ed., pp. 295-325. , Straw, B.E., D'Allaire, S., et al. (Eds.). Iowa State University Press, Ames, IA; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J. Virol., 73, pp. 7607-7618; Sestak, K., Lanza, I., Park, S.K., Weilnau, P.A., Saif, L.J., Contribution of passive immunity to porcine respiratory coronavirus to protection against transmissible gastroenteritis virus challenge exposure in suckling pigs (1996) Am. J. Vet. Res., 57, pp. 664-671; Stone, S.S., Kemeny, L.J., Woods, R.D., Jensen, M.T., Efficacy of isolated colostral IgA, IgG, and IgM(A) to protect neonatal pigs against the coronavirus of transmissible gastroenteritis (1977) Am. J. Vet. Res., 38, pp. 1285-1288; Van Nieuwstadt, A.P., Zetstra, T., Boonstra, J., Infection with porcine respiratory coronavirus does not fully protect pigs against intestinal transmissible gastroenteritis virus (1989) Vet. Rec., 125, pp. 58-60; VanCott, J.L., Brim, T.A., Lunney, J.K., Saif, L.J., Contribution of antibody-secreting cells induced in mucosal lymphoid tissues of pigs inoculated with respiratory or enteric strains of coronavirus to immunity against enteric coronavirus challenge (1994) J. Immunol., 152, pp. 3980-3990; Vaughn, E.M., Halbur, P.G., Paul, P.S., Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes (1995) J. Virol., 69, pp. 3176-3184; Wesley, R.D., Minimum viral dose for protective lactogenic immunity against transmissible gastroenteritis (2000) Proceedings of the 16th International Pig Veterinary Society Congress, p. 572. , Melbourne, Australia; Wesley, R.D., Neutralizing antibody decay and lack of contact transmission after inoculation of 3- and 4-day-old piglets with porcine respiratory coronavirus (2002) J. Vet. Diagn. Invest., 14, pp. 525-527; Wesley, R.D., Woods, R.D., Induction of protective immunity against transmissible gastroenteritis virus after exposure of neonatal pigs to porcine respiratory coronavirus (1996) Am. J. Vet. Res., 57, pp. 157-162; Wesley, R.D., Woods, R.D., Correa, I., Enjuanes, L., Lack of protection in vivo with neutralizing monoclonal antibodies to transmissible gastroenteritis virus (1988) Vet. Microbiol., 18, pp. 197-208; Wesley, R.D., Woods, R.D., Hill, H.T., Biwer, J.D., Evidence for a porcine respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus, in the United States (1990) J. Vet. Diagn. Invest., 2, pp. 312-317; Woods, R.D., Wesley, R.D., Kapke, P.A., Neutralization of porcine transmissible gastroenteritis virus by complement-dependent monoclonal antibodies (1988) Am. J. Vet. Res., 49, pp. 300-304","Wesley, R.D.; Virus/Prion Dis. Livestock Res. U., National Animal Disease Center, USDA, P.O. Box 70, Ames, IA 50010, United States; email: rwesley@nadc.ars.usda.gov",,"Elsevier",03781135,,VMICD,"12935745","English","Vet. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0142043901
"Breiman R.F., Evans M.R., Preiser W., Maguire J., Schnur A., Li A., Bekedam H., MacKenzie J.S.","34567511600;35232918600;7004338253;8682166900;6602639659;57199855638;25228197200;7401614409;","Role of China in the quest to define and control severe acute respiratory syndrome",2003,"Emerging Infectious Diseases","9","9",,"1037","1041",,45,"10.3201/eid0909.030390","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042818018&doi=10.3201%2feid0909.030390&partnerID=40&md5=e54451f6e0b27d2c763e12603782dd83","Intl. Ctr. for Diarrheal Dis. Res., Bangladesh-Ctr. for Hlth./Pop. Res., Dhaka, Bangladesh; Natl. Pub. Health Service for Wales, Cardiff, United Kingdom; Institute for Medical Virology, Frankfurt, Germany; Ctr. for Dis. Control and Prevention, Atlanta, GA, United States; World Health Organization, Beijing, China; University of Queensland, Brisbane, QLD, Australia; Hlth. Syst. and Infect. Dis. Div., ICDDR, B-Centre for Hlth. and Pop. Res., Dhaka, Bangladesh","Breiman, R.F., Intl. Ctr. for Diarrheal Dis. Res., Bangladesh-Ctr. for Hlth./Pop. Res., Dhaka, Bangladesh, Hlth. Syst. and Infect. Dis. Div., ICDDR, B-Centre for Hlth. and Pop. Res., Dhaka, Bangladesh; Evans, M.R., Natl. Pub. Health Service for Wales, Cardiff, United Kingdom; Preiser, W., Institute for Medical Virology, Frankfurt, Germany; Maguire, J., Ctr. for Dis. Control and Prevention, Atlanta, GA, United States; Schnur, A., World Health Organization, Beijing, China; Li, A., World Health Organization, Beijing, China; Bekedam, H., World Health Organization, Beijing, China; MacKenzie, J.S., University of Queensland, Brisbane, QLD, Australia","China holds the key to solving many questions crucial to global control of severe acute respiratory syndrome (SARS). The disease appears to have originated in Guangdong Province, and the causative agent, SARS coronavirus, is likely to have originated from an animal host, perhaps sold in public markets. Epidemiologic findings, integral to defining an animal-human linkage, may be confirmed by laboratory studies; once animal host(s) are confirmed, interventions may be needed to prevent further animal-to-human transmission. Community seroprevalence studies may help determine the basis for the decline in disease incidence in Guangdong Province after February 2002. China will also be able to contribute key data about how the causative agent is transmitted and how it is evolving, as well as identifying pivotal factors influencing disease outcome.",,"antibiotic agent; antivirus agent; corticosteroid; herbaceous agent; ribavirin; artificial ventilation; China; clinical trial; controlled clinical trial; Coronavirus; disease activity; disease course; epidemiological data; hospitalization; human; incidence; infection control; laboratory diagnosis; molecular genetics; pneumonia; randomized controlled trial; review; seroprevalence; severe acute respiratory syndrome; treatment outcome; virus transmission","Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Ludwig, B., Kraus, F.B., Allwinn, R., Doerr, H.W., Preiser, W., Viral zoonoses - A threat under control? (2003) Intervirology, 46, pp. 71-78; Williams, E.S., Yuill, T., Artois, M., Fischer, J., Haigh, S.A., Emerging infectious diseases in wildlife (2002) Rev Sci Tech, 21, pp. 139-157; Riley, S., Fraser, C., Donnelly, C.A., Ghani, A.C., Abu-Raddad, L.J., Hedley, A.J., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, J.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ruan, Y.J., Wei, C.L., Ee, L.A., Vega, V.B., Thoreau, H., Su, S.T., Comparative full-length sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Zhong, N.S., Zeng, G.Q., Our strategies for fighting severe acute respiratory syndrome (SARS) (2003) Am J Respir Crit Care Med, 168, pp. 7-9; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Hsu, L.Y., Lee, C.C., Green, J.A., Ang, B., Paton, N.I., Lee, L., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9, pp. 713-717","Breiman, R.F.; Hlth. Syst. and Infect. Dis. Div., ICDDR, B-Centre for Hlth. and Pop. Res., Dhaka, Bangladesh; email: breiman@icddrb.org",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14519236","English","Emerg. Infect. Dis.",Review,"Final",Open Access,Scopus,2-s2.0-0042818018
"Tsui P.T., Kwok M.L., Yuen H., Lai S.T.","8272927200;8120214200;20636461800;7402937038;","Severe acute respiratory syndrome: Clinical outcome and prognostic correlates",2003,"Emerging Infectious Diseases","9","9",,"1064","1069",,122,"10.3201/eid0909.030362","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042818004&doi=10.3201%2feid0909.030362&partnerID=40&md5=9543fdd2d300a49f9efcc464ce22f1ef","Princess Margaret Hospital, Hong Kong, Hong Kong; Dept. of Medicine and Geriatrics, 2-10 Princess Margaret Hospital Road, Hong Kong, Hong Kong","Tsui, P.T., Princess Margaret Hospital, Hong Kong, Hong Kong, Dept. of Medicine and Geriatrics, 2-10 Princess Margaret Hospital Road, Hong Kong, Hong Kong; Kwok, M.L., Princess Margaret Hospital, Hong Kong, Hong Kong; Yuen, H., Princess Margaret Hospital, Hong Kong, Hong Kong; Lai, S.T., Princess Margaret Hospital, Hong Kong, Hong Kong","Severe acute respiratory syndrome (SARS) poses a major threat to the health of people worldwide. We performed a retrospective case series analysis to assess clinical outcome and identify pretreatment prognostic correlates of SARS, managed under a standardized treatment protocol. We studied 127 male and 196 female patients with a mean age of 41±14 (range 18-83). All patients, except two, received ribavirin and steroid combination therapy. In 115 (36%) patients, the course of disease was limited. Pneumonitis progressed rapidly in the remaining patients. Sixty-seven (21%) patients required intensive care, and 42 (13%) required ventilator support. Advanced age, high admission neutrophil count, and high initial lactate dehydrogenase level were independent correlates of an adverse clinical outcome. SARS-associated coronavirus caused severe illnesses in most patients, despite early treatment with ribavirin and steroid. This study has identified three independent pretreatment prognostic correlates.",,"creatine kinase; lactate dehydrogenase; ribavirin; steroid; adult; aged; article; artificial ventilation; cell count; controlled study; Coronavirus; correlation analysis; creatine kinase blood level; disease course; dose response; female; human; intensive care; lactate dehydrogenase blood level; lymphocytopenia; major clinical study; male; mortality; neutrophil; pneumonia; prognosis; retrospective study; seroprevalence; severe acute respiratory syndrome; thrombocytopenia; treatment outcome","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; SARS Coronavirus Sequencing, , http://www.cdc.gov/ncidod/sars/sequence.htm; Interim Guidelines for National SARS Preparedness, , http://www.wpro.who.int/sars/interim_guidelines/interim_guidelines_26May. pdf; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Outbreak of Severe Acute Respiratory Syndrome (SARS) at Amoy Gardens, Kowloon Bay, Hong Kong, , http://www.info.gov.hk/info/ap/pdf/amoy_e.pdf; http://www.ha.org.hk; HA Information on Management of SARS, , http://www.ha.org.hk/sars/ps/information/infection_control.htm; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Ng, W.F., Lai, S.T., Leung, C.Y., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Severe Acute Respiratory Syndrome (SARS): Laboratory Diagnostic Tests, , http://www.who.int/csr/sars/diagnostictests/en/; HA Information on Management of SARS: Infection Control, , http://www.ha.org.hk/sars/ps/information/treatment.htm; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772","Tsui, P.T.; Dept. of Medicine and Geriatrics, 2-10 Princess Margaret Hospital Road, Hong Kong, Hong Kong; email: tsuipt@netvigator.com",,"Centers for Disease Control and Prevention (CDC)",10806040,,EIDIF,"14519241","English","Emerg. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0042818004
"Ng P.C., So K.W., Leung T.F., Cheng F.W.T., Lyon D.J., Wong W., Cheung K.L., Fung K.S.C., Lee C.H., Li A.M., Hon K.L.E., Li C.K., Fok T.F.","17137242500;26868185900;55443283900;7202811097;7102554823;7403973011;55353862400;8948874600;35234000900;7403291810;8134452900;15122650100;7006455238;","Infection control for SARS in a tertiary neonatal centre",2003,"Archives of Disease in Childhood: Fetal and Neonatal Edition","88","5",,"F405","F409",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042261569&partnerID=40&md5=c5807ea60d3a16a1e02897dfee0cc051","Department of Paediatrics, Clinical Sciences Building, Prince of Wales Hospital, Shatin, N.T., Hong Kong; Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong","Ng, P.C., Department of Paediatrics, Clinical Sciences Building, Prince of Wales Hospital, Shatin, N.T., Hong Kong, Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; So, K.W., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Leung, T.F., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Cheng, F.W.T., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Lyon, D.J., Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Wong, W., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Cheung, K.L., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Fung, K.S.C., Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Lee, C.H., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Li, A.M., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Hon, K.L.E., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Li, C.K., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Fok, T.F., Department of Paediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong","The Severe Acute Respiratory Syndrome (SARS) is a newly discovered infectious disease caused by a novel coronavirus, which can readily spread in the healthcare setting. A recent community outbreak in Hong Kong infected a significant number of pregnant women who subsequently required emergency caesarean section for deteriorating maternal condition and respiratory failure. As no neonatal clinician has any experience in looking after these high risk infants, stringent infection control measures for prevention of cross infection between patients and staff are important to safeguard the wellbeing of the work force and to avoid nosocomial spread of SARS within the neonatal unit. This article describes the infection control and patient triage policy of the neonatal unit at the Prince of Wales Hospital, Hong Kong. We hope this information is useful in helping other units to formulate their own infection control plans according to their own unit configuration and clinical needs.",,"article; cesarean section; Coronavirus; epidemic; health care policy; Hong Kong; human; infection control; intrauterine infection; maternal welfare; newborn; newborn care; priority journal; respiratory failure; severe acute respiratory syndrome; virus pneumonia; Cross Infection; Disease Transmission, Patient-to-Professional; Disinfection; Equipment Contamination; Equipment Design; Female; Handwashing; Hong Kong; Hospitals, Maternity; Humans; Infant, Newborn; Infection Control; Intensive Care Units, Neonatal; Intensive Care, Neonatal; Medical Waste Disposal; Organizational Policy; Pregnancy; Pregnancy Complications, Infectious; Protective Clothing; Risk Assessment; Risk Factors; Severe Acute Respiratory Syndrome; Transportation of Patients; Triage; Visitors to Patients","Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Ho, W., Guideline on management of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1313-1315; SARS Precaution in Hospitals - Infection Control and Risk Management Approach, , www.ha.org.hk/hesd/nsapi; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , www.who.int/csr/sars/casedefinition/en; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Shek, C.C., Ng, P.C., Fung, G.P.G., Infants born to mothers with severe acute respiratory syndrome SARS) (2003) Pediatrics, 112. , in press; Li, T.S.T., Buckley, T.A., Yap, F.H.Y., Severe acute respiratory syndrome (SARS): Infection control (2003) Lancet, 361, p. 1386","Ng, P.C.; Department of Paediatrics, Clinical Sciences Building, Prince of Wales Hospital, Shatin, N.T., Hong Kong; email: pakcheungng@cuhk.edu.hk",,,13592998,,ADCHA,"12937045","English","Arch. Dis. Child. Fetal Neonatal Ed.",Article,"Final",,Scopus,2-s2.0-0042261569
"Franks T.J., Chong P.Y., Chui P., Galvin J.R., Lourens R.M., Reid A.H., Selbs E., McEvoy P.L., Hayden D.L., Fukuoka J., Taubenberger J.K., Travis W.D.","7003695679;56230699400;7005954069;7101906943;6506730644;56247786700;18937104300;7005111775;8948791000;6603028499;7005069763;35376557400;","Lung pathology of severe acute respiratory syndrome (SARS): A study of 8 autopsy cases from Singapore",2003,"Human Pathology","34","8",,"743","748",,163,"10.1016/S0046-8177(03)00367-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041386203&doi=10.1016%2fS0046-8177%2803%2900367-8&partnerID=40&md5=cbf422ce8a28fc832e7d3021915faf97","Dept. of Pulmon./Mediastinal Pathol., Armed Forces Institute of Pathology, Bldg. 54, 6825 16th Street NW, Washington, DC 20306, United States","Franks, T.J., Dept. of Pulmon./Mediastinal Pathol., Armed Forces Institute of Pathology, Bldg. 54, 6825 16th Street NW, Washington, DC 20306, United States; Chong, P.Y.; Chui, P.; Galvin, J.R.; Lourens, R.M.; Reid, A.H.; Selbs, E.; McEvoy, P.L.; Hayden, D.L.; Fukuoka, J.; Taubenberger, J.K.; Travis, W.D.","Severe acute respiratory syndrome (SARS) is an infectious condition caused by the SARS-associated coronavirus (SARS-CoV), a new member in the family Coronaviridae. To evaluate the lung pathology in this life-threatening respiratory illness, we studied postmortem lung sections from 8 patients who died from SARS during the spring 2003 Singapore outbreak. The predominant pattern of lung injury in all 8 cases was diffuse alveolar damage. The histology varied according to the duration of illness. Cases of 10 or fewer days' duration demonstrated acute-phase diffuse alveolar damage (DAD), airspace edema, and bronchiolar fibrin. Cases of more than 10 days' duration exhibited organizing-phase DAD, type II pneumocyte hyperplasia, squamous metaplasia, multinucleated giant cells, and acute bronchopneumonia. In acute-phase DAD, pancytokeratin staining was positive in hyaline membranes along alveolar walls and highlighted the absence of pneumocytes. Multinucleated cells were shown to be both type II pneumocytes and macrophages by pancytokeratin, thyroid transcription factor-1, and CD68 staining. SARS-CoV RNA was identified by reverse transcriptase-polymerase chain reaction in 7 of 8 cases in fresh autopsy tissue and in 8 of 8 cases in formalin-fixed, paraffin-embedded lung tissue, including the 1 negative case in fresh tissue. Understanding the pathology of DAD in SARS patients may provide the basis for therapeutic strategies. Further studies of the pathogenesis of SARS may reveal new insight into the mechanisms of DAD. © 2003 Elsevier Inc. All rights reserved.","Diffuse alveolar damage; SARS; SARS-associated corona virus; Severe acute respiratory syndrome","acute disease; adult; aged; article; autopsy; clinical article; disease duration; female; histology; human; human tissue; immunohistochemistry; lung alveolus; lung disease; lung infection; male; respiratory tract infection; severe acute respiratory syndrome; Singapore; virus infection","McIntosh, K., Ellis, E.F., Hoffman, L.S., The association of viral and bacterial respiratory infections with exacerbations of wheezing in young asthmatic children (1973) J Pediatr, 82, pp. 578-590; McIntosh, K., Chao, R.K., Krause, H.E., Coronavirus infection in acute lower respiratory tract disease of infants (1974) J Infect Dis, 130, pp. 502-507; Wenzel, R.P., Hendley, J.O., Davies, J.A., Coronavirus infections in military recruits. Three-year study with coronavirus strains OC43 and 229E (1974) Am Rev Respir Dis, 109, pp. 621-624; Mertsola, J., Ziegler, T., Ruuskanen, O., Recurrent wheezy bronchitis and viral respiratory infections (1991) Arch Dis Child, 66, pp. 124-129; Krafft, A.E., Duncan, B.W., Bijwaard, K.E., Optimization of the isolation and amplification of RNA from formalin-fixed, paraffin-embedded tissue: The Armed Forces Institute of Pathology experience and literature review (1997) Mol Diagn, 2, pp. 217-230; Taubenberger, J.K., Reid, A.H., Krafft, A.E., Initial genetic characterization of the 1918 ""Spanish"" influenza virus (1997) Science, 275, pp. 1793-1796; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/; Katzenstein, A.L., Bloor, C.M., Leibow, A.A., Diffuse alveolar damage - The role of oxygen, shock, and related factors. A review (1976) Am J Pathol, 85, pp. 209-228; Tomashefski J.F., Jr., Pulmonary pathology of acute respiratory distress syndrome (2000) Clin Chest Med, 21, pp. 435-466; Coronavirus Never Before Seen in Humans is the Cause of SARS, , http://www.who.int/csr/sars/archive/2003_04_16/en/; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Sun, A.P., Ohtsuki, Y., Fujita, J., Immunohistochemical characterisation of pulmonary hyaline membrane in various types of interstitial pneumonia (2003) Pathology, 35, pp. 120-124; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994","Franks, T.J.; Dept. of Pulmon./Mediastinal Pathol., Armed Forces Institute of Pathology, Bldg. 54, 6825 16th Street NW, Washington, DC 20306, United States",,"W.B. Saunders",00468177,,HPCQA,"14506633","English","Hum. Pathol.",Article,"Final",Open Access,Scopus,2-s2.0-0041386203
"Smits S.L., Lavazza A., Matiz K., Horzinek M.C., Koopmans M.P., De Groot R.J.","8571625100;35339480400;6602448973;7102624836;7006736989;7103077066;","Phylogenetic and evolutionary relationships among torovirus field variants: Evidence for multiple intertypic recombination events",2003,"Journal of Virology","77","17",,"9567","9577",,54,"10.1128/JVI.77.17.9567-9577.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042389536&doi=10.1128%2fJVI.77.17.9567-9577.2003&partnerID=40&md5=a54ec4cd50b07f75b36cbd29b8b53ceb","Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Natl. Inst. of Pub. Hlth./Environ., Bilthoven, Netherlands; Ist. Zooprof. S. Lombardia Emilia, Brescia, Italy; Veterinary Institute of Debrecen, Debrecen, Hungary","Smits, S.L., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Lavazza, A., Ist. Zooprof. S. Lombardia Emilia, Brescia, Italy; Matiz, K., Veterinary Institute of Debrecen, Debrecen, Hungary; Horzinek, M.C., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; Koopmans, M.P., Natl. Inst. of Pub. Hlth./Environ., Bilthoven, Netherlands; De Groot, R.J., Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands","Toroviruses (family Coronaviridae, order Nidovirales) are enveloped, positive-stranded RNA viruses that have been implicated in enteric disease in cattle and possibly in humans. Despite their potential veterinary and clinical relevance, little is known about torovirus epidemiology and molecular genetics. Here, we present the first study into the diversity among toroviruses currently present in European swine and cattle herds. Comparative sequence analysis was performed focusing on the genes for the structural proteins S, M, HE, and N, with fecal specimens serving as sources of viral RNA. Sequence data published for animal and human torovirus variants were included. Four genotypes, displaying 30 to 40% divergence, were readily distinguished, exemplified by bovine torovirus (BToV) Breda, porcine torovirus (PToV) Markelo, equine torovirus Berne, and the putative human torovirus. The ungulate toroviruses apparently display host species preference. In phylogenetic analyses, all PToV variants clustered, while the recent European BToVs mostly resembled the New World BToV variant Breda, identified 19 years ago. However, we found ample evidence for recurring intertypic recombination. All newly characterized BToV variants seem to have arisen from a genetic exchange, during which the 3′ end of the HE gene, the N gene, and the 3′ nontranslated region of a Breda virus-like parent had been swapped for those of PToV. Moreover, some PToV and BToV variants carried chimeric HE genes, which apparently resulted from recombination events involving hitherto unknown toroviruses. From these observations, the existence of two additional torovirus genotypes can be inferred. Toroviruses may be even more promiscuous than their closest relatives, the coronaviruses and arteriviruses.",,"structural protein; virus RNA; article; cattle; controlled study; Europe; genetic variability; genotype; molecular evolution; nonhuman; nucleotide sequence; phylogeny; priority journal; sequence analysis; sequence homology; swine; Torovirus; virus recombinant; Animals; Base Sequence; Cattle; Cattle Diseases; DNA, Viral; Epidemiology, Molecular; Europe; Evolution, Molecular; Humans; Microscopy, Electron; Models, Genetic; Molecular Sequence Data; Phylogeny; Recombination, Genetic; Sequence Homology, Nucleic Acid; Sus scrofa; Swine Diseases; Torovirus; Torovirus Infections; Variation (Genetics)","Beards, G.M., Brown, D.W., Green, J., Flewett, T.H., Preliminary characterisation of torovirus-like particles of humans: Comparison with Berne virus of horses and Breda virus of calves (1986) J. Med. Virol., 20, pp. 67-78; Beards, G.M., Hall, C., Green, J., Flewett, T.H., Lamouliatte, F., Du Pasquier, P., An enveloped virus in stools of children and adults with gastroenteritis that resembles the Breda virus of calves (1984) Lancet, 1, pp. 1050-1052; Boom, R., Sol, C.J., Salimans, M.M., Jansen, C.L., Wertheim-van Dillen, P.M., Van der Noordaa, J., Rapid and simple method for purification of nucleic acids (1990) J. Clin. Microbiol., 28, pp. 495-503; Brown, D.W., Beards, G.M., Flewett, T.H., Detection of Breda virus antigen and antibody in humans and animals by enzyme immunoassay (1987) J. Clin. Microbiol., 25, pp. 637-640; Brown, D.W., Selvakumar, R., Daniel, D.J., Mathan, V.I., Prevalence of neutralising antibodies to Berne virus in animals and humans in Vellore, South India (1988) Arch. Virol., 98, pp. 267-269; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Comeron, J.M., K-Estimator: Calculation of the number of nucleotide substitutions per site and the confidence intervals (1999) Bioinformatics, 15, pp. 763-764; Comeron, J.M., A method for estimating the numbers of synonymous and nonsynonymous substitutions per site (1995) J. Mol. Evol., 41, pp. 1152-1159; Cornelissen, L.A., Wierda, C.M., Van der Meer, F.J., Herrewegh, A.A., Horzinek, M.C., Egberink, H.F., De Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J. Virol., 71, pp. 5277-5286; Corpet, F., Multiple sequence alignment with hierarchical clustering (1988) Nucleic Acids Res., 16, pp. 10881-10890; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Duckmanton, L., Luan, B., Devenish, J., Tellier, R., Petric, M., Characterization of torovirus from human fecal specimens (1997) Virology, 239, pp. 158-168; Duckmanton, L., Tellier, R., Richardson, C., Petric, M., The novel hemagglutinin-esterase genes of human torovirus and Breda virus (1999) Virus Res., 64, pp. 137-149; Duckmanton, L.M., Tellier, R., Liu, P., Petric, M., Bovine torovirus: Sequencing of the structural genes and expression of the nucleocapsid protein of Breda virus (1998) Virus Res., 58, pp. 83-96; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Family Coronaviridae (2000) Virus Taxonomy, pp. 835-849. , M. H. V. van Regenmortel (ed.), Academic Press, London, United Kingdom; Gojobori, T., Moriyama, E.N., Kimura, M., Molecular clock of viral evolution, and the neutral theory (1990) Proc. Natl. Acad. Sci. USA, 87, pp. 10015-10018; Hamada, N., Masunaga, K., Ohtsu, Y., Kato, H., Tsuji, K., Maeda, H., Shingu, M., Toyoda, T., Nucleotide sequence of the gene encoding the RNA polymerase and the 3′ non-coding region of a bovine enterovirus Japanese isolate: Rapid synonymous substitutions between European and Japanese strains (1998) Arch. Virol., 143, pp. 815-821; Herrewegh, A.A., De Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J., Detection of feline coronavirus RNA in feces, tissues, and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A., Smeenk, I., Horzinek, M.C., Rottier, P.J., De Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Hoet, A.E., Cho, K.O., Chang, K.O., Loerch, S.C., Wittum, T.E., Saif, L.J., Enteric and nasal shedding of bovine torovirus (Breda virus) in feedlot cattle (2002) Am. J. Vet. Res., 63, pp. 342-348; Jamieson, F.B., Wang, E.E., Bain, C., Good, J., Duckmanton, L., Petric, M., Hum. torovirus: A new nosocomial gastrointestinal pathogen (1998) J. Infect. Dis., 178, pp. 1263-1269; Jia, W., Karaca, K., Parrish, C.R., Naqi, S.A., A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains (1995) Arch. Virol., 140, pp. 259-271; Kapur, V., Elam, M.R., Pawlovich, T.M., Murtaugh, M.P., Genetic variation in porcine reproductive and respiratory syndrome virus isolates in the midwestern United States (1996) J. Gen. Virol., 77, pp. 1271-1276; Kimura, M., The neutral theory of molecular evolution and the world view of the neutralists (1989) Genome, 31, pp. 24-31; Koopmans, M., Cremers, H., Woode, G., Horzinek, M.C., Breda virus (Toroviridae) infection and systemic antibody response in sentinel calves (1990) Am. J. Vet. Res., 51, pp. 1443-1448; Koopmans, M., Horzinek, M.C., Toroviruses of animals and humans: A review (1994) Adv. Virus Res., 43, pp. 233-273; Koopmans, M., Petric, M., Glass, R., Monroe, S., Enzyme-linked immunosorbent assay reactivity of torovirus-like particles in fecal specimens from humans with diarrhea (1993) J. Clin. Microbiol., 31, pp. 2738-2744; Koopmans, M., Van den Boom, U., Woode, G., Horzinek, M.C., Seroepidemiology of Breda virus in cattle with ELISA (1989) Vet. Microbiol., 19, pp. 233-243; Koopmans, M., Van Wuijckhuise-Sjouke, L., Schukken, Y.H., Cremers, H., Horzinek, M.C., Association of diarrhea in cattle with torovirus infections on farms (1991) Am. J. Vet. Res., 52, pp. 1769-1773; Koopmans, M.P., Goosen, E.S., Lima, A.A., McAuliffe, I.T., Nataro, J.P., Barrett, L.J., Glass, R.I., Guerrant, R.L., Association of torovirus with acute and persistent diarrhea in children (1997) Pediatr. Infect. Dis. J., 16, pp. 504-507; Kottier, S.A., Cavanagh, D., Britton, P., Experimental evidence of recombination in coronavirus infectious bronchitis virus (1995) Virology, 213, pp. 569-580; Krishnan, T., Naik, T., Electronmicroscopic evidence of torovirus like particles in children with diarrhoea (1997) Indian J. Med. Res., 105, pp. 108-110; Kroneman, A., Cornelissen, L.A., Horzinek, M.C., De Groot, R.J., Egberink, H.F., Identification and characterization of a porcine torovirus (1998) J. Virol., 72, pp. 3507-3511; Kumar, S., Tamura, K., Jakobsen, I.B., Nei, M., MEGA2: Molecular evolutionary genetics analysis software (2001) Bioinformatics, 17, pp. 1244-1245; Kusters, J.G., Jager, E.J., Niesters, H.G., Van der Zeijst, B.A., Sequence evidence for RNA recombination in field isolates of avian coronavirus infectious bronchitis virus (1990) Vaccine, 8, pp. 605-608; Lai, M.M., RNA recombination in animal and plant viruses (1992) Microbiol. Rev., 56, pp. 61-79; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Lavazza, A., Candotti, P., Perini, S., Vezzali, L., Electron microscopic identification of torovirus-like particles in post-weaned piglets with enteritis (1996) 14th IPVS Congress, , Bologna, Italy; Leitner, T., Albert, J., The molecular clock of HIV-1 unveiled through analysis of a known transmission history (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 10752-10757; Luo, G.X., Taylor, J., Template switching by reverse transcriptase during DNA synthesis (1990) J. Virol., 64, pp. 4321-4328; Makino, S., Keck, J., Stohlman, S., Lai, M., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-737; Matiz, K., Kecskemeti, S., Kiss, I., Adam, Z., Tanyi, J., Nagy, B., Torovirus detection in faecal specimens of calves and pigs in Hungary: Short communication (2002) Acta Vet. Hung., 50, pp. 293-296; Meng, X.J., Heterogeneity of porcine reproductive and respiratory syndrome virus: Implications for current vaccine efficacy and future vaccine development (2000) Vet. Microbiol., 74, pp. 309-329; Motokawa, K., Hohdatsu, T., Hashimoto, H., Koyama, H., Comparison of the amino acid sequence and phylogenetic analysis of the peplomer, integral membrane and nucleocapsid proteins of feline, canine and porcine coronaviruses (1996) Microbiol. Immunol., 40, pp. 425-433; Murtaugh, M.P., Yuan, S., Faaberg, K.S., Appearance of novel PRRSV isolates by recombination in the natural environment (2001) Adv. Exp. Med. Biol., 494, pp. 31-36; Nagy, P.D., Simon, A.E., New insights into the mechanisms of RNA recombination (1997) Virology, 235, pp. 1-9; Pohlenz, J., Cheville, N., Woode, G., Mokresh, A., Cellular lesions in intestinal mucosa of gnotobiotic calves experimentally infected with a new unclassified bovine virus (Breda virus) (1984) Vet. Pathol., 21, pp. 407-417; Sanchez, C.M., Gebauer, F., Sune, C., Mendez, A., Dopazo, J., Enjuanes, L., Genetic evolution and tropism of transmissible gastroenteritis coronaviruses (1992) Virology, 190, pp. 92-105; Snijder, E.J., Den Boon, J.A., Bredenbeek, P.J., Horzinek, M.C., Rijnbrand, R., Spaan, W.J., The carboxyl-terminal part of the putative Berne virus polymerase is expressed by ribosomal frameshifting and contains sequence motifs which indicate that toro- and coronaviruses are evolutionarily related (1990) Nucleic Acids Res., 18, pp. 4535-4542; Snijder, E.J., Den Boon, J.A., Spaan, W.J., Weiss, M., Horzinek, M.C., Primary structure and post-translational processing of the Berne virus peplomer protein (1990) Virology, 178, pp. 355-363; Snijder, E.J., Horzinek, M.C., Toroviruses: Replication, evolution and comparison with other members of the coronavirus-like superfamily (1993) J. Gen. Virol., 74, pp. 2305-2316; Snljder, E.J., Horzinek, M.C., Spaan, W.J., A 3′-coterminal nested set of independently transcribed mRNAs is generated during Berne virus replication (1990) J. Virol., 64, pp. 331-338; Van der Poel, W.H., Vinje, J., Van Der Heide, R., Herrera, M.I., Vivo, A., Koopmans, M.P., Norwalk-like calicivirus genes in farm animals (2000) Emerg. Infect. Dis., 6, pp. 36-41; Van Vliet, A.L., Smits, S.L., Rottier, P.J., De Groot, R.J., Discontinuous and non-discontinuous subgenomic RNA transcription in a nidovirus (2002) EMBO J., 21, pp. 6571-6580; Van Vugt, J.J., Storgaard, T., Oleksiewicz, M.B., Botner, A., High frequency RNA recombination in porcine reproductive and respiratory syndrome virus occurs preferentially between parental sequences with high similarity (2001) J. Gen. Virol., 82, pp. 2615-2620; Vaucher, Y.E., Ray, C.G., Minnich, L.L., Payne, C.M., Beck, D., Lowe, P., Pleomorphic, enveloped, virus-like particles associated with gastrointestinal illness in neonates (1982) J. Infect. Dis., 145, pp. 27-36; Wang, L., Xu, Y., Collisson, E.W., Experimental confirmation of recombination upstream of the S1 hypervariable region of infectious bronchitis virus (1997) Virus Res., 49, pp. 139-145; Weiller, G.F., Phylogenetic profiles: A graphical method for detecting genetic recombinations in homologous sequences (1998) Mol. Biol. Evol., 15, pp. 326-335; Weiss, M., Steck, F., Horzinek, M.C., Purification and partial characterization of a new enveloped RNA virus (Berne virus) (1983) J. Gen. Virol., 64, pp. 1849-1858; Weiss, M., Steck, F., Kaderli, R., Horzinek, M.C., Antibodies to Berne virus in horses and other animals (1984) Vet. Microbiol., 9, pp. 523-531; Woode, G.N., Pohlenz, J.F., Gourley, N.E., Fagerland, J.A., Astrovirus and Breda virus infections of dome cell epithelium of bovine ileum (1984) J. Clin. Microbiol., 19, pp. 623-630; Woode, G.N., Reed, D.E., Runnels, P.L., Herrig, M.A., Hill, H.T., Studies with an unclassified virus isolated from diarrheic calves (1982) Vet. Microbiol., 7, pp. 221-240; Woode, G.N., Saif, L.J., Quesada, M., Winand, N.J., Pohlenz, J.F., Gourley, N.K., Comparative studies on three isolates of Breda virus of calves (1985) Am. J. Vet. Res., 46, pp. 1003-1010; Worobey, M., Holmes, E.C., Evolutionary aspects of recombination in RNA viruses (1999) J. Gen. Virol., 80, pp. 2535-2543; Yuan, S., Nelsen, C.J., Murtaugh, M.P., Schmitt, B.J., Faaberg, K.S., Recombination between North American strains of porcine reproductive and respiratory syndrome virus (1999) Virus Res., 61, pp. 87-98; Zhang, G., Haydon, D.T., Knowles, N.J., McCauley, J.W., Molecular evolution of swine vesicular disease virus (1999) J. Gen. Virol., 80, pp. 639-651","De Groot, R.J.; Virology Division, Dept. of Infect. Dis. and Immunology, Utrecht University, 3584 CL Utrecht, Netherlands; email: R.Groot@vet.uu.nl",,,0022538X,,JOVIA,"12915570","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0042389536
"Pang B.S., Wang Z., Zhang L.M., Tong Z.H., Xu L.L., Huang X.X., Guo W.J., Zhu M., Wang C., Li X.W., He Z.P., Li H.X., Zhao F.J.","7006274811;7410037669;14629733200;7102175576;55547112386;14012367600;36025233200;57199396262;57196394775;7501697688;34770229300;57196364795;55460549200;","Dynamic changes in blood cytokine levels as clinical indicators in severe acute respiratory syndrome",2003,"Chinese Medical Journal","116","9",,"1283","1287",,40,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744230802&partnerID=40&md5=3df67ef969cf2b8e14ffe7ac1b29bbbe","Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Beijing Ditan Hospital, Beijing, China","Pang, B.S., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Wang, Z., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Zhang, L.M., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Tong, Z.H., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Xu, L.L., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Huang, X.X., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Guo, W.J., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Zhu, M., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Wang, C., Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; Li, X.W., Beijing Ditan Hospital, Beijing, China; He, Z.P., Beijing Ditan Hospital, Beijing, China; Li, H.X., Beijing Ditan Hospital, Beijing, China; Zhao, F.J., Beijing Ditan Hospital, Beijing, China","Objective. To investigate the dynamic changes observed in serum levels of interleukins (ILs), tumor necrosis factor-α (TNF-α and transforming growth factor-β1 (TGF-β1) in severe acute respiratory syndrome (SARS) patients. Methods. Sixty-one cases of SARS with positive antibodies to SARS coronavirus (SARS-CoV) were classified into the following categories: initial stage (3 - 7 days), peak stage (8 - 14 days), and remission and recovery stage ( 15 - 27 days). Forty-four healthy individuals were used as controls. Serum levels of ILs, TNF-α and TGF-β1 were measured in all subjects. Serum antibodies to SARS-CoV were detected only in SARS cases. Results. The mean concentration of serum IL -6 in SARS patients did not differ from that in the control group in initial and peak stages, but became significantly higher in remission and recovery stage compared with the control group, initial and peak stages ( P &lt; 0.01). The mean concentration of serum IL-8 in SARS patients did not differ from that of the control group in initial stage, but was significantly higher than control group in peak stage and remission and recovery stage ( P &lt; 0.05). And it was more significantly higher in remission and recovery stage than in peak stage ( P &lt; 0.01). The mean concentrations of IL-16 and TNF-α in SARS patients were higher than those of the control group for every length of the clinical courses investigated, and were especially high in remission and recovery stage ( P &lt;0.01 ). SARS patients experienced higher concentration of serum IL-13 compared with the controls in initial stage ( P &lt; 0.01), but returned to normal levels in peak stage and in remission and recovery stage. The mean concentration of serum IL-18 in SARS patients was significantly lower than that of the control group during all clinical courses ( P &lt; 0.05 ). The mean concentration of serum TGF-β1 in SARS patients was higher than that of the control group during all clinical courses. Although TGF-β1 in serum decreased in remission and recovery stage in SARS patients, the average was still higher than that of the control group ( P &lt;0.01 ). Conclusions. Most proinflammatory cytokines and TGF-β1 were elevated during the early phase of SARS, which may be associated with lung infiltration and proliferation. Concurrently, the mean concentration of serum IL-13 decreased gradually, and the mean concentration of serum IL-18 level in SARS patients was lower than that of the control group during all the courses of SARS, suggesting that the immune state of the patients with SARS was obviously abnormal. Observing the dynamic changes in blood cytokine levels can provide a scientific basis to assess pathogenesis and efficacy of clinical treatment of SARS.","Interleukins; Pneumonia; Severe acute respiratory syndrome; Transforming growth factors; Tumor necrosis factors","cytokine; immunoglobulin G; immunoglobulin M; interleukin 13; interleukin 16; interleukin 18; interleukin 6; interleukin 8; transforming growth factor beta1; tumor necrosis factor alpha; virus antibody; adolescent; adult; aged; antibody blood level; article; controlled study; convalescence; Coronavirus; cytokine production; disease classification; disease course; dynamics; female; human; lung infiltrate; major clinical study; male; protein blood level; remission; SARS coronavirus; severe acute respiratory syndrome; statistical significance; virus pathogenesis; virus pneumonia; Adolescent; Adult; Female; Humans; Interleukins; Male; Middle Aged; Severe Acute Respiratory Syndrome; Transforming Growth Factor beta; Tumor Necrosis Factor-alpha","Xiao, Z.L., Li, Y.M., Chen, R.C., A retrospective study of 78 patients with severe acute respiratory syndrome (2003) Chin. Med. J., 116, pp. 805-810; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome(J/OL) (2003) Lancet, 361, pp. 1773-1778; Zhu, Y.J., Chen, W.B., (2003) Respiratory Medicine, pp. 1396-1422. , eds Beijing: People's Medical Publishing House; Serum antibodies detection for serological diagnosis of severe acute respiratory syndrome (2003) Chin. J. Tuberc. Respir. Dis. (Chin.), 26, pp. 339-342. , Beijing Group of National Research Project for SARS; Xu, X.Y., Wang, G.F., Lu, H.Y., Experiences summary in clinical staging and mean treating points of every stage in SARS patients (2003) J. Peking Univ. (Health Sci.) (Chin.), 35, pp. 5-6; Ma, J., Li, N., Kan, C.L., Dynamic observation of the features of chest radiograph in SARS patients (2003) J. Peking Univ. (Health Sci.) (Chin.), 35, pp. 38-40; Zeng, Q.S., Chen, L., Hu, W.Q., Roentgenography and CT appearance in patients with severe acute respiratory syndrome (2003) Chin. J. Tuberc. Respir. Dis. (Chin.), 26, pp. 347-349; Peiris, J.S., Chu, C.M., Cbeng, V.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Liu, L.Y., Sun, B., Peng, S.Y., Changes of IL-6 in acute lung injury caused by endotoxin in rat (1997) Chin. J. Pathophysi. (Chin.), 13, pp. 729-731; Baggiolini, M., Moser, B., Clark-Lawis, I., Interleukin-8 and related chemotactic cytokines (1994) Chest, 105, pp. 95-98; Zhan, X.Q., Wang, Y.M., Yang, Q., Role of cytokines in lung fibrosis caused by asbestos (1999) Foreign Med. Sci.-Section Hygiene (Chin.), 26, pp. 129-131; Jiang, Z.Y., Cao, Y.Y., Lin, C., Effects of TNF-α and IL-10 on cytomegalovirus infection in human embryonic lung fibroblasts (2002) Chin. J. Pathophysio. (Chin.), 18, pp. 265-268; Wang, J.C., Mao, B.L., Qian, G.S., A preliminary study of IL-13 expression in rat lung with acute lung injury (1999) Chin. J. Pathophysio. (Chin.), 15, pp. 1110-1112; Sime, P.J., Marr, R.A., Gavldie, D., Transfer of tumor necrosis factor-α to rat lung induce severe pulmonary inflammation and patchy interstitial fibrogenesis with induction of transforming growth factor-β and myofibroblasts (1998) AM J. Pathol., 153, pp. 825-832","Wang, C.; Beijing Inst. of Respiratory Med., Beijing Chaoyang Hospital, Capital Univ. of Medical Sciences, Beijing 100020, China; email: cwang29@hotmail.com",,,03666999,,CMDJA,"14527349","English","Chin. Med. J.",Article,"Final",,Scopus,2-s2.0-10744230802
"Oragui J.","6602687671;","Viruses in faeces",2003,"Handbook of Water and Wastewater Microbiology",,,,"473","476",,3,"10.1016/B978-012470100-7/50030-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84941138760&doi=10.1016%2fB978-012470100-7%2f50030-3&partnerID=40&md5=0f962f9db7f5a175930b1b160cdbc7e4","Department of Microbiology, Harefield Hospital, Harefield, Middlesex, UB9 6JH, United Kingdom","Oragui, J., Department of Microbiology, Harefield Hospital, Harefield, Middlesex, UB9 6JH, United Kingdom","Enteroviruses, hepatitis A virus, rotaviruses, parvovirus-like viruses, astroviruses, caliciviruses, adenoviruses and coronaviruses can be present in the human excreta. Besides parvovirus-like viruses, other small, rounded viruses can be detected in the fecal samples from patients with acute diarrhoeal disease. These include astroviruses, caliciviruses, and coronaviruses. Viruses may be divided into three main groups: viruses associated with humans, viruses associated with higher plants and animals, and viruses associated with the microbial flora. Excreta is the commonest source for viruses. The consequent dilution of viruses in feces when discharged into the receiving waters or sewage implies that the sample being tested must be concentrated in order to analyze them. The main disinfection processes for the removal of fecal bacteria include chlorination and ozonation. Several factors can explain the viral inactivation in waste stabilization ponds, including solar radiation, temperature, pH, adsorption onto solids, heavy metals, algal and bacterial activity, and the action of certain chemicals-notably ammonia and sulphide. © 2015 Elsevier Ltd All rights reserved.",,,"Berg, G., Removal of viruses from sewage effluents and water: a review (1973) Bull. World Hlth Org., 49, pp. 451-460; Clarke, N.A., Stevensen, R.E., Chang, S.L., Kabler, P.N., Removal of enteric viruses from sewage by activated sludge treatment. (1961) Am. J. Public Hlth, 51, pp. 1118-1129; Kurtz, J.B., Lee, T.W., Pickering, D., Astrovirus associated gastro-enteritis in a children's ward. (1977) J. Clin. Pathol., 30, pp. 948-952; Malina, J.F., Viral pathogen inactivation during treatment of municipal wastewater (1976) Virus Aspects of Applying Municipal Wastes to Land, pp. 9-23. , Centerfor Environmental Programs, University of Florida, Gainesville, L.B. Baldwin, J.M. Davidson, J.R. Gerber (Eds.); McSwiggan, D.A., Cabitt, D., Moore, W., Caliciviruses associated with winter vomiting disease. (1976) Lancet, 1, pp. 1215-1216; Oragui, J.I., Mara, D.D., Simple method for the detoxification of wastewater ultrafiltration concentrates for rotavirus assay by indirect immunofluorescence. (1989) Appl. Environ. Microbiol., 55, pp. 401-405; Oragui, J.I., Mara, D.D., Enumeration of Rota-viruses in Tropical Wastewaters (1996) Research Monographs inTropical Public Health Engineering No. 10, , Universityof Leeds, Leeds; Pearson, H.W., Mara, D.D., Mills, S.W., Smallman, D.J., Physico-chemical parameters influencing faecal bacterial survival in waste stabilisation ponds. (1987) Wat. Sci. Technol., 19, pp. 145-152; Rao, V.C., Lakhe, S.B., Waghmane, S.V., Dube, P., Virus removal in activated sludge treatment. (1977) Prog. Wat. Technol., 9, pp. 113-127; Sherman, V.R., Kawata, K., Oliveris, V.P., Naparstek, J.D., Virus removals in trickling filter plants. (1975) Wat. Sewage Works, 122, pp. R36-R44; Human Viruses in Water, Wastewater and Soil (1979) Technical Report Series No. 639, , World Health Organization, Geneva","Oragui, J.; Department of Microbiology, Harefield HospitalUnited Kingdom",,"Elsevier Inc.",,9780080478197; 9780124701007,,,"English","Handb. of Water and Wastewater Microbiol.",Book Chapter,"Final",,Scopus,2-s2.0-84941138760
[No author name available],[No author id available],"Articles selected by Faculty of 1000: Identifying antigens involved in autoimmune response; statistics in genomics; mouse full-length cDNA encylopedia; screen for Drosophila neural development genes; proteome of SARS-coronavirus",2003,"Genome Biology","4","10", 343,"","",,,"10.1186/gb-2003-4-10-343","https://www.scopus.com/inward/record.uri?eid=2-s2.0-84974623035&doi=10.1186%2fgb-2003-4-10-343&partnerID=40&md5=c24c7cf589c175b723b0a8eace2b16b4",,"","A selection of evaluations from Faculty of 1000 covering the identification of antigens involved in an autoimmune reseponse, the difference between false positive and false discovery rate, a mouse full-length cDNA encylopedia, analysis of bristle number in Drosophila mutants to identify neural development genes and an analysis of the proteome of SARS-coronavirus. © 2003 BioMed Central Ltd.",,"antigen; complementary DNA; DNA vaccine; proteome; transcriptome; allergic encephalomyelitis; Article; autoimmunity; Drosophila; gene identification; gene mutation; gene targeting; immune response; nerve cell differentiation; nonhuman; protein microarray; quantitative analysis; SARS coronavirus",,,,"BioMed Central Ltd.",14747596,,GNBLF,,"English","Genome Biol.",Article,"Final",Open Access,Scopus,2-s2.0-84974623035
"Ng W.T., Turinici G., Danchin A.","7402229732;55928871000;7103235597;","A double epidemic model for the SARS propagation",2003,"BMC Infectious Diseases","3",, 19,"","",,34,"10.1186/1471-2334-3-19","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2442704222&doi=10.1186%2f1471-2334-3-19&partnerID=40&md5=ca7b0eb441241a1fe322d7819bc7ee17","Department of Mathematics, The University of Hong Kong, Hong Kong, Hong Kong; Inria Rocquencourt Domaine Voluceau, Rocquencourt, France; Ctr. d'Enseignement Recherche Math., Info./Calcul Scientifique-ENPC, Marne La Vallée, France; Genetique des Genomes Bacteriens, Institut Pasteur, Paris, France","Ng, W.T., Department of Mathematics, The University of Hong Kong, Hong Kong, Hong Kong; Turinici, G., Inria Rocquencourt Domaine Voluceau, Rocquencourt, France, Ctr. d'Enseignement Recherche Math., Info./Calcul Scientifique-ENPC, Marne La Vallée, France; Danchin, A., Genetique des Genomes Bacteriens, Institut Pasteur, Paris, France","Background: An epidemic of a Severe Acute Respiratory Syndrome (SARS) caused by a new coronavirus has spread from the Guangdong province to the rest of China and to the world, with a puzzling contagion behavior. It is important both for predicting the future of the present outbreak and for implementing effective prophylactic measures, to identify the causes of this behavior. Results: In this report, we show first that the standard Susceptible-Infected-Removed (SIR) model cannot account for the patterns observed in various regions where the disease spread. We develop a model involving two superimposed epidemics to study the recent spread of the SARS in Hong Kong and in the region. We explore the situation where these epidemics may be caused either by a virus and one or several mutants that changed its tropism, or by two unrelated viruses. This has important consequences for the future: the innocuous epidemic might still be there and generate, from time to time, variants that would have properties similar to those of SARS. Conclusion: We find that, in order to reconcile the existing data and the spread of the disease, it is convenient to suggest that a first milder outbreak protected against the SARS. Regions that had not seen the first epidemic, or that were affected simultaneously with the SARS suffered much more, with a very high percentage of persons affected. We also find regions where the data appear to be inconsistent, suggesting that they are incomplete or do not reflect an appropriate identification of SARS patients. Finally, we could, within the framework of the model, fix limits to the future development of the epidemic, allowing us to identify landmarks that may be useful to set up a monitoring system to follow the evolution of the epidemic. The model also suggests that there might exist a SARS precursor in a large reservoir, prompting for implementation of precautionary measures when the weather cools down. © 2003 Ng et al; licensee BioMed Central Ltd.",,"analytical parameters; article; China; epidemic; Hong Kong; human; mutant; population research; prevalence; SARS coronavirus; severe acute respiratory syndrome; statistical analysis; statistical model; strain difference; virus mutation","Rasschaert, D., Duarte, M., Laude, H., Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions (1990) J. Gen. Virol., 71 (PART 11), pp. 2599-2607; Compton, S.R., Barthold, S.W., Smith, A.L., The cellular and molecular pathogenesis of coronaviruses (1993) Lab. Anim. Sci., 43, pp. 15-28; Haijema, B.J., Volders, H., Rottier, P.J., Switching species tropism: An effective way to manipulate the feline coronavirus genome (2003) J. Virol., 77, pp. 4528-4538; Enjuanes, L., Sanchez, C., Gebauer, F., Mendez, A., Dopazo, J., Ballesteros, M.L., Evolution and tropism of transmissible gastroenteritis coronavirus (1993) Adv. Exp. Med. Biol., 342, pp. 35-42; Ballesteros, M.L., Sanchez, C.M., Martin-Caballero, J., Enjuanes, L., Molecular bases of tropism in the PUR46 cluster of transmissible gastroenteritis coronaviruses (1995) Adv. Exp. Med. Biol., 380, pp. 557-562; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; Anderson, R., May, R., Infectious diseases in humans (1991), Oxford, Oxford University Press; Murray, J.D., (1993) Mathematical Biology, , 2nd edition. Berlin, Springer Verlag; Bailey, N.J.T., (1975) The Mathematical Theory of Infectious Diseases and Its Applications, , London, Griffin; Garwes, D.J., Transmissible gastroenteritis (1988) Vet. Rec., 122, pp. 462-463; Brauer, F., Castillo-Chavez, C., (2001) Mathematical Models in Population Biology and Epidemiology, , Berlin, Springer Verlag; Anderson, H., Britton, T., (2000) Stochastic Epidemic Models and Their Statistical Analysis. Lecture Notes in Statistics, 151. , New York, Springer; Diekmann, O., Heesterbeek, J., (2000) Mathematical Epidemiology of Infectious Disease, , Wiley Series in Mathematical and Computational Biology Chichester, Wiley; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Laude, H., Rasschaert, D., Delmas, B., Eleouët, J.-F., Le coronavirus respiratoire porcin PRCV : Un virus émergent pas comme les autres (1998) Virologie, 2, pp. 305-316; Saif, L.J., van Cott, J.L., Brim, T.A., Immunity to transmissible gastroenteritis virus and porcine respiratory coronavirus infections in swine (1994) Vet. Immunol. Immunopathol., 43, pp. 89-97; Hethcote, H.W., The Mathematics of Infectious Diseases (2000) SIAM Review, 42, pp. 599-653; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, L.J., Anderson, R.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766","Ng, W.T.; Department of Mathematics, The University of Hong Kong, Hong Kong, Hong Kong; email: ntw@maths.hku.hk",,"BioMed Central Ltd.",14712334,,BIDMB,"12964944","English","BMC Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-2442704222
"Lin M., Tseng H.-K., Trejaut J.A., Lee H.-L., Loo J.-H., Chu C.-C., Chen P.-J., Su Y.-W., Lim K.H., Tsai Z.-U., Lin R.-Y., Lin R.-S., Huang C.-H.","25822567800;24476761800;6701579035;35310957000;7006904485;55608553800;56140665300;8501372200;7403174490;7005034057;55213772400;7402887908;57212179893;","Association of HLA class I with severe acute respiratory syndrome coronavirus infection",2003,"BMC Medical Genetics","4",, 9,"","",,75,"10.1186/1471-2350-4-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-2542493298&doi=10.1186%2f1471-2350-4-9&partnerID=40&md5=731c5e4929667cebb01570a10603dcd2","Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan; Taipei Municipal Hoping Hospital, Taipei, Taiwan; Institute of Preventive Medicine, National Taiwan University, Taipei, Taiwan; Mackay Memorial Hospital, Taipei, Taiwan","Lin, M., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Tseng, H.-K., Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan; Trejaut, J.A., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Lee, H.-L., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Loo, J.-H., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Chu, C.-C., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Chen, P.-J., Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan; Su, Y.-W., Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan; Lim, K.H., Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan; Tsai, Z.-U., Transfusion Medicine Laboratory, Mackay Memorial Hospital, Taipei, Taiwan; Lin, R.-Y., Taipei Municipal Hoping Hospital, Taipei, Taiwan; Lin, R.-S., Institute of Preventive Medicine, National Taiwan University, Taipei, Taiwan; Huang, C.-H., Mackay Memorial Hospital, Taipei, Taiwan","Background: The human leukocyte antigen (HLA) system is widely used as a strategy in the search for the etiology of infectious diseases and autoimmune disorders. During the Taiwan epidemic of severe acute respiratory syndrome (SARS), many health care workers were infected. In an effort to establish a screening program for high risk personal, the distribution of HLA class I and II alleles in case and control groups was examined for the presence of an association to a genetic susceptibly or resistance to SARS coronavirus infection. Methods: HLA-class I and II allele typing by PCR-SSOP was performed on 37 cases of probable SARS, 28 fever patients excluded later as probable SARS, and 101 non-infected health care workers who were exposed or possibly exposed to SARS coronavirus. An additional control set of 190 normal healthy unrelated Taiwanese was also used in the analysis. Results: Woolf and Haldane Odds ratio (OR) and corrected P-value (Pc) obtained from two tails Fisher exact test were used to show susceptibility of HLA class I or class II alleles with coronavirus infection. At first, when analyzing infected SARS patients and high risk health care workers groups, HLA-B*4601 (OR = 2.08, P = 0.04, Pc = n.s.) and HLA-B*5401 (OR = 5.44, P = 0.02, Pc = n.s.) appeared as the most probable elements that may be favoring SARS coronavirus infection. After selecting only a ""severe cases"" patient group from the infected ""probable SARS"" patient group and comparing them with the high risk health care workers group, the severity of SARS was shown to be significantly associated with HLA-B*4601 (P = 0.0008 or Pc = 0.0279). Conclusions: Densely populated regions with genetically related southern Asian populations appear to be more affected by the spreading of SARS infection. Up until recently, no probable SARS patients were reported among Taiwan indigenous peoples who are genetically distinct from the Taiwanese general population, have no HLA-B* 4601 and have high frequency of HLA-B"" 1301. While increase of HLA-B* 4601 allele frequency was observed in the "" Probable SARS infected"" patient group, a further significant increase of the allele was seen in the ""Severe cases"" patient group. These results appeared to indicate association of HLA-B* 4601 with the severity of SARS infection in Asian populations. Independent studies are needed to test these results. © 2003 Lin et al; licensee BioMed Central Ltd.",,"DNA; HLA antigen; HLA antigen class 1; HLA antigen class 2; HLA B antigen; HLA A antigen; HLA antigen class 1; HLA B antigen; HLA B*46:01 antigen; HLA DR antigen; HLA DRB1 antigen; HLA-B*46:01 antigen; adult; aged; allele; article; autoimmune disease; clinical article; controlled study; disease severity; disease transmission; DNA probe; epidemic; exposure; female; Fisher exact test; gene frequency; genetic association; genetic difference; genetic susceptibility; health care personnel; high risk patient; human; human cell; infection resistance; male; native species; pathogenesis; polymerase chain reaction; population density; probability; SARS coronavirus; screening test; severe acute respiratory syndrome; South Asia; Taiwan; comparative study; genetic screening; genetics; histocompatibility test; immunology; innate immunity; methodology; middle aged; risk; severe acute respiratory syndrome; Coronavirus; Martes pennanti; SARS coronavirus; Adult; Aged; Aged, 80 and over; Alleles; Female; Gene Frequency; Genetic Testing; Histocompatibility Antigens Class I; Histocompatibility Testing; HLA-A Antigens; HLA-B Antigens; HLA-DR Antigens; HLA-DRB1 Chains; Humans; Immunity, Innate; Male; Middle Aged; Odds Ratio; Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome; Taiwan","(2003), http://www.who.int/csr/sars/casedefinition/en/print.html, Case definition for surveillance of severe acute respiratory syndrome (SARS) Geneva: World Health Organization Accessed June 2; Twu, S.-J., Chen, T.-J., Chen, C.-J., Olsen, S.-J., Lee, L.-T., Fisk, T., Hsu, K.-H., Chiang, I.-H., Control measures for severe acute respiratory syndrome (SARS) in Taiwan (2003) Emerg. Infect. Dis., 9, pp. 718-720; Lin, M., Chu, C.-C., Chang, S.-L., Lee, H.-L., Loo, J.-H., Akaza, T., Juji, T., Tokunaga, K., The origin of Minnan and Hakka, the socalled ""Taiwanese"", inferred by HLA study (2001) Tissue Antigens, 57, pp. 192-199; Haldane, J.B.S., The estimation and significance of the logarithm of a ratio of frequencies (1956) Ann. Hum. Genet., 20, pp. 309-311; Woolf, B., On estimating the relation between blood group and disease (1955) Ann. Hum. Genet., 19, pp. 251-253; Fisher, R.A., Statistical methods for research worker (1958), Edinburg: Oliver and Boyd; Edward, J.H., HLA and disease, the detection of associations (1974) Immunogenet, 1, pp. 249-257; Marsh, S.G.E., Albert, E.D., Bodmer, W.F., Bontrop, R.E., Dupont, B., Erlich, H.A., Gerahty, D.E., Mayr, W.R., Nomenclature for factors of the HLA system, 2002 (2002) Tissue Antigens, 60, pp. 407-464; Lin, M., Chu, C.C., Lee, H.L., Chang, S.L., Ohashi, J., Tokunaga, K., Akaza, T., Juji, T., Heterogeneity of Taiwan's indigenous population: Possible relation to prehistoric mongoloid dispersals (2000) Tissue Antigens, 55, pp. 1-9; De Vries, R.R.P., Meera Khan, V.P., Bernini, L.F., van Loghem, E., van Rood, J.J., Genetic control of survival in epidemics (1979) J. Immunogenet., 6, pp. 271-287; Hill, A.V.S., The immunogenetics of human infectious disease (1998) Annu. Rev. Immunol., 16, pp. 593-617; Liu, C., Carrington, M., Kaslow, R.A., Gao, X., Rinaldo, C.R., Jacobson, L.P., Margolick, J.B., Detels, R., Association of polymorphisms in human leukocyte antigen class I and transporter associated with antigen processing genes with resistance to human immunodeficiency virus type 1 infection (2003) J. Infect. Dis., 187, pp. 1404-1410; Stephen, H.A., Klaythong, R., Sirikong, M., Vaughn, D.W., Green, S., Kalayanarooj, S., Endy, T.P., Innis, B.L., HLA-A and B allele associations with secondary dengue virus infections correlate with disease severity and the infecting viral serotype in ethnic Thais (2002) Tissue Antigens, 60, pp. 309-318; Collins, A.R., Human coronavirus OC43 interacts with major histocompatibility complex class I molecules at the cell surface to establish infection (1994) Immunol. Invest., 23, pp. 313-321; Meachem, W., Origins and development of the Yueh coastal Neolithic: A microcosm of culture change of the mainland of East Asia (1981) The Origins of Chinese Civilization, pp. 147-175. , Edited by: Keightly DK. Berkeley, CA: University of California Press; Chen, R.B., Ye, G.Y., Geng, Z.C., Wang, Z.H., Kong, F.H., Tian, D., Bao, P.Y., Song, F.J., HLA polymorphism of the principal minorities, in mainland China (1992) HLA 1991. Proceedings of the 11th International Histocompatibility Workshop and Conference, 1, pp. 676-679. , Edited by: Tsuji K, Aizawa M, Sasazuki T. Oxford, England: Oxford University Press; CDC: Update: Severe Acute Respiratory Syndrome - United States, 2003 (2003) MMWR, 52, pp. 388-390. , http://www.cdc.gov/mmwr/preview/mmwrhtml/mm5228a4.html, Available at; Imanishi, T., Akaza, T., Kimura, A., Tokunaga, K., Gojobori, T., Allele and haplotype frequencies for HLA and complement loci in various ethnic groups (1992) HLA 1991. Proceedings of the 11th International Histocompatibility Workshop and Conference, 1, pp. 1065-1220. , Edited by: Tsuji K, Aizawa M, Sasazuki T. Oxford, England: Oxford University Press; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W., Wang, T., Chan-Yeung, M., Lam, W.K., Cheung, T.M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985","Huang, C.-H.; Mackay Memorial Hospital, Taipei, Taiwan; email: chhuang@ms2.mmh.org.tw",,,14712350,,BMGMA,"12969506","English","BMC Med. Genet.",Article,"Final",Open Access,Scopus,2-s2.0-2542493298
"O'donnell R., Tasker R.C., Roe M.F.E.","36662861600;7102106496;7102041518;","SARS: Understanding the coronavirus",2003,"BMJ","327","7415",,"620","",,26,"10.1136/bmj.327.7415.620-b","https://www.scopus.com/inward/record.uri?eid=2-s2.0-85007713256&doi=10.1136%2fbmj.327.7415.620-b&partnerID=40&md5=f6428084a5330b68752596c7d7be471a","Clinical School, University of Cambridge, Cambridge CB2 2QQ, United Kingdom","O'donnell, R., Clinical School, University of Cambridge, Cambridge CB2 2QQ, United Kingdom; Tasker, R.C., Clinical School, University of Cambridge, Cambridge CB2 2QQ, United Kingdom; Roe, M.F.E., Clinical School, University of Cambridge, Cambridge CB2 2QQ, United Kingdom",[No abstract available],,,"Wong, R.S., Wu, A., To, K.F., Lee, N., Lam, C.W., Wong, C.K., Haematological manifestations in patients with severe acute respiratory syndrome: retrospective analysis (2003) BMJ, 326, pp. 1358-1362. , (21 June.); Panesar, N.S., Lymphopenia in SARS (2003) Lancet, 361, p. 1985; O'Donnell, D.R., Carrington, D., Peripheral blood lymphopenia and neutrophilia in children with severe respiratory syncytial virus disease (2002) Pediatr Pulmonol, 34, pp. 128-130; Openshaw, P.J., Immunopathological mechanisms in respiratory syncytial virus disease (1995) Springer Semin Immunopathol, 17, pp. 187-201; Hotchkiss, R.S., Chang, K.C., Swanson, P.E., Tinsley, K.W., Hui, J.J., Klender, P., Caspase inhibitors improve survival in sepsis: a critical role of the lymphocyte (2000) Nat Immunol, 1, pp. 496-501",,,,09598138,,,"12969939","English","BMJ",Letter,"Final",,Scopus,2-s2.0-85007713256
"Tambyah P.A., Singh K.S., Habib A.G.","35499886400;34868723700;57213632439;","SARS: Understanding the coronavirus",2003,"BMJ","327","7415",,"620","",,16,"10.1136/bmj.327.7415.620-a","https://www.scopus.com/inward/record.uri?eid=2-s2.0-85007699098&doi=10.1136%2fbmj.327.7415.620-a&partnerID=40&md5=f30054dd48a7c72cdcca246edc23804b","National University of Singapore, National University Hospital, 5 Lower Kent Ridge Road, 119074, Singapore","Tambyah, P.A., National University of Singapore, National University Hospital, 5 Lower Kent Ridge Road, 119074, Singapore; Singh, K.S., National University of Singapore, National University Hospital, 5 Lower Kent Ridge Road, 119074, Singapore; Habib, A.G., National University of Singapore, National University Hospital, 5 Lower Kent Ridge Road, 119074, Singapore",[No abstract available],,"antivirus agent; glucocorticoid; ribavirin; apoptosis; clinical feature; Coronavirus; diagnostic test; epidemic; human; letter; lymphocytopenia; nonhuman; patient monitoring; priority journal; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; virus pneumonia; world health organization","Rainer, T.H., Cameron, P.A., DeVilliers, S., Ong, K.L., Ng, A.W.H., Chan, D.P.N., Evaluation of WHO criteria for identifying patients with severe acute respiratory syndrome out of hospital (2003) BMJ, 326, pp. 1354-1358. , (21 June.); Fisher, D.A., Lim, T.K., Lim, Y.T., Singh, K.S., Tambyah, P.A., Atypical presentations of SARS (2003) Lancet, 361, p. 1740",,,,09598138,,,"12969941","English","BMJ",Letter,"Final",,Scopus,2-s2.0-85007699098
"Yap Y.L., Zhang X.W., Danchin A.","7005551975;57192503733;7103235597;","Relationship of SARS-CoV to other pathogenic RNA viruses explored by tetranucleotide usage profiling",2003,"BMC Bioinformatics","4",, 43,"","",17,15,"10.1186/1471-2105-4-43","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642367621&doi=10.1186%2f1471-2105-4-43&partnerID=40&md5=f565882855177d6437924b8664c57673","HKU-Pasteur Research Centre, 8 Sassoon Road, Pokfulam, Hong Kong; Institute Pasteur, Unite Genet. des Genomes Bacteriens, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France","Yap, Y.L., HKU-Pasteur Research Centre, 8 Sassoon Road, Pokfulam, Hong Kong; Zhang, X.W., HKU-Pasteur Research Centre, 8 Sassoon Road, Pokfulam, Hong Kong; Danchin, A., Institute Pasteur, Unite Genet. des Genomes Bacteriens, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France","Background: The exact origin of the cause of the Severe Acute Respiratory Syndrome (SARS) is still an open question. The genomic sequence relationship of SARS-CoV with 30 different single-stranded RNA (ssRNA) viruses of various families was studied using two non-standard approaches. Both approaches began with the vectorial profiling of the tetra-nucleotide usage pattern V for each virus. In approach one, a distance measure of a vector V, based on correlation coefficient was devised to construct a relationship tree by the neighbor-joining algorithm. In approach two, a multivariate factor analysis was performed to derive the embedded tetra-nucleotide usage patterns. These patterns were subsequently used to classify the selected viruses. Results: Both approaches yielded relationship outcomes that are consistent with the known virus classification. They also indicated that the genome of RNA viruses from the same family conform to a specific pattern of word usage. Based on the correlation of the overall tetra-nucleotide usage patterns, the Transmissible Gastroenteritis Virus (TGV) and the Feline CoronaVirus (FCoV) are closest to SARS-CoV. Surprisingly also, the RNA viruses that do not go through a DNA stage displayed a remarkable discrimination against the CpG and UpA di-nucleotide (z = -77.31, -52.48 respectively) and selection for UpG and CpA (z = 65.79,49.99 respectively). Potential factors influencing these biases are discussed. Conclusion: The study of genomic word usage is a powerful method to classify RNA viruses. The congruence of the relationship outcomes with the known classification indicates that there exist phylogenetic signals in the tetra-nucleotide usage patterns, that is most prominent in the replicase open reading frames. © 2003 Yap et al; licensee BioMed Central Ltd.","Convergent evolution; Factor analysis; Horizontal gene transfer; RNA virus; SARS","nucleotide; virus DNA; virus RNA; virus vector; microsatellite DNA; virus RNA; article; classification; computer program; computer system; controlled study; correlation coefficient; gene expression profiling; gene sequence; genetic algorithm; genome analysis; mathematical computing; multivariate analysis; nonhuman; nucleotide sequence; open reading frame; phylogeny; RNA virus; SARS coronavirus; Transmissible gastroenteritis virus; virus virulence; algorithm; animal; biosynthesis; Calicivirus; cattle; comparative study; Coronavirus; dinucleotide repeat; gene expression profiling; gene expression regulation; genetics; human; methodology; pathogenicity; rabbit; statistics; virus genome; Coronavirus; Felidae; Feline coronavirus; RNA viruses; Transmissible gastroenteritis virus; Algorithms; Animals; Cattle; Coronavirus 229E, Human; Coronavirus, Bovine; Dinucleotide Repeats; Gene Expression Profiling; Gene Expression Regulation, Viral; Genome, Viral; Hemorrhagic Disease Virus, Rabbit; Humans; Microsatellite Repeats; Multivariate Analysis; Open Reading Frames; Phylogeny; Rabbits; RNA Viruses; RNA, Viral; SARS Virus","Cumulative Number of Reported Probable Cases of SARS http://www.who.int/csr/sarscountry/en; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423 (6937), p. 240; Hoey, J., Maskalyk, J., SARS update (2003) CMAJ, 168 (10), pp. 1294-1295; James, J.S., SARS Web information (2003) AIDS Treat. News, p. 6; Situation Updates - SARS http://www.who.int/csr/sars/archive/en; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a Novel CoronaVirus in Patients with Severe Acute Respiratory Syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1967-1976; Van Vugt, J.J., Storgaard, T., Oleksiewicz, M.B., Botner, A., High frequency RNA recombination in porcine reproductive and respiratory syndrome virus occurs preferentially between parental sequences with high similarity (2001) J. Gen. Virol., 82 (PART 11), pp. 2615-2620; Lerner, D.L., Wagaman, P.C., Phillips, T.R., Prospero-Garcia, O., Henriksen, S.J., Fox, H.S., Bloom, F.E., Elder, J.H., Increased mutation frequency of feline immunodeficiency virus lacking functional deoxyuridine-triphosphatase (1995) Proc. Natl. Acad. Sci. USA, 92 (16), pp. 7480-7484. , Aug 1; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The Genome Sequence of the SARS-Associated CoronaVirus (2003) Science, 300 (5624), pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a Novel CoronaVirus Associated with Severe Acute Respiratory Syndrome (2003) Science, 300 (5624), pp. 1394-1399; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A Novel CoronaVirus Associated with Severe Acute Respiratory Syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Hacker, J., Carniel, E., Ecological fitness, genomic islands and bacterial pathogenicity. A Darwinian view of the evolution of microbes (2001) EMBO Rep., 2 (5), pp. 376-381; van Hemert, F.J., Berkhout, B., The tendency of lentiviral open reading frames to become A-rich: Constraints imposed by viral genome organization and cellular tRNA availability (1995) J. Mol. Evol., 41 (2), pp. 132-140; Hubacek, J., Biological function of DNA methylation (1992) Folia Microbiol. (Praha), 37 (5), pp. 323-329; Karlin, S., Doerfler, W., Cardon, L.R., Why is CpG suppressed in the genomes of virtually all small eukaryotic viruses but not in those of large eukaryotic viruses? (1994) J. Virol., 68 (5), pp. 2889-2897; Gantt, R.R., Stromberg, K.J., Montes de Oca, F., Specific RNA methylase associated with avian myeloblastosis virus (1971) Nature, 234, pp. 35-37; Frederico, L.A., Kunkel, T.A., Shaw, B.R., A sensitive genetic assay for the detection of cytosine deamination: Determination of rate constants and the activation energy (2001) Biochemistry, 29 (10), pp. 2532-2537; Bibillo, A., Figlerowicz, M., Ziomek, K., Kierzek, R., The nonenzymatic hydrolysis of oligoribonucleotides. VII. Structural elements affecting hydrolysis (2000) Nucleosides Nucleotides Nucleic Acids, 19 (5-6), pp. 977-994; Beutler, E., Gelbart, T., Han, J.H., Koziol, J.A., Beutler, B., Evolution of the genome and the genetic code: Selection at the dinucleotide level by methylation and polyribonucleotide cleavage (1989) Proc. Natl. Acad. Sci. USA, 86 (1), pp. 192-196; Regenmortel, M.H.V., van Fauquet, C.M., Bishop, D.H.L., Carstens, E.B., Estes, M.K., Lemon, S.M., Maniloff, J., Wickner, R.B., (2000) Virus Taxonomy: Classification and Nomenclature of Viruses. Seventh Report of the International Committee on Taxonomy of Viruses, , Academic Press, San Diego; Bartholomew, D.J., Factor Analysis for Categorical Data (1980) Journal of the Royal Statistical Society. Series B (Methodological), 42 (3), pp. 293-321; Kim, J., Mueller Charles, W., (1978) Introduction to Factor Analysis: What it Is and How to Do It, , Newbury Park, CA: Sage Publications; Bartholomew, D.J., Factor Analysis for Categorical Data (1980) Journal of the Royal Statistical Society. Series B (Methodological), 42 (3), pp. 293-321; Ewens, W.J., Grant, G.R., (2001) Statistical Methods in Bioinformatics, , Springer- Verlag New York, Inc., New York; Bronson, E.C., Anderson, J.N., Nucleotide composition as a driving force in the evolution of retroviruses (1994) J. Mol. Evol., 38 (5), pp. 506-532; Rocha, E.P., Viari, A., Danchin, A., Oligo-nucleotide bias in Bacillus subtilis: General trends and taxonomic comparisons (1998) Nucleic Acids Res., 26 (12), pp. 2971-2980; Leung, M.Y., Marsh, G.M., Speed, T.P., Over- and underrepresentation of short DNA words in herpesvirus genomes (1996) J. Comput. Biol., 3 (3), pp. 345-360; Schbath, S., Prum, B., de Turckheim, E., Exceptional motifs in different Markov chain models for a statistical analysis of DNA sequences (1995) J. Comput. Biol., 2 (3), pp. 417-437; Saitou, N., Nei, M., The neighbor-joining method: A new method for reconstructing trees (1987) Mol. Biol. and Evol., 4, pp. 406-425","Yap, Y.L.; HKU-Pasteur Research Centre, 8 Sassoon Road Pokfulam, Pokfulam, Hong Kong; email: daniely@hkusua.hku.hk",,,14712105,,BBMIC,"14499005","English","BMC Bioinform.",Article,"Final",Open Access,Scopus,2-s2.0-0642367621
"Kliger Y., Levanon E.Y.","6602348305;6602843144;","Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy",2003,"BMC Microbiology","3",, 1,"1","7",,33,"10.1186/1471-2180-3-20","https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042845376&doi=10.1186%2f1471-2180-3-20&partnerID=40&md5=7ac6cc6147efe0f63c1633c2a38b8c7e","Compugen Ltd., Tel Aviv, 69512, Israel","Kliger, Y., Compugen Ltd., Tel Aviv, 69512, Israel; Levanon, E.Y., Compugen Ltd., Tel Aviv, 69512, Israel","Background: Severe acute respiratory syndrome (SARS) is a febrile respiratory illness. The disease has been etiologically linked to a novel coronavirus that has been named the SARS-associated coronavirus (SARS-CoV), whose genome was recently sequenced. Since it is a member of the Coronaviridae, its spike protein (S2) is believed to play a central role in viral entry by facilitating fusion between the viral and host cell membranes. The protein responsible for viral-induced membrane fusion of HIV-1 (gp41) differs in length, and has no sequence homology with S2. Results: Sequence analysis reveals that the two viral proteins share the sequence motifs that construct their active conformation. These include (1) an N-terminal leucine/isoleucine zipper-like sequence, and (2) a C-terminal heptad repeat located upstream of (3) an aromatic residue-rich region juxtaposed to the (4) transmembrane segment. Conclusions: This study points to a similar mode of action for the two viral proteins, suggesting that anti-viral strategy that targets the viral-induced membrane fusion step can be adopted from HIV-1 to SARS-CoV. Recently the FDA approved Enfuvirtide, a synthetic peptide corresponding to the C-terminal heptad repeat of HIV-1 gp41, as an anti-AIDS agent. Enfuvirtide and C34, another anti HIV-1 peptide, exert their inhibitory activity by binding to a leucine/isoleucine zipper-like sequence in gp41, thus inhibiting a conformational change of gp41 required for its activation. We suggest that peptides corresponding to the C-terminal heptad repeat of the S2 protein may serve as inhibitors for SARS-CoV entry.",,"anti human immunodeficiency virus agent; c 34; coronavirus s2 protein; enfuvirtide; glycoprotein gp 41; leucine zipper protein; unclassified drug; virus protein; anti human immunodeficiency virus agent; antivirus agent; glycoprotein gp 41; peptide C34; peptide fragment; virus fusion protein; amino acid composition; amino terminal sequence; article; carboxy terminal sequence; Human immunodeficiency virus 1; membrane fusion; nonhuman; protein motif; protein tertiary structure; SARS coronavirus; sequence analysis; sequence homology; chemistry; drug design; drug effect; genetics; metabolism; molecular genetics; protein conformation; Coronaviridae; Coronavirus; Human immunodeficiency virus; Human immunodeficiency virus 1; SARS coronavirus; Anti-HIV Agents; Antiviral Agents; Drug Design; HIV Envelope Protein gp41; HIV-1; Molecular Sequence Data; Peptide Fragments; Protein Conformation; SARS Virus; Viral Fusion Proteins","Chan, D.C., Fass, D., Berger, J.M., Kim, P.S., Core structure of gp41 from the HIV envelope glycoprotein (1997) Cell, 89, pp. 263-273; Weissenhorn, W., Dessen, A., Harrison, S.C., Skehel, J.J., Wiley, D.C., Atomic structure of the ectodomain from HIV-1 gp41 (1997) Nature, 387, pp. 426-430; Lu, M., Blacklow, S.C., Kim, P.S., A trimeric structural domain of the HIV-1 transmembrane glycoprotein (1995) Nat Struct Biol, 2, pp. 1075-1082; Salzwedel, K., West, J.T., Hunter, E., A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity (1999) J Virol, 73, pp. 2469-2480; LaBonte, J., Lebbos, J., Kirkpatrick, P., Enfuvirtide (2003) Nature Reviews Drug Discovery, 2, p. 345; Chan, D.C., Kim, P.S., HIV entry and its inhibition (1998) Cell, 93, pp. 681-684; Lambert, D.M., Barney, S., Lambert, A.L., Guthrie, K., Medinas, R., Davis, D.E., Bucy, T., Petteway Jr., S.R., Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion (1996) Proc Natl Acad Sci U S A, 93, pp. 2186-2191; 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Tusnady, G.E., Simon, I., The HMMTOP transmembrane topology prediction server (2001) Bioinformatics, 17, pp. 849-850; Wild, C., Greenwell, T., Matthews, T., A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion (1993) AIDS Res Hum Retroviruses, 9, pp. 1051-1053; Chan, D.C., Chutkowski, C.T., Kim, P.S., Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target (1998) Proc Natl Acad Sci U S A, 95, pp. 15613-15617; Xu, Y., Zhang, X., Matsuoka, M., Hattori, T., The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41 (2000) FEBS Lett, 487, pp. 185-188; Kliger, Y., Gallo, S.A., Peisajovich, S.G., Munoz-Barroso, I., Avkin, S., Blumenthal, R., Shai, Y., Mode of action of an antiviral peptide from HIV-1. 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"Wang C.-Z., Chi C.-W.","55766575500;7401898801;","The biological characteristics of SARS virus and its related coronaviruses",2003,"Acta Biochimica et Biophysica Sinica","35","6",,"495","502",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0041885129&partnerID=40&md5=61e21b3fbc8d304f1e58e69134de053e","Inst. of Biochem. and Cell Biology, Shanghai Inst. of Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Dept. of Biochem./Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, China","Wang, C.-Z., Inst. of Biochem. and Cell Biology, Shanghai Inst. of Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China, Dept. of Biochem./Molecular Biology, Shanghai Medical College, Fudan University, Shanghai 200032, China; Chi, C.-W., Inst. of Biochem. and Cell Biology, Shanghai Inst. of Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China","Cases of the life-threatening respiratory disease with no identified cause (designated as ""severe acute respiratory syndrome"", SARS, in March 2003) were first reported in late 2002 from Guangdong Province, China; they were followed by reports from about other 30 countries (or regions) such as Vietnam, Singapore, Thailand, Hong Kong (China), Canada, and USA etc. Because of its ongoing epidemic and high death rate, SARS has shined an intense spotlight all over the world. The World Health Organization (WHO) has promptly established a network of international laboratories consisting of 13 members around the 10 countries to facilitate the identification of the causative agent of SARS. A novel coronavirus, SARS vires, fulfilling all of Koch's postulates was announced to be the primary aetiological agent of SARS on April 16 by WHO shortly after the Canadian scientists released the full-length genome sequence of SARS virus (Tor2) on April 12. China is now facing a formidable task to fight SAPS. In this article, we present a brief summary on the biological characteristics of coronavirus with its associated diseases, and make some suggestions on how to curb this outbreak and how to cure SARS disease based on the potential targets of this novel virus.","Atypical pneumonia; Biological characteristic; Coronavirus; SARS; Treatment; Virus","Coronavirus; disease association; disease classification; epidemic; infection prevention; mortality; nonhuman; severe acute respiratory distress syndrome; short survey; upper respiratory tract infection; virus activation; virus genome; virus identification; virus pneumonia; world health organization; Animals; Antiviral Agents; Coronavirus; Far East; Gene Expression Regulation, Viral; Genome, Viral; Humans; Ribavirin; RNA, Messenger; SARS Virus; Severe Acute Respiratory Syndrome; Viral Structural Proteins; Coronavirus; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 1967-1976; 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(2003) Trends Mol Med, 9 (2), pp. 46-52","Chi, C.-W.; Inst. of Biochem. and Cell Biology, Shanghai Inst. of Biol. Sciences, Chinese Academy of Sciences, Shanghai 200031, China; email: chi@sunm.shcnc.ac.cn",,,05829879,,,"12796808","Chinese","Acta Biochim. Biophys. Sin.",Short Survey,"Final",,Scopus,2-s2.0-0041885129
"Zhang Q.-F., Cui J.-M., Huang X.-J., Lin W., Tan D.-Y., Xu J.-W., Yang Y.-F., Zhang J.-Q., Zhang X., Li H., Zheng H.-Y., Chen Q.-X., Yan X.-G., Zheng K., Wan Z.-Y., Huang J.-C.","8279516600;7401811280;7410248097;57198651727;36914352600;37125748200;56071961200;8629974500;35224294000;56986831800;7403441204;7406336372;8066291300;25937079000;8066291500;8066291600;","Morphology and morphogenesis of severe acute respiratory syndrome (SARS)-associated virus",2003,"Acta Biochimica et Biophysica Sinica","35","6",,"587","591",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0042140675&partnerID=40&md5=afd5a11851543fc7b987312c094739af","State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China","Zhang, Q.-F., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Cui, J.-M., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Huang, X.-J., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Lin, W., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Tan, D.-Y., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Xu, J.-W., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Yang, Y.-F., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Zhang, J.-Q., State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; Zhang, X., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Li, H., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Zheng, H.-Y., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Chen, Q.-X., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Yan, X.-G., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Zheng, K., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Wan, Z.-Y., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China; Huang, J.-C., Ctr. Dis. Contr. of Guangdong Prov., Guangzhou 510300, China","After infecting the Vero E6 cells by nasal/throat swabs collected from SARS patients, we studied the SARS-associated virus by electron microscopy and molecular biological technique. The results show that the diameter of newly isolated virus is about 50nm without envelope or 100 nm with envelope. The virus was proved to be a new coronavirus by RT-PCR and it responded positively to convalescent-phase serum specimen from SARS patients, which is the evidence that this new virus is etiologically linked to the outbreak of SARS. The morphogenesis and distribution of the virus are also discussed in this article.","Coronavirus; Electron microscopy; Severe acute respiratory syndrome (SARS)","article; controlled study; convalescence; Coronavirus; electron microscopy; epidemic; human; human cell; morphogenesis; reverse transcription polymerase chain reaction; severe acute respiratory syndrome; upper respiratory tract infection; Vero cell; virus etiology; virus identification; virus isolation; virus morphology; virus pneumonia; virus transmission; Animals; Cell Nucleus; Cercopithecus aethiops; Humans; Larynx; Microscopy, Electron; Nasopharynx; Nuclear Envelope; SARS Virus; Severe Acute Respiratory Syndrome; Vero Cells; Virion; Coronavirus","Basic information about SARS (2003) CDC, , http://www.cdc.gov/ncidod/sars/pdf/factsheet-chinesetrad.pdf, April 24; Zhong, N.S., Current clinical diagnosis of SARS (2003) Chinese Medical Forum Bulletin, , http://cmbi.bjmu.edu.cn/cmbidata/sars/pages/status.htm, April 29; Severe acute respiratory syndrome (SARS) - Multi-country outbreak - Update 43 (2003) World Health Organization, , http://www.who.int/csr/don/2003_04_30/en, April 30; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Identification of severe acute respiratory syndrome in Canada N Engl J Med, , www.nejm.org/March312003/10.1056/NEJMoa030634, available at, http://content.nejm.org/cgi/reprint/NEJMoa030634vl.pdf; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348 (20), pp. 1986-1994; Tsang, K.W., Ho, P.L., Gai, O.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985. , http://content.nejm.org/cgi/content/full/348/20/1977; Coronavirus never before seen in humans in the cause of SARS (2003) Bali SOS, , http://www.balisos.com/SARS/Update31-CoroniVirusCausesSARS.html, April 16; Garoff, H., Hewson, R., Opstelten, D.J.E., Virus maturation by budding (1998) Microbiol Mol Biol Rev, 62, pp. 1171-1190; Yin, Z., Liu, J.H., (1997) Animal Virology, pp. 671-703. , Beijing Science Press; Siddell, S., Wege, H., Ter Meulen, V., The biology of coronaviruses (1983) J Gen Virol, 64, pp. 761-776; Zhu, Q.Y., Qin, E.D., Wang, C.E., Yu, M., Si, B.Y., Fan, B.C., Chang, G.H., Isolation and identification of a novel coronavirus from patients with SARS (2003) J Chin Biotech, p. 30. , http://www.eastwin.com.cn/download/sars.doc; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Peñaranda, S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome Science, , www.sciencexpress.org/1May2003/Page1/10.1126/science.1085952, Published online, available at, http://www.sciencemag.org/cgi/rapidpdf/1085952vl.pdf; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brook-Wilson, A., Butterfield, Y.S.N., Khattra, J., The genome sequence of the SARS- associated coronavirus Science, , www.sciencexpress.org/1May2003/Page1/10.1126/scienee.1085953, Published online, available at, http://www.sciencemag.org/cgi/rapidpdf/1085953vl.pdf; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., Tong, S., A novel coronavirus associated with severe acute respiratory syndrome N Engl J Med, , www.nejm.org/April102003/10.1056/NEJMoa030781, Published online, available at, http://content.nejm.org/cgi/reprint/NEJMoa030781v2.pdf; International progress in atypical pneumonia etiological study (2003) Chinese Center for Disease Control, , http://www.chinacdc.net.cn/feiyan/bing4.15-1.htm, April 14; Hong, T., Wang, J.W., Sun, Y.L., Duan, S.M., Chen, L.B., Qu, J.G., Ni, A.P., Chlamydia-like particles and coronavirus-like particles are found in autopsied specimen of SARS patients through TEM (2003) Journal of Chinese Medicine, 83 (8), pp. 632-636; Fields, B.N., Knipe, D.M., Howley, P.M., Griffin, D.E., (2001) Fields Virology, 4th Ed., , Philadelphia: Williams Lippincott & Wilkins","Zhang, J.-Q.; State Key Lab. for Biocontrol, Zhongshan University, Guangzhou 510275, China; email: Ls28@zsu.edu.cn",,,05829879,,,"12796822","English","Acta Biochim. Biophys. Sin.",Article,"Final",,Scopus,2-s2.0-0042140675
"Günther M., Wichmann O., Jelinek T.","7102454897;6603891996;56437379400;","Acute viral gastroenteritis [Akute virale gastroenteritis]",2003,"Zeitschrift fur Allgemeinmedizin","79","8",,"380","383",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-17644433240&partnerID=40&md5=8a488bdc0c4f479bf89515be648190c5","Institut für Tropenmedizin, Spandauer Damm 130, D-14050 Berlin, Germany","Günther, M., Institut für Tropenmedizin, Spandauer Damm 130, D-14050 Berlin, Germany; Wichmann, O.; Jelinek, T.","Gastroenteritis is one of the most important diseases in humans. Viruses are a very common cause of this disease, especially in children, but also in elderly and immunocompromised people. The first virus recognized as causal agent was the norwalkvirus. Since then, an increasing number of viruses causing acute gastroenteritis have been detected. Rotaviruses are the most common cause of gastroenteric disease in children under 5 years of age. Human caliciviruses, enteric adenoviruses and astroviruses are also important etiological factors of acute gastroenteritis. Other viruses, such as coronavirus, torovirus and picobirnavirus are increasingly detected as causative factors of diarrhea. In recent years new diagnostic tests, mainly enzyme-linked immunoassays and polymerase-chain-reaction (PCR) techniques, allow a specific detection and classification of viruses. The future development of safe and highly effective vaccines against rotaviruses is exspected and may reduce worldwide morbidity and mortality from severe acute viral gastroenteritis.","Causal agents; Gastroenteritis; New diagnostic tests; Norwalkvirus; Rotaviruses; Vaccines","bicarbonate; glucose; potassium chloride; sodium chloride; acute disease; Adenovirus; age; article; Astrovirus; Calicivirus; Coronavirus; Cytomegalovirus; diagnostic procedure; diarrhea; drug safety; electron microscopy; enzyme linked immunosorbent assay; Epstein Barr virus; futurology; gastroenteritis; human; Human immunodeficiency virus; immune deficiency; Norwalk gastroenteritis virus; Parvovirus; Picobirnavirus; polymerase chain reaction; RNA virus; Rotavirus; virus classification; virus detection; virus identification; virus infection","Kapikian, A.Z., Wyatt, R.G., Dolin, R., Thornhill, S., Kalica, A.R., Chanock, R.M., Visualization by immune electron microscopy of a 27 nm-particle associated with acute infectious nonbacterial gastroenteritis (1972) J Virol, 10, pp. 1075-1081; Bishop, R.F., Davidson, G.P., Holmes, I.H., Ruck, B.J., Virus particles in epithelial cells of duodenal mucosa from children with acute non-bacterial gastroenteritis (1973) Lancet, 2, pp. 1281-1283; Middleton, P.J., Szymanski, M.T., Abbott, G.D., Bortolussi, R., Hamilton, J.R., Orbivirus acute gastroenteritis of infancy (1974) Lancet, 1, pp. 1241-1244; Wilhelmi, I., Roman, E., Sánchez-Fauquier, A., Viruses causing gastroenteritis (2003) Clin Microbiol Infect, 9, pp. 247-262; Koopmans, M., Von Bonsdorff, C.-H., Vinjé, J., De Medici, D., Monroe, S., Foodborne viruses (2002) FEMS Microbiology Reviews, 26, pp. 187-205; Lopman, B.A., Brown, D.W., Koopmans, M., Human caliciviruses in Europe (2002) Journal of Clinical Virology, 24, pp. 137-160; Dalton, R.M., Roman, E.R., Negredo, A.A., Wilhelmi, I.D., Glass, R.I., Sánchez-Fauquier, A., Astroviruses acute gastroenteritis among children in Madrid, Spain (2002) Pediatr Infect Dis J, 21, pp. 1038-1041; Karst, S.M., Wobus, C.E., Lay, M., Davidson, J., Virgin, H.W., STAT1-dependent innate immunity to a norwalk-like-virus (2003) Science, 299, pp. 1575-1578; Meyer, C.G., (2000) Tropenmedizin-Infektionskrankheiten, , Landsberg: Ecomed Verlagsgesellschaft; Rotavirus vaccine for the prevention of rotavirus gastroenteritis among children. Recommendations of the Advisory Committee on Immunization Practices (ACIP) (1999) MMWR, 48, pp. 1-23","Günther, M.; Institut für Tropenmedizin, Spandauer Damm 130, D-14050 Berlin, Germany; email: matthias.guenther@charite.de",,,09376801,,ZALMA,,"German","Z. Allg.med.",Article,"Final",,Scopus,2-s2.0-17644433240
"Pene F., Merlat A., Vabret A., Rozenberg F., Buzyn A., Dreyfus F., Cariou A., Freymuth F., Lebon P.","8912414300;7801327471;7003959575;7004000569;55795133000;7005155254;56779751400;7103410207;7102555618;","Coronavirus 229E-Related Pneumonia in Immunocompromised Patients",2003,"Clinical Infectious Diseases","37","7",,"929","932",,107,"10.1086/377612","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142107410&doi=10.1086%2f377612&partnerID=40&md5=4bd77bbf7ed10d5fc6be92286b67d1a1","Medical Intensive Care Unit, University Paris V, Paris, France; Department of Hematology, University Paris V, Paris, France; Department of Virology, Cochin-S. Vincent de Paul Hospital, University Paris V, Paris, France; Department of Hematology, Necker Hospital, Paris, France; Lab. of Human and Molecular Virology, University Hospital, Caen, France; Serv. de Réanimation Med., Hôpital Cochin, 27 rue du faubourg Saint-Jacques, 75679 Paris Cedex 14, France","Pene, F., Medical Intensive Care Unit, University Paris V, Paris, France, Serv. de Réanimation Med., Hôpital Cochin, 27 rue du faubourg Saint-Jacques, 75679 Paris Cedex 14, France; Merlat, A., Department of Hematology, University Paris V, Paris, France; Vabret, A., Lab. of Human and Molecular Virology, University Hospital, Caen, France; Rozenberg, F., Department of Virology, Cochin-S. Vincent de Paul Hospital, University Paris V, Paris, France; Buzyn, A., Department of Hematology, Necker Hospital, Paris, France; Dreyfus, F., Department of Hematology, University Paris V, Paris, France; Cariou, A., Medical Intensive Care Unit, University Paris V, Paris, France; Freymuth, F., Lab. of Human and Molecular Virology, University Hospital, Caen, France; Lebon, P., Department of Virology, Cochin-S. Vincent de Paul Hospital, University Paris V, Paris, France","Coronaviruses strains 229E and OC43 have been associated with various respiratory illnesses ranging from the self-resolving common cold to severe pneumonia. Although chronic underlying conditions are major determinants of severe respiratory virus infections, few data about coronavirus-related pneumonia in immunocompromised patients are available. Here we report 2 well-documented cases of pneumonia related to coronavirus 229E, each with a different clinical presentation. Diagnosis was made on the basis of viral culture and electron microscopy findings that exhibited typical crown-like particles and through amplification of the viral genome by reverse transcriptase-polymerase chain reaction. On the basis of this report, coronaviruses should be considered as potential causative microorganisms of pneumonia in immunocompromised patients.",,"antibiotic agent; antineoplastic agent; ciprofloxacin; cytarabine; etoposide; ifosfamide; mitoxantrone; piperacillin; adolescent; adult; article; case report; case study; clinical feature; Coronavirus; electron microscopy; female; Hodgkin disease; human; large cell lymphoma; male; priority journal; reverse transcription polymerase chain reaction; virus culture; virus diagnosis; virus genome; virus particle; virus pneumonia; virus strain; Adolescent; Adult; Common Cold; Coronavirus 229E, Human; Coronavirus Infections; Female; Humans; Immunocompromised Host; Male; Pneumonia; Reverse Transcriptase Polymerase Chain Reaction","Soubani, A.O., Miller, K.B., Hassoun, P.M., Pulmonary complications of bone marrow transplantation (1996) Chest, 109, pp. 1066-1077; Hendley, J.O., Fishburne, H.B., Gwaltney J.M., Jr., Coronavirus infections in working adults. Eight-year study with 229 E and OC 43 (1972) Am Rev Respir Dis, 105, pp. 805-811; Wenzel, R.P., Hendley, J.O., Davies, J.A., Gwaltney J.M., Jr., Coronavirus infections in military recruits. Three-year study with coronavirus strains OC43 and 229E (1974) Am Rev Respir Dis, 109, pp. 621-624; Makela, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Vabret, A., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., An Outbreak of coronavirus OC43 respiratory infection in Normandy, France (2003) Clin Infect Dis, 36, pp. 985-989; Peiris, J., Lai, S., Poon, L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Haioun, C., Lepage, E., Gisselbrecht, C., Survival benefit of high-dose therapy in poor-risk aggressive non-Hodgkin's lymphoma: Final analysis of the prospective LNH87-2 protocol - A groupe d'Etude des lymphomes de l'Adulte study (2000) J Clin Oncol, 18, pp. 3025-3030; Puchhammer-Stockl, E., Popow-Kraupp, T., Heinz, F.X., Mandl, C.W., Kunz, C., Detection of varicella-zoster virus DNA by polymerase chain reaction in the cerebrospinal fluid of patients suffering from neurological complications associated with chicken pox or herpes zoster (1991) J Clin Microbiol, 29, pp. 1513-1516; Vabret, A., Mouthon, F., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., Direct diagnosis of human respiratory coronaviruses 229E and OC43 by the polymerase chain reaction (2001) J Virol Methods, 97, pp. 59-66; Papazian, L., Fraisse, A., Garbe, L., Cytomegalovirus: An unexpected cause of ventilator-associated pneumonia (1996) Anesthesiology, 84, pp. 280-287; Gagneur, A., Sizun, J., Vallet, S., Legr, M.C., Picard, B., Talbot, P.J., Coronavirus-related nosocomial viral respiratory infections in a neonatal and paediatric intensive care unit: A prospective study (2002) J Hosp Infect, 51, pp. 59-64; Wesley, A.G., Pather, M., Tait, D., Nosocomial adenovirus infection in a paediatric respiratory unit (1993) J Hosp Infect, 25, pp. 183-190; Oshiro, L.S., Schieble, J.H., Lennette, E.H., Electron microscopic studies of coronavirus (1971) J Gen Virol, 12, pp. 161-168; McIntosh, K., McQuillin, J., Reed, S.E., Gardner, P.S., Diagnosis of human coronavirus infection by immunofluorescence: Method and application to respiratory disease in hospitalized children (1978) J Med Virol, 2, pp. 341-346; Myint, S., Siddell, S., Tyrrell, D., Detection of human coronavirus 229E in nasal washings using RNA:RNA hybridisation (1989) J Med Virol, 29, pp. 70-73; Macnaughton, M.R., Occurrence and frequency of coronavirus infections in humans as determined by enzyme-linked immunosorbent assay (1982) Infect Immun, 38, pp. 419-423; Koetters, P.J., Hassanieh, L., Stohlman, S.A., Gallagher, T., Lai, M.M., Mouse hepatitis virus strain JHM infects a human hepatocellular carcinoma cell line (1999) Virology, 264, pp. 398-409; Sizun, J., Arbour, N., Talbot, P.J., Comparison of immunofluorescence with monoclonal antibodies and RT-PCR for the detection of human coronaviruses 229E and OC43 in cell culture (1998) J Virol Methods, 72, pp. 145-152; Ghosh, S., Champlin, R., Couch, R., Rhinovirus infections in myelosuppressed adult blood and marrow transplant recipients (1999) Clin Infect Dis, 29, pp. 528-532; Glezen, W.P., Greenberg, S.B., Atmar, R.L., Piedra, P.A., Couch, R.B., Impact of respiratory virus infections on persons with chronic underlying conditions (2000) JAMA, 283, pp. 499-505; Ison, M.G., Hayden, F.G., Kaiser, L., Corey, L., Boeckh, M., Rhinovirus infections in hematopoietic stem cell transplant recipients with pneumonia (2003) Clin Infect Dis, 36, pp. 1139-1143; Folz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; Tyrrell, D.A., The efficacy and tolerance of intranasal interferons: Studies at the Common Cold Unit (1986) J Antimicrob Chemother, 18, pp. 153-156; Smith, A.L., Barthold, S.W., De Souza, M.S., Bottomly, K., The role of gamma interferon in infection of susceptible mice with murine coronavirus, MHV-JHM (1991) Arch Virol, 121, pp. 89-100","Pene, F.; Serv. de Réanimation Med., Hôpital Cochin, 27 rue du faubourg Saint-Jacques, 75679 Paris Cedex 14, France; email: frederic.pene@cch.ap-hop-paris.fr",,,10584838,,CIDIE,"13130404","English","Clin. Infect. Dis.",Article,"Final",Open Access,Scopus,2-s2.0-0142107410
"Leung W.K., To K.-F., Chan P.K.S., Chan H.L.Y., Wu A.K.L., Lee N., Yuen K.Y., Sung J.J.Y.","57188802557;7101911940;32067487100;25722700100;7402998681;55503117200;36078079100;35405352400;","Enteric involvement of severe acute respiratory syndrome - Associated coronavirus infection",2003,"Gastroenterology","125","4",,"1011","1017",,148,"10.1016/j.gastro.2003.08.001","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141483076&doi=10.1016%2fj.gastro.2003.08.001&partnerID=40&md5=8294152d5568abb96c4b5d4baf1b7572","Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Dept. of Anat. and Cell. Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Dept. of Medicine and Therapeutics, 9/F, Clinical Sciences Building, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong","Leung, W.K., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong, Dept. of Medicine and Therapeutics, 9/F, Clinical Sciences Building, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong; To, K.-F., Dept. of Anat. and Cell. Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Chan, P.K.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Chan, H.L.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Wu, A.K.L., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Lee, N., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Sung, J.J.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, Hong Kong","Background & Aims: Severe acute respiratory syndrome (SARS) is a recently emerged infection from a novel coronavirus (CoV). Apart from fever and respiratory complications, gastrointestinal symptoms are frequently observed in patients with SARS but the significance remains undetermined. Herein, we describe the clinical, pathologic, and virologic features of the intestinal involvement of this new viral infection. Methods: A retrospective analysis of the gastrointestinal symptoms and other clinical parameters of the first 138 patients with confirmed SARS admitted for a major outbreak in Hong Kong in March 2003 was performed. Intestinal specimens were obtained by colonoscopy or postmortem examination to detect the presence of coronavirus by electron microscopy, virus culture, and reverse-transcription polymerase chain reaction. Results: Among these 138 patients with SARS, 28 (20.3%) presented with watery diarrhea and up to 38.4% of patients had symptoms of diarrhea during the course of illness. Diarrhea was more frequently observed during the first week of illness. The mean number of days with diarrhea was 3.7 ± 2.7, and most diarrhea was self-limiting. Intestinal biopsy specimens obtained by colonoscopy or autopsy showed minimal architectural disruption but the presence of active viral replication within both the small and large intestine. Coronavirus was also isolated by culture from these specimens, and SARS-CoV RNA can be detected in the stool of patients for more than 10 weeks after symptom onset. Conclusions: Diarrhea is a common presenting symptom of SARS. The intestinal tropism of the SARS-CoV has major implications on clinical presentation and viral transmission.",,"virus RNA; acute respiratory tract disease; adult; animal cell; article; autopsy; clinical feature; colonoscopy; Coronavirus; diarrhea; disease course; disease duration; electron microscopy; epidemic; feces analysis; female; fever; gastrointestinal symptom; histopathology; Hong Kong; human; human cell; human tissue; intestine biopsy; major clinical study; male; nonhuman; priority journal; retrospective study; reverse transcription polymerase chain reaction; severe acute respiratory syndrome; symptom; virus culture; virus detection; virus infection; virus isolation; virus replication; virus transmission","Latest Figures on Severe Acute Respiratory Syndrome, , http://www.info.gov.hk/dh/diseases/ap/eng/infected.htm/; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Cumulative Number of Reported Probable Cases of SARS, , http://www.who.int/csr/sars/country/2003_05_31/en/; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, U., Anderson, R.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Bellini, W.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Sanchez, C.M., Izeta, A., Sanchez-Morgado, J.M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., Enjuanes, L., Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis coronavirus is a determinant of its enteric tropism and virulence (1999) J Virol, 73, pp. 7607-7618; Schmidt, W., Schneider, T., Heise, W., Weinke, T., Epple, H.J., Stoffler-Meilicke, M., Liesenfeld, O., Ullrich, R., Stool viruses, coinfections, and diarrhea in HIV-infected patients (1996) J Acquir Immune Defic Syndr Hum Retrovirol, 13, pp. 33-38. , Berlin Diarrhea/Wasting Syndrome Study Group; Gerna, G., Passarani, N., Battaglia, M., Rondanelli, E.G., Human enteric coronaviruses: Antigenic relatedness to human coronavirus OC43 and possible etiologic role in viral gastroenteritis (1985) J Infect Dis, 151, pp. 796-803; Simhon, A., Mata, L., Fecal rotaviruses, adenoviruses, coronavirus-like particles, and small round viruses in a cohort of rural Costa Rican children (1985) Am J Trop Med Hyg, 34, pp. 931-936; Resta, S., Luby, J.P., Rosenfeld, C.R., Siegel, J.D., Isolation and propagation of a human enteric coronavirus (1985) Science, 229, pp. 978-981; Holmes, K.V., Enteric infections with coronaviruses and toroviruses (2001) Novartis Found Symp, 238, pp. 258-269; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Chan, K.S., Hung, I.F.N., Poon, L.L.M., Law, K.I., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Walmsley, S.L., Detsky, A.S., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Updated Interim U.S. Case Definition of Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/casedefinition.htm/; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/; Use of Laboratory Methods for SARS Diagnosis, , http://www.who.int/csr/sars/labmethods/en/; PCR Primers for SARS Developed by WHO Network Laboratories, , http://www.who.int/csr/sars/primers/en/; WHO Environmental Health Team Reports on Amoy Gardens, , http://www.info.gov.hk/gia/general/200305/16/0516114.htm; Nicholls, J.M., Poon, L.L., Lee, K.C., Ng, W.F., Lai, S.T., Leung, C.Y., Chu, C.M., Peiris, J.S., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778","Leung, W.K.; Dept. of Medicine and Therapeutics, 9/F, Clinical Sciences Building, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, Hong Kong; email: wkleung@cuhk.edu.hk",,"W.B. Saunders",00165085,,GASTA,"14517783","English","Gastroenterology",Article,"Final",Open Access,Scopus,2-s2.0-0141483076
"Yam W.C., Chan K.H., Poon L.L.M., Guan Y., Yuen K.Y., Seto W.H., Peiris J.S.M.","7004281720;7406034307;7005441747;7202924055;36078079100;7005799377;7005486823;","Evaluation of reverse transcription-PCR assays for rapid diagnosis of severe acute respiratory syndrome associated with a novel coronavirus",2003,"Journal of Clinical Microbiology","41","10",,"4521","4524",,90,"10.1128/JCM.41.10.4521-4524.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141993032&doi=10.1128%2fJCM.41.10.4521-4524.2003&partnerID=40&md5=20b65b3fa525b8e287c52ef3196dff15","Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, University of Hong Kong, University Pathology Building, Pokfulam, Hong Kong","Yam, W.C., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Chan, K.H., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Poon, L.L.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Seto, W.H., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong, Department of Microbiology, University of Hong Kong, University Pathology Building, Pokfulam, Hong Kong","The reverse transcription (RT)-PCR protocols of two World Health Organization (WHO) severe acute respiratory syndrome (SARS) network laboratories (WHO SARS network laboratories at The University of Hong Kong [WHO-HKU] and at the Bernhard-Nocht Institute in Hamburg, Germany [WHO-Hamburg]) were evaluated for rapid diagnosis of a novel coronavirus (CoV) associated with SARS in Hong Kong. A total of 303 clinical specimens were collected from 163 patients suspected to have SARS. The end point of both WHO-HKU and WHO-Hamburg RT-PCR assays was determined to be 0.1 50% tissue culture infective dose. Using seroconversion to CoV as the ""gold standard"" for SARS CoV diagnosis, WHO-HKU and WHO-Hamburg RT-PCR assays exhibited diagnostic sensitivities of 61 and 68% (nasopharyngeal aspirate specimens), 65 and 72% (throat swab specimens), 50 and 54% (urine specimens), and 58 and 63% (stool specimens), respectively, with an overall specificity of 100%. For patients confirmed to have SARS CoV and from whom two or more respiratory specimens were collected, testing the second specimen increased the sensitivity from 64 and 71% to 75 and 79% for the WHO-HKU and WHO-Hamburg RT-PCR assays, respectively. Testing more than one respiratory specimen will maximize the sensitivity of PCR assays for SARS CoV.",,"animal cell; article; controlled study; Coronavirus; feces analysis; Germany; Hong Kong; human; major clinical study; nonhuman; priority journal; reverse transcription polymerase chain reaction; SARS coronavirus; sensitivity and specificity; severe acute respiratory syndrome; throat culture; tissue culture; urinalysis; virus pneumonia; virus strain; world health organization; Humans; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Sensitivity and Specificity; Severe Acute Respiratory Syndrome; Time Factors; World Health Organization; Animalia; Coronavirus; RNA viruses; SARS coronavirus","Ballew, H.C., Neutralization (1992) Clinical Virology Manual, pp. 229-241. , S. Specter and G. Lancz (ed.). Elsevier, New York, N.Y; Chan, K.H., Maldeis, N., Pope, W., Yup, A., Ozinskas, A., Gill, J., Seto, W.H., Peiris, J.S.M., Evaluation of the Directigen FluA+B test for rapid diagnosis of influenza virus type A and B infections (2002) J. Clin. Microbiol., 40, pp. 1675-1680; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, L.J., Anderson, R.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Drosten, C., Günther, S., Preiser, W., Van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Nelson, S.M., Deike, M.A., Cartwright, C.P., Value of examining multiple sputum specimens in the diagnosis of pulmonary tuberculosis (1998) J. Clin. Microbiol., 36, pp. 467-469; Peiris, J.S.M., Lai, S., Poon, L.L.M., Guan, Y., Yam, L., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Peiris, J.S.M., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.I., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Vabret, A., Mouthon, F., Mourez, T., Gouarin, S., Petitjean, J., Freymuth, F., Direct diagnosis of human respiratory coronaviruses 229E and OC43 by the polymerase chain reaction (2001) J. Virol. Methods, 97, pp. 59-66; Severe acute respiratory syndrome (SARS) (2003) Wkly. Epidemiol. Rec, 78, pp. 86-87","Peiris, J.S.M.; Department of Microbiology, University of Hong Kong, University Pathology Building, Pokfulam, Hong Kong; email: malik@hku.hk",,,00951137,,JCMID,"14532176","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0141993032
"Addie D.D., Schaap I.A.T., Nicolson L., Jarrett O.","7003910352;6507923017;6701397969;7006845693;","Persistence and transmission of natural type I feline coronavirus infection",2003,"Journal of General Virology","84","10",,"2735","2744",,88,"10.1099/vir.0.19129-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141618496&doi=10.1099%2fvir.0.19129-0&partnerID=40&md5=e439314ccc23ebbe007919b482126a85","Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom; Physics of Complex Systems, Division of Physics and Astronomy, Vrije Universiteit, De Boelelaan 1081, HV Amsterdam, Netherlands","Addie, D.D., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom; Schaap, I.A.T., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom, Physics of Complex Systems, Division of Physics and Astronomy, Vrije Universiteit, De Boelelaan 1081, HV Amsterdam, Netherlands; Nicolson, L., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom; Jarrett, O., Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom","To examine the mode of natural transmission and persistence of feline coronavirus (FCoV), FCoV strains shed by domestic cats were investigated over periods of up to 7 years. An RT-PCR that amplified part of the 3′ end of the viral spike (S) gene was devised to distinguish FCoV types I and II. All but 1 of 28 strains of FCoV from 43 cats were type I. Nucleotide identities of the amplified 320 bp product from 49 type I FCoVs ranged from 79 to 100 %. The consensus partial S sequence of isolates recovered from persistently infected cats at time intervals spanning years was generally conserved. While most cats were infected with a single strain, a few may have been infected by more than one strain. Cats that were transiently infected and ceased shedding could be re-infected with either the same, or a different, strain. In most cases, whether a cat became persistently or transiently infected was independent of the virus strain. However, one strain was unusual in that it infected the majority of cats in the household simultaneously and was still being shed 18 months later. Factors that influence whether FCoV establishes lifelong infection in some cats and not others are determined mainly by the host response to infection.",,"nucleotide; virus envelope protein; article; cat disease; controlled study; Coronavirus; domestic animal; gene amplification; gene sequence; genetic conservation; genetic identification; nonhuman; nucleotide sequence; persistent virus infection; priority journal; reinfection; reverse transcription polymerase chain reaction; RNA virus infection; virus gene; virus isolation; virus pathogenesis; virus shedding; virus strain; virus transmission; virus typing; Animals; Carrier State; Cat Diseases; Cats; Coronavirus Infections; Coronavirus, Feline; Membrane Glycoproteins; Phylogeny; Reverse Transcriptase Polymerase Chain Reaction; Sequence Analysis, DNA; Viral Envelope Proteins; Virus Shedding; Animalia; Coronavirus; Felidae; Feline coronavirus; Felis catus; RNA viruses","Addie, D.D., Jarrett, J.O., A study of naturally occurring feline coronavirus infections in kittens (1992) Vet. Rec., 130, pp. 133-137; Addie, D.D., Jarrett, J.O., Use of a reverse-transcriptase polymerase chain reaction for monitoring the shedding of feline coronavirus by healthy cats (2001) Vet. Rec., 148, pp. 649-653; Boom, R., Sol, C.J.A., Salimans, M.M.M., Jansen, C.L., Wertheim-van Dillen, P.M.E., van der Noordaa, J., Rapid and simple method for purification of nucleic acids (1990) J. Clin. Microbiol., 28, pp. 495-503; Cavanagh, D., Mawditt, K., Adzhar, A., Gough, R.E., Picault, J.P., Naylor, C.J., Haydon, D., Britton, P., Does IBV change slowly despite the capacity of the spike protein to vary greatly? (1998) Adv. Exp. Med. Biol., 440, pp. 729-734; Christianson, K.K., Ingersoll, J.D., Landon, R.M., Pfeiffer, N.E., Gerber, J.D., Characterization of a temperature sensitive feline peritonitis coronavirus (1989) Arch. Virol., 109, pp. 185-196; de Groot-Mijnes, J.D.F., van der Most, R.G., van Dun, J., de Groot, R.J., Detection of feline coronavirus-specific CD4+ and CD8+ T cells by flow cytometry (2002), Second International Feline Coronavirus/Feline Infectious Peritonitis Symposium (Glasgow, Scotland, 4-7 August, 2002). Abstract 4.1; den Boon, J.A., Snijder, E.J., Chirnside, E.D., de Vries, A.A., Horzinek, M.C., Spaan, W.J., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J. Virol., 65, pp. 2910-2920; Foley, J.F., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Am. Vet. Med. Assoc., 210, pp. 1307-1312; Godeke, G.J., de Haan, C.A.M., Rossen, J.W.A., Vennema, H., Rottier, P.J.M., Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein (2000) J. Virol., 74, pp. 1566-1571; Gonon, V., Duquesne, V., Klonjkowski, B., Monteil, M., Aubert, A., Eloit, M., Clearance of infection in cats naturally infected with feline coronaviruses is associated with an anti-S glycoprotein antibody response (1999) J. Gen. Virol., 80, pp. 2315-2317; Gunn-Moore, D.A., Gruffydd-Jones, T.J., Harbour, D.A., Detection of feline coronavirus by culture and reverse transcriptase-polymerase chain reaction of blood samples from healthy cats and cats with clinical feline infectious peritonitis (1998) Vet. Microbiol., 62, pp. 193-205; Herrewegh, A.A.P.M., de Groot, R.J., Cepica, A., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., Detection of feline coronavirus RNA in feces, tissues and body fluids of naturally infected cats by reverse transcriptase PCR (1995) J. Clin. Microbiol., 33, pp. 684-689; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., de Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Herrewegh, A.A.P.M., Smeenk, I., Horzinek, M.C., Rottier, P.J.M., de Groot, R.J., Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus (1998) J. Virol., 72, pp. 4508-4514; Hohdatsu, T., Okada, S., Ishizuka, Y., Yamada, H., Koyama, H., The prevalence of types I and II feline coronavirus infections in cats (1992) J. Vet. Med. Sci., 54, pp. 557-562; Hoskins, J.D., Update on feline coronavirus disease (1997) Consultations in Feline Internal Medicine, 3, pp. 44-50. , Edited by J. R. August. Philadelphia: W. B. Saunders; Kass, P.H., Dent, T.H., The epidemiology of feline infectious peritonitis in catteries (1995) Feline Pract., 23, pp. 27-32; Kiss, I., Ros, C., Kecskeméti, S., Tanyi, J., Klingeborn, S.B., Belák, S., Observations on the quasispecies composition of three animal pathogenic RNA viruses (1999) Acta Vet. Hung., 47, pp. 471-480; Motokawa, K., Hohdatsu, T., Aizawa, C., Koyama, H., Hashimoto, H., Molecular cloning and sequence determination of the peplomer protein gene of feline infectious peritonitis virus type I (1995) Arch. Virol., 140, pp. 469-480; Page, R.D.M., TREEVIEW: An application to display phylogenetic trees on personal computers (1996) Comput. Appl. Biosci., 12, pp. 357-358; Pedersen, N.C., Serological studies of naturally occurring feline infectious peritonitis (1976) Am. J. Vet. Res., 37, pp. 1449-1453; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34, pp. 3180-3184; Vennema, H., Genetic drift and genetic shift during feline coronavirus evolution (1999) Vet. Microbiol., 69, pp. 139-141; Vennema, H., de Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J. Virol., 64, pp. 1407-1409; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157","Addie, D.D.; Department of Veterinary Pathology, University of Glasgow, Bearsden Road, Glasgow G61 1QH, United Kingdom; email: D.D.Addie@vet.gla.ac.uk",,,00221317,,JGVIA,"13679608","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141618496
"Ontiveros E., Kim T.S., Gallagher T.M., Perlman S.","56487800200;8756664100;7202310503;7102708317;","Enhanced virulence mediated by the murine coronavirus, mouse hepatitis virus strain JHM, is associated with a glycine at residue 310 of the spike glycoprotein",2003,"Journal of Virology","77","19",,"10260","10269",,54,"10.1128/JVI.77.19.10260-10269.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141856400&doi=10.1128%2fJVI.77.19.10260-10269.2003&partnerID=40&md5=1935d12c2c80ce768ca47b144d20c497","Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Department of Pediatrics, College of Medicine, University of Iowa, Iowa City, IA 52242, United States","Ontiveros, E., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States; Kim, T.S., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States; Gallagher, T.M., Dept. of Microbiology/Immunology, Loyola University Medical Center, Maywood, IL 60153, United States; Perlman, S., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, College of Medicine, University of Iowa, Iowa City, IA 52242, United States","The coronavirus, mouse hepatitis virus strain JHM, causes acute and chronic neurological diseases in rodents. Here we demonstrate that two closely related virus variants, both of which cause acute encephalitis in susceptible strains of mice, cause markedly different diseases if mice are protected with a suboptimal amount of an anti-JHM neutralizing antibody. One strain, JHM.SD, caused acute encephalitis, while infection with JHM.IA resulted in no acute disease. Using recombinant virus technology, we found that the differences between the two viruses mapped to the spike (S) glycoprotein and that the two S proteins differed at four amino acids. By engineering viruses that differed by only one amino acid, we identified a serine-to-glycine change at position 310 of the S protein (S310G) that recapitulated the more neurovirulent phenotype. The increased neurovirulence mediated by the virus encoding glycine at position S310 was not associated with a different tropism within the central nervous system (CNS) but was associated with increased lateral spread in the CNS, leading to significantly higher brain viral titers. In vitro studies revealed that S310G was associated with decreased S1-S2 stability and with enhanced ability to mediate infection of cells lacking the primary receptor for JHM (""receptor-independent spread""). These enhanced fusogenic properties of viruses encoding a glycine at position 310 of the S protein may contribute to spread within the CNS, a tissue in which expression of conventional JHM receptors is low.",,"glycoprotein; neutralizing antibody; amino acid analysis; amino acid substitution; animal model; animal tissue; article; controlled study; Coronavirus; encephalitis; Hepatitis virus; in vitro study; mouse; Murine hepatitis coronavirus; neurologic disease; nonhuman; phenotype; priority journal; protein stability; technology; virogenesis; virus expression; virus recombinant; virus strain; virus virulence; Animals; Cricetinae; Glycine; Membrane Fusion; Membrane Glycoproteins; Mice; Murine hepatitis virus; Structure-Activity Relationship; Viral Envelope Proteins; Virulence","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Bang, F.B., Genetics of resistance of animals to viruses. I. Introduction and studies in mice (1978) Adv. Virus Res., 1978, pp. 269-348; Barnett, E., Cassell, M., Perlman, S., Two neurotropic viruses, herpes simplex virus type 1 and mouse hepatitis virus, spread along different neural pathways from the main olfactory bulb (1993) Neuroscience, 57, pp. 1007-1025; Boyle, J.F., Weismiller, D.G., Holmes, K.V., Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues (1987) J. Virol., 61, pp. 185-189; Buchmeier, M.J., Lewicki, H.A., Talbot, P.J., Knobler, R.L., Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody (1984) Virology, 132, pp. 261-270; Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., Reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) J. Virol., 75, pp. 12359-12369; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Cheever, F.S., Daniels, J.B., Pappenheimer, A.M., Bailey, O.T., A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin (1949) J. Exp. Med., 90, pp. 181-194; Chen, D., Asanaka, M., Yokomori, K., Wang, F., Hwang, S., Li, H., Lai, M.M.C., A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus (1995) Proc. Natl. Acad. Sci. 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Virol., 72, pp. 7237-7244","Perlman, S.; Department of Pediatrics, College of Medicine, University of Iowa, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"12970410","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141856400
"De Groot A.S.","7202864343;","How the SARS vaccine effort can learn from HIV - Speeding towards the future, learning from the past",2003,"Vaccine","21","27-30",,"4095","4104",,25,"10.1016/S0264-410X(03)00489-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0348078300&doi=10.1016%2fS0264-410X%2803%2900489-4&partnerID=40&md5=87c85e2dd92833398c331156cc580b27","TB/HIV Research Laboratory, Brown University, Providence, RI 02912, United States","De Groot, A.S., TB/HIV Research Laboratory, Brown University, Providence, RI 02912, United States","A remarkable collaborative effort coordinated by the severe acute respiratory syndrome (SARS) team at WHO resulted in discovery of the etiologic agent of severe acute respiratory syndrome less than 2 months after the announcement of global alert. The development of a vaccine to prevent SARS should be pursued with the same urgency and cooperative spirit, as SARS is highly lethal and, if not controlled during the first few generations of transmission, is likely to become endemic in regions of the world where health-care infrastructure is underdeveloped and epidemiological control measures are weak. The scientific community already learned many important lessons from HIV vaccine development; these should be heeded. For example, consideration should be given to the development of a vaccine that will protect across regional strains of SARS, as the newly emergent coronavirus SARS-coronavirus (SARS-CoV) is proving to be variable and may be mutating in response to immune pressure. SARS-specific research reagents should also be collected and shared. These would include SARS peptides, adjuvants, DNA vaccine vectors and clinical grade viral vectors. Rapidly developing a collaborative approach to developing a SARS vaccine that will be both effective and safe is the only way to go. This article reviews parallels between HIV and SARS and proposes an approach that would accelerate the development of a SARS vaccine. © 2003 Elsevier Ltd. All rights reserved.","Coronavirus; HIV; SARS; Vaccine","DNA vaccine; epitope; inactivated vaccine; live vaccine; recombinant vaccine; severe acute respiratory syndrome vaccine; unclassified drug; virus vaccine; clinical feature; Coronavirus; diagnostic approach route; diagnostic test; epidemic; gene amplification; gene sequence; host pathogen interaction; Human immunodeficiency virus; immunopathogenesis; infection prevention; nucleotide sequence; priority journal; reverse transcription polymerase chain reaction; review; RNA virus; SARS coronavirus; seasonal variation; severe acute respiratory syndrome; upper respiratory tract infection; virus genome; virus neutralization; virus pneumonia; virus strain; virus transmission","Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 624-629; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; (2003) VaxGen AIDS Vaccine 'Largely Ineffective' at Reducing HIV Infection Rate; African Americans, Asians Show Stronger Protective Effect Kaiser Daily HIV/AIDS Report, , http://www.kaisernetwork.org/daily_reports/print_report.cfm?DR_ID= 16196&dr_cat=1, Monday, 24 February; De Groot, A.S., Sbai, H., Mapping cross-clade HIV-1 vaccine epitopes using a bioinformatics approach Vaccine, , in proofs; Ruan, Y., Wei, C.L., Ee, A.L., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Prentice, E., Dension, M.R., The cell biology of coronavirus infection (2001) Adv. 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Res., 66 (4), pp. 278-281; Pratelli, A., Tinelli, A., Decaro, N., Efficacy of an inactivated canine coronavirus vaccine in pups (2003) New Microbiol., 26 (2), pp. 151-155; Ladman, B.S., Pope, C.R., Ziegler, A.F., Protection of chickens after live and inactivated virus vaccination against challenge with nephropathogenic infectious bronchitis virus (2002) Avian Dis., 46 (4), pp. 938-944; Wang, X., Schnitzlein, W.M., Tripathy, D.N., Girshick, T., Khan, M.I., Construction and immunogenicity studies of recombinant fowl poxvirus containing the S1 gene of Massachusetts 41 strain of infectious bronchitis virus (2002) Avian Dis., 46 (4), pp. 831-838; Chen, H., Schifferli, D.M., Enhanced immune responses to viral epitopes by combining macrophage-inducible expression with multimeric display on a Salmonella vector (2001) Vaccine, 19 (20-22), pp. 3009-3018; Liu, C., Kokuho, T., Kubota, T., DNA mediated immunization with encoding the nucleoprotein gene of porcine transmissible gastroenteritis virus (2001) Virus Res., 80 (1-2), pp. 75-82; Koden, M.J., Borst, M.A., Horsinek, M.C., Spaan, W.J., Immunogenic peptide comprising a mouse hepatitis virus A59 B-cell epitope and an influenza virus T-cell epitope protects against lethal infection (1990) J. Virol., 64 (12), pp. 6270-6273","De Groot, A.S.; TB/HIV Research Laboratory, Brown University, Providence, RI 02912, United States; email: annied@brown.edu",,"Elsevier BV",0264410X,,VACCD,"14505885","English","Vaccine",Note,"Final",,Scopus,2-s2.0-0348078300
"Beugelsdijk T.J., Layne S.P.","6603574058;6701920673;","The role of high-throughput laboratories in homeland security",2003,"JALA - Journal of the Association for Laboratory Automation","8","5",,"11","18",,2,"10.1016/S1535-5535(03)00004-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0842301398&doi=10.1016%2fS1535-5535%2803%2900004-2&partnerID=40&md5=7d839209087273c97724fd8fb729f2b8","Los Alamos National Laboratory, University of California, Los Angeles, CA, United States; School of Public Health, University of California, Los Angeles, CA, United States; IBD Division, Los Alamos National Laboratory, P.O. Box 1663, Los Alamos, NM 87545, United States","Beugelsdijk, T.J., Los Alamos National Laboratory, University of California, Los Angeles, CA, United States, IBD Division, Los Alamos National Laboratory, P.O. Box 1663, Los Alamos, NM 87545, United States; Layne, S.P., School of Public Health, University of California, Los Angeles, CA, United States","Infectious diseases pose threats from natural and manmade sources, and arguably the situation is getting worse. The outbreak of the coronavirus causing the severe acute respiratory syndrome (SARS) shows that the world is linked by thousands of people traveling millions of miles every single day who can spread SARS or new strains of influenza with pandemic potential. The world is also becoming a more dangerous place, with rogue nations and terrorist networks aggressively seeking nuclear, chemical, and biological weapons. Of these, biological weapons are the cheapest to produce and likely the most attractive because they can be used anonymously.","Anthrax; Automation; Biological weapons; Epidemiology; High-throughput testing; Homeland security; Infectious disease; Influenza; SARS; Smallpox; Surveillance","chemical warfare agent; article; atomic bomb; biological warfare; disease transmission; epidemic; health hazard; infection; infection control; Influenza virus; laboratory automation; population movement pattern; public health; SARS coronavirus; sequence database; severe acute respiratory syndrome; virus strain","Layne, S.P., Put high-tech labs into the fight against SARS and Bioterrorism (2003) Los Angeles Times, pp. B17. , April 4; Layne, S.P., Virtually assured detection and response: Utilizing science, technology and policy against bioterrorism (2002) Biological Threats and Terrorism, pp. 211-217. , S. L. Knobler, A. A. Mahmoud, & L. A. Pray (Eds.), Washington, DC: National Academy Press; Layne, S.P., Beugelsdijk, T.J., Laboratory firepower for infectious disease research (1998) Nat. Biotechnol., 16, pp. 825-829; Editorial. Beat Bioterror with Batch Science (1998) Nat. Biotechnol., 16, p. 793; Layne, S.P., Beugelsdijk, T.J., Method and apparatus for globally-accessible automated testing (1988), U.S. Patent 5,841,975; Layne, S.P., Beugelsdijk, T.J., Patel, C.K.N., Tackling grand challenges with powerful technologies (2001) Firepower in the Lab: Automation in the Fight Against Infectious Diseases and Bioterrorism, pp. 5-28. , S. P. Layne, T. J. Beugelsdijk, & C. K. Patel (Eds.), Washington, DC: Joseph Henry Press; Human and agricultural health systems (2002) Making the Nation Safer: The Role of Science and Technology in Countering Terrorism, pp. 65-106. , National Research Council Washington, DC: National Academy Press; Gilchrist, M.J.R., The progress, priorities, and concerns of public health laboratories (2002) Biological Threats and Terrorism, pp. 160-165. , S. L. Knobler, A. A. Mahmoud, & L. A. Pray (Eds.), Washington, DC: National Academy Press; Murch, R.S., Forensic Perspective on Bioterrorism and the Proliferation of bioweapons (2001) Firepower in the Lab: Automation in the Fight Against Infectious Diseases and Bioterrorism, pp. 203-213. , S. P. Layne, T. J. Beugelsdijk, & C. K. Patel (Eds.), Washington, DC: Joseph Henry Press; Keim, P., Price, L.B., Klevyiska, A.M., Smith, K.L., Schupp, J.M., Okinaka, R., Jackson, P.J., Hugh-Jones, M.E., Multiple-locus variable-number tandem repeat analysis reveals genetic relationships within Bacillus anthracis (2000) J. Bacteriol., 182, pp. 2928-2936; Read, T.M., Salzberg, S.L., Pop, M., Shumway, M., Umayam, L., Jiang, L., Holtzapple, E., Fraser, C.M., Comparative Genome Sequencing for Discovery of Novel Polymorphisms in Bacillus anthracis (2002) Science, 296, pp. 2028-2033; Christopher, G.W., Cieslak, T.J., Pavlin, J.A., Eitzen, E.M., Biological warfare: A historical perspective (1997) J. Am. Med. Assoc., 278, pp. 412-417; Fraser, C.M., Dando, M.R., Genomics and future of biological weapons: The need for preventive action by the biomedical community (2001) Nat. Genet., 29, pp. 253-256; Grundmann, J.G., Reliability, availability and maintainability for a laboratory automated storage and retrieval system (1989) Laboratory Robotics and Automation, 1, pp. 95-104; Layne, S.P., Beugelsdijk, T.J., Patel, C.K.N., Taubenberger, J.K., Cox, N.C., Gust, I.D., Hay, A.J., Lavanchy, D., A global lab against influenza (2001) Science, 293, p. 1729; LeDuc, J.W., Damon, I., Meegan, J.M., Relman, D.A., Huggins, J., Jahrling, P.B., Smallpox research activities: U.S. Interagency collaboration 2001 (2002) Emerging Inf. Dis, 8, pp. 743-745; Jackson, R.J., Ramsay, A.J., Christensen, C.D., Beaton, S., Hall, D.F., Ramshaw, I.A., Expression of Mouse Interleukin-4 by a Recombinant Ectromelia Virus Suppresses Cytolytic Lymphocyte Responses and Overcomes Genetic Resistance to Mousepox (2001) J. Virol., 75, pp. 1205-1210; (2001), U.S. Congress. Uniting and Strengthening America by Providing Appropriate Tools Required to Intercept and Obstruct Terrorism (USA Patriot Act) Act of 2001. October 25; Layne, S.P., Fraser, C.M., Scientific speed is the key in fighting bioterror (2002) Los Angeles Times, pp. B13. , May 1","Beugelsdijk, T.J.; IBD Division, Los Alamos National Laboratory, P.O. Box 1663, Los Alamos, NM 87545, United States; email: beugelsdijk@lanl.gov",,,15355535,,JALLF,,"English","JALA J. Assoc. Lab. Autom.",Article,"Final",,Scopus,2-s2.0-0842301398
"Zhang J., Meng B., Liao D., Zhou L., Zhang X., Chen L., Guo Z., Peng C., Zhu B., Lee P.P., Xu X., Zhou T., Deng Z., Hu Y., Li K.","8872599200;57213514796;7202026828;7404125414;55864033600;26662813100;7404658178;56413736600;7401683319;54417589800;7405295865;7402989468;55449479900;8555622800;24802383200;","De Novo Synthesis of PCR Templates for the Development of SARS Diagnostic Assay",2003,"Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology","25","2",,"107","112",,9,"10.1385/MB:25:2:107","https://www.scopus.com/inward/record.uri?eid=2-s2.0-12444310103&doi=10.1385%2fMB%3a25%3a2%3a107&partnerID=40&md5=3291052fb9022278923c74ddd3c7bb3f","Genomapping Inc., Tianjin, China; Shanghai Inst. Brain Funct. Genom., Esat China Normal University, Shanghai, China; Institute of SNP, Inst. of Pharmacy and Pharmacology, Nanhua University, Hengyang, China; Univ. of California in San Diego, San Diego, CA, United States; Department of Medical Genetics, First Military Medical University, Guangzhou, China; Inst. of Life Sci. and Biotechnology, Jinana University, Guangzhou, China; Genomics Group, Loma Linda University, Loma Linda, CA, United States","Zhang, J., Genomapping Inc., Tianjin, China; Meng, B., Shanghai Inst. Brain Funct. Genom., Esat China Normal University, Shanghai, China; Liao, D., Institute of SNP, Inst. of Pharmacy and Pharmacology, Nanhua University, Hengyang, China; Zhou, L., Shanghai Inst. Brain Funct. Genom., Esat China Normal University, Shanghai, China; Zhang, X., Genomapping Inc., Tianjin, China; Chen, L., Genomapping Inc., Tianjin, China; Guo, Z., Genomapping Inc., Tianjin, China; Peng, C., Genomapping Inc., Tianjin, China; Zhu, B.; Lee, P.P., Univ. of California in San Diego, San Diego, CA, United States; Xu, X., Department of Medical Genetics, First Military Medical University, Guangzhou, China; Zhou, T., Inst. of Life Sci. and Biotechnology, Jinana University, Guangzhou, China; Deng, Z., Genomapping Inc., Tianjin, China, Genomics Group, Loma Linda University, Loma Linda, CA, United States; Hu, Y.; Li, K., Genomapping Inc., Tianjin, China, Institute of SNP, Inst. of Pharmacy and Pharmacology, Nanhua University, Hengyang, China, Inst. of Life Sci. and Biotechnology, Jinana University, Guangzhou, China","A novel coronavirus was identified as the cause for severe acute respiratory syndrome (SARS). The complete sequence of SARS genome has provided an opportunity for the development of molecular diagnostic assays. To restrain further outbreak of SARS, the World Health Organization has posted several pairs of polymerase chain reaction (PCR) primers for early diagnosis and urged more research to be done on PCR protocols. Here we report a strategy for the de novo synthesis of PCR templates complimentary to the SARS virus genome, which has the advantage of working on PCR templates without concern about viral infection and also has the advantage that it can be used by those who do not have access to the SARS virus. This highly efficient and safe strategy for obtaining SARS gene fragments is useful for the development of PCR assays, as well as for the preparation of reliable positive controls for PCR testing kits.","Gene synthesis; PCR; SARS; Sequential primer extension","acute respiratory tract disease; article; Coronavirus; diagnostic test; epidemic; nonhuman; polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; synthesis; virus genome; virus infection; world health organization; Base Sequence; Diagnostic Tests, Routine; DNA, Complementary; Molecular Sequence Data; Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome; Templates, Genetic; Coronavirus; SARS coronavirus","Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; (2003) Use of Laboratory Methods for SARS Diagnosis, , http://www.who.int/csr/sars/labmethods/en/print.html; Ashraf, H., Investigations continue as SARS claims more lives (2003) Lancet, 361, p. 1276; Zhang, J., Li, K., Deng, Z., Liao, D., Fang, W., Zhang, X., Efficient mutagenesis method for producing the template of single nucleotide polymorphisms (2003) Mol. Biotechnol., 24, pp. 105-110; Horton, R.M., Cai, Z., Ho, S.N., Pease, L.R., Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction (1990) Biotechniques, 8, pp. 528-535","Li, K.; Genomapping Inc., Tianjin, China; email: kaili34@yahoo.com",,,10736085,,MLBOE,"14526121","English","Appl. Biochem. Biotechnol. Part B Mol. Biotechnol.",Article,"Final",,Scopus,2-s2.0-12444310103
"Wei W.I., Tuen H.H., Ng R.W.M., Lam L.K.","7403321552;6602991320;7102153861;7201984637;","Safe tracheostomy for patients with severe acute respiratory syndrome",2003,"Laryngoscope","113","10",,"1777","1779",,6,"10.1097/00005537-200310000-00022","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141864399&doi=10.1097%2f00005537-200310000-00022&partnerID=40&md5=08f183407b91c4a1cadb4505d67cc99c","Department of Surgery, Univ. of Hong Kong Medical Centre, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong","Wei, W.I., Department of Surgery, Univ. of Hong Kong Medical Centre, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong; Tuen, H.H.; Ng, R.W.M.; Lam, L.K.","Objectives/Hypothesis: Severe acute respiratory syndrome (SARS) caused by coronavirus has become an epidemic affecting many regions worldwide. Fourteen percent to 20% of patients require endotracheal intubation and ventilator support. Some of these patients may require tracheostomy subsequently. This procedure, when performed without protection, may lead to infection of the medical and nursing staff taking care of the patient. Study Design: Based on clinical information of three patients. Methods: The authors carried out an emergency tracheostomy and changed the tracheostomy tube for one patient and performed elective tracheostomy in another two patients. Results: No medical or nursing staff member was infected after carrying out the procedure while taking all the precautions and wearing the appropriate protective apparel. Conclusion: The authors have prepared guidelines for performing a safe tracheostomy under both elective and emergency conditions. Surgeons who might be involved in performing the tracheostomy should become familiar with these guidelines and the appropriate protective apparel.",,"ribavirin; adult; article; artificial ventilation; case report; clinical practice; Coronavirus; emergency treatment; endotracheal intubation; glove; hospital infection; human; infection prevention; male; medical staff; nurse; pneumonia; practice guideline; priority journal; protective clothing; severe acute respiratory syndrome; tracheostomy; treatment indication; Emergency Medical Services; Humans; Intubation, Intratracheal; Male; Middle Aged; Practice Guidelines; Severe Acute Respiratory Syndrome; Surgical Procedures, Elective; Tracheostomy","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., Chan, P., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Kondro, W., SARS virus claims its third victim in Canada (2003) Lancet, 361, p. 1106; Qian, Y., Willeke, K., Grinshpun, S.A., Donnelly, J., Coffey, C.C., Performance of N95 respirators: Filtration efficiency for airborne microbial and inert particles (1998) Am Ind Hyg Assoc J, 59, pp. 128-132","Wei, W.I.; Department of Surgery, Univ. of Hong Kong Medical Centre, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong; email: hrmswwi@hkucc.hku.hk",,,0023852X,,LARYA,"14520105","English","Laryngoscope",Article,"Final",Open Access,Scopus,2-s2.0-0141864399
"Wong G.W.K., Li A.M., Ng P.C., Fok T.F.","55664161600;7403291810;17137242500;7006455238;","Severe acute respiratory syndrome in children",2003,"Pediatric Pulmonology","36","4",,"261","266",,34,"10.1002/ppul.10367","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141743699&doi=10.1002%2fppul.10367&partnerID=40&md5=fd951d22953c4b15c14d19d939fef8ca","Department of Pediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Department of Pediatrics, Prince of Wales Hospital, Shatin, New Territories, Hong Kong","Wong, G.W.K., Department of Pediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong, Department of Pediatrics, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Li, A.M., Department of Pediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Ng, P.C., Department of Pediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong; Fok, T.F., Department of Pediatrics, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong, Hong Kong","Severe acute respiratory syndrome (SARS) is a newly described and highly contagious respiratory infection. Many adult patients will develop progressive hypoxia, and a large proportion will develop respiratory distress syndrome (RDS), possibly related to massive and uncontrolled activation of the immune system. The mortality has been reported to be quite high, especially in the elderly with comorbid conditions. The causative agent has been identified as a novel coronavirus, and children appear to acquire the infection by close-contact household exposure to an infected adult. However, the severity is much milder and the clinical progression much less aggressive in young children. The exact pathophysiology of SARS is still unclear, and the medical treatment of SARS remains controversial. The main treatment regime used in Hong Kong is a combination of ribavirin and steroid. To date, there have been no reported case fatalities in children with this disease. The success of reducing the burden of this infection in children will depend on proper isolation of infected adults early in the course of illness. Strict public health policy and quarantine measures are the key in controlling the infection in the community. © 2003 Wiley-Liss, Inc.","Coronavirus; Respiratory infection; Severe acute respiratory syndrome","cefotaxime; clarithromycin; hydrocortisone; methylprednisolone; prednisolone; ribavirin; steroid; child; childhood disease; communicable disease; community care; comorbidity; Coronavirus; disease course; disease severity; fatality; health care policy; Hong Kong; household; human; hypoxia; immunostimulation; infection control; mortality; pathophysiology; patient care; priority journal; respiratory tract infection; review; severe acute respiratory syndrome; Antiviral Agents; Child; Humans; Infection Control; Public Health; Ribavirin; Severe Acute Respiratory Syndrome","(2003) Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/; Lee, N., Hui, D.S., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Poutanen, S.M., Low, D.E., Henry, B., Finkestein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Hsu, L.Y., Lee, C.C., Green, J.A., Ang, B., Paton, N.I., Lee, L., Villacian, J.S., Leo, Y.S., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9, pp. 713-717; (2003) WHO Collaborative Multi-Centre Research Project on Severe Acute Respiratory Syndrome (SARS) Diagnosis, , http://www.who.int/csr/sars/project/en/; Periris, J.S., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory (2003) N Engl J Med, 348, pp. 1953-1966; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridas (1997) Arch Virol, 142, pp. 629-633; Siddell, S.G., Snijder, E.J., Coronaviruses, toroviruses, and arteriviruses (1998) Tropley and Wilson's Microbiology and Microbial Infections, pp. 463-484. , Mahy BWJ, Collier L, editors. London: Edward Arnold; Wege, H., Siddell, S., Ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr Top Microbiol Immunol, 99, pp. 165-200; Yeager, C.L., Ashmun, R.A., Williams, R.K., Cardellichio, C.B., Shapiro, L.H., Look, A.T., Holmes, K.V., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; (2003) Interpreting SARS Test Results, , http://www.cdc.gov/ncidod/sars/testresultsc.htm; Hon, E.K., Leung, C.W., Cheng, W.T., Chan, P.K., Chu, W.C., Kwan, Y.W., Li, A.M., Fok, T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Chiu, W.K., Cheung, P.C., Ng, K.L., Lp, P.L., Sugunan, V.K., Luk, D.C., Ma, L.C., Lai, W.M., Severe acute respiratory syndrome in children: Experience in a regional hospital in Hong Kong (2003) Pediatr Crit Care Med, 4, pp. 279-283; Wong, G.W.K., Hui, D.S.C., Severe acute respiratory syndrome (SARS): Epidemiology, diagnosis and treatment (2003) Thorax, 58, pp. 558-560; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/casedefinition.htm; Epler, G.R., Bronchiolitis obliterans organizing pneumonia (2001) Arch Intern Med, 161, pp. 158-164; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.I., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Seto, W.H., Tsang, D., Yung, R.W., Ching, T.Y., Ng, T.K., Ho, M., Ho, L.M., Peiris, J.S., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; (2003) First Data on Stability and Resistance of SARS Coronavirus Complied by Members of WHO Laboratory Network, , http://www.who.int/csr/sars/survival_2003_05_04/en/; (2003) Hospital Infection Control Guidance for Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/infectioncontrol/en/","Wong, G.W.K.; Department of Pediatrics, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; email: wingkinwong@cuhk.edu.hk",,,87556863,,PEPUE,"12950037","English","Pediatr. Pulmonol.",Review,"Final",Open Access,Scopus,2-s2.0-0141743699
"Chen H., Coote B., Attree S., Hiscox J.A.","57209632300;6603390953;57153931200;7004565877;","Evaluation of a nucleoprotein-based enzyme-linked immunosorbent assay for the detection of antibodies against infectious bronchitis virus",2003,"Avian Pathology","32","5",,"519","526",,34,"10.1080/0307945031000154125","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142071660&doi=10.1080%2f0307945031000154125&partnerID=40&md5=64bf0dbddcd1d60be238f804a7940312","Sch. of Anim. and Microbial Sci., University of Reading, Reading, United Kingdom; Sch. of Biochem. and Molec. Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom","Chen, H., Sch. of Anim. and Microbial Sci., University of Reading, Reading, United Kingdom; Coote, B.; Attree, S.; Hiscox, J.A., Sch. of Biochem. and Molec. Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom","As an immunogen of the coronavirus, the nucleoprotein (N) is a potential antigen for the serological monitoring of infectious bronchitis virus (IBV). In this report, recombinant N protein from the Beaudette strain of IBV was produced and purified from Escherichia coli as well as Sf9 (insect) cells, and used for the coating of enzyme-linked immunosorbent assay (ELISA) plates. The N protein produced in Sf9 cells was phosphorylated whereas N protein from E. coli was not. Our data indicated that N protein purified from E. coli was more sensitive to anti-IBV serum than the protein from Sf9 cells. The recombinant N protein did not react with the antisera to other avian pathogens, implying that it was specific in the recognition of IBV antibodies. In addition, the data from the detection of field samples and IBV strains indicated that using the recombinant protein as coating antigen could achieve an equivalent performance to an ELISA kit based on infected material extracts as a source of antigen(s). ELISAs based on recombinant proteins are safe (no live virus), clean (only virus antigens are present), specific (single proteins can be used) and rapid (to respond to new viral strains and strains that cannot necessarily be easily cultured).",,"Animals; Antibodies, Viral; Antigens, Viral; Chickens; Coronavirus Infections; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Guinea Pigs; Infectious bronchitis virus; Nucleoproteins; Poultry Diseases; Recombinant Proteins; Safety; Sensitivity and Specificity; Specific Pathogen-Free Organisms; Time Factors; Aves; Avian infectious bronchitis virus; Coronavirus; Escherichia coli; Insecta","Alonso, J.M.M., Balbin, M., Garwes, D.J., Enjuanes, L., Gascon, S., Parra, F., Antigenic structure of transmissible gastroenteritis virus nucleoprotein (1992) Virology, 188, pp. 168-174; Breslin, J.J., Smith, L.G., Guy, J.S., Baculovirus expression of turkey coronavirus nucleocapsid protein (2001) Avian Diseases, 45, pp. 136-143; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , S.G. Siddell (Ed.), New York: Plenum Press; Cavanagh, D., Innovation and discovery: The application of nucleic acid-based technology to avian virus detection and characterization (2001) Avian Pathology, 30, pp. 581-598; Cavanagh, D., Davis, P.J., Darbyshire, J.H., Peters, R.W., Coronavirus Ibv - Virus retaining spike glycopolypeptide-S2 but not S1 is unable to induce virus-neutralizing or hemagglutination-inhibiting antibody, or induce chicken tracheal protection (1986) Journal of General Virology, 67, pp. 1435-1442; Cavanagh, D., Mawditt, K., Sharma, M., Drury, S.E., Ainsworth, H.L., Britton, P., Gough, R.E., Detection of a coronavirus from turkey poults in Europe genetically related to infectious bronchitis virus of chickens (2001) Avian Pathology, 30, pp. 355-368; Cavanagh, D., Naqi, S., Infectious bronchitis (1997) Diseases of Poultry, pp. 511-526. , H.W. Yoda (Ed.), Ames, IA: Iowa State University Press; Chen, B.Y., Hosi, S., Nunoya, T., Itakura, C., Histopathology and immunohistochemistry of renal lesions due to infectious bronchitis virus in chicks (1996) Avian Pathology, 25, pp. 269-284; Chen, H., Wurm, T., Britton, P., Brooks, G., Hiscox, J.A., Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell (2002) Journal of Virology, 76, pp. 5233-5250; Cook, J.K., Cavanagh, D., Detection and differentiation of avian pneumoviruses (metapneumoviruses) (2002) Avian Pathology, 31, pp. 117-132; De Wit, J.J., Detection of infecitous bronchitis virus (2000) Avian Pathology, 29, pp. 71-93; Fouts, D.E., True, H.L., Cengel, K.A., Celander, D.W., Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation (1997) Biochemistry, 43, pp. 13256-13262; Guy, J.S., Smith, L.G., Breslin, J.J., Pakpinyo, S., Development of a competitive enzyme-linked immunosorbent assay for detection of turkey coronavirus antibodies (2002) Avian Diseases, 46, pp. 334-341; Hiscox, I.A., Wurm, T., Wilson, L., Cavanagh, D., Britton, P., Brooks, G., The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus (2001) Journal of Virology, 75, pp. 506-512; Lai, M.M.C., Cavanagh, D., The molecular biology of coronaviruses (1997) Advances in Virus Research, 48, pp. 1-100; Laude, H., Masters, P.S., The coronavirus nucleocapsid protein (1995) The Coronaviridae, pp. 141-163. , S.G. Siddell (Ed.), New York: Plenum Press; Marquardt, W.W., Snyder, D.B., Schlotthober, B.A., Detection and quantification of antibodies to infectious bronchitis virus by enzyme-linked immunosorbent assay (1981) Avian Diseases, 25, pp. 713-722; Masters, P.S., Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus (1992) Archives of Virology, 125, pp. 141-160; Ndifuna, A., Waters, A.K., Zhou, M., Collisson, E.W., Recombinant nucleocapsid protein is potentially an inexpensive, effective serodiagnostic reagent for infectious bronchitis virus (1998) Journal of Virological Methods, 70, pp. 37-44; Peng, D., Koetzner, C.A., McMahon, T., Zhu, Y., Masters, P.S., Construction of murine coronavirus mutants containing interspecies chimeric nucleocapsid proteins (1995) Journal of Virology, 69, pp. 5475-5484; Pulford, D.J., Britton, P., Expression and cellular localisation of porcine transmissible gastroenteritis virus N and M proteins by recombinant vaccinia virus (1991) Virus Research, 18, pp. 203-218; Raj, G.D., Jones, R.C., Immunopathogenesis of infection in SPF chicks and commercial broiler chickens of a variant infectious bronchitis virus of economic importance (1996) Avian Pathology, 25, pp. 481-502; Raj, G.D., Jones, R.C., Infectious bronchitis virus: Immunopathogenesis of infection in the chicken (1997) Avian Pathology, 26, pp. 677-706; Risco, C., Anton, I.M., Enjuanes, L., Carrascosa, J.L., The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins (1996) Journal of Virology, 70, pp. 4773-4777; Seo, S.H., Wang, L., Smith, R., Collisson, E.W., The carboxyl-terminal 120-residue polypeptide of infectious bronchitis virus nucleocapsid induces cytotoxic T lymphocytes and protects chickens from acute infection (1997) Journal of Virology, 71, pp. 7889-7894; Stohlman, S.A., Fleming, J.O., Patton, C.D., Lai, M.M.C., Synthesis and subcellular-localization of the murine coronavirus nucleocapsid protein (1983) Virology, 130, pp. 527-532; Wang, C.H., Hong, C.C., Seak, J.C., An ELISA for antibodies against infectious bronchitis virus using an S1 spike polypeptide (2002) Veterinary Microbiology, 85, pp. 333-342; Wilbur, S.M., Nelson, G.W., Lai, M.M.C., McMillan, M., Stohlman, S.A., Phosphorylation of the mouse hepatitis virus nucleocapsid protein (1986) Biochemistry and Biophysics Research Communication, 141, p. 7; Williams, A.K., Wang, L., Sneed, L.W., Collisson, E.W., Comparative analyses of the nucleocapsid genes of several strains of infectious bronchitis virus and other viruses (1992) Virus Research, 25, pp. 213-222; Wurm, T., Chen, H., Britton, P., Brooks, G., Hiscox, J.A., Localisation to the nucleolus is a common feature of coronavirus nucleoproteins and the protein may disrupt host cell division (2001) Journal of Virology, 75, pp. 9345-9356; Zhou, M.L., Collinson, E.W., The amino and carboxyl domains of the infectious bronchitis virus nucleocapsid protein interact with 3′ genomic RNA (2000) Virus Research, 67, pp. 31-39; Zhou, M.L., Williams, A.K., Chung, S.I., Wang, L., Collisson, E.W., Infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3′ terminus of the genome (1996) Virology, 217, pp. 191-199","Hiscox, J.A.; Sch. of Biochem. and Molec. Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom; email: j.a.hiscox@bmb.leeds.ac.uk",,,03079457,,AVPAD,"14522708","English","Avian Pathol.",Article,"Final",,Scopus,2-s2.0-0142071660
"Van Benten I., Koopman L., Niesters B., Hop W., Van Middelkoop B., De Waal L., Van Drunen K., Osterhaus A., Neijens H., Fokkens W., Van Drunen C.M.","6602761888;6701917899;7006807127;36041163400;6507381206;57194067003;57202301148;55533604400;7005377066;35355799700;6602688670;","Predominance of rhinovirus in the nose of symptomatic and asymptomatic infants",2003,"Pediatric Allergy and Immunology","14","5",,"363","370",,97,"10.1034/j.1399-3038.2003.00064.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744226378&doi=10.1034%2fj.1399-3038.2003.00064.x&partnerID=40&md5=6841f2fec2be16a0cb381d504f1f252d","Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Department of Paediatrics, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Institute for Virology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Biostatistics and Epidemiology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Department of Otorhinolaryngology, Amsterdam Medical Center, PO Box 22660, 1100 DD Amsterdam, Netherlands","Van Benten, I., Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Koopman, L., Department of Paediatrics, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Niesters, B., Institute for Virology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Hop, W., Biostatistics and Epidemiology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Van Middelkoop, B., Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; De Waal, L., Institute for Virology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Van Drunen, K., Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Osterhaus, A., Institute for Virology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Neijens, H., Department of Paediatrics, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Fokkens, W., Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; Van Drunen, C.M., Department of Otorhinolaryngology, Amsterdam Medical Center, PO Box 22660, 1100 DD Amsterdam, Netherlands","Respiratory infections in infancy may protect against developing Th2-mediated allergic disease (hygiene hypothesis). To estimate the relative contribution of particular viruses to the development of the immune system and allergic disease, we investigated longitudinally the prevalence of respiratory viral infections in infants. One hundred and twenty-six healthy infants were included in this prospective birth cohort study in their first year of life. Physical examination was performed and nasal brush samples were taken during routine visits every 6 months and during an upper respiratory tract infection (URTI) (sick visits). The prevalence of respiratory viral infections in infants with URTI, infants with rhinitis without general malaise and infants without nasal symptoms was studied. Rhinovirus was the most prevalent pathogen during URTI and rhinitis in 0- to 2-year-old infants (∼40%). During URTI, also respiratory syncytial virus (∼20%) and coronavirus (∼10%) infections were found, which were rarely detected in infants with rhinitis. Surprisingly, in 20% of infants who did not present with nasal symptoms, rhinovirus infections were also detected. During routine visits at 12 months, a higher prevalence of rhinovirus infections was found in infants who attended day-care compared with those who did not. We did not observe a relation between breast-feeding or smoking by one or both parents and the prevalence of rhinovirus infections. The parental history of atopy was not related to the prevalence of rhinovirus infection, indicating that the genetic risk of allergic disease does not seem to increase the chance of rhinovirus infections. In conclusion, rhinovirus infection is the most prevalent respiratory viral infection in infants. It may therefore affect the maturation of the immune system and the development of allergic disease considerably.","Allergy; Day-care; Infant; Prevalence; Respiratory infection; Rhinovirus; RSV","age; article; atopic dermatitis; atopy; child; child welfare; comparative study; controlled study; Coronavirus; cytomegalic inclusion body disease; day care; environmental exposure; female; follow up; genetic predisposition; genetic risk; hospitalization; human; immune system; infant; infant welfare; longitudinal study; major clinical study; male; Netherlands; newborn; nose infection; Picornavirus infection; prediction and forecasting; preschool child; prevalence; priority journal; prospective study; Respiratory syncytial pneumovirus; respiratory tract infection; rhinitis; Rhinovirus; risk factor; statistical model; symptomatology; Th2 cell; upper respiratory tract infection; virology; virus detection; virus infection; Age Factors; Child Day Care Centers; Child Welfare; Child, Preschool; Coronavirus Infections; Cytomegalovirus Infections; Dermatitis, Atopic; Environmental Exposure; Female; Follow-Up Studies; Genetic Predisposition to Disease; Humans; Infant; Infant Welfare; Infant, Newborn; Logistic Models; Male; Netherlands; Picornaviridae Infections; Predictive Value of Tests; Prevalence; Prospective Studies; Respiratory Syncytial Virus Infections; Respiratory Tract Infections; Rhinovirus; Risk Factors; Severity of Illness Index; Statistics","Gern, J.E., Busse, W.W., Association of rhinovirus infections with asthma (1999) Clin Microbiol Rev, 12, pp. 9-18; Finkelman, F.D., Urban J.F., Jr., The other side of the coin: The protective role of the TH2 cytokines (2001) J Allergy Clin Immunol, 107, pp. 772-780; Hunter, C.A., Reiner, S.L., Cytokines T cells in host defense (2000) Curr Opin Immunol, 12, pp. 413-418; Kuehni, C.E., Davis, A., Brooke, A.M., Silverman, M., Are all wheezing disorders in very young (preschool) children increasing in prevalence? (2001) Lancet, 357, pp. 1821-1825; Prescott, S.L., Macaubas, C., Smallacombe, T., Holt, B.J., Sly, P.D., Holt, P.G., Development of allergen-specific T-cell memory in atopic and normal children (1999) Lancet, 353, pp. 196-200; Strachan, D.P., Hay fever, hygiene, and household size (1989) BMJ, 299, pp. 1259-1260; Bjorksten, B., Naaber, P., Sepp, E., Mikelsaar, M., The intestinal microflora in allergic Estonian and Swedish 2-year-old children (1999) Clin Exp Allergy, 29, pp. 342-346; Matricardi, P.M., Rosmini, F., Riondino, S., Exposure to foodborne and orofecal microbes versus airborne viruses in relation to atopy and allergic asthma: Epidemiological study (2000) BMJ, 320, pp. 412-417; Denny F.W., Jr., The clinical impact of human respiratory virus infections (1995) Am J Respir Crit Care Med, 152 (SUPPL. 4 PART 2), pp. S4-S12; Kramer, U., Heinrich, J., Wjst, M., Wichmann, H.E., Age of entry to day nursery and allergy in later childhood (1999) Lancet, 353, pp. 450-454; Ball, T.M., Castro-Rodriguez, J.A., Griffith, K.A., Holberg, C.J., Martinez, F.D., Wright, A.L., Siblings day-care attendance, and the risk of asthma and wheezing during childhood (2000) N Engl J Med, 343, pp. 538-543; Illi, S., Von Mutius, E., Lau, S., Early childhood infectious diseases and the development of asthma up to school age: A birth cohort study (2001) BMJ, 322, pp. 390-395; Sigurs, N., Bjarnason, R., Sigurbergsson, F., Kjellman, B., Respiratory syncytial virus bronchiolitis in infancy is an important risk factor for asthma and allergy at age 7 (2000) Am J Respir Crit Care Med, 161, pp. 1501-1507; Stein, R.T., Sherrill, D., Morgan, W.J., Respiratory syncytial virus in early life and risk of wheeze and allergy by age 13 years (1999) Lancet, 354, pp. 541-545; Makela, M.J., Puhakka, T., Ruuskanen, O., Viruses and bacteria in the etiology of the common cold (1998) J Clin Microbiol, 36, pp. 539-542; Arruda, E., Pitkaranta, A., Witek T.J., Jr., Doyle, C.A., Hayden, F.G., Frequency natural history of rhinovirus infections in adults during autumn (1997) J Clin Microbiol, 35, pp. 2864-2868; Johnston, S.L., Pattemore, P.K., Sanderson, G., Community study of role of viral infections in exacerbations of asthma in 9-11 year old children (1995) BMJ, 310, pp. 1225-1229; Izurieta, H.S., Thompson, W.W., Kramarz, P., Influenza and the rates of hospitalization for respiratory disease among infants and young children (2000) N Engl J Med, 342, pp. 232-239; Reed, G., Jewett, P.H., Thompson, J., Tollefson, S., Wright, P.F., Epidemiology clinical impact of parainfluenza virus infections in otherwise healthy infants and young children 5 years old (1997) J Infect Dis, 175, pp. 807-813; Rakes, G.P., Arruda, E., Ingram, J.M., Rhinovirus and respiratory syncytial virus in wheezing children requiring emergency care. IgE and eosinophil analyses (1999) Am J Respir Crit Care Med, 159, pp. 785-790; Vesa, S., Kleemola, M., Blomqvist, S., Takala, A., Kilpi, T., Hovi, T., Epidemiology of documented viral respiratory infections and acute otitis media in a cohort of children followed from two to twenty-four months of age (2001) Pediatr Infect Dis J, 20, pp. 574-581; Koopman, L.P., Smit, H.A., Heijnen, M.L., Respiratory infections in infants: Interaction of parental allergy, child care, and siblings-the piama study (2001) Pediatrics, 108, pp. 943-948; Lakwijk, N., Van Strien, R.T., Doekes, G., Brunekreef, B., Gerritsen, J., Validation of a screening questionnaire for atopy with serum IgE tests in a population of pregnant Dutch women (1998) Clin Exp Allergy, 28, pp. 454-458; Godthelp, T., Holm, A.F., Fokkens, W.J., Dynamics of nasal eosinophils in response to a nonnatural allergen challenge in patients with allergic rhinitis and control subjects: A biopsy and brush study (1996) J Allergy Clin Immunol, 97, pp. 800-811; Pitkaranta, A., Arruda, E., Malmberg, H., Hayden, F.G., Detection of rhinovirus in sinus brushings of patients with acute community-acquired sinusitis by reverse transcription-PCR (1997) J Clin Microbiol, 35, pp. 1791-1793; Hyypia, T., Puhakka, T., Ruuskanen, O., Makela, M., Arola, A., Arstila, P., Molecular diagnosis of human rhinovirus infections: Comparison with virus isolation (1998) J Clin Microbiol, 36, pp. 2081-2083; Blomqvist, S., Roivainen, M., Puhakka, T., Kleemola, M., Hovi, T., Virological serological analysis of rhinovirus infections during the first two years of life in a cohort of children (2002) J Med Virol, 66, pp. 263-268; Gergen, P.J., Fowler, J.A., Maurer, K.R., Davis, W.W., Overpeck, M.D., The burden of environmental tobacco smoke exposure on the respiratory health of children 2 months through 5 years of age in the United States. Third National Health Nutrition Examination Survey, 1988 to 1994 (1998) Pediatrics, 101, pp. E8; Cushing, A.H., Samet, J.M., Lambert, W.E., Breast-feeding reduces risk of respiratory illness in infants (1998) Am J Epidemiol, 147, pp. 863-870; Zambon, M.C., Stockton, J.D., Clewley, J.P., Fleming, D.M., Contribution of influenza and respiratory syncytial virus to community cases of influenza-like illness: An observational study (2001) Lancet, 358, pp. 1410-1416; Harsten, G., Prellner, K., Lofgren, B., Heldrup, J., Kalm, O., Kornfalt, R., Serum antibodies against respiratory tract viruses: A prospective three-year follow-up from birth (1989) J Laryngol Otol, 103, pp. 904-908; Van Kempen, M., Bachert, C., Van Cauwenberge, P., An update on the pathophysiology of rhinovirus upper respiratory tract infections (1999) Rhinology, 37, pp. 97-103; Brandenburg, A.H., Kleinjan, A., Van Het Land, B., Type 1-like immune response is found in children with respiratory syncytial virus infection regardless of clinical severity (2000) J Med Virol, 62, pp. 267-277; Nokso-Koivisto, J., Kinnari, T.J., Lindahl, P., Hovi, T., Pitkaranta, A., Human picornavirus and coronavirus RNA in nasopharynx of children without concurrent respiratory symptoms (2002) J Med Virol, 66, pp. 417-420; Gluck, U., Gebbers, J.O., The nose as a bacterial reservoir: Important differences between the vestibule and cavity (2000) Laryngoscope, 110 (SUPPL. 3 PART 1), pp. S426-S428","Van Benten, I.; Department of Otorhinolaryngology, Erasmus Univ. Med. Center Rotterdam, Rotterdam, Netherlands; email: c.m.vandrunen@amc.uva.nl",,,09056157,,PALUE,"14641606","English","Pediatr. Allergy Immunol.",Article,"Final",,Scopus,2-s2.0-10744226378
"Yu H., Yang Y., Zhang W., Xie Y.-H., Qin J., Wang Y., Zheng H.-B., Zhao G.-P., Yang S., Jiang W.-H.","7405852251;7409382210;36066941200;8677139000;7402896300;7601499551;8917917300;7403296532;22837280100;7403697918;","Expression and purification of recombinant sars coronavirus spike protein",2003,"Acta Biochimica et Biophysica Sinica","35","8",,"774","778",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744232797&partnerID=40&md5=251bd97aa5049721ac4c2126bd1dbf43","Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Inst. of Biochem. and Cell Biology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China","Yu, H., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Yang, Y., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Zhang, W., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Xie, Y.-H., Inst. of Biochem. and Cell Biology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Qin, J., Inst. of Biochem. and Cell Biology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Wang, Y., Inst. of Biochem. and Cell Biology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200031, China; Zheng, H.-B., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Zhao, G.-P., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Yang, S., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Jiang, W.-H., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China","A novel coronavirus (SARS-coronavirus, SARS-CoV) was discovered in association with cases of severe acute respiratory syndrome (SARS) recently. The first step in coronavirus infection is binding of the viral spike protein to certain receptor on host cells. The spike protein is the main surface antigen of the coronavirus and there should be antibodies against spike protein in patients' serum. Thus, to develop and expression protein fragment from spike protein gene are the purposes of this experiment. Partial spike gene fragments (751 ∼ 1925 bp, 2005 ∼ 3410 bp, 1 ∼ 1925 bp and 32 ∼ 3659 bp) and its intact gene were cloned into pET32 or pGEX vectors, and transformed into competent Escherichia coli BL21(DE3) (pLysS), respectively. 63, 78, 98, 160 and 164 kD fusion proteins were successfully expressed with amounts of 35%, 34%, 24%, 17% and 5% of total cell protein. The soluble parts of the cell crude extract were then partially purified by GST affinity chromatography.","Coronavirus; Expression; Severe acute respiratory syndrome (SARS); Spike protein","cell extract; cell protein; hybrid protein; membrane antigen; recombinant protein; SARS coronavirus spike protein; unclassified drug; virus antibody; virus protein; affinity chromatography; article; controlled study; Coronavirus; Escherichia coli; expression vector; gene expression; genetic analysis; host cell; molecular cloning; nonhuman; protein binding; protein expression; protein purification; receptor binding; SARS coronavirus; Blotting, Western; Escherichia coli; Membrane Glycoproteins; Recombinant Fusion Proteins; SARS Virus; Viral Envelope Proteins; Coronavirus; Escherichia coli; SARS coronavirus; vectors","Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Identification of severe acute respiratory syndrome in Canada N Engl J Med, , www.nejm.org/, March 31 2003/10.1056/ NEMoa 030634; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., A major outbreak of severe acute respiratory syndrome in Hong Kong N Engl J Med, , www.nejm.org/, April 7 2003/10.1056/NEJ-Moa 030685; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Nicholls, J., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., A novel coronavirus associated with severe acute respiratory syndrome N Engl J Med, , www.nejm.org/, April 10 2003/ 10.1056/NEJMoa 020781; Drosten, C., Günther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becket, S., Rabenau, H., Identification of a novel coronavirus in patients with severe acute respiratory syndrome N Eng J Med, , www.nejm.org/, April 10 2003/10.1056/NEJMoa 030747; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S.N., Khattra, J., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Qin, E.D., Zhu, Q.Y., Yu, M., Fan, B.C., Chang, G.H., Si, B.Y., Yang, B.A., A complete sequence and comparative analysis of strain (BJ01) of the SARS-associated virus (2003) Chinese Sci Bull, 48 (10), pp. 941-948; Rui, W., Zhang, Q.P., Shi, L., Lu, M., Recent trends in research of SARS coronavirus genome, protein and course of invasion into host cell (2003) Chinese Med J, , in press; Pohl-Koppe, A., Raabe, T., Siddell, S.G., Ter, M.V., Detection of human coronavirus 229E-specific antibodies using recombinant fusion proteins (1995) J Virol Methods, 55, pp. 175-183; Wang, C.H., Hong, C.C., Seak, J.C.H., An ELISA for antibodies against infectious bronchitis virus using and S1 spike polypeptide (2002) Vet Microbiol, 85, pp. 333-342; Streatfield, S.J., Jilka, J.M., Hood, E.E., Turner, D.D., Bailey, M.R., Mayor, J.M., Woodard, S.L., Plant-based vaccines: Unique advantages (2001) Vaccine, 19 (17-19), pp. 2742-2748","Yang, S.; Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; email: syang@sibs.ac.cn",,,05829879,,,"12897976","Chinese","Acta Biochim. Biophys. Sin.",Article,"Final",,Scopus,2-s2.0-10744232797
"Hung C.-C., Hsiao C.-H., Chen Y.-C., Chang S.-C.","7403166331;7202806734;7601447585;57201855866;","Severe acute respiratory syndrome (SARS)",2003,"Journal of Internal Medicine of Taiwan","14","3",,"106","117",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141854178&partnerID=40&md5=ab7cc7b9adcb0659b8236ba14ced700d","Department of Internal Medicine, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan; Department of Pathology, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan","Hung, C.-C., Department of Internal Medicine, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan; Hsiao, C.-H., Department of Pathology, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan; Chen, Y.-C., Department of Internal Medicine, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan; Chang, S.-C., Department of Internal Medicine, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan","Severe acute respiratory syndrome (SARS) is an emerging infectious disease in the 21st century, and, as of June 6, 2003, there were more than 8,000 cases reported from 32 countries and regions, and 779 patients died from the disease. Soon after the onset of the epidemic in China, Vietnam, Singapore, Honk Kong, and Canada, the etiology was identified to be a novel coronavirus (SARS-CoV), of which the genomic sequencing was completed. In this article, we review the epidemiology, clinical manifestations, pathology, and treatment of SARS. In order to prevent infection with SARS, the guidelines of respiratory and contact precautions taken at the National Taiwan University Hospital are proposed for the health care workers around the island.","Coronarvirus; SARS-COV; Emerging infectious disease; Infection control and precaution; Severe acute respiratory syndrome; SARS","azithromycin; cephalosporin derivative; clarithromycin; corticosteroid derivative; immunoglobulin; levofloxacin; moxifloxacin; quinoline derived antiinfective agent; ribavirin; Canada; China; clinical feature; computer assisted tomography; Coronavirus; epidemic; gene sequence; health care personnel; hemolytic anemia; Hong Kong; human; infection control; practice guideline; review; SARS coronavirus; severe acute respiratory syndrome; Singapore; Taiwan; thorax radiography; university hospital; Viet Nam; virus genome; virus identification; virus pneumonia","Cumulative number of reported cases of severe acute respiratory syndrome http://www.who.int/csr/sarscountry/2003_06_06/en, WHO. (SARS); Tsang, K.W., Ho, P.L., Oii, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; http://www.cdc.gov.tw/sars, SARS; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Fouchier, R.A.M., Kuiken, T., Schutten, M., Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Hon, K.L.E., Leung, C.W., Cheng, W.T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Nicholls, J.M., Poon, L.L.M., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; So, L.K.Y., Lau, A.C.W., Yam, L.Y.C., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Cinatl, J., Morgenstern, B., Bauer, G., Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronarvirus (2003) Lancet, 361, pp. 2045-2046; Oba, Y., The use of corticosteroids in SARS (2003) N. Engl. J. Med., 348, pp. 2034-2035; Wenzel, R.P., Edmond, M.B., Managing SARS amidst uncertainty (2003) N. Engl. J. Med., 348, pp. 1947-1948; So, L.K., Seto, W.H., Tsang, D., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Severe acute respiratory syndrome; SARS (2003), 13, pp. 85-89","Hung, C.-C.; Department of Internal Medicine, National Taiwan University, Natl. Taiwan Univ. Coll. of Medicine, Taiwan, Taiwan",,,10167390,,JIMTB,,"Chinese","J. Intern. Med. Taiwan",Review,"Final",,Scopus,2-s2.0-0141854178
"Wenzel R.P., Edmond M.B.","36045112800;56452667800;","Listening to SARS: Lessons for Infection Control",2003,"Annals of Internal Medicine","139","7",,"592","593",,24,"10.7326/0003-4819-139-7-200310070-00012","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142028263&doi=10.7326%2f0003-4819-139-7-200310070-00012&partnerID=40&md5=6eefcee2b0b56a5a92b0fc280229348f","Virginia Commonwealth University, Richmond, VA 23298, United States; Virginia Commonwealth University, Old City Hall, 1001 East Broad Street, Richmond, VA 23298, United States","Wenzel, R.P., Virginia Commonwealth University, Richmond, VA 23298, United States, Virginia Commonwealth University, Old City Hall, 1001 East Broad Street, Richmond, VA 23298, United States; Edmond, M.B., Virginia Commonwealth University, Richmond, VA 23298, United States","The coronavirus that causes SARS is the latest in a series of emerging pathogens that challenge our global society. The virus has a remarkable ability to amplify its communicability to become an almost ""perfect"" nosocomial pathogen. We must institutionalize the critical lessons learned from managing the 2003 SARS epidemic as we prepare for the next emerging pathogen.",,"Coronavirus; disease course; disease transmission; epidemic; hospital infection; human; infection control; priority journal; review; severe acute respiratory syndrome; cross infection; epidemic; note; severe acute respiratory syndrome; standard; United States; Cross Infection; Disease Outbreaks; Humans; Infection Control; Severe Acute Respiratory Syndrome; United States","Holmes, K.V., SARS coronavirus: A new challenge for prevention and therapy (2003) J Clin Invest, 111, pp. 1605-1609. , PMID: 12782660; Enserink, M., Infectious diseases. Clues to the animal origins of SARS (2003) Science, 300, p. 1351. , PMID: 12775803; Altman, L., SARS enigma: Cases decline, but doubts remain (2003) New York Times, pp. A10. , 8 June; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809. , PMID: 12734147; Vogel, G., SARS outbreak. Modelers struggle to grasp epidemic's potential scope (2003) Science, 300, pp. 558-559. , PMID: 12714711; Seto, W.H., Tsang, D., Yung, R.W., Ching, T.Y., Ng, T.K., Ho, M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520. , PMID: 12737864; Ho, A.S., Sung, J.Y., Chan-Yeung, M., An outbreak of severe acute respiratory syndrome among hospital workers in a community hospital in Hong Kong (2003) Ann Intern Med, 139, pp. 564-567","Wenzel, R.P.; Virginia Commonwealth University, Old City Hall, 1001 East Broad Street, Richmond, VA 23298, United States",,"American College of Physicians",00034819,,AIMEA,"14530231","English","Ann. Intern. Med.",Review,"Final",Open Access,Scopus,2-s2.0-0142028263
"Ho A.S., Sung J.J.Y., Chan-Yeung M.","7402675199;35405352400;54790582200;","An Outbreak of Severe Acute Respiratory Syndrome among Hospital Workers in a Community Hospital in Hong Kong",2003,"Annals of Internal Medicine","139","7",,"564","567+I47",,70,"10.7326/0003-4819-139-7-200310070-00008","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1642494791&doi=10.7326%2f0003-4819-139-7-200310070-00008&partnerID=40&md5=7bdf1d84045ee6281e04ff63acc10ed5","Alice Ho Miu Ling Nethersole Hosp., Chinese University of Hong Kong, Hong Kong, Hong Kong; University Department of Medicine, Queen Mary Hospital, 4/F Professorial Block, Hong Kong, Hong Kong","Ho, A.S., Alice Ho Miu Ling Nethersole Hosp., Chinese University of Hong Kong, Hong Kong, Hong Kong; Sung, J.J.Y., Alice Ho Miu Ling Nethersole Hosp., Chinese University of Hong Kong, Hong Kong, Hong Kong; Chan-Yeung, M., Alice Ho Miu Ling Nethersole Hosp., Chinese University of Hong Kong, Hong Kong, Hong Kong, University Department of Medicine, Queen Mary Hospital, 4/F Professorial Block, Hong Kong, Hong Kong","Background: During outbreaks, hospital workers are at high risk for nosocomial infection with severe acute respiratory syndrome (SARS)-associated coronavirus. Objective: To examine how hospital workers became infected and whether they transmit the virus to their families. Design: Retrospective descriptive study. Setting: 529-bed community hospital in Hong Kong. Patients: 40 hospital workers infected with SARS-associated coronavirus over a 6-week period (25 March through 5 May 2003). Measurements: Percentage of infected hospital workers according to job category. Results: The cumulative incidence was highest among health care assistants, followed by physicians and nurses (8%, 5%, and 4%, respectively). Most hospital workers were infected from direct contact with patients with SARS, who primarily were in general wards and had unsuspected infection. At the time of contact, all hospital workers had used masks but not necessarily other protective devices. Affected hospital workers did not infect their families. Conclusion: Before isolation of all patients with clinically confirmed or suspected SARS, routine use of several protective devices, and training of staff in infection control, many health care workers were infected with SARS from patients with unsuspected cases.",,"adult; article; community hospital; epidemic; female; high risk population; Hong Kong; hospital infection; hospital personnel; human; infection control; major clinical study; male; priority journal; SARS coronavirus; severe acute respiratory syndrome; cross infection; disease transmission; epidemic; family; Hong Kong; incidence; methodology; middle aged; retrospective study; severe acute respiratory syndrome; Adult; Cross Infection; Disease Outbreaks; Disease Transmission, Patient-to-Professional; Family; Female; Hong Kong; Humans; Incidence; Infection Control; Male; Middle Aged; Personnel, Hospital; Retrospective Studies; Severe Acute Respiratory Syndrome","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325. , PMID: 12711465; (2003) Severe Acute Respiratory Syndrome. Case Definition and Reporting, , www.ha.org.hk/sars/ps/information/clinical_management.htm; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985. , PMID: 12671062; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994. , PMID: 12682352; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005. , PMID: 12671061; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966. , PMID: 12690092; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976. , PMID: 12690091; (2003) CDC Lab Sequences Genome of New Coronavirus, , www.cdc.gov/od/oc/media/pressrel/r030414.htm, Atlanta: Centers for Diseases Control and Prevention; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , PMID: 12730500; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , PMID: 12730501; Atypical Pneumonia, , www.info.gov.hk/info/sars/e_news_may03.htm; Summary of Severe Acute Respiratory (SARS) Cases: Canada and International, , www.hc-sc.gc.ca/pphb-dgspsp/sars-sras/eu-ae/sars20030501_e.html; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772. , PMID: 12781535; Dwosh, H.A., Hong, H.H., Austgarden, D., Herman, S., Schabas, R., Identification and containment of an outbreak of SARS in a community hospital (2003) CMAJ, 168, pp. 1415-1420. , PMID: 12771070; Riley, S., Fraser, C., Donnelly, C.A., Ghani, A.C., Abu-Raddad, L.J., Hedley, A.J., Transmission dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Science, 300, pp. 1961-1966. , PMID: 12766206; Seto, W.H., Tsang, D., Yung, R.W., Ching, T.Y., Ng, T.K., Ho, M., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520. , PMID: 12737864","Chan-Yeung, M.; University Department of Medicine, Queen Mary Hospital, 4/F Professorial Block, Hong Kong, Hong Kong; email: mmwchan@hkucc.hku.hk",,"American College of Physicians",00034819,,AIMEA,"14530227","English","Ann. Intern. Med.",Article,"Final",Open Access,Scopus,2-s2.0-1642494791
"Wu H.-Y., Guy J.S., Yoo D., Vlasak R., Urbach E., Brian D.A.","57129133800;7202723649;7103242554;56244751900;6701388780;7006460232;","Common RNA replication signals exist among group 2 coronaviruses: Evidence for in vivo recombination between animal and human coronavius molecules",2003,"Virology","315","1",,"174","183",,30,"10.1016/S0042-6822(03)00511-7","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242299781&doi=10.1016%2fS0042-6822%2803%2900511-7&partnerID=40&md5=9ee1434863e085b052848cdf2436bfa4","Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States; Department of Pathobiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States; Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. NIG 2W1, Canada; Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; Department of Agronomy, University of Wisconsin, 1575 Linden Dr., Mandison, WI 53706, United States","Wu, H.-Y., Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Pathobiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States; Guy, J.S., Dept. Farm Anim. Hlth./Rsrc. Mgmt., College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606, United States; Yoo, D., Department of Pathobiology, Ontario Veterinary College, University of Guelph, Guelph, Ont. NIG 2W1, Canada; Vlasak, R., Austrian Academy of Sciences, Institute of Molecular Biology, Department of Biochemistry, Billrothstrasse 11, A-5020 Salzburg, Austria; Urbach, E., Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Agronomy, University of Wisconsin, 1575 Linden Dr., Mandison, WI 53706, United States; Brian, D.A., Department of Microbiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Pathobiology, College of Veterinary Medicine, University of Tennessee, Knoxville, TN 37996-0845, United States, Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States","5′ and 3′ UTR sequences on the coronavirus genome are known to carry cis-acting elements for DI RNA replication and presumably also virus genome replication. 5′ UTR-adjacent coding sequences are also thought to harbor cis-acting elements. Here we have determined the 5′ UTR and adjacent 289-nt sequences, and 3′ UTR sequences, for six group 2 coronaviruses and have compared them to each other and to three previously reported group 2 members. Extensive regions of highly similar UTR sequences were found but small regions of divergence were also found indicating group 2 coronaviruses could be subdivided into those that are bovine coronavirus (BCoV)-like (BCoV, human respiratory coronavirus-OC43, human enteric coronavirus, porcine hemagglutinating encephalomyelitis virus, and equine coronavirus) and those that are murine hepatitis virus (MHV)-like (A59, 2, and JHM strains of MHV, puffinosis virus, and rat sialodacryoadenitis virus). The 3′ UTRs of BCoV and MHV have been previously shown to be interchangeable. Here, a reporter-containing BCoV DI RNA was shown to be replicated by all five BCoV-like helper viruses and by MHV-H2 (a human cell-adapted MHV strain), a representative of the MHV-like subgroup, demonstrating group 2 common 5′ and 3′ replication signaling elements. BCoV DI RNA, furthermore, acquired the leader of HCoV-OC43 by leader switching, demonstrating for the first time in vivo recombination between animal and human coronavirus molecules. These results indicate that common replication signaling elements exist among group 2 coronaviruses despite a two-cluster pattern within the group and imply there could exist a high potential for recombination among group members. © 2003 Elsevier Inc. All rights reserved.","DI RNA; Group 2 coronaviruses; Leader switching; RdRp promoter; Recombination between human and animal coronaviruses; RNA replication signals","virus RNA; 3' untranslated region; 5' untranslated region; animal cell; article; controlled study; Coronavirus; helper virus; hepatitis virus; human; human cell; in vivo study; mouse; nonhuman; nucleotide sequence; priority journal; RNA analysis; RNA replication; RNA sequence; sequence analysis; signal transduction; virus classification; virus recombination; virus strain; Animalia; Bovinae; Bovine coronavirus; Coronavirus; Enteric coronavirus; Equidae; Equine coronavirus; Murinae; Murine hepatitis virus; Porcine hemagglutinating encephalomyelitis virus; Puffinosis virus; Rat sialodacryoadenitis coronavirus; Suidae","Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., Episodic evolution mediates interspecies transfer of a murine coronavirus (1997) J. Virol., 71, pp. 1946-1955; Brian, D.A., Spaan, W.J.M., Recombination and coronavirus defective interfering RNAs (1997) Semin. Virol., 8, pp. 101-111; Cavanagh, D., Brian, D.A., Briton, P., Enjuanes, L., Horzinek, M.C., Lai, M.M.C., Laude, H., Talbot, P.J., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 1452, pp. 629-635; Chang, R.-Y., Brian, D.A., Cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication (1996) J. Virol., 70, pp. 2201-2207; Chang, R.-Y., Hofmann, M.A., Sethna, P.B., Brian, D.A., A cis-acting function for the coronavirus leader in defective interfering RNA replication (1994) J. Virol., 68, pp. 8223-8231; Chang, R.-Y., Krishnan, R., Brian, D.A., The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA (1996) J. 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Virol., 73, pp. 8349-8355; Wurzer, W.J., Obojes, K., Vlasak, R., The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: A proposal to reorganize group 2 Coronaviridae (2002) J. Gen. Virol., 83, pp. 395-402; Zhang, X., Lai, M.M.C., A 5′-proximal RNA sequence of murine coronavirus as a potential initiation site for genomic-length mRNA transcription (1996) J. Virol., 70, pp. 705-711; Zhang, X.M., Herbst, W., Kousoulas, K.G., Stortz, J., Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child (1994) J. Med. Virol., 44, pp. 152-161","Brian, D.A.; Department of Microbiology, University of Tennessee, Knoxville, TN 37996-0845, United States; email: dbrian@utk.edu",,"Academic Press Inc.",00426822,,VIRLA,"14592769","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0242299781
"Spiga O., Bernini A., Ciutti A., Chiellini S., Menciassi N., Finetti F., Causarono V., Anselmi F., Prischi F., Niccolai N.","6603012863;7004103621;6602262010;6602341238;6508187838;57200398864;6504367025;57203811542;6505683929;7003440494;","Molecular modelling of S1 and S2 subunits of SARS coronavirus spike glycoprotein",2003,"Biochemical and Biophysical Research Communications","310","1",,"78","83",,62,"10.1016/j.bbrc.2003.08.122","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141514465&doi=10.1016%2fj.bbrc.2003.08.122&partnerID=40&md5=ff87e8fd7a25276f842626cc2311b17d","Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Faculty of Natural Sciences, University of Siena, I-53100 Siena, Italy; BIOMODEM pscrl, I-53100 Siena, Italy","Spiga, O., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Bernini, A., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Ciutti, A., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Chiellini, S., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Menciassi, N., Faculty of Natural Sciences, University of Siena, I-53100 Siena, Italy; Finetti, F., Faculty of Natural Sciences, University of Siena, I-53100 Siena, Italy; Causarono, V., Faculty of Natural Sciences, University of Siena, I-53100 Siena, Italy; Anselmi, F., Faculty of Natural Sciences, University of Siena, I-53100 Siena, Italy; Prischi, F., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; Niccolai, N., Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy, BIOMODEM pscrl, I-53100 Siena, Italy","The S1 and S2 subunits of the spike glycoprotein of the coronavirus which is responsible for the severe acute respiratory syndrome (SARS) have been modelled, even though the corresponding amino acid sequences were not suitable for tertiary structure predictions with conventional homology and/or threading procedures. An indirect search for a protein structure to be used as a template for 3D modelling has been performed on the basis of the genomic organisation similarity generally exhibited by coronaviruses. The crystal structure of Clostridium botulinum neurotoxin B appeared to be structurally adaptable to human and canine coronavirus spike protein sequences and it was successfully used to model the two subunits of SARS coronavirus spike glycoprotein. The overall shape and the surface hydrophobicity of the two subunits in the obtained models suggest the localisation of the most relevant regions for their activity. © 2003 Elsevier Inc. All rights reserved.","Coronavirus; Molecular modelling; Protein structure; SARS; Structure prediction","neurotoxin; neurotoxin b; protein subunit; unclassified drug; virus glycoprotein; adaptation; amino acid sequence; analytic method; article; Clostridium botulinum; Coronavirus; crystal structure; DNA template; genome analysis; hydrophobicity; molecular model; nonhuman; pneumonia; prediction; priority journal; protein analysis; protein localization; protein structure; SARS coronavirus; sequence analysis; sequence homology; severe acute respiratory syndrome; species comparison; structure analysis; surface property; virus genome; Canine coronavirus; Clostridium; Clostridium botulinum; Coronavirus; SARS coronavirus","Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Yu, X.J., Luo, C., Lin, J.C., Hao, P., He, Y.Y., Guo, Z.M., Qin, L., Li, Y.X., Putative hAPN receptor binding sites in SARS-CoV spike protein (2003) Acta Pharmacol. Sin., 24, pp. 481-488; Kontoyiannis, D.P., Pasqualini, R., Arap, W., Aminopeptidase N inhibitors and SARS (2003) Lancet, 361, p. 1558; Williams, R.K., Yeager, C.L., Holmes, K.V., Potential for receptor-based antiviral drugs against SARS (2003) Lancet, 362, p. 77; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Shen, X., Xue, J.H., Yu, C.Y., Luo, H.B., Qin, L., Yu, X.J., Chen, J., Jiang, H.L., Small envelope protein E of SARS: Cloning, expression, purification, CD determination, and bioinformatics analysis (2003) Acta Pharmacol. Sin., 24, pp. 505-511; Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Shindyalov, I.N., Bourne, P.E., The protein data bank (2000) Nucleic Acids Res., 28, pp. 235-242; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., Virus-encoded proteinases and proteolytic processing in the Nidovirales (2000) J. Gen. Virol., 81, pp. 853-879; Binns, M.M., Boursnell, M.E., Cavanagh, D., Pappin, D.J., Brown, T.D., Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV (1985) J. Gen. Virol., 66 (PART 4), pp. 719-726; http://www.ncbi.nlm.nih.gov/; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22, pp. 4673-4680; Jones, D.T., Protein secondary structure prediction based on position-specific scoring matrices (1999) J. Mol. 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Cryst., 26, pp. 283-291; Koradi, R., Billeter, M., Wuthrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J. Mol. Graph., 14, pp. 51-55. , 29-32; Fariselli, P., Riccobelli, P., Casadio, R., Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins (1999) Proteins, 36, pp. 340-346; Goodford, P.J., A computational procedure for determining energetically favorable binding sites on biologically important macromolecules (1985) J. Med. Chem., 28, pp. 849-857; Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein (1982) J. Mol. Biol., 157, pp. 105-132; Klein-Seetharaman, J., Oikawa, M., Grimshaw, S.B., Wirmer, J., Duchardt, E., Ueda, T., Imoto, T., Schwalbe, H., Long-range interactions within a nonnative protein (2002) Science, 295, pp. 1719-1722","Niccolai, N.; Biomol. Structure Research Center, Department of Molecular Biology, University of Siena, I-53100 Siena, Italy; email: niccolai@unisi.it",,"Academic Press Inc.",0006291X,,BBRCA,"14511651","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-0141514465
"Jacomy H., Talbot P.J.","6602526770;7102670281;","Vacuolating encephalitis in mice infected by human coronavirus OC43",2003,"Virology","315","1",,"20","33",,40,"10.1016/S0042-6822(03)00323-4","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242363107&doi=10.1016%2fS0042-6822%2803%2900323-4&partnerID=40&md5=b861c57e2efccd106c6afb82506358af","Laboratory of Neuroimmunovirology, INRS-Institut Armand Frappier, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Jacomy, H., Laboratory of Neuroimmunovirology, INRS-Institut Armand Frappier, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; Talbot, P.J., Laboratory of Neuroimmunovirology, INRS-Institut Armand Frappier, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada","Involvement of viruses in human neurodegenerative diseases and the underlying pathologic mechanisms remain generally unclear. Human respiratory coronaviruses (HCoV) can infect neural cells, persist in human brain, and activate myelin-reactive T cells. As a means of understanding the human infection, we characterized in vivo the neurotropic and neuroinvasive properties of HCoV-OC43 through the development of an experimental animal model. Virus inoculation of 21-day postnatal C57BL/6 and BALB/c mice led to a generalized infection of the whole CNS, demonstrating HCoV-OC43 neuroinvasiveness and neurovirulence. This acute infection targeted neurons, which underwent vacuolation and degeneration while infected regions presented strong microglial reactivity and inflammatory reactions. Damage to the CNS was not immunologically mediated and microglial reactivity was instead a consequence of direct virus-mediated neuronal injury. Although this acute encephalitis appears generally similar to that induced by murine coronaviruses, an important difference rests in the prominent spongiform-like degeneration that could trigger neuropathology in surviving animals. © 2003 Elsevier Inc. All rights reserved.","Coronavirus; Encephalitis; Inflammation; Neurodegenerative disease; Spongiform-like degeneration; Viral meningoencephalomyelitis","animal model; animal tissue; article; brain spongiosis; cell activity; cell vacuole; central nervous system; controlled study; Coronavirus; encephalitis; experimentation; female; immunology; in vivo study; infection; microglia; mouse; mouse strain; nerve cell; nerve degeneration; neuropathology; nonhuman; priority journal; target cell; virus infection; virus strain; virus virulence; Animalia; Coronavirus; Murinae","Agapitos, E., Pavlopoulos, P.M., Patsouris, E., Davaris, P., Subacute necrotizing encephalopathy (Leigh's disease): A clinicopathologic study of ten cases (1997) Gen. Diag. Pathol., 142, pp. 341-355; Allen, I.V., McQuaid, S., McMahon, J., Kirk, J., McConnell, R., The significance of measles virus antigen and genome distribution in the CNS in SSPE for mechanisms of viral spread and demyelination (1996) J. Neuropathol. Exp. 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Neurol., 47, pp. 108-112; Stewart, J.N., Mounir, S., Talbot, P.J., Human coronavirus gene expression in the brains of multiple sclerosis patients (1992) Virology, 191, pp. 502-505; Sun, N., Grzybicki, D.M., Castro, R.F., Murphy, S.P., Perlman, S., Activation of astrocytes in the spinal cord of mice chronically infected with a neurotropic coronavirus (1995) Virology, 213, pp. 482-493; Sun, N., Perlman, S., Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes (1995) J. Virol., 69, pp. 633-641; Sussman, M.A., Shubin, R.A., Kyuwa, S., Stohlman, S.A., T-cell-mediated clearance of mouse hepatitis virus strain JHM from the central nervous system (1989) J. Virol., 63, pp. 3051-3056; Talbot, P.J., Knobler, R.L., Buchmeier, M.J., Western and dot immunoblotting analysis of viral antigens and antibodies: Application to murine hepatitis virus (1984) J. Immunol. Methods, 73, pp. 177-188; Walther, M., Kuklinski, S., Pesheva, P., Guntinas-Lichius, O., Angelov, D.N., Neiss, W.F., Asou, H., Probstmeier, R., Galectin-3 is upregulated in microglial cells in response to ischemic brain lesions, but not to facial nerve axotomy (2000) J. Neurosci. Res., 15, pp. 430-435; Waltrip R.W. II, Buschanan, R.W., Summerfelt, A., Breier, A., Carpenter, W.T., Bryant, N.L., Rubin, S.A., Carbone, K.M., Borna disease virus and schizophrenia (1995) Psychiatry Res., 56, pp. 33-44; Wang, F.I., Stohlman, S.A., Fleming, J.O., Demyelination induced by murine hepatitis virus JHM strain (MHV-4) is immunologically mediated (1990) J. Neuroimmunol., 30, pp. 31-34; Weiner, L.P., Pathogenesis of demyelination induced by mouse hepatitis virus (1973) Arch. Neurol., 28, pp. 298-303; Whitley, R.J., Gnann, J.W., Viral encephalitis: Familiar infections and emerging pathogens (2002) Lancet, 359, pp. 507-513; Woyciechowska, J.L., Trapp, B.D., Patrick, D.H., Shekarchi, I.C., Leinikki, P.O., Sever, J.L., Holmes, K.V., Acute and subacute demyelination induced by mouse hepatitis virus strain A59 in C3H mice (1984) J. Exp. Pathol., 1, pp. 295-306; Zimmer, M.J., Dales, S., In vivo and in vitro models of demyelinating diseases XXIV (1989) The infectious process in cyclosporin A treated Winstar Lewis rats inoculated with JHM virus. Microbial Pathog., 6, pp. 7-16","Talbot, P.J.; Laboratory of Neuroimmunovirology, INRS-Institut Armand Frappier, 531 Boulevard des Prairies, Laval, Que. H7V 1B7, Canada; email: Pierre.Talbot@inrs-iaf.uquebec.ca",,"Academic Press Inc.",00426822,,VIRLA,"14592756","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0242363107
"Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W., Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W., Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.","7202924055;7201780588;35285643800;56082054700;57206210028;34975244700;55254453500;57214069704;57207393660;7202923908;36061616300;57216110882;16444133100;7202378277;7005677034;36078079100;7005486823;7005441747;","Isolation and characterization of viruses related to the SARS coronavirus from animals in Southern China",2003,"Science","302","5643",,"276","278",,1046,"10.1126/science.1087139","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141889936&doi=10.1126%2fscience.1087139&partnerID=40&md5=bedeb4218067d0b805733d34db3d4899","Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Ctr. for Dis. Control and Prevention, Shenzhen, Guangdong Province, China; Department of Pathology, University of Hong Kong, Queen Mary Hospital, Hong Kong S.A.R., Hong Kong; Government Virus Unit, Department of Health, Hong Kong S.A.R., Hong Kong","Guan, Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Zheng, B.J., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; He, Y.Q., Ctr. for Dis. Control and Prevention, Shenzhen, Guangdong Province, China; Liu, X.L., Ctr. for Dis. Control and Prevention, Shenzhen, Guangdong Province, China; Zhuang, Z.X., Ctr. for Dis. Control and Prevention, Shenzhen, Guangdong Province, China; Cheung, C.L., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Luo, S.W., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Li, P.H., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Zhang, L.J., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Guan, Y.J., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Butt, K.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Wong, K.L., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Chan, K.W., Department of Pathology, University of Hong Kong, Queen Mary Hospital, Hong Kong S.A.R., Hong Kong; Lim, W., Government Virus Unit, Department of Health, Hong Kong S.A.R., Hong Kong; Shortridge, K.F., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Peiris, J.S.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; Poon, L.L.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong","A novel coronavirus (SCoV) is the etiological agent of severe acute respiratory syndrome (SARS). SCoV-like viruses were isolated from Himalayan palm civets found in a live-animal market in Guangdong, China. Evidence of virus infection was also detected in other animals (including a raccoon dog, Nyctereutes procyonoides) and in humans working at the same market. All the animal isolates retain a 29-nucleotide sequence that is not found in most human isolates. The detection of SCoV-like viruses in small, live wild mammals in a retail market indicates a route of interspecies transmission, although the natural reservoir is not known.",,"Disease control; Genes; Nucleotides; Viruses; animal; severe acute respiratory syndrome; virus; animal; article; China; controlled study; Coronavirus; Himalayan palm civet; human; market; nonhuman; nucleotide sequence; priority journal; raccoon dog; respiratory tract disease; SARS coronavirus; severe acute respiratory syndrome; virus characterization; virus infection; virus isolation; virus transmission; Amino Acid Sequence; Animals; Animals, Wild; Antibodies, Viral; Blotting, Western; Carnivora; China; Coronavirus; Coronavirus Infections; Disease Reservoirs; Feces; Genome, Viral; Humans; Membrane Glycoproteins; Molecular Sequence Data; Neutralization Tests; Nose; Open Reading Frames; Phylogeny; Polymorphism, Genetic; Reverse Transcriptase Polymerase Chain Reaction; SARS Virus; Sequence Deletion; Sequence Homology, Nucleic Acid; Viral Envelope Proteins; Viral Proteins; China; Animalia; Canis familiaris; Coronavirus; Mammalia; Nyctereutes procyonoides; Procyon lotor; RNA viruses; SARS coronavirus; Viverridae","www.who.int/csr/sars/enl; Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , www.who.int/csr/sars/country/2003_05_20/en/; Peiris, J.S.M., (2003) Lancet, 361, p. 1319; Ksiazek, T.G., (2003) N. Engl. J. Med., 348, p. 1953; Fouchier, R.A., (2003) Nature, 423, p. 240; Zhong, N.S., Lancet, , in press; Holmes, K., unpublished observations; Marra, M.A., (2003) Science, 300, p. 1399; China Species Information System, , www.chinabiodiversity.com; Kumar, S., (2001) Bioinformatics, 17, p. 1244; Kimura, M., (1980) J. Mol. Evol., 16, p. 111; note","Guan, Y.; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Hong Kong Spec. Admin. Reg. (S.A.R.), Hong Kong; email: yguan@hkucc.hku.hk",,,00368075,,SCIEA,"12958366","English","Science",Article,"Final",Open Access,Scopus,2-s2.0-0141889936
"Tanner J.A., Watt R.M., Chai Y.-B., Lu L.-Y., Lin M.C., Peiris J.S.M., Poon L.L.M., Kung H.-F., Huang J.-D.","35513993000;7102907536;7102457077;8686996700;56032965000;7005486823;7005441747;7402514190;8108660600;","The severe acute respiratory syndrome (SARS) coronavirus NTPasefhelicase belongs to a distinct class of 5′ to 3′ viral helicases",2003,"Journal of Biological Chemistry","278","41",,"39578","39582",,86,"10.1074/jbc.C300328200","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141960168&doi=10.1074%2fjbc.C300328200&partnerID=40&md5=1eeaf06d5c557bdddd0d89ba3af68ee9","Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Institute of Molecular Biology, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong","Tanner, J.A., Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Watt, R.M., Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Chai, Y.-B., Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Lu, L.-Y., Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Lin, M.C., Institute of Molecular Biology, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Peiris, J.S.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Poon, L.L.M., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Kung, H.-F., Institute of Molecular Biology, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; Huang, J.-D., Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong","The putative NTPase/helicase protein from severe acute respiratory syndrome coronavirus (SARS-CoV) is postulated to play a number of crucial roles in the viral life cycle, making it an attractive target for anti-SARS therapy. We have cloned, expressed, and purified this protein as an N-terminal hexahistidine fusion in Escherichia coli and have characterized its helicase and NTPase activities. The enzyme unwinds double-stranded DNA, dependent on the presence of a 5′ single-stranded overhang, indicating a 5′ to 3′ polarity of activity, a distinct characteristic of coronaviridae helicases. We provide the first quantitative analysis of the polynucleic acid binding and NTPase activities of a Nidovirus helicase, using a high throughput phosphate release assay that will be readily adaptable to the future testing of helicase inhibitors. All eight common NTPs and dNTPs were hydrolyzed by the SARS helicase in a magnesium-dependent reaction, stimulated by the presence of either single-stranded DNA or RNA. The enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates. Homopolynucleotides significantly stimulated the ATPase activity (15-25-fold) with the notable exception of poly(G) and poly(dG), which were non-stimulatory. We found a large variation in the apparent strength of binding of different homopolynucleotides, with dT24 binding over 10 times more strongly than dA24 as observed by the apparent Km.",,"Binding energy; Bioassay; DNA; Enzymes; Escherichia coli; Pulmonary diseases; Viruses; Nucleotides; Respiratory system; adenosine triphosphate; cytidine triphosphate; enzyme inhibitor; helicase; helicase inhibitor; hexahistidine; histidine; magnesium; nidovirus helicase; phosphate; polyguanylic acid; sars coronavirus helicase; sars coronavirus nucleotide triphosphatase; single stranded DNA; single stranded RNA; unclassified drug; virus enzyme; amino terminal sequence; animal cell; article; controlled study; Coronavirus; dissociation constant; DNA denaturation; DNA strand; enzyme analysis; enzyme assay; enzyme inhibition; enzyme substrate; Escherichia coli; gene expression; gene fusion; hydrolysis; life cycle; Nidovirales; nonhuman; nucleotide sequence; priority journal; protein purification; quantitative diagnosis; respiratory tract disease; SARS coronavirus; severe acute respiratory syndrome; Animals; Base Sequence; Cercopithecus aethiops; DNA Helicases; DNA, Viral; Kinetics; Molecular Sequence Data; Nucleoside-Triphosphatase; RNA Helicases; SARS Virus; Substrate Specificity; Vero Cells; Animalia; Coronaviridae; Coronavirus; Escherichia coli; Nidovirales; RNA viruses; SARS coronavirus","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., (2003) N. Engl. J. Med., 348, pp. 1967-1976; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., (2003) Science, 300, pp. 1399-1404; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., (2003) N. Engl. J. Med., 348, pp. 1953-1966; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, pp. 853-879; Lai, M.M., Cavanagh, D., (1997) Adv. Virus Res., 48, pp. 1-100; Van Dinten, L.C., Van Tol, H., Gorbalenya, A.E., Snijder, E.J., (2000) J. Virol., 74, pp. 5213-5223; Van Marle, G., Van Dinten, L.C., Spaan, W.J., Luytjes, W., Snijder, E.J., (1999) J. Virol., 73, pp. 5274-5281; Kadare, G., Haenni, A.L., (1997) J. Virol., 71, pp. 2583-2590; Holmes, K.V., (2003) J. Clin. Invest., 111, pp. 1605-1609; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., (2003) Science, 300, pp. 1763-1767; Kleymann, G., Fischer, R., Betz, U.A., Hendrix, M., Bender, W., Schneider, U., Handke, G., Rubsamen-Waigmann, H., (2002) Nat. Med., 8, pp. 392-398; Kleymann, G., (2003) Expert Opin. Investig. Drugs, 12, pp. 165-183; Crute, J.J., Grygon, C.A., Hargrave, K.D., Simoneau, B., Faucher, A.M., Bolger, G., Kibler, P., Cordingley, M.G., (2002) Nat. Med., 8, pp. 386-391; Borowski, P., Schalinski, S., Schmitz, H., (2002) Antiviral Res., 55, pp. 397-412; Baykov, A.A., Evtushenko, O.A., Avaeva, S.M., (1988) Anal. Biochem., 171, pp. 266-270; Wardell, A.D., Errington, W., Ciaramella, G., Merson, J., McGarvey, M.J., (1999) J. Gen. Virol., 80, pp. 701-709; Seybert, A., Hegyi, A., Siddell, S.G., Ziebuhr, J., (2000) RNA (N.Y.), 6, pp. 1056-1068; Caruthers, J.M., McKay, D.B., (2002) Curr. Opin. Struct. Biol., 12, pp. 123-133; Yao, N., Hesson, T., Cable, M., Hong, Z., Kwong, A.D., Le, H.V., Weber, P.C., (1997) Nat. Struct. Biol., 4, pp. 463-467; Seybert, A., Van Dinten, L.C., Snijder, E.J., Ziebuhr, J., (2000) J. Virol., 74, pp. 9586-9593; Bautista, E.M., Faaberg, K.S., Mickelson, D., McGruder, E.D., (2002) Virology, 298, pp. 258-270; Kalinina, N.O., Rakitina, D.V., Solovyev, A.G., Schiemann, J., Morozov, S.Y., (2002) Virology, 296, pp. 321-329; Kim, J.L., Morgenstern, K.A., Griffith, J.P., Dwyer, M.D., Thomson, J.A., Murcko, M.A., Lin, C., Caron, P.R., (1998) Structure (Lond.), 6, pp. 89-100; Li, Y.I., Shih, T.W., Hsu, Y.H., Han, Y.T., Huang, Y.L., Meng, M., (2001) J. Virol., 75, pp. 12114-12120; Borowski, P., Niebuhr, A., Mueller, O., Bretner, M., Felczak, K., Kulikowski, T., Schmitz, H., (2001) J. Virol., 75, pp. 3220-3229; Pasternak, A.O., Van den Born, E., Spaan, W.J., Snijder, E.J., (2001) EMBO J., 20, pp. 7220-7228; Laity, J.H., Lee, B.M., Wright, P.E., (2001) Curr. Opin. Struct. Biol., 11, pp. 39-46; Thiel, V., Ivanov, K.A., Putics, A., Hertzig, T., Schelle, B., Bayer, S., Weissbrich, B., Ziebuhr, J., (2003) J. Gen. Virol., 84, pp. 2305-2315","Huang, J.-D.; Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong S. A. R., Hong Kong; email: jdhuang@hkucc.hku.hk",,,00219258,,JBCHA,"12917423","English","J. Biol. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0141960168
"Kesel A.J.","6603578473;","A system of protein target sequences for anti-RNA-viral chemotherapy by a vitamin B6-derived zinc-chelating trioxa-adamantane-triol",2003,"Bioorganic and Medicinal Chemistry","11","21",,"4599","4613",,14,"10.1016/S0968-0896(03)00500-5","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141727554&doi=10.1016%2fS0968-0896%2803%2900500-5&partnerID=40&md5=72b262c0bc69369ea4b61ebc1270d8ba","Chammünsterstr. 47, D-81827 München, Germany","Kesel, A.J., Chammünsterstr. 47, D-81827 München, Germany","The synthesis of the structurally unusual heterotricyclic compound 1-[3-hydroxy-5-(hydroxymethyl)-2-methyl-4-pyridinyl]-2,8,9-trioxaadamantane-3,5, 7-triol (trivially named bananin, BN) from pyridoxylidenephloroglucinol and a theoretical prospect on possible biological activities of BN are presented in this report. Pyridoxylidenephloroglucinol is synthesized by Knoevenagel condensation of the vitamin B6 aldehyde pyridoxal with phloroglucinol. Pyridoxylidenephloroglucinol rearranges to light-yellow (4′RS)-1′,4′-dihydrobananin by refluxing in 5 M hydrochloric acid. Air oxidation subsequently forms BN in the heat which immediately yields orange-yellow (4′RS)-4′-chloro-1′,4′-dihydrobananin by 1,4-addition of hydrogen chloride. This intermediate could be isolated but, interestingly, not a BN hydrochloride. Brown BN is finally achieved by base-catalyzed elimination of hydrogen chloride from (4′RS)-4′ -chloro-1′,4′-dihydrobananin. Regarding possible biological activities, it was demonstrated that BN acts as zinc (Zn2+) chelator. Therefore, a target of interest could be the human immunodeficiency virus type 1 (HIV-1) zinc finger HIV-1 RNA-binding nucleocapsid protein p7 (NCp7). Through suggested zinc ejection from HIV-1 genomic RNA ψ-element-binding and HIV-1-RNA-duplex packaging NCp7 by BN, thus rendering NCp7 functionally obsolete, it is deduced that HIV-1 replication and effective infectious virion encapsidation could be inhibited by BN. Furthermore, theoretical and structural considerations propose that BN is converted into bananin 5′-monophosphate (BNP) by the cell type-ubiquitous human enzyme pyridoxal kinase (EC 2.7.1.35). Together with the putative antilentiviral retinoid vitamin A-vitamin B 6 conjugate analogue B6RA (Kesel, A. J. Biochem. Biophys. Res. Comm. 2003, 300, 793), BNP is postulated to serve as effector in a system of protein target sequences RX(D/E) of RNA virus components. Human immunodeficiency Retroviridae (HIVs) could possibly be influenced by B6RA and BNP. In addition, candidate targets of B6RA and BNP could be adsorption, transcription and/or viral RNA replication of an interestingly wide RNA virus selection including Picornaviridae (poliovirus, human coxsackievirus, hepatitis A virus), Flaviviridae (yellow fever virus, Dengue virus, West Nile virus, Kunjin virus, St. Louis encephalitis virus, hepatitis C virus), Togaviridae (rubella virus), Coronaviridae (human coronavirus, human SARS-associated coronavirus), Rhabdoviridae (rabies virus), Paramyxoviridae (human parainfluenza virus, measles virus, human respiratory syncytial virus), Filoviridae (Marburg virus, Ebola virus), Bornaviridae (Borna disease virus), Bunyaviridae (Hantaan virus), Arenaviridae (Lassa virus), and Reoviridae (human rotavirus). The postulated scope of 'metabolically trapped' BNP might resemble the antiviral spectrum of the RNA-viral virustatic ribavirin. © 2003 Elsevier Ltd. All rights reserved.",,"1 [3 hydroxy 5 (hydroxymethyl) 2 methyl 4 pyridinyl] 2,8,9 trioxaadamantane 3,5,7 triol; 1',4' dihydrobananin; 4' chloro 1',4' dihydrobananin; adamantane derivative; aldehyde; antivirus agent; bananin 5' monophosphate; base; chelating agent; chemical compound; double stranded RNA; hydrochloric acid; nucleocapsid protein; nucleocapsid protein p 7; phloroglucinol; phosphate; pyridoxal; pyridoxal kinase; pyridoxine; pyridoxine derivative; pyridoxylidenephloroglucinol; retinol derivative; ribavirin; unclassified drug; virus RNA; zinc; addition reaction; adsorption; air; amino acid sequence; Arenavirus; article; Borna disease virus; Bunyavirus; catalysis; cell type; chemotherapy; color; Coronavirus; Coxsackie virus; drug activity; drug conjugation; drug mechanism; drug synthesis; Hantavirus; heat; Hepatitis A virus; Human immunodeficiency virus 1; Human rotavirus; inhibition kinetics; isolation procedure; Knoevenagel condensation; Lassa virus; oxidation; Paramyxovirus; Picornavirus; Poliomyelitis virus; protein function; protein RNA binding; protein targeting; Rabies virus; reaction analysis; Reovirus; Retrovirus; Rhabdovirus; RNA replication; RNA sequence; RNA transcription; RNA virus; Rubella virus; SARS coronavirus; sequence analysis; Togavirus; virion; virus genome; virus replication; zinc finger motif; Arenaviridae; Borna disease virus; Bornaviridae; Bunyaviridae; Coronaviridae; Coronavirus; Coxsackievirus; Dengue virus; Ebola virus; Filoviridae; Flaviviridae; Hantaan virus; Hepatitis A virus; Hepatitis C virus; Human immunodeficiency virus; Human immunodeficiency virus 1; Human respiratory syncytial virus; Human rotavirus A; Kunjin virus; Lake Victoria marburgvirus; Lassa virus; Measles virus; Paramyxoviridae; Picornaviridae; Poliovirus; Rabies virus; Reoviridae; Respiratory syncytial virus; Retroviridae; Rhabdoviridae; RNA viruses; Rotavirus; Rubella virus; St. Louis encephalitis virus; Togaviridae; West Nile virus; Yellow fever virus","Woodward, R.B., (1964) Pure Appl. Chem., 9, p. 49; Tsuda, K., Ikuma, S., Kawamura, M., Tachikawa, R., Sakai, K., Tamura, C., Amakasu, O., (1964) Chem. Pharm. Bull., 12, p. 1357; Goto, T., Kishi, Y., Takahashi, S., Hirata, Y., (1965) Tetrahedron, 21, p. 2059; Wagner, H., Fischer, M., Lotter, H., (1985) Z. Naturforsch, 40 B, p. 1226; Wagner, H., Lotter, H., Fischer, M., (1986) Helv. Chim. Acta, 69, p. 359; Schiff, H., (1865) Ann. Chem. Pharm., 3 (SUPPL.), p. 343; Tryfiates, G.P., Gannett, P.M., Bishop, R.E., Shastri, P.K., Ammons, J.R., Arbogast, J.G., (1996) Cancer Res., 56, p. 3670; Kesel, A.J., Urban, S., Oberthür, W., (1996) Tetrahedron, 52, p. 14787; Kesel, A.J., Polborn, K., Gürtler, L., Klinkert, W.E.F., Modolell, M., Oberthür, W., (1998) J. Cancer Res. Clin. Oncol., 124 (SUPPL.), p. 32; Kesel, A.J., Sonnenbichler, I., Polborn, K., Gurtler, L., Klinkert, W.E.F., Modolell, M., Nussler, A.K., Oberthur, W., (1999) Nat. 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Lett., 12, p. 767; Schito, M.L., Goel, A., Song, Y., Inman, J.K., Fattah, R.J., Rice, W.G., Turpin, J.A., Appella, E., (2003) AIDS Res. Hum. Retroviruses, 19, p. 91; Mayasundari, A., Rice, W.G., Diminnie, J.B., Baker, D.C., (2003) Bioorg. Med. Chem., 11, p. 3215; http://www.ncbi.nlm.nih.gov/entrez/query.fcgi; Hirsch, M.S., Kaplan, J.C., D'Aquila, R.T., (1996) Fields Virology, pp. 431-466. , Fields, B. N.; Knipe, D. M.; Howley, P. M.; Chanock, R. M.; Melnick, J. L.; Monath, T. P.; Roizman, B.; Straus, S. E., Eds.; third ed., Lippincott-Raven: Philadelphia","Kesel, A.J.Chammünsterstr. 47, D-81827 München, Germany; email: andreas.kesel@t-online.de",,"Elsevier Ltd",09680896,,BMECE,"14527557","English","Bioorg. Med. Chem.",Article,"Final",,Scopus,2-s2.0-0141727554
"Chou K.-C., Wei D.-Q., Zhong W.-Z.","7201905167;7202909038;57214690924;","Erratum: Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS (Biochemical and Biophysical Research Communications (2003) 308 (148-151))",2003,"Biochemical and Biophysical Research Communications","310","2",,"675","",,10,"10.1016/j.bbrc.2003.09.053","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141458814&doi=10.1016%2fj.bbrc.2003.09.053&partnerID=40&md5=04394c47db757c38dcb342e2b98aef20","Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States; Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China","Chou, K.-C., Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States, Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China; Wei, D.-Q., Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China; Zhong, W.-Z., Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States, Tianjin Inst. Bioinfo./Drug Discov., Tianjin Normal University, Tianjin, China",[No abstract available],,"erratum; error; priority journal; Coronavirus",,"Chou, K.-C.; Gordon Life Science Institute, 7088 Arbor Valley, Kalamazoo, MI 49009, United States; email: kchou@chartermi.net",,"Academic Press Inc.",0006291X,,BBRCA,,"English","Biochem. Biophys. Res. Commun.",Erratum,"Final",Open Access,Scopus,2-s2.0-0141458814
"Gao F., Ou H.-Y., Chen L.-L., Zheng W.-X., Zhang C.-T.","34769702200;7005561046;35226293800;55704745200;55566455000;","Prediction of proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes",2003,"FEBS Letters","553","3",,"451","456",,48,"10.1016/S0014-5793(03)01091-3","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142200324&doi=10.1016%2fS0014-5793%2803%2901091-3&partnerID=40&md5=777cac41424a3e42b50ca2eec7108079","Department of Physics, Tianjin University, Tianjin 300072, China; Laboratory for Computational Biology, Shandong Prov. Res. Ctr. B., Shandong University of Technology, Zibo 255049, China","Gao, F., Department of Physics, Tianjin University, Tianjin 300072, China; Ou, H.-Y., Department of Physics, Tianjin University, Tianjin 300072, China; Chen, L.-L., Department of Physics, Tianjin University, Tianjin 300072, China, Laboratory for Computational Biology, Shandong Prov. Res. Ctr. B., Shandong University of Technology, Zibo 255049, China; Zheng, W.-X., Department of Physics, Tianjin University, Tianjin 300072, China; Zhang, C.-T., Department of Physics, Tianjin University, Tianjin 300072, China","Recently, we have developed a coronavirus-specific gene-finding system, ZCURVE_CoV 1.0. In this paper, the system is further improved by taking the prediction of cleavage sites of viral proteinases in polyproteins into account. The cleavage sites of the 3C-like proteinase and papain-like proteinase are highly conserved. Based on the method of traditional positional weight matrix trained by the peptides around cleavage sites, the present method also sufficiently considers the length conservation of non-structural proteins cleaved by the 3C-like proteinase and papain-like proteinase to reduce the false positive prediction rate. The improved system, ZCURVE_CoV 2.0, has been run for each of the 24 completely sequenced coronavirus genomes in GenBank. Consequently, all the non-structural proteins in the 24 genomes are accurately predicted. Compared with known annotations, the performance of the present method is satisfactory. The software ZCURVE_CoV 2.0 is freely available at http://tubic.tju.edu.cn/sars/. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.","Cleavage site; Coronavirus; Polyprotein; SARS-coronavirus; Severe acute respiratory syndrome","polyprotein; proteinase; article; computer program; controlled study; Coronavirus; gene sequence; nonhuman; nucleotide sequence; prediction; priority journal; protein structure; severe acute respiratory syndrome; virus pneumonia; Coronavirus; SARS coronavirus","Peiris, J.S., (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., (2003) New Engl. J. Med., 348, pp. 1953-1966; Drosten, C., (2003) New Engl. J. Med., 348, pp. 1967-1976; Tsang, K.W., (2003) New Engl. J. Med., 348, pp. 1977-1985; Lee, N., (2003) New Engl. J. Med., 348, pp. 1986-1994; Poutanen, S.M., (2003) New Engl. J. Med., 348, pp. 1995-2005; Rota, P.A., (2003) Science, 300, pp. 1394-1398; Marra, M.A., (2003) Science, 300, pp. 1399-1404; Qin, E'd., (2003) Chin. Sci. Bull., 48, pp. 941-948; Chen, L.L., Ou, H.Y., Zhang, R., Zhang, C.-T., (2003) Biochem. Biophys. Res. Commun., 307, pp. 382-388; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, pp. 853-879; Von Heijne, G., (1986) Nucleic Acids Res., 14, pp. 4683-4690; Von Grotthuss, M., Wyrwicz, L.S., Rychlewski, L., (2003) Cell, 113, pp. 701-702; Brierley, I., Jenner, A.J., Inglis, S.C., (1992) J. Mol. Biol., 227, pp. 463-479; Nam, S.H., Copeland, T.D., Hatanaka, M., Oroszlan, S., (1993) J. Virol., 67, pp. 196-203; Schneider, T.D., Stephens, R.M., (1990) Nucleic Acids Res., 18, pp. 6097-6100","Zhang, C.-T.; Department of Physics, Tianjin University, Tianjin 300072, China; email: ctzhang@tju.edu.cn",,"Elsevier",00145793,,FEBLA,"14572668","English","FEBS Lett.",Article,"Final",Open Access,Scopus,2-s2.0-0142200324
"Zhong N.S., Zheng B.J., Li Y.M., Poon L.L.M., Xie Z.H., Chan K.H., Li P.H., Tan S.Y., Chang Q., Xie J.P., Liu X.Q., Xu J., Li D.X., Yuen K.Y., Peiris J.S.M., Guan Y.","7102137996;7201780588;55925657400;7005441747;57198628286;7406034307;57214069704;57199986636;57216099353;57199945190;56369743100;57213432160;26632045000;36078079100;7005486823;7202924055;","Epidemiology and cause of severe acute respiratory syndrome (SARS) in Guangdong, People's Republic of China, in February, 2003",2003,"Lancet","362","9393",,"1353","1358",,273,"10.1016/S0140-6736(03)14630-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744228014&doi=10.1016%2fS0140-6736%2803%2914630-2&partnerID=40&md5=d9cafa384293719dc37f7bd250b40b0d","Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Guangzhou Chest Hospital, Guangzhou, Guangdong Province, China; Guangzhou Children's Hospital, Guangzhou, Guangdong Province, China; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong","Zhong, N.S., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Zheng, B.J., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Li, Y.M., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Poon, L.L.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Xie, Z.H., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Chan, K.H., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Li, P.H., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Tan, S.Y., Guangzhou Chest Hospital, Guangzhou, Guangdong Province, China; Chang, Q., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Xie, J.P., Guangzhou Children's Hospital, Guangzhou, Guangdong Province, China; Liu, X.Q., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Xu, J., Guangzhou Inst. of Resp. Diseases, Guangzhou Medical College, Guangzhou, Guangdong Province, China; Li, D.X., Guangzhou Chest Hospital, Guangzhou, Guangdong Province, China; Yuen, K.Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Peiris, J.S.M., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong; Guan, Y., Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, Hong Kong, Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong","Background: An epidemic of severe acute respiratory syndrome (SARS) has been associated with an outbreak of atypical pneumonia originating in Guangdong Province, People's Republic of China. We aimed to identify the causative agent in the Guangdong outbreak and describe the emergence and spread of the disease within the province. Methods: We analysed epidemiological information and collected serum and nasopharyngeal aspirates from patients with SARS in Guangdong in mid-February, 2003. We did virus isolation, serological tests, and molecular assays to identify the causative agent. Findings: SARS had been circulating in other cities of Guangdong Province for about 2 months before causing a major outbreak in Guangzhou, the province's capital. A novel coronavirus, SARS coronavirus (CoV), was isolated from specimens from three patients with SARS. Viral antigens were also directly detected in nasopharyngeal aspirates from these patients. 48 of 55 (87%) patients had antibodies to SARS CoV in their convalescent sera. Genetic analysis showed that the SARS CoV isolates from Guangzhou shared the same origin with those in other countries, and had a phylogenetic pathway that matched the spread of SARS to the other parts of the world. Interpretation: SARS CoV is the infectious agent responsible for the epidemic outbreak of SARS in Guangdong. The virus isolated from patients in Guangdong is the prototype of the SARS CoV in other regions and countries.",,"virus antigen; article; blood sampling; China; controlled study; convalescence; Coronavirus; epidemic; female; genetic analysis; human; major clinical study; male; medical information; nucleotide sequence; phylogeny; priority journal; respiratory tract disease; SARS coronavirus; serology; severe acute respiratory syndrome; virus isolation","Peng, G.W., He, J.F., Lin, J.Y., Epidemiological study on severe acute respiratory syndrome in Guangdong province (2003) Chin J Epidemiol, 24, pp. 350-352; (2003) Summary Report of Investigating an Atypical Pneumonia Outbreak in Zhongshan, , January 21; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Update: Outbreak of severe acute respiratory syndrome-Worldwide, 2003 (2003) MMWR Morb Mort Wkl Rep, 52, pp. 241-248; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83; Cumulative Number of Reported Probable Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_07_11/en; Peiris, J., Lai, S., Poon, L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/; Marra, M.A., Jones, S.J., Astell, C.R., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Guan, Y., Peiris, J.M., Lipatov, A.S., Emergence of multiple genotypes of H5N1 avian influenza viruses in Hong Kong SAR (2002) Proc Natl Acad Sci USA, 99, pp. 8950-8955; Kumar, S., Tarnura, K., Jakobsen, I.B., Nei, M., MEGA2: Molecular evolutionary genetics analysis software (2001) Bioinformatics, 17, pp. 1244-1245; Holmes, K.V., Coronaviruses (2001) Field Virology 4th Edn., pp. 1187-1203. , D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott Williams and Wilkins; Holland, J.J., De La Torre, J.C., Clarke, D.K., Quantitation of relative fitness and great adaptability of clonal populations of RNA viruses (1991) J Virol, 65, pp. 1960-2967; Domingo, E., Holland, J.J., RNA virus mutations and fitness for survival (1997) Annu Rev Microbiol, 51, pp. 151-178; De Jong, J.C., Claas, E.C., Osterhaus, A.D., A pandemic warning? (1997) Nature, 389, p. 544; Subbarao, K., Klimov, A., Katz, J., Characterisation of an avian influenza A (H5N1) virus isolated from a child with a fatal respiratory illness (1998) Science, 279, pp. 393-396; Shortridge, K.F., Stuart-Harris, C.H., An influenza epicentre? (1982) Lancet, 2, pp. 812-813","Guan, Y.; Department of Microbiology, University of Hong Kong, Queen Mary Hospital, Pokfulam Road, Hong Kong, Hong Kong; email: yguan@hkucc.hku.hk",,"Elsevier Limited",01406736,,LANCA,"14585636","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-10744228014
"Yount B., Curtis K.M., Fritz E.A., Hensley L.E., Jahrling P.B., Prentice E., Denison M.R., Geisbert T.W., Baric R.S.","6603564156;7102811088;7005504811;55303564700;7004533817;7003706540;7101971810;35449300200;7004350435;","Reverse genetics with a full-length infectious cDNA of severe acute respiratory syndrome coronavirus",2003,"Proceedings of the National Academy of Sciences of the United States of America","100","22",,"12995","13000",,212,"10.1073/pnas.1735582100","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242268397&doi=10.1073%2fpnas.1735582100&partnerID=40&md5=2a64ac83e0c7ed01f5a4ba386452bab5","Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Carolina Vaccine Institute, University of North Carolina, Chapel Hill, NC 27599-7435, United States; US Army Med. Res. Inst. Infect. Dis., Fort Detrick, MD 21702, United States; Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States","Yount, B., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Curtis, K.M., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7435, United States; Fritz, E.A., US Army Med. Res. Inst. Infect. Dis., Fort Detrick, MD 21702, United States; Hensley, L.E., US Army Med. Res. Inst. Infect. Dis., Fort Detrick, MD 21702, United States; Jahrling, P.B., US Army Med. Res. Inst. Infect. Dis., Fort Detrick, MD 21702, United States; Prentice, E., Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States; Denison, M.R., Department of Pediatrics, Elizabeth B. Lamb Ctr. Pediat. Res., Vanderbilt University Medical Center, Nashville, TN 37232, United States; Geisbert, T.W., US Army Med. Res. Inst. Infect. Dis., Fort Detrick, MD 21702, United States; Baric, R.S., Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7435, United States, Carolina Vaccine Institute, University of North Carolina, Chapel Hill, NC 27599-7435, United States","A previously undescribed coronavirus (CoV) is the etiologic agent responsible for severe acute respiratory syndrome (SARS). Using a panel of contiguous cDNAs that span the entire genome, we have assembled a full-length cDNA of the SARS-CoV Urbani strain, and have rescued molecularly cloned SARS viruses (infectious clone SARS-CoV) that contained the expected marker mutations inserted into the component clones. Recombinant viruses replicated as efficiently as WT virus and both were inhibited by treatment with the cysteine proteinase inhibitor (2S,3S)-transepoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester. In addition, subgenomic transcripts were initiated from the consensus sequence ACGAAC in both the WT and infectious clone SARS-CoV. Availability of a SARS-CoV full-length cDNA provides a template for manipulation of the viral genome, allowing for the rapid and rational development and testing of candidate vaccines and therapeutics against this important human pathogen.",,"aloxistatin; antivirus agent; complementary DNA; cysteine proteinase inhibitor; virus vaccine; animal cell; article; consensus sequence; controlled study; Coronavirus; gene insertion; genetic analysis; human; lower respiratory tract infection; molecular cloning; nonhuman; priority journal; protein function; reverse transcription; severe acute respiratory syndrome; transcription initiation; viral genetics; virus assembly; virus genome; virus mutation; virus recombinant; virus replication; virus strain; virus transcription; wild type; Animals; Base Sequence; Cercopithecus aethiops; Cloning, Molecular; Consensus Sequence; DNA, Complementary; Genetic Markers; Genetic Techniques; Humans; Open Reading Frames; SARS Virus; Severe Acute Respiratory Syndrome; Transcription, Genetic; Vero Cells; Animalia; Coronavirus; DNA viruses; insertion sequences; RNA viruses; SARS coronavirus","Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Cheung, T.M., (2003) N. Engl. J. Med., 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., To, K.F., (2003) N. Engl. J. Med., 348, pp. 1986-1994; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.I., Chan, C.S., (2003) Lancet, 361, pp. 1767-1772; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Ayers, M., (2003) N. Engl. J. Med., 348, pp. 1995-2005; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Cheung, M.T., (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C., Zaki, S.R., Peret, T., Emery, S., Tong, S., Lim, W., (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Gunter, S., Preisner, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Fouchier, R.A., (2003) N. Engl. J. 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Virol., 72, pp. 2265-2271; Von Grotthuss, M., Wyrwicz, L.S., Rychlewski, L., (2003) Cell, 113, pp. 701-702; Yount, B., Denison, M.R., Weiss, S.R., Baric, R.S., (2002) J. Virol., 76, pp. 11065-11078; Yount, B., Curtis, C., Baric, R.S., (2000) J. Virol., 76, pp. 10600-10611; Almazon, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Durin, J., Enjuanes, L., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 5516-5521; Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., (2001) J. Virol., 75, pp. 12359-12369; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., (2001) J. Gen. Virol., 82, pp. 1273-1281; Curtis, K.M., Yount, B., Baric, R.S., (2002) J. Virol., 76, pp. 1422-1434; Pensaert, M.B., De Bouck, P., (1978) Arch. Virol., 58, pp. 243-247; Pensaert, M., Callebaut, P., Vergote, J., (1986) Vet. Q, 8, pp. 257-261; Duarte, M., Tobler, K., Bridgen, A., Rasschaert, D., Ackermann, M., Laude, H., (1994) Virology, 198, pp. 466-476; Baric, R.S., Yount, B., Hensley, L., Peel, S.A., Chen, W., (1997) J. Virol., 71, pp. 1946-1955; Baric, R.S., Sullivan, E., Hensley, L., Yount, B., Chen, W., (1999) J. Virol., 73, pp. 638-649; Fischer, F., Stegen, C.F., Koetzner, C.A., Masters, P.S., (1998) J. Virol., 71, pp. 7885-7894; De Haan, C.A., Masters, P.S., Shen, X., Weiss, S., Rottier, P.J., (2002) Virology, 296, pp. 177-189; Sola, I., Alanso, S., Zuniga, S., Balasch, M., Plana-Duran, J., Enjuanes, L., (2002) J. Virol., 77, pp. 4357-4369; Ortega, J., Escors, D., Laude, H., Enjuanes, L., (2002) J. Virol., 76, pp. 11518-11529; Enjuanes, L., Van der Zeijst, B.A.M., (1995) The Coronaviridae, pp. 337-376. , ed. Siddell, S. G. (Plenum, New York); Ladman, B.S., Pope, C.R., Ziegler, A.F., Swieczkowski, T., Callahan, C.J., Davison, S., Gelb J., Jr., (2002) Avian Dis., 46, pp. 938-944; Saif, L.J., (1999) Adv. Vet. Med., 41, pp. 429-446; Van Nieuwstadt, A.P., Zetstra, T., Boonstra, J., (1989) Vet. Res., 125, pp. 58-60; Crouch, C.F., Oliver, S., Hearle, D.C., Buckley, A., Chapman, A.J., Francis, M.J., (2000) Vaccine, 19, pp. 189-196; Park, S., Sestak, K., Hodgins, D.C., Shoup, D.I., Ward, L.A., Jackwood, D.J., Saif, L.J., (1998) Am. J. Vet. Res., 59, pp. 1002-1008; Rottier, P.J., (1999) Vet. Microbiol., 69, pp. 117-125; Vennema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J., (1997) J. Virol., 64, pp. 1407-1409; Wang, X., Schnitzlein, W.N., Tripathy, D.N., Girshieck, T., Khan, M.I., (2002) Avian Dis., 46, pp. 831-838; Baron, M.D., Foster-Cuevas, M., Baron, J., Barrett, T., (1997) J. Gen. Virol., 80, pp. 2031-2039; Fouchier, R.A.M., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doorman, G.J., Van den Hoogen, B.G., Peris, M., Osterhaus, M.D., (2003) Nature, 423, p. 240; Komatsu, K., Inazuki, K., Hosoya, J., Satoh, S., (1986) Exp. Neurol., 91, pp. 23-29; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., (2003) Science, 300, pp. 1763-1767","Baric, R.S.; Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599-7435, United States; email: rbaric@email.unc.edu",,,00278424,,PNASA,"14569023","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0242268397
"Granzow H.","7004101171;","Detection and ultrastructural characterization of a novel virus from cyprinids",2003,"Microscopy and Microanalysis","9","SUPPL. 3",,"514","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142027600&partnerID=40&md5=a3b618a4768891e7f452f9cd1bb2c9fb","Friedrich Loeffler Institutes, Fed. Res. Ctr. Virus Dis. of Anim., Boddenblick 5 A, D-17493 Greifswald-Insel Riems, Germany","Granzow, H., Friedrich Loeffler Institutes, Fed. Res. Ctr. Virus Dis. of Anim., Boddenblick 5 A, D-17493 Greifswald-Insel Riems, Germany","During routine investigations on fish a virus was isolated from a white bream (Blicca bjoerkna L.) a tench (Tinca tinca L.) and a goldfish (Carassius auratus L.), order Cypriniformes with novel morphological features and hitherto undescribed morphogenesis (Granzow, H., F. Weiland, D. Fichtner, H. Schütze, A. Karger, E. Mundt, B. Dresenkamp, P. Martin, and T. C. Mettenleiter. 2001. Identification and characterization of a novel virus isolated from fish. J. gen. Virol. 82:2849-2859). Cell-free virions consist of a rod-shaped nucleocapsid (120-150 nm x 19-22 nm) similar to that seen in baculoviruses. The virion has a bacilliform shape (170-200 nm x 75-88 nm) reminiscent of rhabdoviruses with an envelope containing spikes (20-25 nm) like coronaviruses. This virus replicated well in various fish cells with a pronounced cytopathic effect. Ultrastructurally, morphogenesis of virus progeny was detected only in the cytoplasm. Nucleocapsids were observed to bud through membranes of the endoplasmic reticulum and/or Golgi apparatus into dilated vesicles. Egress of mature virions occurs primarily by exocytosis and, only very rarely, by budding at the plasma membrane. Morphologically similar viruses have been isolated from grass carp (Ctenopharyngodon idella L.), from the blue crab (Callinectis sapidus L.), from the European shore crab (Carcinus maenas L.), and from shrimps (Penaeus monodon L.). In summary, we present the first ultrastructural characterization of a new virus which might represent a member of a novel virus family which has morphological features resembling those found in rhabdo-, corona-, and baculoviridae.",,"Baculoviridae; Blicca bjoerkna; Callinectes; Callinectes sapidus; Carassius auratus; Carcinus maenas; Ctenopharyngodon idella; Cyprinidae; Cypriniformes; Cyprinus carpio; Decapoda (Crustacea); Grapsidae; Hyperoglyphe porosa; Monodon; Penaeus monodon; Tinca tinca; unidentified baculovirus",,"Granzow, H.; Friedrich Loeffler Institutes, Fed. Res. Ctr. Virus Dis. of Anim., Boddenblick 5 A, D-17493 Greifswald-Insel Riems, Germany",,,14319276,,MIMIF,,"English","Microsc. Microanal.",Conference Paper,"Final",,Scopus,2-s2.0-0142027600
"De Haan C.A.M., Van Genne L., Stoop J.N., Volders H., Rottier P.J.M.","7003682643;6507333385;8285293300;6507537974;7006145490;","Coronaviruses as Vectors: Position Dependence of Foreign Gene Expression",2003,"Journal of Virology","77","21",,"11312","11323",,55,"10.1128/JVI.77.21.11312-11323.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142124183&doi=10.1128%2fJVI.77.21.11312-11323.2003&partnerID=40&md5=2f217e8073cd981360083e47afadab86","Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands","De Haan, C.A.M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Van Genne, L., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Stoop, J.N., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Volders, H., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands; Rottier, P.J.M., Dept. of Infect. Dis. and Immunology, Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, Netherlands, Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands","Coronaviruses are the enveloped, positive-stranded RNA viruses with the largest RNA genomes known. Several features make these viruses attractive as vaccine and therapeutic vectors: (i) deletion of their nonessential genes is strongly attenuating; (ii) the genetic space thus created allows insertion of foreign information; and (iii) their tropism can be modified by manipulation of the viral spike. We studied here their ability to serve as expression vectors by inserting two different foreign genes and evaluating systematically the genomic position dependence of their expression, using a murine coronavirus as a model. Renilla and firefly luciferase expression cassettes, each provided with viral transcription regulatory sequences (TRSs), were inserted at several genomic positions, both independently in different viruses and combined within one viral genome. Recombinant viruses were generated by using a convenient method based on targeted recombination and host cell switching. In all cases high expression levels of the foreign genes were observed without severe effects on viral replication in vitro. The expression of the inserted gene appeared to be dependent on its genomic position, as well as on the identity of the gene. Expression levels increased when the luciferase gene was inserted closer to the 3′ end of the genome. The foreign gene insertions generally reduced the expression of upstream viral genes. The results are consistent with coronavirus transcription models in which the transcription from upstream TRSs is attenuated by downstream TRSs. Altogether, our observations clearly demonstrate the potential of coronaviruses as (multivalent) expression vectors.",,"luciferase; virus RNA; virus vector; article; attenuation; Coronavirus; disease model; essential gene; expression vector; gene cassette; gene deletion; gene expression; gene identification; gene insertion; gene structure; nonhuman; priority journal; Renilla; RNA gene; RNA virus; sequence analysis; transcription regulation; transcription regulatory sequence; vaccine production; virus envelope; virus recombinant; Animals; Anthozoa; Base Sequence; Beetles; Cell Line; Coronavirus; Gene Expression Regulation, Viral; Genetic Vectors; Genome, Viral; Luciferases; Mice; Molecular Sequence Data; Murine hepatitis virus; Plasmids; Recombination, Genetic; Regulatory Sequences, Nucleic Acid; Transcription, Genetic; Virus Replication","Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc. 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Virol., 75, pp. 12359-12369; Curtis, K.M., Yount, B., Baric, R.S., Heterologous gene expression from transmissible gastroenteritis virus replicon particles (2002) J. Virol., 76, pp. 1422-1434; De Groot, R.J., Ter Haar, R.J., Horzinek, M.C., Van der Zeijst, B.A., Intracellular RNAs of the feline infectious peritonitis coronavirus strain 79-1146 (1987) J. Gen. Virol., 68, pp. 995-1002; De Haan, C.A., Kuo, L., Masters, P.S., Vennema, H., Rottier, P.J., Coronavirus particle assembly: Primary structure requirements of the membrane protein (1998) J. Virol., 72, pp. 6838-6850; De Haan, C.A., Masters, P.S., Shen, X., Weiss, S., Rottier, P.J., The group-specific murine coronavirus genes are not essential, but their deletion, by reverse genetics, is attenuating in the natural host (2002) Virology, 296, pp. 177-189; De Haan, C.A., Volders, H., Koetzner, C.A., Masters, P.S., Rottier, P.J., Coronaviruses maintain viability despite dramatic rearrangements of the strictly conserved genome organization (2002) J. Virol., 76, pp. 12491-12502; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Enjuanes, L., Sola, I., Almazan, F., Ortego, J., Izeta, A., Gonzalez, J.M., Alonso, S., Sanchez, C., Coronavirus derived expression systems (2001) J. 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Virus Res., 48, pp. 1-100; Luytjes, W., Coronvirus gene expression (1995) The Coronaviridae, pp. 33-54. , S. G. Siddell (ed.), Plenum Press, Inc., New York, N.Y; Luytjes, W., Bredenbeek, P.J., Noten, A.F., Horzinek, M.C., Spaan, W.J., Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus (1988) Virology, 166, pp. 415-422; Makino, S., Joo, M., Effect of intergenic consensus sequence flanking sequences on coronavirus transcription (1993) J. Virol., 67, pp. 3304-3311; Makino, S., Joo, M., Makino, J.K., A system for study of corona-virus mRNA synthesis: A regulated, expressed subgenomic defective interfering RNA results from intergenic site insertion (1991) J. Virol., 65, pp. 6031-6041; Masters, P.S., Koetzner, C.A., Kerr, C.A., Heo, Y., Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the coronavirus mouse hepatitis virus (1994) J. Virol., 68, pp. 328-337; Navas, S., Seo, S.H., Chua, M.M., Sarma, J.D., Lavi, E., Hingley, S.T., Weiss, S.R., Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis (2001) J. Virol., 75, pp. 2452-2457; Ontiveros, E., Kuo, L., Masters, P.S., Perlman, S., Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS (2001) Virology, 289, pp. 230-238; Ozdarendeli, A., Ku, S., Rochat, S., Williams, G.D., Senanayake, S.D., Brian, D.A., Downstream sequences influence the choice between a naturally occurring noncanonical and closely positioned upstream canonical heptameric fusion motif during bovine coronavirus subgenomic mRNA synthesis (2001) J. Virol., 75, pp. 7362-7374; Phillips, J.J., Chua, M.M., Lavi, E., Weiss, S.R., Pathogenesis of chimeric MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence (1999) J. Virol., 73, pp. 7752-7760; Raamsman, M.J., Locker, J.K., De Hooge, A., De Vries, A.A., Griffiths, G., Vennema, H., Rottier, P.J., Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E (2000) J. Virol., 74, pp. 2333-2342; Rottier, P.J., Horzinek, M.C., Van der Zefjst, B.A., Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin (1981) J. Virol., 40, pp. 350-357; Sarma, J.D., Scheen, E., Seo, S.H., Koval, M., Weiss, S.R., Enhanced green fluorescent protein expression may be used to monitor murine coronavirus spread in vitro and in the mouse central nervous system (2002) J. Neurovirol., 8, pp. 381-391; Sawicki, D., Wang, T., Sawicki, S., The RNA structures engaged in replication and transcription of the A59 strain of mouse hepatitis virus (2001) J. Gen. 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Plenum Press, Inc., New York, N.Y; Sola, I., Alonso, S., Zuniga, S., Balasch, M., Plana-Duran, J., Enjuanes, L., Engineering the transmissible gastroenteritis virus genome as an expression vector inducing lactogenic immunity (2003) J. Virol., 77, pp. 4357-4369; Stirrups, K., Shaw, K., Evans, S., Dalton, K., Casais, R., Cavanagh, D., Britton, P., Expression of reporter genes from the defective RNA CD-61 of the coronavirus infectious bronchitis virus (2000) J. Gen. Virol., 81, pp. 1687-1698; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus (2001) J. Gen. Virol., 82, pp. 1273-1281; Van der Most, R.G., De Groot, R.J., Spaan, W.J., Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation (1994) J. Virol., 68, pp. 3656-3666; Van Marle, G., Luytjes, W., Van der Most, R.G., Van der Straaten, T., Spaan, W.J., Regulation of coronavirus mRNA transcription (1995) J. Virol., 69, pp. 7851-7856; Yount, B., Curtis, K.M., Baric, R.S., Strategy for systematic assembly of large RNA and DNA genomes: Transmissible gastroenteritis virus model (2000) J. Virol., 74, pp. 10600-10611; Yount, B., Denison, M.R., Weiss, S.R., Baric, R.S., Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59 (2002) J. Virol., 76, pp. 11065-11078","Rottier, P.J.M.; Virology Division, Dept. of Infect. Dis. and Immunology, Yalelaan 1, 3584CL Utrecht, Netherlands; email: p.rottier@vet.uu.nl",,,0022538X,,JOVIA,"14557617","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0142124183
"Schwegmann-Wessels C., Zimmer G., Schröder B., Breves G., Herrler G.","6506344309;7102982629;7102045143;7005092152;7006339246;","Binding of Transmissible Gastroenteritis Coronavirus to Brush Border Membrane Sialoglycoproteins",2003,"Journal of Virology","77","21",,"11846","11848",,36,"10.1128/JVI.77.21.11846-11848.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142060813&doi=10.1128%2fJVI.77.21.11846-11848.2003&partnerID=40&md5=1a4374d528d9633134103d096bf99d4d","Institut für Virologie, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany; Physiologisches Institut, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany; Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany","Schwegmann-Wessels, C., Institut für Virologie, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany, Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany; Zimmer, G., Institut für Virologie, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany; Schröder, B., Physiologisches Institut, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany; Breves, G., Physiologisches Institut, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany; Herrler, G., Institut für Virologie, Tierärztliche Hochsch. Hannover, 30559 Hannover, Germany","Transmissible gastroenteritis coronavirus (TGEV) is a porcine pathogen causing enteric infections that are lethal for suckling piglets. The enterotropism of TGEV is connected with the sialic acid binding activity of the viral surface protein S. Here we show that, among porcine intestinal brush border membrane proteins, TGEV recognizes a mucin-type glycoprotein designated MGP in a sialic acid-dependent fashion. Virus binding assays with cryosections of the small intestine from a suckling piglet revealed the binding of TGEV to mucin-producing goblet cells. A nonenteropathogenic mutant virus that lacked a sialic acid binding activity was unable to bind to MGP and to attach to goblet cells. Our results suggest a role of MGP in the enteropathogenicity of TGEV.",,"glycoprotein MGP; membrane protein; mucin; sialic acid; sialoglycoprotein; unclassified drug; virus protein; animal tissue; article; controlled study; enzyme linked immunosorbent assay; goblet cell; intestine brush border; jejunum; mucus; nonhuman; polyacrylamide gel electrophoresis; priority journal; swine; Transmissible gastroenteritis virus; virus cell interaction; Animals; Animals, Suckling; Cell Membrane; Gastroenteritis, Transmissible, of Swine; Intestine, Small; Microvilli; Sialoglycoproteins; Swine; Transmissible gastroenteritis virus","Cone, R.A., Mucus (1999) Mucosal Immunology, pp. 43-64. , P. L. Ogra, J. Mestecky, M. E. Lamm, W. Strober, J. Bienenstock, and J. R. McGhee (ed.). Academic Press, San Diego, Calif; Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjostrom, H., Noren, O., Laude, H., Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy, pp. 835-849. , M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carsten, M. K. Estes, S. M. Lemon, M. A. Mayo, D. J. McGeoch, C. R. Pringle, and R. B. Wickner (ed.). Academic Press, New York, N.Y; Gebauer, F., Posthumus, W.P., Correa, I., Sune, C., Smerdou, C., Sanchez, C.M., Lenstra, J.A., Enjuanes, L., Residues involved in the antigenic sites of transmissible gastroenteritis coronavirus S glycoprotein (1991) Virology, 183, pp. 225-238; Krempl, C., Ballesteros, M.L., Zimmer, G., Enjuanes, L., Klenk, H.D., Herrler, G., Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants (2000) J. Gen. Virol., 81, pp. 489-496; Krempl, C., Herrler, G., Sialic acid binding activity of transmissible gastroenteritis coronavirus affects sedimentation behavior of virions and solubilized glycoproteins (2001) J. Virol., 75, pp. 844-849; Krempl, C., Schultze, B., Laude, H., Herrler, G., Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus (1997) J. Virol., 71, pp. 3285-3287; Kyhse-Anderson, J., Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose (1984) J. Biochem. Biophys. Methods, 10, pp. 203-209; Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Sanchez, C.M., Jimenez, G., Laviada, M.D., Correa, I., Sune, C., Bullido, M., Gebauer, F., Escribano, J.M., Antigenic homology among coronaviruses related to transmissible gastroenteritis virus (1990) Virology, 174, pp. 410-417; Schröder, B., Hattenhauer, O., Breves, G., Phosphate transport in pig proximal small intestines during postnatal development: Lack of modulation by calcitriol (1998) Endocrinology, 139, pp. 1500-1507; Schultze, B., Krempl, C., Ballesteros, M.L., Shaw, L., Schauer, R., Enjuanes, L., Herrler, G., Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity (1996) J. Virol., 70, pp. 5634-5637; Schwegmann-Wessels, C., Zimmer, G., Laude, H., Enjuanes, L., Herrler, G., Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins (2002) J. Virol., 76, pp. 6037-6043; Zimmer, G., Trotz, I., Herrler, G., N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus (2001) J. Virol., 75, pp. 4744-4751","Schwegmann-Wessels, C.; Institut für Virologie, Tierärztliche Hochsch. Hannover, Bünteweg 17, 30559 Hannover, Germany; email: Christel.Schwegmann@tiho-hannover.de",,,0022538X,,JOVIA,"14557669","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0142060813
"Ng M.L., Tan S.H., See E.E., Ooi E.E., Ling A.E.","36747598400;55455679900;6602403458;7004519587;7102194546;","Early events of SARS coronavirus infection in vero cells",2003,"Journal of Medical Virology","71","3",,"323","331",,35,"10.1002/jmv.10499","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141869946&doi=10.1002%2fjmv.10499&partnerID=40&md5=71ab51097fc42ec48be99582ebc8bfd6","Department of Microbiology, Faculty of Medicine, National University of Singapore, Singapore, Singapore; Electron Microscopy Unit, Faculty of Medicine, National University of Singapore, Singapore, Singapore; Environmental Health Institute, National Environment Agency, Singapore, Singapore; Department of Pathology, Singapore General Hospital, Singapore, Singapore; Department of Microbiology, National University of Singapore, 5 Science Drive 2, Singapore 117597, Singapore","Ng, M.L., Department of Microbiology, Faculty of Medicine, National University of Singapore, Singapore, Singapore, Electron Microscopy Unit, Faculty of Medicine, National University of Singapore, Singapore, Singapore, Department of Microbiology, National University of Singapore, 5 Science Drive 2, Singapore 117597, Singapore; Tan, S.H., Electron Microscopy Unit, Faculty of Medicine, National University of Singapore, Singapore, Singapore; See, E.E., Environmental Health Institute, National Environment Agency, Singapore, Singapore; Ooi, E.E., Environmental Health Institute, National Environment Agency, Singapore, Singapore; Ling, A.E., Department of Pathology, Singapore General Hospital, Singapore, Singapore","An isolate from a patient in the recent severe acute respiratory syndrome (SARS) outbreak in Singapore was used to infect Vero E6 cells. This study concentrated on the first 30 min of infection. It was discovered that the SARS coronavirus attached, entered, and uncoated the nucleocapsids, all within a 30-min period. At 5 min after infection, several virus particles lined the Vero cell plasma membrane. Virus particles were at various stages of fusion at the cell surface, since entry was not a synchronised process. After entry (10 and 15 min), spherical core particles moved into the cytoplasm within large vacuoles. Quite surprising at such early stages of infection (20 min), a virus-induced change in the infected cells was evident. The induction of myelin-like membrane whorls was obvious within the same vacuoles as the core particles. The significance of this virus-induced change is unknown at this stage. By 25-30 min postinfection (p.i.), the spherical core particles appeared to be disassociating and, in their place, doughnut-shaped electron-dense structures were observed. These could be the virus genomes together with the helical nucleocapsids. They were no longer in large vacuoles but packaged into smaller vacuoles in the cytoplasm, and occasionally in small groups. © 2003 Wiley-Liss, Inc.","Early events; SARS infection; Virus entry","animal cell; article; cell surface; cell vacuole; Coronavirus; cytoplasm; epidemic; nonhuman; SARS coronavirus; severe acute respiratory syndrome; Singapore; Vero cell; virus genome; virus infection; virus nucleocapsid; virus particle; virus pneumonia; Animals; Cell Membrane; Cercopithecus aethiops; Cytoplasm; Humans; Microscopy, Electron; SARS Virus; Time Factors; Vero Cells; Coronavirus; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Ruan, Y.J., Wei, C.L., Ling, A.E., Vega, V.B., Thoreau, H., Se Thoe, S.Y., Chia, J.M., Liu, E.T., Comparative full length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785","Ng, M.L.; Department of Microbiology, National University of Singapore, 5 Science Drive 2, Singapore 117597, Singapore; email: micngml@nus.edu.sg",,,01466615,,JMVID,"12966536","English","J. Med. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0141869946
"Liu Y., Cai Y., Zhang X.","27167942300;49962967600;55715175900;","Induction of Caspase-Dependent Apoptosis in Cultured Rat Oligodendrocytes by Murine Coronavirus Is Mediated during Cell Entry and Does Not Require Virus Replication",2003,"Journal of Virology","77","22",,"11952","11963",,35,"10.1128/JVI.77.22.11952-11963.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242331747&doi=10.1128%2fJVI.77.22.11952-11963.2003&partnerID=40&md5=eb3f03352659a749a88b8d8e0ef4419d","Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205-7199, United States","Liu, Y., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Cai, Y., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States; Zhang, X., Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, Little Rock, AR 72205, United States, Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205-7199, United States","Murine coronavirus mouse hepatitis virus (MHV) causes demyelination of the central nervous system (CNS) in rats and mice. Apoptotic oligodendrocytes have been detected in the vicinity of the CNS demyelinating lesions in these animals. However, whether MHV can directly induce oligodendrocyte apoptosis has not been documented. Here, we established a rat oligodendrocyte culture that is morphologically and phenotypically indistinguishable from the primary rat oligodendrocytes. Using this culture, we showed that mature rat oligodendrocytes were permissive to MHV infection but did not support productive virus replication. Significantly, oligodendrocytes infected with both live and ultraviolet light-inactivated viruses underwent apoptosis to a similar extent, which was readily detectable at 24 h postinfection as revealed by apoptotic bodies and DNA fragmentation, indicating that MHV-induced apoptosis is mediated during the early stages of the virus life cycle and does not require virus replication. Prior treatment of cells with the lysosomotropic agents NH4Cl and chloroquine as well as the vacuolar proton pump-ATPase inhibitor bafilomycin A1, all of which block the acidification of the endosome, prevented oligodendrocytes from succumbing to apoptosis induced by MHV mutant OBLV60, which enters cells via endocytosis, indicating that fusion between the viral envelope and cell membranes triggers the apoptotic cascade. Treatment with the pan-caspase inhibitor Z-VAD-fmk blocked MHV-induced apoptosis, suggesting an involvement of the caspase-dependent pathway. Our results, thus, for the first time provide unequivocal evidence that infection of oligodendrocytes with MHV directly results in apoptosis. This finding provides an explanation for the destruction of oligodendrocytes and the damage of myelin sheath in MHV-infected CNS and suggests that oligodendrocyte apoptosis may be one of the underlying mechanisms for the pathogenesis of MHV-induced demyelinating diseases in animals.",,"ammonium chloride; bafilomycin A1; caspase; chloroquine; DNA fragment; proton transporting adenosine triphosphate synthase inhibitor; acidification; animal cell; animal disease; apoptosis; article; cell culture; cell structure; controlled study; demyelination; endosome; Murine hepatitis coronavirus; myelin sheath; nonhuman; oligodendroglia; pathogenesis; phenotype; priority journal; rat; ultraviolet radiation; virus inactivation; virus mutant; virus replication; Animals; Apoptosis; Caspases; Cells, Cultured; Demyelinating Diseases; Membrane Fusion; Murine hepatitis virus; Oligodendroglia; Rats; Rats, Sprague-Dawley; Virus Replication","An, S., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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Neurovirol., 2, pp. 101-110; Jan, J.T., Chatterjee, S., Griffin, D.E., Sindbis virus entry into cells triggers apoptosis by activating sphingomyelinase, leading to the release of ceramide (2000) J. Virol., 74, pp. 6425-6432; Jan, J.T., Griffin, D.E., Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication (1999) J. Virol., 73, pp. 10296-10302; Kalicharran, K., Mohandas, D., Wilson, G., Dales, S., Regulation of the initiation of coronavirus JHM infection in primary oligodendrocytes and L-2 fibroblasts (1996) Virology, 225, pp. 33-43; Knobler, R.L., Dubois-Dalcq, M., Haspel, M.V., Claysmith, A.P., Lampert, P.W., Oldstone, M.B., Selective localization of wild type and mutant mouse hepatitis virus (JHM strain) antigens in CNS tissue by fluorescence, light and electron microscopy (1981) J. 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Res., 31, pp. 193-204; Matthews, A.E., Lavi, E., Weiss, S.R., Paterson, Y., Neither B cells nor T cells are required for CNS demyelination in mice persistently infected with MHV-A59 (2002) J. Neurovirol., 8, pp. 257-264; Matthews, A.E., Weiss, S.R., Paterson, Y., Murine hepatitis virus-a model for virus-induced CNS demyelination (2002) J. Neurovirol., 8, pp. 76-85; McNulty, S., Crouch, M., Smart, D., Rumsby, M., Differentiation of bipolar CG-4 line oligodendrocytes is associated with regulation of CREB, MAP kinase and PKC signaling pathways (2001) Neurosci. Res., 41, pp. 217-226; Miura, T.A., Morris, K., Ryan, S., Cook, J.L., Routes, J.M., Adenovirus E1A, not human papillomavirus E7, sensitizes tumor cells to lysis by macrophages through nitric oxide- and TNF-alpha-dependent mechanisms despite up-regulation of 70-kDa heat shock protein (2003) J. Immunol., 170, pp. 4119-4126; Nash, T.C., Buchmeier, M.J., Entry of mouse hepatitis virus into cells by endosomal and nonendosomal pathways (1997) Virology, 233, pp. 1-8; Niemann, H., Klenk, H.D., Coronavirus glycoprotein E1, a new type of viral glycoprotein (1981) J. Mol. Biol., 153, pp. 993-1010; Nijhawan, D., Honarpour, N., Wang, X., Apoptosis in neural development and disease (2000) Annu. Rev. Neurosci., 23, pp. 73-87; Pasick, J.M., Dales, S., Infection by coronavirus JHM of rat neurons and oligodendrocyte-type-2 astrocyte lineage cells during distinct developmental stages (1991) J. Virol., 65, pp. 5013-5028; Ramsey-Ewing, A., Moss, B., Apoptosis induced by a post binding step of vaccinia virus entry into Chinese hamster ovary cells (1998) Virology, 242, pp. 138-149; Roulston, A., Marcellus, R., Branton, P., Viruses and apoptosis (1999) Annu. Rev. Microbiol., 53, pp. 577-628; Schwartz, T., Fu, L., Lavi, E., Programmed cell death in MHV-induced demyelination (2001) Adv. Exp. Med. Biol., 494, pp. 163-167; Slee, E.A., Zhu, H., Chow, S.C., MacFarlane, M., Nicholson, D.W., Cohen, G.M., Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32 (1996) Biochem. J., 315, pp. 21-24; Stohlman, S.A., Lai, M.M.C., Phosphoproteins of murine hepatitis viruses (1979) J. Virol., 32, pp. 672-675; Sturman, L.S., Ricard, C.S., Holmes, K.V., Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37 degrees C correlates with virus aggregation and virus-induced cell fusion (1990) J. Virol., 64, pp. 3042-3050; Tyler, K.L., Squier, M.K., Rodgers, S.E., Schneider, B.E., Oberhaus, S.M., Grdina, T.A., Cohen, J.J., Dermody, T.S., Differences in the capacity of reovirus strains to induce apoptosis are determined by the viral attachment protein sigma 1 (1995) J. Virol., 69, pp. 6972-6979; Van Dinter, S., Flintoff, W.F., Rat glial C6 cells are defective in murine coronavirus internalization (1987) J. Gen. 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Virol., 73, pp. 8771-8780; Wu, G.F., Dandekar, A.A., Pewe, L., Perlman, S., CD4 and CD8 T cells have redundant but not identical roles in virus-induced demyelination (2000) J. Immunol., 165, pp. 2278-2286; Wyllie, A.H., Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation (1980) Nature, 284, pp. 555-556; Yokomori, K., Banner, L.R., Lai, M.M.C., Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses (1991) Virology, 183, pp. 647-657; Yokomori, K., La Monica, N., Makino, S., Shieh, C.K., Lai, M.M.C., Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus (1989) Virology, 173, pp. 683-691; Yokomori, K., Lai, M.M., Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors (1992) J. Virol., 66, pp. 6194-6199; Yu, D.S., Hsu, C.M., Lee, W.H., Chang, S.Y., Ma, C.P., Flow cytometric DNA and cytomorphometric analysis in renal cell carcinoma: Its correlation with histopathology and prognosis (1993) J. Surg. Res., 55, pp. 480-485; Yu, X., Bi, W., Weiss, S.R., Leibowitz, J.L., Mouse hepatitis virus gene 5b protein is a new virion envelope protein (1994) Virology, 202, pp. 1018-1023","Zhang, X.; Dept. of Microbiology and Immunology, Univ. of Arkansas for Med. Sciences, 4301 W. Markham St., Little Rock, AR 72205-7199, United States; email: zhangxuming@uams.edu",,,0022538X,,JOVIA,"14581532","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0242331747
[No author name available],[No author id available],"Consensus for the management of severe acute respiratory syndrome",2003,"Chinese Medical Journal","116","11",,"1603","1636",,15,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346266032&partnerID=40&md5=7640938e1aca2934f1dfb9f9c565a54e",,"","SARS, first reported in Guangdong Province, China, in November 2002, eventually spread out over 24 provinces, autonomous regions, and municipalities in China, and later affected over 32 countries and areas in Asia, America and Europe. The epidemic situation of the disease gained high attention from scientists all around the world beginning in January 2003. Because China was the first area being affected by the epidemic, Chinese scientists focused on the search for the pathogen involved in the infection after excluding many ordinary ones. WHO set up a global network laboratory on March 17, 2003 to expedite the collaborative research on the causative agent of SARS. On April 16, 2003, WHO announced in Geneva that a new pathogen, a member of the coronavirus family never before seen in humans, is the cause of SARS. The identification of the virus was the result of the close international collaboration of a network of 13 laboratories in 9 countries, and was based on research into viral morphology, molecular biology, and serology, and involved animal experiments. The new coronavirus has been named SARS coronavirus (SARS-CoV). Infections of classical coronaviruses usually occur during the seasons of winter and spring. These viruses are spread worldwide and have been classified into three groups. Groups 1 and 2 mainly include mammalian coronaviruses, and Group 3 mainly includes avian coronaviruses. Coronaviruses affecting humans include 2 serological types, HcoV-229E and HcoV-OC43, both responsible for infections of the human respiratory tract. This group of viruses causes about 20% of common colds in humans. They also form one of the main causes of acute aggravation from chronic bronchitis in adults. Genomic studies suggest that the genotype of SARS-CoV is not the same as the genotype of the three known types of coronavirus. Serum infected with a Group 1 coronavirus can react with SARS-CoV, but serum from SARS patients does not react with known coronaviruses. Thus, SARS-CoV can be included in Group 4 as a new type of coronavirus.",,"Artemisia annua extract; Atractylodes extract; bamboo extract; Bupleurum root; Codonopsis extract; Coptis rhizome; Cornus extract; Cyperus extract; Ephedra extract; Gardenia extract; ginger extract; ginseng extract; Glycyrrhiza extract; lopinavir; Magnolia extract; methylprednisolone; oxygen; Paeonia radix; Paeonia suffruticosa extract; plant medicinal product; Polygala extract; prednisolone; prednisone; Rehmnnia extract; ribavirin; ritonavir; Salvia miltiorrhiza extract; Saussurea extract; Trichosanthes extract; unclassified drug; unindexed drug; acupuncture; antibody detection; article; Chinese herb; clinical feature; differential diagnosis; disease classification; epidemic; geographic distribution; histopathology; human; immune response; infection control; infection risk; infection sensitivity; laboratory diagnosis; mortality; pathogenesis; polymerase chain reaction; population distribution; psychotherapy; radiodiagnosis; SARS coronavirus; severe acute respiratory syndrome; social aspect; T lymphocyte subpopulation; virus genome; virus morphology; virus transmission; Humans; Severe Acute Respiratory Syndrome","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. 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(Chin), 26, pp. 329-333; Li, X.W., Jiang, R.M., Guo, J.Z., Glucocorticoid in the treatment of severe acute respiratory syndrome patients: A preliminary report (2003) Chin. J. Intern. Med. (Chin), 42, pp. 378-381; Liu, Y.N., Fan, B.X., Fang, X.Q., The quantitative detection of anti-coronavirus antibody titer in medical personnel closely contacted with severe acute respiratory syndrome patients (2003) Chin. J. Tuberc. Respir. Dis. (Chin), 26, pp. 583-585; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809",,,,03666999,,CMDJA,"14642124","English","Chin. Med. J.",Article,"Final",,Scopus,2-s2.0-0346266032
"González J.M., Gomez-Puertas P., Cavanagh D., Gorbalenya A.E., Enjuanes L.","57201828108;6701710022;26642890500;7005626044;7006565392;","A comparative sequence analysis to revise the current taxonomy of the family Coronaviridae",2003,"Archives of Virology","148","11",,"2207","2235",,200,"10.1007/s00705-003-0162-1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344304518&doi=10.1007%2fs00705-003-0162-1&partnerID=40&md5=e1faa03761b570283473c4105aaea62b","Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, Madrid, Spain; Bioinfo. Lab. Ctro. de Astrobiologia, Torrejón de Ardoz, Madrid, Spain; Institute for Animal Health, Compton Laboratory, Compton, Newbury, United Kingdom; Center of Infectious Diseases, Leiden University, Medical Center, Leiden, Netherlands; Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, CSIC, Cantoblanco, 28049 Madrid, Spain; Center of Infectious Diseases, Leiden University, Medical Center, 2333 ZA Leiden, Netherlands","González, J.M., Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, Madrid, Spain; Gomez-Puertas, P., Bioinfo. Lab. Ctro. de Astrobiologia, Torrejón de Ardoz, Madrid, Spain; Cavanagh, D., Institute for Animal Health, Compton Laboratory, Compton, Newbury, United Kingdom; Gorbalenya, A.E., Center of Infectious Diseases, Leiden University, Medical Center, Leiden, Netherlands, Center of Infectious Diseases, Leiden University, Medical Center, 2333 ZA Leiden, Netherlands; Enjuanes, L., Ctro. Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, Madrid, Spain, Dept. of Molecular and Cell Biology, Ctro. Nac. de Biotecnología, CSIC, Cantoblanco, 28049 Madrid, Spain","The Coronaviridae family, comprising the Coronavirus and Torovirus genera, is part of the Nidovirales order that also includes two other families, Arteriviridae and Roniviridae. Based on genetic and serological relationships, groups 1, 2 and 3 were previously recognized in the Coronavirus genus. In this report we present results of comparative sequence analysis of the spike (S), envelope (E), membrane (M), and nucleoprotein (N) structural proteins, and the two most conserved replicase domains, putative RNA-dependent RNA polymerase (RdRp) and RNA helicase (HEL), aimed at a revision of the Coronaviridae taxonomy. The results of pairwise comparisons involving structural and replicase proteins of the Coronavirus genus were consistent and produced percentages of sequence identities that were distributed in discontinuous clusters. Inter-group pairwise scores formed a single cluster in the lowest perceritile. No homologs of the N and E proteins have been found outside coronaviruses, and the only (very) distant homologs of S and M proteins were identified in toroviruses. Intragroup sequence conservation was higher, although for some pairs, especially those from the most diverse group 1, scores were close or even overlapped with those from the intergroup comparisons. Phylogenetic analysis of six proteins using a neighbor-joining algorithm confirmed three coronavirus groups. Comparative sequence analysis of RdRp and HEL domains were extended to include arterivirus and ronivirus homologs. The pairwise scores between sequences of the genera Coronavirus and Torovirus (22-25% and 21-25%) were found to be very close to or overlapped with the value ranges (12 to 22% and 17 to 25%) obtained for interfamily pairwise comparisons, but were much smaller than values derived from pairwise comparisons within the Coronavirus genus (63-71 % and 59-67%). Phylogenetic analysis confirmed toroviruses and coronaviruses to be separated by a large distance that is comparable to those between established nidovirus families. Based on comparison of these scores with those derived from analysis of separate ranks of several multi-genera virus families, like the Picornaviridae, a revision of the Coronaviridae taxonomy is proposed. We suggest the Coronavirus and Torovirus genera to be re-defined as two subfamilies within the Coronavirdae or two families within Nidovirales, and the current three informal coronavirus groups to be converted into three genera within the Coronaviridae.",,"Conserved Sequence; Coronaviridae; Phylogeny; RNA Helicases; RNA Replicase; Torovirus; Viral Structural Proteins; Arteriviridae; Arterivirus; Coronaviridae; Coronavirus; Nidovirales; Picornaviridae; Prokaryota; Roniviridae; Torovirus","Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J., Basic local alignment search tool (1990) J Mol Biol, 215, pp. 403-410; Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res, 25, pp. 3389-3402; Bateman, A., Birney, E., Durbin, R., Eddy, S.R., Finn, R.D., Sonnhammer, E.L., Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins (1999) Nucleic Acids Res, 27, pp. 260-262; Berke, T., Matson, D.O., Reclassification of the Caliciviridae into distinct genera and exclusion of hepatitis E virus from the family on the basis of comparative phylogenetic analysis (2000) Arch Virol, 145, pp. 1421-1436; Bradley, D.W., Balayan, M.S., Virus of enterically transmitted non-A, non-B hepatitis (1988) Lancet, 1, p. 819; Brian, D.A., Hogue, B.G., Kienzle, T.E., The coronavirus hemagglutinin esterase glycoprotein (1995) The Coronaviridae, pp. 165-176. , Siddell SG (ed) Plenum press, New York; Brierley, I., Ribosomal frameshifting on viral RNAs (1995) J Gen Virol, 76, pp. 1885-1892; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , Siddell SG (ed) Plenum press, New York; Cavanagh, D., Brian, D.A., Briton, M., Enjuanes, L., Holmes, K.V., Lai, M.M.C., Laude, H., Talbot, P., Revision of the taxonomy of the Coronavirus, Torovirus, and Arterivirus genera (1994) Arch Virol, 135, pp. 227-237; Cavanagh, D., Mawditt, K., Welchman, DdB., Britton, P., Gough, R.E., Coronaviruses from pheasants (Phasianus colchicus) are genetically closely related to coronaviruses of domestic fowl (infectious bronchitis virus) and turkeys (2002) Avian Pathol, 31, pp. 81-93; Chouljenko, V.N., Lin, X.Q., Kousoulas, K.G., Gorbalenya, A.E., Comparison of genomic and predicted amino acid sequences of respiratory and enteric bovine coronaviruses isolated from the same animal with fatal shipping pneumonia (2001) J Gen Virol, 82, pp. 2927-2933; Cornelissen, L.A.H.M., Wierda, C.M.H., Van Der Meer, F.J., Herrewegh, A.P.M., Horzinek, M.C., Egberonk, H.F., Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J Virol, 71, pp. 5277-5286; Cowley, J.A., Dimmock, C.M., Spann, K.M., Walker, P.J., Gill-associated virus of Penaeus monodon prawns: An invertebrate virus with ORF1a and ORF1b genes related to arteri-and coronaviruses (2000) J Gen Virol, 81, pp. 1473-1484; Cowley, J.A., Dimmock, C.M., Walker, P.J., Gill-associated nidovirus of Penaeus monodon prawns transcribes 3′-coterminal subgenomic mRNAs that do not possess 5′-leader sequences (2002) J Gen Virol, 83, pp. 927-935; Cowley, J.A., Walker, P.J., The complete genome sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses (2002) Arch Virol, 147, pp. 1977-1987; De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses (1997) Semin Virol, 8, pp. 33-47; Den Boon, J.A., Snijder, E.J., Chirnside, E.D., De Vries, A.A.F., Horzinek, M.C., Spaan, W.J.M., Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily (1991) J Virol, 65, pp. 2910-2920; Den Boon, J.A., Snijder, E.J., Locker, J.K., Horzinek, M.C., Rottier, J.M., Another triple-spanning envelope protein among intracellularly budding RNA viruses: The torovirus e protein (1991) Virology, 182, pp. 655-663; Doolittle, R.F., (1986) Of URFs and ORFs: A Primer on How to Analyze Derived Amino Acid Sequences, , University Science Books, Mill Valley, CA; Duckmanton, L., Luan, B., Devinish, J., Tellier, R., Petric, M., Characterization of torovirus from human fecal specimens (1997) Virology, 239, pp. 158-168; Enjuanes, L., Brian, D., Cavanagh, D., Holmes, K., Lai, M.M.C., Laude, H., Masters, P., Talbot, P., Coronaviridae (2000) Virus Taxonomy. 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Nac. de Biotecnología, CSIC, Campus Universidad Autónoma, Cantoblanco, Madrid, Spain",,,03048608,,ARVID,"14579179","English","Arch. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0344304518
"Nicholls J., Dong X.-P., Jiang G., Peiris M.","7201463077;56268793500;55343448700;7005486823;","SARS: Clinical virology and pathogenesis",2003,"Respirology","8",,,"S6","S8",,32,"10.1046/j.1440-1843.2003.00517.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345732171&doi=10.1046%2fj.1440-1843.2003.00517.x&partnerID=40&md5=30ba6e581ae59c82b035231364b9a4fb","Department of Pathology, University of Hong Kong, Hong Kong, Hong Kong; Institute of Virology, China; Department of Pathology, Beijing University, Beijing, China; Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Department of Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, SAR, Hong Kong","Nicholls, J., Department of Pathology, University of Hong Kong, Hong Kong, Hong Kong, Department of Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, SAR, Hong Kong; Dong, X.-P., Institute of Virology, China; Jiang, G., Department of Pathology, Beijing University, Beijing, China; Peiris, M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong","Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus, called the SARS coronavirus (SARS-CoV). Over 95% of well characterized cohorts of SARS have evidence of recent SARS-CoV infection. The genome of SARS-CoV has been sequenced and it is not related to any of the previously known human or animal coronaviruses. It is probable that SARS-CoV was an animal virus that adapted to human-human transmission in the recent past. The virus can be found in nasopharyngeal aspirate, urine and stools of SARS patients. Second generation reverse transcriptase polymerase chain reaction assays are able to detect SARS-CoV in nasopharyngeal aspirates of approximately 80% of patients with SARS within the first 3 days of illness. Seroconversion for SARS-CoV using immunofluorescence on infected cells is an excellent method of confirming the diagnosis, but antibody responses only appear around day 10 of the illness. Within the first 10 days the histological picture is that of acute phase diffuse alveolar damage (DAD) with a mixture of inflammatory infiltrate, oedema and hyaline membrane formation. Desquamation of pneumocytes is prominent and consistent. After 10 days of illness the picture changes to one of organizing DAD with increased fibrosis, squamous metaplasia and multinucleated giant cells. The role of cytokines in the pathogenesis of SARS is still unclear.","Histology; Pathology; SARS coronavirus; Severe acute respiratory syndrome","antibody response; giant cell; immunofluorescence; inflammatory infiltrate; lung edema; lung fibrosis; pathogenesis; priority journal; reverse transcription polymerase chain reaction; review; SARS coronavirus; seroconversion; severe acute respiratory syndrome; squamous cell metaplasia; virus genome; virus transmission; Histological Techniques; Humans; SARS Virus; Severe Acute Respiratory Syndrome","Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Chu, C.M., Cheng, V.C., Clinical progression and viral load in a community outbreak of coronavirus associated-SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Chan, K.H., Poon, L.L.M., Cheng, V.C.C., Detection of SARS coronavirus (SCoV) by RT-PCR, culture and serology in patients with severe acute respiratory syndrome (SARS) (2003) Emerg. Infect. Dis., , in press; Kuiken, T., Fouchier, R.A., Schutten, M., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: KOCKS postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Poutanen, S.M., Low, D.E., Henry, B., National Microbiology Laboratory Canada; Canadian Severe Acute Respiratory Syndrome Study Team. Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Guan, Y., Zheng, B.J., He, Y.Q., Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China (2003) Science, 302, pp. 276-278; Poon, L.L.M., Chan, K.H., Wong, O.K., Early diagnosis of SARS Coronavirus infection by real-time RT-PCR (2003) J. Clin. Virol., 28, pp. 233-238; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe, acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Lung pathology of severe acute respiratory syndrome (SARS). A study of 8 autopsy cases from Singapore (2003) Hum. Pathol., 34, p. 729; Ding, Y.Q., Wang, H.J., Shen, H., Study on etiology and pathology of severe acute respiratory syndrome (2003) Zhonghua Bing Li Xue Za Zhi, 32, pp. 195-200; Ding, Y., Wang, H., Shen, H., The clinical pathology of severe acute respiratory syndrome (SARS): A report from China (2003) J. Pathol., 200, pp. 282-289; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Cavanagh, D., The coronavirus suface glycoprotein (1995) The Coronaviridae, pp. 73-113. , Siddell S, ed. Plenum Press, New York; Nichols, J.E., Niles, J.A., Roberts Jr., N.J., Human lymphocyte apoptosis after exposure to influenza A virus (2001) J. Virol., 75, pp. 5921-5929; Julkunen, I., Sareneva, T., Pirhonen, J., Molecular pathogenesis of influenza A virus infection and virus-induced regulation of cytokine gene expression (2001) Cytokine Growth Factor Rev., 12, pp. 171-180; Ricard, J.D., Dreyfuss, D., Saumon, G., Production of inflammatory cytokines in ventilator-induced lung injury: A reappraisal (2001) Am. J. Respir. Crit. Care Med., 163, pp. 1176-1180; Miyazaki, Y., Araki, K., Vesin, C., Expression of a tumor necrosis factor-alpha transgene in murine lung causes lymphocytic and fibrosing alveolitis. A mouse model of progressive pulmonary fibrosis (1995) J. Clin. Invest., 96, pp. 250-259","Nicholls, J.; Department of Pathology, Queen Mary Hospital, University of Hong Kong, Hong Kong, SAR, Hong Kong; email: nicholls@pathology.hku.hk",,,13237799,,RSPIF,"15018126","English","Respirology",Review,"Final",,Scopus,2-s2.0-0345732171
"Hartmann K., Binder C., Hirschberger J., Cole D., Reinacher M., Schroo S., Frost J., Egberink H., Lutz H., Hermanns W.","7201407340;7102159579;7004025795;35597156900;7003284148;6504350060;7202439178;7004767057;57202819852;55922114000;","Comparison of Different Tests to Diagnose Feline Infectious Peritonitis",2003,"Journal of Veterinary Internal Medicine","17","6",,"781","790",,105,"10.1892/0891-6640(2003)017<0781:CODTTD>2.3.CO;2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744222628&doi=10.1892%2f0891-6640%282003%29017%3c0781%3aCODTTD%3e2.3.CO%3b2&partnerID=40&md5=bae2992ddbdfc499128b5f3ea51256fc","Department of Small Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Medizinische Tierklinik, München, Germany; Department of Large Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Inst. F. Veterinärpathologie, Universität Gießen, Gießen, Germany; Staatliches Untersuchungsamt Hessen, Gießen, Germany; Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Veterinärmedizinisches Labor, Dept. F. Inn. Veterinärmedizin, Universität Zürich, Zürich, Switzerland; Institut für Tierpathologie, Ludwig-Maximilians-Universität, München, Germany; Lehrst. F. Inn. Med. Kleinen H., Ludwig-Maximilians-Univ. Munchen, Veterinärstraße 13, 80539 München, Germany","Hartmann, K., Department of Small Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States, Lehrst. F. Inn. Med. Kleinen H., Ludwig-Maximilians-Univ. Munchen, Veterinärstraße 13, 80539 München, Germany; Binder, C., Medizinische Tierklinik, München, Germany; Hirschberger, J., Medizinische Tierklinik, München, Germany; Cole, D., Department of Large Animal Medicine, College of Veterinary Medicine, University of Georgia, Athens, GA, United States; Reinacher, M., Inst. F. Veterinärpathologie, Universität Gießen, Gießen, Germany; Schroo, S., Inst. F. Veterinärpathologie, Universität Gießen, Gießen, Germany; Frost, J., Staatliches Untersuchungsamt Hessen, Gießen, Germany; Egberink, H., Institute of Virology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, Netherlands; Lutz, H., Veterinärmedizinisches Labor, Dept. F. Inn. Veterinärmedizin, Universität Zürich, Zürich, Switzerland; Hermanns, W., Institut für Tierpathologie, Ludwig-Maximilians-Universität, München, Germany","Clinical data from 488 cats (1979-2000) with histopathologically confirmed feline infectious peritonitis (FIP) and 620 comparable controls were evaluated retrospectively to assess the value of several diagnostic tests frequently used in the evaluation of cats with suspected FIP. Diagnostic utility of serum albumin to globulin ratio for the diagnosis of FIP was greater than of the utility of serum total protein and γ-globulin concentrations. Diagnostic utility of these variables was higher when performed on effusion. On effusion, positive and negative predictive values of Rivalta's test, a test that distinguishes between exudates and transudates (0.86 and 0.97), anti-coronavirus antibody detection (0.90 and 0.79), and immunofluorescence staining of coronavirus antigen in macrophages (1.00 and 0.57) were investigated. The positive and negative predictive values of presence of anti-coronavirus antibodies were 0.44 and 0.90, respectively, antibody concentrations (1:1,600) were 0.94 and 0.88, presence of immune complexes measured by a competitive enzyme-linked immunosorbent assay were 0.67 and 0.84, and detection of viral RNA by serum reverse-transcriptase polymerase chain reaction (RT-PCR) were 0.90 and 0.47. Effusion RT-PCR was performed in 6 cats; it was positive in all 5 cats with FIP and negative in the cat with another disease. Diagnostic assays on the fluid in cats with body effusion had good predictive values. Definitive diagnosis of FIP on the basis of measurement of various variables in serum was not possible. Serum tests can only be used to facilitate the decision for more invasive diagnostic methods.","Cat; Diagnosis; FCoV; Feline coronavirus; FIP","immunoglobulin; plasma protein; serum albumin; serum globulin; virus antibody; antibody detection; article; cat; cat disease; Coronavirus; diagnostic test; effusion; enzyme linked immunosorbent assay; exudate; histopathology; immunofluorescence; intermethod comparison; macrophage; nonhuman; peritonitis; prediction; reverse transcription polymerase chain reaction; Animals; Antibodies, Viral; Antigen-Antibody Complex; Antigens, Viral; Ascitic Fluid; Blood Proteins; Case-Control Studies; Cats; Coronavirus Infections; Coronavirus, Feline; Enzyme-Linked Immunosorbent Assay; Feline Infectious Peritonitis; Fluorescent Antibody Technique; gamma-Globulins; Predictive Value of Tests; Retrospective Studies; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; ROC Curve; Sensitivity and Specificity; Serum Albumin; Coronavirus; Felidae; Feline coronavirus; Felis catus","Rohrbach, B.W., Legendre, A.M., Baldwin, C.A., Epidemiology of feline infectious peritonitis among cats examined at veterinary medical teaching hospitals (2001) J Am Vet Med Assoc, 218, pp. 1111-1115; Pedersen, N.C., Coronavirus diseases (coronavirus enteritis, feline infectious peritonitis) (1987) Diseases of the Cat. Medicine and Surgery, 1, pp. 193-214. , Holzworth J, ed. Philadelphia, PA: WB Saunders; Pedersen, N.C., Serologic studies of naturally occurring feline infectious peritonitis (1976) Am J Vet Res, 37, pp. 1449-1453; Loeffler, D.G., Ott, R.L., Evermann, J.F., Alexander, J.E., The incidence of naturally occurring antibodies against feline infectious peritonitis in selected cat populations (1978) Feline Pract, 8, pp. 43-47; Addie, D.D., Jarrett, J.O., Feline coronavirus antibodies in cats (1992) Vet Rec, 131, pp. 202-203; Sparkes, A.H., Gruffydd-Jones, T.J., Howard, P.E., Harbour, D.A., Coronavirus serology in healthy pedigree cats (1992) Vet Rec, 131, pp. 35-36; Pedersen, N.C., Feline infectious peritonitis: Something old, something new (1976) Feline Pract, 6, pp. 42-51; Addie, D.D., Jarrett, O., Feline coronavirus infection (1990) Infectious Diseases of the Dog and Cat, pp. 58-69. , Greene CE, ed. Philadelphia, PA: WB Saunders; Osterhaus, A., Horzinek, M.C., Reynolds, D.J., Seroepidemiology of feline infectious peritonitis virus infections using transmissible gastroenteritis virus as antigens (1977) Zentralbl Veterinarmed, 24, pp. 835-841; Berti-Bock, G., Vial, F., Premuda, L., Rulliere, R., Exudates, transudates and the Rivalta reaction (1895). 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Part I (1983) Feline Pract, 13, pp. 13-19; Sparkes, A.H., Gruffydd Jones, T.J., Harbour, D.A., Feline infectious peritonitis: A review of clinicopathological changes in 65 cases, and a critical assessment of their diagnostic value (1991) Vet Rec, 129, pp. 209-212; Paltrinieri, S., Grieco, V., Comazzi, S., Cammarata Parodi, M., Laboratory profiles in cats with different pathological and immunohistochemical findings due to feline infectious peritonitis (FIP) (2001) J Feline Med Surg, 3, pp. 149-159; Weiss, R.C., The diagnosis and clinical management of feline infectious peritonitis (1991) Vet Med Praha, 86, pp. 308-319; Wolf, A., Feline infectious peritonitis, Part 2 (1997) Feline Pract, 25, pp. 24-28; Walter, J.H., Rudolph, R., Untersuchungen zur Häufigkeit und zur Pathogenese der felinen infektiósen Periotonitis (FIP) (1989) Dtsch Tierarztl Wochenschr, 96, pp. 194-201; Lutz, H., Hauser, B., Horzinek, M.C., Feline infectious peritonitis (FIP): The present state of knowledge (1986) J Small Anim Pract, 27, pp. 108-116; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Feline Pract, 23, pp. 7-20; Shelly, S.M., Scarlett Kranz, J., Blue, J.T., Protein electrophoresis on effusions from cats as a diagnostic test for feline infectious peritonitis (1988) J Am Anim Hosp Assoc, 24, pp. 495-500; Rohrer, C., Suter, P.F., Lutz, H., The diagnosis of feline infectious peritonitis (FIP): Retrospective and prospective study (1994) Eur J Comp Anim Pract, 4, pp. 23-29; Sparkes, A.H., Gruffydd Jones, T.J., Harbour, D.A., An appraisal of the value of laboratory tests in the diagnosis of feline infectious peritonitis (1994) J Am Anim Hosp Assoc, 30, pp. 345-350; Duthie, S., Eckersall, P.D., Addie, D.D., Value of alpha 1-acid glycoprotein in the diagnosis of feline infectious peritonitis (1997) Vet Rec, 141, pp. 299-303; Stoddart, M.E., Whicher, J.T., Harbour, D.A., Cats inoculated with feline infectious peritonitis virus exhibit a biphasic acute phase plasma protein response (1988) Vet Rec, 123, pp. 622-624; Gunn-Moore, D.A., Gruffydd-Jones, T.J., Harbour, D.A., Detection of feline coronaviruses by culture and reverse transcriptase-polymerase chain reaction of blood samples from healthy cats and cats with clinical feline infectious peritonitis (1998) Vet Microbiol, 62, pp. 193-205; Pedersen, N.C., The history and interpretation of feline coronavirus serology (1995) Feline Pract, 23, pp. 46-51; Gouffaux, M., Pastoret, P.P., Henroteaux, M., Massip, A., Feline infectious peritonitis. Proteins of plasma and ascitic fluid (1975) Vet Pathol, 12, pp. 335-348; Horzinek, M.C., Osterhaus, A.D., Feline infectious peritonitis: A worldwide serosurvey (1979) Am J Vet Res, 40, pp. 1487-1492; Horzinek, M.C., Ederveen, J., Egberink, H., Virion polypeptide specificity of immune complexes and antibodies in cats inoculated with feline infectious peritonitis virus (1986) Am J Vet Res, 47, pp. 754-761; Goitsuka, R., Ohashi, T., Ono, K., IL-6 activity in feline infectious peritonitis (1990) J Immunol, 144, pp. 2599-2603; Hirschberger, J., Hartmann, K., Wilhelm, N., Klinik und Diagnostik der Felinen Infektiösen Peritonitis (1995) TierarztlPrax, 23, pp. 92-99; Kasbohm, C., Effusions of body cavities in the dog (2). 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(1995) Vet Q, 17, pp. 24-25; Herrewegh, A.A., Mahler, M., Hedrich, H.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Fehr, D., Bolla, S., Herrewegh, A.A., Detection of ferine coronavirus using RT-PCR: Basis for the study of the pathogenesis of feline infectious peritonitis (FIP) (1996) Schweiz Arch Tierheilkd, 138, pp. 74-79; Hök, K., Demonstration of feline infectious peritonitis in conjunctival epithelial cells from cats (1989) APMIS, 97, pp. 820-824; Tammer, R., Evensen, O., Lutz, H., Reinacher, M., Immunohistological demonstration of feline infectious peritonitis virus antigen in paraffin-embedded tissues using feline ascites or murine monoclonal antibodies (1995) Vet Immunol Immunopathol, 49, pp. 177-182; Jacobse Geels, H.E.L., Daha, M.R., Horzinek, M.C., Isolation and characterization of feline C3 and evidence for the immune complex pathogenesis of feline infectious peritonitis (1980) J Immunol, 125, pp. 1606-1610; Barlough, J.E., Cats, coronaviruses and coronavirus antibody tests (1985) J Small Anim Pract, 26, pp. 353-362","Hartmann, K.; Lehrst. F. Inn. Med. Kleinen H., Ludwig-Maximilians-Univ. Munchen, Veterinärstraße 13, 80539 München, Germany; email: Katrin.Hartmann@med.vetmed.uni-muenchen.de",,,08916640,,,"14658713","English","J. Vet. Intern. Med.",Article,"Final",,Scopus,2-s2.0-10744222628
"Lam W.K., Zhong N.S., Tan W.C.","7203021937;7102137996;13403886200;","Overview on SARS in Asia and the World",2003,"Respirology","8",,,"S2","S5",,37,"10.1046/j.1440-1843.2003.00516.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346363224&doi=10.1046%2fj.1440-1843.2003.00516.x&partnerID=40&md5=991b6b0235dc5e0a7f7d2a45cc08a8f5","Department of Medicine, University of Hong Kong, Hong Kong SAR, Hong Kong; Guangzhou Inst. of Resp. Diseases, Guangzhou, China; Department of Medicine, National University of Singapore, Singapore, Singapore; Department of Medicine, University of Hong Kong, Queen Mary Hospital, 102 Pokfulam Road, Hong Kong SAR, Hong Kong","Lam, W.K., Department of Medicine, University of Hong Kong, Hong Kong SAR, Hong Kong, Department of Medicine, University of Hong Kong, Queen Mary Hospital, 102 Pokfulam Road, Hong Kong SAR, Hong Kong; Zhong, N.S., Guangzhou Inst. of Resp. Diseases, Guangzhou, China; Tan, W.C., Department of Medicine, National University of Singapore, Singapore, Singapore","Severe Acute Respiratory Syndrome (SARS) is the first major novel, infectious disease to hit the international community in the 21st century. It originated in southern China in November 2002, reached Hong Kong in February 2003 and spread rapidly thereafter to 29 countries/regions on five continents. At the end of the epidemic, the global cumulative total was 8098 with 774 deaths. Seven Asian countries/regions were among the top ten on the list. Mainland China and Hong Kong, SAR, accounted for 87% of all cases and 84% of all deaths. Severe acute respiratory syndrome is caused by a novel coronavirus. It has alarmed the world with its infectivity and significant morbidity and mortality, its lack of a rapid, reliable diagnostic test and lack of effective specific treatment and vaccination. The adverse impact on travel and business around the world, particularly in Asia, has been enormous. Some lessons learnt from this epidemic included: (1) any outbreak of infectious disease can rapidly spread around the world by air travel; (2) early reporting of the outbreak to neighbouring countries/regions and the World Health Organization is essential to prevent international spread; and (3) infection control, tracing and quarantine of contacts are essential to control the epidemic. Many questions remain unanswered, including the origin and pathogenesis of the novel coronavirus, the natural history and the best specific treatment of the disease. The SARS-CoV has probably jumped from an animal host to humans. There is an urgent need to evaluate the human-animal habitat in southern China and to remove animal reservoirs if found.","Global impact; Severe acute respiratory syndrome; Tracing and quarantine","Asia; aviation; China; diagnostic test; disease carrier; epidemic; Hong Kong; human; infection control; infection prevention; pathogenesis; priority journal; review; SARS coronavirus; severe acute respiratory syndrome; virus infectivity; world health organization; China; Communicable Disease Control; Cost of Illness; Disease Outbreaks; Hong Kong; Humans; Severe Acute Respiratory Syndrome; Travel; World Health","Zhong, N.S., Zeng, G.Q., Our strategies for fighting severe acute respiratory syndrome (SARS) (2003) Am. J. Respir. Crit. Care Med., 168, pp. 7-9; Report on Pneumonia of Unknown Reason in Zhong Shan City, , In Office Document of Guangdong Department of Public Health (YWB-2003-2); Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Lee, N., Hui Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Severe acute respiratory syndrome - Singapore (2003) MMWR, 52, pp. 405-411; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Tsang, K.W., Mok, T.Y., Wong, P.C., Ooi, G.C., Severe acute respiratory syndrome (SARS) in Hong Kong (2003) Respirology, 8, pp. 259-265; (2003) Severe Acute Respiratory Syndrome (SARS), , http://http.www.who.int/csr/2003_03_12/en, Cited 12 March; Severe acute respiratory syndrome - Singapore (2003) MMWR, 52, pp. 405-411; (2003) JAMA, 289, pp. 3231-3234. , Reprinted; (2003) Summary Probable SARS Cases with Onset of Illness from 1 November 2002 to 31 July 2003 (Revised 26 September 2003), , http://www.who.int/csr/sars/country/table2003_09_23/en/, Cited 30 September; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/2003_04_16/en, Cited 16 April; Zhong, N.S., Zheng, B.J., Li, Y.M., Epidemiological and aetiological studies of patients with severe acute respiratory syndrome (SARS) from Guangdong in February (2003) Lancet, 362, pp. 1353-1358; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; (2003) SARS and Air Travel, , http://www.who.int/csr/sars/travel/airtravel/en/, Cited 5 August; (2003) Affected Areas - SARS, , http://www.who.int/csr/sars/areas/2003/en, Cited 16 March to 4 July; (2003) Civil International Air Transport Movement of Aircraft, , http://www.info.gov.hk/cad/english/aircraft.html, Cited 30 July; (2003) Hotel Room Occupancy Report, , http://www.discoverhongkong.com/partnernet.hktourismboard.com, Cited 14 July; (2003) CAACJ, 2537, p. 1. , CAAC Journal. Issue no. 2537, 25 July 2003. (In Chinese.); Guan, Y., Zheng, B.J., He, Y.Q., Isolation and characterization of viruses related to the SARS Coronavirus from animals in southern China (2003) Science, , http://www.sciencemag.org/cgi/content/abstract/1087139, Cited 5 September; (2003) Communicable Disease Surveillance & Response, Update 83 - One Hundred Days into the Outbreak, , http://www.who.int/csr/don/2003_06_18/en/, Cited 18 June","Lam, W.K.; Department of Medicine, University of Hong Kong, Queen Mary Hospital, 102 Pokfulam Road, Hong Kong SAR, Hong Kong; email: lamwk@hkucc.hku.hk",,,13237799,,RSPIF,"15018125","English","Respirology",Review,"Final",,Scopus,2-s2.0-0346363224
"Dandekar A.A., Jacobsen G., Waldschmidt T.J., Perlman S.","7005818765;7102705077;7005484313;7102708317;","Antibody-Mediated Protection against Cytotoxic T-Cell Escape in Coronavirus-Induced Demyelination",2003,"Journal of Virology","77","22",,"11867","11874",,12,"10.1128/JVI.77.22.11867-11874.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242363263&doi=10.1128%2fJVI.77.22.11867-11874.2003&partnerID=40&md5=c5d3fee0bcc24abd024aee22337f8598","Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Department of Pathology, University of Iowa, Iowa City, IA 52242, United States; Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States; Department of Pediatrics, University of Iowa, 2042 Medical Laboratories, Iowa City, IA 52242, United States","Dandekar, A.A., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States; Jacobsen, G., Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States; Waldschmidt, T.J., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States, Department of Pathology, University of Iowa, Iowa City, IA 52242, United States; Perlman, S., Interdisc. Program in Immunology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, Iowa City, IA 52242, United States, Department of Microbiology, University of Iowa, Iowa City, IA 52242, United States, Department of Pediatrics, University of Iowa, 2042 Medical Laboratories, Iowa City, IA 52242, United States","C57BL/6 (B6) mice infected with mouse hepatitis virus (MHV) strain JHM develop a clinically evident, demyelinating encephalomyelitis. Infectious virus can be isolated from the spinal cords of these mice and is invariably mutated in the immunodominant CD8 T-cell epitope recognized in this strain. We showed previously that these persistently infected mice did not mount a measurable serum anti-MHV neutralizing antibody response. Here we show that cytotoxic T-lymphocyte (CTL) escape was not detected in MHV-infected BALB/b mice (H-2 b haplotype), even though the same CD8 T-cell epitopes were recognized as in B6 mice. BALB/b mice had 25-fold more MHV-specific antibody-secreting cells in the central nervous system, the site of infection, than B6 mice, suggesting that local production of anti-MHV antibody contributed to this absence of CTL escape. Additionally, administration of anti-MHV neutralizing antibody to infected B6 mice suppressed the development of CTL escape mutants. These findings indicate a key role for the anti-MHV antibody response in suppressing virus replication, thereby minimizing the emergence and competitive advantage of CTL escape mutants.",,"CD8 antigen; neutralizing antibody; virus antibody; animal cell; animal experiment; animal model; animal tissue; antibody production; antibody response; article; cytotoxic T lymphocyte; demyelinating disease; haplotype; immunological tolerance; male; mouse; mouse strain; Murine hepatitis coronavirus; nonhuman; priority journal; spinal cord; virus inhibition; virus isolation; virus mutant; virus strain; Animals; Antibodies, Viral; Antibody-Producing Cells; B-Lymphocytes; Brain; Demyelinating Diseases; Immunization, Passive; Mice; Mice, Inbred BALB C; Murine hepatitis virus; Spleen; T-Lymphocytes, Cytotoxic","Banner, L., Keck, J.G., Lai, M.M.C., A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus (1990) Virology, 175, pp. 548-555; Bergmann, C., McMillan, M., Stohlman, S.A., Characterization of the Ld-restricted cytotoxic T-lymphocyte epitope in the mouse hepatitis virus nucleocapsid protein (1993) J. 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Med., 5, pp. 723-725; Erickson, A.L., Kimura, Y., Igarashi, S., Eichelberger, J., Houghton, M., Sidney, J., McKinney, D., Walker, C.M., The outcome of hepatitis C virus infection is predicted by escape mutations in epitopes targeted by cytotoxic T lymphocytes (2001) Immunity, 15, pp. 883-895; Heyman, B., Regulation of antibody responses via antibodies, complement, and Fc receptors (2000) Annu. Rev. Immunol., 18, pp. 709-737; Jacobsen, G., Perlman, S., Localization of virus and antibody response in mice infected persistently with MHV-JHM (1990) Adv. Exp. Med. Biol., 276, pp. 573-578; Karlsson, M.C., Wernersson, S., Diaz de Stahl, T., Gustavsson, S., Heyman, B., Efficient IgG-mediated suppression of primary antibody responses in Fcgamma receptor-deficient mice (1999) Proc. Natl. Acad. Sci. 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Academic Press, San Diego, Calif; Pewe, L., Wu, G., Barnett, E.M., Castro, R., Perlman, S., Cytotoxic T-cell-resistant variants are selected in a virus-induced demyelinating disease (1996) Immunity, 5, pp. 253-262; Pewe, L., Xue, S., Perlman, S., Cytotoxic T-cell-resistant variants arise at early times after infection in C57BL/6 but not in SCID mice infected with a neurotropic coronavirus (1997) J. Virol., 71, pp. 7640-7647; Pircher, H., Moskophidis, D., Rohrer, U., Burki, K., Hengartner, H., Zinkernagel, R., Viral escape by selection of cytotoxic T-cell-resistant virus variants in vivo (1990) Nature, 346, pp. 629-633; Price, G.E., Ou, R., Jiang, H., Huang, L., Moskophidis, D., Viral escape by selection of cytotoxic T-cell-resistant variants in influenza A virus pneumonia (2000) J. Exp. Med., 191, pp. 1853-1867; Ramakrishna, C., Stohlman, S.A., Atkinson, R.D., Shlomchik, M.J., Bergmann, C.C., Mechanisms of central nervous system viral persistence: The critical role of antibody and B cells (2002) J. Immunol., 168, pp. 1204-1211; Schwender, S., Imrich, H., Dorries, R., The pathogenic role of virus-specific antibody-secreting cells in the central nervous system of rats with different susceptibility to coronavirus-induced demyelinating encephalitis (1991) Immunology, 74, pp. 533-538; Shinall, S.M., Gonzalez-Fernandez, M., Noelle, R.J., Waldschmidt, T.J., Identification of murine germinal center B-cell subsets defined by the expression of surface isotypes and differentiation antigens (2000) J. Immunol., 164, pp. 5729-5738; Stohlman, S.A., Bergmann, C.C., Perlman, S., Mouse hepatitis virus (1998) Persistent Viral Infections, pp. 537-557. , R. Ahmed and I. Chen (ed.). John Wiley & Sons, New York, N.Y; Street, N., Mosmann, T.R., Functional diversity of T lymphocytes due to secretion of different cytokine patterns (1991) FASEB J., 5, pp. 171-177; Sun, N., Perlman, S., Spread of a neurotropic coronavirus to spinal cord white matter via neurons and astrocytes (1995) J. Virol., 69, pp. 633-641; Tao, T.W., Uhr, J., Capacity of pepsin-digested antibody to inhibit antibody formation (1966) Nature, 212, pp. 208-209; Tschen, S.I., Bergmann, C.C., Ramakrishna, C., Morales, S., Atkinson, R., Stohlman, S.A., Recruitment kinetics and composition of anti-body-secreting cells within the central nervous system following viral encephalomyelitis (2002) J. Immunol., 168, pp. 2922-2929; Tyor, W.R., Griffin, D.E., Virus specificity and isotype expression of intraparenchymal antibody-secreting cells during Sindbis virus encephalitis in mice (1993) J. Neuroimmunol., 48, pp. 37-44","Perlman, S.; Department of Pediatrics, University of Iowa, 2042 Medical Laboratories, Iowa City, IA 52242, United States; email: Stanley-Perlman@uiowa.edu",,,0022538X,,JOVIA,"14581523","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0242363263
"Bastone P., Truyen U., Löchelt M.","56571579500;35300805300;7003575587;","Potential of Zoonotic Transmission of Non-Primate Foamy Viruses to Humans",2003,"Journal of Veterinary Medicine Series B: Infectious Diseases and Veterinary Public Health","50","9",,"417","423",,18,"10.1046/j.0931-1793.2003.00704.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344549648&doi=10.1046%2fj.0931-1793.2003.00704.x&partnerID=40&md5=a3297322cb9e6f08b0f4b173ce3184d8","Abt. Genomveranderung Carcinogenese, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, Heidelberg, Germany; Inst. Tierhygiene Offentliches V., Universität Leipzig, Leipzig, Germany; Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Heidelberg, Germany","Bastone, P., Abt. Genomveranderung Carcinogenese, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, Heidelberg, Germany, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Heidelberg, Germany; Truyen, U., Inst. Tierhygiene Offentliches V., Universität Leipzig, Leipzig, Germany, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Heidelberg, Germany; Löchelt, M., Abt. Genomveranderung Carcinogenese, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, Heidelberg, Germany, Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Heidelberg, Germany","The zoonotic introduction of an animal pathogen into the human population and the subsequent extension or alteration of its host range leading to the successful maintenance of the corresponding pathogen by human-to-human transmission pose a serious risk for world-wide health care. Such a scenario occurred for instance by the introduction of simian immunodeficiency viruses into the human population resulting in the human immunodeficiency viruses (HIV) and the subsequent AIDS pandemic or the proposed recent host range switch of the SARS coronavirus from a presently unknown animal species to humans. The occurrence of zoonotic transmissions of animal viruses to humans is a permanent threat to human health and is even increased by changes in the human lifestyle. In this review, the potential of the zoonotic transmission of bovine, feline and equine foamy retroviruses will be discussed in the light of well-documented cases of zoonotic transmissions of different simian foamy viruses to humans.",,"animal; cat; cattle; disease transmission; horse; human; pathogenicity; Retrovirus infection; short survey; Spuma virus; virology; zoonosis; Animals; Cats; Cattle; Horses; Humans; Retroviridae Infections; Spumavirus; Zoonoses; Animalia; Bos taurus; Bovinae; Coronavirus; Equidae; Equus caballus; Felidae; Felis catus; Foamy retrovirus; Human immunodeficiency virus; Human spumaretrovirus; Primates; SARS coronavirus; Simiae; Simian foamy virus; Simian immunodeficiency virus; Spumavirus; unidentified retrovirus","Achong, B.G., Mansell, P.W., Epstein, M.A., Clifford, P., An unusual virus in cultures from a human nasopharyngeal carcinoma (1971) J. Natl. Cancer Inst., 46, pp. 299-307; Aguzzi, A., The foamy virus family: Molecular biology, epidemiology and neuropathology (1993) Biochim. Biophys. Acta, 1155, pp. 1-24; Ali, M., Taylor, G.P., Pitman, R.J., Parker, D., Rethwilm, A., Cheingsong-Popov, R., Weber, J.N., McClure, M.O., No evidence of antibody to human foamy virus in widespread human populations (1996) AIDS Res. Hum. 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Virol., 75, pp. 7184-7187; Zemba, M., Wilk, T., Rutten, T., Wagner, A., Flügel, R.M., Löchelt, M., The carboxy-terminal p3Gag domain of the human foamy virus Gag precursor is required for efficient virus infectivity (1998) Virology, 247, pp. 7-13","Löchelt, M.; Forschungsschwerpunkt Infektion K., Deutsches Krebsforschungszentrum, Heidelberg, Germany; email: m.loechelt@dkfz-heidelberg.de",,,09311793,,JVMBE,"14633194","English","J. Vet. Med. Ser. B Infect. Dis. Vet. Public Health",Short Survey,"Final",,Scopus,2-s2.0-0344549648
"Yam L.Y.C., Chen R.C., Zhong N.S.","7102764741;57200034537;7102137996;","SARS: Ventilatory and intensive care",2003,"Respirology","8",,,"S31","S35",,9,"10.1046/j.1440-1843.2003.00521.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347624087&doi=10.1046%2fj.1440-1843.2003.00521.x&partnerID=40&md5=0af574ee77e8d0308ea5e610ae3a4227","Department of Medicine, Pamela Youde Nethersole E. Hospital, Chai Wan, Hong Kong SAR, Hong Kong; Guangzhou Resp. Dis. Res. Institute, Guangzhou, China","Yam, L.Y.C., Department of Medicine, Pamela Youde Nethersole E. Hospital, Chai Wan, Hong Kong SAR, Hong Kong; Chen, R.C., Guangzhou Resp. Dis. Res. Institute, Guangzhou, China; Zhong, N.S., Guangzhou Resp. Dis. Res. Institute, Guangzhou, China","Severe acute respiratory syndrome (SARS) is an emerging infection caused by a novel coronavirus. It is characterised by a highly infectious syndrome of fever and respiratory symptoms, and is usually associated with bilateral lung infiltrates. The clinical syndrome of SARS often progresses to varying degrees of respiratory failure, with about 20% of patients requiring intensive care. Despite concern about potential aerosol generation, non-invasive ventilation (NIV) has been reported to be efficacious in the treatment of SARS-related ARF without posing infection risks to health care workers (HCW). Spontaneous pneumomediastinum and pneumothorax in SARS is common. The incidence of NIV-associated barotrauma ranged from 6.6% to 15%. Patients who fail to tolerate NIV or fail NIV with progressive dyspnoea, tachypnoea and hypoxaemia should be intubated and mechanically ventilated. Mortality rates in intensive care units for SARS patients were high: 34-53% at 28 days, when some patients were still being ventilated. Strict adherence to infection control measures including isolation, use of appropriate personal protective equipment and negative pressure environment had been reported to eliminate cross-infection to HCW.","Acute respiratory distress syndrome; Infection control; Mechanical ventilation; Non-invasive ventilation; Severe acute respiratory syndrome","artificial ventilation; barotrauma; clinical feature; cross infection; disease course; dyspnea; fever; health care personnel; hypoxemia; infection control; infection risk; intensive care; lung infiltrate; mortality; patient care; pneumomediastinum; pneumothorax; priority journal; protective equipment; respiratory failure; respiratory tract intubation; review; SARS coronavirus; severe acute respiratory syndrome; tachypnea; Humans; Infection Control; Intensive Care; Intensive Care Units; Positive-Pressure Respiration; Severe Acute Respiratory Syndrome","Fowler, R.A., Lapinsky, S.E., Hallet, D., Critically ill patients with severe acute respiratory distress syndrome (2003) JAMA, 290, pp. 367-373; Lew, T.W.K., Kwek, T., Tai, D., Acute respiratory distress syndrome in critically ill patients with severe acute respiratory syndrome (2003) JAMA, 290, pp. 374-380; Lee, N., Hui, D., Wu, A., Chan, P., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. 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March 9; So, L.K.Y., Lau, A.C.W., Yam, L.Y.C., Cheung, M.T., Poon, E., Yung, R.Y.H., Development of a standard treatment protocol for severe acute respiratory syndrome (2003) Lancet, 361, pp. 1615-1617; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus associated SARS pneumonia: A prospective study (2003) Lancet, 316, pp. 1767-1721; Luo, D., Qian, S.C., SARS treatment: Experience from a team in Guangdong, China (2003) Chin. Med. J., 116, pp. 838-839; Xue, X.Y., Gao, Z.C., Xu, Y., Clinical analysis of 45 patients with severe acute respiratory distress syndrome (2003) Chin. Med. J., 116, pp. 819-822; Zhao, Z., Zhang, F., Xu, M., Description and clinical treatment of an early outbreak of severe acute respiratory syndrome (SARS) in Guangzhou, PR China (2003) J. Med. Microb., 52, pp. 715-720; Wu, W., Wang, J.F., Liu, P.M., A hospital outbreak of severe acute respiratory syndrome in Guangzhou, China (2003) Chin. Med. 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Dis., 26, pp. 329-333; Li, Y.M., Chen, S.B., Xu, Y.D., Mechanical ventilation strategies in critical SARS patients (2003) Chin. J. Emerg. Med., 12, pp. 369-372; Lapinsky, S.E., Hawryluck, L., ICU management of severe acute respiratory syndrome (2003) Intensive Care Med., 29, pp. 870-875; (2003) Interim Domestic Infection Control Precautions for Aerosol-Generating Procedures on Patients with Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/aerosolinfectioncontrol.htm, Cited 20 May; Wong, T.W., Li, C.K., Tam, W., A cluster or severe acute respiratory syndrome among medical students exposed to a single patient in Hong Kong (2003) Emerg. Infec. Dis.; (1994) Guidelines for Preventing the Transmission of Mycobacterium Tuberculosis in Health Care Facilities, , Centres for Disease Control and Prevention, Atlanta","Yam, L.Y.C.; Department of Medicine, Pamela Youde Nethersole E. Hospital, Chai Wan, Hong Kong SAR, Hong Kong; email: lycyam@ha.org.hk",,,13237799,,RSPIF,"15018131","English","Respirology",Review,"Final",,Scopus,2-s2.0-0347624087
"Groneberg D.A., Zhang L., Welte T., Zabel P., Chung K.F.","7004564948;14629733200;7007156174;7004888257;35403525000;","Severe acute respiratory syndrome: Global initiatives for disease diagnosis",2003,"QJM - Monthly Journal of the Association of Physicians","96","11",,"845","852",,28,"10.1093/qjmed/hcg146","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242720705&doi=10.1093%2fqjmed%2fhcg146&partnerID=40&md5=a124e49a649d45d860701616febcaf9d","Dept. of Med./Pediatric Pneumology, Charité School of Medicine, Humboldt-University, Augustenberger Platz 1, 13353 Berlin, Germany; Fujian University of Medicine, Fujian, China; Div. of Pulmon./Intensive Care Med., Department of Medicine, University of Magdeburg, Magdeburg, Germany; Div. of Clin. Infectiology/Immunol., Department of Medicine, Research Center Borstel, Borstel, Germany; Division of Thoracic Medicine, Department of Medicine, University of Lübeck, Lübeck, Germany; Department of Thoracic Medicine, National Heart and Lung Institute, Imperial College London, London, United Kingdom","Groneberg, D.A., Dept. of Med./Pediatric Pneumology, Charité School of Medicine, Humboldt-University, Augustenberger Platz 1, 13353 Berlin, Germany; Zhang, L., Fujian University of Medicine, Fujian, China; Welte, T., Div. of Pulmon./Intensive Care Med., Department of Medicine, University of Magdeburg, Magdeburg, Germany; Zabel, P., Div. of Clin. Infectiology/Immunol., Department of Medicine, Research Center Borstel, Borstel, Germany, Division of Thoracic Medicine, Department of Medicine, University of Lübeck, Lübeck, Germany; Chung, K.F., Department of Thoracic Medicine, National Heart and Lung Institute, Imperial College London, London, United Kingdom","We present a retrospective analysis of the available articles on severe acute respiratory syndrome (SARS) published since the outbreak of the disease. SARS is a new infectious disease caused by a novel coronavirus. Originating in Guangdong, Southern China, at the end of 2002, it has spread to regions all over the world, affecting more than 8000 people. With high morbidity and mortality, SARS is an important respiratory disease which may be encountered world-wide. The causative virus was identified by a WHO-led network of laboratories, which identified the genome sequence and developed the first molecular assays for diagnosis. For the respiratory physician, detecting SARS in its earliest stages, identifying pathways of transmission, and implementing preventive and therapeutic strategies are all important. The WHO and the CDC have published helpful definitions of 'suspected' and 'probable' cases. However, the symptoms of the disease may change, and laboratory tests and definitions are still limited. Even in a situation of no new cases of infection, SARS remains a major respiratory health hazard. As with influenza virus outbreaks, new epidemics may arise at the end of each year.",,"antibiotic agent; salbutamol; article; bacterial pneumonia; China; Coronavirus; diagnostic test; early diagnosis; epidemic; gene sequence; health hazard; histopathology; human; infection control; infection prevention; Influenza virus; laboratory test; medical literature; morbidity; mortality; priority journal; respiratory tract infection; retrospective study; SARS coronavirus; severe acute respiratory syndrome; symptomatology; thorax radiography; virus identification; virus transmission; world health organization; Antibodies, Viral; Coronavirus; Disease Outbreaks; Humans; Lung; Severe Acute Respiratory Syndrome; Time Factors; Viral Load","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Gunther, S., Preiser, W., van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Reilley, B., Van Herp, M., Sermand, D., Dentico, N., SARS and Carlo Urbani (2003) N. Engl. J. Med., 348, pp. 1951-1952; A multicentre collaboration to investigate the cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1730-1733; Oxford, J.S., Bossuyt, S., Lambkin, R., A new infectious disease challenge: Urbani severe acute respiratory syndrome (SARS) associated coronavirus (2003) Immunology, 109, pp. 326-328; Rosling, L., Rosling, M., Pneumonia causes panic in Guangdong province (2003) Br. Med. J., 326, p. 416; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., Sung, J.J., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Tsang, K.W., Ho, P.L., Ooi, G.C., Yee, W.K., Wang, T., Chan-Yeung, M., Lam, W.K., Lai, K.N., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1977-1985; Vu, T.H., Cabau, J.F., Nguyen, N.T., Lenoir, M., SARS in Northern Vietnam (2003) N. Engl. J. Med., 348, p. 2035; Yeoh, S.C., Lee, E., Lee, B.W., Goh, D.L., Severe acute respiratory syndrome: Private hospital in Singapore took effective control measures (2003) Br. Med. J., 326, p. 1394; Tan, Y.M., Chow, P.K., Soo, K.C., Severe acute respiratory syndrome: Clinical outcome after inpatient outbreak of SARS in Singapore (2003) Br. Med. J., 326, p. 1394; Wilder-Smith, A., Paton, N.I., Severe acute respiratory syndrome: Imported cases of severe acute respiratory syndrome to Singapore had impact on national epidemic (2003) Br. Med. J., 326, pp. 1393-1394; Spurgeon, D., Canada reports more than 300 suspected cases of SARS (2003) Br. Med. J., 326, p. 897; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Rachlis, A.R., Rose, D.B., Dwosh, H.A., Walmsley, S.L., Detsky, A.S., Clinical features and short-term outcomes of 144 patients with SARS in the greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McCeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348, pp. 1995-2005; Tomlinson, B., Cockram, C., SARS: Experience at Prince of Wales Hospital, Hong Kong (2003) Lancet, 361, pp. 1486-1487; Chan-Yeung, M., Yu, W.C., Outbreak of severe acute respiratory syndrome in Hong Kong Special Administrative Region: Case report (2003) Br. Med. J., 326, pp. 850-852; Lew, T.W., Kwek, T.K., Tai, D., Earnest, A., Loo, S., Singh, K., Kwan, K.M., Goh, S.K., Acute respiratory distress syndrome in critically ill patients with severe acute respiratory syndrome (2003) JAMA, 290, pp. 374-380; Chan, J.W., Ng, C.K., Chan, Y.H., Mok, T.Y., Lee, S., Chu, S.Y., Law, W.L., Li, P.C., Short term outcome and risk factors for adverse clinical outcomes in adults with severe acute respiratory syndrome (SARS) (2003) Thorax, 58, pp. 686-689; Fowler, R.A., Lapinsky, S.E., Hallett, D., Detsky, A.S., Sibbald, W.J., Slutsky, A.S., Stewart, T.E., Critically ill patients with severe acute respiratory syndrome (2003) JAMA, 290, pp. 367-373; Cavanagh, D., Nidovirales: A new order comprising Coronaviridae and Arteriviridae (1997) Arch. Virol., 142, pp. 629-633; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Siddell, S., Wege, H., ter Meulen, V., The structure and replication of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 131-163; Wege, H., Siddell, S., ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Kuiken, T., Fouchier, R.A., Schutten, M., Rimmelzwaan, G.F., van Amerongen, G., van Riel, D., Laman, J.D., Osterhaus, A.D., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Donnelly, C.A., Ghani, A.C., Leung, G.M., Hedley, A.J., Fraser, C., Riley, S., Abu-Raddad, L.J., Anderson, R.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.I., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Hon, K.L., Leung, C.W., Cheng, W.T., Chan, P.K., Chu, W.C., Kwan, Y.W., Li, A.M., Fok, T.F., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Goh, J.S., Tsou, I.Y., Kaw, G.J., Severe acute respiratory syndrome (SARS): Imaging findings during the acute and recovery phases of disease (2003) J. Thorac. Imaging, 18, pp. 195-199; Muller, N.L., Ooi, G.C., Khong, P.L., Nicolaou, S., Severe Acute Respiratory Syndrome: Radiographic and CT Findings (2003) Am. J. Roentgenol., 181, pp. 3-8; Wu, E.B., Sung, J.J., Haemorrhagic-fever-like changes and normal chest radiograph in a doctor with SARS (2003) Lancet, 361, pp. 1520-1521; Wong, K.T., Antonio, G.E., Hui, D.S., Lee, N., Yuen, E.H., Wu, A., Leung, C.B., Ahuja, A.T., Severe Acute Respiratory Syndrome: Radiographic Appearances and Pattern of Progression in 138 Patients (2003) Radiology, 228, pp. 401-406; Wong, K.T., Antonio, G.E., Hui, D.S., Lee, N., Yuen, E.H., Wu, A., Leung, C.B., Ahuja, A.T., Thin-Section CT of Severe Acute Respiratory Syndrome: Evaluation of 73 Patients Exposed to or with the Disease (2003) Radiology, 228, pp. 395-400; Nicholls, J.M., Poon, L.L., Lee, K.C., Ng, W.F., Lai, S.T., Leung, C.Y., Chu, C.M., Peiris, J.S., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Franks, T.J., Chong, P.Y., Chui, P., Galvin, J.R., Lourens, R.M., Reid, A.H., Selbs, E., Travis, W.D., Lung pathology of severe acute respiratory syndrome (SARS): A study of 8 autopsy cases from Singapore (2003) Hum. Pathol., 34, p. 729; Ding, Y., Wang, H., Shen, H., Li, Z., Geng, J., Han, H., Cai, J., Yao, K., The clinical pathology of severe acute respiratory syndrome (SARS): A report from China (2003) J. Pathol., 200, pp. 282-289; Updated Interim U.S. Case Definition for Severe Acute Respiratory Syndrome (SARS) (2003), http://www.cdc.gov/ncidod/sars/casedefinition.htm, Accessed August 20; (2003), http://www.who.int/csr/sars/casedefinition/en, Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS). Accessed August 20; Wang, H., Ding, Y., Li, X., Yang, L., Zhang, W., Kang, W., Fatal aspergillosis in a patient with SARS who was treated with corticosteroids (2003) N. Engl. J. Med., 349, pp. 507-508","Groneberg, D.A.; Dept. of Med./Pediatric Pneumology, Biomedical Research Center OR-1, Augustenberger Platz 1, 13353 Berlin, Germany; email: david.groneberg@charite.de",,,14602725,,QMJPF,"14566040","English","QJM Mon. J. Assoc. Phys.",Article,"Final",Open Access,Scopus,2-s2.0-0242720705
"Warner F.J., Guy J.L., Lambert D.W., Hooper N.M., Turner A.J.","7005760146;8081356600;36983440100;7101602467;7401819735;","Angiotensin converting enzyme-2 (ACE2) and its possible roles in hypertension, diabetes and cardiac function",2003,"Letters in Peptide Science","10","5-6",,"377","385",,2,"10.1007/BF02442567","https://www.scopus.com/inward/record.uri?eid=2-s2.0-15044360690&doi=10.1007%2fBF02442567&partnerID=40&md5=f28ab889109a8d5ddf192a76f22f654b","Baker Heart Research Institute, Peptide Biology, Melbourne, Vic. 3004, Australia; Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom","Warner, F.J., Baker Heart Research Institute, Peptide Biology, Melbourne, Vic. 3004, Australia, Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom; Guy, J.L., Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom; Lambert, D.W., Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom; Hooper, N.M., Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom; Turner, A.J., Proteolysis Research Group, Sch. of Biochem. and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom","Angiotensin converting enzyme-2 (ACE2) is a recently described homologue of the vasoactive peptidase, angiotensin converting enzyme (ACE). Like ACE, ACE2 is an integral (type I) membrane zinc metallopeptidase, which exists as an ectoenzyme. ACE2 is less widely distributed than ACE in the body, being expressed at highest concentrations in the heart, kidney and testis. ACE2 also differs from ACE in its substrate specificity, functioning exclusively as a carboxypeptidase rather than a peptidyl dipeptidase. A key role for ACE2 appears to be emerging in the conversion of angiotensin II to angiotensin (1-7), allowing it to act as a counter-balance to the actions of ACE. ACE2 has been localised to the endothelial and epithelial cells of the heart and kidney where it may have a role at the cell surface in hydrolysing bioactive peptides such as angiotensin II present in the circulation. A role for ACE2 in the metabolism of other biologically active peptides also needs to be considered. ACE2 also serendipitously appears to act as a receptor for the severe acute respiratory syndrome (SARS) coronavirus. Studies using ace2-/- mice, and other emerging studies in vivo and in vitro, have revealed that ACE2 has important functions in cardiac regulation and diabetes. Together with its role as a SARS receptor, ACE2 is therefore likely to be an important therapeutic target in a diverse range of disease states. © 2004 Kluwer Academic Publishers.","ACE2; Angiotensin-converting enzyme; Apelin; Bradykinin; diabetes; Heart; Hypertension; Kidney; Renin-angiotensin; SARS","angiotensin; angiotensin receptor antagonist; angiotensin[1-7]; captopril; carboxypeptidase; dipeptidyl carboxypeptidase; dipeptidyl carboxypeptidase 2; dipeptidyl carboxypeptidase inhibitor; dx 512; enalapril; lisinopril; metalloproteinase; unclassified drug; virus receptor; article; cell surface; diabetes mellitus; dose response; drug design; drug mechanism; drug potency; endothelium cell; enzyme localization; enzyme specificity; epithelium cell; heart failure; heart function; heart ventricle remodeling; human; hydrolysis; hypertension; kidney; nonhuman; protein expression; protein function; protein metabolism; regulatory mechanism; renin angiotensin aldosterone system; SARS coronavirus; testis; Coronavirus","Weir, M.R., (1999) Am. 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Renin Angiotensin Aldersterone Syst., 4, p. 186; Blaufarb, I.S., Sonnenblick, E.H., (1996) Am. J. Cardiol., 77, pp. 8C; Donoghue, M., Wakimoto, H., Maguire, C.T., Acton, S., Hales, P., Stagliano, N., Fairchild-Huntress, V., Breitbart, R.E., (2003) J. Mol. Cell. Cardiol., 35, p. 1043; Polontchouk, L., Ebelt, B., Jackels, M., Dhein, S., (2002) FASEB J., 16, p. 87; Benjafield, A.M., Wang, W.Y.S., Morris, B.J., (2004) B.J. Am. J. Hyper., 17, p. 624","Warner, F.J.; Baker Heart Research Institute, Peptide Biology, Melbourne, Vic. 3004, Australia; email: Fiona.Warner@baker.edu.au",,,09295666,,LPSCE,,"English","Lett. Pept. Sci.",Article,"Final",,Scopus,2-s2.0-15044360690
"Chen H.-C., Young Y.-H., Luo J.-P., Tsai H.-J., Ho S.-J., Yeh C.-H., Huang L.-C.","57207070373;7101887708;7404183007;57143433100;55248465400;7401672158;55660354800;","Initial Otolaryngological Manifestations of Severe Acute Respiratory Syndrome in Taiwan",2003,"Archives of Otolaryngology - Head and Neck Surgery","129","11",,"1157","1160",,2,"10.1001/archotol.129.11.1157","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242576336&doi=10.1001%2farchotol.129.11.1157&partnerID=40&md5=ccab2771e0f4882f1d2b49510caf06de","Department of Otolaryngology, Municipal Ho-Ping Hospital, Taipei, Taiwan; Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan; Department of Otolaryngology, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 1 Chang-Te St, Taipei, Taiwan","Chen, H.-C., Department of Otolaryngology, Municipal Ho-Ping Hospital, Taipei, Taiwan; Young, Y.-H., Department of Otolaryngology, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 1 Chang-Te St, Taipei, Taiwan; Luo, J.-P., Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan; Tsai, H.-J., Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan; Ho, S.-J., Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan; Yeh, C.-H., Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan; Huang, L.-C., Department of Medicine, Municipal Ho-Ping Hospital, Taipei, Taiwan","Objective: To provide a clue for screening severe acute respiratory syndrome (SARS), a highly transmissible disease with health care workers at particular risk, in the early stage from an otolaryngological perspective. Design: Prospective study. Setting: Community hospital. Patients: Between April 17 and April 26, 2003, 32 consecutive patients with SARS were encountered. Investigation consisted of local examination of ear, nose, and throat fields; palpation of the nuchal areas; and plain chest radiography. Analyses of throat swab samples using reverse transcription-polymerase chain reaction were conducted. Results: Clinical manifestations included fever in 31 patients (97%), followed by cough, dyspnea, chill, headache, sore throat, diarrhea, rhinorrhea, and otalgia. Neither the pharyngeal wall nor the tonsillar area demonstrated hyperemia. There was no lymphadenopathy in the neck. Plain chest radiographs revealed consolidation in 25 (78%) of 32 patients. Results of reverse transcription-polymerase chain reaction analysis targeting the novel coronavirus present in throat swab samples were positive in 19 (66%) of 29 patients tested. Twenty-eight patients required supplemental oxygen, and 14 patients were intubated with mechanical ventilation. Twenty-eight patients survived and 4 patients died. Conclusions: When presented with a patient with flulike symptoms such as fever and/or cough, but no pharyngeal hyperemia or neck lymphadenopathy, physicians should be alerted to the possibility of SARS. In contrast, evidence of inflammatory signs in the otolaryngological field may explain the flulike symptoms, and serve as a differential diagnostic tool between influenza and SARS.",,"adolescent; adult; aged; article; artificial ventilation; chill; clinical article; clinical feature; community hospital; controlled study; Coronavirus; coughing; death; diarrhea; dyspnea; female; fever; headache; health care personnel; human; hyperemia; infection risk; lymphadenopathy; male; mass screening; otalgia; otorhinolaryngology; outcomes research; oxygen supply; oxygen therapy; palpation; pharynx disease; respiratory tract intubation; reverse transcription polymerase chain reaction; rhinorrhea; severe acute respiratory syndrome; sore throat; survival rate; Taiwan; thorax radiography; throat culture; tonsil disease; virus pneumonia; Adolescent; Adult; Female; Humans; Influenza, Human; Male; Middle Aged; Prospective Studies; Severe Acute Respiratory Syndrome; Taiwan","(2003) Acute Respiratory Syndrome in China - Update 3: Disease Outbreak Reported, , http://www.who.int/csr/don/2003_2_20/en, Geneva, Switzerland: World Health Organization; (2003) Severe Acute Respiratory Syndrome (SARS), , http:/www.cdc.gov/ncidod/sars/, Atlanta, Ga: Centers for Disease Control and Prevention; Tsang, K.W., Ho, P.I., Oo, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Hsu, L.Y., Lee, C.C., Green, J.A., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9, pp. 713-717; Twu, S.J., Chen, T.J., Chen, C.J., Control measures for severe acute respiratory syndrome (SARS) in Taiwan (2003) Emerg Infect Dis, 9, pp. 718-720; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Dwosh, H.A., Hong, H.H.L., Austgarden, D., Herman, S., Schabas, R., Identification and containment of an outbreak of SARS in a community hospital (2003) CMAJ, 168, pp. 1415-1420; Donnelly, C.A., Ghani, A.C., Leung, G.M., Epidemiological determinants of spread of causal agent of severe acute respiratory syndrome in Hong Kong (2003) Lancet, 361, pp. 1761-1766; Hon, K.L.E., Leung, C.W., Cheng, W.F.T., Clinical presentation and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772","Young, Y.-H.; Department of Otolaryngology, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 1 Chang-Te St, Taipei, Taiwan; email: youngyh@ha.mc.ntu.edu.tw",,,08864470,,AONSE,"14623743","English","Arch. Otolaryngol. Head Neck Surg.",Article,"Final",Open Access,Scopus,2-s2.0-0242576336
"Chan-Yeung M., Xu R.-H.","54790582200;7402813893;","SARS: Epidemiology",2003,"Respirology","8",,,"S9","S14",,76,"10.1046/j.1440-1843.2003.00518.x","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345732174&doi=10.1046%2fj.1440-1843.2003.00518.x&partnerID=40&md5=237d70eef5153bf09044d8519f90999f","University of Hong Kong, Hong Kong, SAR, Hong Kong; Centre for Diseases Control, Guangzhou, China; University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, SAR, Hong Kong","Chan-Yeung, M., University of Hong Kong, Hong Kong, SAR, Hong Kong, University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, SAR, Hong Kong; Xu, R.-H., Centre for Diseases Control, Guangzhou, China","Severe acute respiratory syndrome (SARS) originated in Southern China in November 2002, and was brought to Hong Kong in February 2003. From Hong Kong, the disease spread rapidly worldwide but mostly to Asian countries. At the end of the epidemic in June, the global cumulative total was 8422 cases with 916 deaths (case fatality rate of 11%). People of all ages were affected, but predominantly females. Health care workers were at high risk and accounted for one-fifth of all cases. Risk factors for death included old age and comorbid illnesses, especially diabetes. The disease is caused by a novel coronavirus and is transmitted by droplets or direct inoculation from contact with infected surfaces. Contaminated sewage was found to be responsible for the outbreak in a housing estate in Hong Kong affecting over 300 residents. The mean incubation period was 6.4 days (range 2-10). The duration between onset of symptoms and hospitalisation was from 3 to 5 days. The relatively prolonged incubation period allowed asymptomatic air travellers to spread the disease globally. The number of individuals infected by each case has been estimated to be 2.7. Effective control of nosocomial transmission included early detection of disease, strict isolation of patients, practice of droplet and contact precautions and compliance with the use of personal protective equipment. Effective control of disease spread in the community included tracing and quarantine of contacts. Development of a validated diagnostic test and an effective vaccine as well as elimination of possible animal reservoirs are measures needed to prevent another epidemic.","Epidemiology; Fatality rate; Risk factors; Severe acute respiratory syndrome; Transmission","Asia; aviation; China; comorbidity; diabetes mellitus; diagnostic test; disease carrier; epidemic; health care personnel; Hong Kong; hospital infection; hospitalization; incubation time; infection control; mortality; priority journal; protective equipment; review; risk factor; SARS coronavirus; senescence; severe acute respiratory syndrome; virus transmission; Adolescent; Adult; Age Distribution; Aged; Asia; Australasia; Canada; Child; Child, Preschool; Communicable Disease Control; Disease Outbreaks; Humans; Infant; Infant, Newborn; Middle Aged; SARS Virus; Severe Acute Respiratory Syndrome","(2003) Acute Respiratory Syndrome in Hong Kong Special Administration of China/Vietnam, , http://www.who.int/csr/2003_03_12/en, Cited 12 March; Tsang, K.W., Ho, P.L., Ooi, G., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. Med. J., 348, pp. 1977-1985; (2003) Severe Acute Respiratory Syndrome (SARS) - Multi-country Outbreak, , http://www.who.int/csr/2003-03-15/en, Cited 15 March; (2003) Severe Acute Respiratory Syndrome (SARS). Status of the Outbreak and Lessons for the Immediate Future, , http://www.who.int/csr/media/sars_who.pdf, Communicable Disease Surveillance and Response 20 May; (2003) Summary of Probable SARS Cases with Onset of Illness from 1 November 2002 to 31 July 2003, , http://www.who.int/csr/2003_10_15/en, Cited 15 July; (2003) Severe Acute Respiratory Syndrome (SARS) Multi-country Outbreak - Update 10, , http://www.who.int/csr/2003_03_26/en, Cited 26 March; World Health Organization (2003) Severe Acute Respiratory Syndrome (SARS) Multi-country Outbreak - Update 34, , http://www.who.int/csr/2003_04_20/en, Cited 20 April; (2003) Update 87 - World Health Organization Changed its Remaining Travel Recommendation-for Beijing, China, , http://www.who.int/csr/2003_06_24/en, Cited 15 March; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Eng. J. Med., 358, pp. 1986-1994; (2003) Main Findings of an Investigation into the Outbreak of Severe Acute Respiratory Syndrome at Amoy Gardens, , http://www.info.gov.hk/dh, Cited 17 April; (2003) Severe Acute Respiratory Syndrome (SARS) Multi-country Outbreak, , http://www.who.int/csr/2003_04_12/en, Cited 12 April; (2003) Update 70 - Singapore Removed from List of Areas with Local SARS Transmission, , http://www.who.int/csr/2003_05_30/en, Cited 30 May; (2003) Update 93 - Toronto Removed from List of Areas with Recent Local Transmission, , http://www.who.int/csr/2003_07_02/en, Cited April 17; (2003) Update 96 - Taiwan, China SARS. Transmission Interrupted in Last Outbreak Area, , http://www.who.int/csr/2003_07_02/en, Cited 2 July; (2003) SARS Daily Updated Graphs, , http://www.hku.hk/ctc/sars_hk_23.htm, Cited 20 June; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Morbidity and Mortality Weekly Report. Severe acute respiratory syndrome-Singapore (2003) JAMA, 289, pp. 3231-3234; He, J.-F., Xu, R.-H., Yu, D.-W., Severe acute respiratory syndrome in Guangdong Province of China: Epidemiology and control measures (2003) Chin. J. Prev. Med., 37, pp. 227-232; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; (2003) CDC Laboratory Sequences Genome of New Coronavirus, , http://www.cdc.gov/od/oc/media/pressrel/r030414.htm, Cited April 16; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Ruan, Y.J.L.W., Chia, A.E., Ling, Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; (2003) Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/2003_03_24/en, [Cited 24 March] (civet cat); Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; (2003) First Data on Stability and Resistance of SARS Coronavirus Compiled by Members of WHP Laboratory Network, , http://www.who.int/csr/sars/survival_2003_05_04/en/index.html, Cited 4 May; Donnelly, C.A., Ghani, A.C., Leung, G.M., (2003) Epidemiological Determinants of Spread of Causal Agent of Severe Acute Respiratory Syndrome in Hong Kong, , http://image.thelancet.com/extras/03art4453web.pdf, Cited 26 September; Ho, A., Sung, J.J.Y., Chan-Yeung, M., An outbreak of Severe Acute Respiratory Syndrome (SARS) among hospital workers in a Community Hospital in Hong Kong (2003) Ann. Int. Med., 139, pp. 564-567; Riley, S., Fraser, C., Donnelly, C.A., Transmission Dynamics of the etiological agent of SARS in Hong Kong: Impact of public health interventions (2003) Sciencexpress, , http://www.sciencexpress.org/23May2003/Page1/10.1126/science, Cited 23 May","Chan-Yeung, M.; University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, SAR, Hong Kong; email: mmwchan@hkucc.hku.hk",,,13237799,,RSPIF,"15018127","English","Respirology",Review,"Final",,Scopus,2-s2.0-0345732174
"Paltrinieri S., Ceciliani F., Gabanti E., Sironi G., Giordano A., Addie D.","7003879241;6603889706;16635823800;7006084402;7201681218;7003910352;","Expression patterns in feline blood and tissues of α1-acid glycoprotein (AGP) and of an AGP-related protein (AGPrP)",2003,"Comparative Clinical Pathology","12","3",,"140","146",,3,"10.1007/s00580-003-0489-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347588279&doi=10.1007%2fs00580-003-0489-8&partnerID=40&md5=e02f87a70def88ea1e614d3814a233e1","Università di Milano, Milan, Italy; Fondazione Inst. Neurol. C. Mondino, Pavia, Italy; University of Glasgow, Glasgow, United Kingdom; Dipartimento di Patologia Animale, Igiene e Sanita Pubblica Veterinaria, Università di Milano, Via Celoria 10, 120133 Milano, Italy","Paltrinieri, S., Università di Milano, Milan, Italy, Dipartimento di Patologia Animale, Igiene e Sanita Pubblica Veterinaria, Università di Milano, Via Celoria 10, 120133 Milano, Italy; Ceciliani, F., Università di Milano, Milan, Italy; Gabanti, E., Fondazione Inst. Neurol. C. Mondino, Pavia, Italy; Sironi, G., Università di Milano, Milan, Italy; Giordano, A., Università di Milano, Milan, Italy; Addie, D., University of Glasgow, Glasgow, United Kingdom","α1-Acid glycoprotein (AGP) is an acute-phase protein (APP) that modulates immune responses, probably - at least in humans - owing to the modification of its glycosylation pattern. On this perspective, feline AGP can be a useful comparative model, as it has different concentrations in cats susceptible or resistant to some disease. As a preliminary approach to the study of feline AGP (fAGP) we have purified this protein from feline serum by HPLC using human AGP (hAGP) as a model. Immunoblotting with a polyclonal antibody against fAGP and with a monoclonal antibody against hAGP was performed on serum from healthy cats, from cats exposed to feline coronavirus (FCoV) infection and from cats with purulent inflammations, such as feline infectious peritonitis (FIP), feline immunodeficiency virus (FIV) and feline leukemia virus (FeLV). Immunohistochemistry on tissues from healthy cats and from cats with different diseases (FIP, FIV, FeLV, locally extensive inflammation) was also performed with the same antibodies. Both hAGP and fAGP have been purified to homogenity as determined by SDS-PAGE. fAGP did not react with the anti-hAGP antibody which, in contrast, detected in feline serum a low MW protein that we called fAGP-related protein (fAGPrP). This protein was underexpressed in cats with FeLV and FIP. Both fAGP and fAGPrP were immunohistochemically detected in plasma and hepatocytes with a stronger intensity in cats with FIP and some inflammatory conditions. Moreover, fAGPrP was detected in the cytoplasm of tissue cells, most likely identifiable with plasma cells. These cells were rarely detectable in cats with FIV and FeLV, and numerous in cats with FIP and with locally extensive inflammation. In conclusion, purified fAGP has physicochemical characteristics similar to those of hAGP, but does not cross-react with anti-hAGP antibodies. In contrast, the anti-hAGP detected an AGP-related protein whose blood concentration and tissue distribution was not related to that of fAGP. Moreover, both fAGP and fAGPrP were differently expressed in cats with pathologic conditions compared to controls. Further study of these proteins by analysing their structural characteristics is required.","α1-acid glycoprotein (AGP); AGP-related protein (AGPrP); FeLV; FIP; FIV; Inflammation","acute phase protein; monoclonal antibody; orosomucoid; orosomucoid related protein; polyclonal antibody; unclassified drug; animal experiment; animal model; animal tissue; article; cat disease; controlled study; Coronavirus; cross reaction; cytoplasm; disease predisposition; disease resistance; Feline immunodeficiency virus; Feline leukemia virus; high performance liquid chromatography; human; immunoblotting; immunohistochemistry; immunomodulation; inflammatory disease; liver cell; nonhuman; physical chemistry; plasma cell; polyacrylamide gel electrophoresis; protein analysis; protein blood level; protein expression; protein glycosylation; protein purification; protein structure; tissue distribution; virus infection","Biou, D., Bauvy, C., N'Guyen, H., Alterations of the glycan moiety of human alpha-1-acid glycoprotein in late-term pregnancy (1991) Clin. Chim. Acta, 204, pp. 1-12; Bories, P.N., Feger, J., Benbernou, N., Prevalence of tri- and tetraantennary glycans of human alpha-1-acid glycoprotein in release of macrophage inhibitor of interleukin-1 activity (1990) Inflammation, 14, pp. 315-323; Cattoretti, G., Pileri, S., Parravicini, C., Antigen unmasking on formalin-fixed, paraffin-embedded tissue sections (1993) J. Pathol., 171, pp. 83-98; Ceciliani, F., Giordano, A., Spagnolo, V., The systemic reaction during inflammation: The acute phase proteins (2002) Protein Peptide Lett., 3, pp. 211-223; Costello, M., Fiedel, B.A., Gewurz, H., Inhibition of platelet aggregation by native and desialised alpha-1-acid glycoprotein (1979) Nature, 281, pp. 677-678; Duthie, S., Eckersall, P.D., Addie, D.D., Value of alpha-1-acid glycoprotein in the diagnosis of feline infectious peritonitis (1997) Vet. Rec., 141, pp. 299-303; Duthie, S., Eckersall, P.D., Addie, D.D., AGP Measurement as an aid to the diagnosis of feline infectious peritonitis (2002) Proc. 2nd International Feline Coronavirus/Feline Infectious Peritonitis Symposium, p. 15; Fournier, T., Medjoubi-N, N., Porquet, D., Alpha-1-acid glycoprotein (2000) Biochim. Biophys. Acta, pp. 157-171. , 1482; Giordano, A., Spagnolo, V., Colombo, A., Changes in some acute phase proteins and in imunnoglobulin concentrations in cats affected by feline infectious peritonitis or exposed to feline coronavirus infection (2003) Vet. J., , (in press); Hochepied, T., Berger, F.G., Baumann, H., Alpha-1-acid glycoprotein: An acute phase protein with inflammatory and immunomodulating properties (2003) Cytokine Growth Factor Rev., 14, pp. 25-34; Hsu, S.M., Raine, L., Farger, H., Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures (1980) J. Histochem. Cytochem., 29, pp. 577-580; Kaneko, J.J., Serum protein and the dysproteinemias (1997) Clinical Biochemistry of Domestic Animals, pp. 117-138. , Kaneko JJ, Harvey JW, Bruss ML, eds. San Diego, Academic Press; Kim, Y.J., Varki, A., Perspectives on the significance of altered glycosylation of glycoproteins in cancer (1997) Glycocon. J., 14, pp. 569-576; Laemmli, U.K., Cleavage of structural proteins during assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685; Lögdberg, L., Wester, L., Immunocalins: A lipocalin subfamily that modulates immune and inflammatory responses (2000) Biochim. Biophys. Acta, pp. 284-297. , 1482; Mackiewicz, A., Mackiewicz, K., Glycoforms of serum alpha-1-acid glycoprotein as markers of inflammation and cancer (1995) Glycocon. J., 12, pp. 241-247; Pedersen, N.C., An overview of feline enteric coronavirus and feline infectious peritonitis virus infection (1995) Feline Pract., 23, pp. 7-20; Rabehi, L., Ferriere, F., Saffar, L., Alpha-1-acid glycoprotein binds human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein via N-linked glycans (1995) Glycocon. J., 12, pp. 7-16; Selting, K.A., Ogilvie, G.K., Lana, S.E., Serum alpha-1-acid glycoprotein concentrations in healthy and tumor-bearing cats (2000) J. Vet. Intern. Med., 14, pp. 503-506; Shiyan, S.D., Bovin, N.V., Carbohydrate composition and immunomodulatory activity of different glycoforms of alpha-1-acid glycoprotein (1997) Glycocon. J., 14, pp. 631-638; Vasson, M.P., RochArveiller, M., Couderc, R., Effects of alpha-1-acid glycoprotein on human polymorphonuclear neutrophils: Influence of glycan microheterogeneity (1994) Clin. Chim. Acta, 224, pp. 65-71; Williams, J.P., Weiser, M.R., Pechet, T.T.V., Alpha-1-acid glycoprotein reduces local and remote injuries after intestinal ischemia in the rat (1997) Am. J. Physiol., 273, pp. 1031-1035; Waly, N., Gruffyd-Jones, T.J., Stokes, C.R., The distribution of leococytes subsets in the small intestine of healthy cats (2001) J. Comp. Pathol., 124, pp. 172-182","Paltrinieri, S.; Dipartimento di Patologia Animale, Igiene e Sanita Pubblica Veterinaria, Università di Milano, Via Celoria 10, 120133 Milano, Italy; email: saverio.paltrinieri@unimi.it",,,16185641,,CCPOA,,"English","Comp. Clin. Pathol.",Article,"Final",,Scopus,2-s2.0-0347588279
"Manocha S., Walley K.R., Russell J.A.","7005616896;7006495859;7404208893;","Severe acute respiratory distress syndrome (SARS): A critical care perspective",2003,"Critical Care Medicine","31","11",,"2684","2692",,32,"10.1097/01.CCM.0000091929.51288.5F","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344442309&doi=10.1097%2f01.CCM.0000091929.51288.5F&partnerID=40&md5=56eeb0656f666a6046b165923a97c6a0","Section of Critical Care Medicine, Department of Medicine, University of British Columbia, Vancouver, BC, Canada","Manocha, S., Section of Critical Care Medicine, Department of Medicine, University of British Columbia, Vancouver, BC, Canada; Walley, K.R., Section of Critical Care Medicine, Department of Medicine, University of British Columbia, Vancouver, BC, Canada; Russell, J.A., Section of Critical Care Medicine, Department of Medicine, University of British Columbia, Vancouver, BC, Canada","Objective: To review the epidemiology, clinical features, etiology, diagnosis, and management of severe acute respiratory syndrome (SARS) from a critical care perspective. Data Sources: A MEDLINE search was performed using the following terms: severe acute respiratory syndrome and SARS virus. Additional information and references were obtained from the Web sites for the Centers for Disease Control and Prevention, World Health Organization, and Health Canada. Study Selection: Recent case series were used to develop a review of the epidemiology, clinical features, outcomes, and management of patients with SARS from an intensive care unit (ICU) perspective. This was supplemented by epidemiology information obtained from other Web-based sources. Recent published studies describing the etiology of SARS were also included. Data Synthesis: SARS has rapidly spread from Southeast Asia to numerous countries, including Canada and the United States. A new coronavirus has been isolated and detected from many affected patients. The mortality rate worldwide is approximately 10.5%. From five cohorts, the ICU admission rate ranged from 20% to 38%. Fifty-nine percent to 100% of the ICU patients required mechanical ventilatory support. The mortality rate of SARS patients admitted to the ICU ranged from 5% to 67%. The most common clinical symptoms and signs are fever, cough, dyspnea, myalgias, malaise, and inspiratory crackles. Common laboratory abnormalities included mild leukopenia, lymphopenia, and increased aspartate transaminase, alanine transaminase, lactic dehydrogenase, and creatine kinase. The chest radiograph pattern ranged from focal infiltrates to diffuse airspace disease. Management consisted of isolation, strict respiratory and contact precautions, ventilatory support as needed, empiric broad-spectrum antibiotics, ribavirin, and corticosteroids. Predictors of mortality included advanced age, the presence of comorbidities, and a high lactic dehydrogenase or high neutrophil count at admission. Conclusions: SARS is a highly contagious, infectious process that can advance to significant hypoxemic respiratory failure requiring ICU monitoring and support. Early recognition is critical for effective management and containment of this disease.","Corona-virus; Critical care; Mechanical ventilation; SARS; Severe acute respiratory syndrome","antibiotic agent; beta lactam antibiotic; cefotaxime; clarithromycin; corticosteroid; hydrocortisone; lactate dehydrogenase; levofloxacin; macrolide; methylprednisolone; oseltamivir; prednisolone; ribavirin; artificial ventilation; assisted ventilation; cell count; clinical feature; comorbidity; Coronavirus; diagnostic accuracy; diagnostic test; disease classification; disease transmission; drug efficacy; drug megadose; epidemiological data; hemolysis; hospital admission; human; infection control; infection prevention; intensive care; laboratory test; low drug dose; MEDLINE; mortality; neutrophil; pathogenesis; patient monitoring; pneumonia; prediction; priority journal; review; SARS coronavirus; severe acute respiratory distress syndrome; thorax radiography; treatment outcome; Adult; Coronavirus Infections; Critical Care; Enzyme-Linked Immunosorbent Assay; Female; Humans; Intensive Care Units; Male; Middle Aged; Reverse Transcriptase Polymerase Chain Reaction; Severe Acute Respiratory Syndrome","(2003) Summary of Severe Acute Respiratory Syndrome (SARS) Cases: Canada and International, June 26, 2003, , http://www.sars.ca, Ottawa, Health Canada; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; (2003) Cluster of Severe Acute Respiratory Syndrome Cases among Protected Health Care Workers - Toronto, April 2003 Canada Communicable Disease Report Preview, 15 May 2003, , http://www.hc-sc.gc.ca/pphb-dgspsp/publicat/ccdr-rmtc/03vol29/prev/ dr-sars0515.html, Ottawa, Health Canada; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peiris, J.M., Lai, S.T., Poon, L.L., Coronavirus as a cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto Area (2003) JAMA, 289, pp. 2801-2809; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Folz, R.J., Elkordy, M.A., Coronavirus pneumonia following autologous bone marrow transplantation for breast cancer (1999) Chest, 115, pp. 901-905; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; 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Mandell, L.A., Marrie, T.J., Grossman, R.F., Canadian guidelines for the initial management of community-acquired pneumonia: An evidence-based update by the Canadian Infectious Diseases Society and the Canadian Thoracic Society (2000) Clin Infect Dis, 31, pp. 383-421; Niederman, M.S., Mandell, L.A., Anzueto, A., Guidelines for the management of adults with community-acquired pneumonia: Diagnosis, assessment of severity, antimicrobial therapy, and prevention (2001) Am J Respir Crit Care Med, 163, pp. 1730-1754","Manocha, S.; Section of Critical Care Medicine, Department of Medicine, University of British Columbia, Vancouver, BC, Canada",,,00903493,,CCMDC,"14605542","English","Crit. Care Med.",Review,"Final",,Scopus,2-s2.0-0344442309
"Cai Y., Liu Y., Yu D., Zhang X.","49962967600;27167942300;56332050700;55715175900;","Down-regulation of transcription of the proapoptotic gene BNip3 in cultured astrocytes by murine coronavirus infection",2003,"Virology","316","1",,"104","115",,8,"10.1016/j.virol.2003.07.007","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242352468&doi=10.1016%2fj.virol.2003.07.007&partnerID=40&md5=f8557ed647a5b7a6ff6ca2dd230cc3ef","Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States","Cai, Y., Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States; Liu, Y., Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States; Yu, D., Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States; Zhang, X., Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States","Murine coronavirus mouse hepatitis virus (MHV) causes encephalitis and demyelination in the central nervous system of susceptible rodents. Astrocytes are the major target for MHV persistence. However, the mechanisms by which astrocytes survive MHV infection and permit viral persistence are not known. Here we performed DNA microarray analysis on differential gene expression in astrocyte DBT cells by MHV infection and found that the mRNA of the proapoptotic gene BNip3 was significantly decreased following MHV infection. This finding was further confirmed by quantitative reverse transcription- polymerase chain reaction, Western blot analysis, and BNip3-promoter-luciferase reporter system. Interestingly, infection with live and ultraviolet light-inactivated viruses equally repressed BNip3 expression, indicating that the down-regulation of BNip3 expression does not require virus replication and is mediated during cell entry. Furthermore, treatment of cells with chloroquine, which blocks the acidification of endosomes, significantly inhibited the repression of the BNip3 promoter activity induced by the acidic pH-dependent MHV mutant OBLV60, which enters cells via endocytosis, indicating that the down-regulation of BNip3 expression is mediated by fusion between viral envelope and cell membranes during entry. Deletion analysis showed that the sequence between nucleotides 262 and 550 of the 588-base-pair BNip3 promoter is necessary and sufficient for driving the BNip3 expression and that it contains signals that are responsible for MHV-induced down-regulation of BNip3 expression in DBT cells. These results may provide insights into the mechanisms by which MHV evades host antiviral defense and promotes cell survival, thereby allowing its persistence in the host astrocytes. © 2003 Elsevier Inc. All rights reserved.",,"apoptosis inducing factor; bcl 2 and nineteen kilodalton protein interacting protein 3; chlorine; luciferase; messenger RNA; unclassified drug; acidification; acidity; animal cell; article; astrocyte; cell membrane; DNA microarray; down regulation; endocytosis; endosome; gene expression; gene repression; molecular dynamics; mouse; Murine hepatitis coronavirus; nonhuman; nucleotide sequence; pH; priority journal; promoter region; reporter gene; reverse transcription polymerase chain reaction; ultraviolet radiation; virus cell interaction; virus envelope; virus inactivation; virus infection; virus mutant; virus replication; Western blotting; Coronavirus; Murinae; Murine hepatitis virus; Rodentia","Adami, C., Pooley, J., Glomb, J., Stecker, E., Fazal, F., Fleming, J.O., Baker, S., Evolution of mouse hepatitis virus (MHV) during chronic infection: Quasispecies nature of the persisting MHV RNA (1995) Virology, 209, pp. 337-346; An, S., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J. 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Exp. Med. Biol., 494, pp. 329-334","Zhang, X.; Dept. of Microbiology and Immunology, Univ. of AR for Medical Sciences, 4301 W. Markham Street, Slot 511, Little Rock, AR 72205, United States; email: zhangxuming@uams.edu",,"Academic Press Inc.",00426822,,VIRLA,"14599795","English","Virology",Article,"Final",Open Access,Scopus,2-s2.0-0242352468
"Yang H., Yang M., Ding Y., Liu Y., Lou Z., Zhou Z., Sun L., Mo L., Ye S., Pang H., Gao G.F., Anand K., Bartlam M., Hilgenfeld R., Rao Z.","55731078500;7404925978;7404136267;56014846700;7101735895;57198734785;55628530893;8266234700;7202088279;7102237558;7403171212;56371191700;6701775559;7006843618;7102549060;","The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor",2003,"Proceedings of the National Academy of Sciences of the United States of America","100","23",,"13190","13195",,349,"10.1073/pnas.1835675100","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345255626&doi=10.1073%2fpnas.1835675100&partnerID=40&md5=d1ca9c0ec58566460adfa03f4f51c741","Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Institute of Biochemistry, University of Lübeck, 23538 Lübeck, Germany; Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China","Yang, H., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Yang, M., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Ding, Y., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Liu, Y., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Lou, Z., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Zhou, Z., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Sun, L., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Mo, L., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Ye, S., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Pang, H., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Gao, G.F., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Anand, K., Institute of Biochemistry, University of Lübeck, 23538 Lübeck, Germany; Bartlam, M., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China; Hilgenfeld, R., Institute of Biochemistry, University of Lübeck, 23538 Lübeck, Germany; Rao, Z., Laboratory of Structural Biology, Tsinghua University, Institute of Biophysics, 100084 Beijing, China, Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China","A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.",,"proteinase; virus protein; article; conformational transition; controlled study; Coronavirus; crystal structure; enzyme structure; epidemic; nonhuman; pH; priority journal; protein degradation; respiratory tract disease; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; virus replication; Amino Acid Chloromethyl Ketones; Binding Sites; Crystallography, X-Ray; Cysteine; Cysteine Endopeptidases; Endopeptidases; Glutathione Transferase; Histidine; Hydrogen-Ion Concentration; Models, Chemical; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Tertiary; SARS Virus; Substrate Specificity; Time Factors; Viral Proteins; Coronavirus; RNA viruses; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Fouchier, R.A., (2003) N. Engl. J. Med., 348, pp. 1967-1976; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Peiris, M., Osterhaus, A.D., (2003) Nature, 423, p. 240; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Lim, W., (2003) N. Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Cheung, M.T., (2003) Lancet, 361, pp. 1319-1325; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Chan, S.Y., (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Chen, M.H., (2003) Science, 300, pp. 1394-1399; Ruan, Y.J., Wei, C.L., Ee, A.L., Vega, V.B., Thoreau, H., Su, S.T., Chia, J.M., Lim, L., (2003) Lancet, 361, pp. 1779-1785; Thiel, V., Herold, J., Schelle, B., Siddell, S.G., (2001) J. Virol., 75, pp. 6676-6681; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., (2003) Science, 300, pp. 1763-1767; Ziebuhr, J., Snijder, E.J., Gorbalenya, A.E., (2000) J. Gen. Virol., 81, pp. 853-879; Zhu, J., Li, P., Wu, T., Gao, F., Ding, Y., Zhang, C.W., Rao, Z., Tien, P., (2003) Protein Eng., 16, pp. 373-379; Otwinowski, Z., Minor, W., (1997) Macromolecular Crystallography, Part A, 276, pp. 307-326. , ed. Sweet, R. M. (Academic, New York); Matthews, B.W., (1968) J. Mol. Biol., 33, pp. 491-497; Laskowski, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., (1993) J. Appl. Crystallogr., 26, pp. 283-291; Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Pannu, N.S., (1998) Acta Crystallogr. D, 54, pp. 905-921; Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Crystallogr. A, 47, pp. 110-119; Ziebuhr, J., Heusipp, G., Siddell, S.G., (1997) J. Virol., 71, pp. 3992-3997; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., (2002) EMBO J., 21, pp. 3213-3224","Rao, Z.; Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China; email: raozh@xtal.tsinghua.edu.cn",,,00278424,,PNASA,"14585926","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0345255626
"Kanra G., Kara A.","7004528527;7102824838;","Severe acute respiratory syndrome (SARS) [SARS: Şiddetli akut solunum yetmezliǧi sendromu]",2003,"Cocuk Sagligi ve Hastaliklari Dergisi","46","3",,"155","161",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242299103&partnerID=40&md5=53f9c61c8b62b37dd0ce3a3f270e88f7","Department of Pediatrics, Hacettepe University, Faculty of Medicine, Ankara, Turkey","Kanra, G., Department of Pediatrics, Hacettepe University, Faculty of Medicine, Ankara, Turkey; Kara, A., Department of Pediatrics, Hacettepe University, Faculty of Medicine, Ankara, Turkey","Severe acute respiratory syndrome (SARS) has recently been recognized as a newly emerging infectious disease that is highly contagious with significant morbidity and mortality. Earliest cases of SARS has been described in patients in Asia, North America, and Europe. Etiological agent of SARS is shown to be a coronavirus. Most coronaviruses cause disease in only one host species. All known coronaviruses are found in three serologically unrelated groups. A corona of large, distinctive spikes in the envelope makes possible the identification of coronaviruses by electron microscopy. In this way the first identification of agent was possible. Microbiologic and genetic analyses have shown that the SARS-associated coronavirus is neither a mutant nor a recombinant of any known coronaviruses. It is a previously unknown coronavirus, probably from a nonhuman host, that somehow acquired the ability to infect humans. Serologic tests of wild and domestic animals and birds in the region where the outbreak first appeared may identify the usual host. The incubation period for SARS is typically 2-7 days; however, isolated reports have suggested an incubation period as long as 10 days. The illness begins generally with a prodrome of fever (>38.0°C). Fever often is high, is sometimes associated with chills and rigors, and might be accompanied by other symptoms, including headache, malaise, and myalgia. At the onset of illness, some persons have mild respiratory symptoms. Typically, rash and neurologic or gastrointestinal findings are absent; however, some patients have reported diarrhea during the febrile prodrome. After 3-7 days, a lower respiratory phase begins with the onset of a dry, nonproductive cough or dyspnea, which might be accompanied by or progress to hypoxemia. In 10%-20% of cases, the respiratory illness is severe enough to require intubation and mechanical ventilation. The case-fatality rate among persons with illness meeting the current WHO case definition of SARS is approximately 3%. Chest radiographs might be normal during the febrile prodrome and throughout the course of illness. However, in a substantial proportion of patients, the respiratory phase is characterized by early focal interstitial infiltrates progressing to more generalized, patchy, interstitial infiltrates. Some chest radiographs from patients in the late stages of SARS have also shown areas of consolidation. Early in the course of disease, the absolute lymphocyte count is often decreased. Overall white blood cell counts have generally been normal or decreased. At the peak of the respiratory illness, approximately 50% of patients have leukopenia and thrombocytopenia or low-normal platelet counts (50,000-150,000/μL). Early in the respiratory phase, elevated creatine phosphokinase levels (as high as 3,000 IU/L) and hepatic transaminases (2-6 times the upper limits of normal) have been noted. Treatment regimens have included several antibiotics to presumptively treat known bacterial agents of atypical pneumonia. In several locations, therapy has also included antiviral agents such as oseltamivir or ribavirin. Steroids have also been administered orally or intravenously to patients in combination with ribavirin and other antimicrobials. Although there are no approved drugs with proven efficacy against coronaviruses, there are potential targets for the development of new drugs. Protease inhibitors could prevent processing of the RNA polymerase or cleavage of the viral S glycoprotein. Inhibitors of coronavirus acetylesterase activity might limit viral replication.","Atypic pneumonia; Emerging infection; Pneumonia; Severe acute respiratory syndrome (SARS)","aminotransferase; antibiotic agent; antiinfective agent; antivirus agent; creatine kinase; liver enzyme; new drug; oseltamivir; proteinase inhibitor; ribavirin; s glycoprotein; steroid; unclassified drug; virus glycoprotein; artificial ventilation; chill; Coronavirus; coughing; dyspnea; fatality; fever; headache; human; hypoxemia; incubation time; intubation; leukopenia; malaise; myalgia; respiratory tract disease; review; rigor; SARS coronavirus; severe acute respiratory syndrome; thorax radiography; thrombocytopenia; virus pneumonia","Lyons, A.S., Petrucelli, R.J., (1987) Medicine An Illustrated History, , New York: Harry N. Abrams Inc; Acute respiratory syndrome China, Hong Kong Special Administrative Region of China, and Vietnam (2003) WER, 78, pp. 73-74; Severe acute respiratory syndrome (SARS) (2003) WER, 78, p. 89; http://www.who.int/csr/sarsarchive/2003_03_15/en/; http://www.who.int/csr/sars/project/en/; http://www.cdc.gov/mmwr/preview/mmwrhtml/mm5212a5.htm; http://www.cdc.gov/od/oc/media/pressrel/r030324.htm; http://www.cdc.gov/mmwr/preview/mmwrhtml/mm5212al.htm; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; http://www.who.int/csr/sarsarchive/2003_04_16/en/; Donnelly, C.A., Ghani, A.C., Leung, G.M., (2003) Epidemiological Determinants of Spread of Causal Agent of Severe Acute Respiratory Syndrome in Hong Kong, , http://image.thelancet.com/extras/03art4453web.pdf, Published online May 7; Holmes, K.V., Enjuanes, L., Virology. The SARS coronavirus: A postgenomic era (2003) Science, 300, pp. 1377-1378; www.cdc.gov/ncidod/sars; www.who.int/csr/sars; http://link.springer.de/link/service/journals/00134/contents/03/01821/ paper/s00134-003-1821-0ch000.html","Kanra, G.; Department of Pediatrics, Hacettepe University, Faculty of Medicine, Ankara, Turkey",,,00100161,,CSHDA,,"Turkish","Cocuk Sagligi Hast. Derg.",Review,"Final",,Scopus,2-s2.0-0242299103
"Jenwitheesuk E., Samudrala R.","6602308039;7004155573;","Identifying inhibitors of the SARS coronavirus proteinase",2003,"Bioorganic and Medicinal Chemistry Letters","13","22",,"3989","3992",,52,"10.1016/j.bmcl.2003.08.066","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242348704&doi=10.1016%2fj.bmcl.2003.08.066&partnerID=40&md5=b42a70b185b4bc58f2504bec153333f9","Computational Genomics Group, Department of Microbiology, Univ. of WA School of Medicine, Seattle, WA 98195, United States","Jenwitheesuk, E., Computational Genomics Group, Department of Microbiology, Univ. of WA School of Medicine, Seattle, WA 98195, United States; Samudrala, R., Computational Genomics Group, Department of Microbiology, Univ. of WA School of Medicine, Seattle, WA 98195, United States","The Severe Acute Respiratory Syndrome (SARS) is a serious respiratory illness that has recently been reported in parts of Asia and Canada. In this study, we use molecular dynamics (MD) simulations and docking techniques to screen 29 approved and experimental drugs against the theoretical model of the SARS CoV proteinase as well as the experimental structure of the transmissible gastroenteritis virus (TGEV) proteinase. Our predictions indicate that existing HIV-1 protease inhibitors, L-700,417 for instance, have high binding affinities and may provide good starting points for designing SARS CoV proteinase inhibitors. © 2003 Elsevier Ltd. All rights reserved.",,"l 700417; proteinase inhibitor; rupintrivir; unclassified drug; article; binding affinity; calculation; computer prediction; computer program; computer simulation; Coronavirus; dielectric constant; drug binding site; drug conformation; drug protein binding; drug screening; enzyme substrate complex; genetic algorithm; molecular dynamics; severe acute respiratory syndrome; structure activity relation; theoretical model; Transmissible gastroenteritis virus; virus inhibition; virus pneumonia; Coronavirus; Human immunodeficiency virus 1; SARS coronavirus; Transmissible gastroenteritis virus","Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Yuen, K.Y., (2003) Lancet, 361, p. 1319; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., (2003) Science, 300, p. 1399; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., (2003) Science, 300, p. 1763; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., (2002) EMBO J., 21, p. 3213; Clarke, T., Nature, , http://www.nature.com/nsu/030512/030512-11.html, Science Update; Jenwitheesuk, E., Samudrala, R., (2003) BMC Struct. Biol., 3, p. 2; Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Belew, R.K., Olson, A.J., (1998) J. Comput. Chem., 19, p. 1639; Kale, L., Skeel, R., Bhandarkar, M., Brunner, R., Gursoy, A., Krawetz, N., Phillips, J., Schulten, K., (1999) J. Comput. Phys., 151, p. 283; Brunger, A.T., (1992) In X-PLOR version 3.1, A System for X-ray Crystallography and NMR, , Yale University Press: New Haven, CT; Bone, R., Vacca, J.P., Anderson, P.S., Holloway, M.K., (1991) J. Am. Chem. Soc., 113, p. 9382","Samudrala, R.; Computational Genomics Group, Department of Microbiology, Univ. of WA School of Medicine, Seattle, WA 98195, United States; email: ram@compbio.washington.edu",,"Elsevier Ltd",0960894X,,BMCLE,"14592491","English","Bioorg. Med. Chem. Lett.",Article,"Final",Open Access,Scopus,2-s2.0-0242348704
"Smales F.C., Samaranyake L.P.","7004018285;57191921359;","Maintaining dental education and specialist dental care during an outbreak of a new coronavirus infection. Part 1: A deadly viral epidemic begins",2003,"British Dental Journal","195","10",,"557","561",,,"10.1038/sj.bdj.4810723","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542389573&doi=10.1038%2fsj.bdj.4810723&partnerID=40&md5=c0a82501509f5602743bfaf6c2df8ac7","Faculty of Dentistry, Prince Philip Dental Hospital, Hong Kong, Hong Kong; Department of Oral Microbiology, Prince Philip Dental Hospital, Hong Kong, Hong Kong; University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong","Smales, F.C., Faculty of Dentistry, Prince Philip Dental Hospital, Hong Kong, Hong Kong, University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong; Samaranyake, L.P., Department of Oral Microbiology, Prince Philip Dental Hospital, Hong Kong, Hong Kong","During the three months from March 2003 the economically vibrant city of Hong Kong was seriously dislocated after becoming 'second port of call' of the new and potentially fatal disease, Severe Acute Respiratory Syndrome (SARS). The uncertainties during that period had a significant impact on the provision of dental care. However the city's only dental hospital continued to function and to support the Faculty of Dentistry of the University of Hong Kong in educating dental students and other members of the dental team. At the time of writing no transmissions of the disease have been attributed to procedures associated with dental healthcare. This article chronicles the sequence of events during the outbreak from a dental perspective. It highlights information that may be useful to dental colleagues who might someday be confronted with similar outbreaks of newly emerged potentially lethal infections.",,"dental care; dental education; disease control; epidemic; health care management; health care organization; Hong Kong; hospital; human; medical student; review; severe acute respiratory syndrome; article; Coronavirus; disease transmission; epidemic; health care delivery; infection control; organization and management; pathogenicity; severe acute respiratory syndrome; university hospital; Coronavirus; Delivery of Health Care; Dental Care; Dental Service, Hospital; Disease Outbreaks; Disease Transmission, Horizontal; Education, Dental; Hong Kong; Hospitals, University; Humans; Infection Control, Dental; Schools, Dental; Severe Acute Respiratory Syndrome; Universal Precautions","Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Update: Outbreak of Severe Acute Respiratory Syndrome - Worldwide, 2003 (2003) MMWR, 52, pp. 241-248. , Atlanta: Centres for Disease Control and Prevention 2003; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Sci, 300, pp. 1394-1399. , May 30; Samaranayake, L.P., (2002) Essential Microbiology for Dentistry. 2nd Ed., , Edinburgh: Churchill Livingstone; Seto, W.H., Tsang, D., Yung, R.W., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361 (9638), pp. 1519-1520; Stohr, K.A., Multicentre collaboration to investigate the cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1730-1733; Interim Domestic Infection Control Precautions for Aerosol-generating Procedures on Patients with Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/aerosolinfectioncontrol.htm, Atlanta: Centers for Disease Control and Prevention. May 2003 Last retrieval on 4th June 2003","Smales, F.C.; University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong; email: fcsmales@hkusua.hku.hk",,,00070610,,,"14631425","English","Brit. Dent. J.",Review,"Final",Open Access,Scopus,2-s2.0-1542389573
"He M.-L., Zheng B., Peng Y., Peiris J.S.M., Poon L.L.M., Yuen K.Y., Lin M.C.M., Kung H.-F., Guan Y.","35080389700;7201780588;7403419265;7005486823;7005441747;36078079100;56032965000;7402514190;7202924055;","Inhibition of SARS-Associated Coronavirus Infection and Replication by RNA Interference [5]",2003,"Journal of the American Medical Association","290","20",,"2665","2666",,74,"10.1001/jama.290.20.2665","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344430079&doi=10.1001%2fjama.290.20.2665&partnerID=40&md5=4d7647cf4db085f8d61c23b20bebd836","University of Hong Kong, Hong Kong, Hong Kong","He, M.-L., University of Hong Kong, Hong Kong, Hong Kong; Zheng, B., University of Hong Kong, Hong Kong, Hong Kong; Peng, Y., University of Hong Kong, Hong Kong, Hong Kong; Peiris, J.S.M., University of Hong Kong, Hong Kong, Hong Kong; Poon, L.L.M., University of Hong Kong, Hong Kong, Hong Kong; Yuen, K.Y., University of Hong Kong, Hong Kong, Hong Kong; Lin, M.C.M., University of Hong Kong, Hong Kong, Hong Kong; Kung, H.-F., University of Hong Kong, Hong Kong, Hong Kong; Guan, Y., University of Hong Kong, Hong Kong, Hong Kong",[No abstract available],,"RNA; Coronavirus; cytopathogenic effect; gene sequence; human; immunofluorescence test; letter; mammal cell; nonhuman; priority journal; reverse transcription polymerase chain reaction; RNA replication; SARS coronavirus; severe acute respiratory syndrome; virus infection; virus pneumonia; Animals; Antigens, Viral; Cell Line; Cytopathogenic Effect, Viral; Genome, Viral; Humans; RNA Interference; RNA Replicase; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Transfection; Virus Replication","Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poon, L.L.M., Wong, O.K., Luk, W., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 1-3; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; McManus, M.T., Sharp, P.A., Gene silencing in mammals by small interfering RNAs (2002) Nat Rev Genet, 3, pp. 737-747; Elbashir, S.M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., Tuschl, T., Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells (2001) Nature, 411, pp. 494-498","He, M.-L.; University of Hong Kong, Hong Kong, Hong Kong",,,00987484,,JAMAA,"14645307","English","J. Am. Med. Assoc.",Letter,"Final",Open Access,Scopus,2-s2.0-0344430079
"Li W., Moore M.J., Vasllieva N., Sui J., Wong S.K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greeneugh T.C., Choe H., Farzan M.","55718630900;57214386991;6505524620;7006812991;36912447800;57130529500;6701489001;35426559600;7003728717;6504423951;7103055410;7003535041;","Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus",2003,"Nature","426","6965",,"450","454",,1090,"10.1038/nature02145","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344395657&doi=10.1038%2fnature02145&partnerID=40&md5=a8e4fd143d5f294458e2ff5b8b16d9e1","Brigham and Women's Hospital, Dept. Med. Microbiol./Molec. Genet., Harvard Medical School, Boston, MA 02115, United States; Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115, United States; Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115, United States; Tufts University Core Facility, Tufts University School of Medicine, Boston, MA 02111, United States; Program in Molecular Medicine, Univ. of Massachusetts Med. School, Worcester, MA 01605, United States","Li, W., Brigham and Women's Hospital, Dept. Med. Microbiol./Molec. Genet., Harvard Medical School, Boston, MA 02115, United States; Moore, M.J., Brigham and Women's Hospital, Dept. Med. Microbiol./Molec. Genet., Harvard Medical School, Boston, MA 02115, United States; Vasllieva, N., Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115, United States; Sui, J., Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115, United States; Wong, S.K., Brigham and Women's Hospital, Dept. Med. Microbiol./Molec. Genet., Harvard Medical School, Boston, MA 02115, United States; Berne, M.A., Tufts University Core Facility, Tufts University School of Medicine, Boston, MA 02111, United States; Somasundaran, M., Program in Molecular Medicine, Univ. of Massachusetts Med. School, Worcester, MA 01605, United States; Sullivan, J.L., Program in Molecular Medicine, Univ. of Massachusetts Med. School, Worcester, MA 01605, United States; Luzuriaga, K., Program in Molecular Medicine, Univ. of Massachusetts Med. School, Worcester, MA 01605, United States; Greeneugh, T.C., Program in Molecular Medicine, Univ. of Massachusetts Med. School, Worcester, MA 01605, United States; Choe, H., Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115, United States; Farzan, M., Brigham and Women's Hospital, Dept. Med. Microbiol./Molec. Genet., Harvard Medical School, Boston, MA 02115, United States","Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2, isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.",,"Antibodies; Association reactions; Cells; Pulmonary diseases; Viruses; Cellular receptors; Severe acute respiratory syndrome (SARS); Enzymes; dipeptidyl carboxypeptidase; dipeptidyl carboxypeptidase 2; unclassified drug; virus protein; virus receptor; biochemistry; protein; animal cell; article; controlled study; Coronavirus; enzyme isolation; genetic transfection; human; human cell; Human immunodeficiency virus 1; nonhuman; pneumonia; priority journal; protein binding; protein domain; protein expression; severe acute respiratory syndrome; virus replication; Animals; Antibodies; Carboxypeptidases; Cell Line; Cercopithecus aethiops; Giant Cells; Humans; Membrane Glycoproteins; Molecular Weight; Peptidyl-Dipeptidase A; Protein Binding; Protein Structure, Tertiary; Receptors, Virus; SARS Virus; Solubility; Transfection; Vero Cells; Viral Envelope Proteins; Virus Replication; Animalia; Coronavirus; Human immunodeficiency virus; Human immunodeficiency virus 1; RNA viruses; SARS coronavirus","Gallagher, T.M., Buchmeler, M.J., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Donoghue, M., A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin 1 to angiotensin 1-9 (2000) Circ. Res., 87, pp. E1-E9; Tipnis, S.R., A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase (2000) J. Biol. Chem., 275, pp. 33238-33243; Holmes, K.V., Coronavirus receptor specificity (1993) Adv. Exp. Med. Biol., 342, pp. 261-266; Dveksler, G.S., Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59 (1993) J. Virol., 67, pp. 1-8; Delmas, B., Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV (1992) Nature, 357, pp. 417-420; Tresnan, D.B., Holmes, K.V., Feline aminopeptidase N is a receptor for all group I coronaviruses (1998) Adv. Exp. Med. Biol., 440, pp. 69-75; Yeager, C.L., Human aminopeptidase N is a receptor for human coronavirus 229E (1992) Nature, 357, pp. 420-422; Ksiazek, T.G., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Kuiken, T., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362, pp. 263-270; Fouchier, R.A., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Rota, P.A., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., The Genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Sturman, L.S., Holmes, K.V., Proteolytic cleavage of peplomeric glycoprotein E2 of MHV yields two 90K subunits and activates cell fusion (1984) Adv. Exp. Med. Biol., 173, pp. 25-35; Jackwood, M.W., Spike glycoprotein cleavage recognition site analysis of infectious bronchitis virus (2001) Avian Dis., 45, pp. 366-372; Spaan, W., Cavanagh, D., Horzinek, M.C., Coronaviruses: Structure and genome expression (1988) J. Gen. Virol., 69, pp. 2939-2952; Bonavia, A., Zelus, B.D., Wentworth, D.E., Talbot, P.J., Holmes, K.V., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Breslin, J.J., Human coronavirus 229E: Receptor binding domain and neutralization by soluble receptor at 37 degrees C (2003) J. Virol., 77, pp. 4435-4438; Kubo, H., Yamada, Y.K., Taguchi, F., Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68, pp. 3403-5410; Komatsu, T., Molecular cloning, mRNA expression and chromosomal localization of mouse angiotensin-converting enzyme-related carboxy peptidase (mACE2) (2002) DNA Seq., 13, pp. 217-220; Harmer, D., Gilbert, M., Borman, R., Clark, K.L., Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme (2002) FEBS Lett., 532, pp. 107-110; Choe, H., The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates (1996) Cell, 85, pp. 1135-1148; Leung, W.K., Enteric involvement of severe acute respiratory syndrome-associated coronavirus infection (2003) Gastroenterology, 125, pp. 1011-1017; Crackower, M.A., Angiotensin-converting enzyme 2 is an essential regulator of heart function (2002) Nature, 417, pp. 822-828; Vickers, C., Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase (2002) J. Biol. Chem., 277, pp. 14838-14843; Delmas, B., Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site (1994) J. Virol., 68, pp. 5216-5224; Huang, L., Novel peptide inhibitors of angiotensin-converting enzyme 2 (2003) J. Biol. Chem., 278, pp. 15532-15540; Dales, N.A., Substrate-based design of the first class of angiotensin-converting enzyme-related carboxypeptidase (ACE2) inhibitors (2002) J. Am. Chem. Soc., 124, pp. 11852-11853","Choe, H.; Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115, United States; email: hyeryun.choe@tch.harvard.edu",,,00280836,,NATUA,"14647384","English","Nature",Article,"Final",Open Access,Scopus,2-s2.0-0344395657
"He R., Leeson A., Andonov A., Li Y., Bastien N., Cao J., Osiowy C., Dobie F., Cutts T., Ballantine M., Li X.","7202418164;8057524200;6701413300;35187394200;6602480468;7403354429;6602293103;20336995500;6601985113;6603180402;35330008400;","Activation of AP-1 signal transduction pathway by SARS coronavirus nucleocapsid protein",2003,"Biochemical and Biophysical Research Communications","311","4",,"870","876",,79,"10.1016/j.bbrc.2003.10.075","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744220599&doi=10.1016%2fj.bbrc.2003.10.075&partnerID=40&md5=e72a764d6c988d6498e7ea025d0a0023","National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Centre for Biologics Research, Biol./Genetic Therapies Directorate, Health Canada, Tunney's Pasture, Ottawa, Ont. K1A 0K9, Canada","He, R., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Leeson, A., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; Andonov, A., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Li, Y., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Bastien, N., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Cao, J., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Osiowy, C., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada, Department of Medical Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; Dobie, F., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; Cutts, T., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; Ballantine, M., National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; Li, X., Centre for Biologics Research, Biol./Genetic Therapies Directorate, Health Canada, Tunney's Pasture, Ottawa, Ont. K1A 0K9, Canada","In March 2003, a novel coronavirus was isolated from patients exhibiting atypical pneumonia and subsequently proven to be the causative agent of the disease now referred to as severe acute respiratory syndrome (SARS). The complete genome of the SARS coronavirus (SARS-CoV) has since been sequenced. The SARS-CoV nucleocapsid (SARS-CoV N) shares little homology with other members of the coronavirus family. To determine if the N protein is involved in the regulation of cellular signal transduction, an ELISA-based assay on transcription factors was used. We found that the amount of transcription factors binding to promoter sequences of c-Fos, ATF2, CREB-1, and FosB was increased by the expression of SARS-CoV N. Since these factors are related to AP-1 signal transduction pathway, we investigated whether the AP-1 pathway was activated by SARS-CoV N protein using the PathDetect system. The results demonstrated that the expression of N protein, not the membrane protein (M), activated AP-1 pathway. We also found that SARS-CoV N protein does not activate NF-κB pathway, demonstrating that activation of important cellular pathways by SAS-CoV N protein is selective. Thus our data for the first time indicate that SARS-CoV has encoded a strategy to regulate cellular signaling process. © 2003 Elsevier Inc. All rights reserved.",,"cyclic AMP responsive element binding protein; membrane protein; nucleocapsid protein; protein c fos; protein fos; transcription factor AP 1; animal cell; article; controlled study; Coronavirus; gene sequence; human; human cell; nonhuman; nucleotide sequence; priority journal; promoter region; protein binding; protein DNA interaction; protein expression; protein protein interaction; SARS coronavirus; signal transduction; Coronavirus; SARS coronavirus","Holmes, K.V., (2001) Field's Virology, 1. , Lippincott, Williams & Wilkins, Philadelphia 1187-1203; Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Mcgeer, A.J., Identification of severe acute respiratory syndrome in Canada (2003) N. Engl. J. Med., 348 (20), pp. 1995-2005; Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., SARS working group. A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Hiscox, J.A., Wurm, T., Wilson, L., Britton, P., Cavanagh, D., Brooks, G., The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus (2001) J. Virol., 75 (1), pp. 506-512; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Rowland, R.R., Kervin, R., Kuckleburg, C., Sperlich, A., Benfield, D.A., The localization of porcine reproductive and respiratory syndrome virus nucleocapsid protein to the nucleolus of infected cells and identification of a potential nucleolar localization signal sequence (1999) Virus Res., 64 (1), pp. 1-12; Chen, H., Wurm, T., Britton, P., Brooks, G., Hiscox, J.A., Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell (2002) J. Virol., 76 (10), pp. 5233-5250; Smith, S.A., Kotwal, G.J., Immune response to poxvirus infections in various animals (2002) Crit. Rev. Microbiol., 28 (3), pp. 149-185; Kotwal, G.J., Poxviral mimicry of complement and chemokine system components: What's the end game? (2000) Immunol. Today, 21 (5), pp. 242-248; Shaulian, E., Karin, M., AP-1 as a regulator of cell life and death (2002) Nat. Cell Biol., 4, pp. 131-E136; Degawa-Yamauchi, M., Uotani, S., Yamaguchi, Y., Takahashi, R., Abe, T., Kuwahara, H., Yamasaki, H., Eguchi, K., Ethanol inhibits leptin-induced STAT3 activation in Huh7 cells (2002) FEBS Lett., 525 (1), pp. 116-120; Wisdom, R., AP-1: One switch for many signals (1999) Exp. Cell Res., 253, pp. 180-185; Karin, M., Liu, Z., Zandi, E., AP-1 function and regulation (1997) Curr. Opin. Cell Biol., 9, pp. 240-246","He, R.; National Microbiology Laboratory, Health Canada, 1015 Arlington Street, Winnipeg, MB R3E 3R2, Canada; email: Runtao_He@hc-sc.gc.ca",,"Academic Press Inc.",0006291X,,BBRCA,"14623261","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-10744220599
"Battilani M., Coradin T., Scagliarini A., Ciulli S., Ostanello F., Prosperi S., Morganti L.","56059625300;57198266534;6602273786;55879930100;6603098151;6603623491;57213660634;","Quasispecies composition and phylogenetic analysis of feline coronaviruses (FCoVs) in naturally infected cats",2003,"FEMS Immunology and Medical Microbiology","39","2",,"141","147",,20,"10.1016/S0928-8244(03)00237-2","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242475197&doi=10.1016%2fS0928-8244%2803%2900237-2&partnerID=40&md5=c6750fde6bd2769936bc41a9bd00e070","Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy","Battilani, M., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Coradin, T., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Scagliarini, A., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Ciulli, S., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Ostanello, F., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Prosperi, S., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy; Morganti, L., Dipartimento di Sanita’ Pubblica Veterinaria e Patologia Animale-Servizio MIPAV, Alma Mater Studiorum, University of Bologna, Via Tolara di Sopra, 50, 40064 Ozzano Emilia (Bo), Italy","Quasispecies composition and tissue distribution of feline coronaviruses (FCoVs) were studied in naturally infected cats. The genomic complexity of FCoVs was investigated using single-strand conformational polymorphism (SSCP) analysis of N and ORF7b amplicons, and the evolutionary process was investigated by sequence-based phylogenetic analysis. SSCP analysis showed high heterogeneity of the FCoV genome which was correlated with the seriousness of the clinical form. The two genomic regions analysed showed different levels of variation; the N region demonstrated significant heterogeneity as compared to ORF7b. Phylogenetic analysis of the nucleotide sequences showed the clear separation of sequences analysed on the basis of virulence and geographical origin. A maximum likelihood analysis of N and ORF7b data sets showed a situation of strong heterogeneity for the N region. © 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.","Feline coronavirus; Phylogenetic analysis; Quasispecies","amino terminal sequence; amplicon; article; cat disease; controlled study; Coronavirus; correlation analysis; disease severity; genetic heterogeneity; genomics; geographical variation (species); maximum likelihood method; molecular evolution; molecular phylogeny; nonhuman; nucleotide sequence; open reading frame; priority journal; sequence analysis; single strand conformation polymorphism; virus genome; virus infection; virus virulence","De Vries, A.A.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The genome organization of the Nidovirales: Similarities and differences between Arteri-, Toro-, and Coronaviruses (1997) Semin. Virol., 8, pp. 33-47; Pedersen, N.C., Boyle, J.F., Floyd, K., Infection studies in kittens using feline infectious peritonitis virus propagated in cell culture (1981) Am. J. Vet. Res., 42, pp. 363-367; Horzinek, M.C., Lutz, H., An update of feline infectious peritonitis (2001) Vet. Sci. Tomorrow, 1, , http://www.vetscite.org/cgi-bin/pw.exe/vst/reviews/index_1_0800.htm; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Herrewegh, A.A.P.M., Mähler, M., Hedrich, H.J., Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat breeding colony (1997) Virology, 234, pp. 349-363; Eigen, M., Self-organization of matter and the evolution of biological macromolecules (1971) Naturwissenschaften, 58, pp. 465-523; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Horzinek, M.C., Herrewegh, A.A.P.M., De Groot, R.J., Perspectives on feline coronavirus evolution (1995) Feline Pract., 23 (3), pp. 34-39; Domingo, E., Escarmis, C., Sevilla, N., Moya, A., Elena, S.F., Quer, J., Novella, I.S., Holland, J.J., Basic concepts in RNA virus evolution (1996) FASEB J., 10, pp. 859-864; Orita, M., Iwahana, H., Kanazawa, H., Hayashi, K., Sekiya, T., Detection of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms (1989) Proc. Natl. Acad. Sci. USA, 86, pp. 2766-2770; Orita, M., Suzuki, Y., Sekiya, T., Hayashi, K., Rapid and sensitive detection of point mutations and DNA polymorphims using the polymerase chain reaction (1989) Genomics, 5, pp. 874-879; Gut, M., Leutenegger, C.M., Huder, J.B., Pedersen, N.C., Lutz, H., One-tube fluorogenic reverse transcription-polymerase chain reaction for the quantitation of feline coronaviruses (1999) J. Virol. Methods, 77, pp. 37-46; Kiss, I., Kecskeméti, S., Tanyi, J., Klingeborn, B., Belák, S., Preliminary studies of feline coronavirus distribution in naturally and experimentally infected cats (2000) Res. Vet. Sci., 68, pp. 237-242; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22, pp. 4673-4680; Xia, X., Xie, Z., DAMBE: Software package for data analysis in molecular biology and evolution (2001) J. Hered., 92, pp. 371-373; Nicholas, K.B., Nicholas, H.B., Jr., Deerfield, D.W., GeneDoc: Analysis and visualization of genetic variation (1997) Embnew. News, 4, p. 14; Swofford, D.L., (2001) PAUP* Phylogenetic Analysis Using Parsimony (*and other methods) 4.0b10, , Sinauer Associates, Sunderland, MA; Felsenstein, J., Distance methods for inferring phylogenies: A justification (1984) Evolution, 38, pp. 16-24; Hasegawa, M., Kishino, H., Yano, T.-A., Dating of the human-ape splitting by a molecular clock of michondrial DNA (1985) J. Mol. Evol., 22, pp. 160-174; Tamura, K., Nei, M., Estimation of the number of nucleotide substitutions in the control region of mitochondrial DNA in humans and chimpanzees (1993) Mol. Biol. Evol., 10, pp. 512-526; Felsenstein, J., (2001) PHYLIP: Phylogenetic Inference Package 3.6 (alpha3), , Distributed by the author, Department of Genetics, University of Washington, Seattle, WA; Strimmer, K., Von Haeseler, A., Quartet puzzling: A quartet maximum-likelihood method for reconstructing tree topologies (1996) Mol. Biol. Evol., 13, pp. 964-969; Felsenstein, J., Confidence limits on phylogenies: An approach using the bootstrap (1985) Evolution, 39, pp. 783-791; Page, R.D., TreeView: An application to display phylogenetic trees on personal computers (1996) Mol. Biol. Evol., 4, pp. 406-425; Strimmer, K., Von Haeseler, A., Likelihood-mapping: A simple method to visualize phylogenetic content of a sequence alignment (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 6815-6819; Eigen, E., Biebricher, C., Sequence space and quasispecies distribution (1988) RNA Genetics, 3, pp. 211-245. , Domingo, E., Holland, J.J. and Ahlquist, P., Eds. CRC Press, Boca Raton, FL; Domingo, E., Holland, J.J., RNA virus mutations and fitness for survival (1997) Annu. Rev. Microbiol., 51, pp. 151-178; Makino, S., Keck, J.G., Stohlman, S.A., Lai, M.M.C., High-frequency RNA recombination of murine coronaviruses (1986) J. Virol., 57, pp. 729-739; Gunn-Moore, D.A., Gunn-Moore, F.J., Gruffydd-Jones, T.J., Harbour, D.A., Detection of FCoV quasispecies using denaturing gel electrophoresis (1999) Vet. Microbiol., 69, pp. 127-130; Domingo, E., Quasispecies and the implication for virus persistence and escape (1998) Clin. Diagn. Virol., 10, pp. 97-101; Herrewegh, A.A.P.M., Vennema, H., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., The molecular genetics of feline coronaviruses: Comparative sequence analysis of the ORF 7a/7b transcription unit of different biotypes (1995) Virology, 212, pp. 622-631",,,,09288244,,,"14625097","English","FEMS Immunol. Med. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0242475197
"Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S., Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.H., Song H.C., Abrignani S., Covacci A., Rappuoli R.","55913596100;55446677800;24432172000;7102740671;7003816836;6701795733;6602825305;6603149430;7004003650;7102515482;7003921934;8664208600;8119065200;57206904667;7003304561;56976632300;","Phylogeny of the SARS Coronavirus [3]",2003,"Science","302","5650",,"1504","1505",,63,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344827226&partnerID=40&md5=5789dad63148f10ef8d070c4edc7092d","Institute for Virology, University of Marburg, 35037 Marburg, Germany; Institute of Medicial Virology, University of Frankfurt, 60596 Frankfurt, Germany; IRIS, Chiron Vaccines, 53100 Siena, Italy; Chiron Corporation, Emeryville, CA 94608-2916, United States","Eickmann, M., Institute for Virology, University of Marburg, 35037 Marburg, Germany; Becker, S., Institute for Virology, University of Marburg, 35037 Marburg, Germany; Klenk, H.-D., Institute for Virology, University of Marburg, 35037 Marburg, Germany; Doerr, H.W., Institute of Medicial Virology, University of Frankfurt, 60596 Frankfurt, Germany; Stadler, K., IRIS, Chiron Vaccines, 53100 Siena, Italy; Censini, S., IRIS, Chiron Vaccines, 53100 Siena, Italy; Guidotti, S., IRIS, Chiron Vaccines, 53100 Siena, Italy; Masignani, V., IRIS, Chiron Vaccines, 53100 Siena, Italy; Scarselli, M., IRIS, Chiron Vaccines, 53100 Siena, Italy; Mora, M., IRIS, Chiron Vaccines, 53100 Siena, Italy; Donati, C., IRIS, Chiron Vaccines, 53100 Siena, Italy; Han, J.H., Chiron Corporation, Emeryville, CA 94608-2916, United States; Song, H.C., Chiron Corporation, Emeryville, CA 94608-2916, United States; Abrignani, S., IRIS, Chiron Vaccines, 53100 Siena, Italy; Covacci, A., IRIS, Chiron Vaccines, 53100 Siena, Italy; Rappuoli, R., IRIS, Chiron Vaccines, 53100 Siena, Italy",[No abstract available],,"amino terminal sequence; China; consensus sequence; Coronavirus; food contamination; genome analysis; letter; molecular phylogeny; nucleotide sequence; priority journal; receptor binding; SARS coronavirus; viral contamination; viral genetics; virus genome; Algorithms; Amino Acid Sequence; Consensus Sequence; Coronavirus; Genome, Viral; Membrane Glycoproteins; Nucleocapsid; Phylogeny; SARS Virus; Viral Envelope Proteins; Viral Matrix Proteins; Viral Proteins; Coronavirus; SARS coronavirus","Drosten, C., (2003) N. Engl. J. Med., 348, p. 1967; Marra, M.A., (2003) Science, 300, p. 1399; Peiris, J.S., (2003) Lancet, 361, p. 1319; Rota, P.A., (2003) Science, 300, p. 1394; Guan, Y., (2003) Science, 302, p. 276; Snijder, E.J., (2003) J. Mol. Biol., 331, p. 991","Rappuoli, R.; IRIS, Chiron Vaccines, 53100 Siena, Italy; email: rino_rappuoli@chiron.it",,,00368075,,SCIEA,"14645828","English","Science",Letter,"Final",,Scopus,2-s2.0-0344827226
"Chim S.S.C., Tsui S.K.W., Chan K.C.A., Au T.C.C., Hung E.C.W., Tong Y.K., Chiu R.W.K., Ng E.K.O., Chan P.K.S., Chu C.M., Sung J.J.Y., Tam J.S., Fung K.P., Waye M.M.Y., Lee C.Y., Yuen K.Y., Lo Y.M.D.","6701728226;7004961364;13403797200;24597501100;7004256338;7202614141;7103038413;21135553700;32067487100;7404345558;35405352400;24788939600;7202934739;7006687733;55526554300;36078079100;7401935391;","Genomic characterisation of the severe acute respiratory syndrome coronavirus of Amoy Gardens outbreak in Hong Kong",2003,"Lancet","362","9398",,"1807","1808",,41,"10.1016/S0140-6736(03)14901-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744223100&doi=10.1016%2fS0140-6736%2803%2914901-X&partnerID=40&md5=dc9ef2dbdcfcb3a45cb8dbd3636a206e","Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Department of Medicine, United Christian Hospital, Hong Kong, Hong Kong; Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, New Territories, Hong Kong","Chim, S.S.C., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Tsui, S.K.W., Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Chan, K.C.A., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Au, T.C.C., Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Hung, E.C.W., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Tong, Y.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Chiu, R.W.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Ng, E.K.O., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Chan, P.K.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Chu, C.M., Department of Medicine, United Christian Hospital, Hong Kong, Hong Kong; Sung, J.J.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Tam, J.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Fung, K.P., Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Waye, M.M.Y., Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Lee, C.Y., Department of Biochemistry, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong, Hong Kong; Yuen, K.Y., Department of Microbiology, Queen Mary Hospital, University of Hong Kong, Hong Kong, Hong Kong; Lo, Y.M.D., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, New Territories, Hong Kong","Severe acute respiratory syndrome (SARS) is a global health concern. In Hong Kong, two major outbreaks, one hospital based and the other in the Amoy Gardens apartments, were identified. The frequency of diarrhoea, admission to intensive care, and mortality differed significantly between the two outbreaks. We did genomic sequencing for viral isolates from five Amoy Gardens patients. The virus sequence was identical in four of these five patients. The sequence data from one hospital case and the four identical community cases had only three nucleotide differences. Alterations in the SARS coronavirus genome are unlikely to have caused the distinctive clinical features of the Amoy Gardens patients, and these results highlight the importance of non-viral genomic factors in this outbreak.",,"article; clinical article; epidemic; gene sequence; genome analysis; Hong Kong; hospital patient; human; nucleotide sequence; open reading frame; priority journal; SARS coronavirus; severe acute respiratory syndrome; virus characterization; virus isolation","Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Outbreak of severe acute respiratory syndrome (SARS) at Amoy Gardens, Kowloon Bay, Hong Kong: main findings of the investigation, , http://www.info.gov.uk/info/ap/pdf/amoy_e.pdf; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J.M., Astell, C.R., The genomic sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404","Lo, Y.M.D.; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing Street, Shatin, New Territories, Hong Kong; email: loym@cuhk.edu.hk",,"Elsevier Limited",01406736,,LANCA,"14654320","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-10744223100
"Zarudnaya M.I., Potyahaylo A.L., Hovorun D.M.","55894919800;6602976010;6701750269;","Conservative structural motifs in the 3' untranslated region of SARS coronavirus",2003,"Biopolymers and Cell","19","3",,"298","303",,3,"10.7124/bc.000661","https://www.scopus.com/inward/record.uri?eid=2-s2.0-69949128305&doi=10.7124%2fbc.000661&partnerID=40&md5=0d89d3b9513bcba952235330a8db7e71","Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine","Zarudnaya, M.I., Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine; Potyahaylo, A.L., Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine; Hovorun, D.M., Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine","Signal elements in the 3' untranslated region (UTR) of «plus»-RNA viruses function as control elements in RNA replication, transcription and translation. Here we performed computer-assisted (Zuker, 2003) secondary structure analysis and prediction of tertiary structure of 3' UTR of SARS coronavirus. We found that this region contains a sequence potentially able to form a pseudoknot which was earlier observed in 3' UTR of every coronavirus genome that was sequenced. The SARS-CoV pseudoknot structure is similar to the pseudoknot structure of the group 1 coronaviruses. As in the case of other coronaviruses the formation of the SARS-CoV pseudoknot interferes with the formation of a bulged stem-loop structure with high negative free energy value located in the most upstream part of 3' UTR. Besides the SARS-CoV 3' UTR, like the same region of 1BV coronavirus, contains the s2m motif which is absent in 3' UTR of a number of group 1 and 2 coronaviruses. Other structural motifs in 3' UTR of SARS-CoV has been discussed as well. As a result, the SARS-CoV 3' UTR structure established supports the present opinion on a unique character of this virus which cannot be assigned to any of three known groups of coronaviruses.",,,"Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Pong, S., Lim, W., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Chen, M.-H., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science., , In press (Publ. online 1 May 2003; 1.0.1126/science. l085952.); Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, V.S.N., Khattra, J., Chan, S.Y., The genome sequence of the SARS-associated coronavirus (2003) Science., , In press (Publ. online 1 May 2003; 10.1126/science. 1085953.); Zuker, M., Mfold web server for nucleic acid folding and hybridization prediction (2003) Nucl. Acids Res., 31 (13), pp. 1-10; Sawicki, S.G., Sawicki, D.L., A new model for coronavirus transcription (1998) Adv. Exp. Med. Biol., 440, pp. 215-219; Hsue, B., Hartshorne, T., Masters, P.S., Characterization of an essential RNA secondary structure in the 3' untranslated region of the murine coronavirus genome (2000) J. Virol., 74 (15), pp. 6911-6921; Hsue, B., Masters, P.S., A bulged stem-loop structure in the 3' untranslated region of the genome of the coronavirus mouse hepatitis virus is essential for replication (1997) J. Virol., 71 (10), pp. 7567-7578; Williams, G.D., Chang, R.-Y., Brian, D.A., A phylogenetically conserved hairpin-type 3' untranslated region pseudoknot functions in coronavirus RNA replication (1999) J. Virol., 73 (10), pp. 8349-8355; Liu, Q., Johnson, R.F., Leibowitz, J.L., Secondary structural elements within the 3' untranslated region of mouse hepatitis virus strain JHM genomic RNA (2001) J. Virol., 75 (24), pp. 12105-12113; Berkhout, B., Ooms, M., Beerens, N., Huthoff, H., Southern, E., Verhoef, K., In vitro evidence that the untranslated leader of the HIV-1 genome is an RNA checkpoint that regulates multiple functions through conformational changes (2002) J. Biol. Chem., 277 (22), pp. 19967-19975; Huthoff, H., Berkhout, B., Multiple secondary structure rearrangements during HIV-1 RNA dimerization (2002) Biochemistry., 41 (33), pp. 10439-10445; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3' end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J. Gen. Virol., 79 (PART 4), pp. 715-718; Lin, Y.-J., Liao, C.-L., Lai, M.M.C., Identification of the as-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription (1994) J. Virol., 68 (12), pp. 8131-8140; Yu, W., Leibowitz, J.L., Specific binding of host cellular proteins to multiple sites within the 3' end of mouse hepatitis virus genomic RNA (1995) J. Virol., 69 (4), pp. 2016-2023; Liu, Q., Yu, W., Leibomtz, J.L., A specific host cellular protein binding element near the 3' end of mouse hepatitis virus genomic RNA (1997) Virology., 232 (1), pp. 74-85; Yu, W., Leibowitz, J.L., A conserved motif at the 3' end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication (1995) Virology., 214 (1), pp. 128-138; Spagnolo, J.F., Hogue, B.G., Host protein interactions with the 3' end of bovine coronavirus RNA and the requirement of the poly (A) tail for coronavirus defective genome replication (2000) J. Virol., 74 (11), pp. 5053-5065; Huang, P., Lai, M.M.C., Heterogeneous nuclear ribonucleoprotein At binds to the 3' untranslated region and mediates potential 5'-3'-end cross talks of mouse hepatitis virus RNA (2001) J. Virol., 75 (11), pp. 5009-5017","Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine",,,02337657,,,,"English","Bioplym. Cell",Article,"Final",Open Access,Scopus,2-s2.0-69949128305
"Zhang X.-L., Wang J.-R., Zhang Y., Chen M.-L.., Zhang W., Yang S., Jiang W.-H.","7410266420;55878810200;7601312081;56134516900;36066941200;22837280100;7403697918;","Expression, purification and identification of recombinant SARS coronavirus membrane protein",2003,"Acta Biochimica et Biophysica Sinica","35","12",,"1140","1144",,4,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1642401471&partnerID=40&md5=c73272650aff8dc147a8dd0aeca2e6c2","Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Shenyang Pharmaceutical University, China; Jilin University, China","Zhang, X.-L., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Wang, J.-R., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China, Shenyang Pharmaceutical University, China; Zhang, Y., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China, Jilin University, China; Chen, M.-L.., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China, Jilin University, China; Zhang, W., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Yang, S., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; Jiang, W.-H., Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China","A novel coronavirus (SARS-coronavirus, SARS-CoV) was discovered as the pathogen of the severe acute respiratory syndrome (SARS). According to studies with other coronaviruses, the membrane protein (M protein) is the main structural protein and the recombinant M protein may be useful as an antigen for detecting antibodies against coronavirus and for preparing vaccine. In this work, the M protein of SARS-CoV was expressed in E. coli as fusion protein with maltose binding protein at N-terminus and MxeGyrA intein CBD at C-terminus. The recombinant protein was identified by Western blot and mass spectrometry. The soluble parts of the cell crude extract were then partially purified by MBP affinity chromatography. The purified protein will be used for the studies on M protein's structure and the development of diagnostic method of SARS.","Coronavirus; Recombinant M protein; Severe acute respiratory syndrome (SARS)","hybrid protein; intein; M protein; maltose binding protein; membrane protein; recombinant protein; virus antibody; virus protein; affinity chromatography; amino terminal sequence; article; carboxy terminal sequence; Escherichia coli; mass spectrometry; nonhuman; protein analysis; protein expression; protein purification; protein structure; SARS coronavirus; severe acute respiratory syndrome; Western blotting; Amino Acid Sequence; Blotting, Western; Carrier Proteins; Gene Expression Regulation, Viral; Recombinant Fusion Proteins; Recombinant Proteins; SARS Virus; Sequence Analysis, Protein; Viral Matrix Proteins; Coronavirus; Escherichia coli; SARS coronavirus","Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348 (20), pp. 1995-2005; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348 (20), pp. 1986-1994; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Guan, Y., Yam, L.Y.C., Lim, W., Nicholls, J., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348 (20), pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Peñaranda, S., Characterization of a novel corona-virus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1377-1378; Marra, M.A., Jones, S.J.M., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S.N., Khattra, J., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Qin, E.D., Zhu, Q.Y., Yu, M., Fan, B.C., Chang, G.H., Si, B.Y., Yang, B.A., A complete sequence and comparative analysis of strain (BJ01) of the SARS-associated virus (2003) Chinese Sci Bull, 48 (10), pp. 941-948; De Haan, C.A.M., Smeets, M., Vernooij, F., Vennema, H., Rottier, P.J.M., Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein (1999) J Virol, 73 (9), pp. 7441-7452; Kopecky, S.A., Willingham, M.C., Lyles, D.S., Matrix protein and another viral component contribute to induction of apoptosis in cells infected with vesicular stomatitis virus (2001) J Virol, 75 (24), pp. 12169-12181; Kopecky, S.A., Lyles, D.S., Constrasting effects of matrix protein on apoptosis in HeLa and BHK cells infected with vesicular stomatitis virus are due to inhibition of host gene expression (2003) J Virol, 77 (8), pp. 4658-4669; Wang, L.F., Gould, A.R., Selleck, P.W., Expression of equine morbillivirus (EMV) matrix and fusion proteins and their evaluation as diagnostic reagents (1997) Arch Virol, 142, pp. 2269-2279; Elia, G., Fiermonte, G., Pratelli, A., Martella, V., Camero, M., Cirone, F., Buonavoglia, C., Recombinant M protein-based ELISA test for detection of antibodies to canine coronavirus (2003) J Virol Methods, 109 (2), pp. 139-142; Shao, X.X., Zeng, R., Xia, Q.C., Peptide mapping and primary structural analysis of cytochrome C by liquid chromatography-mass spectrometry (1998) J Chinese Mass Spectrometry Society, 19 (4), pp. 1-7","Yang, S.; Inst. of Plant Physiol. and Ecology, Shanghai Institutes for Biol. Sci., Chinese Academy of Sciences, Shanghai 200032, China; email: syang@sibs.ac.cn",,,05829879,,,"14673508","Chinese","Acta Biochim. Biophys. Sin.",Article,"Final",,Scopus,2-s2.0-1642401471
"Lai M.M.C.","7401808497;","SARS virus: The beginning of the unraveling of a new coronavirus",2003,"Journal of Biomedical Science","10","6 II",,"664","675",,38,"10.1159/000074077","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346787886&doi=10.1159%2f000074077&partnerID=40&md5=e863ece22b98cadcc5ecacc438da2cc1","Dept. of Molec. Microbiol./Immunol., University of Southern California, Keck School of Medicine, Los Angeles, CA, United States; Office of the Vice President, Institute of Molecular Biology, Academia Sinica, Nankang, Taiwan; Dept. of Molec. Microbiol./Immunol., University of Southern California, Keck School of Medicine, Los Angeles, CA 90033, United States","Lai, M.M.C., Dept. of Molec. Microbiol./Immunol., University of Southern California, Keck School of Medicine, Los Angeles, CA, United States, Office of the Vice President, Institute of Molecular Biology, Academia Sinica, Nankang, Taiwan, Dept. of Molec. Microbiol./Immunol., University of Southern California, Keck School of Medicine, Los Angeles, CA 90033, United States","Severe acute respiratory syndrome (SARS) virus caused a severe outbreak in several regions of the world in 2003. The virus is a novel coronavirus, which may have an origin in wild animals such as civet cats in southern China. Its genome structure, gene expression pattern and protein profiles are similar to those of other coronaviruses. However, distinct patterns of several open reading frames in the SARS virus genome may contribute to its severe virulence. The potential mutability of the coronavirus genome may pose problems in the control of future SARS outbreaks. The mechanism of SARS pathogenesis may involve both direct viral cytocidal effects on the target cells and immune-mediated mechanisms. The life cycle of the SARS virus is largely unknown; however, based on the analogy with other coronaviruses, several potential targets for antiviral development are identified. Vaccines offer an important preventive measure for possible future recurrences of SARS, but the prospect for their development is still unknown because of the uncertainty regarding the role of immune responses in SARS virus pathogenesis. The comparative studies of other coronaviruses offer insights into the understanding of SARS virus. Copyright © 2003 National Science Council, ROC and S. Karger AG, Basel.","Coronavirus; Drug targets; Genetics; Mutations; Origin; Pathogenesis; Replication; RNA; Severe acute respiratory syndrome; Taxonomy; Vaccines; Viral proteins","antivirus agent; corona virus vaccine; structural protein; unclassified drug; virus vaccine; cat; China; comparative study; drug efficacy; epidemic; gene expression; gene mutation; gene structure; gene targeting; human; immune response; nonhuman; open reading frame; pathogenesis; priority journal; review; SARS coronavirus; severe acute respiratory syndrome; taxonomy; vaccination; virus gene; virus infection; virus transmission; Chromosome Mapping; Gene Expression; SARS Virus; Severe Acute Respiratory Syndrome; Viral Structural Proteins; Animalia; Coronavirus; Felis catus; SARS coronavirus","Abbott, A., Pet theory comes to the fore in fight against SARS (2003) Nature, 423, p. 576; Almazan, F., Gonzalez, J.M., Penzes, Z., Izeta, A., Calvo, E., Plana-Duran, J., Enjuanes, L., Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome (2000) Proc Natl Acad Sci USA, 97, pp. 5516-5521; An, S., Chen, C.-J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of E protein as an apoptosis inducer (1999) J Virol, 73, pp. 7853-7859; Anand, K., Palm, G.J., Mesters, J.R., Siddell, S.G., Ziebuhr, J., Hilgenfeld, R., Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain (2002) EMBO J, 21, pp. 3213-3224; Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R., Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs (2003) Science, 300, pp. 1763-1767; Baker, S.C., Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., Lai, M.M.C., Identification of the catalytic sites of a papain-like cystein proteinase of murine coronavirus (1993) J Virol, 67, pp. 6056-6063; Ballesteros, M.L., Sanchez, C.M., Enjuanes, L., Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism (1997) Virology, 227, pp. 378-388; 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Casais, R., Thiel, V., Siddell, S.G., Cavanagh, D., Britton, P., Reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) J Virol, 75, pp. 12359-12369; Charley, B., Laude, H., Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of transmembrane glycoprotein E 1 (1988) J Virol, 62, pp. 8-11; Chouljenko, V.N., Kousoulas, K.G., Lin, X., Storz, J., Nucleotide and predicted amino acid sequences of all genes encoded by the 3′ genomic protion (9.5 kb) of respiratory bovine coronaviruses and comparisons among respiratory and enteric coronaviruses (1998) Virus Genes, 17, pp. 33-42; Corapi, W.V., Olsen, C.W., Scott, F.W., Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus (1992) J Virol, 66, pp. 6695-6705; De Groot, R.J., Van Leen, R.W., Dalderup, M.J.M., Vennema, H., Horzinek, M.C., Spaan, W.J.M., Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice (1989) Virology, 171, pp. 493-502; 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Microbiol./Immunol., University of Southern California, Keck School of Medicine, Los Angeles, CA 90033, United States; email: michlai@hsc.usc.edu",,,10217770,,JBCIE,"14631105","English","J. Biomed. Sci.",Review,"Final",Open Access,Scopus,2-s2.0-0346787886
"Gao L., Qi J., Wei H., Sun Y., Hao B.","56505975000;13608357200;55239502800;56175079900;7005338571;","Molecular phylogeny of coronaviruses including human SARS-CoV",2003,"Chinese Science Bulletin","48","12",,"1170","1174",,27,"10.1360/03wc0254","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1242268097&doi=10.1360%2f03wc0254&partnerID=40&md5=32646b45b18205097ec00e51864e767c","Institute of Theoretical Physics, Chinese Academy of Sciences, Beijing 100080, China; T-Life Research Center, Fudan University, Shanghai 200433, China; Graduate School, Zhejiang University, Hangzhou 310027, China; Hangzhou Branch, Beijing Genomics Institute, Chinese Academy of Sciences, Hangzhou 310008, China","Gao, L., Institute of Theoretical Physics, Chinese Academy of Sciences, Beijing 100080, China, T-Life Research Center, Fudan University, Shanghai 200433, China; Qi, J., Institute of Theoretical Physics, Chinese Academy of Sciences, Beijing 100080, China, T-Life Research Center, Fudan University, Shanghai 200433, China; Wei, H., Graduate School, Zhejiang University, Hangzhou 310027, China, Hangzhou Branch, Beijing Genomics Institute, Chinese Academy of Sciences, Hangzhou 310008, China; Sun, Y., Graduate School, Zhejiang University, Hangzhou 310027, China, Hangzhou Branch, Beijing Genomics Institute, Chinese Academy of Sciences, Hangzhou 310008, China; Hao, B., T-Life Research Center, Fudan University, Shanghai 200433, China, Hangzhou Branch, Beijing Genomics Institute, Chinese Academy of Sciences, Hangzhou 310008, China","Phylogenetic tree of coronaviruses (CoVs) including the human SARS-associatcd virus is reconstructed from complete genomes by using our newly developed K-string composition approach. The relation of the human SARS-CoV to other coronaviruses, i.e. the rooting of the tree is suggested by choosing an appropriate outgroup. SARS-CoV makes a separate group closer but still distant from G2 (CoVs in mammalian host). The relation between different isolates of the human SARS virus is inferred by first constructing an ultrametric distance matrix from counting sequence variations in the genomes. The resulting tree is consistent with clinic relations between the SARS-CoV isolates. In addition to a larger variety of coronavirus genomes these results provide phylogenetic knowledge based on independent novel methodology as compared to recent phylogenetic studies on SARS-CoV.","Composition distance; Coronavirus; Molecular phylogeny; Severe acute respiratory syndrome (SARS); Ultramericity","Coronavirus; Mammalia; SARS coronavirus","Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Qin, E.D., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronovirus isolates and common mutations associated with putative origins of infection (2003) The Lancet, 361 (9371), pp. 1779-1785; Qi, J., Wang, B., Hao, B.L., Whole genome prokaryote phylogeny without sequence alignment: A K-string composition approach (2003) J. Mol. Evol., , in print; Chu, K.H., Qi, J., Yu, Z.G., Origin and phylogeny of chloroplasts: A simple correlation analysis of complete genomes Mol. Biol. Evol., , under revision; Nei, M., Kumar, S., (2000) Molecular Evolution and Phylogenetics, pp. 87-103. , New York: Oxford University Press; Rammal, R., Toulouse, G., Virasoro, M., Ultrametricity for physicists (1986) Rev. Mod. Phys., 58, pp. 765-788","Hao, B.; T-Life Research Center, Fudan University, Shanghai 200433, China; email: hao@itp.ac.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-1242268097
"Wang J., Wen J., Li J., Yin J., Zhu Q., Wang H., Yang Y., Qin E., You B., Li W., Li X., Huang S., Yang R., Zhang X., Yang L., Zhang T., Yin Y., Cui X., Tang X., Wang L., He B., Ma L., Lei T., Zeng C., Fang J., Yu J., Wang J., Yang H., West M.B., Bhatnagar A., Lu Y., Xu N., Liu S.","8272121600;49664305200;8644253500;7401693537;7403313352;56608115200;36124366800;6701908544;57199280134;56127183500;7501700961;8613102900;55547041600;23029398300;57198986719;57206941902;57206977950;57209994665;36124056400;57201266722;55456316000;7403574073;8322357900;8236325500;7402966086;8679878600;57200022156;34573719100;8340204500;7202474550;57205512724;55771049200;7409459608;","Assessment of Immunoreactive Synthetic Peptides from the Structural Proteins of Severe Acute Respiratory Syndrome Coronavirus",2003,"Clinical Chemistry","49","12",,"1989","1996",,46,"10.1373/clinchem.2003.023184","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344514885&doi=10.1373%2fclinchem.2003.023184&partnerID=40&md5=4fc256e4d61ef6cd9ec456741ceccd0a","Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China; James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Inst. of Microbiol. and Epidemiology, Chinese Acad. of Mil. Med. Sciences, Beijing 100071, China; Capital Institute of Pediatrics, Beijing 100022, China; Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Department of Medicine, University of Louisville, Louisville, KY 40202, United States","Wang, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Wen, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Department of Medicine, University of Louisville, Louisville, KY 40202, United States; Li, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Yin, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Zhu, Q., Inst. of Microbiol. and Epidemiology, Chinese Acad. of Mil. Med. Sciences, Beijing 100071, China; Wang, H., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Yang, Y., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Qin, E., Inst. of Microbiol. and Epidemiology, Chinese Acad. of Mil. Med. Sciences, Beijing 100071, China; You, B., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Li, W., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Li, X., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Huang, S., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Yang, R., Inst. of Microbiol. and Epidemiology, Chinese Acad. of Mil. Med. Sciences, Beijing 100071, China; Zhang, X., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Yang, L., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Zhang, T., Capital Institute of Pediatrics, Beijing 100022, China; Yin, Y., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Cui, X., Capital Institute of Pediatrics, Beijing 100022, China; Tang, X., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Wang, L., Capital Institute of Pediatrics, Beijing 100022, China; He, B., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Ma, L., Capital Institute of Pediatrics, Beijing 100022, China; Lei, T., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Zeng, C., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Fang, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Yu, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; Wang, J., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Yang, H., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China; West, M.B., Department of Medicine, University of Louisville, Louisville, KY 40202, United States; Bhatnagar, A., Department of Medicine, University of Louisville, Louisville, KY 40202, United States; Lu, Y., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Xu, N., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China; Liu, S., Beijing Genomics Institute (BGI), Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China, James D. Watson Inst. of Genome Sci., Zhijiang Campus, Zhejiang University, Hangzhou 310008, China, Beijing Proteomics Institute (BPI), I-Zone, Shunyi, Beijing 101300, China, Department of Medicine, University of Louisville, Louisville, KY 40202, United States","Background: The widespread threat of severe acute respiratory syndrome (SARS) to human life has spawned challenges to develop fast and accurate analytical methods for its early diagnosis and to create a safe antiviral vaccine for preventive use. Consequently, we thoroughly investigated the immunoreactivities with patient sera of a series of synthesized peptides from SARS-coronavirus structural proteins. Methods: We synthesized 41 peptides ranging in size from 16 to 25 amino acid residues of relatively high hydrophilicity. The immunoreactivities of the peptides with SARS patient sera were determined by ELISA. Results: Four epitopic sites, S599, M137, N66, and N371-404, located in the SARS-coronavirus S, M, and N proteins, respectively, were detected by screening synthesized peptides. Notably, N371 and N385, located at the COOH terminus of the N protein, inhibited binding of antibodies to SARS-coronavirus lysate and bound to antibodies in >94% of samples from SARS study patients. N385 had the highest affinity for forming peptide-antibody complexes with SARS serum. Conclusions: Five peptides from SARS structural proteins, especially two from the COOH terminus of the N protein, appear to be highly immunogenic and may be useful for serologic assays. The identification of these antigenic peptides contributes to the understanding of the immunogenicity and persistence of SARS coronavirus. © 2003 American Association for Clinical Chemistry.",,"guanine nucleotide binding protein; protein m; protein S; structural protein; synthetic peptide; unclassified drug; virus protein; antigen binding; article; clinical article; clinical trial; controlled clinical trial; controlled study; Coronavirus; enzyme linked immunosorbent assay; human; hydrophilicity; immunoreactivity; medical assessment; multicenter study; peptide synthesis; protein structure; respiratory tract disease; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; Animals; Antibodies, Viral; Cercopithecus aethiops; Enzyme-Linked Immunosorbent Assay; Epitope Mapping; Humans; Peptide Fragments; SARS Virus; Serologic Tests; Severe Acute Respiratory Syndrome; Vero Cells; Viral Structural Proteins; Coronavirus; SARS coronavirus","Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The genome sequence of the SARS associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Ruan, Y.J., Wei, C.L., Ee, A.L., Vega, V.B., Thoreau, H., Su, S.T., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785; Qin, E.D., Zhu, Q.Y., Yu, M., Fan, B.C., Chang, G.H., Si, B.Y., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJO1) (2003) Chin Sci Bull, 48, pp. 941-948; Poon, L.L., Wong, O.K., Luk, W., Yuen, K.Y., Peiris, J.S., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 953-955; Landini, M.P., New approaches and perspectives in cytomegagaovirus diagnosis (1993) Prog Med Virol, 40, pp. 157-177; Geysen, H.M., Meloen, R.H., Barteling, S.J., Use of peptide synthesis to probe vial antigens for epitopes to a resolution of a single amino acid (1984) Proc Natl Acad Sci U S A, 81, pp. 3998-4002; Zhu, Q.Y., Qin, E.D., Wang, C.E., Yu, M., Si, B.Y., Fan, B.C., Isolation and identification of a novel coronavirus from patients with SARS (2003) J Chin Biotech, 23, pp. 106-112; Hopp, T.P., Woods, K.R., Prediction of protein antigenic determinants from amino acid sequences (1981) Proc Natl Acad Sci U S A, 78, pp. 3824-3828; Cavanagh, D., Davis, P.J., Evolution of avian coronavirus IBV: Sequence of the matrix glycoprotein gene and intergenic region of several serotypes (1988) J Gen Virol, 69, pp. 621-629; Wege, H., Schliephake, A., Korner, H., Flory, E., Wege, H., An immunodominant CD4+ T cell site on the nucleocapsid protein of murine coronavirus contributes to protection against encephalomyelitis (1993) J Gen Virol, 74, pp. 1287-1294; Akin, A., Lin, T.L., Wu, C.C., Bryan, T.A., Hooper, T., Schrader, D., Nucleocapsid protein gene sequence analysis reveals close genomic relationship between turkey coronavirus and avian infectious bronchitis virus (2001) Acta Virol, 45, pp. 31-38; Casal, J.I., Rodriguez, M.J., Sarraseca, J., Garcia, J., Plana-Duran, J., Sanz, A., Identification of a common antigenic site in the nucleocapsid protein of European and North American isolates of porcine reproductive and respiratory syndrome virus (1998) Adv Exp Med Biol, 440, pp. 469-477; Collisson, E.W., Pei, J., Dzielawa, J., Seo, S.H., Cytotoxic T lymphocytes are critical in the control of infectious bronchitis virus in poultry (2000) Dev Comp Immunol, 24, pp. 187-200","Wen, J.; Department of Medicine, University of Louisville, Louisville, KY 40202, United States; email: siqiliu@louisville.edu",,,00099147,,CLCHA,"14633869","English","Clin. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0344514885
"Shi H., Ma W., Wu Q., Zhang B., Song Y., Guo Q., Xiao W., Wang Y., Zheng W.","57210756634;7402704123;57193241784;7406903776;7404919409;7401662959;7202456517;16044156100;7403566536;","Design and application of 60mer oligonucleotide microarray in SARS coronavirus detection",2003,"Chinese Science Bulletin","48","12",,"1165","1169",,4,"10.1360/03wc0216","https://www.scopus.com/inward/record.uri?eid=2-s2.0-28644447607&doi=10.1360%2f03wc0216&partnerID=40&md5=f0422864f7f85abc6b31285c8d285da1","Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Department of Medical Research, Guangzhou Liu Hua Qiao Hospital, Guangzhou 510010, China","Shi, H., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Ma, W., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Wu, Q., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Zhang, B., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Song, Y., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Guo, Q., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Xiao, W., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Wang, Y., Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; Zheng, W., Department of Medical Research, Guangzhou Liu Hua Qiao Hospital, Guangzhou 510010, China","The 60mer oligonucleotide microarray was designed and applied to detecting of SARS (severe acute respiratory syndrome) coronavirus. Thirty 60mer specific oligos were designed to cover the whole genome of the first submitted coronavirus strain, according to the sequence of TOR2 (GENEBANK Accession: AY274119). These primers were synthesized and printed into a microarray with 12×12 spots. RNAs were extracted from the throat swab and gargling fluid of SARS patients and reverse-transcripted into the double strand cDNAs. The cDNAs were prepared as restricted cDNA fragments by the restriction display (RD) technique and labeled by PCR with the Cy5-universal primer. The labeled samples were then applied to the oligo microarray for hybridization. The diagnostic capability of the microarray was evaluated after the washing and scanning steps. The scanning result showed that samples of SARS patients were hybridized with multiple SARS probes on the microarray, and there is no signal on the negative and blank controls. These results indicate that the genome of SARS coronavirus can be detected in parallel by the 60mer oligonucleotide microarray, which can improve the positive ratio of the diagnosis. The oligo microarray can also be used for monitoring the behavior of the virus genes in different stages of the disease status.","Fluorescent labeling; Molecular hybridization; Oligonucleotide microarray; RD technique; SARS coronavirus","Coronavirus; SARS coronavirus","Peiris, J., Lai, S., Poon, L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Qin, E.D., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Wang, Y., Ma, W.L., Song, Y.B., Gene sequence analysis of SARS-associated coronavirus by nested RT-PCR (2003) Di Yi Jun Yi Da Xue Xue Bao (in Chinese), 23 (5), pp. 421-423; Shi, R., Ma, W.L., Song, Y.B., Two restriction fluorescence labeling methods for enhancing the signal-to-noise ratio of cDNA microarray hybridization (2003) Di Yi Jun Yi Da Xue Xue Bao (in Chinese), 23 (2), pp. 124-126; Zhang, B., Ma, W.L., Wu, Q.H., Construction of a cDNA fragment library from SH-SY5Y cells using restriction display PCR (2002) Br. J. Biomed. Sci., 59 (1), pp. 35-37","Ma, W.; Institute of Molecular Biology, First Military Medical University, Guangzhou 510515, China; email: wenli@fimmu.edu.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-28644447607
"Odynets K.A., Kornelyuk A.I.","6506635813;6507004007;","Molecular aspects of organization and expression of SARS-CoV coronavirus genome",2003,"Biopolymers and Cell","19","5",,"414","431",,1,"10.7124/bc.00066F","https://www.scopus.com/inward/record.uri?eid=2-s2.0-69949129928&doi=10.7124%2fbc.00066F&partnerID=40&md5=7c1ecffae3ce4110c195b669c8a1fd30","Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine","Odynets, K.A., Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine; Kornelyuk, A.I., Institute of Molecular Biology and Genetics, NAS of Ukraine, 150, Akademika Zabolotnogo Str, Kyiv, 03680, Ukraine","The molecular aspects of SARS-CoV coronavirus genome structure-the ethiological agent of atypical pneumony or Severe Acute Respiratory Syndrom are discussed. The general characterization of coronaviruses and virion structure are considered in the review. The data about 36 completely sequenced genomes of different SARS-CoV isolates and their phylogenetic analysis are discussed. The predited propoerties of eight subgenomic mRNAs and 14 open reading frames are described, as well as a synthesis of polyproteins, their processing and mature SARS-CoV proteins. The properties of the viral proteins and their functions are analyzed. The surface S-protein is one of the most important antigens of SARS-CoV and it plays an important role in the virus interaction with cell receptor. The potential sites of of S-protein binding with a putative receptor-aminopeptidase hAPN are predicted using both bioinformatics and stu.ctu.ral methods. The main Mpro (3CLpro) proteinase is a potential protein target for antiviral therapy. The modeling of 3D structure of Mpro (3CLpro) proteinase and its active site organization is considered in terms of design of potential SARS-CoV ihibitors.",,,"Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nichotls Yee, W.K., Yuen, K.Y., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Law, K.L., Yuen, K.Y., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet., 361 (9371), pp. 1767-1772; Drosten, C., Gunther, S., Preiser, W., van der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Doerr, H.I.V., Identificalion of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. 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"Cavanagh D.","26642890500;","Severe acute respiratory syndrome vaccine development: Experiences of vaccination against avian infectious bronchitis coronavirus",2003,"Avian Pathology","32","6",,"567","582",,193,"10.1080/03079450310001621198","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1342313389&doi=10.1080%2f03079450310001621198&partnerID=40&md5=b64dbc5cac4f7fef2789c7fbeda98292","Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Cavanagh, D., Institute for Animal Health, Division of Molecular Biology, Compton Laboratory, Compton, Newbury, Berkshire RG20 7NN, United Kingdom","Vaccines against infectious bronchitis of chickens (Gallus gallus domesticus) have arguably been the most successful, and certainly the most widely used, of vaccines for diseases caused by coronaviruses, the others being against bovine, canine, feline and porcine coronaviruses. Infectious bronchitis virus (IBV), together with the genetically related coronaviruses of turkey (Meleagris gallopavo) and ring-necked pheasant (Phasianus colchicus), is a group 3 coronavirus, Severe acute respiratory syndrome (SARS) coronavirus being tentatively in group 4, the other known mammalian coronaviruses being in groups 1 and 2. IBV replicates not only in respiratory tissues (including the nose, trachea, lungs and airsacs, causing respiratory disease), but also in the kidney (associated with minor or major nephritis), oviduct, and in many parts of the alimentary tract - the oesophagus, proventriculus, duodenum, jejunum, bursa of Fabricius, caecal tonsils, rectum and cloaca, usually without clinical effects. The virus can persist, being re-excreted at the onset of egg laying (4 to 5 months of age), believed to be a consequence of the stress of coming into lay. Genetic lines of chickens differ in the extent to which IBV causes mortality in chicks, and in respect of clearance of the virus after the acute phase. Live attenuated (by passage in chicken embryonated eggs) IBV strains were introduced as vaccines in the 1950s, followed a couple of decades later by inactivated vaccines for boosting protection in egg-laying birds. Live vaccines are usually applied to meat-type chickens at 1 day of age. In experimental situations this can result in sterile immunity when challenged by virulent homologous virus. Although 100% of chickens may be protected (against clinical signs and loss of ciliary activity in trachea), sometimes 10% of vaccinated chicks may not respond with a protective immune response. Protection is short lived, the start of the decline being apparent 9 weeks after vaccination with vaccines based on highly attenuated strains. IBV exists as scores of serotypes (defined by the neutralization test), cross-protection often being poor. Consequently, chickens may be re-vaccinated, with the same or another serotype, two or three weeks later. Single applications of inactivated virus has generally led to protection of <50% of chickens. Two applications have led to 90 to 100% protection in some reports, but remaining below 50% in others. In practice in the field, inactivated vaccines are used in laying birds that have previously been primed with two or three live attenuated virus vaccinations. This increases protection of the laying birds against egg production losses and induces a sustained level of serum antibody, which is passed to progeny. The large spike glycoprotein (S) comprises a carboxy-terminal S2 subunit (approximately 625 amino acid residues), which anchors S in the virus envelope, and an amino-terminal S1 subunit (approximately 520 residues), believed to largely form the distal bulbous part of S. The S1 subunit (purified from IBV virus, expressed using baculovirus or expressed in birds from a fowlpoxvirus vector) induced virus neutralizing antibody. Although protective immune responses were induced, multiple inoculations were required and the percentage of protected chickens was too low (<50%) for commercial application. Remarkably, expression of S1 in birds using a non-pathogenic fowl adenovirus vector induced protection in 90% and 100% of chickens in two experiments. Differences of as little as 5% between the S1 sequences can result in poor cross-protection. Differences in S1 of 2 to 3% (10 to 15 amino acids) can change serotype, suggesting that a small number of epitopes are immunodominant with respect to neutralizing antibody. Initial studies of the role of the IBV nucleocapsid protein (N) in immunity suggested that immunization with bacterially expressed N, while not inducing protection directly, improved the induction of protection by a subsequent inoculation with inactivated IBV. In another study, two intramuscular immunizations of a plasmid expressing N induced protective immunity. The basis of immunity to IBV is not well understood. Serum antibody levels do not correlate with protection, although local antibody is believed to play a role. Adoptive transfer of IBV-infection-induced αβ T cells bearing CD8 antigen protected chicks from challenge infection. In conclusion, live attenuated IBV vaccines induce good, although short-lived, protection against homologous challenge, although a minority of individuals may respond poorly. Inactivated IBV vaccines are insufficiently efficacious when applied only once and in the absence of priming by live vaccine. Two applications of inactivated IBV are much more efficacious, although this is not a commercially viable proposition in the poultry industry. However, the cost and logistics of multiple application of a SARS inactivated vaccine would be more acceptable for the protection of human populations, especially if limited to targeted groups (e.g. health care workers and high-risk contacts). Application of a SARS vaccine is perhaps best limited to a minimal number of targeted individuals who can be monitored, as some vaccinated persons might, if infected by SARS coronavirus, become asymptomatic excretors of virus, thereby posing a risk to non-vaccinated people. Looking further into the future, the high efficacy of the fowl adenovirus vector expressing the IBV S1 subunit provides optimism for a live SARS vaccine, if that were deemed to be necessary, with the possibility of including the N protein gene.",,"live vaccine; virus vaccine; animal; animal disease; Avian infectious bronchitis virus; bird disease; chicken; human; immunology; review; SARS coronavirus; severe acute respiratory syndrome; virology; virus infection; Animals; Chickens; Coronavirus Infections; Humans; Infectious bronchitis virus; Poultry Diseases; SARS Virus; Severe Acute Respiratory Syndrome; Vaccines, Attenuated; Viral Vaccines; Adenoviridae; Animalia; Aves; Avian infectious bronchitis virus; Bovinae; Coronavirus; Enterobacter; Felidae; Fowlpox virus; Galliformes; Gallus; Gallus gallus; Mammalia; Meleagris gallopavo; Phasianus colchicus; SARS coronavirus; Suidae; unidentified baculovirus","Addie, D.D., Jarrett, O., Use of a reverse-transcriptase polymerase chain reaction for monitoring the shedding of feline coronavirus by healthy cats (2001) Veterinary Record, 148, pp. 649-653; Addie, D.D., Schaap, I.A.T., Nicolson, O., Jarrett, O., Persistence and transmission of natural type 1 feline coronavirus infection (2003) Journal of General Virology, 84, pp. 2735-2744; Adzhar, A., Cough, R.E., Haydon, D., Shaw, K., Britton, P., Cavanagh, D., Molecular analysis of the 793/B serotype of infectious bronchitis virus in Great Britain (1997) Avian Pathologyogy, 26, pp. 625-640; Alexander, D.J., Allan, W.H., Biggs, P.M., Bracewell, C.D., Darbyshire, J.H., Dawson, P.S., Harris, A.H., Wilding, G.P., A standard technique for haemagglutination inhibition test for antibodies to avian infectious bronchitis virus (1983) The Veterinary Record, 113, p. 64; Ambali, A.C., Jones, R.C., Early pathogenesis in chicks with an enterotropic strain of infectious bronchitis virus (1990) Avian Diseases, 34, pp. 809-817; Bhattacharjee, P.S., Jones, R.C., Susceptibility of organ cultures from chicken tissues for strains of infectious bronchitis virus isolated from the intestine (1997) Avian Pathology, 26, pp. 553-563; Boots, A.M.H., Benaissa-Trouw, B.J., Hesselink, W., Rijke, E., Schrier, G., Hensen, E.J., Induction of anti-viral immune responses by immunization with recombinant-DNA encoded avian coronavirus nucleocapsid protein (1992) Vaccine, 10, pp. 119-124; Box, P.G., Beresford, A.W., Roberts, B., Protection of laying hens against infectious bronchitis with inactivated emulsion vaccines (1980) The Veterinary Record, 106, pp. 264-268; Box, P.G., Ellis, K.R., Infectious bronchitis in laying hens: Interference with response to emulsion vaccine by attenuated live vaccine (1985) Avian Pathologyogy, 14, pp. 9-22; Bumstead, N., Huggins, M.B., Cook, J.K.A., Genetic differences in susceptibility to a mixture of avian infectious bronchitis virus and Escherichia coli (1989) British Poultry Science, 30, pp. 39-48; Casais, R., Thiel, V., Siddell, S., Cavanagh, D., Britton, P., A reverse genetics system for the avian coronavirus infectious bronchitis virus (2001) Journal of Virology, 75, pp. 12359-12369; Casais, R., Dove, B., Cavanagh, D., Britton, P., A recombinant avian infectious bronchitis virus expressing a heterologous spike gene demonstrates that the spike protein is a determinant of cell tropism (2003) Journal of Virology, 77, pp. 9084-9089; Cavanagh, D., Coronavirus IBV: Structural characterisation of the spike protein (1983) Journal of General Virology, 64, pp. 2577-2583; Cavanagh, D., The coronavirus surface glycoprotein (1995) The Coronaviridae, pp. 73-113. , S.G. 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"Veiga E., De Lorenzo V., Fernández L.A.","8932432200;7005588312;16238777700;","Neutralization of Enteric Coronaviruses with Escherichia coli Cells Expressing Single-Chain Fv-Autotransporter Fusions",2003,"Journal of Virology","77","24",,"13396","13398",,18,"10.1128/JVI.77.24.13396-13398.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344304569&doi=10.1128%2fJVI.77.24.13396-13398.2003&partnerID=40&md5=f7d1f5c8b00a954beee2085a4966603a","Dept. of Microbial Biotechnology, Ctro. Nacional de Biotecnologia CSIC, Campus de Cantoblanco, 28049 Madrid, Spain","Veiga, E., Dept. of Microbial Biotechnology, Ctro. Nacional de Biotecnologia CSIC, Campus de Cantoblanco, 28049 Madrid, Spain; De Lorenzo, V., Dept. of Microbial Biotechnology, Ctro. Nacional de Biotecnologia CSIC, Campus de Cantoblanco, 28049 Madrid, Spain; Fernández, L.A., Dept. of Microbial Biotechnology, Ctro. Nacional de Biotecnologia CSIC, Campus de Cantoblanco, 28049 Madrid, Spain","We report here that fusions of single-chain antibodies (scFvs) to the autotransporter β domain of the IgA protease of Neisseria gonorrhoeae are instrumental in locating virus-neutralizing activity on the cell surface of Escherichia coli. E. coli cells displaying scFvs against the transmissible gastroenteritis coronavirus on their surface blocked in vivo the access of the infectious agent to cultured epithelial cells. This result raises prospects for antiviral strategies aimed at hindering the entry into target cells by bacteria that naturally colonize the same intestinal niches.",,"antibody scFvs; immunoglobulin A; unclassified drug; virus antibody; antiviral activity; article; bacterial cell; cell surface; Coronavirus; epithelium cell; Escherichia coli; gastroenteritis; Neisseria gonorrhoeae; nonhuman; priority journal; protein expression; virus neutralization; Animals; Antibodies, Viral; Cells, Cultured; Escherichia coli; Immunoglobulin Fragments; Neisseria gonorrhoeae; Neutralization Tests; Recombinant Fusion Proteins; Serine Endopeptidases; Swine; Transmissible gastroenteritis virus","Brandon, L.D., Goldberg, M.B., Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA (2001) J. 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Biol., 246, pp. 28-34; Sola, I., Castilla, J., Pintado, B., Sanchez-Morgado, J.M., Whitelaw, B., Clark, J., Enjuanes, L., Transgenic mice secreting coronavirus neutralizing antibodies into the milk (1998) J. Virol., 72, pp. 3762-3772; Staats, H.F., Jackson, R.J., Marinaro, M., Takahashi, I., Kiyono, H., McGhee, J.R., Mucosal immunity to infection with implications for vaccine development (1994) Curr. Opin. Immunol., 6, pp. 572-583; Valls, M., Atrian, S., De Lorenzo, V., Fernandez, L.A., Engineering a mouse metallothionein on the cell surface of Ralstonia eutropha CH34 for immobilization of heavy metals in soil (2000) Nat. Biotechnol., 18, pp. 661-665; Veiga, E., De Lorenzo, V., Fernandez, L.A., Probing secretion and translocation of a beta-autotransporter using a reporter single-chain Fv as a cognate passenger domain (1999) Mol. Microbiol., 33, pp. 1232-1243; Veiga, E., Sugawara, E., Nikaido, H., De Lorenzo, V., Fernandez, L.A., Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains (2002) EMBO J., 21, pp. 2122-2131; Worn, A., Plückthun, A., Stability engineering of antibody single-chain Fv fragments (2001) J. Mol. Biol., 305, pp. 989-1010","De Lorenzo, V.; Dept. of Microbial Biotechnology, Ctro. Nacional de Biotecnologia CSIC, Campus de Cantoblanco, 28049 Madrid, Spain; email: vdlorenzo@cnb.uam.es",,,0022538X,,JOVIA,"14645594","English","J. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0344304569
"Shi Y., Yi Y., Li P., Kuang T., Li L., Dong M., Ma O., Cao C.","57199386357;7202372661;56461680300;7004899914;55768805700;57199850479;7004452840;7401501779;","Diagnosis of Severe Acute Respiratory Syndrome (SARS) by Detection of SARS Coronavirus Nucleocapsid Antibodies in An Antigen-Capturing Enzyme-Linked Immunosorbent Assay",2003,"Journal of Clinical Microbiology","41","12",,"5781","5782",,70,"10.1128/JCM.41.12.5781-5782.2003","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347423199&doi=10.1128%2fJCM.41.12.5781-5782.2003&partnerID=40&md5=626ffbfd79e7d8e13a45765d995499a8","Beijing Institute of Biotechnology, Beijing 100850, China; Gen. Hospital of Guangzhou Command, Guangzhou 510010, China; 309 Army Hospital, Beijing 100083, China; Beijing Institute of Biotechnology, 27 Taiping Rd., Beijing 100850, China","Shi, Y., Beijing Institute of Biotechnology, Beijing 100850, China, Gen. Hospital of Guangzhou Command, Guangzhou 510010, China; Yi, Y., Beijing Institute of Biotechnology, Beijing 100850, China; Li, P., Beijing Institute of Biotechnology, Beijing 100850, China; Kuang, T., 309 Army Hospital, Beijing 100083, China; Li, L., Gen. Hospital of Guangzhou Command, Guangzhou 510010, China; Dong, M., 309 Army Hospital, Beijing 100083, China; Ma, O., Beijing Institute of Biotechnology, Beijing 100850, China; Cao, C., Beijing Institute of Biotechnology, Beijing 100850, China, Beijing Institute of Biotechnology, 27 Taiping Rd., Beijing 100850, China","Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein was employed to establish an antigen-capturing enzyme-linked immunosorbent assay (ELISA). Antinucleocapsid protein antibodies could be detected in 68.4% of probable SARS patients 6 to 10 days after illness and in 89.6% of the patients 11 to 61 days after illness. No false-positive results were observed in 20 non-SARS fever patients, 24 non-SARS respiratory illness patients, and 20 health care workers. Among 940 other non-SARS clinical serum samples, only 1 was found to be weakly positive. This method provides a new, sensitive, and specific approach for SARS diagnosis.",,"nucleocapsid protein; nucleocapsid protein antibody; protein antibody; recombinant protein; unclassified drug; virus antigen; antibody detection; article; enzyme linked immunosorbent assay; fever; health care personnel; human; nucleotide sequence; priority journal; SARS coronavirus; sensitivity and specificity; serodiagnosis; severe acute respiratory syndrome; Antibodies, Viral; Base Sequence; DNA Primers; Enzyme-Linked Immunosorbent Assay; Humans; Nucleocapsid; Polymerase Chain Reaction; SARS Virus; Severe Acute Respiratory Syndrome; Coronavirus; RNA viruses; SARS coronavirus","Ducan, R.J.S., The use of ELISA for rapid viral diagnosis: Antibody detection (1988) ELISA and Other Solid Phase Immunoassays. Theoretical and Practical Aspects, pp. 309-310. , D. M. Kemeny and S. J. Challacombe (ed.). John Wiley & Sons, New York, N.Y; Hon, K.L.E., Li, A.M., Cheng, F.W.T., Personal view of SARS: Confusing definition, confusing diagnosis (2003) Lancet, 361, pp. 1984-1985; Ksiazek, T., Technology in SARS discovery (2003) SARS in the Context of Emerging Infectious Threats: A New York Academy of Sciences Conference, May 17, 2003, pp. 22-26. , http://www.nyas.columbia.edu/sars/web/s8/conference_transcript.pdf, [Online.] New York, N.Y; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404","Cao, C.; Beijing Institute of Biotechnology, 27 Taiping Rd., Beijing 100850, China; email: caoc@nic.bmi.ac.cn",,,00951137,,JCMID,"14662982","English","J. Clin. Microbiol.",Article,"Final",Open Access,Scopus,2-s2.0-0347423199
"Huang D.-Z., Lang Z.-W., Wen T., He L.-X., Xie L., Zhou Y.-S.","7403891319;7005478031;57202926700;7403374259;57198836637;37025005900;","Detection of SARS coronavirus RNA in lung tissues from patients with severe acute respiratory syndrome by in situ reverse transcription polymerase chain reaction",2003,"Chinese Journal of Microbiology and Immunology","23","12",,"926","929",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542349284&partnerID=40&md5=9cfa2289c980b610b367019c1811d172","Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China","Huang, D.-Z., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; Lang, Z.-W., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; Wen, T., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; He, L.-X., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; Xie, L., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; Zhou, Y.-S., Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China","Objective: To identify the location and distribution of SARS coronavirus RNA in lung tissues samples of patients with severe acute respiratory syndrome. Methods: Postmortem lung tissues of three patients were studied by in situ RT-PCR methods. Lung tissue sections were carefully placed on poly-L-lysine-coated glass slides to be target cells, Digoxigenin-dNTP labeling was mixed into the PCR reaction system to make the amplified genomic DNA product with Dig labeling material. The positive SARS RNA signals were seen as small blue-purple particles inside the cells. Results: Among the three cases, the positive signals of SARS nucleic acids were found in two lung samples. These signals were identified nuclei or cytoplasma of cells. The positive cells were predominantly scattered among the epithelium cells of lung alveolus or bronchia and monocytes of alveoli interval. The inflammation reaction was obvious in lung tissues with alveolar damages: red cells leakage, diffuse exudation, increase of monocytes in the interval at various degree severity. Conclusion: The detection of SARS nucleic acid signals from lung tissues of SARS infected patients may offer a direct approach of etiological diagnosis.","In situ reverse transcription polymerase chain reaction(in situ RT-PCR); Lung tissues; SARS coronavirus; Severe acute respiratory syndrome (SARS)","nucleic acid; polylysine; virus RNA; adult; aged; article; case report; cytoplasm; disease severity; female; human; human cell; human tissue; lung alveolus epithelium; lung parenchyma; male; monocyte; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; signal transduction; virus detection","Chinese source; Chinese source; Chinese source; Chinese source; Chinese source","Huang, D.-Z.; Beijing Munic. Hepatitis Institute, Beijing You'an Hospital, Cap. University of Medical Sciences, Beijing 100054, China; email: wentao528@tom.com",,,02545101,,ZWMZD,,"Chinese","Chin. J. Microbiol. Immunol.",Article,"Final",,Scopus,2-s2.0-1542349284
"Ng M.-L., Tan S.-H., See E.-E., Ooi E.-E., Ling A.-E.","36747598400;55455679900;6602403458;7004519587;7102194546;","Proliferative growth of SARS coronavirus in Vero E6 cells",2003,"Journal of General Virology","84","12",,"3291","3303",,60,"10.1099/vir.0.19505-0","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0348013197&doi=10.1099%2fvir.0.19505-0&partnerID=40&md5=2b71cfd32ae82a06c6e619d0a75f7cce","Department of Microbiology, Electron Microscopy Unit, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore; Faculty of Medicine, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore; Environmental Health Institute, National Environmental Agency, Singapore, Singapore; Department of Pathology, Singapore General Hospital, Singapore, Singapore","Ng, M.-L., Department of Microbiology, Electron Microscopy Unit, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore, Faculty of Medicine, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore; Tan, S.-H., Faculty of Medicine, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore; See, E.-E., Environmental Health Institute, National Environmental Agency, Singapore, Singapore; Ooi, E.-E., Environmental Health Institute, National Environmental Agency, Singapore, Singapore; Ling, A.-E., Department of Pathology, Singapore General Hospital, Singapore, Singapore","An isolate of SARS coronavirus (strain 2003VA2774) was obtained from a patient and used to infect Vero E6 cells. The replication cycle of the virus was followed from 1 to 30 h post-infection (p.i.). It was surprising to observe the swift growth of this human virus in Vero cells. Within the first hour of infection, the most obvious ultrastructural change was the proliferation of the Golgi complexes and related vesicles accompanied by swelling of some of the trans-Golgi sacs. Extracellular virus particles were present by 5 h p.i. in about 5 % of the cells and this increased dramatically to about 30 % of the cell population within an hour (6 h p.i.). Swollen Golgi sacs contained virus nucleocapsids at different stages of maturation. These virus precursors were also in large vacuoles and in close association with membrane whorls. The membrane whorls could be the replication complexes, since they appeared rather early in the replication cycle. As infection progressed from 12 to 21 h p.i., the cytoplasm of the infected cells was filled with numerous large, smooth-membraned vacuoles containing a mixture of mature virus and spherical cores. Several of these vacuoles were close to the cell periphery, ready to export out the mature progeny virus particles via exocytosis. By 24 to 30 h p.i., crystalline arrays of the extracellular virus particles were seen commonly at the cell surface.",,"animal cell; article; cell maturation; cell membrane; cell population; cell proliferation; cell surface; cell vacuole; controlled study; Coronavirus; cytoplasm; exocytosis; Golgi complex; human; human cell; nonhuman; priority journal; progeny; SARS coronavirus; Vero cell; virogenesis; virus isolation; virus nucleocapsid; virus particle; virus replication; virus strain; Animals; Cell Membrane; Cercopithecus aethiops; Cytoplasm; Golgi Apparatus; Humans; Microscopy, Electron; SARS Virus; Species Specificity; Time Factors; Vero Cells; Virus Replication; Animalia; Apus apus; Coronavirus; RNA viruses; SARS coronavirus","Chaloner-Larsson, G., Johnson-Lussenburg, C.M., Establishment and maintenance of a persistent infection of L123 cells by human coronavirus strain 299E (1981) Arch. Virol., 69, pp. 117-129; David-Ferreira, J.F., Manaker, R.A., An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells (1965) J. Cell Biol., 24, pp. 57-78; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976. , & 23 other authors; Fleming, J.O., Trousdale, M.D., Stohlman, S.A., Weiner, L.P., Pathogenic characteristics of neutralization-resistant variants of JHM coronavirus (MHV-4) (1987) Adv. Exp. Med. Biol., 218, pp. 333-342; Fleming, J.O., el-Zaatari, F.A., Gilmore, W., Berne, J.D., Burks, J.S., Stohlman, S.A., Tourtellotte, W.W., Weiner, L.P., Antigenic assessment of coronaviruses isolated from patients with multiple sclerosis (1988) Arch. Neurol., 45, pp. 629-633; Frana, M.F., Behnke, J.N., Sturman, L.S., Holmes, K.V., Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion (1985) J. Virol., 56, pp. 912-920; Holmes, K.V., Coronaviridae and their replication (1990) Virology, pp. 841-856. , 2nd edition, Edited by B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, T. P. Monath, J. L. Melnick, B. Roizman & S. E. Straus. New York: Raven Press; Holmes, K.V., Behnke, J.N., Evolution of a coronavirus during persistent infection in vitro (1981) Adv. Exp. Med. Biol., 142, pp. 287-299; Holmes, K.V., Doller, E.W., Behnke, J.N., Analysis of the functions of coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin (1981) Adv. Exp. Med. Biol., 142, pp. 133-142; Holmes, K.V., Doller, E.W., Sturman, L.S., Tunicamycin resistant glycosylation of coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein (1981) Virology, 115, pp. 334-344; Holmes, K.V., Frana, M.F., Robbins, S.G., Sturman, L.S., Coronavirus maturation (1984) Adv. Exp. Med. Biol., 173, pp. 37-52; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966. , & 23 other authors; Lamontagne, L.M., Dupuy, J.M., Persistent infection with mouse hepatitis virus 3 in mouse lymphoid cell lines (1984) Infect. Immun., 44, pp. 716-723; Luby, J.P., Clinton, R., Kurtz, S., Adaptation of human enteric coronavirus to growth in cell lines (1999) J. Clin. Virol., 12, pp. 43-51; Lucas, A., Coulter, M., Anderson, R., Dales, S., Flintoff, W., In vivo and in vitro models of demyelinating diseases. II. Persistence and host-regulated thermosensitivity in cells of neural derivation infected with mouse hepatitis and measles viruses (1978) Virology, 88, pp. 325-337; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , & 56 other authors; Ng, M.-L., Tan, S.-H., See, E.-E., Ooi, E.-E., Ling, A.-E., Entry and early events of severe acute respiratory syndrome coronavirus (2003) J. Med. Virol., 71, pp. 323-331; Oshiro, L.S., Coronaviruses (1973) Ultrastructure of Animal Viruses and Bacteriophages: an Atlas, pp. 331-343. , Edited by A. J. Dalton & F. Haguenau. Orlando: Academic Press; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , & 32 other authors; Ruan, Y.J., Wei, C.L., Ling, A.-E., Comparative full length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1785. , & 17 other authors. erratum 361, 1832; Sturman, L.S., Takemoto, K.K., Enhanced growth of a murine coronavirus in transformed mouse cells (1972) Infect. Immun., 6, pp. 501-507; Sturman, L.S., Holmes, K.V., The molecular biology of coronaviruses (1983) Adv. Virus Res., 28, pp. 35-112; Sturman, L.S., Holmes, K.V., Behnke, J., Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid (1980) J. Virol., 33, pp. 449-462; Sussman, M.A., Fleming, J.O., Allen, H., Stohlman, S.A., Immune mediated clearance of JHM virus from the central nervous system (1987) Adv. Exp. Med. Biol., 218, pp. 399-410; Tooze, J., Tooze, S.A., Infection of AtT20 murine pituitary tumor cells by mouse hepatitis virus strain A59: Virus budding is restricted to the Golgi region (1985) Eur. J. Cell Biol., 37, pp. 203-212; Tooze, J., Tooze, S.A., Warren, G., Replication of coronavirus MHV-A59 in sac- cells: Determination of the first site of budding of progeny virions (1984) Eur. J. Cell Biol., 33, pp. 281-293; Wege, H., Siddell, S., ter Meulen, V., The biology and pathogenesis of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 165-200; Wilhelmsen, K.C., Leibowitz, J.L., Bond, C.W., Robb, J.A., The replication of murine coronaviruses in enucleated cells (1981) Virology, 110, pp. 225-230","Ng, M.-L.; Department of Microbiology, Electron Microscopy Unit, National University of Singapore, 5 Science Drive 2, 117597 Singapore, Singapore; email: micngml@nus.edu.sg",,,00221317,,JGVIA,"14645910","English","J. Gen. Virol.",Article,"Final",Open Access,Scopus,2-s2.0-0348013197
"Wu J.-X., Zhou J.-Y., Zhou X.-P.","56093911200;13003901200;55743222700;","Transgenic Potato Containing Immunogenic Gene of Avian Coronavirus and Its Immunogenicity in Mice",2003,"Acta Biochimica et Biophysica Sinica","35","11",,"1011","1015",,1,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346847626&partnerID=40&md5=affa97ced451702b76f274e08d6e8658","Inst. of Prev. Veterinary Medicine, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China; Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China","Wu, J.-X., Inst. of Prev. Veterinary Medicine, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China; Zhou, J.-Y., Inst. of Prev. Veterinary Medicine, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China; Zhou, X.-P., Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China","To check the feasibility of expression of the immunogenic gene of avian coronavirus infectious bronchitis virus (IBV) in plants, the transformation of S1 gene of IBV into potato and the immunogenicity of its expression product was studied. The S1 gene of IBV-ZJ971 strain was inserted into plasmid pBI121 under the control of 35 S promoter. Agrobacterium fumefaciens EHA105 with the recombinant vector pBI121 was obtained by tri-parental mating method. So, an efficient potato transformation system mediated by Agrobacterium fumefaciens was established. The rates of calli and shoots differentiation were 100%, and more than 95% respectively, for transgenic potato with S1 gene of IBV. PCR and Southern blot analyses showed that IBV S1 gene was integrated into genomic DNA of the potato plant and most transgenic plants had two copies of S1 gene of IBV. In our experiments, 47 transgenic plantlets have been obtained. Northern blot and ELISA analyses indicated that most transgenic plants could normally transcribe and translate S1 gene of IBV, though the levels of transcription and translation were different in various transgenic plants. Immunity assay with BALB/C mice showed that expression products of transgenic potato with S1 gene of IBV were immunogenic, and ELISA antibody titer reached 1:20 to 1:40 and 1:80 to 1:160 with doses of 0.5 g and 1 g, respectively. Virus neutralization (VN) antibodies were detected by tracheal organ cultures, and the results showed that VN titers reached respectively 1:160 to 1:320 and 1:320 to 1:2048 with doses of 0.5 g and 1 g.","Chicken; Coronavirus; Immunogenic gene; Immunogenicity; Transgenic potato","genomic DNA; neutralizing antibody; Agrobacterium tumefaciens; animal tissue; antibody detection; antibody titer; article; Avian infectious bronchitis virus; Coronavirus; enzyme linked immunosorbent assay; expression vector; feasibility study; fowl; gene expression; gene insertion; genetic transcription; genetic transformation; immunity; immunogenetics; immunogenicity; mouse; nonhuman; Northern blotting; organ culture; plasmid vector; polymerase chain reaction; potato; promoter region; RNA translation; shoot; Southern blotting; trachea; transgenic plant; virus gene; virus neutralization; virus strain; Animals; Antibodies, Viral; Blotting, Northern; Blotting, Southern; Culture Techniques; DNA, Plant; Gene Expression; Infectious bronchitis virus; Membrane Glycoproteins; Mice; Mice, Inbred BALB C; Neutralization Tests; Plants, Genetically Modified; RNA, Plant; Solanum tuberosum; Transformation, Genetic; Viral Envelope Proteins; Agrobacterium; Agrobacterium tumefaciens; Animalia; Aves; Avian infectious bronchitis virus; Coronavirus; Galliformes; Gallus gallus; Solanum tuberosum","Schalk, A.F., Hawn, M.C., An apparently new respiratory disease of baby chicks (1931) J Am Vet Med Assoc, 78, pp. 413-422; Zhou, J.Y., Analyses of construction proteins and S1 gene construction of avian proventriculopathic infectious bronchitis virus Chinese isolate ZJ971 (2000) Chinese J Vet Sci, 20 (5), pp. 428-433; Caplan, A., Herrera-Estrella, L., Inze, D., Van Haute, E., Van Montagu, M., Schell, J., Zambryski, P., Introduction of genetic material into plant cells (1983) Science, 222 (4625), pp. 815-821; Mason, H.S., Lam, D.M., Arntzen, C.J., Expression of hepatitis B surface antigen in transgenic plants (1992) Proc Natl Acad Sci USA, 89 (24), pp. 11745-11749; Mason, H.S., Arntzen, C.J., Transgenic plants as vaccine production systems (1995) Trends Biotechnol, 13 (9), pp. 388-392; Moffat, A.S., Exploring transgenic plants as a new vaccine source (1995) Science, 268 (5211), pp. 658-660; McGarvey, P.B., Hammond, J., Dienelt, M.M., Hooper, D.C., Fu, Z.F., Dietzschold, B., Koprowski, H., Expression of the rabies virus glycoprotein in transgenic tomatoes (1995) Biotechnology, 13 (13), pp. 1484-1487; Mason, H.S., Ball, J.M., Shi, J.J., Jiang, X., Estes, M.K., Arntzen, C.J., Expression of Norwalk virus capsid protein in transgenic tobacco and potato and its oral immunogenicity in mice (1996) Proc Natl Acad Sci USA, 93 (11), pp. 5335-5340; Arakawa, T., Chong, D.K., Langridge, W.H., Efficiency of a food plant-based oral cholera toxin B subunit vaccine (1998) Nat Biotechnol, 16 (3), pp. 292-297; Haq, T.A., Mason, H.S., Clements, J.D., Arntzen, C.J., Oral immunization with a recombinant bacterial antigen produced in transgenic plants (1995) Science, 268 (5211), pp. 714-716; Tacket, C.O., Mason, H.S., A review of oral vaccination with transgenic vegetables (1999) Microbes Infect, 1 (10), pp. 777-783; Gomez, N., Carrillo, C., Salinas, J., Parra, F., Broca, M.V., Escribano, J.M., Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants (1998) Virology, 249 (2), pp. 352-358; Gomez, N., Wigdorovitz, A., Castanon, S., Gil, F., Ordas, R., Borca, M.V., Escribano, J.M., Oral immunogenicity of the plant derived spike protein from swine-transmissible gastroenteritis coronavirus (2000) Arch Virol, 145 (8), pp. 1725-1732; Streatfield, S.J., Jilka, J.M., Hood, E.E., Turner, D.D., Bailey, M.R., Mayor, J.M., Woodard, S.L., Plant-based vaccines: Unique advantages (2001) Vaccine, 19 (17-19), pp. 2742-2748; Fu, R.Z., Sun, Y.R., Jia, S.R., (1994) Plant Genetic Transformation, p. 132. , Beijing: Chinese Science and Technology Press; Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K., (1995) Short Protocols in Molecular Biology, 3rd Ed., , New York: John Wiley&Sons Inc; Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., , New York: Cold Spring Harbor Laboratory Press; Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254; Zhou, J.Y., Wu, J.X., Cheng, L.Q., Zheng, X.J., Gong, H., Shang, S.B., Zhou, E.M., Expression of immunogenic S1 glycoprotein of infectious bronchitis virus in transgenic potato (2003) J Virol, 77, pp. 9090-9093; Wang, G.Q., Wang, Y.Z., Yang, J.S., Qian, M., Ge, K., Abnormal expression of foreign genes in transgenic Solanum tuberosum (1997) Journal of Fudan University (Natural Science), 36 (5), pp. 537-542; Twell, D., Ooms, G., The 5′ flanking DNA of a patatin gene directs tuber-specific expression of a chimaeric gene in potato (1987) Plant Mol Biol, 9, pp. 365-375","Zhou, J.-Y.; Inst. of Prev. Veterinary Medicine, Institute of Biotechnology, Zhejiang University, Hangzhou 310029, China; email: jyzhou@zju.edu.cn",,,05829879,,,"14614539","Chinese","Acta Biochim. Biophys. Sin.",Article,"Final",,Scopus,2-s2.0-0346847626
"Ng E.K.O., Hui D.S., Chan K.C.A., Hung E.C.W., Chiu R.W.K., Lee N., Wu A., Chim S.S.C., Tong Y.K., Sung J.J.Y., Tam J.S., Lo Y.M.D.","21135553700;7101862411;13403797200;7004256338;7103038413;55503117200;7402998681;6701728226;7202614141;35405352400;24788939600;7401935391;","Quantitative Analysis and Prognostic Implication of SARS Coronavirus RNA in the Plasma and Serum of Patients with Severe Acute Respiratory Syndrome",2003,"Clinical Chemistry","49","12",,"1976","1980",,76,"10.1373/clinchem.2003.024125","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345411820&doi=10.1373%2fclinchem.2003.024125&partnerID=40&md5=41c03feaead1679754ef026300346be2","Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing St., Shatin, New Territories, Hong Kong","Ng, E.K.O., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Hui, D.S., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Chan, K.C.A., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Hung, E.C.W., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Chiu, R.W.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Lee, N., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Wu, A., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Chim, S.S.C., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Tong, Y.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Sung, J.J.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Tam, J.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China; Lo, Y.M.D., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, China, Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing St., Shatin, New Territories, Hong Kong","Background: The availability of an early diagnostic tool for severe acute respiratory syndrome (SARS) would have major public health implications. We investigated whether the SARS coronavirus (SARS-CoV) can be detected in serum and plasma samples during the early stages of SARS and studied the potential prognostic implications of such an approach. Methods: We developed two real-time quantitative reverse transcription-PCR (RT-PCR) assays, one for the polymerase and the other for the nucleocapsid region of the virus genome, for measuring the concentration of SARS-CoV RNA in serum/plasma samples from SARS patients. Plasma samples were obtained from 12 confirmed SARS patients on the day of hospital admission, as well as on days 7 and 14 after fever onset. Serum samples were also obtained from 23 confirmed SARS patients on the day of hospital admission, 11 of whom subsequently required intensive care. Viral RNA was extracted from the plasma/serum samples. The extracted RNA was subjected to analysis by the RT-PCR assays. Results: The RT-PCR system for the polymerase region detected SARS-CoV RNA in 50% of plasma and 78% of serum samples from SARS patients during the first week of illness. The detection rates for plasma dropped to 25% at day 14 after fever onset. The median serum SARS-CoV concentrations in patients who required and did not require intensive care unit admission during the course of hospitalization were 5800 and 140 copies/mL, respectively (Mann-Whitney test, P <0.005). These data were confirmed by the RT-PCR system for the nucleocapsid region, which showed an even higher detection rate of 87%. The correlation between the results obtained by the two RT-PCR systems was high (Pearson correlation analysis, r = 0.998; P <0.001). Conclusion: Plasma/serum SARS-CoV quantification represents a potentially useful early diagnostic and prognostic tool for SARS. © 2003 American Association for Clinical Chemistry.",,"analytic method; article; blood sampling; clinical article; concentration response; controlled study; Coronavirus; correlation analysis; disease course; hospital admission; hospitalization; human; intensive care unit; nucleotide sequence; prognosis; quantitative analysis; rank sum test; respiratory tract disease; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; virus detection; virus genome; virus nucleocapsid; Humans; Prognosis; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Coronavirus; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poon, L.L., Wong, O.K., Luk, W., Yuen, K.Y., Peiris, J.S., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 953-955; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Damond, F., Descamps, D., Farfara, I., Telles, J.N., Puyeo, S., Campa, P., Quantification of proviral load of human immunodeficiency virus type 2 subtypes a and B using real-time PCR (2001) J Clin Microbiol, 39, pp. 4264-4268; White, P.A., Pan, Y., Freeman, A.J., Marinos, G., Ffrench, R.A., Lloyd, A.R., Quantification of hepatitis C virus in human liver and serum samples by using LightCycler reverse transcriptase PCR (2002) J Clin Microbiol, 40, pp. 4346-4348; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Tsui, S.K., Chim, S.S., Lo, Y.M.D., Coronavirus genomic-sequence variations and the epidemiology of the severe acute respiratory syndrome (2003) N Engl J Med, 349, pp. 187-188","Lo, Y.M.D.; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30-32 Ngan Shing St., Shatin, New Territories, Hong Kong; email: loym@cuhk.edu.hk",,,00099147,,CLCHA,"14633867","English","Clin. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0345411820
"Liu S., Guo T., Ji X., Sun Z.","7409459255;57199360693;7402840255;7404239472;","Bioinformatical study on the proteomics and evolution of SARS-CoV",2003,"Chinese Science Bulletin","48","13",,"1277","1287",,5,"10.1360/03wc0276","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1242313117&doi=10.1360%2f03wc0276&partnerID=40&md5=c8b1aafbe0fdb0513f81e54e86c237ff","Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China","Liu, S., Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China; Guo, T., Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China; Ji, X., Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China; Sun, Z., Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China","A novel coronavirus has been identified as the causative agent of the severe acute respiratory syndrome (SARS). For all the SARS-CoV associated proteins derivated from the SARS-CoV genome, the physiochemical properties such as the molecular weight, isoelectric point and extinction coefficient of each protein were calculated. The transmembrane segments and subcellular localization (SubLocation) prediction and conserved protein motifs search against database were employed to analyze the function of SARS-CoV proteins. Also, the homology protein sequence alignment and evolutionary distance matrix calculation between SARS-CoV associated proteins and the corresponding proteins of other coronaviruses were employed to identify the classification and phylogenetic relationship between SARS-CoV and other coronaviruses. The results showed that SARS-CoV is a novel coronavirus which is different from any of the three previously known groups of coronviruses, but it is closer to Bo-CoV and MHV than to other coronaviruses. This study is in aid of experimental determination of SARS-CoV proteomics and the development of antiviral vaccine.","Conserved protein motif; Evolution; SARS; SARS-CoV; Sequence alignment","Coronavirus; Murine hepatitis virus; SARS coronavirus","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1947-1958; Qin, E.D., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of strain (BJO1) of SARS-associated virus (2003) Chinese Science Bulletin, 48, pp. 941-948; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Jun, R.Y., Lin, W.C., Ling, A.E., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolateds and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1790; Gallagher, T.M., Buchmeier, M.J., Coronavirus spike protein in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Bonavia, A., Zelus, B.D., Wentworth, D.E., Identification of a receptor binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Garoff, H., Hewson, R., Opstelten, D.J., Virus maturation by budding, Microbiol (1998) Mol. Biol. Rev., 62, pp. 1171-1190; Boeckmann, B., Bairoch, A., Apweiler, R., The Swiss-Prot protein knowledgebase and its supplement TrEMBL in 2003 (2003) Nucleic. Acids. Res., 31, pp. 365-370; Herold, J., Raabe, T., Schelle-Prinz, B., Nucleotide sequence of the human coronavirus 229E RNA polymerase locus (1993) Virology, 195, pp. 680-691; Brendel, V., Bucher, P., Nourbakhsh, I., Methods and algorithms for statistical analysis of protein sequences (1992) Proc. Natl. Acad. Sci. USA., 89, pp. 2002-2006; Subramaniam, S., The biology workbench - A seamless database and analysis environment for the biologist (1998) Proteins, 32, pp. 1-2; Persson, B., Argos, P., Prediction of transmembrane segments in proteins utilising multiple sequence alignments (1994) J. Mol. Biol., 237, pp. 182-192; Sonnhammer, E.L., Von Heijne, G., Krogh, A., A hidden Markov model for predicting transmembrane helices in protein sequences (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol., 6, pp. 175-182; Bateman, A., Birney, E., Cerruti, L., The Pfam protein families database (2002) Nucleic Acids Res., 30, pp. 276-280; Wallace, J.C., Henikoff, S., PATMAT: A searching and extraction program for sequence, pattern and block queries and databases (1992) Comput. Appl. Biosci., 8, pp. 249-254; Altschul, S.F., Madden, T.L., Schaffer, A.A., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic. Acids. Res., 25, pp. 3389-3402; Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic. Acids. Res., 22, pp. 4673-4680; Felsenstein, J., PHYLIP - Phylogeny Inference Package (Version 3.2) (1989) Cladistics, 5, pp. 164-166; Saraste, M., Sibbald, P.R., Wittinghofer, A., The P-loop - A common motif in ATP- and GTP-binding proteins (1990) Trends. Biochem. Sci., 15, pp. 430-434; Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein (1982) J. Mol. Biol., 157, pp. 105-132; Bonavia, A., Zelus, B.D., Wentworth, D.E., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Ortego, J., Escors, D., Laude, H., Generation of a replication-competent, propagation-deficient virus vector based on the transmissible gastroenteritis coronavirus genome (2002) J. Virol., 76, pp. 11518-11529; Kuo, L., Masters, P.S., The small envelope protein E is not essential for murine coronavirus replication (2003) J Virol., 77, pp. 4597-4608; Cyranoskiand, D., Abbott, A., Virus detectives seek source of SARS in China's wild animals (2003) Nature, 423, p. 467","Sun, Z.; Institute of Bioinformatics, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China; email: sunzhr@mail.tsinghua.edu.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Review,"Final",,Scopus,2-s2.0-1242313117
"Qi Z., Hu Y., Li W., Chen Y., Zhang Z., Sun S., Lu H., Zhang J., Bu D., Ling L., Chen R.","55118867700;55338013500;57201905416;55870438000;55721800700;7404509946;56131256200;7601357257;7003550200;7202813605;8587708000;","Phylogeny of SARS-CoV as inferred from complete genome comparison",2003,"Chinese Science Bulletin","48","12",,"1175","1178",,9,"10.1360/03wc0253","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1242335650&doi=10.1360%2f03wc0253&partnerID=40&md5=d069d99fa42ba90a8f65dc47fd9bd466","Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China","Qi, Z., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Hu, Y., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Li, W., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China; Chen, Y., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Zhang, Z., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Sun, S., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Lu, H., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Zhang, J., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Bu, D., Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China; Ling, L., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Chen, R., Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, Institute of Computing Technology, Chinese Academy of Sciences, Beijing 100080, China, Beijing Genomics Institute, Chinese Academy of Sciences, Beijing 101300, China","SARS-CoV, as the pathogeny of severe acute respiratory syndrome (SARS), is a mystery that the origin of the virus is still unknown even a few isolates of the virus were completely sequenced. To explore the genesis of SARS-CoV, the FDOD method previously developed by us was applied to comparing complete genomes from 12 SARS-CoV isolates to those from 12 previously identified coronaviruses and an unrooted phylogenetic tree was constructed. Our results show that all SARS-CoV isolates were clustered into a clique and previously identified coronaviruses formed the other clique. Meanwhile, the three groups of coronaviruses depart from each other clearly in our tree that is consistent with the results of prevenient papers. Differently, from the topology of the phylogenetic tree we found that SARS-CoV is more close to group 1 within genus coronavirus. The topology map also shows that the 12 SARS-CoV isolates may be divided into two groups determined by the association with the SARS-CoV from the Hotel M in Hong Kong that may give some information about the infectious relationship of the SARS.","Coronavirus; Function of degree of disagreement (FOOD); Infection relationship; Phytogeny; SARS-associated coronavirus (SARS-CoV)","Coronavirus; SARS coronavirus","Marra, M.A., Jones, S.J., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, 300 (5624), pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe Stephan, S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300 (5624), pp. 1394-1399; Ruan, Y.J., Wei, C.L., Ee, L.A., Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361 (9371), pp. 1779-1785; Qin, E.D., Zhu, Q.Y., Wang, J., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Enjuanes, L., Brian, D., Cavanagh, D., Coronaviridae (2000) Virus Taxonomy, Classification and Nomenclature of Viruses, pp. 835-849. , (eds. van Regenmortel, M. H. V., Fauquet, C. M., Bishop, D. H. L. et al.), New York: Academic Press; Lai, M.M.C., Holmes, K.V., Coronavmidae: The viruses and their replication (2001) Fields Virology, p. 1163. , (eds. Knipe, D. M., Howley, P. M.), 4th ed., New York: Lippincott Williams and Wilkins; Bush, R.M., Smith, C.B., Cox, N.J., Effects of passage history and sampling bias on phylogenetic reconstruction of human influenza a evolution (2000) Proc. Natl. Acad. Sci. USA, 7, pp. 6974-6980; Fang, W.W., The characterization of a measure of information discrepancy (2000) Information Sciences, 125, pp. 207-232; Li, W., Fang, W.W., Ling, L.J., Phylogeny based on whole genome as inferred from complete information set analysis (2002) Journal of Biological Physics, 28 (3), pp. 439-449; Wu, C.F.J., Jackknife, bootstrap and other resampling plans in regression analysis (1986) Annals of Statistics, 14, pp. 1261-1295; Hillis, D.M., Bull, J.J., An emprical test of bootstrapping as a method for assessing confidence in phylogenetic analysis (1993) Syst. Biol., 42, pp. 182-192; John, G., Rob, D., Ward, W., Alignment-ambiguous nucleotide sites and the exclusion of systematic data (1993) Mol. Phylogenet. Evol., 2, pp. 152-157; Ward, W., John, G., Rob, D., Elision: A method for accommodating multiple molecular sequence alignments with alignment-ambiguous sites (1995) Mol. Phylogenet. Evol., 4, pp. 1-9; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Rannala, B., Huelsenbeck, J.P., Yang, Z., Taxon sampling and the accuracy of large phytogenies (1998) Syst. Biol., 47, pp. 702-710","Chen, R.; Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; email: crs@sun5.ibp.ac.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-1242335650
"Lu Y., Chen Y.","57209874685;36071613100;","Spike protein homology between the SARS-associated virus and murine hepatitis virus implies existence of a putative receptor-binding region",2003,"Chinese Science Bulletin","48","11",,"1115","1117",,3,"10.1360/03wc0197","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344459386&doi=10.1360%2f03wc0197&partnerID=40&md5=14c648cc25fd99c57086c706f8e2b530","Department of Biology, Tsinghua University, Protein Science Laboratory of Ministry of Education, Beijing 100084, China","Lu, Y., Department of Biology, Tsinghua University, Protein Science Laboratory of Ministry of Education, Beijing 100084, China; Chen, Y., Department of Biology, Tsinghua University, Protein Science Laboratory of Ministry of Education, Beijing 100084, China","Coronavirus has been determined to be the cause of the recent outbreak of severe acute respiratory syndrome (SARS). Human coronavirus 229E had been studied well and its receptor-binding domain was restricted to aa417 -547 of S protein. However, this region has no homology with the newly separated SARS-associatcd virus (Hong Kong isolate CUHK-W1). Then we analyzed the phylogenesis of S1 subunit of the coronavirus spike protein (SARS-associated virus, Hong Kong isolate CUHK-W1). Interestingly, the highest homology between murine hepatitis virus (MHV) and SARS-associated coronavirus was found. And the important sites (aa62-65 and aa214-216) on the spike protein of MHV with receptor-binding capacity were highly conservative in comparison with the newly separated SARS-associated virus (the corresponding sites are aa51-54 and aa195 -197). These results from bioinformatics analysis might help us to study the receptor-binding sites of SARS-associated virus and the mechanism of the virus entry into the target cell, and design antiviral drugs and potent vaccines.","Human coronavirus; Murine hepatitis virus; Receptor-binding sites; SARS-associated virus","Coronavirus; Human coronavirus 229E; Murine hepatitis virus; SARS coronavirus","Siddell, S., Wege, H., Ter Meulen, V., The structure and replication of coronaviruses (1982) Curr. Top. Microbiol. Immunol., 99, pp. 131-163; Holmes, K.V., Tresnan, D.B., Zelus, B.D., Virus-receptor interactions in the enteric tract, Virus-receptor interactions (1997) Adv. Exp. Med-Biol., 412, pp. 125-133; Bonavia, A., Zelus, B.D., Wentworth, D.E., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77 (4), pp. 2530-2538; Abraham, S., Kienzle, T.E., Lapps, W., Deduced sequence of the bovine coronavirus spike protein and identification of the internal proteolytic cleavage site (1990) Virology, 176 (1), pp. 296-301; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated coronavirus (2003) Science, p. 1085953; Kubo, H., Yamada, Y.K., Taguchi, F., Location of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein (1994) J. Virol., 68 (9), pp. 5403-5410; Taguchi, F., Kubo, H., Suzuki, H., Location of neutralizing epitopes and receptor-binding site in murine coronavirus spike protein (1995) Adv. Exp. Med. Biol., 380, pp. 359-365; Wessner, D.R., Shick, P.C., Lu, J.H., Mutational analysis of the virus and monoclonal antibody binding sites in MHVR, the cellular receptor of the murine coronavirus mouse hepatitis virus strain A59 (1998) J. Virol., 72 (3), pp. 1941-1948; Suzuki, H., Taguchi, F., Analysis of the receptor binding site of murine coronavirus spike glycoprotein (1996) J. Virol., 70, pp. 2632-2636; Saeki, K., Ohtsuka, N., Taguchi, F., Identification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants (1997) J. Virol., 71 (12), pp. 9024-9031; Saeki, K., Ohtsuka, N., Taguchi, F., Isolation and characterization of murine coronavirus mutants resistant to neutralization by soluble receptor (1998) Adv. Exp. Med. Biol., 440, pp. 11-16; Qin, E., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJO1) (2003) Chinese Sci. Bull., 48 (10), pp. 941-948","Chen, Y.; Department of Biology, Tsinghua University, Protein Science Laboratory of Ministry of Education, Beijing 100084, China; email: chenyh@mail.tsinghua.edu.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-0344459386
"Strasser P., Unger U., Strobl B., Vilas U., Vlasak R.","16209521800;6701882758;6701482578;6507502550;56244751900;","Recombinant viral sialate-O-acetylesterases",2003,"Glycoconjugate Journal","20","9",,"551","561",,20,"10.1023/B:GLYC.0000043292.64358.f1","https://www.scopus.com/inward/record.uri?eid=2-s2.0-14844309479&doi=10.1023%2fB%3aGLYC.0000043292.64358.f1&partnerID=40&md5=71c3e95e4d3744a0a648d85a40967c03","Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria; Angewandte Biotechnologie GmbH, Department of Cell Biology, University Salzburg, Hellbrunnerstr. 34, A-5020 Salzburg, Austria; Christian Doppler Clinic, Department of Neurology, General Hospital Salzburg, Ignaz-Harrer-Str. 79, A-5020 Salzburg, Austria; Baxter BioScience AG, Global Pathogen Safety, Benatzkygasse 2-6, A-1220 Vienna, Austria; Institute of Animal Breeding and Genetics, Veterinary University Vienna, Veterinaerplatz 1, A-1210 Vienna, Austria","Strasser, P., Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria, Christian Doppler Clinic, Department of Neurology, General Hospital Salzburg, Ignaz-Harrer-Str. 79, A-5020 Salzburg, Austria; Unger, U., Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria, Baxter BioScience AG, Global Pathogen Safety, Benatzkygasse 2-6, A-1220 Vienna, Austria; Strobl, B., Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria, Institute of Animal Breeding and Genetics, Veterinary University Vienna, Veterinaerplatz 1, A-1210 Vienna, Austria; Vilas, U., Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria; Vlasak, R., Applied Biotechnology, Department of Cell Biology, University Salzburg, A-5020 Salzburg, Austria, Angewandte Biotechnologie GmbH, Department of Cell Biology, University Salzburg, Hellbrunnerstr. 34, A-5020 Salzburg, Austria","Viral O-acetylesterases were first identified in several viruses, including influenza C viruses and coronaviruses. These enzymes are capable of removing cellular receptors from the surface of target cells. Hence they are also known as ""receptor destroying"" enzymes. We have cloned and expressed several recombinant viral O-acetylesterases. These enzymes were secreted from Sf9 insect cells as chimeric proteins fused to eGFP. A purification scheme to isolate the recombinant O-acetylesterase of influenza C virus was developed. The recombinant enzymes derived from influenza C viruses specifically hydrolyze 9-O-acetylated sialic acids, while that of sialodacryoadenitis virus, a rat coronavirus related to mouse hepatitis virus, is specific for 4-O-acetylated sialic acid. The recombinant esterases were shown to specifically de-O-acetylate sialic acids on glycoconjugates. We have also expressed esterase knockout proteins of the influenza C virus hemagglutinin-esterase. The recombinant viral proteins can be used to unambiguously identify O-acetylated acids in a variety of assays. © 2004 Kluwer Academic Publishers.","Influenza C virus; O-acetylated sialic acids; Rat coronavirus; Receptor-destroying enzyme; Virus receptor","acetylesterase; green fluorescent protein; hemagglutinin; recombinant protein; sialic acid; virus protein; glycoconjugate; mucin; n acetylneuraminic acid; acetylation; cloning; conference paper; Coronavirus; enzyme isolation; enzyme purification; enzyme release; Hepatitis virus; human; human cell; hydrolysis; Influenza virus C; insect cell; nonhuman; priority journal; protein expression; animal; article; Baculovirus; cattle; cell membrane; chemistry; HeLa cell; immunoprecipitation; metabolism; molecular cloning; plasmid; polyacrylamide gel electrophoresis; protein tertiary structure; time; Coronavirus; Influenza C virus; Influenzavirus C; Insecta; Murine hepatitis virus; Rat coronavirus; Rat sialodacryoadenitis coronavirus; Acetylesterase; Animals; Baculoviridae; Cattle; Cell Membrane; Cloning, Molecular; Coronavirus; Electrophoresis, Polyacrylamide Gel; Glycoconjugates; Green Fluorescent Proteins; Hela Cells; Humans; Immunoprecipitation; Influenzavirus C; Mucins; N-Acetylneuraminic Acid; Plasmids; Protein Structure, Tertiary; Recombinant Proteins; Time Factors; Viral Proteins","Shen, Y., Tiralongo, J., Iwersen, M., Sipos, B., Kalthoff, H., Schauer, R., Characterization of the sialate-7(9)-O-acetyltransferase from the microsomes of human colonic mucosa (2002) Biol Chem, 383, pp. 307-317; Higa, H.H., Butor, C., Diaz, S., Varki, A., O-acetylation and de-O-acetylation of sialic acids. O-acetylation of sialic acids in the rat liver Golgi apparatus involves an acetyl intermediate and essential histidine and lysine residues - A transmembrane reaction? (1989) J Biol Chem, 264, pp. 19427-19434; Mason, D.Y., Andre, P., Bensussan, A., Buckley, C., Civin, C., Clark, E., De Haas, M., Zola, H., CD antigens 2001 (2001) Tissue Antigens, 58, pp. 425-430; Varki, A., Hooshmand, F., Diaz, S., Varki, N.M., Hedrick, S.M., Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetylesterase (1991) Cell, 65, pp. 65-74; Klein, A., Krishna, M., Varki, N.M., Varki, A., 9-O-acetylated sialic acids have widespread but selective expression: Analysis using a chimeric dual-function probe derived from influenza C hemagglutinin-esterase (1994) Proc Natl Acad Sci USA, 91, pp. 7782-7786; Shi, W.X., Chammas, R., Varki, A., Regulation of sialic acid 9-O-acetylation during the growth and differentiation of murine erythroleukemia cells (1996) J Biol Chem, 271, pp. 31517-31525; Shi, W.X., Chammas, R., Varki, N.M., Powell, L., Varki, A., Sialic acid 9-O-acetylation on murine erythroleukemia cells affects complement activation, binding to I-type lectins, and tissue homing (1996) J Biol Chem, 271, pp. 31526-31532; Krishna, M., Varki, A., 9-O-acetylation of sialomucins: A novel marker of murine CD4 T cells that is regulated during maturation and activation (1997) J Exp Med, 185, pp. 1997-2013; Schauer, R., Kamerling, J.P., Chemistry, biochemistry and biology of sialic acids (1997) Glycoproteins II, pp. 243-402. , edited by Montreuil J, Vliegenthart JFG, Schachter H (Amsterdam, Elsevier); Varki, A., Sialic acids as ligands in recognition phenomena (1997) Faseb J, 11, pp. 248-255; Schauer, R., Schmid, H., Pommerencke, J., Iwersen, M., Kohla, G., Metabolism and role of O-acetylated sialic acids (2001) The Molecular Immunology of Complex Carbohydrates 2, 491, pp. 325-342. , edited by Wu AM, New York, Kluwer Academic/Plenum Publishers; Angata, T., Varki, A., Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective (2002) Chem Rev, 102, pp. 439-469; Chen, H.Y., Varki, A., O-acetylation of GD3: An enigmatic modification regulating apoptosis? (2002) J Exp Med, 196, pp. 1529-1533; Herrler, G., Rott, R., Klenk, H.D., Muller, H.P., Shukla, A.K., Schauer, R., The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase (1985) Embo J, 4, pp. 1503-1506; Rogers, G.N., Herrler, G., Paulson, J.C., Klenk, H.D., Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells (1986) J Biol Chem, 261, pp. 5947-5951; Vlasak, R., Krystal, M., Nacht, M., Palese, P., The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities (1987) Virology, 160, pp. 419-425; Vlasak, R., Luytjes, W., Spaan, W., Palese, P., Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses (1988) Proc Natl Acad Sci USA, 85, pp. 4526-4529; Schultze, B., Wahn, K., Klenk, H.D., Herrler, G., Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity (1991) Virology, 180, pp. 221-228; Wurzer, W.J., Obojes, K., Vlasak, R., The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: A proposal to reorganize group 2 Coronaviridae (2002) J Gen Virol, 83, pp. 395-402; Falk, K., Namork, E., Rimstad, E., Mjaaland, S., Dannevig, B.H., Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.) (1997) J Virol, 71, pp. 9016-9023; Kristiansen, M., Froystad, M.K., Rishovd, A.L., Gjoen, T., Characterization of the receptor-destroying enzyme activity from infectious salmon anaemia virus (2002) J Gen Virol, 83, pp. 2693-2697; Hellebo, A., Vilas, U., Falk, K., Vlasak, R., Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-acetylated sialic acids (2004) J Virol, 78, pp. 3055-3062; Falk, K., Aspehaug, V., Vlasak, R., Endresen, C., Identification and characterization of viral structural proteins of infectious salmon anemia virus (2004) J Virol, 78, pp. 3063-3071; Cornelissen, L.A., Wierda, C.M., Van Der Meer, F.J., Herrewegh, A.A., Horzinek, M.C., Egberink, H.F., De Groot, R.J., Hemagglutinin-esterase, a novel structural protein of torovirus (1997) J Virol, 71, pp. 5277-5286; Vlasak, R., Vilas, U., Strobl, B., Kreil, G., cDNA cloning and expression of secreted Xenopus laevis dipeptidyl aminopeptidase IV (1997) Eur J Biochem, 247, pp. 107-113; Vlasak, R., Unger-Ullmann, C., Kreil, G., Frischauf, A.M., Nucleotide sequence of cloned cDNA coding for honeybee prepromelittin (1983) Eur J Biochem, 135, pp. 123-126; Klausegger, A., Strobl, B., Regl, G., Kaser, A., Luytjes, W., Vlasak, R., Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus (1999) J Virol, 73, pp. 3737-3743; Regl, G., Kaser, A., Iwersen, M., Schmid, H., Kohla, G., Strobl, B., Vilas, U., Vlasak, R., The hemagglutinin-esterase of mouse hepatitis virus strain S is a sialate-4-O-acetylesterase (1999) J Virol, 73, pp. 4721-4727; Strobl, B., Vlasak, R., The receptor-destroying enzyme of influenza C virus is required for entry into target cells (1993) Virology, 192, pp. 679-682; Rosenthal, P.B., Zhang, X., Formanowski, F., Fitz, W., Wong, C.H., Meier-Ewert, H., Skehel, J.J., Wiley, D.C., Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus (1998) Nature, 396, pp. 92-96; Muchmore, E.A., Varki, A., Selective inactivation of influenza C esterase: A probe for detecting 9-O-acetylated sialic acids (1987) Science, 236, pp. 1293-1295; Vlasak, R., Muster, T., Lauro, A.M., Powers, J.C., Palese, P., Influenza C virus esterase: Analysis of catalytic site, inhibition, and possible function (1989) J Virol, 63, pp. 2056-2062; Edwardson, J.M., Effects of monensin on the processing and intracellular transport of influenza virus haemagglutinin in infected MDCK cells (1984) J Cell Sci, 65, pp. 209-221; Yoo, D., Pei, Y., Christie, N., Cooper, M., Primary structure of the sialodacryoadenitis virus genome: Sequence of the structural-protein region and its application for differential diagnosis (2000) Clin Diagn Lab Immunol, 7, pp. 568-573; Tessier, D.C., Thomas, D.Y., Khouri, H.E., Laliberte, F., Vernet, T., Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide (1991) Gene, 98, pp. 177-183; Shi, W.X., Chammas, R., Varki, A., Regulation of sialic acid 9-O-acetylation during the growth and differentiation of murine erythroleukemia cells (1996) J Biol Chem, 271, pp. 31517-31525; Ariga, T., Blaine, G.M., Yoshino, H., Dawson, G., Kanda, T., Zeng, G.C., Kasama, T., Yu, R.K., Glycosphingolipid composition of murine neuroblastoma cells: O-acetylesterase gene downregulates the expression of O-acetylated GD3 (1995) Biochemistry, 34, pp. 11500-11507; Birkle, S., Ren, S., Slominski, A., Zeng, G., Gao, E., Yu, R.K., Down-regulation of the expression of O-acetyl-GD3 by the O-acetylesterase cDNA in hamster melanoma cells: Effects on cellular proliferation, differentiation, and melanogenesis (1999) J Neurochem, 72, pp. 954-961; Malisan, F., Franchi, E., Tomassini, B., Ventura, N., Condo, I., Rippo, M.R., Rufini, A., Testi, R., Acetylation suppresses the proapoptotic activity of GD3 ganglioside (2002) J Exp Med, 196, pp. 1535-1541; Chatterjee, M., Chava, A.K., Kohla, G., Pal, S., Merling, A., Hinderlich, S., Unger, U., Mandal, C., Identification and characterization of adsorbed serum sialoglycans on Leishmania donovani promastigotes (2003) Glycobiology, 13, pp. 351-361; Iwersen, M., Vandamme-Feldhaus, V., Schauer, R., Enzymatic 4-O-acetylation of N-acetylneuraminic acid in guinea-pig liver (1998) Glycoconj J, 15, pp. 895-904; Morimoto, N., Nakano, M., Kinoshita, M., Kawabata, A., Morita, M., Oda, Y., Kuroda, R., Kakehi, K., Specific distribution of sialic acids in animal tissues as examined by LC-ESI-MS after derivatization with 1,2-diamino-4,5- methylenedioxybenzene (2001) Anal Chem, 73, pp. 5422-5428; Bulai, T., Bratosin, D., Pons, A., Montreuil, J., Zanetta, J.P., Diversity of the human erythrocyte membrane sialic acids in relation with blood groups (2003) FEBS Lett, 534, pp. 185-189","Vlasak, R.; Angewandte Biotechnologie GmbH, Department of Cell Biology, University Salzburg, Hellbrunnerstr. 34, A-5020 Salzburg, Austria; email: rvlasak@applied-biotech.at",,,02820080,,GLJOE,"15454694","English","Glycoconjugate J.",Conference Paper,"Final",,Scopus,2-s2.0-14844309479
"Björkman C., Svensson C., Christensson B., De Verdier K.","7006946407;7202512724;7004298922;56418694900;","Cryptosporidium parvum and Giardia intestinalis in Calf diarrhoea in Sweden",2003,"Acta Veterinaria Scandinavica","44","3-4",,"145","152",,43,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842628941&partnerID=40&md5=fcf1d826aa7ba220729fac104c533af3","Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. of Agricultural Sciences, Uppsala, Sweden; Dept. of Anim. Environ. and Health, Swed. Univ. of Agricultural Sciences, Skara, Sweden; Department of Parasitology, National Veterinary Institute, Swed. Univ. of Agricultural Sciences, Uppsala, Sweden; Dept. of Ruminant and Porcine Dis., National Veterinary Institute, Uppsala, Sweden; Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. of Agricultural Sciences, P.O. Box 7019, SE-750 07, Uppsala, Sweden","Björkman, C., Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. of Agricultural Sciences, Uppsala, Sweden, Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. of Agricultural Sciences, P.O. Box 7019, SE-750 07, Uppsala, Sweden; Svensson, C., Dept. of Anim. Environ. and Health, Swed. Univ. of Agricultural Sciences, Skara, Sweden; Christensson, B., Department of Parasitology, National Veterinary Institute, Swed. Univ. of Agricultural Sciences, Uppsala, Sweden; De Verdier, K., Dept. of Ruminant and Porcine Dis., National Veterinary Institute, Uppsala, Sweden","The objective of this study conducted in 75 herds was to investigate the presence and significance of Cryptosporidium parvum and Giardia intestinalis in Swedish dairy calves in comparison with rotavirus, coronavirus and Escherichia coli K99+. The farmers were asked to collect faecal samples from each heifer calf that had diarrhoea between birth and 90 days of age, and also from a healthy calf of the same age. In total, 270 samples were collected and analysed. C. parvum, either alone or together with G. intestinalis and/or rotavirus, was detected in 16 (11%) and 6 (5%) of the samples from diarrhoeic and healthy calves, respectively. Even though a higher proportion of diarrhoeic calves shed C. parvum, the difference between the groups was not statistically significant (p=0.067), possibly due to the low number of positive samples. G. intestinalis was found in 42 (29%) of the diarrhoea samples and in 29 (23%) of the samples from healthy calves. Rotavirus and coronavirus were demonstrated in 24% and 3% of the diarrhoea samples, respectively, whereas E. coli K99+ was only found in samples from 2 healthy calves. C. parvum and G. intestinalis were found in samples from calves 7 to 84 days of age and during all seasons. The results confirm that C. parvum is present in Swedish dairy herds and might have clinical significance. G. intestinalis was the most common agent found but the importance of this parasite remains unclear. Both parasites have suggested zoonotic potential and thus warrant further attention. In addition, rotavirus is a major pathogen in neonatal enteritis in Sweden, whereas coronavirus and E. coli K99+ seem to be of less importance.","Calf diarrhoea; Coronavirus; Cryptosporidium parvum; Escherichia coli; Giardia intestinalis; Rotavirus","article; bacterial infection; cattle disease; controlled study; Coronavirus; cryptosporidiosis; Cryptosporidium parvum; diarrhea; Escherichia coli; feces analysis; Giardia lamblia; giardiasis; microbiological examination; nonhuman; Rotavirus; seasonal variation; statistical significance; Sweden; virus detection; virus infection; Animals; Cattle; Cattle Diseases; Coronavirus Infections; Cryptosporidiosis; Cryptosporidium parvum; Diarrhea; Feces; Female; Giardia lamblia; Giardiasis; Rotavirus Infections; Sweden; Bacteria (microorganisms); Bos taurus; Bovinae; Coronavirus; Cryptosporidium; Cryptosporidium parvum; Escherichia coli; Giardia; Giardia intestinalis; Rotavirus","(2001) SWEPAR Triennial Report 1998-2000, 71p. , Swedish National Veterinary Institute and Swedish University of Agricultural Sciences, Uppsala; Appelbee, A.J., Frederick, L.M., Heitman, T.L., Olson, M.E., Prevalence and genotyping of Giardia duodenalis from beef calves in Alberta, Canada (2003) Vet. Parasitol., 112, pp. 289-294; Butler, D.G., Clarke, R.C., Diarrhoea and dysentery in calves (1994) Escherichia Coli in Domestic Animals and Humans, pp. 91-116. , Gyles CL (ed), CAB International, Oxon; De Graaf, D.C., Vanopdenbosch, E., Ortega-Mora, L.M., Abbassi, H., Peeters, J.E., A review of the importance of cryptosporidiosis in farm animals (1999) Int. J. Parasitol., 29, pp. 1269-1287; De Verdier Klingenberg, K., Svensson, L., Group a rotavirus as a cause of neonatal enteritis in Sweden (1998) Acta Vet. Scand., 39, pp. 195-199; Enemark, H.L., (2002) Cryptosporidium. Studies of Molecular Characteristics and Pathogenicity, , PhD thesis, The Royal Veterinary and Agricultural University. Copenhagen; Fayer, R., Gasbarre, L., Pasquali, P., Canals, A., Almeria, S., Zarlenga, D., Cryptosporidium parvum infection in bovine neonates: Dynamic clinical, parasitic and immunologic patterns (1998) Int. J. Parasitol., 28, pp. 49-56; Henriksen, S.A., Pohlenz, J.F.L., Staining of Cryptosporidia by a modified Ziehl-Neelsen technique (1981) Acta Vet. Scand., 22, pp. 594-596; Huetink, R.E.C., Giessen, J.W.Bvd., Noordhuizen, J.P.T.M., Ploeger, H.W., Epidemiology of Cryptosporidium parvum and Giardia duodenalis on a dairy farm (2001) Vet. Parasitol., 102, pp. 53-67; Kulda, J., Nohýková, E., Giardia in humans and animals (1995) Parasitic Protozoa. 2nd Ed., 10, pp. 225-430. , Kreier JP (ed), Academic Press, San Diego; Ljungström, B.-L., Svärd, S., Schwan, O., Presence and clinical importance of Giardia infection in Swedish lambs (2001) Svensk Vet-Tidn., 53, pp. 693-695. , In Swedish; McDonough, S.P., Stull, C.L., Osburn, B.I., Enteric pathogens in intensively reared veal calves (1994) Am. J. Vet. Res., 55, pp. 1516-1520; Mebus, C.A., Stair, E.L., Rhodes, M.B., Twiehaus, M.J., Pathology of neonatal calf diarrhea induced by a coronavirus-like agent (1973) Vet. Pathol., 10, pp. 45-64; O'Donoghue, P.J., Cryptosporidium and cryptosporidiosis in man and animals (1995) Int. J. Parasitol., 25, pp. 139-195; O'Handley, R.M., Olson, M.E., Fraser, D., Adams, P., Rca, T., Prevalence and genotypic characterisation of Giardia in dairy calves from Western Australia and Western Canada (2000) Vet. Parasitol., 90, pp. 193-200; Ortman, K., Svensson, C., Antimicrobial use in Swedish dairy calves and replacement heifers (2003) Vet. Record, , In press; Panciera, R.J., Thomassen, R.W., Garner, F.M., Cryptosporidial infection in a calf (1971) Vet. Pathol., 8, pp. 479-484; Quilez, J., Sánchez-Acedo, C., Cacho, Ed., Clavel, A., Causapé, A.C., Prevalence of Cryptosporidium and Giardia infections in cattle in Aragon (northeast Spain) (1996) Vet. Parasitol., 66, pp. 139-146; Saif, L.J., Rosen, B.I., Parwani, A.V., Bovine rotavirus (1994) Viral Infections of the Gastrointestinal Tract. 2nd Ed., pp. 279-368. , Kapikian AZ (ed), Marcel Dekker Inc., New York; Scott, C.A., Smith, H.V., Mtambo, M.M.A., Gibbs, H.A., An epidemiological study of Cryptosporidium parvum in two herds of adult beef cattle (1995) Vet. Parasitol., pp. 277-288; Snodgrass, D.R., Terzolo, H.R., Sherwood, D., Campbell, I., Menzies, J.D., Synge, B.A., Aetiology of diarrhoea in young calves (1986) Vet. Record, 119, pp. 31-34; Svensson, C., Lundborg, K., Emanuelson, U., Olsson, S.-O., Morbidity in Swedish dairy calves from birth to 90 days of age and individual calf-level risk factors for infectious diseases (2003) Prev. Vet. Med., 55, pp. 179-197; Svensson, L., Uhnoo, I., Grandien, M., Wadell, G., Molecular epidemiology of rotavirus infections in Uppsala, Sweden (1986) J. Med. Virol., 18, pp. 101-111; Tråvén, M., Uggla, A., Viring, S., Ewerlöf, N., Outbreak of cryptosporidiosis in dairy calves (1989) Svensk VetTidn., 41, pp. 533-538. , In Swedish; Tzipori, S., The aethiology and diagnosis of calf diarrhoea (1981) Vet. Record, 108, pp. 510-515; Tzipori, S., Smith, M., Halpin, C., Angus, K.W., Sherwood, D., Campbell, I., Experimental cryptosporidiosis in calves: Clinical manifestations and pathological findings (1983) Vet. Record, 112, pp. 116-120; Uga, S., Matsuo, J., Kono, E., Kimura, K., Inoue, M., Rai, S.K., Ono, K., Prevalence of Cryptosporidium parvum infection and pattern of oocyst shedding in calves in Japan (2000) Vet. Parasitol., 94, pp. 27-32; Wade, S.E., Mohammed, H.O., Schaaf, S.L., Prevalence of Giardia sp., Cryptosporidium parvum and Cryptosporidium muris (C. andersoni) in 109 dairy herds in five counties of southeastern New York (2000) Vet. Parasitol., 93, pp. 1-11; Wahlström, H., (2001) Zoonoses in Sweden Up to and Including 1999, 48p. , National Veterinary Institute, Uppsala; Van Keulen, Hv., Macechko, P.T., Wade, S., Schaaf, S., Wallis, P.M., Erlandsen, S.L., Presence of human Giardia in domestic, farm and wild animals, and environmental samples suggests a zoonotic potenital for giardiasis (2002) Vet. Parasitol., 108, pp. 97-107; Viring, S., Olsson, S.-O., Alenius, S., Emanuelsson, U., Jacobsson, S.-O., Larsson, B., Linde, N., Uggla, A., Studies of enteric pathogens and -globulin levels of neonatal calves in Sweden (1993) Acta Vet. Scand., 34, pp. 271-279; Xiao, L., Giardia infection in farm animals (1994) Parasitology Today, 10, pp. 436-438; Xiao, L., Herd, R.P., Infection patterns of Cryptosporidium and Giardia in calves (1994) Vet. Parasitol., 55, pp. 257-262","Björkman, C.; Dept. Ruminant Med. Vet. Epidemiol., Swed. Univ. of Agricultural Sciences, P.O. Box 7019, SE-750 07, Uppsala, Sweden; email: camilla.bjorkman@idmed.slu.se",,,0044605X,,AVSCA,"15074627","English","Acta Vet. Scand.",Article,"Final",,Scopus,2-s2.0-1842628941
"Bermejo Martín J.F., Muñoz-Fernández M.A.","35274537000;25931106800;","SARS in children: Key data concerning pathophysiology, therapy, vaccine development and control of its transmission [Síndrome respiratorio agudo grave en niños: Datos clave para la fisiopatogenia, terapia, desarrollo de vacunas y control de diseminación]",2003,"Acta Pediatrica Espanola","61","11",,"624","628",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0742320305&partnerID=40&md5=f33ce3dfea2f0b6986458056abe1b3d5","Lab. de Inmunobiologia Molecular, Hosp. Gen. Univ. Gregorio Maranon, Madrid, Spain; Departamento de Inmunología, Hosp. Gen. Univ. Gregorio Maranon, C/ Doctor Esquerdo, 46, 28007 Madrid, Spain","Bermejo Martín, J.F., Lab. de Inmunobiologia Molecular, Hosp. Gen. Univ. Gregorio Maranon, Madrid, Spain; Muñoz-Fernández, M.A., Lab. de Inmunobiologia Molecular, Hosp. Gen. Univ. Gregorio Maranon, Madrid, Spain, Departamento de Inmunología, Hosp. Gen. Univ. Gregorio Maranon, C/ Doctor Esquerdo, 46, 28007 Madrid, Spain","Severe acute respiratory syndrome (SARS) is a new viral disease that is causing great concern for health authorities and the general population. The causal agent for SARS is known to be a new coronavirus that fulfills Koch's postulates. In our view, there is an open question in SARS pathogenesis. What is the underlying cause of the evolution to respiratory distress: direct viral cytopathic damage, immune-mediated damage in response to the viral infection or both factors? Findings from autopsies and in serum and blood from adult patients suggest an important immune-inflammatory component in response to the new coronavirus. But the strongest support for this immune role is the fact that the severity is much milder and the clinical progression much less aggressive in young children. To date, there have been no reported fatalities in children with this disease. This fact, in itself, rules out an important direct viral cytopathic effect: children would be the most severely affected patients because of the immaturity of their immune systems; on the other hand, the severity of the disease is most marked in patients with an adult immune system, which is able to develop a complete immune-inflammatory response. Vaccine development is affected by this observation: the designers of vaccines must avoid those SARS coronavirus antigens that could lead to an immune-mediated inflammatory damage like that caused by the natural disease. We should also be aware of pauci-symptomatic children who could transmit the virus to their relatives and close contacts. In conclusion, children show us again that they are not scale models of adults, but do present features that could help us to understand adult diseases.",,"child; cytopathogenic effect; data analysis; disease severity; disease transmission; human; infection control; pathophysiology; respiratory distress; review; SARS coronavirus; severe acute respiratory syndrome; vaccine production; virus infection; virus transmission","Ron, A., Fouchier, M., Kuiken, T., Schutten, M., Van Amerongen, G., Gerard, J., Koch's postulates fulfilled for SRAG virus (2003) Nature, 423, p. 240. , mayo; Kuiken, T., Fouchier, R.A., Schutten, M., Rimmelzwaan, G.F., Van Amerongen, G., Van Riel, D., Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome (2003) Lancet, 362 (9380), pp. 263-270. , julio; Nicholls, J.M., Poon, L.L.M., Lee, C.K., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, p. 9370. , http://image.thelancet.com/extras/03art4347web.pdf; Karras, A., Herraine, O., Hemophagocytic syndrome (2002) Rev Med Intern, 23 (9), pp. 768-778. , sept; Wang, C., Dynamic changes in blood cytokine levels as clinical indicators in severe acute respiratory syndrome (2003) Clin Med J (Engl), 116 (9), pp. 1283-1287. , sept; Duan, Z.P., Chen, Y., Zhang, J., Zhao, J., Lang, Z.W., Meng, F.K., Bao, X.L., Clinical characteristics and mechanism of liver injury in patients with severe acute respiratory syndrome (2003) Zhonghua Gan Zang Bing Za Zhi, 11 (8), pp. 493-495. , ag; Bermejo Martín, J.F., Jiménez, J.L., Muñoz-Ferndndez, M.A., Pentoxifylline and severe acute respiratory syndrome (SRAG): A drug to be considered (2003) Med Sci Monit, 9 (6), pp. SR29-SR34; Chiu, W.K., Cheung, P.C., Ng, K.L., Ip, P.L., Sugunan, V.K., Luk, D.C., Severe acute respiratory syndrome in children: Experience in a regional hospital in Hong Kong (2003) Pediatr Crit Care Med, 4 (3), pp. 279-283. , julio; Wong, G.W., Li, A.M., Ng, P.C., Fok, T.F., Severe acute respiratory syndrome in children (2003) Pediatr Pulmonol, 36 (4), pp. 261-266. , oct; Hon, K.L., Leung, C.W., Cheng, W.T., Chan, P.K., Chu, W.C., Kwan, Y.W., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361 (9370), pp. 1701-1703. , mayo; SRAG spares kids (2003) Nature Science Update, p. 15. , http://www.nature.com/nsu/030915/030915-1.html, sept; Bitnun, A., Allen, U., Heurter, H., King, S.M., Opavsky, M.A., Ford-Jones, E.L., Children hospitalized with severe acute respiratory syndrome-related illness in Toronto (2003) Pediatrics, 112 (4), p. 261. , oct; Tsou, I.Y., Loh, L.E., Kaw, G.J., Chan, I., Chee, T.S., Severe acute respiratory syndrome (SRAG) in a paediatric cluster in Singapore (2003) Pediatr Radiol, p. 20. , agosto; Sit, S.C., Yau, E.K.C., Lam, Y.Y., Ng, D.K.K., Fong, N.C., Hui, Y.W., A Young Infant with Severe Acute Respiratory Syndrome (2003) Pediatrics, 112 (4), pp. 257-259. , oct; Gasparoni, A., Ciardelli, L., Avanzini, A., Castellazzi, A.M., Carini, R., Rondini, G., Chirico, G., Age-related changes in intracellular TH1/TH2 cytokine production, immunoproliferative T lymphocyte response and natural killer cell activity in newborns, children and adults (2003) Biol Neonat, 84 (4), pp. 297-303","Bermejo Martín, J.F.; Lab. de Inmunobiologia Molecular, Hosp. Gen. Univ. Gregorio Maranon, Madrid, Spain",,,00016640,,APESA,,"Spanish","Acta Pediatr. Esp.",Review,"Final",,Scopus,2-s2.0-0742320305
"Wang D., Urisman A., Liu Y.-T., Springer M., Ksiazek T.G., Erdman D.D., Mardis E.R., Hickenbotham M., Magrini V., Eldred J., Latreille J.P., Wilson R.K., Ganem D., DeRisi J.L.","16403747800;6505489507;36071758200;7103099984;7101963789;7005380414;7003499321;6507371507;6602548928;6602181124;7006495956;56713341900;7101880208;7004334309;","Viral discovery and sequence recovery using DNA microarrays",2003,"PLoS Biology","1","2",,"","",,311,"10.1371/journal.pbio.0000002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-4243142644&doi=10.1371%2fjournal.pbio.0000002&partnerID=40&md5=22c4c92361501c01d9e7958465b49456","Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States; Dept. of Microbiology and Immunology, Univ. of California San Francisco, San Francisco, CA, United States; Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States","Wang, D., Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States; Urisman, A., Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States; Liu, Y.-T., Dept. of Microbiology and Immunology, Univ. of California San Francisco, San Francisco, CA, United States; Springer, M., Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States; Ksiazek, T.G., Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Erdman, D.D., Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Mardis, E.R., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Hickenbotham, M., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Magrini, V., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Eldred, J., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Latreille, J.P., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Wilson, R.K., Department of Genetics, Genome Sequencing Center, Washington Univ. School of Medicine, St. Louis, MO, United States; Ganem, D., Dept. of Microbiology and Immunology, Univ. of California San Francisco, San Francisco, CA, United States; DeRisi, J.L., Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States","Because of the constant threat posed by emerging infectious diseases and the limitations of existing approaches used to identify new pathogens, there is a great demand for new technological methods for viral discovery. We describe herein a DNA microarray-based platform for novel virus identification and characterization. Central to this approach was a DNA microarray designed to detect a wide range of known viruses as well as novel members of existing viral families; this microarray contained the most highly conserved 70mer sequences from every fully sequenced reference viral genome in GenBank. During an outbreak of severe acute respiratory syndrome (SARS) in March 2003, hybridization to this microarray revealed the presence of a previously uncharacterized coronavirus in a viral isolate cultivated from a SARS patient. To further characterize this new virus, approximately 1 kb of the unknown virus genome was cloned by physically recovering viral sequences hybridized to individual array elements. Sequencing of these fragments confirmed that the virus was indeed a new member of the coronavirus family. This combination of array hybridization followed by direct viral sequence recovery should prove to be a general strategy for the rapid identification and characterization of novel viruses and emerging infectious disease.",,"article; controlled study; Coronavirus; DNA microarray; epidemic; female; gene sequence; HeLa cell; human; human cell; hybridization; infection; severe acute respiratory syndrome; virus characterization; virus culture; virus detection; virus genome; virus isolation; communicable disease; DNA sequence; genetic procedures; genetics; methodology; molecular genetics; nucleic acid hybridization; nucleotide sequence; polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; virology; virus gene; Coronavirus; Base Sequence; Communicable Diseases, Emerging; Genes, Viral; Genetic Techniques; Genome, Viral; Humans; Molecular Sequence Data; Nucleic Acid Hybridization; Oligonucleotide Array Sequence Analysis; Polymerase Chain Reaction; SARS Virus; Sequence Analysis, DNA; Severe Acute Respiratory Syndrome","Chang, Y., Cesarman, E., Pessin, M.S., Lee, F., Culpepper, J., Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma (1994) Science, 266, pp. 1865-1869. , Find this article online; Choo, Q.L., Kuo, G., Weiner, A.J., Overby, L.R., Bradley, D.W., Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome (1989) Science, 244, pp. 359-362. , Find this article online; Jonassen, C.M., Jonassen, T.O., Grinde, B., A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus (1998) J Gen Virol, 79, pp. 715-718. , Find this article online; Kellam, P., Molecular identification of novel viruses (1998) Trends Microbiol, 6, pp. 160-165. , Find this article online; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966. , Find this article online; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404. , Find this article online; Muerhoff, A.S., Leary, T.P., Desai, S.M., Mushahwar, I.K., Amplification and subtraction methods and their application to the discovery of novel human viruses (1997) J Med Virol, 53, pp. 96-103. , Find this article online; Nichol, S.T., Spiropoulou, C.F., Morzunov, S., Rollin, P.E., Ksiazek, T.G., Genetic identification of a hantavirus associated with an outbreak of acute respiratory illness (1993) Science, 262, pp. 914-917. , Find this article online; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399. , Find this article online; Wang, D., Coscoy, L., Zylberberg, M., Avila, P.C., Boushey, H.A., Microarray-based detection and genotyping of viral pathogens (2002) Proc Natl Acad Sci USA, 99, pp. 15687-15692. , Find this article online","DeRisi, J.L.; Dept. of Biochemistry and Biophysics, Univ. of California San Francisco, San Francisco, CA, United States; email: joe@derisilab.ucsf.edu",,,15449173,,PBLIB,"14624234","English","PloS Biol.",Article,"Final",Open Access,Scopus,2-s2.0-4243142644
"Numazaki K.","7005787970;","Glycyrrhizin therapy for viral infections",2003,"African Journal of Biotechnology","2","10",,"456","458",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-3042689218&partnerID=40&md5=9ecd68667bb4d2403a0718fa64434fa4","Department of Pediatrics, Sapporo Medical University, School of Medicine, Sapporo, Hokkaido, 060-8543, Japan","Numazaki, K., Department of Pediatrics, Sapporo Medical University, School of Medicine, Sapporo, Hokkaido, 060-8543, Japan","Glycyrrhizin (GL) was reported as the most active in inhibiting replication of the severe acute respiratory syndrome (SARS)-associated coronavirus. Therapeutic effect of GL for liver dysfunction associated with cytomegalovirus (CMV) infection in immunocompetent individuals was evaluated. Liver dysfunction in 4 cases improved and CMV disappeared from urinary samples after administration of GL intravenously by the age of 12 months. GL treatment also should be applied for the patients with SARS.","Cytomegalovirus; Glycyrrhizin; SARS","antivirus agent; cysteine; glycine; glycyron; glycyrrhizic acid; methionine; unclassified drug; article; congenital infection; controlled study; Cytomegalovirus; cytomegalovirus infection; disease association; drug inhibition; human; immunocompetence; infant; liver dysfunction; perinatal infection; SARS coronavirus; treatment outcome; urinalysis; virus infection; Coronavirus; Cucumber mosaic virus; Cytomegalovirus; SARS coronavirus","Cinatl, J., Morgenstern, B., Bauer, G., Chandra, P., Rabenau, H., Doerr, H.W., Glycyrrhizin, an active component of liquorice roots, and replication of SARS-associated coronavirus (2003) Lancet, 361, pp. 2045-2046. , Pubmed; Miyaji, C., Miyakawa, R., Watanabe, H., Kawamura, H., Abo, T., Mechanisms underlying the activation of cytotoxic function mediated by hepatic lymphocytes following the administration of glycyrrhizin (2002) Int. Immunopharmacol., 2, pp. 1079-1086. , Pubmed; Numazaki, K., Chiba, S., Natural course and trial of treatment for infantile liver dysfunction associated with cytomegalovirus infections (1993) In Vivo, 7, pp. 477-480. , Pubmed; Numazaki, K., Nagata, N., Sato, T., Chiba, S., Effect of glycyrrhizin, cyclosporin A, and tumor necrosis factor on infection of U-937 and MRC-5 cells by human cytomegalovirus (1994) J. Leukocyte Biol., 55, pp. 24-28. , Pubmed; Numazaki, K., Umetsu, M., Chiba, S., Effect of glycyrrhizin in children with liver dysfunction associated with cytomegalovirus infection (1994) Tohoku J. Exp. Med., 172, pp. 147-153. , Pubmed; Numazaki, K., Glycyrrhizin therapy for liver dysfunction associated with cytomegalovirus infection in immunocompetent children (1998) Antimicrobics and Infectious Diseases Newsletter, 117, pp. 70-71","Numazaki, K.; Department of Pediatrics, Sapporo Medical University, School of Medicine, Sapporo, Hokkaido, 060-8543, Japan; email: numazaki@sapmed.ac.jp",,,16845315,,,,"English","Afr. J. Biotechnol.",Article,"Final",,Scopus,2-s2.0-3042689218
"Palmieri G.","23985683800;","Prophylaxis of aiways and lung viral infections: Role of the enhancement of the immunitary defences [Profilassi delle infezioni virali a carico delle vie aeree del polmone: Il ruolo del potenziamento delle difese immunitarie]",2003,"GIMT - Giornale Italiano delle Malattie del Torace","57","1",,"57","62",,3,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-22144443648&partnerID=40&md5=c3989fd369b645aac1e52cb665b54340","Ospedale di Niguarda, Milano, Italy","Palmieri, G., Ospedale di Niguarda, Milano, Italy","Evidences on the well known facilitation played by viral infections on bacterial superinfections derive either from the present epidemic event SARS: Severe Acute Respiratory Syndrome, where to a substantial etiologic role of a Coronavirus bacterial copathogens seems often associated. The mechanisms of such a synergy are examined. Possible enhancement of immune responce in preventive terms, of a PBML (pouvaient batterie mechanical lisate) on such events that are facilitated by viral infections, are examined also at the light of recent evidences.","Bacterial mechanical polilysate; Bacterial superinfection; SARS; Vaccination; Viruses","bacterium lysate; polyvalent bacterium mechanical lysate; unclassified drug; Chlamydophila pneumoniae; dendritic cell; Haemophilus influenzae; host resistance; human; immunomodulation; immunostimulation; infection prevention; infection resistance; lung infection; nonhuman; review; severe acute respiratory syndrome; Staphylococcus aureus; Streptococcus pneumoniae; superinfection; vaccination; virus infection; virus resistance","www.who.int; Allegra L. L'Influenza e le Sue Complicanze. Mattioli 1885 Ed, Fidenza 2002; Raza, W., Ahmer, O., Ogilvie, M., Infection with respiratory syncytial virus enhances expression of native receptors for nonpilate Neisseria meningitidis to Hep-2 cells (1999) FEMS Immunol Med Microbiol, 23, pp. 115-124; Sanford, B., Davison, V., Ramsay, M., Fibrinogen-mediated adherence of group A Streptococcus to influenza A virus-infected cell cultures (1982) Infect Immun, 38, pp. 513-520; Sanford, B., Davison, V., Ramsay, M., Staphylococcus aureus adherence to influenza A virus-infected and control cell cultures: Evidence for multiple adhesins (1986) Proc Soc Exp Biol Med, 181, pp. 104-111; Huang, R.T., Rott, R., Wahn, K., Klenk, H.D., Kohama, T., The function of the neuraminidase in membrane fusion induced by myxoviruses (1980) Virology, 107, pp. 313-319; Murphy, B., Fields, R., (1990) Virology, pp. 1091-1152. , 2nd Edition; Yoshima, M., (1982) Virology, 43, pp. 284-293; Garten, W., Bosch, F.X., Linder, D., Rott, R., Klenk, H.D., Proteolytic activation of the influenza virus hemagglutinin: The structure of the cleavage site and the enzymes involved in cleavage (1981) Virology, 115, pp. 361-374; Tashiro, M., Ciborowski, P., Klenk, H.D., Pulverer, G., Rott, R., Role of Staphylococcus protease in the development of influenza pneumonia (1987) Nature, 325, pp. 536-537; Tashiro, M., Ciborowski, P., Reinacher, M., Pulverer, G., Klenk, H.D., Rott, R., Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity (1987) Virology, 157, pp. 421-430; Tashiro, M., Klenk, H.D., Rott, R., Inhibitory effect of a protease inhibitor, leupeptin, on the development of influenza pneumonia, mediated by concomitant bacteria (1987) J Gen Virol, 68, pp. 2039-2041; Roitt, I., Immunologia, Hill, M., (1996); Lambrecht, B.N., Prins, J.-B., Hoogsteden, H.C., Lung dendritic cells host immunity to infection (2001) Eur Resp J, 18, pp. 692-704; Reynolds, H.Y., Advances in understanding pulmonary host defense mechanisms: Dendritic cell function and immunomodulation (2000) Curr Opin Pulm Med, 6, pp. 209-216; Melioli, G., The immunoresponse against bacterial antigens is generated in vivo by a mechanical bacterial lysate through a cross-talk between innate and adaptive immunity (2003) European Respiratory Society Annual Congress, , Abstract book; Melioli, G., Opsonizzazione: Mangiare o essere mangiato. (2002) Giorn It Mal Tor, 56, pp. 245-248; Harrison. Principi di Medicina Interna. XIV Ediz.; 1,1999, McGraw-Hill; Rossi S, Tazza R. Valutazione dell'efficacia e della tollerabilità di un nuovo vaccino immunostimolante (Ismigen), ottenuto per lisi meccanica, nella prevenzione delle patologie infettive delle basse vie respiratorie. Italian Chapter American College of Chest Physicians 2002. Abstract book","Palmieri, G.; Ospedale di Niguarda, Milano, Italy",,,11270810,,GGIMA,,"Italian","GIMT G. Ital. Mal. Torace",Review,"Final",,Scopus,2-s2.0-22144443648
"Blasi F.","57211284402;","Winter and ""atypical"" respiratory infections [Focus: Inverno e infezioni respiratorie ""atipiche""]",2003,"GIMT - Giornale Italiano delle Malattie del Torace","57","3",,"192","198",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4944252521&partnerID=40&md5=dc69c27a805171a403a40a2c52947414","Istituto Malattie Respiratorie, Università di Milano, IRCCS Ospedale Maggiore, Milano, Italy","Blasi, F., Istituto Malattie Respiratorie, Università di Milano, IRCCS Ospedale Maggiore, Milano, Italy","Next winter we shall face the usual peak of respiratory infections due to rhino, parainfluenza, influenza viruses and further more the threat of a new outbreak of SARS-associated coronavirus infection. We can't forget that in the same winter season other ""usual"" pathogens may be involved in respiratory infections and pneumonia, Chlamydia, Mycoplasma, Legionella, Streptococcus pneumoniae and so on. The risk of an influenza pandemia is probably higher than a larger outbreak of SARS. We must then implement a correct vaccine prophylaxis, an adequate use of antiviral agents and a judicious use of antibiotics.","Atypical pathogens; Coronavirus; Influenza; Pneumonia; SARS; Virus respiratory","antibiotic agent; antivirus agent; oseltamivir; zanamivir; Chlamydia; drug use; epidemic; human; infection control; infection risk; Influenza virus; Legionella; Mycoplasma; Parainfluenza virus; respiratory tract infection; review; SARS coronavirus; severe acute respiratory syndrome; Streptococcus pneumoniae; vaccination; winter","Thompson, W.W., Mortality associated with influenza and respiratory syncytial virus in the United States (2003) JAMA, 289, pp. 179-186; Nguyen-Van-Tam, J.S., The epidemiology and clinical impact of pandemic influenza (2003) Vaccine, 21, pp. 1762-1768; Cox, N.J., Influenza pandemic planning (2003) Vaccine, 21, pp. 1801-1803; Cooper, N.J., Effectiveness of neuraminidase inhibitors in treatment and prevention of influenza A and B: Systematic review and meta-analyses of randomised controlled trials (2003) BMJ, 326, pp. 1235-1240; Stohr, K., Preventing and treating influenza (2003) BMJ, 326, pp. 1223-1224; Sampathkumar, P., SARS: Epidemiology, clinical presentation, management, and infection control measures (2003) Mayo Clin Proc, 78, pp. 882-890; Seto, W.H., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Lieberman, D., Atypical pathogens in community-acquired pneumonia (1999) Clin Chest Med, 20, pp. 489-497; Allegra, L., Problems and Perspectives in the treatment of respiratory infections caused by atypicals (2001) Pulm Pharmacol Ther, 14, pp. 21-27; American Thoracic Society: Guidelines for the management of adults with community-acquired pneumonia: Diagnosis, assessment of severity, antimicrobial therapy, and prevention (2001) Am J Respir Crit Care Med, 163, pp. 1730-1754; Bartlett, J.G., Practice guidelines for the management of community-acquired pneumonia in adults (2000) Clin Infect Dis, 31, pp. 347-382; Mandell, L.A., Canadian guidelines for the initial management of community-acquired pneumonia: An evidence-based update by the Canadian Infectious Diseases Society and the Canadian Thoracic Society (2000) Clin Infect Dis, 31, pp. 383-421; Dudas, V., Antimicrobial selection for hospitalized patients with presumed community-acquired pneumonia: A survey of nonteaching US community hospitals (2000) Ann Pharmacotherap, 34, pp. 446-452; Lentino, J.R., Association between initial empiric therapy and decreased length of stay among veteran patients hospitalized with community acquired pneumonia (2002) Int J Antimicrob Agents Chemother, 19, pp. 61-66; Martinez, J.A., Addition of a macrolide to a beta-lactam -based empiric antibiotic regimen is associated with lower in-hospital mortality for patients with bacteremic pneumococcal pneumonia (2003) Clin Infect Dis, 36, pp. 389-395; Gleason, P.P., Associations between initial antimicrobial therapy and medical outcomes for hospitalized elderly patients with pneumonia (1999) Arch Intern Med, 159, pp. 2562-2572","Blasi, F.; Istituto Malattie Respiratorie, Università di Milano, IRCCS Ospedale Maggiore, Milano, Italy",,,11270810,,GGIMA,,"Italian","GIMT G. Ital. Mal. Torace",Review,"Final",,Scopus,2-s2.0-4944252521
"Sirtori C.","55729842400;","Enhancement of antioxidant and anticytokine defences in severe pulmonary viral infections [Potenziamento delle difese antiossidanti ed anticitochine nelle infezioni virali polmonari gravi]",2003,"GIMT - Giornale Italiano delle Malattie del Torace","57","1",,"45","56",,2,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4944250771&partnerID=40&md5=6a9981a0ddec61939fe1b3861b8c187d","Ordinario di Farmacologia Clinica, Università degli Studi di Milano","Sirtori, C., Ordinario di Farmacologia Clinica, Università degli Studi di Milano","The recent epidemic events related to SARS (Severe Acute Respiratory Syndrome) in China seem etiologically linked to a Coronavirus, although Chlamydia pneumoniae and Paramixovirus (Metapneumovirus) have been previously suspected. The relationship between viral infections and respiratory system is very strict, so that the question arises on the role of viruses and their lesional mechanisms on the lungs: oxidative stress and cytokines activity inductions seem the main possible mechanisms. This observation induces the consideration on the possible therapeutical use, in such condition, of antioxidant and anticytokines molecules, the most documented of which is N-acetylcysteine.","Anticytokines; Antioxidants; Oxidative stress; Respiratory system; SARS; Viruses","acetylcysteine; adenosine triphosphatase (calcium); albumin; alpha tocopherol; ascorbic acid; beta carotene; bilirubin; CCAAT binding factor; cytokine; glutathione; immunoglobulin enhancer binding protein; interleukin 6; interleukin 8; reactive oxygen metabolite; reduced nicotinamide adenine dinucleotide phosphate oxidase; ribavirin; transcription factor AP 1; tumor necrosis factor alpha; uric acid; antiinflammatory activity; antioxidant activity; bronchiolitis; bronchitis; Chlamydophila pneumoniae; clinical feature; conjunctivitis; Coronavirus; Coxsackie virus; cytokine production; Echo virus; epiglottitis; host resistance; human; immunopathogenesis; Influenza virus; laryngitis; Metapneumovirus; nonhuman; oxidative stress; Parainfluenza virus; pathophysiology; pharyngitis; review; rhinitis; Rhinovirus; severe acute respiratory syndrome; tracheobronchitis; virus pneumonia","Hong, B.A., Kong health chief falls ill of suspected SARS virus (2003) Lancet, 361, p. 1106; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Peiris, I.S.M., Lai, S.T., Poon, L.J.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel Coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel Coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Blasi, F., Capone, P., Molisano, A., Efficacy and safety of Thiamphenicol in the clinical setting (2003) GIMMOC, 7, p. 7; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Greenberg, S., Allen, M., Wilson, J., Atmar, R., Respiratory viral infections in adults with and without chronic obstructive pulmonary disease (2000) Am J Resp Crit Care Med, 162, pp. 163-173; Seemungal, T., Harper-Owen, R., Bhowmik, A., Respiratory viruses, symptoms, and inflammatory markers in acute exacerbations and stable chronic obstructive pulmonary disease (2001) Am J Resp Crit Care Med, 164, pp. 1618-1623; Zambon, M., Stockton, J., Clewley, J., Fleming, D., Contribution of inluenza and respiratory syncytial virus to community cases of inluenza-like illness: An observational study (2001) Lancet, 358, pp. 1410-1416; Allegra, L.L., Influenza e Ie sue Complicanze (2002) Mattioli, p. 1885. , Editore, Fidenza; Rizzato G: Rapporti tra BPCO riacutizzata e virus respiratori: il ruolo dello stress ossidativo. L'Internista 2002; 10: 30-5; La Placa M. Principi di Microbiologia Medica. VII Ediz.. Soc. Ed. Esculapio 1995; Rizzato G. Le Nuove Frontiere della Terapia con Antiossidanti N-Acetilcisteina. Effe Edizioni Verona, 2001; Halliwell B: Le specie reattive dell'ossigeno nei sistemi viventi: origine, biochimica e ruolo nelle malattie dell'uomo. In: Allegra L, Crystal R., Grassi C: GSH-System. Glutathione in Antioxidant Defense. Excerpta Medica (Elsevier), Amsterdam, 1992: 24-38; Peterhans, E., Oxidants and antioxidants in viral diseases. Metabolic regulation and autotoxicity (1994) Natural Antioxidants in Human Health and Disease, pp. 489-514. , Frei B, Ed, Academic Press, San Diego, CA; Choi, A.M.K., Oxidant stress responses in influenza virus pneumonia: Gene expression and transcription factor activation (1996) Am J Physiol, 271, pp. 383-391; Knobil, K., Choi, A.M., Weigand, G.W., Jacoby, D.B., Role of oxidants in influenza virus-induced gene expression (1998) Am J Physiol, 274, pp. L134-L142; Biagioli, M.C., Kaul, P., Singh, I., Turner, R.B., The role of oxidative stress in rhinovirus induced elaboration of IL-8 by respiratory epithelial cells (1999) Free Radical Biol Med, 26, p. 454; Kaul, P., Rhinovirus-induced oxidative stress and interleukin-8 elaboration involves p47-phox but is independent of attachment to intercellular adhesion molecule-1 and viral application (2000) J Infect Dis, 181, pp. 1885-1890; Matsuse, T., Latent adenoviral infection inthe pathogenesis of chronic airways obstruction (1992) Am Rev Respir Dis, 146, pp. 177-184; Nevins, J.R., Regulation of the primary expression of the early adenovirus transcription units (1979) J Virol, 32, pp. 727-733; Dyson, N., Harlow, E., Adenovirus E1A targets key regulators of cells proliferation (1992) Cancer Surv, 12, pp. 161-195; Turner, R.B., Association between nasal secretion interleukin-8 concentration and symptom severity in experimental rhinovirus colds (1998) Clin Infect Dis, 26, pp. 840-846; Eleouet, J.F., Chilmonczyk, S., Besnardeau, L., Laude, H., Transmissible gastroenteritis Coronavirus induced programmed cell death in infected cells through a caspase-dependent pathway (1998) J Virol, 72, pp. 4918-4924; Call, M., Frei, B., Can antioxidant vitamins materially reduce oxidative damage in humans? (1999) Free Rad Biol Med, 26, pp. 1034-1053; Albertini A. Ossidanti ed antiossidanti: determinanti fisiopatologici e agenti terapeutici. In: Allegra 1, Crystal R, Grassi C: GSH-System. Glutathione in Antioxidant Defense. Excerpta Medica (Elsevier), Amsterdam, 1992: 20-3; Moldeus, P., Cotgreave, I., Berggren, M., Lung protection by a thio-containing antioxidant: N-acetylcysteine (1986) Respiration, 50, pp. 31-42; Blesa, S., Cortijo, J., Mata, M., Serrano, A., Oral N-acetylcysteine attenuates the rat pulmonary inflammatory response to antigen (2003) Eur Respir J, 21, pp. 394-400; Vernhet, L., Allain, N., Le Vée, M., Blockage of multidrug resistance-associated proteins potentiates the inhibitory effects of arsenic trioxide on CYP1A1 induction by polycyclic aromatic hydrocarbons (2003) J Pharmacol Exp Ther, 304, pp. 145-155; Ghezzi P, Ungheri D. Activity of N-Acetylcysteine alone or in association with Ribavirin in a mouse model of influenza viral infection. 42nd ICAAC Abstracts, American Society for Microbiology, September 27-30, San Diego, CA, 2002: p 431; Ungheri D, Pinasi C, Sanson G, et al. Protective effect of N-Acetylcysteine in a model of influenza infection in mice. I J I P P 2000; 13: 123-8; De Flora, S., Grassi, C., Carati, L., Attenuation of influenza-like symptomatology and improvement of cell-mediated immunity with long-term N-Acetylcysteine treatment (1997) Eur Respir J, 10, pp. 1535-1541; Cristal, R.G., Bast, A., Oxidants and antioxidants: Pathophysiologic determinants and therapeutic agents (1991) Am J Med, 91, pp. 1-145; Spies, C.D., Reinhart, K., Witt, I., Influence of N-Acetylcysteine on indirect indicators of tissue oxygenation in septic shock patients: Results from a prospective, randomized, double-blind study (1994) Crit Care Med, 22, pp. 1738-1746; Henderson, A., Hayes, P., Acetylcysteine as a cytoprotective antioxidant in patients with severe sepsis: Potential new use for an old drug (1994) Ann Pharmacother, 28, pp. 1086-1088","Sirtori, C.; Ordinario di Farmacologia Clinica, Università degli Studi di MilanoItaly",,,11270810,,GGIMA,,"Italian","GIMT G. Ital. Mal. Torace",Review,"Final",,Scopus,2-s2.0-4944250771
"Icardi G., Ansaldi F., Gasparini R.","7004251953;6603564504;7003538152;","SARS-Coronavirus, an emerging pathogen: What are the implications for the safety of blood transfusion? [Il SARS-Coronavirus, un patogeno emergente: Quali implicazioni per la sicurezza del sangue?]",2003,"Blood Transfusion","1","3",,"215","223",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-47749132292&partnerID=40&md5=97ab9a3b85b048770c555147f9bcdbb7","Department of Health Sciences, University of Genoa; Standing Group for the Control of SARS - Ministry of Health, Subgroup on Epidemiological Scenarios; Department of Public Health, University of Trieste; Standing Group for the Control of SARS - Ministry of Health, Subgroup on Diagnosis, Subgroup on SARS and Blood Donation; Standing Group for the Control of SARS - Ministry of Health, Subgroup on Epidemiological Surveillance; Dipartimento di Scienze Della Salute, Via Pastore 1, 16132 Genova, Italy","Icardi, G., Department of Health Sciences, University of Genoa, Standing Group for the Control of SARS - Ministry of Health, Subgroup on Epidemiological Scenarios, Dipartimento di Scienze Della Salute, Via Pastore 1, 16132 Genova, Italy; Ansaldi, F., Department of Public Health, University of Trieste, Standing Group for the Control of SARS - Ministry of Health, Subgroup on Diagnosis, Subgroup on SARS and Blood Donation; Gasparini, R., Department of Health Sciences, University of Genoa, Standing Group for the Control of SARS - Ministry of Health, Subgroup on Epidemiological Surveillance",[No abstract available],,,"Woolhouse, M.E.J., Population biology of emerging and re-emerging pathogens (2002) Trends in Microbiol, 10, pp. S3-S7; Leport, C., Janowski, M., Brun-Vezinet, F., West Nile virus meningomyeloencephalitis - value of interferon assays in primary encephalitis (1984) Ann Med Intern, 135, pp. 460-463; Han, L.L., Popovici, F., Alexander Jr, J.P., Risk factors for West Nile virus infection and meningoencephalitis, Romania,1996 (1999) J Infect Dis, 179, pp. 230-233; Mukinda, V.B., Mwema, G., Kilundu, M., Re-emergence of human monkeypox in Zaire in 1996. Monkeypox Epidemiologic Working Group (1997) Lancet, 349, pp. 1449-1450; Multistate outbreak of monkeypox-Illinois, Indiana, and Wisconsin, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 537-540. , CDC; Scholtissek, C., Burger, H., Bachman, P.A., Hannoun, C., Genetic relatedness of haemaggglutinins of the H1 subtype of influenza A viruses isolated from swine and birds (1983) Virology, 129, pp. 521-523; Hinshaw, V.S., Webster, R.G., Turner, B., Novel influenza A viruses isolated from Canadian feral ducks: Including strain antigenically related to swine influenza (Hsw1N1) viruses (1978) J Gen Virol, 41, pp. 115-127; Guo, Y., Wang, M., Kawaosoka, Y., Characterization of a new avian-like influenza A viruses from horses in China (1992) Virology, 188, pp. 245-255; Scholtissek, C., Burger, H., Kistner, O., Shortridge, K.F., The nucleoprotein as a possible major factor in determining host specificity of influenza H3N2 viruses (1985) Virology, 147, pp. 287-294; Scholtissek, C., Pigs as ""mixing vessels"" for the creation of new pandemic influenza A viruses (1990) Med Principles Pract, 2, pp. 65-71; Chan, P.K., Outbreak of avian influenza A(H5N1) virus infection in Hong Kong in 1997 (2002) Clin Infect Dis, 34, pp. S58-S64; Lin, Y.P., Shaw, M., Gregory, V., Avian-to-human transmission of H9N2 subtype influenza A viruses: Relationship between H9N2 and H5N1 human isolates (2000) Proc Natl Acad Sci USA, 97, pp. 9654-9658; Tsang, K.W., Ho, P.L., Ooi, G., A cluster of cases of Severe Acute Respiratory Syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1977-1985; Poutanen, S.M., Low, D.E., Henry, B., Identification of Severe Acute Respiratory Syndrome in Canada (2003) N Engl J Med, 348, pp. 1995-2005; Ksiatek, T.G., Erdman, D., Gordsmith, C., A novel Coronavirus associated with Severe Acute Respiratory Syndrome (2003) N Engl J Med, 348, pp. 1947-1958; Drosten, C., Gunther, S., Preiser, W., Identification of a novel Coronavirus in patients with Severe Acute Respiratory Syndrome (2003) N Engl J Med, 348, pp. 1667-1676; Marra, M.A., Jones, S.J.M., Astell, C.R., The genome sequence of the SARS-associated Coronavirus (2003) Science, 300, pp. 1399-1404; Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel Coronavirus associated with Severe Acute Respiratory Syndrome (2003) Science, 300, pp. 1394-1399; Lai, M.M.C., RNA recombination in animal and plant viruses (1992) Microbiol Rev, 56, pp. 61-79; Guan, Y., Zheng, B.J., Shortridge, K.F., (2003), Isolation and characterization of viruses related to SARS Coronavirus from animals in Southern China. Personal Communication in WHO Global Conference on Severe Acute Respiratory Syndrome. Kuala Lumpur, Malaysia, 17-18 June; Weirgartl, H., Copps, J., Drebot, M., (2003), Susceptibility of pigs and chickens to SARS Coronavirus. Personal Communication in WHO Global Conference on Severe Acute Respiratory Syndrome. Kuala Lumpur, Malaysia, 17-18 June; Peiris, J.S.M., SARS: aetiology. Personal Communication in WHO Global Conference on Severe Acute Respiratory Syndrome. Kuala Lumpur, Malaysia, 17-18 June 2003; Peiris, J.S.M., Chu, C.M., Cheng, V.C.C., Clinical progression and viral load in a community outbreak of Coronavirus associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1771; Ruan, Y.J., Wei, C.L., Ee, A.L., Comparative full-length genome sequence analysis of 14 SARS Coronavirus isolates and common mutations associated with putative origins of infection (2003) Lancet, 361, pp. 1779-1786; WHO SARS Team. SARS laboratory diagnosis. Personal Communication in WHO Global Conference on Severe Acute Respiratory Syndrome. Kuala Lumpur, Malaysia, 17-18 June 2003; Dhingra, N., SARS as an emerging pathogen: implications for blood safety. Personal Communication in WHO Global Conference on Severe Acute Respiratory Syndrome. Kuala Lumpur, Malaysia, 17-18 June 2003; Lloyd, N., Blood safety, WHO strategies. Personal Communication in: The impact of SARS and other emerging pathogens on transfusion medicine. Brussels, Belgium, 16 June 2003","Icardi, G.; Dipartimento di Scienze Della Salute, Via Pastore 1, 16132 Genova, Italy",,,17232007,,,,"Italian; English","Blood Transfusion",Review,"Final",,Scopus,2-s2.0-47749132292
"Enjuanes L., Almazán F., Ortego J.","7006565392;6603712040;35254237800;","Virus-based vectors for gene expression in mammalian cells: Coronavirus",2003,"New Comprehensive Biochemistry","38",,,"151","168",,8,"10.1016/S0167-7306(03)38010-X","https://www.scopus.com/inward/record.uri?eid=2-s2.0-36148930917&doi=10.1016%2fS0167-7306%2803%2938010-X&partnerID=40&md5=5d4cf59a74eab9def0cd370ff6695138","Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, CSIC, Campus Univ. Autonoma, Cantoblanco, 28049 Madrid, Spain","Enjuanes, L., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, CSIC, Campus Univ. Autonoma, Cantoblanco, 28049 Madrid, Spain; Almazán, F., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, CSIC, Campus Univ. Autonoma, Cantoblanco, 28049 Madrid, Spain; Ortego, J., Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, CSIC, Campus Univ. Autonoma, Cantoblanco, 28049 Madrid, Spain",[No abstract available],,,,"Enjuanes, L.; Department of Molecular and Cell Biology, Centro Nacional de Biotecnología, CSIC, Campus Univ. Autonoma, Cantoblanco, 28049 Madrid, Spain; email: l.enjuanes@cnb.uam.es",,,01677306,044451371X; 9780444513717,,,"English","New Compr. Biochem.",Review,"Final",Open Access,Scopus,2-s2.0-36148930917
[No author name available],[No author id available],"Erratum: Outbreak of Severe Acute Respiratory Syndrome (SARS) and coronavirus testing - United States, 2003 (Morbidity and Mortality Weekly Report 52:14 (301))",2003,"Morbidity and Mortality Weekly Report","52","15",,"345","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-32544439380&partnerID=40&md5=a030e410713b7ffd69a104b38672bdd8",,"",[No abstract available],,,,,,,01492195,,,,"English","Morb. Mortal. Wkly. Rep.",Erratum,"Final",,Scopus,2-s2.0-32544439380
"Zwijnenberg R.","6507138069;","The recent availability in Australia of a vaccine to protect dogs against both coronavirus and Leptospira icterohaemorrhagiae.",2003,"Australian veterinary journal","81","12",,"731","",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342648806&partnerID=40&md5=d33ff56ad9f7b05c03cc86590108a9f2",,"Zwijnenberg, R.",[No abstract available],,"bacterial vaccine; virus vaccine; animal; animal disease; Australia; Coronavirus; dog; dog disease; immunology; Leptospira; leptospirosis; letter; vaccination; virus infection; Animals; Australia; Bacterial Vaccines; Coronavirus; Coronavirus Infections; Dog Diseases; Dogs; Leptospira; Leptospirosis; Vaccination; Viral Vaccines",,"Zwijnenberg, R.",,,00050423,,,"15080481","English","Aust Vet J",Letter,"Final",,Scopus,2-s2.0-2342648806
"Jalava K.","6603787185;","What have we learned about the coronaviruses in animals? [Mitä opimme eläinten koronaviruksista?]",2003,"Duodecim; laaketieteellinen aikakauskirja","119","17",,"1609","1610",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0642312515&partnerID=40&md5=54bcd6fec28705532ece095a5eb21502",,"Jalava, K.",[No abstract available],,"animal; animal disease; Coronavirus; disease carrier; disease transmission; ecosystem; editorial; epidemic; genetics; human; pathogenicity; public health; SARS coronavirus; severe acute respiratory syndrome; virus infection; Animals; Coronavirus; Coronavirus Infections; Disease Outbreaks; Disease Reservoirs; Ecosystem; Humans; Public Health; SARS Virus; Severe Acute Respiratory Syndrome",,"Jalava, K.",,,00127183,,,"14587440","Finnish","Duodecim",Editorial,"Final",,Scopus,2-s2.0-0642312515
"Hemilä H.","56223570700;","Vitamin C and SARS coronavirus [6]",2003,"Journal of Antimicrobial Chemotherapy","52","6",,"1049","1050",,2,"10.1093/jac/dkh002","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346888667&doi=10.1093%2fjac%2fdkh002&partnerID=40&md5=7815d7763aad926de75ddd9226992afa","Department of Public Health, University of Helsinki, Helsinki FIN-00014, Finland","Hemilä, H., Department of Public Health, University of Helsinki, Helsinki FIN-00014, Finland",[No abstract available],"Ascorbic acid; Pneumonia; Severe acute respiratory syndrome","ascorbic acid; interferon; placebo; cytokine production; drug mechanism; epidemic; human; immune system; infection sensitivity; letter; lymphocyte transformation; phagocyte; SARS coronavirus; severe acute respiratory syndrome; T lymphocyte; Ascorbic Acid; Humans; SARS Virus; Severe Acute Respiratory Syndrome","Holmes, K.V., SARS-associated coronavirus (2003) New England Journal of Medicine, 348, pp. 1948-1951; Leibovitz, B., Siegel, B.V., Ascorbic acid and the immune response (1981) Advances in Experimental Medicine and Biology, 135, pp. 1-25; Hemilä, H., Douglas, R.M., Vitamin C and acute respiratory infections (1999) International Journal of Tuberculosis and Lung Diseases, 3, pp. 756-761; Atherton, J.G., Kratzing, C.C., Fisher, A., The effect of ascorbic acid on infection of chick-embryo ciliated tracheal organ cultures by coronavirus (1978) Archives of Virology, 56, pp. 195-199; Davelaar, F.G., Bos, J., Ascorbic acid and infectious bronchitis infections in broilers (1992) Avian Pathology, 21, pp. 581-589; Hemilä, H., Vitamin C intake and susceptibility to pneumonia (1997) Pediatric Infectious Diseases Journal, 16, pp. 836-837","Hemilä, H.; Department of Public Health, University of Helsinki, Helsinki FIN-00014, Finland; email: harri.hemila@helsinki.fi",,,03057453,,JACHD,"14613951","English","J. Antimicrob. Chemother.",Letter,"Final",Open Access,Scopus,2-s2.0-0346888667
"Ng E.K.O., Ng P.-C., Hon K.L.E., Cheng W.T.F., Hung E.C.W., Chan K.C.A., Chiu R.W.K., Li A.M., Poon L.L.M., Hui D.S., Tam J.S., Fok T.-F., Lo Y.M.D.","21135553700;17137242500;8134452900;14122898400;7004256338;13403797200;7103038413;7403291810;7005441747;7101862411;24788939600;7006455238;7401935391;","Serial Analysis of the Plasma Concentration of SARS Coronavirus RNA in Pediatric Patients with Severe Acute Respiratory Syndrome",2003,"Clinical Chemistry","49","12",,"2085","2088",,41,"10.1373/clinchem.2003.024588","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345376994&doi=10.1373%2fclinchem.2003.024588&partnerID=40&md5=3f241a4e80dbbbe131e572c13f646092","Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30 - 32 Ngan Shing St., Shatin, New Territories, Hong Kong","Ng, E.K.O., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Ng, P.-C., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Hon, K.L.E., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Cheng, W.T.F., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Hung, E.C.W., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Chan, K.C.A., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Chiu, R.W.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Li, A.M., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Poon, L.L.M., Department of Microbiology, University of Hong Kong, Hong Kong, Hong Kong; Hui, D.S., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Tam, J.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Fok, T.-F., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong; Lo, Y.M.D., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Hong Kong SAR, Hong Kong, Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30 - 32 Ngan Shing St., Shatin, New Territories, Hong Kong",[No abstract available],,"virus RNA; adolescent; article; blood sampling; child; clinical article; controlled study; Coronavirus; human; nucleotide sequence; quantitative analysis; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; virus load; virus pneumonia; Adolescent; Child; Child, Preschool; Humans; Infant; Plasma; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sensitivity and Specificity; Severe Acute Respiratory Syndrome; Coronavirus; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Fouchier, R.A., Kuiken, T., Schutten, M., Van Amerongen, G., Van Doornum, G.J., Van Den Hoogen, B.G., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Poon, L.L., Wong, O.K., Luk, W., Yuen, K.Y., Peiris, J.S., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 953-955; Peiris, J.S., Chu, C.M., Cheng, V.C., Chan, K.S., Hung, I.F., Poon, L.L., Clinical progression and viral load in a community outbreak of coronavirus-associated SARS pneumonia: A prospective study (2003) Lancet, 361, pp. 1767-1772; Ng, E.K.O., Hui, D.S., Chan, K.C., Hung, E.C., Chiu, R.W., Lee, N., Quantitative analysis and prognostic implication of SARS-coronavirus RNA in the plasma and serum of patients with severe acute respiratory syndrome (2003) Clin Chem, 49, pp. 1976-1980; Chiu, W.K., Cheung, P.C., Ng, K.L., Ip, P.L., Sugunan, V.K., Luk, D.C., Severe acute respiratory syndrome in children: Experience in a regional hospital in Hong Kong (2003) Pediatr Crit Care Med, 4, pp. 279-283; Hon, K.L., Leung, C.W., Cheng, W.T., Chan, P.K., Chu, W.C., Kwan, Y.W., Clinical presentations and outcome of severe acute respiratory syndrome in children (2003) Lancet, 361, pp. 1701-1703; Tsui, S.K., Chim, S.S., Lo, Y.M.D., Coronavirus genomic-sequence variations and the epidemiology of the severe acute respiratory syndrome (2003) N Engl J Med, 349, pp. 187-188","Lo, Y.M.D.; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, 30 - 32 Ngan Shing St., Shatin, New Territories, Hong Kong; email: loym@cuhk.edu.hk",,,00099147,,CLCHA,"14633884","English","Clin. Chem.",Article,"Final",Open Access,Scopus,2-s2.0-0345376994
"Hung E.C.W., Chim S.S.C., Chan P.K.S., Tong Y.K., Ng E.K.O., Chiu R.W.K., Leung C.-B., Sung J.J.Y., Tam J.S., Lo Y.M.D.","7004256338;6701728226;32067487100;7202614141;21135553700;7103038413;16750769500;35405352400;24788939600;7401935391;","Detection of SARS Coronavirus RNA in the Cerebrospinal Fluid of a Patient with Severe Acute Respiratory Syndrome",2003,"Clinical Chemistry","49","12",,"2108","2109",,32,"10.1373/clinchem.2003.025437","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344945638&doi=10.1373%2fclinchem.2003.025437&partnerID=40&md5=2bacbe609dd04ecf7579a6eca5ea1fd9","Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong","Hung, E.C.W., Department of Paediatrics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chim, S.S.C., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chan, P.K.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Tong, Y.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Ng, E.K.O., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Chiu, R.W.K., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Leung, C.-B., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Sung, J.J.Y., Dept. of Medicine and Therapeutics, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Tam, J.S., Department of Microbiology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; Lo, Y.M.D., Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong",[No abstract available],,"antibiotic agent; antifungal agent; phenytoin; propofol; ribavirin; steroid; valproic acid; virus RNA; adult; case report; cerebrospinal fluid examination; clinical feature; Coronavirus; diagnostic imaging; disease activity; disease course; female; human; laboratory test; letter; neurologic disease; oxygen saturation; patient; peritoneal dialysis; peritonitis; pneumonia; respiratory failure; SARS coronavirus; seizure; seroconversion; severe acute respiratory distress syndrome; treatment failure; treatment outcome; virus detection; virus isolation; Female; Humans; Middle Aged; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Severe Acute Respiratory Syndrome; Coronavirus; SARS coronavirus","Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Peiris, J., Lai, S., Poon, L., Guan, Y., Yam, L., Lim, W., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ng, E.K.O., Hui, D.S., Chan, A.K.C., Hung, E.C.W., Chiu, R.W.K., Lee, N., Quantitative analysis and prognostic implication of SARS-coronavirus RNA in the plasma and serum of patients with severe acute respiratory syndrome (2003) Clin Chem, 49; Arbour, N., Day, R., Newcombe, J., Talbot, P.J., Neuroinvasion by human respiratory coronaviruses (2000) J Virol, 74, pp. 8913-8921; Matthews, A.E., Weiss, S.R., Paterson, Y., Murine hepatitis virus - A model for virus-induced CNS demyelination (2002) J Neurovirol, 8, pp. 76-85","Lo, Y.M.D.; Department of Chemical Pathology, Chinese University of Hong Kong, Prince of Wales Hospital, Shatin, New Territories, Hong Kong; email: loym@cuhk.edu.hk",,,00099147,,CLCHA,"14633896","English","Clin. Chem.",Letter,"Final",Open Access,Scopus,2-s2.0-0344945638
[No author name available],[No author id available],"Prevalence of IgG antibody to SARS-associated coronavirus in animal traders - Guangdong Province, China, 2003",2003,"Morbidity and Mortality Weekly Report","52","41",,"986","987",,77,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0141906365&partnerID=40&md5=b530462e76a5e3e8bb5449fe1f9c476b",,"",[No abstract available],,"immunoglobulin G; virus antibody; animal; animal husbandry; article; blood; China; disease carrier; epidemiology; heterozygote; human; isolation and purification; occupational exposure; SARS coronavirus; severe acute respiratory syndrome; Animal Husbandry; Animals; Antibodies, Viral; Carrier State; China; Disease Reservoirs; Humans; Immunoglobulin G; Occupational Exposure; SARS Virus; Seroepidemiologic Studies; Severe Acute Respiratory Syndrome","Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Li, L.H., Peng, G.W., Liang, W.J., Epidemiological analysis on SARS clustered cases in Guangdong province (2003) South China J Prev Med, 29, pp. 3-5; Guan, Y., Zheng, B.J., He, Y.Q., Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China (2003) Science, 302, pp. 276-278; Ng, S.K., Possible role of an animal vector in the SARS outbreak at Amoy Gardens (2003) Lancet, 362, pp. 570-572; He, J.F., Xu, R.H., Yu, D.W., Severe acute respiratory syndrome in Guangdong Province of China: Epidemiology and control measures (2003) Chin J Prev Med, 37, pp. 227-232; Large outbreak of severe acute respiratory syndrome (SARS) in Beijing (2003) Emerg Infect Dis, , (in press)",,,,01492195,,,"14561956","English","Morb. Mortal. Wkly. Rep.",Review,"Final",,Scopus,2-s2.0-0141906365
[No author name available],[No author id available],"Severe Acute Respiratory Syndrome (SARS) and coronavirus testing - United States, 2003",2003,"Morbidity and Mortality Weekly Report","52","14",,"297","302",,64,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038439230&partnerID=40&md5=9d42c4d28e50075a9cab7d93b545c518",,"",[No abstract available],,"adult; article; case report; China; communicable disease; Coronavirus; diagnosis, measurement and analysis; female; Hong Kong; human; infection control; isolation and purification; male; middle aged; pregnancy; pregnancy complication; risk factor; SARS coronavirus; severe acute respiratory syndrome; Singapore; travel; United States; virology; Adult; China; Communicable Diseases, Emerging; Coronavirus; Female; Hong Kong; Humans; Infection Control; Laboratory Techniques and Procedures; Male; Middle Aged; Pregnancy; Pregnancy Complications, Infectious; Risk Factors; SARS Virus; Severe Acute Respiratory Syndrome; Singapore; Travel; United States","Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR, 52, pp. 241-248; Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en; Cumulative Number of Reported Cases of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sarscountry/2003_04_02/en; Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada N Eng J Med., , http://content.nejm.org/cgi/content/abstract/NEJMoa030634v1; Summary on Major Findings in Relation to Coronavirus by Members of the WHO Multi-centre Collaborative Network on SARS Aetiology and Diagnosis, , http://www.who.int/csr/sars/findings/en; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, , http://www.thelancet.com/journal/vol361/iss9364/full/llan.361.9364. early_online_publication.25242.1; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, , http://content.nejm.org/cgi/reprint/NEJMoa030666v1; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Eng J Med, , http://content.nejm.org/cgi/content/abstract/NEJMoa030666v1; Hayden, F.G., Antiviral drugs (other than antiretrovirals) (2000) Mandell, Douglas, and Bennett's Principles and Practice of Infectious Diseases, 5th Ed., , Mandell GL, Bennett JE, Dolin R, eds. Philadelphia, Pennsylvania: Churchill Livingstone",,,,01492195,,,"12731699","English","Morb. Mortal. Wkly. Rep.",Review,"Final",,Scopus,2-s2.0-0038439230
"Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T., Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lü F., Tan G., Cao W., Yang R., Wang J., Li W., Xu Z., Li Y., Wu Q., Lin W., Chen W., Tang L., Deng Y., Han Y., Li C., Lei M., Li G., Li W., Lü H., Shi J., Tong Z., Zhang F., Li S., Liu B., Liu S., Dong W., Wang J., Wong G.K.-S., Yu J., Yang H.","6701908544;7403313352;56512847900;7102879235;7402308930;36124063300;56306611900;8266260600;56661639900;14019808300;12141082300;7409748910;57196199263;8266261300;7502086390;15318951200;55718189300;7402967940;57207324580;57199658059;55547041600;57200022156;56127183500;36007796100;57207045546;7404602222;57211371580;35236384200;57198909361;8214333500;35310510700;55696002400;57206922669;54684251100;55718638800;55488128800;55491813100;57205922887;57216131818;7409241896;24366565200;7409459608;57198833517;55552724800;55554420600;8679878600;34573719100;","A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJ01)",2003,"Chinese Science Bulletin","48","10",,"941","948",,82,"10.1360/03wc0186","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038083173&doi=10.1360%2f03wc0186&partnerID=40&md5=b34d0d9be5c6567ca61da22b67675999","Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China","Qin, E., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Zhu, Q., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Yu, M., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Fan, B., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Chang, G., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Si, B., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Yang, B., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Peng, W., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Jiang, T., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Liu, B., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Deng, Y., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Liu, H., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Zhang, Y., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Wang, C., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Li, Y., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Gan, Y., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Li, X., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Lü, F., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Tan, G., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Cao, W., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Yang, R., Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; Wang, J.; Li, W.; Xu, Z.; Li, Y.; Wu, Q.; Lin, W.; Chen, W.; Tang, L.; Deng, Y.; Han, Y.; Li, C.; Lei, M.; Li, G.; Li, W.; Lü, H.; Shi, J.; Tong, Z.; Zhang, F.; Li, S.; Liu, B.; Liu, S.; Dong, W.; Wang, J.; Wong, G.K.-S.; Yu, J.; Yang, H.","The genome sequence of the Severe Acute Respiratory Syndrome (SARS)-associated virus provides essential information for the identification of pathogen(s), exploration of etiology and evolution, interpretation of transmission and pathogenesis, development of diagnostics, prevention by future vaccination, and treatment by developing new drugs. We report the complete genome sequence and comparative analysis of an isolate (BJ01) of the coronavirus that has been recognized as a pathogen for SARS. The genome is 29725 nt in size and has 11 ORFs (Open Reading Frames). It is composed of a stable region encoding an RNA-dependent RNA polymerase (composed of 2 ORFs) and a variable region representing 4 CDSs (coding sequences) for viral structural genes (the S, E, M, N proteins) and 5 PUPs (putative uncharacterized proteins). Its gene order is identical to that of other known coronaviruses. The sequence alignment with all known RNA viruses places this virus as a member in the family of Coronaviridae. Thirty putative substitutions have been identified by comparative analysis of the 5 SARS-associatcd virus genome sequences in GenBank. Fifteen of them lead to possible amino acid changes (non-synonymous mutations) in the proteins. Three amino acid changes, with predicted alteration of physical and chemical features, have been detected in the S protein that is postulated to be involved in the immunoreactions between the virus and its host. Two amino acid changes have been detected in the M protein, which could be related to viral envelope formation. Phylogenetic analysis suggests the possibility of non-human origin of the SARS-associated viruses but provides no evidence that they are man-made. Further efforts should focus on identifying the etiology of the SARS-associated virus and ruling out conclusively the existence of other possible SARS-related pathogen(s).","Coronavirus; Genome; Phylogeny; Severe Acute Respiratory Syndrome (SARS)","Coronaviridae; Coronavirus; RNA viruses","Poutanen, S.M., Low, D.E., Henry, B., Identification of severe acute respiratory syndrome in Canada (2003) N Engl. J. Med., , www.nejm.org, March 31, 10.1056/NEMoa 030634; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., , www.nejm.org, April 7, 10.1056/NEJMoa 030685; Peiris, J., Lai, S., Poon, L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl. J. Med., , www.nejm.org, April 10, 10.1056/NEJMoa 020781; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl. J. Med., , www.nejm.org, April 10, 10.1056/ NEJMoa 030747; Zhu, Q.-Y., Qin, E.D., Wang, C.E., Isolation and identification of a novel coronavirus from patients with SARS (2003) J. Chin. Biotech., p. 30. , in press; Alam, S.L., Atkins, J.F., Gesteland, R.F., Programmed ribosomal frameshifting: Much ado about knotting! (1999) Proc. Natl. Acad. Sci. USA, 96, pp. 14177-14179; (2001) Virus Taxonomy (7th Ed), , Regenmortel, V., (edi) Academic Press; Uchil, P.D., Satchidanandam, V., Characterization of RNA synthesis, replication mechanism, and in vitro RNA-dependent RNA polymerase activity of Japanese encephalitis virus (2003) Virology, 307, pp. 358-371; Henkel, J., Attacking AIDS with a ""cocktail"" therapy? (1999) FDA Consum, 33, pp. 12-17; Popova, R., Zhang, X., The spike but not the hemagglutinin/esterase protein of bovine coronavirus is necessary and sufficient for viral infection (2002) Virology, 294, pp. 222-236","Zhu, Q.; Institute of Microbiology and Epidemiology, Chinese Academy of Military Medical Sciences, Beijing 100071, China; email: zhuqy@nic.bmi.ac.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-0038083173
"Duan Q., Zhu H., Yang Y., Li W., Zhou Y., He J., He K., Zhang H., Zhou T., Song L., Gan Y., Tan H., Jin B., Li H., Zuo T., Chen D., Zhang X.","56647628200;57188808751;57211151359;7501794094;57191653017;36080126400;57203963362;55796541100;57213730865;14061152200;15318951200;57198663342;7201509667;15034157000;57206179002;55334730900;56174604800;","Reovirus, isolated from SARS patients",2003,"Chinese Science Bulletin","48","13",,"1293","1296",,11,"10.1360/03wc0294","https://www.scopus.com/inward/record.uri?eid=2-s2.0-24644522157&doi=10.1360%2f03wc0294&partnerID=40&md5=f06949be4faaa5b1593385e000078f1a","Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; National Center of Biomedical Analysis, Beijing 100850, China","Duan, Q., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Zhu, H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Yang, Y., National Center of Biomedical Analysis, Beijing 100850, China; Li, W., National Center of Biomedical Analysis, Beijing 100850, China; Zhou, Y., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; He, J., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; He, K., National Center of Biomedical Analysis, Beijing 100850, China; Zhang, H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Zhou, T., National Center of Biomedical Analysis, Beijing 100850, China; Song, L., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Gan, Y., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Tan, H., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Jin, B., National Center of Biomedical Analysis, Beijing 100850, China; Li, H., National Center of Biomedical Analysis, Beijing 100850, China; Zuo, T., Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; Chen, D., National Center of Biomedical Analysis, Beijing 100850, China; Zhang, X., National Center of Biomedical Analysis, Beijing 100850, China","Beijing has been severely affected by SARS, and SARS-associated coronavirus has been confirmed as its cause. However, clinical and experimental evidence implicates the possibility of co-infection. In this report, reovirus was isolated from throat swabs of SARS patients, including the first case in Beijing and her mother. Identification with the electron microscopy revealed the characteristic features of reovirus. 24 of 38 samples from other SARS cases were found to have serologic responses to the reovirus. Primers designed for reovirus have amplified several fragments of DNA, one of which was sequenccd (S2 gene fragment), which indicates it as a unique reovirus (orthoreovirus). Preliminary animal experiment showed that inoculation of the reovirus in mice caused death with atypical pneumonia. Nevertheless, the association of reovirus with SARS outbreak requires to be further investigated.","Coronavirus; Electron microscopy; Reovirus; SARS","Animalia; Coronavirus; Orthoreovirus; Reovirus sp.; SARS coronavirus","Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361 (9366), pp. 1319-1325; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1953-1966; Drosten, C., Günther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348 (20), pp. 1967-1976; Qin, E.D., Zhu, Q.Y., Yu, M., A complete sequence and comparative analysis of a SARS-associated virus (Isolate BJO1) (2003) Chinese Science Bulletin, 48 (10), pp. 941-948; Enserink, M., Calling all coronavirologists (2003) Science, 300 (18), pp. 413-414; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348 (20), pp. 1986-1994; Tillotson, J.R., Lerner, A.M., Reovirus type 3 associated with fatal pneumonia (1967) N. Engl. J. Med., 276 (19), pp. 1060-1063; Bellum, S.C., Dove, D., Harley, R.A., Respiratory reovirus 1/L induction of intraluminal fibrosis, A model for the study of bronchiolitis obliterans organizing pneumonia (1997) Am. J. Pathol., 130 (6), pp. 2243-2254; London, L., Majeski, E.I., Paintlia, M.K., Respiratory reovirus 1/L induction of diffuse alveolar damage: A model of acute respiratory distress syndrome (2003) Exp. Mol. Pathol., 72 (1), pp. 24-36; Lamirande, E.W., Nichols, D.K., Owens, J.W., Isolation and experimental transmission of a reovirus pathogenic in ratsnakes (Elaphe species) (1999) Virus Res., 63 (1-2), pp. 135-141","Duan, Q.; Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Beijing 100071, China; email: duanq@nic.bmi.ac.cn",,,10016538,,CSBUE,,"English","Chin. Sci. Bull.",Article,"Final",,Scopus,2-s2.0-24644522157
"Liu T.C.-Y., Zeng C.-C., Jiao J.-L., Liu S.-H.","36087645000;56048141100;7102382944;34979082300;","On the mechanism of low intensity laser irradiation effects on virus",2003,"Proceedings of SPIE - The International Society for Optical Engineering","5254",,,"150","154",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1842529215&partnerID=40&md5=641e6f0daadf8374b581656ff67b4d76","Lab. of Laser Sports Medicine, South China Normal University, Guangzhou 510631, China; Key Lab. of Biomedical Photonics, Ministry of Education of China, State Key Lab. of Laser Technology, Wuhan 430074, China; Sch. Info./Optoelectron. Sci./Eng., South China Normal University, Guangzhou 510631, China; TCM Department, Medical College, Jinan University, Guangzhou 510632, China","Liu, T.C.-Y., Lab. of Laser Sports Medicine, South China Normal University, Guangzhou 510631, China, Key Lab. of Biomedical Photonics, Ministry of Education of China, State Key Lab. of Laser Technology, Wuhan 430074, China; Zeng, C.-C., Sch. Info./Optoelectron. Sci./Eng., South China Normal University, Guangzhou 510631, China; Jiao, J.-L., TCM Department, Medical College, Jinan University, Guangzhou 510632, China; Liu, S.-H., Sch. Info./Optoelectron. Sci./Eng., South China Normal University, Guangzhou 510631, China","Liu TCY et al have suggested the membrane receptor mediated signal transduction mechanism (STM) on photobiomodulation, which was verified by successful applications. In this paper, STM is extended to virus, and called VSTM. The key of VSTM is the conformational changes of envelope glycoproteins, which is realized by light induced electron excitation. As the frequency of the absorption light of envelope glycoproteins is greater than the one of light from UVA (320-400 nm) to IR, the envelope glycoprotein absorption of the light is non-resonant, and its transition rate is extraordinarily small, but can be amplified by the coherent state of the identical and independent envelope glycoproteins. We apply VSTM to discuss the possibility that light from UVA to ER is used to inactivate the coronavirus of severe acute respiratory syndrome.","Low intensity laser; SARS coronavirus; Virus","Low intensity lasers; SARS coronavirus; Severe acute respiratory syndrome (SARS); Biological membranes; Light absorption; Monochromators; Physiological models; Proteins; Pulmonary diseases; Viruses; Laser beam effects","Prodouz, K.N., Fratantoni, J.C., Boone, E.J., Bonner, R.F., Use of laser-UV for inactivation of virus in blood products. Blood (1987) Blood, 70 (2), pp. 589-592; Perrin, D., Jolivald, J.R., Triki, H., Garbarg-Chenon, A., Lamotte, D.B., Lefevre, B., Malka, G., Nicolas, J.C., Effect of laser irradiation on latency of herpes simplex virus in a mouse model (1997) Pathol Biol (Paris), 45 (1), pp. 24-27; Schindl, A., Neumann, R., Low-intensity laser therapy is an effective treatment for recurrent herpes simplex infection. Results from a randomized double-blind placebo-controlled study (1999) J Invest Dermatol, 113 (2), pp. 221-223; Leonova, G.N., Maistrovskaia, O.S., Krylova, N.V., Effect of low-intensity radiation on the course of experimental tick-borne encephalitis (1997) Vopr Virusol, 42 (3), pp. 129-133. , in Russian; Jiang, Y.Q., Li, C.Y., Zhou, Y., Zhang, L.J., Xiao, L.T., Jia, S.T., Ma, C.G., Zhou, G.S., The mechanism study of low energy laser intravascular irradiation therapy (2001) Acta Laser Biology Sinica, 10 (3), pp. 208-211; Karu, T.I., (1998) The Science of Low-Power Laser Therapy, , Gordon and Breach Science Publishers, Amsterdam; Liu, T.C.Y., Zhao, Y.P., Information Biology on Low Intensity Laser (1999) SPIE, 3863, pp. 444-451; Liu, T.C.Y., Duan, R., Li, Y., Li, Y.L., Collective phototransduction: A potential mechanism of laser biomodulation (2001) Lasers Surg. Med, S13, p. 10; Liu, T.C.Y., Duan, R., Yin, P.J., Li, Y., Li, S.L., Membrane mechanism of low intensity laser Biostimulation on a cell (2000) SPIE, 4224, pp. 186-192; Liu, T.C.Y., Jiao, J.L., Liu, S.H., Extended biological information model of laser biomodulation (2003) Lasers Surg. Med, S15, p. 42; Liu, T.C., Li, Y., Duan, R., Cai, X.W., Biomodulation of light on cells in laser surgery (2002) SPIE, 4536, pp. 123-126; Leung, P.C., Ooi, E.E., (2003) SARS War, , Singapore: World Scientific Publishing Co., Inc; Masters, P., (2003) Molecular Biology of Coronaviruses, , New York: SARS in the Context of Emerging Infectious Threats; Kathryn, V.H., (2003) Coronavirus Transmission and Persistence, , New York: SARS in the Context of Emerging Infectious Threats; Thomas, M.G., Michael, J.B., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374","Liu, T.C.-Y.; Lab. of Laser Sports Medicine, South China Normal University, Guangzhou 510631, China; email: liutcy@scnu.edu.cn","Luo Q.Tuchin V.V.Gu M.Wang L.V.",,0277786X,,PSISD,,"English","Proc SPIE Int Soc Opt Eng",Conference Paper,"Final",,Scopus,2-s2.0-1842529215
"Engel W.K.","35258839100;","Intravenous immunoglobulin G is remarkably beneficial in chronic immune dysschwannian/dysneuronal polyneuropathy, diabetes-2 neuropathy, and potentially in severe acute respiratory syndrome",2003,"Acta Myologica","22","DEC.",,"97","103",,8,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-1542720562&partnerID=40&md5=7a9667ede325c86bc3629e5013d5a81d","University of Southern California, Keck School of Medicine, Good Samaritan, Hospital, Los Angeles, CA, United States","Engel, W.K., University of Southern California, Keck School of Medicine, Good Samaritan, Hospital, Los Angeles, CA, United States","Chronic Immune Dysschwannian/Dysneuronal Polyneuropathy is an autoimmune peripheral-nerve and/or nerve-root disorder known to usually respond to intravenous immunoglobulin-G treatment. Benefit can involve any combination of motor-nerve fibers and large and small sensory-nerve fibers responsible for a progressively crippling, unbalancing, discomforting or painful disorder. ""Diabetic neuropathy"" is commonly considered untreatable. However, 81% of my 48 recently-summarized type-2 diabetes patients with polyneuropathy, adequately-treated with intravenous immunoglobulin-G, off-label, were relieved, sometimes completely, of various motor and sensory symptoms, including pain, thereby resembling Chronic Immune Dysschwannian/Dysneuronal Polyneuropathy. Spinal fluid protein in them is often elevated, higher values seeming to auger a better intravenous immunoglobulin-G response. Continuing the improvement requires continuing the intravenous immunoglobulin-G treatment, indicating both intravenous immunoglobulin-G responsiveness and dependency. The intravenous immunoglobulin-G responsive type-2 diabetes polyneuropathy usually is dysschwannian, sometimes mainly dysneuronal intravenous immunoglobulin-G, the most beneficial and safest treatment, is costly, but if intravenous immunoglobulin-G-treatability of a dysimmune component of type-2 diabetes neuropathy is overlooked, dismissed or rejected, as commonly happens, other costs are high regarding the patient's worsening morbidity and disability, and resultant need for increased medical care. A novel intravenous immunoglobulin-G regimen effective for fragile patients is Two Non-Consecutive-Days Every Week, using 0.4 gm/kg body wt/day. Possible molecular mechanisms of intravenous immunoglobulin-G benefit are discussed. I propose that a) there is a higher incidence of Chronic Immune Dysschwannian/Dysneuronal Polyneuropathy-like neuropathy in type-2 diabetes patients and in patients with a strong family history of type-2 diabetes, and b) the intravenous immunoglobulin-G-treatable neuropathy in type-2 diabetes can be brought on by the genetico-diabetoid-2 state. The genetic-metabolic milieu (but not necessarily glucose dysmetabolism per se.) of type-2 diabetes putatively predisposes to the presumably-dysimmune intravenous immunoglobulin-G-responsive polyneuropathy. In some of our patients, especially ones having a strong type-2 diabetes genetic background, the intravenous immunoglobulin-G-responsive neuropathy preceded the diagnosis of type-2 diabetes by 5-10 years. Accordingly, Chronic Immune Dysschwannian/Dysneuronal Polyneuropathy patients having a strong type-2 diabetes genetic background are designated ""genetico-diabetoid-2 neuropathy"" prior to their manifesting type-2 diabetes. Intravenous immunoglobulin-G is herein suggested as a treatment for Severe Acute Respiratory Syndrome, a recent, and feared-repetitive, pandemic with many fatalities caused by a highly-contagious mutant coronavirus, for which there is no definitive treatment. Intravenous immunoglobulin-G might: a) combat a dysimmune component of Severe Acute Respiratory Syndrome, including the reactive cytokine-chemokine storm against respiratory tissues; b) contain some antibodies effective against the coronavirus non-specific components of Severe Acute Respiratory Syndrome; c) block host-cell receptors for the virus; and d) counteract secondary infections.",,"chemokine; cytokine; immunoglobulin G; virus antibody; autoimmune disease; chronic disease; chronic immune dysschwannian; cost of illness; diabetic neuropathy; disability; disease exacerbation; disease predisposition; drug efficacy; drug safety; dysneuronal polyneuropathy; fatality; headache; host cell; human; hypertension; incidence; kidney failure; migraine; morbidity; motor nerve; non insulin dependent diabetes mellitus; peripheral neuropathy; polyneuropathy; protein cerebrospinal fluid level; radiculopathy; review; SARS coronavirus; sensory nerve; severe acute respiratory syndrome; side effect; superinfection; symptomatology; treatment outcome; Chronic Disease; Diabetes Mellitus, Type 2; Diabetic Neuropathies; Genetic Predisposition to Disease; Humans; Immunoglobulin G; Immunoglobulins, Intravenous; Neural Conduction; Neurons; Polyneuropathies; Severe Acute Respiratory Syndrome","Engel, W.K., Rapid and continued improvement from intravenous immunoglobulin treatment of asymmetrical chronic progressive muscular atrophy after 19 years of disease progression (1995) Ann Neurol, 38, pp. 333-334; Engel, W.K., Hanna, C.J., Intravenous immunoglobulin: Excellent benefit in otherwise refractory progressive muscular atrophy with IgM monoclonal gammopathy (1992) Ann Neurol, 32, p. 279; Velazquez, L., Engel, W.K., Chronic relapsing-progressive neuropathy (CRPN) associated with chronic lymphocytic leukemia (CLL): Sustained improvement of neuropathy and CLL from repeated IVIG treatments (1994) Neurology, 44, p. 215; Engel, W.K., Hanna, C.J., Misra, A.K., HTLV-I-associated myelopathy [successfully treated with anti-dysimmune therapy] (1990) New Engl J Med, 323, p. 552; Engel, W.K., Prentice, A.F., Some polyneuropathies in insulin-requiring adult-onset diabetes can benefit remarkably from anti-dysimmune treatments (1993) Neurology, 43, pp. 255-256; Engel, W.K., Polyneuropathy in type-2 diabetes mellitus (2001) The Lancet, 358, p. 2086; Engel, W.K., In type-2 diabetes (D2), diabetic neuropathy and diabeto-2-genetic (D2-Gen) neuropathy are often dysimmune and respond to intravenous IgG (IVIG) treatment (2001) Proc Soc Neurosci, pp. A27; Engel, W.K., Intravenous immunoglobulin. - An often overlooked treatment - Produces rapid, remarkable, sustained benefit in diabetic neuropathy complex, suggesting a dysimmune mechanism (1997) Ann Neurol, 42, p. 414; Engel, W.K., In Type-2 Diabetes, Diabetic Neuropathy is usually responsive to Intravenous IgG (IVIG) Treatment, ergo presumably dysimmune (2002) Acta Myol, 21, pp. A79; Sharma, K.R., Cross, J., Farronay, O., Demyelinating neuropathy in diabetes mellitus (2002) Arch Neurol, 59, pp. 758-765; Krendel, D.A., Costigan, D.A., Hopkins, L.C., Successful treatment of neuropathies in patients with diabetes mellitus (1995) Arch Neurol, 52, pp. 1053-1061; Sharma, K.R., Cross, J., Ayyar, D.R., Diabetic demyelinating polyneuropathy responsive to intravenous immunoglobulin therapy (2002) Arch Neurol, 59, pp. 751-757; Haq, R.U., Pendlebury, W.W., Fries, T.J., Tandan, R., Chronic inflammatory polyradiculoneuropathy in diabetic patients (2003) Muscle Nerve, 27, pp. 465-470; Singleton, J.R., Smith, A.G., Bromberg, M.B., Painful sensory polyneuropathy associated with impaired glucose tolerance (2001) Muscle Nerve, 24, pp. 1225-1228; Sumner, C.J., Sheth, S., Griffin, J.W., The Spectrum of neuropathy in diabetes and impaired glucose tolerance (2003) Neurology, 60, pp. 108-111; Kyle, R.A., ""Benign"" monoclonal gammopathy - After 20 to 35 years of follow-up (1993) Mayo Clin Proc, 68, pp. 26-36; Griffin, J.W., Metabolic neuropathies (2000) Cecil Textbook of Medicine, 21st Edn., pp. 2197-2198. , Goldman L, Bennett JC, eds; Eaton, S.E.M., Harris, N.D., Rajbhandari, S.M., Spinal cord involvement in diabetic peripheral neuropathy (2001) Lancet, 358, pp. 35-36; Polydefkis, M., Griffin, J.W., McArthur, J., New insights into diabetic polyneuropathy (2003) JAMA, 290, pp. 1371-1376; Mendell, J.R., Diabetic neuropathies (2001) Diagnosis and Management of Peripheral Neuropathies, pp. 373-399. , JR Mendell, JT Kissel, DR Cornblath eds. Oxford Univ. Press, Oxford, UK; Gominak, S., Parry, G.J., Neuropathies and diabetes (2000) Peripheral Neuropathy, pp. 109-120. , Cros D ed. Lippincott, Williams and Williams, Philadelphia; Simmons, Z., Feldman, E.L., Update on diabetic neuropathy (2002) Curr Opin Neurol, 15, pp. 595-603; Lavenstein, B., Dalakas, M.C., Engel, W.K., Polyneuropathy in nonsecretory osteosclerotic multiple myeloma with immunoglobin deposition in peripheral nerve tissue (1979) Neurology, 29, p. 611; Dalakas, M.C., Engel, W.K., Polyneuropathy with monoclonal gammopathy. Studies of 11 patients (1981) Ann Neurol, 10, pp. 45-54; Dalakas, M.C., Engel, W.K., Chronic relapsing (dysimmune) polyneuropathy: Pathogenesis and treatment (1981) Ann Neurol, 9 (SUPPL.), pp. 134-145; Sander, H.W., Latov, N., Research criteria for defining patients with CIDP (2003) Neurology, 60, pp. S8-S15; Latov, N., Diagnosis of CIDP (2002) Neurology, 59, pp. S2-S6; Wenzel, R.P., Edmond, M.B., Managing SARS amidst uncertainty (2003) N Engl J Med, 348, pp. 1947-1948; Nicholls, J.M., Poon, L.L., Lee, K.C., Lung pathology of fatal severe acute respiratory syndrome (2003) Lancet, 361, pp. 1773-1778; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966","Engel, W.K.; University of Southern California, Keck School of Medicine, Good Samaritan, Hospital, Los Angeles, CA, United States",,,11282460,,ACMYF,"15088499","English","Acta Myologica",Review,"Final",,Scopus,2-s2.0-1542720562
"Hsueh P.-R., Yang P.-C.","7103390478;7403932080;","Severe acute respiratory syndrome (SARS) - An emerging infection of the 21st century",2003,"Journal of the Formosan Medical Association","102","12",,"825","839",,10,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-2342561924&partnerID=40&md5=73269e0c5c955d3606e08444a0678197","Department of Laboratory Medicine, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 7 Chung-Shan South Road, Taipei, Taiwan; Department of Internal Medicine, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 7 Chung-Shan South Road, Taipei, Taiwan","Hsueh, P.-R., Department of Laboratory Medicine, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 7 Chung-Shan South Road, Taipei, Taiwan, Department of Internal Medicine, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 7 Chung-Shan South Road, Taipei, Taiwan; Yang, P.-C., Department of Laboratory Medicine, National Taiwan University Hospital, Natl. Taiwan Univ. Coll. of Medicine, 7 Chung-Shan South Road, Taipei, Taiwan","Severe acute respiratory syndrome (SARS) is an emerging infection caused by a novel coronavirus known as SARS-CoV. The disease has a high propensity to spread to household members and healthcare workers and may be associated with transmission and outbreaks in the community. Severe illness in immunocompromised patients, sophiscated hospital facilities and treatment procedures, particularly those that gene generate aerosols, and lack of adequate isolation and control measures, can amplify transmission and contribute to so-called ""super-spreading"" events. The presence of non-specific clinical manifestations at presentation and a lack of validated early diagnostic methods and effective management pose great difficulty for frontline physicians in the containment of this disease. The mortality of SARS is in the region of 10 to 15%; the presence of underlying disease, high initial C-reactive protein levels, and positive SARS-CoV in nasopharyngeal aspirate samples are associated with a higher risk of respiratory failure and mortality. Despite the disapprearance of SARS cases worldwide; the potential evolution of SARS-CoV in animals suggests the disease may re-emerge in the future. Heightened levels of clinical suspicion, rapid case detection and isolation, and contact tracing are essential to effective management of future outbreaks. Further ongoing requirements for successful management include research on the immunopathogenesis of SARS and the development of timely and reliable diagnostic tests, effective antiviral and immunomodulatory agents, and vaccines for the disease.","Disease transmission; Infection control; Review; SARS virus; Taiwan","antivirus agent; azauridine; beta lactam antibiotic; C reactive protein; corticosteroid; gamma interferon; glycyrrhizic acid; immunoglobulin G; immunomodulating agent; l 700417; lopinavir plus ritonavir; macrolide; methylprednisolone; mycophenolic acid; pirazofurin; proteinase inhibitor; quinoline derived antiinfective agent; ribavirin; virus antibody; virus vaccine; aerosol; blood analysis; child care; Chlamydophila pneumoniae; clinical feature; computer assisted tomography; coughing; diagnostic test; disease course; disease severity; disease transmission; drug potentiation; dyspnea; early diagnosis; epidemic; fever; health care facility; health care personnel; histopathology; household; human; hypoxia; immune deficiency; immunopathogenesis; infection control; Legionella pneumophila; medical research; mortality; Mycoplasma pneumoniae; nonhuman; nose smear; nucleotide sequence; pathogenesis; patient care; physician; pneumonia; polymerase chain reaction; reliability; respiratory distress; respiratory failure; reverse transcription polymerase chain reaction; review; risk assessment; SARS coronavirus; severe acute respiratory syndrome; symptom; thorax radiography; throat culture; virus transmission; Communicable Diseases, Emerging; Humans; Severe Acute Respiratory Syndrome; Taiwan","Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. 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Dis., 9, pp. 718-720; Hsueh, P.R., Hsiao, C.H., Yeh, S.H., Microbiologic characteristics, serologic response, and clinical manifestations in severe acute respiratory syndrome, Taiwan (2003) Emerg. Infect. Dis., 9, pp. 1163-1167; Singh, K., Hsu, L.Y., Villacian, J.S., Severe acute respiratory syndrome: Lessons from Singapore (2003) Emerg. Infect. Dis., 9, pp. 1294-1298; Oh, V.M., Lim, T.K., Singapore's experience of SARS (2003) Clin. Med., 3, pp. 448-451; Ksiazek, T.G., Erdman, D., Goldsmith, C., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. 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"Chan-Yeung M., Ooi G.C., Hui D.S., Ho P.L., Tsang K.W.","54790582200;16239781100;7101862411;7402211363;7201555024;","Severe acute respiratory syndrome",2003,"International Journal of Tuberculosis and Lung Disease","7","12",,"1117","1130",,12,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345733808&partnerID=40&md5=d2e2615674772bae20def91908b3633c","Div. of Resp. and Critical Care Med., Department of Medicine, University of Hong Kong, Hong Kong, Hong Kong; Department of Diagnostic Radiology, University of Hong Kong, Hong Kong, Hong Kong; Department of Medicine, Chinese University of Hong Kong, Hong Kong, Hong Kong; Department of Microbiology, Queen Mary Hospital, Hong Kong, Hong Kong; University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong","Chan-Yeung, M., Div. of Resp. and Critical Care Med., Department of Medicine, University of Hong Kong, Hong Kong, Hong Kong, University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong; Ooi, G.C., Department of Diagnostic Radiology, University of Hong Kong, Hong Kong, Hong Kong; Hui, D.S., Department of Medicine, Chinese University of Hong Kong, Hong Kong, Hong Kong; Ho, P.L., Department of Microbiology, Queen Mary Hospital, Hong Kong, Hong Kong; Tsang, K.W., Div. of Resp. and Critical Care Med., Department of Medicine, University of Hong Kong, Hong Kong, Hong Kong","Severe acute respiratory syndrome (SARS) is a new disease that poses a threat to international health. The SARS epidemic earlier this year affected more than 30 countries and regions, with a cumulative global total of 8098 cases. It is caused by a novel coronavirus, probably of animal origin. The mean incubation period is 6.4 days (range 2-11 days). Patients usually present with high fever, chills, myalgia and dry cough, with or without chest X-ray evidence of pneumonia at the onset of disease. A history of contact with or travel to an area with local transmission is common. Diagnosis is based on clinical criteria, as a valid rapid diagnostic test is not yet available. There is no specific antiviral therapy for this disease, and no controlled clinical trial for any treatment modality has been conducted. In several retrospective studies steroids have been shown to be useful in a proportion of patients who deteriorated despite antibiotics and supportive treatment. SARS has a high morbidity (about 25% required intensive care) and fatality (9.6%). A high index of suspicion for the disease, isolation of patients, strict observation of infection control practices and compliance with use of personal protective equipment are necessary to prevent nosocomial infection. Contact tracing and quarantine are essential measures to prevent community spread of disease. Prevention of future outbreaks requires strengthening of infection control practices in hospitals, development of a rapid diagnostic test and a vaccine, and removal of any animal reservoir and environmental conditions that led to the spread of the disease.","Clinical features; Coronavirus; Diagnosis; Epidemic; Prevention; Radiology; SARS","antibiotic agent; corticosteroid; glycyrrhizic acid; hydrocortisone; immunoglobulin G; methylprednisolone; pentoxifylline; prednisolone; recombinant interferon; ribavirin; steroid; adolescent; adult; chill; coughing; disease transmission; epidemic; female; fever; hemolysis; hospital infection; human; incubation time; infection control; infection prevention; male; morbidity; myalgia; patient compliance; pneumonia; priority journal; protective equipment; review; SARS coronavirus; severe acute respiratory syndrome; thorax radiography; Adolescent; Adult; Age Distribution; Aged; Aged, 80 and over; Child; Child, Preschool; China; Communicable Diseases, Emerging; Disease Outbreaks; Disease Transmission; Female; Hong Kong; Humans; Incidence; Male; Middle Aged; Quarantine; Risk Assessment; Severe Acute Respiratory Syndrome; Sex Distribution; Survival Analysis; World Health","Tsang, K.W., Ho, P.L., Ooi, G., A cluster of cases of severe acute respiratory syndrome in Hong Kong (2003) N Engl Med J, 348, pp. 1977-1985; (2003) Severe Acute Respiratory Syndrome (SARS)-Multi-Country Outbreak, , http://www.who.int/csr/2003_03_15/en, 15 March; (2002) Cumulative Number of Reported Probable Cases of SARS, , http://www.who.int/csr/2003_09_23/en, 1 Nov to 31 July; Severe acute respiratory syndrome (SARS). 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Implications for glove reuse and handwashing (1988) Ann Intern Med, 109, pp. 394-398; (2003) MMWR Update: Severe Acute Respiratory Syndrome Cases among Protected Health-Care Workers-Toronto, , http://www.cdc.gov/mmwr/preview/mmwrhtml/mm5219a1.htm, Canada, April; Ho, P.L., High risk procedures (2003) Clinical Management Workshop, , 13-14 June, Hong Kong, China; Chan-Yeung, M., Seto, W.H., Sung, J.J.Y., Nosocomial infection by coronavirus associated with severe acute respiratory syndrome (SARS) (2003) BMJ, 326, p. 1393; Ho, A., Sung, J.J.Y., Chan-Yeung, M., An outbreak of severe acute respiratory syndrome (SARS) among hospital workers in a community hospital in Hong Kong (2003) Ann Intern Med, 139, pp. 564-567; Tsang, T., Lam, T.H., Public health issues (2003) Respirol, (SUPPL.). , in press; Communicable Disease Surveillance and Response. Update 83-One Hundred Days into the Outbreak, , http://www.who.int/csr/2003_06_18/en/; Communicable Disease Surveillance and Response. Severe Acute Respiratory Syndrome (SARS) in Singapore-2, , http://www.who.int/csr/2003_09_26/en/","Chan-Yeung, M.; University Department of Medicine, Queen Mary Hospital, Professorial Block, Hong Kong, Hong Kong; email: mmwchan@hkucc.hku.hk",,,10273719,,IJTDF,"14677886","English","Int. J. Tuberc. Lung Dis.",Review,"Final",,Scopus,2-s2.0-0345733808
"Allegra L., Blasi F., Petrigni G., Terzano C., Valenti V.","7007020786;57211284402;6602862485;7003888036;57194562752;","SARS and influenza, two respiratory diseases of viral origin: Possible sceneries for the present winter [SARS e influenza, due malattie respiratorie di origine virale: Possibili scenari per quest'inverno]",2003,"GIMT - Giornale Italiano delle Malattie del Torace","57","5",,"364","372",,,,"https://www.scopus.com/inward/record.uri?eid=2-s2.0-4944264794&partnerID=40&md5=6b6aa783ab9d3c96d7327d9082090c61","Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di Milano, Italy; Serv. di Fisiopatologia Respiratoria, Fondazione Spencer-Cenci, Università La Sapienza, Roma, Italy","Allegra, L., Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di Milano, Italy; Blasi, F., Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di Milano, Italy; Petrigni, G., Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di Milano, Italy; Terzano, C., Serv. di Fisiopatologia Respiratoria, Fondazione Spencer-Cenci, Università La Sapienza, Roma, Italy; Valenti, V., Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di Milano, Italy","The outbreak of SARS, appeared in november 2002 in the chinese Province of Guangdong and initially underevaluated, has successively demonstrated its alarming characteristics (especially in several Far Eastern Countries and in Canada) during the spring 2003, being declared extinct in these Countries between end of June and beginning of July 2003. In the entire world such disappearance has been hopefully linked to the extinction of the responsible pathogen (a coronavirus mutated by deletion: the most credited), with the definitive disappearance of the disease in this case. It is but also possible that the microorganism could temporarily be hidden in an animal (or human? Improbable!) ""reservoir"" so that it could in the future re-appear in humans. The most likely season for such possibility should be late-autumn/winterly, a season characterized by outbreaks or at least extended diffusion of diseases linked to the cold season, that in the acute cases are mostly of viral origin. It's so quite clear that, at least in the initial phase, characterized by high body temperature and initial respiratory simptomatology, SARS could be confused mainly with the most common and diffuse of such diseases, namely influenza, especially in case of ambiguous information on the subject's geographic recent travels or suspect contacts: it could lead not only to difficulties in the differential diagnosis but also to more or less justified alarm both for the patient's family and friends and for the Doctor himself or the outpatients' Hospital staff, followed by possible false orientation and inappropriate prophylactic measures. For these reasons we have considered useful the presentation of a synoptic confrontation between SARS and influenza, two diseases that, at least at the very beginning, could in some cases induce wrong interpretations as for the identification of the disease than for necessary measures to be adopted in case of suspect or probable SARS. For the two diseases we have the listed, the ones vs the others, definition, initial symptomatology and clinical features, follow-up of body temperature and main signs and symptoms, imaging of SARS and of unfrequent pneumonic complications of influenza.","Definition; Follow-up; Influenza; SARS; Symptomatology","article; clinical examination; differential diagnosis; early diagnosis; epidemic; follow up; human; infection control; infection risk; influenza; severe acute respiratory syndrome; symptom; winter; world health organization","Poutanen, S.M., Low, D.E., Henry, B., Finkelstein, S., Rose, D., Green, K., Tellier, R., McGeer, A.J., Identification of Severe Acute Respiratory Syndrome in Canada New Engl J Med, , www.nejm.org, e.pub online; Tsang, K.W., Ho, P.L., Ooi, G.C., A cluster of cases of severe acute respiratory syndrome in Hong Kong New Engl J Med, , www.nejm.org, e.pub online; Lee, N., Hi, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong New Engl J Med, , www.nejm.org, e.pub online; Peiris, J.S.M., Lai, S.T., Poon, L.L.M., Coronavirus as a possible cause of severe acute respiratory syndrome Lancet, , http://image.the-lancet.com/extras/03art3477web.pdf, e.pub online; Allegra, L., Bassetti, D., Bassetti, M., Blasi, F., Valenti, V., SARS: Una nuova entità nosografica con la quale fare i conti (anche in Italia?) (2003) GIMT, 57 (1), pp. 71-76. , feb; Abdullah, A.S., Tomlinson, B., Cockram, C.S., Thomas, G.N., Lessons from the severe acute respiratory syndrome outbreak in Hong Kong (2003) Emerg Infect Dis, 9 (9), pp. 1042-1045. , sep; Vigevani, G., (2003), Comunicazione personale; Allegra, L., Bassetti, D., Bassetti, M., Sindrome Acuta Respiratoria Severa: Il caso di Genova e le sue inusuali caratteristiche cliniche (2003) GIMT, 57 (1), pp. 64-69. , feb; Nicholson, K.G., Nguyen-Van Tam, J.S., Ahmed, A.H., Wiselka, M.J., Leese, J., Ayres, J., Campbell, J.H., Woodhead, M.A., Randomised placebo-controlled crossover trial on effect of inactivated influenza vaccine on pulmonary function in asthma (1998) Lancet, 351 (9099), pp. 326-331. , Jan 31; Hsu, L.Y., Lee, C.C., Green, J.A., Ang, B., Paton, N.I., Lee, L., Villacian, J.S., Leo, Y.S., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9 (6), pp. 713-717. , Jun","Istituto Malattie Respiratorie, Università degli Studi, IRCCS Ospedale Policlinico di MilanoItaly",,,11270810,,GGIMA,,"Italian","GIMT G. Ital. Mal. Torace",Article,"Final",,Scopus,2-s2.0-4944264794
"Dean G.A., Olivry T., Stanton C., Pedersen N.C.","7103363034;7006667701;57196832838;7202299909;","In vivo cytokine response to experimental feline infectious peritonitis virus infection",2003,"Veterinary Microbiology","97","1-2",,"1","12",,32,"10.1016/j.vetmic.2003.08.010","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344154638&doi=10.1016%2fj.vetmic.2003.08.010&partnerID=40&md5=4f0abdf8628f346511dd6e3761470e66","Dept. of Molec. Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Dept. of Vet. Med. and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Dean, G.A., Dept. of Molec. Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Olivry, T., Department of Clinical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Stanton, C., Dept. of Molec. Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; Pedersen, N.C., Dept. of Vet. Med. and Epidemiology, School of Veterinary Medicine, University of California, Davis, CA 95616, United States","Feline infectious peritonitis virus (FIPV) is a coronavirus that causes sporadic fatal disease in cats characterized by vasculitis, granulomatous inflammation and effusive pleuritis/peritonitis. Histologic changes in lymphoid tissues include lymphoid hyperplasia, lymphoid depletion, histiocytosis, and granuloma formation. Although viremia occurs, histologic lesions are not found uniformly throughout lymphoid tissues. We used experimental infection of cats with a highly pathogenic FIPV isolate, UCD8, to study histologic lesions, virus replication, and cytokine expression in multiple lymphoid tissues during the effusive phase of disease. Viral RNA was found in 76% of central tissues (mediastinal lymph node, spleen, mesenteric lymph node) examined, as compared to 27% of peripheral tissues (popliteal lymph node, cervical lymph node, femoral bone marrow). All tissues positive for virus replication also demonstrated lymphoid depletion. Generally, affected tissues had lower levels of IL-4 and IL-12-p40 mRNA and higher levels of IL-10 mRNA. Although no differences in IFN-γ or TNF-α mRNA were measured, TNF-α protein expression was greater in affected tissues and demonstrated a shift in the source of TNF-α from macrophages to lymphocytes. Together, these results colocalize FIPV replication, lymphocyte depletion in tissues, and alterations in cytokine transcription and translation. A possible role for TNF-α in the previously described FIPV-induced lymphocyte apoptosis is also suggested. © 2003 Elsevier B.V. All rights reserved.","Coronavirus; Cytokines; Feline infectious peritonitis; IL-10; TNF-α","cytokine; gamma interferon; interleukin 10; interleukin 12; interleukin 4; tumor necrosis factor alpha; virus RNA; apoptosis; article; bone marrow; cat; cervical lymph node; clinical feature; comparative study; Coronavirus; effusion; femur; genetic transcription; granuloma; granulomatous inflammation; histiocytosis; histology; in vivo study; lymph node; lymphatic system disease; lymphocyte; lymphoid hyperplasia; lymphoid tissue; macrophage; mediastinum lymph node; mesentery lymph node; nonhuman; peritonitis; pleurisy; protein expression; RNA translation; vasculitis; viremia; virus infection; virus replication; Coronavirus; Felidae; Feline infectious peritonitis virus; Felis catus","Addie, D.D., Toth, S., Murray, G.D., Jarrett, O., The risk of typical and antibody enhanced feline infectious peritonitis among cats from feline coronavirus endemic households (1995) Feline Pract., 23, pp. 24-26; An, S., Chen, C.J., Yu, X., Leibowitz, J.L., Makino, S., Induction of apoptosis in murine coronavirus-infected cultured cells and demonstration of e protein as an apoptosis inducer (1999) J. Virol., 73, pp. 7853-7859; Ayala, A., Herdon, C.D., Lehman, D.L., Demaso, C.M., Ayala, C.A., Chaudry, I.H., The induction of accelerated thymic programmed cell death during polymicrobial sepsis: Control by corticosteroids but not tumor necrosis factor (1995) Shock, 3, pp. 259-267; Barlough, J.E., Feline infectious peritonitis (1988) Manual of Small Animal Infectious Diseases, pp. 63-78. , Barlough, J.E. (Ed.). Churchill Livingstone, New York; Belyavsky, M., Belyavskaya, E., Levy, G.A., Leibowitz, J.L., Coronavirus MHV-3-induced apoptosis in macrophages (1998) Virology, 250, pp. 41-49; Boehme, S.A., Lenardo, M.J., Propriocidal apoptosis of mature T lymphocytes occurs at S phase of the cell cycle (1993) Eur. J. Immunol., 23, pp. 1552-1560; Bone, R.C., Toward a theory regarding the pathogenesis of the systemic inflammatory response syndrome: What we do and do not know about cytokine regulation (1996) Crit. Care Med., 24, pp. 163-172; Chicheportiche, Y., Bourdon, P.R., Xu, H., Hsu, Y.M., Scott, H., Hession, C., Garcia, I., Browning, J.L., TWEAK, a new secreted ligand in the tumor necrosis factor family that weakly induces apoptosis (1997) J. Biol. Chem., 272, pp. 32401-32410; Dean, G.A., Reubel, G.H., Moore, P.F., Pedersen, N.C., Proviral burden and infection kinetics of feline immunodeficiency virus in lymphocyte subsets of blood and lymph node (1996) J. Virol., 70, pp. 5165-5169; Dean, G.A., Higgins, J., Lavoy, A., Fan, Z., Pedersen, N.C., Measurement of feline cytokine gene expression by quantitative- competitive RT-PCR (1998) J. Vet. Immunol. Immunopathol., 63, pp. 73-82; De Groot, R.J., Horzineck, M.C., Feline infectious peritonitis (1995) The Coronaviridae, pp. 293-315. , Sidell, S.G. (Ed.). Plenum Press, New York; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Patterns of feline coronavirus infection and fecal shedding from cats in multiple-cat environments (1997) J. Am Vet. Med. Assoc., 210, pp. 1307-1312; Goitsuka, R., Hirota, Y., Hasegawa, A., Tomoda, I., Release of interleukin-1 from peritoneal exudate cells of cats with feline infectious peritonitis (1987) Nippon Juigaku Zasshi, 49, pp. 811-818; Goitsuka, R., Onda, C., Hirota, Y., Hasegawa, A., Tomoda, I., Feline interleukin-1 production induced by feline infectious peritonitis virus (1988) Nippon Juigaku Zasshi, 50, pp. 209-214; Goitsuka, R., Ohashi, T., Ono, K., Yasukawa, K., Koishibara, Y., Fukui, H., Ohsugi, Y., Hasegawa, A., IL-6 activity in feline infectious peritonitis (1990) J. Immunol., 144, pp. 2599-2603; Goitsuka, R., Furusawa, S., Mizoguchi, M., Hasegawa, A., Detection of interleukin-1 in ascites from cats with feline infectious peritonitis (1991) J. Vet. Med. Sci., 53, pp. 487-489; Haagmans, B.L., Egberink, H.F., Horzinek, M.C., Apoptosis and T-cell depletion during feline infectious peritonitis (1996) J. Virol., 70, pp. 8977-8983; Hickman, A., Morris, J.G., Rogers, Q.R., Pedersen, N.C., Treatment of feline infectious peritonitis with immunomodulating agents and antiviral drugs: A review (1995) Feline Pract., 23, pp. 103-107; Hotchkiss, R.S., Swanson, P.E., Cobb, J.P., Jacobson, A., Buchman, T.G., Karl, I.E., Apoptosis in lymphoid and parenchymal cells during sepsis: Findings in normal and T- and B-cell-deficient mice (1997) Crit. Care Med., 25, pp. 1298-1307; Jacobse, G.H., Daha, M.R., Horzinek, M.C., Isolation and characterization of feline C3 and evidence for the immune complex pathogenesis of feline infectious peritonitis (1980) J. Immunol., 125, pp. 1606-1610; Lenardo, M.J., Interleukin-2 programs mouse alpha beta T lymphocytes for apoptosis (1991) Nature, 353, pp. 858-861; Liu, C., Xu, H.Y., Liu, D.X., Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus (2001) J. Virol., 75, pp. 6402-6409; Marsters, S.A., Sheridan, J.P., Donahue, C.J., Pitti, R.M., Gray, C.L., Goddard, A.D., Bauer, K.D., Ashkenazi, A., Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-kappa B (1996) Curr. Biol., 6, pp. 1669-1676; Okada, H., Kobune, F., Sato, T.A., Kohama, T., Takeuchi, Y., Abe, T., Takayama, N., Tashiro, M., Extensive lymphopenia due to apoptosis of uninfected lymphocytes in acute measles patients (2000) Arch. Virol., 145, pp. 905-920; Pedersen, N.C., Morphologic and physical characteristics of feline infectious peritonitis virus and its growth in autochthonous peritoneal cell cultures (1976) Am. J. Vet. Res., 37, pp. 567-572; Pedersen, N.C., Virologic and immunologic aspects of feline infectious peritonitis virus infection (1987) Adv. Exp. Med. Biol., 218, pp. 529-550; Pedersen, N.C., Boyle, J.F., Immunologic phenomena in the effusive form of feline infectious peritonitis (1980) Am. J. Vet. Res., 41, pp. 868-876; Poland, A.M., Vennema, H., Foley, J.E., Pedersen, N.C., Two related strains of feline infectious peritonitis virus isolated from immunocompromised cats infected with a feline enteric coronavirus (1996) J. Clin. Microbiol., 34, pp. 3180-3184; Russell, J.H., White, C.L., Loh, D.Y., Meleedy-Rey, P., Receptor-stimulated death pathway is opened by antigen in mature T cells (1991) Proc. Natl. Acad. Sci. U.S.A., 88, pp. 2151-2155; Scott, F.W., Immunization against feline coronaviruses (1987) Adv. Exp. Med. Biol., 218, pp. 569-576; Scott, F.W., Olsen, C.W., Corapi, W.V., Antibody-dependent enhancement of feline infectious peritonitis virus infection (1995) Feline Pract., 23, pp. 77-80; Sirinarumitr, T., Kluge, J.P., Paul, P.S., Transmissible gastroenteritis virus induced apoptosis in swine testes cell cultures (1998) Arch. Virol., 143, pp. 2471-2485; Stoddart, C.A., Scott, F.W., Intrinsic resistance of feline peritoneal macrophages to coronavirus infection correlates with in vivo virulence (1989) J. Virol., 63, pp. 436-440; Tartaglia, L.A., Goeddel, D.V., Two TNF receptors (1992) Immunol. Today, 13, pp. 151-153; Vennema, H., De Groot, R.J., Harbour, D.A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M.C., Spaan, W.J., Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization (1990) J. Virol., 64, pp. 1407-1409; Vennema, H., Poland, A., Hawkins, K.F., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs and what they tell us about the relationships between feline coronaviruses and their evolution (1995) Feline Pract., 23, pp. 40-45; Vennema, H., Poland, A., Foley, J., Pedersen, N.C., Feline infectious peritonitis viruses arise by mutation from endemic feline enteric coronaviruses (1998) Virology, 243, pp. 150-157; Wang, S.D., Huang, K.J., Lin, Y.S., Lei, H.Y., Sepsis-induced apoptosis of the thymocytes in mice (1994) J. Immunol., 152, pp. 5014-5021; Weiss, R.C., Cox, N.R., Evaluation of immunity to feline infectious peritonitis in cats with cutaneous viral-induced delayed hypersensitivity (1989) Vet. Immunol. Immunopathol., 21, pp. 293-309; Weiss, R.C., Scott, F.W., Antibody-mediated enhancement of disease in feline infectious peritonitis: Comparisons with dengue hemorrhagic fever (1981) Comp. Immunol. Microbiol. Infect. Dis., 4, pp. 175-189; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Nature and development of viremia (1981) Am. J. Vet. Res., 42, pp. 382-390; Weiss, R.C., Scott, F.W., Pathogenesis of feline infectious peritonitis: Pathologic changes and immunofluorescence (1981) Am. J. Vet. Res., 42, pp. 2036-2048; Zachar, V., Thomas, R.A., Goustin, A.S., Absolute quantification of target DNA: A simple competitive PCR for efficient analysis of multiple samples (1993) Nucleic Acids Res., 21, pp. 2017-2018","Dean, G.A.; Dept. of Molec. Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, 4700 Hillsborough Street, Raleigh, NC 27606, United States; email: gregg_dean@ncsu.edu",,"Elsevier",03781135,,VMICD,"14637034","English","Vet. Microbiol.",Article,"Final",,Scopus,2-s2.0-0344154638
"Gao W., Tamin A., Soloff A., D'Aiuto L., Nwanegbo E., Robbins P.D., Bellini W.J., Barratt-Boyes S., Gambotto A.","40561183300;6602551546;6507143535;6603293266;6505981165;17339473100;7005204113;6701568751;7004136619;","Effects of a SARS-associated coronavirus vaccine in monkeys",2003,"Lancet","362","9399",,"1895","1896",,172,"10.1016/S0140-6736(03)14962-8","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0345549412&doi=10.1016%2fS0140-6736%2803%2914962-8&partnerID=40&md5=94b56498013d62c3af7e858596e91a2d","Department of Surgery Molecular, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Dept. of Molec. Genet. and Biochem., Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Department of Medicine, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Dept. of Infect. Dis. and Microbiol., Graduate School of Public Health, University of Pittsburgh, Pittsburgh, PA, United States; Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Departments of Surgery and Medicine, University of Pittsburgh, Molecular Medicine Institute, 300 Technology Drive, Pittsburgh, PA 15219, United States","Gao, W., Department of Surgery Molecular, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Tamin, A., Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Soloff, A., Dept. of Infect. Dis. and Microbiol., Graduate School of Public Health, University of Pittsburgh, Pittsburgh, PA, United States; D'Aiuto, L., Department of Surgery Molecular, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Nwanegbo, E., Department of Surgery Molecular, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Robbins, P.D., Dept. of Molec. Genet. and Biochem., Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States; Bellini, W.J., Natl. Center for Infectious Diseases, Centers for Dis. Contr. and Prev., Atlanta, GA, United States; Barratt-Boyes, S., Dept. of Infect. Dis. and Microbiol., Graduate School of Public Health, University of Pittsburgh, Pittsburgh, PA, United States; Gambotto, A., Department of Surgery Molecular, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States, Dept. of Molec. Genet. and Biochem., Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States, Department of Medicine, Division of Infectious Diseases, Univ. of Pittsburgh Sch. of Medicine, Pittsburgh, PA, United States, Departments of Surgery and Medicine, University of Pittsburgh, Molecular Medicine Institute, 300 Technology Drive, Pittsburgh, PA 15219, United States","The causative agent of severe acute respiratory syndrome (SARS) has been identified as a new type of coronavirus. Here, we have investigated the ability of adenoviral delivery of codon-optimised SARS-CoV strain Urbani structural antigens spike protein S1 fragment, membrane protein, and nucleocapsid protein to induce virus-specific broad immunity in rhesus macaques. We immunised rhesus macaques intramuscularly with a combination of the three Ad5-SARS-CoV vectors or a control vector and gave a booster vaccination on day 28. The vaccinated animals all had antibody responses against spike protein S1 fragment and T-cell responses against the nucleocapsid protein. All vaccinated animals showed strong neutralising antibody responses to SARS-CoV infection in vitro. These results show that an adenoviral-based vaccine can induce strong SARS-CoV-specific immune responses in the monkey, and hold promise for development of a protective vaccine against the SARS causal agent.",,"neutralizing antibody; severe acute respiratory syndrome vaccine; unclassified drug; virus vaccine; Adenovirus; animal experiment; animal model; article; codon; controlled study; monkey; nonhuman; priority journal; SARS coronavirus; severe acute respiratory syndrome; T lymphocyte; vaccination; virus immunity","Rota, P.A., Oberste, M.S., Monroe, S.S., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Anton, I.M., Gonzalez, S., Bullido, M.J., Cooperation between transmissible gastroenteritis coronavirus (TGEV) structural proteins in the in vitro induction of virus-specific antibodies (1996) Virus Res, 46, pp. 111-124; Brown, K., Gao, W., Alber, S., Adenovirus-transduced dendritic cells injected into skin or lymph node prime potent siv-specific t-cell immunity in monkeys J Immunol, , in press; Weiss, R.C., Scott, W., Antibody-mediated enhancement of disease in feline infectious peritonitis: Comparisons with dengue hemorrhagic fever (1981) Comp Immunol Microbiol Infect Dis, 4, pp. 175-189; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240","Gambotto, A.; Departments of Surgery and Medicine, University of Pittsburgh, Molecular Medicine Institute, 300 Technology Drive, Pittsburgh, PA 15219, United States; email: agamb@pitt.edu",,"Elsevier Limited",01406736,,LANCA,"14667748","English","Lancet",Article,"Final",Open Access,Scopus,2-s2.0-0345549412
"Xu X., Liu Y., Weiss S., Arnold E., Sarafianos S.G., Ding J.","56754377800;49761779700;57203567044;35482342100;21035958300;55519885200;","Molecular model of SARS coronavirus polymerase: Implications for biochemical functions and drug design",2003,"Nucleic Acids Research","31","24",,"7117","7130",,85,"10.1093/nar/gkg916","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346888670&doi=10.1093%2fnar%2fgkg916&partnerID=40&md5=4f3ce43733b509fa02fbec7ce14c4ed1","Key Laboratory of Proteomics, Inst. of Biochemistry/Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China; Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; CABM, Rutgers University, Dept. of Chemistry/Chemical Biology, 679 Hoes Lane, Piscataway, NJ 08854-5638, United States","Xu, X., Key Laboratory of Proteomics, Inst. of Biochemistry/Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China; Liu, Y., Key Laboratory of Proteomics, Inst. of Biochemistry/Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China; Weiss, S., Department of Microbiology, Univ. of Pennsylvania School of Med., 36th Street and Hamilton Walk, Philadelphia, PA 19104-6076, United States; Arnold, E., CABM, Rutgers University, Dept. of Chemistry/Chemical Biology, 679 Hoes Lane, Piscataway, NJ 08854-5638, United States; Sarafianos, S.G., CABM, Rutgers University, Dept. of Chemistry/Chemical Biology, 679 Hoes Lane, Piscataway, NJ 08854-5638, United States; Ding, J., Key Laboratory of Proteomics, Inst. of Biochemistry/Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, CABM, Rutgers University, Dept. of Chemistry/Chemical Biology, 679 Hoes Lane, Piscataway, NJ 08854-5638, United States","The causative agent of severe acute respiratory syndrome (SARS) is a previously unidentified coronavirus, SARS-CoV. The RNA-dependent RNA polymerase (RdRp) of SARS-CoV plays a pivotal role in viral replication and is a potential target for anti-SARS therapy. There is a lack of structural or biochemical data on any coronavirus polymerase. To provide insights into the structure and function of SARS-CoV RdRp, we have located its conserved motifs that are shared by all RdRps, and built a three-dimensional model of the catalytic domain. The structural model permits us to discuss the potential functional roles of the conserved motifs and residues in replication and their potential interactions with inhibitors of related enzymes. We predict important structural attributes of potential anti-SARS-CoV RdRp nucleotide analog inhibitors: hydrogen-bonding capability for the 2′ and 3′ groups of the sugar ring and C3′ endo sugar puckering, and the absence of a hydrophobic binding pocket for non-nucleoside analog inhibitors similar to those observed in hepatitis C virus RdRp and human immunodeficiency virus type 1 reverse transcriptase. We propose that the clinically observed resistance of SARS to ribavirin is probably due to perturbation of the conserved motif A that controls rNTP binding and fidelity of polymerization. Our results suggest that designing anti-SARS therapies can benefit from successful experiences in design of other antiviral drugs. This work should also provide guidance for future biochemical experiments.",,"antivirus agent; nucleoside analog; ribavirin; RNA directed DNA polymerase inhibitor; RNA directed RNA polymerase; article; controlled study; drug design; drug efficacy; enzyme active site; enzyme structure; gene targeting; genetic conservation; hydrogen bond; hydrophobicity; molecular model; nonhuman; nucleotide sequence; polymerization; priority journal; protein function; protein motif; SARS coronavirus; severe acute respiratory syndrome; virus replication; Amino Acid Motifs; Amino Acid Sequence; Antiviral Agents; Binding Sites; Catalytic Domain; Conserved Sequence; Drug Design; Drug Resistance, Viral; Enzyme Inhibitors; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Protein Structure, Tertiary; Ribavirin; RNA Replicase; SARS Virus; Sequence Alignment; Sequence Homology, Amino Acid; Coronavirus; Hepatitis C virus; Human immunodeficiency virus; Human immunodeficiency virus 1; RNA viruses; SARS coronavirus","Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., To, K.F., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. 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Biol., 2, pp. 293-302; Esnouf, R., Ren, J., Ross, R., Jones, Y., Stammers, D., Stuart, D., Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors (1995) Nature Struct. Biol., 2, pp. 303-308; Das, K., Ding, J., Hsiou, Y., Clark, J.A.D., Moereels, H., Koymans, L., Andries, K., Boyer, P.L., Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant (1996) J. Mol. Biol., 264, pp. 1085-1100; Gouet, P., Courcelle, E., Stuart, D.I., Metoz, F., ESPript: Multiple sequence alignments in PostScript (1999) Bioinformatics, 15, pp. 305-308","Ding, J.; Key Laboratory of Proteomics, Inst. of Biochemistry/Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China; email: jpding@sibs.ac.cn",,,03051048,,NARHA,"14654687","English","Nucleic Acids Res.",Article,"Final",Open Access,Scopus,2-s2.0-0346888670
"Cebra C.K., Mattson D.E., Baker R.J., Sonn R.J., Dearing P.L.","7006400364;7102211747;55340881900;6603079783;6701475587;","Potential pathogens in feces from unweaned llamas and alpacas with diarrhea",2003,"Journal of the American Veterinary Medical Association","223","12",,"1806","1808",,57,"10.2460/javma.2003.223.1806","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346955853&doi=10.2460%2fjavma.2003.223.1806&partnerID=40&md5=8607989b069bda31103ecfafc80d5af2","Department of Clinical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States; Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States","Cebra, C.K., Department of Clinical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States; Mattson, D.E., Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States; Baker, R.J., Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States; Sonn, R.J., Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States; Dearing, P.L., Department of Biomedical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States","Objective - To identify potential pathogens in feces from llama and alpaca crias with diarrhea. Design - Prospective observational study. Animals-45 unweaned crias with diarrhea. Procedure - Fecal samples were evaluated for Eimeria spp, Giardia spp, Cryptosporidium spp, enteric viruses, and Salmonella spp. A questionnaire yielded information concerning herd management and presence of other affected camelids. Results - 28 crias were ≤ 31 days old, 11 were 32 to 62 days old, and 6 were 63 to 210 days old. Potential pathogens were isolated from feces from 32 of the 45 crias. A total of 39 potential pathogens were obtained, including coronavirus (n = 19 crias; 42%), Giardia spp (8; 18%), Eimeria spp (6; 13%), Cryptosporidium spp (4; 9%), rotavirus (1; 2%), and nematode ova (1; 2%). Salmonella spp were not isolated. Most crias from which potential pathogens were isolated were identified during outbreaks of diarrhea involving other camelids, although only coronavirus was isolated from crias identified during outbreaks involving adult camelids. Coronavirus was detected throughout the year, whereas protozoa were most commonly isolated during the fall and winter. Conclusions and Clinical Relevance - Results suggest that a variety of potential pathogens may be isolated from young crias with diarrhea. Many crias shed coronavirus, which may also have been affecting older camelids. Protozoa were isolated most often during wetter months, suggesting that crias born during these months may have greater exposure to protozoal pathogens.",,"article; Artiodactyla; autumn; Coronavirus; Cryptosporidium; diarrhea; Eimeria; enteric virus; feces microflora; Giardia; nematode; parasite isolation; prospective study; Rotavirus; Salmonella; virus detection; virus isolation; virus shedding; winter; Animals; Animals, Suckling; Camelids, New World; Carrier State; Coronavirus; Cryptosporidium; Diarrhea; Eimeria; Feces; Female; Giardia; Male; Prospective Studies; Seasons; Animalia; Artiodactyla; Coronavirus; Cryptosporidium; Eimeria; Giardia; Lama (camel); Lama glama; Lama pacos; Protozoa; Rotavirus; Salmonella","Rulofson, F.C., Atwill, E.R., Holmberg, C.A., Fecal shedding of Giardia duodenalis, Cryptosporidium parvun, Salmonella organisms, and Escherichia coli O157:H7 from llamas in California (2001) Am J Vet Res, 62, pp. 637-642; Jarvinen, J.A., Prevalence of Eimeria macusaniensis (Apicomplexa: Eimeriidae) in midwestern Lama spp (1999) J Parasitol, 85, pp. 373-376; Rickard, L.G., Bishop, J.K., Prevalence of Eimeria spp (Apicomplexa: Eimeriidae) in Oregon llamas (1988) J Protozool, 35, pp. 335-336; Rosadio, R.H., Ameghino, E.E., Coccidial infections in neonatal Peruvian alpacas (1994) Vet Rec, 135, pp. 459-460; Shrey, C.F., Abbott, T.A., Stewart, V.A., Coccidia of the llama, Lama glama, in Colorado and Wyoming (1991) Vet Parasitol, 40, pp. 21-28; Bishop, J.K., Rickard, L.G., Fecal survey of llamas (Lama glama) in Oregon: Incidental recovery of Nematodirus battus (1987) J Am Vet Med Assoc, 191, pp. 1579-1581; Windsor, R.S., Type II ostertagiasis in llamas (1997) Vet Rec, 141, p. 608; Bidewell, C.A., Cattell, J.H., Cryptosporidiosis in young alpacas (1998) Vet Rec, 142, p. 287; Hovda, L.R., McGuirk, S.M., Lunn, D.P., Total parenteral nutrition in a neonatal llama (1990) J Am Vet Med Assoc, 196, pp. 319-322; Parreno, V., Constantini, V., Cheetham, S., First isolation of rotavirus associated with neonatal diarrhea in guanacos (Lama guanicoe) in the Argentinean Patagonia region (2001) J Vet Med B Infect Dis Vet Public Health, 48, pp. 713-720; Kiorpes, A.L., Kirkpatrick, C.E., Bowman, D.D., Isolation of Giardia from a llama and from sheep (1987) Can J Vet Res, 51, pp. 277-280; Foreyt, W.J., Lagerquist, J., Experimental infections of Eimeria alpacae and Eimeria punoensis in llamas (Lama glama) (1992) J Parasitol, 78, pp. 906-909; Saif, L.J., Brock, K.V., Redman, D.R., Winter dysentery in dairy herds: Electron microscope and serological evidence for an association with coronavirus infection (1991) Vet Rec, 128, pp. 447-449; Montes Perez, R.C., Rodriguez Vivas, R.I., Torres Acosta, J.F., Annual follow-up of the gastrointestinal parasitosis of white-tailed deer Odocoileus virginianus in captivity in Yucatan, Mexico (1998) Rev Biol Trop, 46, pp. 821-827; Kistemann, T., Classen, T., Koch, C., Microbial load of drinking water reservoir tributaries during extreme rainfall and runoff (2002) Appl Environ Microbiol, 68, pp. 2188-2197","Cebra, C.K.; Department of Clinical Sciences, College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331-4802, United States",,,00031488,,JAVMA,"14690211","English","J. Am. Vet. Med. Assoc.",Article,"Final",,Scopus,2-s2.0-0346955853
"Paltrinieri S., Ponti W., Comazzi S., Giordano A., Poli G.","7003879241;6701320152;6701819007;7201681218;7201724087;","Shifts in circulating lymphocyte subsets in cats with feline infectious peritonitis (FIP): Pathogenic role and diagnostic relevance",2003,"Veterinary Immunology and Immunopathology","96","3-4",,"141","148",,18,"10.1016/S0165-2427(03)00156-9","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0142226938&doi=10.1016%2fS0165-2427%2803%2900156-9&partnerID=40&md5=caf467ad6c03de6cdb59b910822e5120","Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy","Paltrinieri, S., Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy; Ponti, W., Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy; Comazzi, S., Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy; Giordano, A., Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy; Poli, G., Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy","Cats with feline infectious peritonitis (FIP) are usually lymphopenic and have lymphoid depletion evident in spleen and lymph nodes. In particular, the number of CD4+ lymphocytes in tissues decreases during the evolution of FIP lesions. This decrease is most likely due to increased lymphocyte apoptotic rate. In contrast, cats infected with the Feline Coronavirus (FCoV) develop a follicular hyperplasia in the peripheral lymph nodes. The current study was devised to evaluate the possible pathogenic role of shifts in circulating lymphocyte subsets in FIP. Peripheral blood from cats with FIP was evaluated and compared with peripheral blood from clinically healthy cats living in both FCoV-free and FCoV-endemic catteries. Blood from cats with diseases other than FIP was also examined in order to define the diagnostic relevance of the changes. Lymphocyte subsets were analysed by flow cytometry, using a whole blood indirect immunofluorescence technique and mAbs specific for feline CD5, CD4, CD8, CD21. The results of the current study suggest that cats recently infected with FCoV that do not develop the disease have a transient increase in T cells; cats from groups with high prevalence of FIP have a moderate but persistent decrease in T cell subsets; cats with FIP have a very severe decrease in all the subsets of lymphocytes. Moreover, during FIP many lymphocytes do not express any membrane antigen, most likely due to early apoptosis. Cats with diseases other than FIP also had decreased number of lymphocytes: as a consequence, the diagnostic relevance of these findings is very low. Nevertheless, the lack of flow cytometric changes had a high negative predictive value (NPV), thus allowing to exclude FIP from the list of possible diagnoses in cats with normal cytograms. © 2003 Elsevier B.V. All rights reserved.","Diagnosis; Feline coronavirus; Feline infectious peritonitis; Flow cytometry; Lymphocytes","CD4 antigen; CD5 antigen; CD8 antigen; complement component C3d receptor; membrane antigen; monoclonal antibody; animal cell; animal model; antibody specificity; apoptosis; article; blood; cat disease; cell count; cell function; comparative study; controlled study; Coronavirus; diagnostic test; evaluation; female; flow cytometry; immunofluorescence; lymphocyte subpopulation; male; nonhuman; pathogenicity; prediction; prevalence; Coronavirus; Felidae; Feline coronavirus; Felis catus","Addie, D.D., Jarrett, O., Control of feline coronavirus infection in breeding catteries by serotesting, isolation and early weaning (1995) Fel. Pract., 23, pp. 92-95; Addie, D.D., Jarrett, O., Use of a reverse-transcriptase polymerase chain reaction for monitoring the shedding of feline coronavirus by healthy cats (2001) Vet. Rec., 148, pp. 649-653; Addie, D.D., Dennis, J.M., Toth, S., Callanan, J.J., Reid, S., Jarrett, O., Long-term impact on a closed household of pet cats of natural infection with feline coronavirus, feline leukaemia virus and feline immunodeficiency virus (2000) Vet. Rec., 146, pp. 419-424; Byrne, K.M., Kim, H.W., Chew, B.P., Reinhardt, G.A., Hayeck, M.G., A standardized gating technique for the generation of flow cytometry data for normal canine and normal feline blood lymphocytes (2000) Vet. Immunol. Immunopathol., 73, pp. 167-182; Calvelli, T., Denny, T.N., Paxton, H., Gelman, R., Kagan, J., Guideline for the flow cytometric immunophenotyping: A report from the National Institute of Allergy and Infectious Disease, Division of AIDS (1993) Cytometry, 14, pp. 702-715; Clinkenbeard, K.D., Meinkoth, J., Normal hematology of the cat (2000) Schalm's Veterinary Hematology, 5th Ed., pp. 382-390. , Feldmann, B., Jain, N.C. (Eds.) Lippincot Williams & Wilkins, Philadelphia; Cowell, R.L., Decker, L.S., Interpretation of feline leukocyte responses (2000) Schalm's Veterinary Hematology, 5th Ed., pp. 1064-1068. , Feldmann, B., Jain, N.C. (Eds.) Lippincot Williams & Wilkins, Philadelphia; De Groot-Mijnes, J.D.F., Van Der Most, R.G., Van Dun, J., De Groot, R.J., Detection of feline coronavirus specific CD4+ and CD8 + T cells by flow cytometry (2002) Proceedings of the Second International FCoV/FIP Symposium, p. 23. , Glasgow, 2002; Foley, J.E., Pedersen, N.C., The inheritance of susceptibility to feline infectious peritonitis in purebreed catteries (1996) Fel. Pract., 24, pp. 14-22; Foley, J.E., Poland, A., Carlson, J., Pedersen, N.C., Risk factors for feline infectious peritonitis among cats in multiple-cat environments with endemic feline enteric coronavirus (1997) JAVMA, 210, pp. 1313-1318; Giordano, A., Spagnolo, V., Colombo, A., Paltrinieri, S., Changes in some acute phase proteins and in immunoglobulin concentrations in cats with FIP or exposed to FCoV Vet. J., , in press; Gunn-Moore, D.A., Caney, S.M.A., Gruffydd-Jones, T.J., Helps, C.R., Harbour, D.A., Antibody and cytokine responses in kittens during the development of feline infectious peritonitis (FIP) (1998) Vet. Immunol. Immunopathol., 65, pp. 221-242; Haagmans, B.L., Egbernik, H.F., Horxinek, M.C., Apoptosis and T-Cell depletion during feline infectious peritonitis (1996) J. Virol., 70, pp. 8977-8983; Heerewegh, A.A.P.M., Mahler, M., Hedrich, H.J., Haagmans, B.L., Egbernik, H.F., Horzinek, M.C., Rottier, P.J.M., De Groot, R.J., Persistence and evolution of feline coronavirus in a closed cat-breeding colony (1997) Virology, 234, pp. 349-363; Hodatsu, T., Yamada, H., Ishizuka, Y., Koyama, H., Enhancement and neutralization of feline infectious peritonitis virus infection in feline macrophages by neutralizing monoclonal antibodies recognizing different epitopes (1993) Microbiol. Immunol., 37, pp. 499-504; Hsu, S.M., Raine, L., Farger, H., Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures (1980) J. Histochem. Cytochem., 29, pp. 577-580; Jacobse-Geels, H.E.L., Daha, M.R., Horzinek, M.C., Isolation and characterization of feline C3 and evidence of the immune complex pathogenesis of feline infectious peritonitis (1980) J. Immunol., 125, pp. 1606-1610; Jacobson, R.H., How well do serodiagnostic tests predict the infection or disease status of cats? (1991) JAVMA, 199, pp. 1343-1347; Kass, P., Dent, T., The epidemiology of FIP in catteries (1995) Fel. Pract., 23, pp. 27-32; Kipar, A., Bellmann, S., Kremendhal, J., Reinacher, M., Cellular composition, coronavirus antigen expression and production of specific antibodies in lesions in feline infectious peritonitis (1998) Vet. Immunol. Immunopathol., 65, pp. 243-257; Kipar, A., Bellmann, S., Gunn-Moore, D.A., Leukert, W., Kohler, K., Menger, S., Reinacher, M., Histopathological alterations of lymphatic tissues in cats without feline infectious peritonitis after long term exposure to FIP virus (1999) Vet. Microbiol., 69, pp. 131-137; Kipar, A., Köhler, K., Leukert, W., Reinacher, M., A comparison of lymphatic tissues from cats with spontaneous feline infectious peritonitis (FIP), cats with FIP virus infection but no FIP, and cats with no infection (2001) J. Comp. Pathol., 125, pp. 182-191; Knotek, Z., Toman, M., Faldyna, M., Clinical and immunological characteristics of cats affected by feline infectious peritonitis (2000) Acta Vet. Brno., 69, pp. 51-60; Lumsden, J.H., Reference values (2000) Schalm's Veterinary Hematology, 5th Ed., pp. 12-15. , Feldmann, B., Jain, N.C. (Eds.) Lippincot Williams & Wilkins, Philadelphia; Paltrinieri, S., Cammarata Parodi, M., Cammarata, G., Mambretti, M., Type IV hypersensitivity in the pathogenesis of FIPV-induced lesions (1998) J. Vet. Med. B, 45, pp. 151-159; Paltrinieri, S., Cammarata Parodi, M., Cammarata, G., In vivo diagnosis of feline infectious peritonitis by comparison of protein content, cytology, and direct immunofluorescence test on peritoneal and pleural effusions (1999) J. Vet. Diagn. Invest., 11, pp. 358-361; Pedersen, N.C., An overview of feline enteric coronavirus and infectious peritonitis virus infections (1995) Fel. Pract., 23, pp. 7-20; Potter, A., Kim, C., Gollahon, K.A., Rabinovitch, P.S., Apoptotic human lymphocytes have diminished CD4 and CD8 receptor expression (1999) Cell. Immunol., 193, pp. 36-47; Reichert, T., De Bruyere, M., Deneys, V., Totterman, T., Lydyard, P., Yuskel, F., Chapel, H., Buchner, L., Lymphocyte subsets reference ranges in adult Caucasian (1991) Clin. Immunol. Immunopathol., 60, pp. 190-208; Rocchi, M., Ponti, W., Peri, E., Jarrett, O., Bo, S., Valutazione delle sottopopolazioni linfocitarie in gatti sani ed affetti da FIV (1992) Proceedings of the 46th Meeting of the Italian Society of Veterinary Sciences (SISVet), 46, pp. 1197-1201; Rottier, P.J.M., The molecular dynamics of feline coronaviruses (1999) Vet. Microbiol., 69, pp. 117-125; Sparkes, A.H., Gruffydd-Jones, T.J., Harbour, D.A., An appraisal of the value of laboratory tests in the diagnosis of feline infectious peritonitis (1994) JAAHA, 30, pp. 345-350; Vennema, H., Poland, A., Floyd Hawkins, K., Pedersen, N.C., A comparison of the genomes of FECVs and FIPVs: What they tell us about relationship between feline coronaviruses and their evolution (1995) Vet. Rec., 23, pp. 40-44","Paltrinieri, S.; Dipartimento di Patologia Animale, Igiene e San. Pubblica Veterinaria, Sezione Patol. Gen. Vet. P., Via Celoria 10, 20133 Milan, Italy; email: saverio.paltrinieri@unimi.it",,"Elsevier",01652427,,VIIMD,"14592727","English","Vet. Immunol. Immunopathol.",Article,"Final",,Scopus,2-s2.0-0142226938
"Zeng F., Chow K.Y.C., Leung F.C.","7202911544;7202180875;55440652300;","Estimated Timing of the Last Common Ancestor of the SARS Coronavirus [8]",2003,"New England Journal of Medicine","349","25",,"2469","2470",,10,"10.1056/NEJM200312183492523","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0348011687&doi=10.1056%2fNEJM200312183492523&partnerID=40&md5=b0931c9dee0b32daeac6dff1b4b14d62","University of Hong Kong, Hong Kong, Hong Kong","Zeng, F., University of Hong Kong, Hong Kong, Hong Kong; Chow, K.Y.C., University of Hong Kong, Hong Kong, Hong Kong; Leung, F.C., University of Hong Kong, Hong Kong, Hong Kong",[No abstract available],,"China; Coronavirus; Hong Kong; human; Human immunodeficiency virus 1; letter; major clinical study; nonhuman; phylogeny; priority journal; regression analysis; respiratory tract infection; SARS coronavirus; severe acute respiratory syndrome; virus infection; virus mutation; Coronavirus; Epidemiology, Molecular; Evolution, Molecular; Linear Models; Phylogeny; SARS Virus","Guan, Y., Pieris, J.S.M., Zheng, B., Molecular epidemiology of the novel coronavirus causing severe acute respiratory syndrome (SAKS) Lancet, , in press; Korber, B., Muldoon, M., Theiler, J., Timing the ancestor of the HIV-1 pandemic strains (2000) Science, 288, pp. 1789-1796; Appling, D.R., (2003) J Am Chem Soc, 125, p. 10482. , www.graphpad.com, 5755 Oberlin Drive, #110, San Diego, CA 92121, see Web site for pricing information; Korber, B., Theiler, J., Wolinsky, S., Limitations of a molecular clock applied to considerations of the origin of HIV-1 (1998) Science, 280, pp. 1868-1871; Severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 81-83","Zeng, F.; University of Hong Kong, Hong Kong, Hong Kong",,,00284793,,NEJMA,"14681521","English","New Engl. J. Med.",Letter,"Final",,Scopus,2-s2.0-0348011687
"Grant P.R., Garson J.A., Tedder R.S., Chan P.K.S., Tam J.S., Sung J.J.Y.","8215533200;7006765284;56945667500;32067487100;24788939600;35405352400;","Detection of SARS Coronavirus in Plasma by Real-Time RT-PCR [7]",2003,"New England Journal of Medicine","349","25",,"2468","2469",,57,"10.1056/NEJM200312183492522","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346750842&doi=10.1056%2fNEJM200312183492522&partnerID=40&md5=06c14b8fa2f1bb7a1ec0c9968adc560d","Roy. Free and Univ. Coll. Med. Sch., London WlT 4JF, United Kingdom; Prince of Wales Hospital, Shatin, NT, Hong Kong","Grant, P.R., Roy. Free and Univ. Coll. Med. Sch., London WlT 4JF, United Kingdom; Garson, J.A., Roy. Free and Univ. Coll. Med. Sch., London WlT 4JF, United Kingdom; Tedder, R.S., Roy. Free and Univ. Coll. Med. Sch., London WlT 4JF, United Kingdom; Chan, P.K.S., Prince of Wales Hospital, Shatin, NT, Hong Kong; Tam, J.S., Prince of Wales Hospital, Shatin, NT, Hong Kong; Sung, J.J.Y., Prince of Wales Hospital, Shatin, NT, Hong Kong",[No abstract available],,"virus RNA; acute disease; clinical article; Coronavirus; diagnostic accuracy; fever; human; letter; nonhuman; plasma; priority journal; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; severe acute respiratory syndrome; virus detection; virus diagnosis; virus infection; virus load; Antibodies, Viral; Humans; Reverse Transcriptase Polymerase Chain Reaction; RNA, Viral; SARS Virus; Sensitivity and Specificity; Severe Acute Respiratory Syndrome; Viral Load","Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Poon, L.L., Wong, O.K., Luk, W., Yuen, K.Y., Peiris, J.S., Guan, Y., Rapid diagnosis of a coronavirus associated with severe acute respiratory syndrome (SARS) (2003) Clin Chem, 49, pp. 953-955; Drosten, C., Gunther, S., Preiser, W., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1967-1976; Tsang, K.W., Mok, T.Y., Wong, P.C., Ooi, G.C., Severe acute respiratory syndrome (SARS) in Hong Kong (2003) Respirology, 8, pp. 259-265","Grant, P.R.; Roy. Free and Univ. Coll. Med. Sch., London WlT 4JF, United Kingdom; email: paul.grant@ucl.ac.uk",,,00284793,,NEJMA,"14681520","English","New Engl. J. Med.",Letter,"Final",,Scopus,2-s2.0-0346750842
"Olsen S.J., Chang H.-L., Cheung T.Y.-Y., Tang A.F.-Y., Fisk T.L., Ooi S.P.-L., Kuo H.-W., Jiang D.D.-S., Chen K.-T., Lando J., Hsu K.-H., Chen T.-J., Dowell S.F.","7202568721;35797866800;57213837008;7201845865;6701575728;7003536324;25421570000;7401574443;7410239362;7006183560;57207086112;7405543674;7004419871;","Transmission of the Severe Acute Respiratory Syndrome on Aircraft",2003,"New England Journal of Medicine","349","25",,"2416","2422",,288,"10.1056/NEJMoa031349","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0346750857&doi=10.1056%2fNEJMoa031349&partnerID=40&md5=0823b379d2e01137e0ce0fde21735a21","Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Nonthaburi, Thailand; Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Department of Health, Hong Kong Spec. Admin. Region, China; Emory University School of Medicine, Atlanta, GA, United States; Epidemiol. and Dis. Control Division, Ministry of Health, Singapore, Singapore; Natl. Ctr. for Chron. Dis. Prev., Ctrs. for Dis. Contr. and Prevention, Atlanta, GA, United States; Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Box 68, American Embassy APO, AP 96546, United States","Olsen, S.J., Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Nonthaburi, Thailand, Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Box 68, American Embassy APO, AP 96546, United States; Chang, H.-L., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Cheung, T.Y.-Y., Department of Health, Hong Kong Spec. Admin. Region, China; Tang, A.F.-Y., Department of Health, Hong Kong Spec. Admin. Region, China; Fisk, T.L., Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Nonthaburi, Thailand, Emory University School of Medicine, Atlanta, GA, United States; Ooi, S.P.-L., Epidemiol. and Dis. Control Division, Ministry of Health, Singapore, Singapore; Kuo, H.-W., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Jiang, D.D.-S., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Chen, K.-T., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Lando, J., Natl. Ctr. for Chron. Dis. Prev., Ctrs. for Dis. Contr. and Prevention, Atlanta, GA, United States; Hsu, K.-H., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Chen, T.-J., Taiwan Center for Disease Control, Department of Health, Taipei, Taiwan; Dowell, S.F., Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Nonthaburi, Thailand","BACKGROUND: The severe acute respiratory syndrome (SARS) spread rapidly around the world, largely because persons infected with the SARS-associated coronavirus (SARS-CoV) traveled on aircraft to distant cities. Although many infected persons traveled on commercial aircraft, the risk, if any, of in-flight transmission is unknown. METHODS: We attempted to interview passengers and crew members at least 10 days after they had taken one of three flights that transported a patient or patients with SARS. All index patients met the criteria of the World Health Organization for a probable case of SARS, and index or secondary cases were confirmed to be positive for SARS-COV on reverse-transcriptase polymerase chain reaction or serologic testing. RESULTS: After one flight carrying a symptomatic person and 119 other persons, laboratory-confirmed SARS developed in 16 persons, 2 others were given diagnoses of probable SARS, and 4 were reported to have SARS but could not be interviewed. Among the 22 persons with illness, the mean time from the flight to the onset of symptoms was four days (range, two to eight), and there were no recognized exposures to patients with SARS before or after the flight. Illness in passengers was related to the physical proximity to the index patient, with illness reported in 8 of the 23 persons who were seated in the three rows in front of the index patient, as compared with 10 of the 88 persons who were seated elsewhere (relative risk, 3.1; 95 percent confidence interval, 1.4 to 6.9). In contrast, another flight carrying four symptomatic persons resulted in transmission to at most one other person, and no illness was documented in passengers on the flight that carried a person who had presymptomatic SARS. CONCLUSIONS: Transmission of SARS may occur on an aircraft when infected persons fly during the symptomatic phase of illness. Measures to reduce the risk of transmission are warranted.",,"acute disease; aircraft; article; aviation; China; Coronavirus; disease transmission; Hong Kong; human; interview; major clinical study; priority journal; respiratory tract infection; reverse transcription polymerase chain reaction; SARS coronavirus; serology; severe acute respiratory syndrome; travel; virus detection; virus infection; virus transmission; Aged; Aircraft; Disease Transmission, Horizontal; Environmental Exposure; Hong Kong; Humans; Male; Middle Aged; Risk Factors; Severe Acute Respiratory Syndrome; Travel","(2003) Summary of Probable SARS Cases with Onset of Illness from 1 November 2002 to 31 July 2003, , http://www.who.int/csr/sars/country/table2003_09_23/en/, Geneva; Update: Outbreak of severe acute respiratory syndrome - Worldwide, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 241-246; Erratum (2003) MMWR. Morb Mortal Wkly Rep, 52, p. 284; (2003) Update 11 - WHO Recommends New Measures to Prevent Travel-Related Spread of SARS, , http://www.who.int/csr/sars/archive/2003_03_27/en/, Geneva; (2003) Interim Guidance for Cleaning of Commercial Passenger Aircraft Following a Flight with a Passenger with Suspected Severe Acute Respiratory Syndrome (SARS), , http://www.cdc.gov/ncidod/sars/aircraftcleanup.htm, Atlanta; (2003) Interim Guidelines about Severe Acute Respiratory Syndrome (SARS) for Airline Flight Crew Members, , http://www.cdc.gov/ncidod/sars/flight_crew_guidelines.htm, Atlanta; (2003) Case Definitions for Surveillance of Severe Acute Respiratory Syndrome (SARS), , http://www.who.int/csr/sars/casedefinition/en/, Geneva; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Kahn, J., Rosenthal, E., Illness spreads to remote China (2003) International Herald Tribune, 1, p. 4. , Taipei; Lakshmanan, I.A.R., (2003) Air China Flight 112: Tracking the Genesis of a Plague, , Boston Globe. May 18; WHO recommended measures for persons undertaking international travel from areas affected by severe acute respiratory syndrome (SARS) (2003) Wkly Epidemiol Rec, 78, pp. 97-99; Hsu, L.-Y., Lee, C.-C., Green, J.A., Severe acute respiratory syndrome (SARS) in Singapore: Clinical features of index patient and initial contacts (2003) Emerg Infect Dis, 9, pp. 713-717. , http://www.cdc.gov/ncidod/EID/vol9no6/03-0264.htm; Booth, C.M., Matukas, L.M., Tomlinson, G.A., Clinical features and short-term outcomes of 144 patients with SARS in the Greater Toronto area (2003) JAMA, 289, pp. 2801-2809; Erratum (2003) JAMA, 290, p. 334. , http://jama.ama-assn.org/cgi/content/full/289.21JOC30885v1; Kenyon, T.A., Valway, S.E., Ihle, W.W., Onorato, I.M., Castro, K.G., Transmission of multidrug-resistant Mycobacterium tuberculosis during a long airplane flight (1996) N Engl J Med, 334, pp. 933-938; Garner, J.S., (1997) Guideline for Isolation Precautions in Hospitals, , http://www.cdc.gov/ncidod/hip/isolat/isolat.htm, Atlanta; Seto, W.H., Tsang, D., Yung, R.W.H., Effectiveness of precautions against droplets and contact in prevention of nosocomial transmission of severe acute respiratory syndrome (SARS) (2003) Lancet, 361, pp. 1519-1520; Musher, D.M., How contagious are common respiratory tract infections? (2003) N Engl J Med, 348, pp. 1256-1266; Moser, M.R., Bender, T.R., Margolis, H.S., Noble, G.R., Kendal, A.P., Ritter, D.G., An outbreak of influenza aboard a commercial airliner (1979) Am J Epidemiol, 110, pp. 1-6; Exposure of passengers and flight crew to Mycobacterium tuberculosis on commercial aircraft, 1992-1995 (1995) MMWR Morb Mortal Wkly Rep, 44, pp. 137-140; Erratum (1995) MMWR Morb Mortal Wkly Rep, 44, p. 175; Severe acute respiratory syndrome - Singapore, 2003 (2003) MMWR Morb Mortal Wkly Rep, 52, pp. 405-411; (2003) Did You Know That? Facts about the Industry Response to SARS, , http://www.iata.org/WHIP/_Files/Wgld_0263/Did%20You%20Know%20That.doc; (2003) Update 59 - Report on Guangxi (China) Visit, Situation in Taiwan, Risk of SARS Transmission during Air Travel, , http://www.who.int/csr/sars/archive/2003_05_19/en/print.html, Geneva; Wenzel, R.P., Airline travel and infection (1996) N Engl J Med, 334, pp. 981-982; Demers, R.R., Bacterial/viral filtration: Let the breather beware! (2001) Chest, 120, pp. 1377-1389; (2003) Update 62-More Than 8000 Cases Reported Globally, Situation in Taiwan, Data on in-Flight Transmission, Report on Henan Province, China, , http://www.who.int/csr/don/2003_05_22/en/, Geneva","Olsen, S.J.; Intl. Emerging Infections Program, Ctrs. for Dis. Contr. and Prevention, Box 68, American Embassy APO, AP 96546, United States; email: sco2@cdc.gov",,,00284793,,NEJMA,"14681507","English","New Engl. J. Med.",Article,"Final",Open Access,Scopus,2-s2.0-0346750857
"Smales F.C., Samaranyake L.P.","7004018285;57191921359;","Maintaining dental education and specialist dental care during an outbreak of a new coronavirus infection. Part 2: Control of the disease, then elimination",2003,"British Dental Journal","195","12",,"679","681",,,"10.1038/sj.bdj.4810819","https://www.scopus.com/inward/record.uri?eid=2-s2.0-1342289020&doi=10.1038%2fsj.bdj.4810819&partnerID=40&md5=5587b7a056625102bbfb31ca0d3fed96","Faculty of Dentistry, Prince Philip Dental Hospital, Hong Kong, Hong Kong; Department of Oral Microbiology, Prince Philip Dental Hospital, Hong Kong, Hong Kong; University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong","Smales, F.C., Faculty of Dentistry, Prince Philip Dental Hospital, Hong Kong, Hong Kong, University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong; Samaranyake, L.P., Department of Oral Microbiology, Prince Philip Dental Hospital, Hong Kong, Hong Kong","On Thursday 27th March 2003 the decision had been made to stop all clinical teaching and all non-elective patient care at the Prince Philip Dental Hospital, the teaching hospital of the Faculty of Dentistry of the University of Hong Kong. A lethal respiratory disease of unknown aetiology was spreading through the community but also in medical hospitals where it was infecting healthcare workers with apparent ease. Infections in an apartment block called Amoy Gardens seemed to have taken place by the deadly long distance airborne transmission route. The daily numbers of new cases of Severe Acute Respiratory Syndrome were rising exponentially. Normally bustling streets and public buildings of Hong Kong had fallen silent. © British Dental Journal 2003.",,"airborne infection; clinical education; dental care; dental clinic; dental education; disease control; disease transmission; health service; human; infection control; medical specialist; patient care; review; severe acute respiratory syndrome; university hospital; virus infection; world health organization; article; dental clinic; dental education; epidemic; Hong Kong; infection control; methodology; severe acute respiratory syndrome; university; Dental Clinics; Disease Outbreaks; Hong Kong; Humans; Infection Control, Dental; Schools, Dental; Severe Acute Respiratory Syndrome; Universities","Ksiazek, T.G., Erdman, D., Goldsmitn, C.S., A novel coronavirus associated with severe acute respiratory syndrome (2003) N Engl J Med, 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Lee, N., Hui, D., Wu, A., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N Engl J Med, 348, pp. 1986-1994; Fouchier, R.A., Kuiken, T., Schutten, M., Aetiology: Koch's postulates fulfilled for SARS virus (2003) Nature, 423, p. 240; Holmes, K.V., SARS-associated coronavirus (2003) N Engl J Med, 348, pp. 1948-1951; (2003) Basic Information about SARS, , http://www.cdc.gov/ncidod/sars/factsheet.htm, Atlanta: Centres for Disease Control and Prevention. May; Li, R.W.K., Leung, K.W.C., Sun, F.C.S., Samaranayake, L.P., Severe acute respiratory syndrome and the general practitioner Br Dent J, , In press","Smales, F.C.; University of Hong Kong, Prince Philip Dental Hospital, 34 Hospital Road, Hong Kong, Hong Kong; email: fcsmales@hkusua.hku.hk",,,00070610,,,"14718953","English","Brit. Dent. J.",Review,"Final",Open Access,Scopus,2-s2.0-1342289020
"Kushner D.B., Lindenbach B.D., Grdzelishvili V.Z., Noueiry A.O., Paul S.M., Ahlquist P.","7102619306;6603129948;6506169674;6602298964;55851946620;7005504033;","Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus",2003,"Proceedings of the National Academy of Sciences of the United States of America","100","26",,"15764","15769",,196,"10.1073/pnas.2536857100","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0347364637&doi=10.1073%2fpnas.2536857100&partnerID=40&md5=4894dbff050620ecfc74bde113cda803","Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States; Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706, United States; Department of Biology, Dickinson College, Carlisle, PA 17013, United States; Center for the Study of Hepatitis C, Rockefeller University, New York, NY 10021, United States; Department of Bacteriology, University of Wisconsin, Madison, WI 53726, United States; Institute for Molecular Virology, University of Wisconsin, 1525 Linden Drive, Madison, WI 53706, United States","Kushner, D.B., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States, Department of Biology, Dickinson College, Carlisle, PA 17013, United States; Lindenbach, B.D., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States, Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706, United States, Center for the Study of Hepatitis C, Rockefeller University, New York, NY 10021, United States; Grdzelishvili, V.Z., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States; Noueiry, A.O., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States; Paul, S.M., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States, Department of Bacteriology, University of Wisconsin, Madison, WI 53726, United States; Ahlquist, P., Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706, United States, Howard Hughes Medical Institute, University of Wisconsin, Madison, WI 53706, United States, Institute for Molecular Virology, University of Wisconsin, 1525 Linden Drive, Madison, WI 53706, United States","Positive-strand RNA viruses are the largest virus class and include many pathogens such as hepatitis C virus and the severe acute respiratory syndrome coronavirus (SARS). Brome mosaic virus (BMV) is a representative positive-strand RNA virus whose RNA replication, gene expression, and encapsulation have been reproduced in the yeast Saccharomyces cerevisiae. By using traditional yeast genetics, host genes have been identified that function in controlling BMV translation, selecting BMV RNAs as replication templates, activating the replication complex, maintaining a lipid composition required for membrane-associated RNA replication, and other steps. To more globally and systematically identify such host factors, we used engineered BMV derivatives to assay viral RNA replication in each strain of an ordered, genome-wide set of yeast single-gene deletion mutants. Each deletion strain was transformed to express BMV replicase proteins and a BMV RNA replication template with the capsid gene replaced by a luciferase reporter. Luciferase expression, which is dependent on viral RNA replication and RNA-dependent mRNA synthesis, was measured in intact yeast cells. Approximately 4,500 yeast deletion strains (≈80% of yeast genes) were screened in duplicate and selected strains analyzed further. This functional genomics approach revealed nearly 100 genes whose absence inhibited or stimulated BMV RNA replication and/or gene expression by 3- to >25-fold. Several of these genes were shown previously to function in BMV replication, validating the approach. Newly identified genes include some in RNA, protein, or membrane modification pathways and genes of unknown function. The results further illuminate virus and cell pathways. Further refinement of virus screening likely will reveal contributions from additional host genes.",,"luciferase; virus RNA; article; fungal gene; gene deletion; gene expression; gene function; gene identification; gene replication; genetic engineering; genome; Hepatitis C virus; lipid composition; messenger RNA synthesis; Mosaic virus; nonhuman; priority journal; protein modification; reporter gene; RNA replication; RNA virus; Saccharomyces cerevisiae; SARS coronavirus; virus capsid; virus replication; yeast cell; Bromovirus; Coronavirus; Enzymes; Genome, Viral; Hepacivirus; Humans; RNA Viruses; RNA, Viral; Viral Proteins; Virus Replication; Brome mosaic virus; Bromus; Coronavirus; Hepatitis C virus; RNA viruses; Saccharomyces; Saccharomyces cerevisiae; SARS coronavirus","Lai, M.M.C., (1998) Virology, 244, pp. 1-12; Ahlquist, P., Noueiry, A.O., Lee, W.M., Kushner, D.B., Dye, B.T., (2003) J. Virol., 77, pp. 8181-8186; Kao, C.C., Sivakumaran, K., (2000) Mol. 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Biol., 23, pp. 4094-4106; Tomita, Y., Mizuno, T., Diez, J., Naito, S., Ahlquist, P., Ishikawa, M., (2003) J. Virol., 77, pp. 2990-2997; Noueiry, A.O., Ahlquist, P., (2003) Annu. Rev. Phytopathol., 41, pp. 77-98; Winzeler, E.A., Shoemaker, D.D., Astromoff, A., Liang, H., Anderson, K., Andre, B., Bangham, R., Bussey, H., (1999) Science, 285, pp. 901-906; Brachmann, C.B., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P., Boeke, J.D., (1998) Yeast, 14, pp. 115-132; Guthrie, C., Fink, G.R., (1991) Methods Enzymol., 194. , Academic, San Diego; Chen, D.C., Yang, B.C., Kuo, T.T., (1992) Curr. Genet., 21, pp. 83-84; Ishikawa, M., Janda, M., Krol, M.A., Ahlquist, P., (1997) J. Virol., 71, pp. 7781-7790; Mumberg, D., Muller, R., Funk, M., (1994) Nucleic Acids Res., 22, pp. 5767-5768; Mascorro-Gallardo, J.O., Covarrubias, A.A., Gaxiola, R., (1996) Gene, 172, pp. 169-170; Sikorski, R.S., Hieter, P., (1989) Genetics, 122, pp. 19-27; Johnston, M., Davis, R.W., (1984) Mol. Cell. Biol., 4, pp. 1440-1448; French, R., Janda, M., Ahlquist, P., (1986) Science, 231, pp. 1294-1297; Vieites, J.M., Navarro-Garcia, F., Perez-Diaz, R., Pla, J., Nombela, C., (1994) Yeast, 10, pp. 1321-1327; Srikantha, T., Klapach, A., Lorenz, W.W., Tsai, L.K., Laughlin, L.A., Gorman, J.A., Soll, D.R., (1996) J. Bacteriol., 178, pp. 121-129; Wickner, R.B., (1996) Microbiol. Rev., 60, pp. 250-265; Gu, Z., Steinmetz, L.M., Gu, X., Scharfe, C., Davis, R.W., Li, W.H., (2003) Nature, 421, pp. 63-66; Gao, G., Guo, X., Goff, S.P., (2002) Science, 297, pp. 1703-1706; Izaurralde, E., Lewis, J., McGuigan, C., Jankowska, M., Darzynkiewicz, E., Mattaj, I.W., (1994) Cell, 78, pp. 657-668; Ishigaki, Y., Li, X., Serin, G., Maquat, L.E., (2001) Cell, 106, pp. 607-617; Sullivan, M., Ahlquist, P., (1999) J. Virol., 73, pp. 2622-2632; Fischer, N., Weis, K., (2002) EMBO J., 21, pp. 2788-2797; Coller, J.M., Tucker, M., Sheth, U., Valencia-Sanchez, M.A., Parker, R., (2001) RNA, 7, pp. 1717-1727; Benard, L., Carroll, K., Valle, R.C., Masison, D.C., Wickner, R.B., (1999) J. Virol., 73, pp. 2893-2900; Araki, Y., Takahashi, S., Kobayashi, T., Kajiho, H., Hoshino, S., Katada, T., (2001) EMBO J., 20, pp. 4684-4693; Enenkel, C., Lehmann, A., Kloetzel, P.M., (1998) EMBO J., 17, pp. 6144-6154; Restrepo-Hartwig, M., Ahlquist, P., (1996) J. Virol., 70, pp. 8908-8916; DeGroot, R.J., Rümenapf, T., Kuhn, R.J., Strauss, E.G., Strauss, J.H., (1991) Biochemistry, 88, pp. 8967-8971; Kim, S.H., Palukaitis, P., Park, Y.I., (2002) EMBO J., 21, pp. 2292-2300; Lee, W.M., Ahlquist, P., (2003) J. Virol., 77, pp. 12819-12828; Gaigg, B., Neergaard, T.B., Schneiter, R., Hansen, J.K., Faergeman, N.J., Jensen, N.A., Andersen, J.R., Knudsen, J., (2001) Mol. Biol. Cell., 12, pp. 1147-1160; Tu, H., Gao, L., Shi, S.T., Taylor, D.R., Yang, T., Mircheff, A.K., Wen, Y., Lai, M.M., (1999) Virology, 263, pp. 30-41; Kellis, M., Patterson, N., Endrizzi, M., Birren, B., Lander, E.S., (2003) Nature, 423, pp. 241-254","Ahlquist, P.; Institute for Molecular Virology, University of Wisconsin, 1525 Linden Drive, Madison, WI 53706, United States; email: ahlquist@wisc.edu",,,00278424,,PNASA,"14671320","English","Proc. Natl. Acad. Sci. U. S. A.",Article,"Final",Open Access,Scopus,2-s2.0-0347364637
"Lau L.T., Fung Y.-W.W., Wong F.P.-F., Lin S.S.-W., Wang C.R., Li H.L., Dillon N., Collins R.A., Tam J.S.-L., Chan P.K.S., Wang C.G., Yu A.C.-H.","7101892115;7202871650;7201409682;7407159027;9845836100;15034136600;7005728858;36875056600;24788939600;32067487100;55947457900;7401478731;","A real-time PCR for SARS-coronavirus incorporating target gene pre-amplification",2003,"Biochemical and Biophysical Research Communications","312","4",,"1290","1296",,22,"10.1016/j.bbrc.2003.11.064","https://www.scopus.com/inward/record.uri?eid=2-s2.0-10744225752&doi=10.1016%2fj.bbrc.2003.11.064&partnerID=40&md5=5671c86eb31dbd0761350e3fafdd43f7","Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China; Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong SAR, Hong Kong; Natl. Emergency Action on SARS Res., Beijing, China","Lau, L.T., Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China, Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Fung, Y.-W.W., Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Wong, F.P.-F., Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Lin, S.S.-W., Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Wang, C.R., Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China; Li, H.L., Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China; Dillon, N., Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Collins, R.A., Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong; Tam, J.S.-L., Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong SAR, Hong Kong; Chan, P.K.S., Department of Microbiology, Prince of Wales Hospital, Chinese University of Hong Kong, Hong Kong SAR, Hong Kong; Wang, C.G., Natl. Emergency Action on SARS Res., Beijing, China; Yu, A.C.-H., Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China, Hong Kong DNA Chips Ltd., Cosmos Centre, 108 Soy Street, Kowloon, SAR, Hong Kong, Natl. Emergency Action on SARS Res., Beijing, China","An enhanced polymerase chain reaction (PCR) assay to detect the coronavirus associated with severe acute respiratory syndrome (SARS-CoV) was developed in which a target gene pre-amplification step preceded TaqMan real-time fluorescent PCR. Clinical samples were collected from 120 patients diagnosed as suspected or probable SARS cases and analyzed by conventional PCR followed by agarose gel electrophoresis, conventional TaqMan real-time PCR, and our enhanced TaqMan real-time PCR assays. An amplicon of the size expected from SARS-CoV was obtained from 28/120 samples using the enhanced real-time PCR method. Conventional PCR and real-time PCR alone identified fewer SARS-CoV positive cases. Results were confirmed by viral culture in 3/28 cases. The limit of detection of the enhanced real-time PCR method was 102-fold higher than the standard real-time PCR assay and 107-fold higher than conventional PCR methods. The increased sensitivity of the assay may help control the spread of the disease during future SARS outbreaks. © 2003 Elsevier Inc. All rights reserved.","Coronavirus; PCR; SARS; SARS-CoV; Severe acute respiratory syndrome; TaqMan real-time fluorescent polymerase chain reaction","agar gel electrophoresis; amplicon; article; blood sampling; controlled study; Coronavirus; diagnostic accuracy; epidemic; gene amplification; gene targeting; human; intermethod comparison; major clinical study; polymerase chain reaction; priority journal; SARS coronavirus; severe acute respiratory syndrome; virus culture; virus detection; virus diagnosis; virus identification; virus isolation; virus particle; virus pneumonia; virus strain; virus transmission; Coronavirus; SARS coronavirus","Drosten, C., Gunther, S., Preiser, W., Van Der Werf, S., Brodt, H.R., Becker, S., Rabenau, H., Fouchier, R.A., Identification of a novel coronavirus in patients with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1967-1976; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Lim, W., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Peiris, J.S., Lai, S.T., Poon, L.L., Guan, Y., Yam, L.Y., Lim, W., Nicholls, J., Cheung, M.T., Coronavirus as a possible cause of severe acute respiratory syndrome (2003) Lancet, 361, pp. 1319-1325; Lee, N., Hui, D., Wu, A., Chan, P., Cameron, P., Joynt, G.M., Ahuja, A., To, K.F., A major outbreak of severe acute respiratory syndrome in Hong Kong (2003) N. Engl. J. Med., 348, pp. 1986-1994; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Chen, M.H., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Chan, S.Y., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Stohr, K., A multicentre collaboration to investigate the cause of severe acute respiratory syndrome (2003) Lancet, 360, pp. 1730-1733; Patrick, D.M., The race to outpace severe acute respiratory syndrome (SARS) (2003) CMAJ, 168, pp. 1265-1266; Falsey, A.R., Walsh, E.E., Novel coronavirus and severe acute respiratory syndrome (2003) Lancet, 361, pp. 1312-1313; McIntosh, K., The SARS coronavirus: Rapid diagnostics in the limelight (2003) Clin. Chem., 49, pp. 845-846; Tsang O.T-Y, Chau, T.-N., Choi, K.-W., Tso E.Y-K, Lim, W., Chiu, M.-C., Tong, W.-L., Lai, S.-T., Coronavirus-positive nasopharyngeal aspirate as predictor for severe acute respiratory syndrome mortality Emerg. Infect. Dis., 9. , http://www.cdc.gov/ncidod/EID/vol9no11/03-0400.htm, November 2003; Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res., 25, pp. 3389-3402; Tatusova, T.A., Madden, T.L., Blast 2 sequences - A new tool for comparing protein and nucleotide sequences (1999) FEMS Microbiol. Lett., 174, pp. 247-250; Ng, S.K.C., Possible role of an animal vector in the SARS outbreak at Amoy Gardens (2003) Lancet, 362, pp. 570-572","Yu, A.C.-H.; Neuroscience Research Institute, Peking University, Department of Neurobiology, 38 Xue Yuan Road, Beijing 100083, China; email: achy@dnachip.com.hk",,"Academic Press Inc.",0006291X,,BBRCA,"14652014","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-10744225752
"Xiao X., Chakraborti S., Dimitrov A.S., Gramatikoff K., Dimitrov D.S.","7402168892;7006780922;7101600999;6507884540;7202564539;","The SARS-CoV S glycoprotein: Expression and functional characterization",2003,"Biochemical and Biophysical Research Communications","312","4",,"1159","1164",,195,"10.1016/j.bbrc.2003.11.054","https://www.scopus.com/inward/record.uri?eid=2-s2.0-0344064125&doi=10.1016%2fj.bbrc.2003.11.054&partnerID=40&md5=4f67f260c52c994f9f6a6aa0f7a7011f","Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States; Abgent, San Diego, CA 92121, United States","Xiao, X., Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States; Chakraborti, S., Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States; Dimitrov, A.S., Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States; Gramatikoff, K., Abgent, San Diego, CA 92121, United States; Dimitrov, D.S., Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States","We have cloned, expressed, and characterized the full-length and various soluble fragments of the SARS-CoV (Tor2 isolate) S glycoprotein. Cells expressing S fused with receptor-expressing cells at neutral pH suggesting that the recombinant glycoprotein is functional, its membrane fusogenic activity does not require other viral proteins, and that low pH is not required for triggering membrane fusion; fusion was not observed at low receptor concentrations. S and its soluble ectodomain, Se, were not cleaved to any significant degree. They ran at about 180-200kDa in SDS gels suggesting post-translational modifications as predicted by previous computer analysis and observed for other coronaviruses. Fragments containing the N-terminal amino acid residues 17-537 and 272-537 but not 17-276 bound specifically to Vero E6 cells and purified soluble receptor, ACE2, recently identified by M. Farzan and co-workers [Nature 426 (2003) 450-454]. Together with data for inhibition of binding by antibodies developed against peptides from S, these findings suggest that the receptor-binding domain is located between amino acid residues 303 and 537. These results also confirm that ACE2 is a functional receptor for the SARS virus and may help in the elucidation of the mechanisms of SARS-CoV entry and in the development of vaccine immunogens and entry inhibitors.","Binding; Fusion; Inhibitor; Receptor; S glycoprotein; SARS-CoV; Vaccine","amino acid; antibody; glycoprotein; peptide; protein; receptor; virus protein; virus vaccine; article; computer analysis; Coronavirus; expression vector; immunogenetics; immunoprecipitation; membrane fusion; nonhuman; pH; plasmid; priority journal; protein expression; protein purification; rabbit; receptor binding; respiratory tract infection; severe acute respiratory syndrome; virus characterization; virus envelope; virus expression; virus infection; virus inhibition; Western blotting; Coronavirus; Oryctolagus cuniculus; SARS coronavirus; vectors","Dimitrov, D.S., Cell biology of virus entry (2000) Cell, 101, pp. 697-702; Holmes, K.V., SARS-associated coronavirus (2003) N. Engl. J. Med., 348, pp. 1948-1951; Lai, M.M., Cavanagh, D., The molecular biology of coronaviruses (1997) Adv. Virus Res., 48, pp. 1-100; Ksiazek, T.G., Erdman, D., Goldsmith, C.S., Zaki, S.R., Peret, T., Emery, S., Tong, S., Anderson, L.J., A novel coronavirus associated with severe acute respiratory syndrome (2003) N. Engl. J. Med., 348, pp. 1953-1966; Rota, P.A., Oberste, M.S., Monroe, S.S., Nix, W.A., Campagnoli, R., Icenogle, J.P., Penaranda, S., Bellini, W.J., Characterization of a novel coronavirus associated with severe acute respiratory syndrome (2003) Science, 300, pp. 1394-1399; Marra, M.A., Jones, S.J., Astell, C.R., Holt, R.A., Brooks-Wilson, A., Butterfield, Y.S., Khattra, J., Roper, R.L., The genome sequence of the SARS-associated coronavirus (2003) Science, 300, pp. 1399-1404; Gallagher, T.M., Buchmeier, M.J., Coronavirus spike proteins in viral entry and pathogenesis (2001) Virology, 279, pp. 371-374; Kunkel, F., Herrler, G., Structural and functional analysis of the surface protein of human coronavirus OC43 (1993) Virology, 195, pp. 195-202; Bonavia, A., Zelus, B.D., Wentworth, D.E., Talbot, P.J., Holmes, K.V., Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E (2003) J. Virol., 77, pp. 2530-2538; Li, W., Moore, M.J., Vasilieva, N., Sui, J., Wong, S.K., Berne, M.A., Somasundaran, M., Farzan, M., Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus (2003) Nature, 426, pp. 450-454","Dimitrov, D.S.; Lab. of Exp. and Compl. Biology, CCR, NIH, Frederick, MD 21702-1201, United States; email: dimitrov@ncifcrf.gov",,"Academic Press Inc.",0006291X,,BBRCA,"14651994","English","Biochem. Biophys. Res. Commun.",Article,"Final",Open Access,Scopus,2-s2.0-0344064125