Skip to main content
PMC home page
Elsevier - PMC COVID-19 Collection logoLink to Elsevier - PMC COVID-19 Collection
. 2008 Mar 1;48:1–100. doi: 10.1016/S0065-3527(08)60286-9

The Molecular Biology of Coronaviruses

Michael MC Lai *, David Cavanagh †
PMCID: PMC7130985  PMID: 9233431

Publisher Summary

This chapter discusses the manipulation of clones of coronavirus and of complementary DNAs (cDNAs) of defective-interfering (DI) RNAs to study coronavirus RNA replication, transcription, recombination, processing and transport of proteins, virion assembly, identification of cell receptors for coronaviruses, and processing of the polymerase. The nature of the coronavirus genome is nonsegmented, single-stranded, and positive-sense RNA. Its size ranges from 27 to 32 kb, which is significantly larger when compared with other RNA viruses. The gene encoding the large surface glycoprotein is up to 4.4 kb, encoding an imposing trimeric, highly glycosylated protein. This soars some 20 nm above the virion envelope, giving the virus the appearance-with a little imagination-of a crown or coronet. Coronavirus research has contributed to the understanding of many aspects of molecular biology in general, such as the mechanism of RNA synthesis, translational control, and protein transport and processing. It remains a treasure capable of generating unexpected insights.

References

  1. Anderson R., Wong F. Membrane and phospholipid binding by murine coronaviral nucleocapsid N protein. Virology. 1993;194:224–232. doi: 10.1006/viro.1993.1253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Armstrong J., Patel S. The Golgi sorting domain of coronavirus E1 protein. J. Cell Sci. 1991;98:567–575. doi: 10.1242/jcs.98.4.567. [DOI] [PubMed] [Google Scholar]
  3. Armstrong J., Niemann H., Smeekens S., Rottier P., Warren G. Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus. Nature (London) 1984;308:751–752. doi: 10.1038/308751a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Armstrong J., Patel S., Riddle P. Lysosomal sorting mutants of coronavirus E1 protein, a Golgi membrane protein. J. Cell Sci. 1990;95:191–197. doi: 10.1242/jcs.95.2.191. [DOI] [PubMed] [Google Scholar]
  5. Asanaka M., Lai M.M.C. Cell fusion studies identified multiple cellular factors involved in mouse hepatitis virus entry. Virology. 1993;197:732–741. doi: 10.1006/viro.1993.1649. [DOI] [PubMed] [Google Scholar]
  6. Baker S.C., Shieh C.-K., Soe L.H., Chang M.-F., Vannier D.M., Lai M.M.C. Identification of a domain required for the autoproteolytic cleavage of murine coronavirus gene A polyprotein. J. Virol. 1989;63:3693–3699. doi: 10.1128/jvi.63.9.3693-3699.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Baker S.C., Yokomori K., Dong S., Carlisle R., Gorbalenya A.E., Koonin E.V., Lai M.M.C. Identification of the catalytic sites of a papain-like cystein proteinase of murine coronavirus. J. Virol. 1993;67:6056–6063. doi: 10.1128/jvi.67.10.6056-6063.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ballesteros M.L., Sanchez C.M., Enjuanes L. Two amino acid changes at the N-terminus of transmissible gastroenteritis coronavirus spike protein result in the loss of enteric tropism. Virology. 1997;227(2):378–388. doi: 10.1006/viro.1996.8344. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Banner L.R., Lai M.M.C. Random nature of coronavirus RNA recombination in the absence of selection pressure. Virology. 1991;185:441–445. doi: 10.1016/0042-6822(91)90795-D. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Banner L.R., Keck J.G., Lai M.M.C. A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus. Virology. 1990;175:548–555. doi: 10.1016/0042-6822(90)90439-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Baric R.S., Stohlman S.A., Razavi M.K., Lai M.M.C. Characterization of leader-related small RNAs in coronavirus-infected cells: Further evidence for leader-primed mechanism of transcription. Virus Res. 1985;3:19–33. doi: 10.1016/0168-1702(85)90038-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Baric R.S., Shieh C.-K., Stohlman S.A., Lai M.M.C. Analysis of intracellular small RNAs of mouse hepatitis virus: Evidence for discontinuous transcription. Virology. 1987;156:342–354. doi: 10.1016/0042-6822(87)90414-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Baric R.S., Nelson G.W., Fleming J.O., Deans R.J., Keck J.G., Casteel N., Stohlman S.A. Interactions between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription. J. Virol. 1988;62:4280–4287. doi: 10.1128/jvi.62.11.4280-4287.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Baric R.S., Fu K., Schaad M.C., Stohlman S.A. Establishing a genetic recombination map for murine coronavirus strain A59 complementation groups. Virology. 1990;177:646–656. doi: 10.1016/0042-6822(90)90530-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Baric R.S., Yount B., Hensley L., Peel S.A., Chen W. Episodic evolution mediates interspecies transfer of a murine coronavirus. J. Virol. 1997;71:1946–1955. doi: 10.1128/jvi.71.3.1946-1955.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B. Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus. J. Virol. 1997;71:734–737. doi: 10.1128/jvi.71.1.734-737.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Beushausen S., Narindrasorasak S., Sanwal B.D., Dales S. In vivo and in vitro models of demyelinating disease: Activation of the adenylate cyclase system influences JHM virus expression in explanted rat oligodendrocytes. J. Virol. 1987;61:3795–3803. doi: 10.1128/jvi.61.12.3795-3803.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Bonilla P.J., Gorbalenya A.E., Weiss S.R. Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: Heterogeneity among MHV strains. Virology. 1994;198:736–740. doi: 10.1006/viro.1994.1088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Bonilla P.J., Hughes S.A., Pinon J.D., Weiss S.R. Characterization of the leader papain-like proteinase of MHV-A59: Identification of a new in vitro cleavage site. Virology. 1995;209:489–497. doi: 10.1006/viro.1995.1281. [DOI] [PubMed] [Google Scholar]
  20. Bonilla P.J., Hughes S.A., Weiss S.R. Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59. J. Virol. 1997;71:900–909. doi: 10.1128/jvi.71.2.900-909.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Bos E.C.W., Heunen L., Luytjes W., Spaan W.J.M. Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion. Virology. 1995;214:453–463. doi: 10.1006/viro.1995.0056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Bos E.C.W., Luytjes W., van der Meulen H., Koerten H.K., Spaan W.J.M. The production of recombinant infectious DI-particles of a murine coronavirus in the absence of helper virus. Virology. 1996;218:52–60. doi: 10.1006/viro.1996.0165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Boursnell M.E.G., Brown T.D.K., Foulds I.J., Green P.F., Tomley F.M., Binns M.M. Completion of the sequence of the genome of the coronavirus avian infectious bronchitis virus. J. Gen. Virol. 1987;68:57–77. doi: 10.1099/0022-1317-68-1-57. [DOI] [PubMed] [Google Scholar]
  24. Brayton P.R., Ganges R.G., Stohlman S.A. Host cell nuclear function and murine hepatitis virus replication. J. Gen. Virol. 1981;56:457–460. doi: 10.1099/0022-1317-56-2-457. [DOI] [PubMed] [Google Scholar]
  25. Brayton P.R., Lai M.M.C., Patton C.D., Stohlman S.A. Characterization of two RNA polymerase activities induced by mouse hepatitis virus. J. Virol. 1982;42:847–853. doi: 10.1128/jvi.42.3.847-853.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Brayton P.R., Stohlman S.A., Lai M.M.C. Further characterization of mouse hepatitis virus RNA dependent RNA polymerases. Virology. 1984;133:197–201. doi: 10.1016/0042-6822(84)90439-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Bredenbeek P.J., Pachuk C.J., Noten A.F.H., Charite J., Luytjes W., Weiss S.R., Spaan W.J.M. The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59: A highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism. Nucleic Acids Res. 1990;18:1825–1832. doi: 10.1093/nar/18.7.1825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Brierley I., Boursnell M.E.G., Binns M.M., Bilimoria B., Blok V.C., Brown T.D.K., Inglis S.C. An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV. EMBO J. 1987;6:3779–3785. doi: 10.1002/j.1460-2075.1987.tb02713.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Brierley I., Digard P., Inglis S.C. Characterization of an efficient coronavirus ribosomal frame-shifting signal: Requirement for an RNA pseudoknot. Cell (Cambridge, Mass.) 1989;57:537–547. doi: 10.1016/0092-8674(89)90124-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Brierly I., Boursnell M.E., Binss M.M., Bilimoria B., Rolley N.J., Brown T.D., Inglis S.C. Products of the polymerase-encoding region of the coronavirus IBV. Adv. Exp. Med. Biol. 1990;276:275–281. doi: 10.1007/978-1-4684-5823-7_38. [DOI] [PubMed] [Google Scholar]
  31. Britton P. Coronavirus motif [letter] Nature (London) 1991;353:394. doi: 10.1038/353394a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Brown T.D.K., Brierly I. The coronavirus nonstructural proteins. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 191–218. [Google Scholar]
  33. Budzilowicz C.J., Weiss S.R. In vitro synthesis of two polypeptides from a nonstructural gene of coronavirus mouse hepatitis virus strain A59. Virology. 1987;157:509–515. doi: 10.1016/0042-6822(87)90293-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Budzilowicz C.J., Wilczynski S.P., Weiss S.R. Three intergenic regions of coronavirus mouse hepatitis virus strain A59 genome RNA contain a common nucleotide sequence that is homologous to the 3′-end of the viral mRNA leader sequence. J. Virol. 1985;53:834–840. doi: 10.1128/jvi.53.3.834-840.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Cabirac G.F., Soike K.F., Zhang J.Y., Hoel K., Butunoi C., Cai G.Y., Johnson S., Murray R.S. Entry of coronavirus into primate CNS following peripheral infection. Microb. Pathog. 1994;16:349–357. doi: 10.1006/mpat.1994.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Caul E.O., Egglestone S.I. Further studies on human enteric coronavirus. Arch. Virol. 1977;54:107–117. doi: 10.1007/BF01314383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Cavanagh D. Coronavirus IBV glycopolypeptides: Size of their polypeptide moieties and nature of their oligosaccharides. J. Gen. Virol. 1983;64:1187–1191. doi: 10.1099/0022-1317-64-5-1187. [DOI] [PubMed] [Google Scholar]
  38. Cavanagh D. Coronavirus IBV: Further evidence that the surface projections are associated with two glycopolypeptides. J. Gen. Virol. 1983;64:1787–1791. doi: 10.1099/0022-1317-64-8-1787. [DOI] [PubMed] [Google Scholar]
  39. Cavanagh D. Coronavirus IBV: Structural characterization of the spike protein. J. Gen. Virol. 1983;64:2577–2583. doi: 10.1099/0022-1317-64-12-2577. [DOI] [PubMed] [Google Scholar]
  40. Cavanagh D. The coronavirus surface glycoprotein. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 73–113. [Google Scholar]
  41. Cavanagh D., Davis P.J. Coronavirus IBV: Removal of spike glycopolypep-tide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells. J. Gen. Virol. 1986;67:1443–1448. doi: 10.1099/0022-1317-67-7-1443. [DOI] [PubMed] [Google Scholar]
  42. Cavanagh D., Davis P.J. Sequence analysis of strains of avian infectious bronchitis coronavirus isolated during the 1960s in the UK. Arch. Virol. 1992;130:471–472. doi: 10.1007/BF01309675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Cavanagh D., Macnaughton M. Coronaviruses. In: Zuckerman Bantvala A.J., E J., Pattison J.R., editors. “Principles and Practice of Clinical Virology”. Wiley; Chichester: 1995. pp. 325–336. [Google Scholar]
  44. Cavanagh D., Davis P.J., Pappin D.J., Binns M.M., Boursnell M.E., Brown T.D. Coronavirus IBV: Partial amino terminal sequencing of the spike poly-peptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41. Virus Res. 1986;4:133–143. doi: 10.1016/0168-1702(86)90037-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Cavanagh D., Davis P.J., Pappin D.J.C. Coronavirus IBV glycopolypep-tides: Locational studies using proteases and saponin, a membrane permeabilizer. Virus Res. 1986;4:145–156. doi: 10.1016/0168-1702(86)90038-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Cavanagh D., Davis P.J., Mockett A.P. Amino acids within hypervariable region 1 of avian coronarvirus IBV (Massachusetts serotype) spike glycoprotein are associated with neutralization epitopes. Virus Res. 1988;11:141–150. doi: 10.1016/0168-1702(88)90039-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Cavanagh D., Brian D.A., Enjuanes L., Holmes K.V., Lai M.M.C., Laude H., Siddell S.G., Spaan W., Taguchi F., Talbot P.J. Recommendations of the Coronavirus Study Group for the nomenclature of the structural proteins, mRNAs and genes of coronaviruses. Virology. 1990;176:306–307. doi: 10.1016/0042-6822(90)90259-T. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Cavanagh D., Brian D.A., Brinton M.A., Enjuanes L., Holmes K.V., Horzinek M.C., Lai M.M.C., Laude H., Plagemann P.G.W., Siddell S.G., Spaan W., Taguchi F., Talbot P.J. Revision of the taxonomy of the Coronavirus, Torovirus and Arterivirus genera. Arch. Virol. 1994;135:227–237. doi: 10.1007/BF01309782. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Cavanagh D., Brian D.A., Brinton M.A., Enjuanes L., Holmes K.V., Horzinek M.C., Lai M.M.C., Laude H., Plagemann P.G.W., Siddell S.G., Spaan W., Taguchi F., Talbot P.J. Coronaviridae. In: Murphy F.A., Fauquet C.M., LBishop D.H., Ghabrial S.A., Jarvis A.W., Martelli G.P., Mayo M.A., Summers M.D., editors. “Virus Taxonomy. Sixth Report of the International Committee on Taxonomy of Viruses”. Springer-Verlag; Vienna and New York: 1995. pp. 407–411. [Google Scholar]
  50. Chang R.Y., Brian D.A. Cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication. J. Virol. 1996;70:2201–2207. doi: 10.1128/jvi.70.4.2201-2207.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Chang R.Y., Hofman M.A., Sethna P.B., Brian D.A. A cis-acting function for the coronavirus leader in defective-interfering RNA replication. J. Virol. 1994;68:8223–8231. doi: 10.1128/jvi.68.12.8223-8231.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Chang R.Y., Krishnan R., Brian D.A. The UCUAAAC promoter motif is not required for high-frequency leader recombination in bovine coronavirus defective interfering RNA. J. Virol. 1996;70:2720–2729. doi: 10.1128/jvi.70.5.2720-2729.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Charley B., Laude H. Induction of alpha interferon by transmissible gastroenteritis coronavirus: Role of transmembrane glycoprotein E1. J. Virol. 1988;62:8–11. doi: 10.1128/jvi.62.1.8-11.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Chen B.Y., Itakura C. Cytopathology of chick renal epithelial cells experimentally infected with avian infectious bronchitis virus. Avian Pathol. 1996;25:675–690. doi: 10.1080/03079459608419174. [DOI] [PubMed] [Google Scholar]
  55. Chen D.S., Asanaka M., Yokomori K., Wang F.-L, Hwang S.B., Li H.-P., Lai M.M.C. A pregnancy-specific glycoprotein is expressed in the brain and serves as a receptor for mouse hepatitis virus. Proc. Natl. Acad. Sci. U.S.A. 1995;92:12095–12099. doi: 10.1073/pnas.92.26.12095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Chen D.S., Asanaka M., Chen F.S., Shively J.E., Lai M.M. Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors. J. Virol. 1997;71:1688–1691. doi: 10.1128/jvi.71.2.1688-1691.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Chen W., Baric R.S. Function of a 5′-end genomic RNA mutation that evolves during persistent mouse hepatitis virus infection in vitro. J. Virol. 1995;69:7529–7540. doi: 10.1128/jvi.69.12.7529-7540.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Chen W., Baric R.S. Molecular anatomy of mouse hepatitis virus persistence: Coevolution of increased host cell resistance and virus virulence. J. Virol. 1996;70:3947–3960. doi: 10.1128/jvi.70.6.3947-3960.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Collins A.R. Human coronavirus OC43 interacts with major histocompatibility complex class I molecules at the cell surface to establish infection. Immunol. Invest. 1994;23:313–321. doi: 10.3109/08820139409066826. [DOI] [PubMed] [Google Scholar]
  60. Collins A.R., Knobler R.L., Powell H., Buchmeier M.J. Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion. Virology. 1982;119:358–371. doi: 10.1016/0042-6822(82)90095-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Compton S.R. Enterotropic strains of mouse coronavirus differ in their use of murine carcinoembryonic antigen-related glycoprotein receptors. Virology. 1994;203:197–201. doi: 10.1006/viro.1994.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Compton S.R., Rogers D.B., Holmes K.V., Fertsch D., Remenick J., McGowan J.J. In vitro replication of mouse hepatitis virus strain A59. J. Virol. 1987;61:1814–1820. doi: 10.1128/jvi.61.6.1814-1820.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Cook J.K.A., Mockett A.P.A. Epidemiology of infectious bronchitis virus. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 317–336. [Google Scholar]
  64. Corapi W.V., Olsen C.W., Scott F.W. Monoclonal antibody analysis of neutralization and antibody-dependent enhancement of feline infectious peritonitis virus. J. Virol. 1992;66:6695–6705. doi: 10.1128/jvi.66.11.6695-6705.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Coutelier J.P., Godfraind C., Dveksler G.S., Wysocka M., Cardellichio C.B., Noel H., Holmes K.V. B lymphocyte and macrophage expression of carcinoembryonic antigen-related adhesion molecules that serve as receptors for murine corona-virus. Eur. J. Immunol. 1994;24:1383–1390. doi: 10.1002/eji.1830240622. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Cox E., Pensaert M.B., Callebaut P., van Deun K. Intestinal replication of a respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus. Vet. Microbiol. 1990;23:237–243. doi: 10.1016/0378-1135(90)90154-N. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Cox G.J., Parker M.D., Babiuk L.A. Bovine coronavirus nonstructural protein ns2 is a phosphoprotein. Virology. 1991;185:509–512. doi: 10.1016/0042-6822(91)90810-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Dackiw A.P.B., Zakrezewski K., Nathens A.B., Cheung P.Y.C., Fingerote R., Levy G.A., Rotstein O.D. Induction of macrophage procoagulant activity by murine hepatitis virus strain 3: Role of tyrosine phosphorylation. J. Virol. 1995;69:5824–5828. doi: 10.1128/jvi.69.9.5824-5828.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Dales S., Anderson R. Pathogenesis and diseases of the central nervous system caused by murine coronaviruses. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 257–292. [Google Scholar]
  70. Dalziel R.G., Lampert P.W., Talbot P.J., Buchmeier M.J. Site-specific alteration of murine hepatitis virus type-4 (MHV-4) peplomer glycoprotein E2 results in reduced neurovirulence. J. Virol. 1986;59:463–471. doi: 10.1128/jvi.59.2.463-471.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. David-Ferreira J.F., Manaker R.A. An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells. J. Cell Biol. 1965;24:57–78. doi: 10.1083/jcb.24.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Dea S., Tijssen P. Identification of the structural proteins of turkey enteric coronavirus. Arch. Virol. 1988;99:173–186. doi: 10.1007/BF01311068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. de Groot R.J., Luytjes W., Horzinek M.C., van der Zeijst B.A.M., Spaan W.J.M., Lenstra J.A. Evidence for a coiled-coil structure in the spike proteins of coronavirus. J. Mol. Biol. 1987;196:963–966. doi: 10.1016/0022-2836(87)90422-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. de Groot R.J., Van Leer R.W., Dalderup M.J., Vennema H., Horzinek M.C., Spaan W.J. Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice. Virology. 1989;171:493–502. doi: 10.1016/0042-6822(89)90619-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. de Groot R.J., Rumenapf T., Kuhn R.J., Strauss E.G., Strauss J.H. Sindbis virus RNA polymerase is degraded by the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 1991;88:8967–8971. doi: 10.1073/pnas.88.20.8967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. de Groot R.M., van der Most R.G., Spaan W.J. The fitness of defective interfering murine coronavirus DI-a and its derivatives is decreased by nonsense and frameshift mutations. J. Virol. 1992;66:5898–5905. doi: 10.1128/jvi.66.10.5898-5905.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Delmas B., Laude H. Assembly of coronavirus spike protein into trimers and its role in epitope expression. J. Virol. 1990;64:5367–5375. doi: 10.1128/jvi.64.11.5367-5375.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Delmas B., Gelfi J., Haridon R., Vogel L.K., Sjöstrom H., Noren O., Laude H. Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature (London) 1992;357:417–420. doi: 10.1038/357417a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Delmas B., Gelfi J., Kut E., Sjöstrom H., Noren O., Laude H. Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct from the enzymatic site. J. Virol. 1994;68:5216–5224. doi: 10.1128/jvi.68.8.5216-5224.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. den Boon J.A., Spaan W.J., Snijder E.J. Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies. Virology. 1995;213:364–372. doi: 10.1006/viro.1995.0009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Denison M.R., Perlman S. Translation and processing of mouse hepatitis virus virion RNA in a cell-free system. J. Virol. 1986;60:12–18. doi: 10.1128/jvi.60.1.12-18.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Denison M.R., Zoltick P.W., Hughes S.A., Giangreco B., Olson A.L., Perlman S., Leibowitz J.L., Weiss S.R. Intracellular processing of the N-terminal ORF la proteins of the coronavirus MHV-A59 requires multiple proteolytic events. Virology. 1992;189:274–284. doi: 10.1016/0042-6822(92)90703-R. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Denison M.R., Hughes S.R., Weiss S.R. Identification and characterization of a 65-kDa protein processed from the gene 1 polyprotein of the murine coronavirus MHV-A59. Virology. 1995;207:316–320. doi: 10.1006/viro.1995.1085. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Dennis D.E., Brian D.A. RNA-dependent RNA polymerase activity in coronavirus-infected cells. J. Virol. 1982;42:153–164. doi: 10.1128/jvi.42.1.153-164.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Deregt D., Babiuk L.A. Monoclonal antibodies to bovine coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins. Virology. 1987;161:410–420. doi: 10.1016/0042-6822(87)90134-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Deregt D., Gifford G.A., Khalid Ijaz M., Watts T.C., Gilchrist J.E., Haines D.M., Babiuk L.A. Monoclonal antibodies to bovine coronavirus glycoproteins E2 and E3: Demonstration of in vivo neutralizing activity. J. Gen. Virol. 1989;70:993–998. doi: 10.1099/0022-1317-70-4-993. [DOI] [PubMed] [Google Scholar]
  87. Dong S.H., Baker S.C. Determinants of the p28 cleavage site recognized by the first papain-like cysteine proteinase of murine coronavirus. Virology. 1994;204:541–549. doi: 10.1006/viro.1994.1567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Doughri A.M., Storz J., Hajer I., Fernando H.S. Morphology and morphogenesis of a coronavirus infecting intestinal epithelial cells of newborn calves. Exp. Mol. Pathol. 1976;25:355–370. doi: 10.1016/0014-4800(76)90045-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Duarte M., Tobler K., Bridgen A., Rasschaert D., Ackermann M., Laude H. Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF. Virology. 1994;198:466–476. doi: 10.1006/viro.1994.1058. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Dubois-Dalcq M.E., Doller E.W., Haspel M.V., Holmes K.V. Cell tropism and expression of mouse hepatitis viruses (MHV) in mouse spinal cord cultures. Virology. 1982;119:317–331. doi: 10.1016/0042-6822(82)90092-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Dupuy J.M., Lamontagne L. Genetically-determined sensitivity to MHV3 infections is expressed in vitro in lymphoid cells and macrophages. Adv. Exp. Med. Biol. 1987;218:455–463. doi: 10.1007/978-1-4684-1280-2_57. [DOI] [PubMed] [Google Scholar]
  92. Dveksler G.S., Pensiero M.N., Cardellichio C.B., Williams R.K., Jiang G., Holmes K.V., Dieffenbach C.W. Cloning of the mouse hepatitis virus (MHV) receptor: Expression in human and hamster cell lines confers susceptibility to MHV. J. Virol. 1991;65:6881–6891. doi: 10.1128/jvi.65.12.6881-6891.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. Dveksler G.S., Dieffenbach C.W., Cardellichio C.B., McCuaig K., Pensiero M.N., Jiang G., Beauchemin N., Holmes K.V. Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59. J. Virol. 1993;67:1–8. doi: 10.1128/jvi.67.1.1-8.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Dveksler G.S., Pensiero M.N., Dieffenbach C.W., Cardellichio C.B., Basile A.A., Elia P.E., Holmes K.V. Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor. Proc. Natl. Acad. Sci. USA. 1993;90:1716–1720. doi: 10.1073/pnas.90.5.1716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Dveksler G.S., Basile A.A., Cardellichio C.B., Holmes K.V. Mouse hepatitis virus receptor activities of an MHVR/mph chimera and MHVR mutants lacking N-linked glycosylation of the N-terminal domain. J. Virol. 1995;69:543–546. doi: 10.1128/jvi.69.1.543-546.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Ebner D., Raabe T., Siddell S.G. Identification of the coronavirus MHV-JHM mRNA 4 product. J. Gen. Virol. 1988;69:1041–1050. doi: 10.1099/0022-1317-69-5-1041. [DOI] [PubMed] [Google Scholar]
  97. Eleouet J.F., Rasschaert D., Lambert P., Levy L., Vende P., Laude H. Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus. Virology. 1995;206:817–822. doi: 10.1006/viro.1995.1004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Enjuanes L., van der Zeijst B.A.M. Molecular basis of transmissible gastroenteritis virus epidemiology. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 337–376. [Google Scholar]
  99. Evans M.R., Simpson R.W. The coronavirus avian infectious bronchitis virus requires the cell nucleus and hosttranscriptional factors. Virology. 1980;105:582–591. doi: 10.1016/0042-6822(80)90058-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  100. Fischer F., Peng D., Hingley S.T., Weiss S.R., Masters P.S. The internal open reading frame within the nucleocapsid gene of mouse hepatitis virus encodes a structural protein that is not essential for viral replication. J. Virol. 1997;71:996–1003. doi: 10.1128/jvi.71.2.996-1003.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  101. Fleming J.O., Trousdale M.D., El-Zaatari F.A.K., Stohlman S.A., Weiner L.P. Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies. J. Virol. 1986;58:869–875. doi: 10.1128/jvi.58.3.869-875.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Fleming J.O., Trousdale M.D., Bradbury J., Stohlman S.A., Weiner L.P. Experimental demyelination induced by coronavirus JHM (MHV-4): Molecular identification of a viral determinant of paralytic disease. Microb. Pathog. 1987;3:9–20. doi: 10.1016/0882-4010(87)90033-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Flintoff W.F. Replication of murine coronaviruses in somatic cell hybrids between murine fibroblasts and rat schwannoma cells. Virology. 1984;134:450–459. doi: 10.1016/0042-6822(84)90312-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Fosmire J.A., Hwang K., Makino S. Identification and characterization of a coronavirus packaging signal. J. Virol. 1992;66:3522–3530. doi: 10.1128/jvi.66.6.3522-3530.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Fraha M.F., Behnke J.N., Sturman L.S., Holmes K.V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion. J. Virol. 1985;56:912–920. doi: 10.1128/jvi.56.3.912-920.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Fu K., Baric R.S. Evidence for variable rates of recombination in the MHV genome. Virology. 1992;189:88–102. doi: 10.1016/0042-6822(92)90684-H. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Fu K., Baric R.S. Map locations of mouse hepatitis virus temperature-sensitive mutants: Confirmation of variable rates of recombination. J. Virol. 1994;68:7458–7466. doi: 10.1128/jvi.68.11.7458-7466.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Furuya T., Lai M.M.C. Three different cellular proteins bind to the complementary sites on the 5′-end positive-and 3′-end negative-strands of mouse hepatitis virus RNA. J. Virol. 1993;67:7215–7222. doi: 10.1128/jvi.67.12.7215-7222.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Furuya T., Macnaughton T.B., La Monica N., Lai M.M.C. Natural evolution of coronavirus defective-interfering RNA involves RNA recombination. Virology. 1993;194:408–413. doi: 10.1006/viro.1993.1277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Gagneten S., Gout O., Dubois-Dalcq M., Rottier P., Rossen J. Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein. J. Virol. 1995;69:889–895. doi: 10.1128/jvi.69.2.889-895.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Gallagher T.M. Murine coronavirus membrane fusion is blocked by modification of thiols buried within the spike protein. J. Virol. 1996;70:4683–4690. doi: 10.1128/jvi.70.7.4683-4690.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Gallagher T.M., Parker S.E., Buchmeier M.J. Neutralization-resistant variants of a neurotropic coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein. J. Virol. 1990;64:731–741. doi: 10.1128/jvi.64.2.731-741.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Gallagher T.M., Escarmis C., Buchmeier M.J. Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein. J. Virol. 1991;65:1916–1928. doi: 10.1128/jvi.65.4.1916-1928.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Gallagher T.M., Buchmeier M.J., Perlman S. Cell receptor-independent infection by a neurotropic murine coronavirus. Virology. 1992;191:517–522. doi: 10.1016/0042-6822(92)90223-C. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Garwes D.J., Pocock D.H. The polypeptide structure of transmissible gastroenteritis virus. J. Gen. Virol. 1975;29:25–34. doi: 10.1099/0022-1317-29-1-25. [DOI] [PubMed] [Google Scholar]
  116. Garwes D.J., Pocock D.H., Pike B.V. Isolation of subviral components from transmissible gastroenteritis virus. J. Gen. Virol. 1976;32:283–294. doi: 10.1099/0022-1317-32-2-283. [DOI] [PubMed] [Google Scholar]
  117. Garwes D.J., Stewart F., Britton P. The polypeptide of Mr 14,000 of porcine transmissible gastroenteritis virus: Gene assignment and intracellular location. J. Gen. Virol. 1989;70:2495–2499. doi: 10.1099/0022-1317-70-9-2495. [DOI] [PubMed] [Google Scholar]
  118. Godet M., Haridon R., Vautherot J.F., Laude H. TGEV coronavirus ORF4 encodes a membrane protein that is incorporated into virions. Virology. 1992;188:666–675. doi: 10.1016/0042-6822(92)90521-P. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Godet M., Grosclaude J., Delmas B., Laude H. Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein. J. Virol. 1994;68:8008–8016. doi: 10.1128/jvi.68.12.8008-8016.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Godfraind C., Langreth S.G., Cardellichio C.B., Knobler R., Coutelier J.P., Dubois-Dalcq M., Holmes K.V. Tissue and cellular distribution of an adhesion molecule in the carcinoembryonic antigen family that serves as a receptor for mouse hepatitis virus. Lab. Invest. 1995;73:615–627. [PubMed] [Google Scholar]
  121. Gombold J.L., Hingley S.T., Weiss S.R. Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal. J. Virol. 1993;67:4504–4512. doi: 10.1128/jvi.67.8.4504-4512.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. Gorbalenya A.E., Blinov V.M., Donchenko A.P., Koonin E.V. An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication. J. Mol. Evol. 1989;28:256–258. doi: 10.1007/BF02102483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Gorbalenya A.E., Koonin E.V., Donchencko A.P., Blinov V.M. Coronavirus genome: Prediction of putative functional domains in the nonstructural polyprotein by comparative amino acid sequence analysis. Nucleic Acids Res. 1989;17:4847–4861. doi: 10.1093/nar/17.12.4847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Gorbalenya A.E., Koonin E.V., Lai M.M.C. Putative papain-related thiol proteases of positive-strand RNA viruses. FEBS Lett. 1991;288:201–205. doi: 10.1016/0014-5793(91)81034-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Grosse B., Siddell S.G. Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody. Virology. 1994;202:814–824. doi: 10.1006/viro.1994.1403. [DOI] [PubMed] [Google Scholar]
  126. Grötzinger C., Heusipp G., Ziebuhr J., Harms U., Suss J., Siddell S.G. Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E. Virology. 1996;222:227–235. doi: 10.1006/viro.1996.0413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Haspel M.V., Lampert P.W., Oldstone M.B.A. Temperature-sensitive mutants of mouse hepatitis virus produce a high incidence of demyelination. Proc. Natl. Acad. Sci. U.S.A. 1978;75:4033–4036. doi: 10.1073/pnas.75.8.4033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  128. Herold J., Siddell S.G. An “elaborated” pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA. Nucleic Acids Res. 1993;21:5838–5842. doi: 10.1093/nar/21.25.5838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Herold J., Raabe T., Schelke-Prinz B., Siddell S.G. Nucleotide sequence of the human coronavirus 229E RNA polymerase locus. Virology. 1993;195:680–691. doi: 10.1006/viro.1993.1419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Hilton A., Mizzen L., MacIntyre G., Cheley S., Anderson R. Translational control in murine hepatitis virus infection. J. Gen. Virol. 1986;67:923–932. doi: 10.1099/0022-1317-67-5-923. [DOI] [PubMed] [Google Scholar]
  131. Hiscox J.A., Cavanagh D., Britton P. Quantification of individual subgenomic mRNA species during replication of the coronavirus transmissible gastroenteritis virus. Virus Res. 1995;36:119–130. doi: 10.1016/0168-1702(94)00108-O. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. Hiscox J.A., Mawditt K.L., Cavanagh D., Britton P. Investigation of the control of coronavirus subgenomic mRNA transcription by using T7-generated negative-sense RNA transcripts. J. Virol. 1995;69:6219–6227. doi: 10.1128/jvi.69.10.6219-6227.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Hodgman T.C. A new superfamily of replicative proteins [letter] Nature (London) 1988;333:22–23. doi: 10.1038/333022b0. (erratum published in Nature (London) 333, 1578(1988) [DOI] [PubMed] [Google Scholar]
  134. Hofmann M.A., Brian D.A. The 5′-end of coronavirus minus-strand RNAs contains a short poly(U) tract. J. Virol. 1991;65:6331–6333. doi: 10.1128/jvi.65.11.6331-6333.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Hofmann M.A., Sethna P.B., Brian D.A. Bovine coronavirus mRNA replication continues throughout persistent infection in cell culture. J. Virol. 1990;64:4108–4114. doi: 10.1128/jvi.64.9.4108-4114.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Hofmann M.A., Chang R.Y., Ku S., Brian D.A. Leader-mRNA junction sequences are unique for each subgenomic mRNA species in the bovine coronavirus and remain so throughout persistent infection. Virology. 1993;196:163–171. doi: 10.1006/viro.1993.1464. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Hofmann M.A., Senanayake S.D., Brian D.A. A translation-attenuating intraleader open reading frame is selected on coronavirus mRNAs during persistent infection. Proc. Natl. Acad. Sci. U.S.A. 1993;90:11733–11737. doi: 10.1073/pnas.90.24.11733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Hogue B.G., Brian D.A. Structural proteins of human respiratory coronavirus OC43. Virus Res. 1986;5:131–144. doi: 10.1016/0168-1702(86)90013-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  139. Hogue B.G., Kienzle T.E., Brian D.A. Synthesis and processing of the bovine enteric coronavirus hemagglutinin protein. J. Gen. Virol. 1989;70:345–352. doi: 10.1099/0022-1317-70-2-345. [DOI] [PubMed] [Google Scholar]
  140. Holmes K.V. Coronaviridae and their replication. In: Fields B.N., Knipe D.M., editors. “Fields Virology”. Raven Press; New York: 1990. pp. 841–856. [Google Scholar]
  141. Holmes K.V., Doller E.W., Sturman L.S. Tunicamycin-resistant glycosylation of coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein. Virology. 1981;115:334–344. doi: 10.1016/0042-6822(81)90115-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  142. Horsburgh B.C., Brierley I., Brown T.D. Analysis of a 9.6 kb sequence from the 3′ end of canine coronavirus genomic RNA. J. Gen. Virol. 1992;73:2849–2862. doi: 10.1099/0022-1317-73-11-2849. [DOI] [PubMed] [Google Scholar]
  143. Hughes S.A., Bonilla P.J., Weiss S.R. Identification of the murine coronavirus p28 cleavage site. J. Virol. 1995;69:809–813. doi: 10.1128/jvi.69.2.809-813.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Ignjatovic J., Galli L. The S1 glycoprotein but not the N or M proteins of avian infectious bronchitis virus induces protection in vaccinated chickens. Arch. Virol. 1994;138:117–134. doi: 10.1007/BF01310043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  145. Jacobs L., Spaan W.J., Horzinek M.C., van der Zeijst B.A. Synthesis of subgenomic mRNA's of mouse hepatitis virus is initiated independently: Evidence from UV transcription mapping. J. Virol. 1981;39:401–406. doi: 10.1128/jvi.39.2.401-406.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Jeong Y.S., Makino S. Mechanism of coronavirus transcription: Duration of primary transcription initiation activity and effects of subgenomic RNA transcription on RNA replication. J. Virol. 1992;66:3339–3346. doi: 10.1128/jvi.66.6.3339-3346.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Jeong Y.S., Makino S. Evidence for coronavirus discontinuous transcription. J. Virol. 1994;68:2615–2623. doi: 10.1128/jvi.68.4.2615-2623.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Jeong Y.S., Repass J.F., Kim Y.N., Hwang S.M., Makino S. Coronavirus transcription mediated by sequences flanking the transcription consensus sequence. Virology. 1996;217:311–322. doi: 10.1006/viro.1996.0118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Jia W., Karaca K., Parrish C.R., Naqi S.A. A novel variant of avian infectious bronchitis virus resulting from recombination among three different strains. Arch. Virol. 1995;140:259–271. doi: 10.1007/BF01309861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Joo M., Makino S. Mutagenic analysis of the coronavirus intergenic consensus sequence. J. Virol. 1992;66:6330–6337. doi: 10.1128/jvi.66.11.6330-6337.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Joo M., Makino S. The effect of two closely inserted transcription consensus sequences on coronavirus transcription. J. Virol. 1995;69:272–280. doi: 10.1128/jvi.69.1.272-280.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  152. Kapke P.A., Tung F.Y.T., Hogue B.G., Brian D.A., Woods R.D., Wesley R. The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation. Virology. 1988;165:367–376. doi: 10.1016/0042-6822(88)90581-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. Keck J.G., Stohlman S.A., Soe L.H., Makino S., Lai M.M.C. Multiple recombination sites at the 5′-end of murine coronavirus RNA. Virology. 1987;156:331–341. doi: 10.1016/0042-6822(87)90413-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Keck J.G., Hogue B.G., Brian D.A., Lai M.M.C. Temporal regulation of bovine coronavirus RNA synthesis. Virus Res. 1988;9:343–356. doi: 10.1016/0168-1702(88)90093-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Keck J.G., Matsushima G.K., Makino S., Fleming J.O., Vannier D.M., Stohlman S.A., Lai M.M.C. In vivo RNA-RNA recombination of coronavirus in mouse brain. J. Virol. 1988;62:1810–1813. doi: 10.1128/jvi.62.5.1810-1813.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Keck J.G., Soe L.H., Makino S., Stohlman S.A., Lai M.M.C. RNA recombination of murine coronaviruses: Recombination between fusion-positive MHV-A59 and fusion-negative MHV-2. J. Virol. 1988;62:1989–1998. doi: 10.1128/jvi.62.6.1989-1998.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Kennedy D.A., Johnson-Lussenberg C.M. Inhibition of coronavirus 229E replication by actinomycin D. J. Virol. 1978;29:401–404. doi: 10.1128/jvi.29.1.401-404.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Kienzle T.E., Abraham S., Hogue B.G., Brian D.A. Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein. J. Virol. 1990;64:1834–1838. doi: 10.1128/jvi.64.4.1834-1838.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Kim J.C., Spence R.A., Currier P.F., Lu X.T., Denison M.R. Coronavirus protein processing and RNA synthesis is inhibited by the cysteine proteinase inhibitor E64d. Virology. 1995;208:1–8. doi: 10.1006/viro.1995.1123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Kim K.H., Makino S. Two murine coronavirus genes suffice for viral RNA synthesis. J. Virol. 1995;69:2313–2321. doi: 10.1128/jvi.69.4.2313-2321.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Kim Y.N., Makino S. Characterization of a murine coronavirus defective interfering RNA internal cis-acting replication signal. J. Virol. 1995;69:4963–4971. doi: 10.1128/jvi.69.8.4963-4971.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. Kim Y.-N., Lai M.M.C., Makino S. Generation and selection of coronavirus defective interfering RNA with large open reading frame by RNA recombination and possible editing. Virology. 1993;194:244–253. doi: 10.1006/viro.1993.1255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. Kim Y.-N., Jeong Y.S., Makino S. Analysis of cis-acting sequences essential for coronavirus defective interfering RNA replication. Virology. 1993;197:53–63. doi: 10.1006/viro.1993.1566. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. King B., Potts B.J., Brian D.A. Bovine coronavirus hemagglutinin protein. Virus Res. 1985;2:53–59. doi: 10.1016/0168-1702(85)90059-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. King D.J., Cavanagh D. Infectious bronchitis. In: Calnek B.W., Barnes H.J., Beard C.W., Reid W.M., Yoder H.W., editors. “Diseases of Poultry”. Iowa State University Press; Ames: 1991. pp. 471–484. [Google Scholar]
  166. Klumperman J., Locker J.K., Meijer A., Horzinek M.C., Geuze H.J., Rottier P.J. Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding. J. Virol. 1994;68:6523–6534. doi: 10.1128/jvi.68.10.6523-6534.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  167. Knobler R.L., Taylor B.A., Wooddell M.K., Beamer W.G., Oldstone M.B.A. Host genetic control of mouse hepatitis virus type-4 (JHM strain) replication. II. The gene locus for susceptibility is linked to the Svp-2 locus on mouse chromosome 7. Exp. Clin. Immunogenet. 1984;1:217–222. [PubMed] [Google Scholar]
  168. Koetzner C.A., Parker M.M., Ricard C.S., Sturman L.S., Masters P.S. Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination. J. Virol. 1992;66:1841–1848. doi: 10.1128/jvi.66.4.1841-1848.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  169. Konings D.A.M., Bredenbeek P.J., Noten J.F.H., Hogeweg P., Spaan W.J.M. Differential premature termination of transcription as a proposed mechanism for the regulation of coronavirus gene expression. Nucleic Acids Res. 1988;16:10849–10860. doi: 10.1093/nar/16.22.10849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  170. Kooi C., Mizzen L., Alderson C., Daya M., Anderson R. Early events of importance in determining host cell permissiveness to mouse hepatitis virus infection. J. Gen. Virol. 1988;69:1125–1135. doi: 10.1099/0022-1317-69-6-1125. [DOI] [PubMed] [Google Scholar]
  171. Kooi C., Cervin M., Anderson R. Differentiation of acid-pH-dependent and -nondependent entry pathways for mouse hepatitis virus. Virology. 1991;180:108–119. doi: 10.1016/0042-6822(91)90014-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  172. Koolen M.J., Osterhaus A.D.M.E., van Steenis G., Horzinek M.C., van der Zeijst B.A.M. Temperature-sensitive mutants of mouse hepatitis virus strain A59: Isolation, characterization and neuropathogenic properties. Virology. 1983;125:393–402. doi: 10.1016/0042-6822(83)90211-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Koopmans M., Horzinek M.C. Toroviruses of animals and humans: A review. Adv. Virus Res. 1994;43:233–273. doi: 10.1016/S0065-3527(08)60050-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. Kotier S.A., Cavanagh D., Britton P. Experimental evidence of recombination in coronavirus infectious bronchitis virus. Virology. 1995;213:569–580. doi: 10.1006/viro.1995.0029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  175. Krijnse-Locker J., Ericsson M., Rottier P.J.M., Griffiths G. Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol. 1994;124:55–70. doi: 10.1083/jcb.124.1.55. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Krishnan R., Chang R.Y., Brian D.A. Tandem placement of a coronavirus promoter results in enhanced mRNA synthesis from the downstream-most initiation site. Virology. 1996;218:400–405. doi: 10.1006/viro.1996.0210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  177. Krzystyniak K., Dupuy J.M. Early interaction between mouse hepatitis virus 3 and cells. J. Gen. Virol. 1981;57:53–61. doi: 10.1099/0022-1317-57-1-53. [DOI] [PubMed] [Google Scholar]
  178. Krzystyniak K., Dupuy J.M. Entry of mouse hepatitis virus 3 into cells. J. Gen. Virol. 1984;65:227–231. doi: 10.1099/0022-1317-65-1-227. [DOI] [PubMed] [Google Scholar]
  179. Kubo H., Yamada Y.K., Taguchi F. Localization of neutralizing epitopes and the receptor-binding site within the ammo-terminal 330 amino acids of the murine coronavirus spike protein. J. Virol. 1994;68:5403–5410. doi: 10.1128/jvi.68.9.5403-5410.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  180. Kunkel F., Herrler G. Structural and functional analysis of the surface protein of human coronavirus OC43. Virology. 1993;195:195–202. doi: 10.1006/viro.1993.1360. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Kusters J.G., Niesters H.G.M., Lenstra J.A., Horzinek M.C., van der zeijst B.A.M. Phylogeny of antigenic variants of avian coronavirus IBV. Virology. 1989;169:217–221. doi: 10.1016/0042-6822(89)90058-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  182. Labonte P., Mounir S., Talbot P.J. Sequence and expression of the ns2 protein gene of human coronavirus OC43. J. Gen. Virol. 1995;76:431–435. doi: 10.1099/0022-1317-76-2-431. [DOI] [PubMed] [Google Scholar]
  183. Lai M.M.C. Coronavirus leader RNA-primed transcription: An alternative mechanism to RNA splicing. BioEssays. 1986;5:257–260. doi: 10.1002/bies.950050606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  184. Lai M.M.C. Coronavirus: Organization, replication and expression of genome. Annu. Rev. Microbiol. 1990;44:303–333. doi: 10.1146/annurev.mi.44.100190.001511. [DOI] [PubMed] [Google Scholar]
  185. Lai M.M.C. RNA recombination in animal and plant viruses. Microbiol. Rev. 1992;56:61–79. doi: 10.1128/mr.56.1.61-79.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  186. Lai M.M.C., Brayton P.R., Armen R.C., Patton C.D., Pugh C., Stohlman S.A. Mouse hepatitis virus A59: Messenger RNA structure and genetic localization of the sequence divergence from the hepatotropic strain MHV 3. J. Virol. 1981;39:823–834. doi: 10.1128/jvi.39.3.823-834.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  187. Lai M.M.C., Patton C.D., Stohlman S.A. Further characterization of mRNAs of mouse hepatitis virus: Presence of common 5′-end nucleotides. J. Virol. 1982;41:557–656. doi: 10.1128/jvi.41.2.557-565.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  188. Lai M.M.C., Patton C.D., Baric R.S., Stohlman S.A. The presence of leader sequences in the mRNA of mouse hepatitis virus. J. Virol. 1983;46:1027–1033. doi: 10.1128/jvi.46.3.1027-1033.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  189. Lai M.M.C., Baric R.S., Brayton P.R., Stohlman S.A. Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus-a cytoplasmic RNA virus. Proc. Natl. Acad. Sci. U.S.A. 1984;81:3626–3630. doi: 10.1073/pnas.81.12.3626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  190. Lai M.M.C., Baric R.S., Makino S., Keck J.G., Egbert J., Leibowitz J.L., Stohlman S.A. Recombination between nonsegmented RNA genomes of mu-rine coronaviruses. J. Virol. 1985;56:449–456. doi: 10.1128/jvi.56.2.449-456.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  191. Lai M.M.C., Makino S., Soe L.H., Shieh C.-K., Keck J.G., Fleming J.O. Coronavirus: A jumping RNA transcription. Cold Spring Harbor Lab. Symp. 1987;52:359–365. doi: 10.1101/sqb.1987.052.01.041. [DOI] [PubMed] [Google Scholar]
  192. Lai M.M.C., Liao C.-L., Lin Y.-J., Zhang X. Coronavirus: How a large RNA viral genome is replicated and transcribed. Infect. Agents Dis. 1994;3:98–105. [PubMed] [Google Scholar]
  193. La Monica N., Banner L.R., Morris V.L., Lai M.M.C. Localization of extensive deletions in the structural genes of two neurotropic variants of murine coronavirus JHM. Virology. 1991;182:883–888. doi: 10.1016/0042-6822(91)90635-O. [DOI] [PMC free article] [PubMed] [Google Scholar]
  194. La Monica N., Yokomori K., Lai M.M.C. Coronavirus mRNA synthesis: Identification of novel transcription initiation signals which are differentially regulated by different leader sequences. Virology. 1992;188:402–407. doi: 10.1016/0042-6822(92)90774-J. [DOI] [PMC free article] [PubMed] [Google Scholar]
  195. Lapps W., Hogue B.G., Brian D.A. Sequence analysis of the bovine coronavirus nucleocapsid and matrix protein genes. Virology. 1987;157:47–57. doi: 10.1016/0042-6822(87)90312-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  196. Laude H. Porcine respiratory coronavirus: Molecular features and virus-host interactions. Vet. Res. 1993;24:125–150. [PubMed] [Google Scholar]
  197. Laude H., Masters P.S. The coronavirus nucleocapsid protein. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 141–158. [Google Scholar]
  198. Laude H., Rasschaert D., Huet J.C. Sequence and N-terminal processing of the transmembrane protein E1 of the coronavirus transmissible gastrenteritis virus. J. Gen. Virol. 1987;68:1687–1693. doi: 10.1099/0022-1317-68-6-1687. [DOI] [PubMed] [Google Scholar]
  199. Laude H., Gelfi J., Lavenant L., Charley B. Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus. J. Virol. 1992;66:743–749. doi: 10.1128/jvi.66.2.743-749.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Laviada M.D., Videgain S.P., Moreno L., Alonso F., Enjuanes L., Escribano J.M. Expression of swine transmissible gastroenteritis virus envelope antigens on the surface of infected cells: Epitopes externally exposed. Virus Res. 1990;16:247–254. doi: 10.1016/0168-1702(90)90051-C. [DOI] [PMC free article] [PubMed] [Google Scholar]
  201. Le S.Y., Sonenberg N., Maizel J.V.J. Distinct structural elements and internal entry of ribosomes in mRNA3 encoded by infectious bronchitis virus. Virology. 1994;198:405–411. doi: 10.1006/viro.1994.1051. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Lee H.-J., Shieh C.-K., Gorbalenya A.E., Koonin E.V., La Monica N., Tuler J., Bagdzyahdzhyan A., Lai M.M.C. The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase. Virology. 1991;180:567–582. doi: 10.1016/0042-6822(91)90071-I. [DOI] [PMC free article] [PubMed] [Google Scholar]
  203. Leibowitz J.L., DeVries J.R. Synthesis of virus-specific RNA in permeabilized murine coronavirus-infected cells. Virology. 1988;166:66–75. doi: 10.1016/0042-6822(88)90147-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  204. Leibowitz J.L., Wilhelmsen K.C., Bond C.W. The virus specific intracellular RNA species of two murine coronaviruses: MHV A59 and MHV-JHM. Virology. 1981;114:39–51. doi: 10.1016/0042-6822(81)90250-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  205. Leibowitz J.L., DeVries J.R., Haspel M.V. Genetic analysis of murine hepatitis virus strain JHM. J. Virol. 1982;42:1080–1087. doi: 10.1128/jvi.42.3.1080-1087.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  206. Leibowitz J.L., Weiss S.R., Paavola E., Bond C.W. Cell-free translation of murine coronavirus RNA. J. Virol. 1982;43:905–913. doi: 10.1128/jvi.43.3.905-913.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. Leibowitz J.L., Perlman S., Weinstock G., DeVries J.R., Budzilowicz C., Weissemann J.M., Weiss S.R. Detection of a murine coronavirus nonstructural protein encoded in a downstream open reading frame. Virology. 1988;164:156–164. doi: 10.1016/0042-6822(88)90631-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Lewis E.L., Harbour D.A., Beringer J.E., Grinsted J. Differential in vitro inhibition of feline enteric coronavirus and feline infectious peritonitis virus by actinomycin D. J. Gen. Virol. 1993;73:3285–3288. doi: 10.1099/0022-1317-73-12-3285. [DOI] [PubMed] [Google Scholar]
  209. Li D., Cavanagh D. Coronavirus IBV-induced membrane fusion occurs at near-neutral pH. Arch. Virol. 1992;122:307–316. doi: 10.1007/BF01317192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  210. Liao C.-L., Lai M.M.C. RNA recombination in a coronavirus: Recombination between viral genomic RNA and transfected RNA fragments. J. Virol. 1992;66:6117–6124. doi: 10.1128/jvi.66.10.6117-6124.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  211. Liao C.-L., Lai M.M.C. Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription. J. Virol. 1994;68:4727–4737. doi: 10.1128/jvi.68.8.4727-4737.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  212. Liao C.L., Lai M.M.C. A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA. Virology. 1995;209:428–436. doi: 10.1006/viro.1995.1275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  213. Liao C.L., Zhang X., Lai M.M.C. Coronavirus defective-interfering RNA as an expression vector: The generation of a pseudorecombinant mouse hepatitis virus expressing hemagglutinin-esterase. Virology. 1995;208:319–327. doi: 10.1006/viro.1995.1155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Lin Y.-J., Lai M.M.C. Deletion mapping of a mouse hepatitis virus defective-interfering RNA reveals the requirement of an internal and discontiguous sequence for replication. J. Virol. 1993;67:6110–6118. doi: 10.1128/jvi.67.10.6110-6118.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  215. Lin Y.-J., Liao C.L., Lai M.M.C. Identification of the cis-acting signal for minus-strand RNA synthesis of a murine coronavirus: Implications for the role of minus-strand RNA in RNA replication and transcription. J. Virol. 1994;68:8131–8140. doi: 10.1128/jvi.68.12.8131-8140.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  216. Lin Y.-J., Zhang X., Wu R.-C., Lai M.M.C. The 3′ untranslated region of the coronaviral RNA is required for subgenomic mRNA transcription from a defective-interfering RNA. J. Virol. 1996;70:7236–7240. doi: 10.1128/jvi.70.10.7236-7240.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. Liu D.X., Brown T.D.K. Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein. Virology. 1995;209:420–427. doi: 10.1006/viro.1995.1274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. Liu D.X., Inglis S.C. Identification of two new polypeptides encoded by mRNA5 of the coronavirus infectious bronchitis virus. Virology. 1992;186:342–347. doi: 10.1016/0042-6822(92)90094-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Liu D.X., Inglis S.C. Internal entry of ribosomes on a tricistronic mRNA encoded by infectious bronchitis virus. J. Virol. 1992;66:6143–6154. doi: 10.1128/jvi.66.10.6143-6154.1992. erratum published in J. Virol. 66, 6840(1992) [DOI] [PMC free article] [PubMed] [Google Scholar]
  220. Liu D.X., Cavanagh D., Green P., Inglis S.C. A polycistronic mRNA specified by the coronavirus infectious bronchitis virus. Virology. 1991;184:531–544. doi: 10.1016/0042-6822(91)90423-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  221. Liu D.X., Brierley I., Tibbies K.W., Brown T.D.K. A 100-kilodalton polypeptide encoded by open reading frame (ORF) 1b of the coronavirus infectious bronchitis virus is processed by ORF 1a products. J. Virol. 1994;68:5772–5780. doi: 10.1128/jvi.68.9.5772-5780.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  222. Locker J.K., Griffiths G., Horzinek M.C., Rottier P.J.M. O-glycosylation of the coronavirus M protein. Differential localization of sialyltransferases in N-and O-linked glycosylation. J. Biol. Chem. 1992;267:14094–14101. doi: 10.1016/S0021-9258(19)49683-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  223. Locker J.K., Rose J.K., Horzinek M.C., Rottier P.J.M. Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation. J. Biol. Chem. 1992;267:21911–21918. doi: 10.1016/S0021-9258(19)36699-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  224. Locker J.K., Klumperman J., Oorschot V., Horzinek M.C., Geuze H.J., Rottier P.J. The cytoplasmic tail of mouse hepatitis virus M protein is essential but not sufficient for its retention in the Golgi complex. J. Biol. Chem. 1994;269:28263–28269. [PubMed] [Google Scholar]
  225. Locker J.K., Opstelten D.J.E., Ericsson M., Horzinek M.C., Rottier P.J.M. Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention. J. Biol. Chem. 1995;270:8815–8821. doi: 10.1074/jbc.270.15.8815. [DOI] [PubMed] [Google Scholar]
  226. Lu X.T., Lu Y.Q., Denison M.R. Intracellular and in vitro-translated 27-kDa proteins contain the 3C-like proteinase activity of the coronavirus MHV-A59. Virology. 1996;222:375–382. doi: 10.1006/viro.1996.0434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  227. Lu Y.Q., Lu X.T., Denison M.R. Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59. J. Virol. 1995;69:3554–3559. doi: 10.1128/jvi.69.6.3554-3559.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  228. Luytjes W., Sturman L.S., Bredenbeek P.J., Charite J., van der Zeijst B.A.M., Horzinek M.C., Spaan W.J.M. Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site. Virology. 1987;161:479–487. doi: 10.1016/0042-6822(87)90142-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Luytjes W., Bredenbeek P.J., Noten A.F.H., Horzinek M.C., Spaan W.J.M. Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA-recombination between coronavirus and influenza C virus. Virology. 1988;166:415–422. doi: 10.1016/0042-6822(88)90512-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  230. Luytjes W., Geerts D., Posthumus W., Meloen R., Spaan W. Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses. J. Virol. 1989;63:1408–1412. doi: 10.1128/jvi.63.3.1408-1412.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  231. Luytjes W., Gerritsma H., Spaan W.J.M. Replication of synthetic defective interfering RNAs derived from coronavirus mouse hepatitis virus-A59. Virology. 1996;216:174–183. doi: 10.1006/viro.1996.0044. [DOI] [PMC free article] [PubMed] [Google Scholar]
  232. Luytjes W., Gerritsma H., Bos E., Spaan W. Characterization of two temperature-sensitive mutants of coronavirus mouse hepatitis virus strain A59 with maturation defects in the spike protein. J. Virol. 1997;71:949–955. doi: 10.1128/jvi.71.2.949-955.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  233. Machamer C.E., Rose J.K. A specific transmembrane domain of a coronavirus E1 glycoprotein is required for its retention in the Golgi region. J. Cell Biol. 1987;105:1205–1214. doi: 10.1083/jcb.105.3.1205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. Machamer C.E., Mentone S.A., Rose J.K., Farquhar M.G. The E1 glycoprotein of an avian coronavirus is targeted to the cis Golgi complex. Proc. Natl. Acad. Sci. U.S.A. 1990;87:6944–6948. doi: 10.1073/pnas.87.18.6944. [DOI] [PMC free article] [PubMed] [Google Scholar]
  235. Machamer C.E., Grim M.G., Esquela A., Chung S.W., Rolls M., Ryan K., Swift A.M. Retention of a cis Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain. Mol. Biol. Cell. 1993;4:695–704. doi: 10.1091/mbc.4.7.695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  236. Macnaughton M.R., Davies H.A. Two particle types of avian infectious bronchitis virus. J. Gen. Virol. 1980;47:365–372. doi: 10.1099/0022-1317-47-2-365. [DOI] [PubMed] [Google Scholar]
  237. Macnaughton M.R., Davies H.A., Nermut M.V. Ribonucleoprotein-like structures from coronavirus particles. J. Gen. Virol. 1978;39:545–549. doi: 10.1099/0022-1317-39-3-545. [DOI] [PubMed] [Google Scholar]
  238. Mahy B.W., Siddell S., Wege H., Meulen V. RNA-dependent RNA polymerase activity in murine coronavirus-infected cells. J. Gen. Virol. 1983;64:103–111. doi: 10.1099/0022-1317-64-1-103. [DOI] [PubMed] [Google Scholar]
  239. Makino S., Joo M. Effect of intergenic consensus sequence flanking sequences on coronavirus transcription. J. Virol. 1993;67:3304–3311. doi: 10.1128/jvi.67.6.3304-3311.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  240. Makino S., Lai M.M.C. Evolution of the 5′-end of genomic RNA of murine coronaviruses during passages in vitro. Virology. 1989;169:227–232. doi: 10.1016/0042-6822(89)90060-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  241. Makino S., Lai M.M.C. High-frequency leader sequence switching during coronavirus defective interfering RNA replication. J. Virol. 1989;63:5285–5292. doi: 10.1128/jvi.63.12.5285-5292.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  242. Makino S., Fujioka N., Fujiwara K. Structure of the intracellular defective viral RNAs of defective interfering particles of mouse hepatitis virus. J. Virol. 1985;54:329–336. doi: 10.1128/jvi.54.2.329-336.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  243. Makino S., Keck J.G., Stohlman S.A., Lai M.M.C. High-frequency RNA recombination of murine coronaviruses. J. Virol. 1986;57:729–737. doi: 10.1128/jvi.57.3.729-737.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  244. Makino S., Stohlman S.A., Lai M.M.C. Leader sequences of murine coronavirus mRNAs can be freely reasserted: Evidence for the role of free leader RNA in transcription. Proc. Natl. Acad. Sci. U.S.A. 1986;83:4204–4208. doi: 10.1073/pnas.83.12.4204. [DOI] [PMC free article] [PubMed] [Google Scholar]
  245. Makino S., Fleming J.O., Keck J.G., Stohlman S.A., Lai M.M.C. RNA recombination of coronaviruses: Localization of neutralizing epitopes and neuropatho-genic determinants on the carboxyl terminus of peplomers. Proc. Natl. Acad. Sci. U.S.A. 1987;84:6567–6571. doi: 10.1073/pnas.84.18.6567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  246. Makino S., Shieh C.-K., Keck J.G., Lai M.M.C. Defective interfering particles of murine coronavirus: Mechanism of synthesis of defective viral RNAs. Virology. 1988;163:104–111. doi: 10.1016/0042-6822(88)90237-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  247. Makino S., Shieh C.-K., Soe L.H., Baker S.C., Lai M.M.C. Primary structure and translation of a defective-interfering RNA of murine coronavirus. Virology. 1988;166:550–560. doi: 10.1016/0042-6822(88)90526-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  248. Makino S., Soe L.H., Shieh C.-K., Lai M.M.C. Discontinuous transcription generates heterogeneity at the leader fusion sites of coronavirus mRNAs. J. Virol. 1988;62:3870–3873. doi: 10.1128/jvi.62.10.3870-3873.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  249. Makino S., Yokomori K., Lai M.M.C. Analysis of efficiently packaged defective-interfering RNAs of murine coronavirus: Localization of a possible RNA-packaging signal. J. Virol. 1990;64:6045–6053. doi: 10.1128/jvi.64.12.6045-6053.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  250. Makino S., Joo M., Makino J.K. A system for study of coronavirus mRNA synthesis: A regulated, expressed subgenomic defective-interfering RNA results from intergenic site insertion. J. Virol. 1991;65:6031–6041. doi: 10.1128/jvi.65.11.6031-6041.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  251. Masters P.S. Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus. Arch. Virol. 1992;125:141–160. doi: 10.1007/BF01309634. [DOI] [PMC free article] [PubMed] [Google Scholar]
  252. Masters P.S., Koetzner C.A., Kerr C.A., Heo Y. Optimization of targeted RNA recombination and mapping of a novel nucleocapsid gene mutation in the corona-virus mouse hepatitis virus. J. Virol. 1994;68:328–337. doi: 10.1128/jvi.68.1.328-337.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  253. Mayer T., Tamura T., Falk M., Niemann H. Membrane integration and intracellular transport of the coronavirus glycoprotein E1, a class III membrane glyco-protein. J. Biol. Chem. 1988;263:14956–14963. doi: 10.1016/S0021-9258(18)68131-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  254. Mendez A., Smerdou C., Izeta A., Gebauer F., Enjuanes L. Molecular characterization of transmissible gastroenteritis coronavirus defective interfering genomes: Packaging and heterogeneity. Virology. 1996;217:495–507. doi: 10.1006/viro.1996.0144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  255. Mizzen L., Hilton A., Cheley S., Anderson R. Attenuation of murine corona-virus infection by ammonium chloride. Virology. 1985;142:378–388. doi: 10.1016/0042-6822(85)90345-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  256. Mohandas D.V., Dales S. Endosomal association of a protein phosphatase with high dephosphorylating activity against a coronavirus nucleocapsid protein. FEBS Lett. 1991;282:419–424. doi: 10.1016/0014-5793(91)80528-B. [DOI] [PMC free article] [PubMed] [Google Scholar]
  257. Mounir S., Talbot P.J. Human coronavirus OC43 RNA 4 lacks two open reading frames located downstream of the S gene of bovine coronavirus. Virology. 1993;192:355–360. doi: 10.1006/viro.1993.1043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  258. Murray R.S., Cai G., Hoel K., Zhang J., Soike K.F., Cabirac G.F. Coronavirus infects and causes demyelination in primate central nervous system. Virology. 1992;188:274–284. doi: 10.1016/0042-6822(92)90757-G. [DOI] [PMC free article] [PubMed] [Google Scholar]
  259. Nakada S., Creager R.S., Krystal M., Aaronson R.P., Palese P. Influenza C virus hemagglutinin: Comparison with influenza A and B virus hemagglutinins. J. Virol. 1984;50:118. doi: 10.1128/jvi.50.1.118-124.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  260. Nedellec P., Dveksler G.S., Daniels E., Turbide C., Chow B., Basile A.A., Holmes K.V., Beauchemin N. Bgp2, a new member of the carcinoembryonic antigen-related gene family, encodes an alternative receptor for mouse hepatitis virus. J. Virol. 1994;68:4525–4537. doi: 10.1128/jvi.68.7.4525-4537.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  261. Nelson G.W., Stohlman S.A. Localization of the RNA-binding domain of MHV nucleocapsid protein. J. Gen. Virol. 1993;74:1975–1979. doi: 10.1099/0022-1317-74-9-1975. [DOI] [PubMed] [Google Scholar]
  262. Niemann H., Boschek B., Evans D., Rosing M., Tamura T., Klenk H.D. Post-translational glycosylation of coronavirus glycoprotein E1: Inhibition by monensin. EMBO J. 1982;1:1499–1504. doi: 10.1002/j.1460-2075.1982.tb01346.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  263. Niemann H., Geyer R., Klenk H.D., Under D., Stirm S., Wirth M. The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein E1. EMBO J. 1984;3:665–670. doi: 10.1002/j.1460-2075.1984.tb01864.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  264. Oberst M.D., Gollan T.J., Gupta M., Peura S.R., Zydlewski J.D., Sudarsanan P., Lawson T.G. The encephalomyocarditis virus 3C protease is rapidly degraded by an ATP-dependent proteolytic system in reticulocyte lysate. Virology. 1993;193:28–40. doi: 10.1006/viro.1993.1100. [DOI] [PubMed] [Google Scholar]
  265. Oleszak E.L., Leibowitz J.L. Immunoglobulin Fc binding activity is associated with the mouse hepatitis virus E2 peplomer protein. Virology. 1990;176:70–80. doi: 10.1016/0042-6822(90)90231-F. [DOI] [PMC free article] [PubMed] [Google Scholar]
  266. Oleszak E.L., Perlman S., Leibowitz J.L. MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity. Virology. 1992;186:122–132. doi: 10.1016/0042-6822(92)90066-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  267. Oleszak E.L., Kuzmak J., Hogue B., Parr R., Collisson E.W., Rodkey L.S., Leibowitz J.L. Molecular mimicry between Fc receptor and S peplomer protein of mouse hepatitis virus, bovine coronavirus, and transmissible gastroenteritis virus. Hybridoma. 1995;14:1–8. doi: 10.1089/hyb.1995.14.1. [DOI] [PubMed] [Google Scholar]
  268. Olsen C.W., Corapi W.V., Ngichabe C.K., Baines J.D., Scott F.W. Monoclonal antibodies to the spike protein of feline infectious peritonitis virus mediate antibody-dependent enhancement of infection of feline macrophages. J. Virol. 1992;66:956–965. doi: 10.1128/jvi.66.2.956-965.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  269. Opstelten D.J.E., de Groote P., Horzinek M.C., Vennema H., Rottier P.J.M. Bisulfide bonds in folding and transport of mouse hepatitis coronavirus glyco-proteins. J. Virol. 1993;67:7394–7401. doi: 10.1128/jvi.67.12.7394-7401.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  270. Opstelten D.J.E., Raamsman M.J., Wolfs K., Horzinek M.C., Rottier P.J.M. Envelope glycoprotein interactions in coronavirus assembly. J. Cell Biol. 1995;131:339–349. doi: 10.1083/jcb.131.2.339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  271. Parker M.D., Cox G.J., Deregt D., Fitzpatrick D.R., Babiuk L.A. Cloning and in vitro expression of the gene for the E3 haemagglutinin glycoprotein of bovine coronavirus. J. Gen. Virol. 1989;70:155–164. doi: 10.1099/0022-1317-70-1-155. [DOI] [PubMed] [Google Scholar]
  272. Parker M.D., Yoo D., Babiuk L.A. Expression and secretion of the bovine coronavirus hemagglutinin-esterase glycoprotein by insect cells infected with recombinant baculoviruses. J. Virol. 1990;64:1625–1629. doi: 10.1128/jvi.64.4.1625-1629.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  273. Parker M.M., Masters P.S. Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein. Virology. 1990;179:463–468. doi: 10.1016/0042-6822(90)90316-J. [DOI] [PMC free article] [PubMed] [Google Scholar]
  274. Parker S.E., Gallagher T.M., Buchmeier M.J. Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus. Virology. 1989;173:664–673. doi: 10.1016/0042-6822(89)90579-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  275. Payne H.R., Storz J. Analysis of cell fusion induced by bovine coronavirus infection. Arch. Virol. 1988;103:27–33. doi: 10.1007/BF01319806. [DOI] [PMC free article] [PubMed] [Google Scholar]
  276. Peng D., Koetzner C.A., Masters P.S. Analysis of second-site revertants of a murine coronavirus nucleocapsid protein deletion mutant and construction of nucleocapsid protein mutants by targeted RNA recombination. J. Virol. 1995;69:3449–3457. doi: 10.1128/jvi.69.6.3449-3457.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  277. Peng D., Koetzner C.A., McMahon T., Zhu Y., Masters P.S. Construction of murine coronavirus mutants containinginterspecies chimeric nucleocapsid proteins. J. Virol. 1995;69:5475–5484. doi: 10.1128/jvi.69.9.5475-5484.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  278. Pensaert M., Callebaut P., Vengote J. Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis. Vet. Q. 1986;8:257–261. doi: 10.1080/01652176.1986.9694050. [DOI] [PubMed] [Google Scholar]
  279. Penzes Z., Tibbies K., Shaw K., Britton P., Brown T.D.K., Cavanagh D. Characterization of a replicating and packaged defective RNA of avian coronavirus infectious bronchitis virus. Virology. 1994;203:286–293. doi: 10.1006/viro.1994.1486. [DOI] [PMC free article] [PubMed] [Google Scholar]
  280. Penzes Z., Wroe C., Brown T.D.K., Britton P., Cavanagh D. Replication and packaging of coronavirus infectious bronchitis virus defective RNAs lacking a long open reading frame. J. Virol. 1996;70:8660–8668. doi: 10.1128/jvi.70.12.8660-8668.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  281. Perlman S., Ries D., Bolger E., Chang L.J., Stoltzfus C.M. MHV nucleocapsid synthesis in the presence of cyclohexamide and accumulation of negative-strand MHV RNA. Virus Res. 1986;6:261–272. doi: 10.1016/0168-1702(86)90074-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  282. Pfleiderer M., Routledge E., Siddell S.G. Functional analysis of the coronavirus MHV-JHM surface glycoproteins in vaccinia virus recombinants. Adv. Exp. Med. Biol. 1990;276:21–31. doi: 10.1007/978-1-4684-5823-7_4. [DOI] [PubMed] [Google Scholar]
  283. Pfleiderer M., Routledge E., Herder G., Siddell S.G. High level transient expression of the murine coronavirus haemagglutinin-esterase. J. Gen. Virol. 1991;72:1309–1315. doi: 10.1099/0022-1317-72-6-1309. [DOI] [PubMed] [Google Scholar]
  284. Plagemann P.G.W., Moennig V. Lactate dehydrogenase-elevating virus, equine arteritis virus and simian haemorrhagic fever virus, a new group of positive strand RNA viruses. Adv. Virus Res. 1992;41:99–192. doi: 10.1016/S0065-3527(08)60036-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  285. Rasschaert D., Duarte M., Laude H. Porcine respiratory coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions. J. Gen. Virol. 1990;71:2599–2607. doi: 10.1099/0022-1317-71-11-2599. [DOI] [PubMed] [Google Scholar]
  286. Ricard C.S., Koetzner C.A., Sturman L.S., Masters P.S. A conditionallethal murine coronavirus mutant that fails to incorporate the spike glycoprotein into assembled virions. Virus Res. 1995;39:261–276. doi: 10.1016/0168-1702(95)00100-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  287. Risco C., Anton I.M., Sune C., Pedregosa A.M., Martin-Alonso J.M., Parra F., Carrascosa J.L., Enjuanes L. Membrane protein molecules of transmissible gastroenteritis coronavirus also expose the carboxy-terminal region on the external surface of the virion. J. Virol. 1995;69:5269–5277. doi: 10.1128/jvi.69.9.5269-5277.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  288. Risco C., Anton I.M., Enjuanes L., Carrascosa J.L. The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins. J. Virol. 1996;70:4773–4777. doi: 10.1128/jvi.70.7.4773-4777.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  289. Robb J.A., Bond C.W., Leibowitz J.L. Pathogenic murine coronaviruses. III. Biological and biochemical characterization of temperature-sensitive mutants of JHMV. Virology. 1979;94:385–399. doi: 10.1016/0042-6822(79)90469-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  290. Robbins S.G., Frana M.F., McGowan J.J., Boyle J.F., Holmes K.V. RNA-binding proteins of coronavirus MHV: Detection of monomeric and multimeric N protein with an RNA overlay-protein blot assay. Virology. 1986;150:402–410. doi: 10.1016/0042-6822(86)90305-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  291. Rossen J.W.A., Bekker C.P.J., Voorhout W.F., Strous G.J.A.M., van der Ende A., Rottier P.J.M. Entry and release of transmissible gastroenteritis coronavirus are restricted to apical surfaces of polarized epithelial cells. J. Virol. 1994;68:7966–7973. doi: 10.1128/jvi.68.12.7966-7973.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  292. Rossen J.W.A., Voorhout W.F., Horzinek M.C., van der Ende A., Strous G.J.A.M., Rottier P.J.M. MHV-A59 enters polarized murine epithelial cells through the apical surface but is released basolaterally. Virology. 1995;210:54–66. doi: 10.1006/viro.1995.1316. [DOI] [PMC free article] [PubMed] [Google Scholar]
  293. Rossen J.W.A., Horzinek M.C., Rottier P.J.M. Coronavirus infection of polarised epithelial cells. Trends Microbiol. 1995;3:486–490. doi: 10.1016/S0966-842X(00)89018-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  294. Rossen J.W., Strous G.J., Horzinek M.C.A.M., Rottier P.J.M. Mouse hepatitis virus strain A59 is released from opposite sides of different epithelial cell types. J. Gen. Virol. 1997;78:61–69. doi: 10.1099/0022-1317-78-1-61. [DOI] [PubMed] [Google Scholar]
  295. Rottier P., Branderberg D., Armstrong J., van der Zeijst B., Warren G. Assembly in vitro of a spanning membrane protein of the endoplasmic reticulum: The E1 glycoprotein of coronavirus mouse hepatitis virus A59. Proc. Natl. Acad. Sci. U.S.A. 1984;81:1421–1425. doi: 10.1073/pnas.81.5.1421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  296. Rottier P.J.M., Welling G.W., Welling-Wester S., Niesters H.G.M., Lenstra J.A., van der Zeijst B.A.M. Predicted membrane topology of the coronavirus protein E1. Biochemistry. 1986;25:1335–1339. doi: 10.1021/bi00354a022. [DOI] [PubMed] [Google Scholar]
  297. Rottier P.J.M. The coronavirus membrane glycoprotein. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 115–139. [Google Scholar]
  298. Routledge E., Stauber R., Pfleiderer M., Siddell S.G. Analysis of murine coronavirus surface glycoprotein functions by using monoclonal antibodies. J. Virol. 1991;65:254–262. doi: 10.1128/jvi.65.1.254-262.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  299. Rowe C.L., Baker S.C., Nathan M.J., Fleming J.O. Evolution of mouse hepatitis virus: Detection and characterization of spike deletion variants during persistent infection. J. Virol. 1997;71:2959–2969. doi: 10.1128/jvi.71.4.2959-2969.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  300. Sawicki S.G., Sawicki D.L. Coronavirus minus-strand RNA synthesis and effect of cycloheximide on coronavirus RNA synthesis. J. Virol. 1986;57:328–334. doi: 10.1128/jvi.57.1.328-334.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  301. Sawicki S.G., Sawicki D.L. Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis. J. Virol. 1990;64:1050–1056. doi: 10.1128/jvi.64.3.1050-1056.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  302. Sawicki S.G., Lu J.H., Holmes K.V. Persistent infection of cultured cells with mouse hepatitis virus (MHV) results from epigenetic expression of the MHV receptor. J. Virol. 1995;69:5535–5543. doi: 10.1128/jvi.69.9.5535-5543.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  303. Schaad M.C., Baric R.S. Evidence for new transcriptional units encoded at the 3′ end of the mouse hepatitis virus genome. Virology. 1993;196:190–198. doi: 10.1006/viro.1993.1467. [DOI] [PubMed] [Google Scholar]
  304. Schaad M.C., Baric R.S. Genetics of mouse hepatitis virus transcription: Evidence that subgenomic negative strands are functional templates. J. Virol. 1994;68:8169–8179. doi: 10.1128/jvi.68.12.8169-8179.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  305. Schaad M.C., Stohlman S.A., Egbert J., Lum K., Fu K., Wei T., Baric R.S. Genetics of mouse hepatitis virus transcription: Identification of cistrons which may function in positive and negative strand RNA synthesis. Virology. 1990;177:634–645. doi: 10.1016/0042-6822(90)90529-Z. [DOI] [PMC free article] [PubMed] [Google Scholar]
  306. Schmidt I., Skinner M., Siddell S. Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM. J. Gen. Virol. 1987;68:47–56. doi: 10.1099/0022-1317-68-1-47. [DOI] [PubMed] [Google Scholar]
  307. Schmidt M.F.G. Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses. Virology. 1982;116:327–338. doi: 10.1016/0042-6822(82)90424-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  308. Schultze B., Herrler G. Bovine coronavirus uses JV-acetyl-9-0-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells. J. Gen. Virol. 1992;73:901–906. doi: 10.1099/0022-1317-73-4-901. [DOI] [PubMed] [Google Scholar]
  309. Schultze B., Gross H.J., Borssmer R., Klenk H.D., Herrler G. Hemagglutinating encephalomyelitis virus attaches to N-acetyl-9-O-acetylneuraminic acid-containing receptors on erythrocytes: Comparison with bovine coronavirus and influenza C virus. Virus Res. 1990;16:185–194. doi: 10.1016/0168-1702(90)90022-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  310. Schultze B., Gross H.J., Brossmer R., Herrler G. The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant. J. Virol. 1991;65:6232–6237. doi: 10.1128/jvi.65.11.6232-6237.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  311. Schultze B., Wahn K., Klenk H.-D., Herrler G. Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity. Virology. 1991;180:221–228. doi: 10.1016/0042-6822(91)90026-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  312. Schultze B., Cavanagh D., Herrler G. Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes. Virology. 1992;189:792–794. doi: 10.1016/0042-6822(92)90608-R. [DOI] [PMC free article] [PubMed] [Google Scholar]
  313. Schwarz B., Routledge E., Siddell S.G. Murine coronavirus nonstructural protein ns2 is not essential for virus replication in transformed cells. J. Virol. 1990;64:4784–4791. doi: 10.1128/jvi.64.10.4784-4791.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  314. Senanayake S.D., Hofinann M.A., Maki J.L., Brian D.A. The nucleocapsid protein gene of bovine coronavirus is bicistronic. J. Virol. 1992;66:5277–5283. doi: 10.1128/jvi.66.9.5277-5283.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  315. Sethna P.B., Hung S.L., Brian D.A. Coronavirus subgenomic minusstrand RNAs and the potential for mRNA replicons. Proc. Natl. Acad. Sci. U.S.A. 1989;86:5626–5630. doi: 10.1073/pnas.86.14.5626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  316. Sethna P.B., Hofmann M.A., Brian D.A. Minusstrand copies of replicating coronavirus mRNAs contain antileaders. J. Virol. 1991;65:320–325. doi: 10.1128/jvi.65.1.320-325.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  317. Seybert A., Ziebuhr J., Siddell S.G. Expression and characterization of a recombinant murine coronavirus 3C-like proteinase. J. Gen. Virol. 1997;78:71–75. doi: 10.1099/0022-1317-78-1-71. [DOI] [PubMed] [Google Scholar]
  318. Shieh C.-K., Lee H.-J., Yokomori K., La Monica N., Makino S., Lai M.M.C. Identification of a new transcriptional initiation site and the corresponding functional gene 2b in the murine coronavirus UNA genome. J. Virol. 1989;63:3729–3736. doi: 10.1128/jvi.63.9.3729-3736.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  319. Shif I., Bang F.B. In vitro interaction of mouse hepatitis virus and macro-phages from gneetically resistant mice. I. Adsorption of virus and growth curves. J. Exp. Med. 1970;131:843–862. doi: 10.1084/jem.131.4.843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  320. Siddell S.G. “The Coronaviridae.”. Plenum; New York: 1995. [Google Scholar]
  321. Siddell S.G. The Coronaviridae: An introduction. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 1–10. [Google Scholar]
  322. Siddell S.G. The small membrane protein. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 181–190. [Google Scholar]
  323. Siddell S., Wege H., Barthel A., Meulen V. Coronavirus JHM: Intracellular protein synthesis. J. Gen. Virol. 1980;53:145–155. doi: 10.1099/0022-1317-53-1-145. [DOI] [PubMed] [Google Scholar]
  324. Smith A.L., Cardellichio C.B., Winograd D.F., de Souza M.S., Barthold S.W., Holmes K.V. Monoclonal antibody to the receptor for murine coronavirus MHV-A59 inhibits viral replication in vivo. J. Infect. Dis. 1991;163:879–882. doi: 10.1093/infdis/163.4.879. [DOI] [PMC free article] [PubMed] [Google Scholar]
  325. Smith A.R., Boursnell M.E., Binns M.M., Brown T.D., Inglis S.C. Identification of a new membrane-associated polypeptide specified by the coronavirus infectious bronchitis virus. J. Gen. Virol. 1990;71:3–11. doi: 10.1099/0022-1317-71-1-3. [DOI] [PubMed] [Google Scholar]
  326. Snijder E.J., Horzinek M.C. Toroviruses: Replication, evolution and comparison with other members of the coronavirus-like superfamily. J. Gen. Virol. 1993;74:2305–2316. doi: 10.1099/0022-1317-74-11-2305. [DOI] [PubMed] [Google Scholar]
  327. Snyder E.J., Horzinek M.C. The molecular biology of toroviruses. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. pp. 219–238. [Google Scholar]
  328. Snyder E.J., Spaan W.J.M. The coronavirus superfamily. In: Siddell S.G., editor. “The Coronaviridae”. Plenum; New York: 1995. [Google Scholar]
  329. Snyder E.J., den Boon J.A., Horzinek M.C., Spaan W.J. Comparison of the genome organization of toro-and coronaviruses: Evidence for two nonhomologous RNA recombination events during Berne virus evolution. Virology. 1991;180:448–452. doi: 10.1016/0042-6822(91)90056-H. [DOI] [PMC free article] [PubMed] [Google Scholar]
  330. Soe L.H., Shieh C.-K., Baker S.C., Chang M.-F., Lai M.M.C. Sequence and translation of the murine coronavirus 5′-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase. J. Virol. 1987;61:3968–3976. doi: 10.1128/jvi.61.12.3968-3976.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  331. Somogyi P., Jenner A.J., Brierley L, Inglis S.C. Ribosomal pausing during translation of an RNA pseudoknot. Mol. Cell. Biol. 1993;13:6931–6940. doi: 10.1128/mcb.13.11.6931. [DOI] [PMC free article] [PubMed] [Google Scholar]
  332. Spaan W.J.M., Rottier P.J.M., Horzinek M.C., van der Zeyst B.A.M. Isolation and identification of virus-specific mRNA in cells infected with mouth hepatitis virus (MHV-A59) Virology. 1981;108:424–434. doi: 10.1016/0042-6822(81)90449-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  333. Spaan W.J.M., Delius H., Skinner M., Armstrong J., Rottier P., Smeekens S., van der Zeijst B.A.M., Siddell S.G. Coronavirus mRNA synthesis involves fusion of non-contiguous sequences. EMBO J. 1983;2:1839–1844. doi: 10.1002/j.1460-2075.1983.tb01667.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  334. Stauber R., Pfleiderer M., Siddell S. Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity. J. Gen. Virol. 1993;74:183–191. doi: 10.1099/0022-1317-74-2-183. [DOI] [PubMed] [Google Scholar]
  335. Stern D.F., Kennedy S.I.T. Coronavirus multiplication strategy. I. Identification and characterization of virus-specified RNA. J. Virol. 1980;34:665–674. doi: 10.1128/jvi.34.3.665-674.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  336. Stern D.F., Kennedy S.I.T. Coronavirus multiplication strategy. II. Mapping the avian infectious bronchitis virus intracellular RNA species to the genome. J. Virol. 1980;36:440–449. doi: 10.1128/jvi.36.2.440-449.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  337. Stern D.F., Sefton B.M. Synthesis of coronavirus mRNAs: Kinetics of inactivation of infectious bronchitis virus RNA synthesis by UV light. J. Virol. 1982;42:755–759. doi: 10.1128/jvi.42.2.755-759.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  338. Stern D.F., Sefton B.M. Coronavirus proteins: Structure and function of the oligosaccharides of the avian infectious bronchitis virus glycoproteins. J. Virol. 1982;44:804–812. doi: 10.1128/jvi.44.3.804-812.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  339. Stohlman S.A., Lai M.M.C. Phosphoproteins of murine hepatitis viruses. J. Virol. 1979;32:672–675. doi: 10.1128/jvi.32.2.672-675.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  340. Stohlman S.A., Baric R.S., Nelson G.N., Soe L.H., Welter L.M., Deans R.J. Specific interaction between coronavirus leader RNA and nucleocapsid protein. J. Virol. 1988;62:4288–4295. doi: 10.1128/jvi.62.11.4288-4295.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  341. Storz J., Herrler G., Snodgrass D.R., Hussain K.A., Zhang X.M. Monoclonal antibodies differentiate between the haemagglutinating and the receptor-destroying activities of bovine coronavirus. J. Gen. Virol. 1991;72:2817–2820. doi: 10.1099/0022-1317-72-11-2817. [DOI] [PubMed] [Google Scholar]
  342. Sturman L.S., Holmes K.V. The molecular biology of coronaviruses. Adv. Virus Res. 1983;28:35–112. doi: 10.1016/S0065-3527(08)60721-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  343. Sturman L.S., Holmes K.V., Behnke J. Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid. J. Virol. 1980;33:449–462. doi: 10.1128/jvi.33.1.449-462.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  344. Sturman L.S., Ricard C.S., Holmes K.V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. J. Virol. 1985;56:904–911. doi: 10.1128/jvi.56.3.904-911.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  345. Sturman L.S., Ricard C.S., Holmes K.V. Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37 degrees C correlates with virus aggregation and virus-induced cell fusion. J. Virol. 1990;64:3042–3050. doi: 10.1128/jvi.64.6.3042-3050.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  346. Sugiyama K., Amano Y. Hemagglutination and structural polypeptides of a new coronavirus associated with diarrhea in infant mice. Arch. Virol. 1980;66:95–105. doi: 10.1007/BF01314978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  347. Suzuki H., Taguchi F. Analysis of receptor-binding site of murine coronavirus spike protein. J. Virol. 1996;70:2632–2636. doi: 10.1128/jvi.70.4.2632-2636.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  348. Swift A.M., Machamer C.E. A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein. J. Cell Biol. 1991;115:19–30. doi: 10.1083/jcb.115.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
  349. Taguchi F. Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant c1-2. J. Virol. 1993;67:1195–1202. doi: 10.1128/jvi.67.3.1195-1202.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  350. Taguchi F. The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding. J. Virol. 1995;70:7260–7263. doi: 10.1128/jvi.69.11.7260-7263.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  351. Tahara S.M., Dietlin T.A., Bergmann C.C., Nelson G.W., Kyuwa S., Anthony R.P., Stohlman S.A. Coronavirus translational regulation: Leader affects mRNA efficiency. Virology. 1994;202:621–630. doi: 10.1006/viro.1994.1383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  352. Talbot P.J., Paquette J.S., Ciurli C., Antel J.P., Ouellet F. Myelin basic protein and human coronavirus 229E cross-reactive T cells in multiple sclerosis. Ann. Neurol. 1996;39:233–240. doi: 10.1002/ana.410390213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  353. Thiel V., Siddell S.G. Internal ribosome entry in the coding region of murine hepatitis virus mRNA 5. J. Gen. Virol. 1994;75:3041–3046. doi: 10.1099/0022-1317-75-11-3041. [DOI] [PubMed] [Google Scholar]
  354. Tibbles K.W., Brierley I., Cavanagh D., Brown T.D.K. A region of the coronavirus infectious bronchitis virus 1a polyprotein encoding the 3C-like protease domain is subject to rapid turnover when expressed in rabbit reticulocyte lysate. J. Gen. Virol. 1995;76:3059–3070. doi: 10.1099/0022-1317-76-12-3059. [DOI] [PubMed] [Google Scholar]
  355. Tibbles K.W., Brierly I., Cavanagh D., Brown T.D.K. Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus. J. Virol. 1996;70:1923–1930. doi: 10.1128/jvi.70.3.1923-1930.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  356. Tooze J., Tooze S.A. Infection of AtT20 murine pituitary tumour cells by mouse hepatitis virus strain A59: Virus budding is restricted to the Golgi region. Eur. J. Cell Biol. 1985;37:203–212. [PubMed] [Google Scholar]
  357. Tooze J., Tooze S.A., Warren G. Replication of coronavirus MHV-A59 in sac-cells: Determination of the first site of budding of progeny virions. Eur. J. Cell Biol. 1984;33:281–293. [PubMed] [Google Scholar]
  358. Tooze J., Tooze S.A., Fuller S.D. Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells. J. Cell Biol. 1987;105:1215–1226. doi: 10.1083/jcb.105.3.1215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  359. Tooze S.A., Tooze J., Warren G. Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59. J. Cell Biol. 1988;106:1475–1487. doi: 10.1083/jcb.106.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  360. Torres J.M., Sanchez C., Sune C., Smerdou C., Prevec L., Graham F., Enjuanes L. Induction of antibodies protecting against transmissible gastroenteritis coronavirus (TGEV) by recombinant adenovirus expressing TGEV spike protein. Virology. 1995;213:503–516. doi: 10.1006/viro.1995.0023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  361. Tresnan D.B., Levis R., Holmes K.V. Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I. J. Virol. 1996;70:8669–8674. doi: 10.1128/jvi.70.12.8669-8674.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  362. Tsunemitsu H., Elkanawati Z.R., Smith D.R., Reed H.H., Saif L.J. Isolation of coronaviruses antigenically indistinguishable from bovine coronavirus from wild ruminants with diarrhea. J. Clin. Microbiol. 1995;33:3264–3269. doi: 10.1128/jcm.33.12.3264-3269.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  363. Tung F.Y.T., Abraham S., Sethna M., Hung S.-L., Sethna P., Hogue B.G., Brian D.A. The 9-kDa hydrophobic protein encoded at the 3′-end of the porcine transmissible gastroenteritis coronavirus genome is membrane-associated. Virology. 1992;186:676–683. doi: 10.1016/0042-6822(92)90034-M. [DOI] [PMC free article] [PubMed] [Google Scholar]
  364. van Berlo M.F., van den Brink W.J., Horzinek M.C., van der Zegst B.A.M. Fatty acid acylation of viral proteins murine hepatitis virus-infected cells. Brief report. Arch. Virol. 1987;95:123–128. doi: 10.1007/BF01311339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  365. van der Most R.G., Bredenbeek P.J., Spaan W.J.M. A domain at the 3′-end of the polymerase gene is essential for encapsidation of coronavirus defective interfering RNAs. J. Virol. 1991;65:3219–3226. doi: 10.1128/jvi.65.6.3219-3226.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  366. van der Most R.G., Heijnen L., Spaan W.J.M., de Groot R.J. Homologous RNA recombination allows efficient introduction of site-specific mutations into the genome of coronavirus MHV-A59 via synthetic co-replicating RNAs. Nucleic Acids Res. 1992;20:3375–3381. doi: 10.1093/nar/20.13.3375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  367. van der Most R.G., de Groot R.J., Spaan W.J.M. Subgenomic RNA synthesis directed by a synthetic defective interfering RNA of mouse hepatitis virus: A study of coronavirus transcription initiation. J. Virol. 1994;68:3656–3666. doi: 10.1128/jvi.68.6.3656-3666.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  368. van der Most R.G., Luytjes W., Rutjes S., Spaan W.J.M. Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus. J. Virol. 1995;69:3744–3751. doi: 10.1128/jvi.69.6.3744-3751.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  369. van Dinter S., Flintoff W.F. Rat glial C6 cells are defective in murine coronavirus internalization. J. Gen. Virol. 1987;68:1677–1685. doi: 10.1099/0022-1317-68-6-1677. [DOI] [PubMed] [Google Scholar]
  370. Van Marie G., Luytjes W., van der Most R.G., van der Straaten T., Spaan W.J.M. Regulation of coronavirus mRNA transcription. J. Virol. 1995;69:7851–7856. doi: 10.1128/jvi.69.12.7851-7856.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  371. Vaughn E.M., Halbur P.G., Paul P.S. Sequence comparison of porcine respiratory coronavirus isolates reveals heterogeneity in the S, 3, and 3-1 genes. J. Virol. 1995;69:3176–3184. doi: 10.1128/jvi.69.5.3176-3184.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  372. Vennema H., Heijnen L., Zijderveld A., Horzinek M.C., Spaan W.J.M. Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly. J. Virol. 1990;64:339–346. doi: 10.1128/jvi.64.1.339-346.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  373. Vennema H., de Groot R.J., Harbour D.A., Dalderup M., Gruffydd-Jones T., Horzinek M.C., Spaan W.J.M. Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization. J. Virol. 1990;64:1407–1409. doi: 10.1128/jvi.64.3.1407-1409.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  374. Vennema H., de Groot R.J., Harbour D.A., Horzinek M.C., Spaan W.J.M. Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens. Virology. 1991;181:327–335. doi: 10.1016/0042-6822(91)90499-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  375. Vennema H., Heijnen L., Rottier P.J.M., Horzinek M.C., Spaan W.J.M. A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal. J. Virol. 1992;66:4951–4956. doi: 10.1128/jvi.66.8.4951-4956.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  376. Vennema H., Godeke G.J., Rossen J.W.A., Voorhout W.F., Horzinek M.C., Opstelten D.J.E., Rottier P.J.M. Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes. EMBO J. 1996;15:2020–2028. doi: 10.1002/j.1460-2075.1996.tb00553.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  377. Vlasak R., Luytjes W., Lieder J., Spaan W.J.M., Palese P. The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetyltransferase activity. J. Virol. 1988;62:4686–4690. doi: 10.1128/jvi.62.12.4686-4690.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  378. Vlasak R., Luytjes W., Spaan W.J.M., Palese P. Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc. Natl. Acad. Sci. U.S.A. 1988;85:4526–4529. doi: 10.1073/pnas.85.12.4526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  379. Wang F.-I., Fleming J.O., Lai M.M.C. Sequence analysis of the spike protein gene of murine coronavirus variants: Study of genetic sites affecting neuropa-thogenicity. Virology. 1992;186:742–749. doi: 10.1016/0042-6822(92)90041-M. [DOI] [PMC free article] [PubMed] [Google Scholar]
  380. Wang L., Junker D., Collison E.W. Evidence of natural recombination within the S1 gene of the infectious bronchitis virus. Virology. 1993;192:710–716. doi: 10.1006/viro.1993.1093. [DOI] [PubMed] [Google Scholar]
  381. Wang L., Junker D., Hock L., Ebiary E., Collisson E.W. Evolutionary implications of genetic variations in the S1 gene of infectious bronchitis virus. Virus Res. 1994;34:327–338. doi: 10.1016/0168-1702(94)90132-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  382. Wege H., Stephenson J.R., Koga M., Wege H., Meulen V. Genetic variation of neurotropic and non-neurotropic murine coronaviruses. J. Gen. Virol. 1981;54:67–74. doi: 10.1099/0022-1317-54-1-67. [DOI] [PubMed] [Google Scholar]
  383. Wege H., Winter J., Meyermann R. The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: Definition of critical epitopes by variant analysis. J. Gen. Virol. 1988;69:87–98. doi: 10.1099/0022-1317-69-1-87. [DOI] [PubMed] [Google Scholar]
  384. Weingartl H.M., Derbyshire J.B. Evidence for a putative second receptor for porcine transmissible gastroenteritis virus on the villous enterocytes of newborn pigs. J. Virol. 1994;68:7253–7259. doi: 10.1128/jvi.68.11.7253-7259.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  385. Weismiller D.G., Sturman L.S., Buchmeier M.J., Fleming J.O., Holmes K.V. Monoclonal antibodies tp the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunlt released under mild alkaline conditions. J. Virol. 1990;64:3051–3055. doi: 10.1128/jvi.64.6.3051-3055.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  386. Weiss M., Horzinek M.C. The proposed family Toroviridae: agents of enteric infections. Brief review. Arch. Virol. 1987;92:1–15. doi: 10.1007/BF01310058. [DOI] [PMC free article] [PubMed] [Google Scholar]
  387. Weiss R.C., Scott F.W. Pathogenesis of feline infectious peritonitis: nature and development of viremia. Am. J. Vet. Res. 1981;42:382–390. [PubMed] [Google Scholar]
  388. Weisz O.A., Swift A.M., Machamer C.E. Oligomerization of a membrane protein correlates with its retention in the Golgi complex. J. Cell Biol. 1993;122:1185–1196. doi: 10.1083/jcb.122.6.1185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  389. Welsh R.M., Haspel M.V., Parker D.C., Holmes K.V. Natural cytotoxicily against mouse hepatitis virus-infected cells. II. A cytotoxic effector cell with a B lymphocyte phenotype. J. Immunol. 1986;136:1454–1460. [PubMed] [Google Scholar]
  390. Wesley R.D., Woods R.D., Hill H.T., Biwer J.D. Evidence for a porcirw, respiratory coronavirus, antigenically similar to transmissible gastroenteritis virus in the United States. J. Vet. Diagn. Invest. 1990;2:312–317. doi: 10.1177/104063879000200411. [DOI] [PubMed] [Google Scholar]
  391. Wesley R.D., Woods R.D., Cheung A.K. Genetic analysis of porcinu respiratory coronavirus, an attenuated variant of transmissible gastroenteritis virus. J. Virol. 1991;65:3369–3373. doi: 10.1128/jvi.65.6.3369-3373.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  392. Wilhelmsen K.C., Leibowitz J.L., Bond C.W., Robb J.A. The replication of murine coronaviruses in enucleated cells. Virology. 1981;110:225–230. doi: 10.1016/0042-6822(81)90027-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  393. Williams G.D., Chang R.-Y., Brian D.A. Evidence for a pseudoknot in the 3′-untranslated region of the bovine coronavirus genome. In: Talbot P.J., Levy G.A., editors. “Corona and Related Viruses”. Plenum; New York: 1995. pp. 511–514. [DOI] [PubMed] [Google Scholar]
  394. Williams R.K., Jiang G., Holmes K.V. Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins. Proc. Natl. Acad. Sci. U.S.A. 1991;88:5533–5536. doi: 10.1073/pnas.88.13.5533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  395. Wilson G.A.R., Dales S. In vivo and in vitro models of demyelinating disease: Efficiency of virus spread and formation of infectious centers among glial cells is genetically determined by the murine host. J. Virol. 1988;62:3371–3377. doi: 10.1128/jvi.62.9.3371-3377.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  396. Wilson G.A.R., Mohandas D.V., Dales S. In vivo and in vitro models of demyelinating disease. Possible relationship between induction of regulatory subunit from cAMP dependent protein kinases and inhibition of JHMV replication in cultured oligodendrocytes. Adv. Exp. Med. Biol. 1990;276:261–266. doi: 10.1007/978-1-4684-5823-7_36. [DOI] [PubMed] [Google Scholar]
  397. Woo K., Joo M., Narayanan K., Kim K.H., Makino S. Murine coronavirus packaging signal confers packaging to nonviral RNA. J. Virol. 1997;71:824–827. doi: 10.1128/jvi.71.1.824-827.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  398. Yeager C.L., Ashumn R.A., Williams R.K., Cardellichio C.B., Shapiro L.H., Look A.T., Holmes K.V. Human aminopeptidase N is a receptor for human coronavirus 229E. Nature (London) 1992;357:420–422. doi: 10.1038/357420a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  399. Yokomori K., Lai M.M.C. Mouse hepatitis virus S RNA sequence reveals that nonstructural proteins NS 4 and NS 5a are not essential for murine coronavirus replication. J. Virol. 1991;65:5605–5608. doi: 10.1128/jvi.65.10.5605-5608.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  400. Yokomori K., Lai M.M.C. Mouse hepatitis virus utilizes two carcinoembryonic antigens as alternative receptors. J. Virol. 1992;66:6194–6199. doi: 10.1128/jvi.66.10.6194-6199.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  401. Yokomori K., Lai M.M.C. The receptor for mouse hepatitis virus in the resistant mouse strain SJL is functional: Implications for the requirement of a second factor for viral infection. J. Virol. 1992;66:6931–6938. doi: 10.1128/jvi.66.12.6931-6938.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  402. Yokomori K., La Monica N., Makino S., Shieh C.-K., Lai M.M.C. Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. Virology. 1989;173:683–691. doi: 10.1016/0042-6822(89)90581-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  403. Yokomori K., Banner L.R., Lai M.M.C. Heterogeneity of gene expression of hemagglutinin-esterase (HE) protein of murine coronaviruses. Virology. 1991;183:647–657. doi: 10.1016/0042-6822(91)90994-M. [DOI] [PMC free article] [PubMed] [Google Scholar]
  404. Yokomori K., Baker S.C., Stohlman S.A., Lai M.M.C. Hemagglutinin-esterase (HE)-specific monoclonal antibodies alter the neuropathogenicity of mouse hepatitis virus. J. Virol. 1992;66:2865–2874. doi: 10.1128/jvi.66.5.2865-2874.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  405. Yokomori K., Banner L.R., Lai M.M.C. Coronavirus mRNA transcription: UV light transcriptional mapping studies suggest an early requirement for a genomic-length template. J. Virol. 1992;66:4671–4678. doi: 10.1128/jvi.66.8.4671-4678.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  406. Yokomori K., Asanaka M., Stohlman S.A., Lai M.M.C. A spike protein-dependent cellular factor other than the viral receptor is required for mouse hepatitis virus entry. Virology. 1993;196:45–56. doi: 10.1006/viro.1993.1453. [DOI] [PubMed] [Google Scholar]
  407. Yokomori K., Asanaka M., Stohlman S.A., Makino S., Shubin R.A., Gilmore W., Weiner L.P., Wang F.I., Lai M.M.C. Neuropathogenicity of mouse hepatitis virus JHM isolates differing in hemagglutinin-esterase protein expression. J. Neurovirol. 1995;1:330–339. doi: 10.3109/13550289509111022. [DOI] [PubMed] [Google Scholar]
  408. Yoo D., Graham F.L., Prevec L., Parker M.D., Benko M., Zamb T., Babiuk L.A. Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus. J. Gen. Virol. 1992;73:2591–2600. doi: 10.1099/0022-1317-73-10-2591. [DOI] [PubMed] [Google Scholar]
  409. Yoo D.W., Parker M.D., Babiuk L.A. The S2 subunit of the spike glycoprotein of bovine coronavirus mediates membrane fusion in insect cells. Virology. 1991;180:395–399. doi: 10.1016/0042-6822(91)90045-D. [DOI] [PMC free article] [PubMed] [Google Scholar]
  410. Yoshikura H., Taguchi F. Mouse hepatitis virus strain MHV-S: Formation of pseudotypes with a murine leukemia virus envelope. Intervirology. 1978;10:132–136. doi: 10.1159/000148978. [DOI] [PubMed] [Google Scholar]
  411. Yu W., Leibowitz J.L. A conserved motif at the 3′ end of mouse hepatitis virus genomic RNA required for host protein binding and viral RNA replication. Virology. 1995;214:128–138. doi: 10.1006/viro.1995.9947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  412. Yu W., Leibowitz J.L. Specific binding of host cellular proteins to multiple sites within the 3′-end of mouse hepatitis virus genomic RNA. J. Virol. 1995;69:2016–2023. doi: 10.1128/jvi.69.4.2016-2023.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  413. Yu X., Bi W., Weiss S.R., Leibowitz J.L. Mouse hepatitis virus gene 5b protein is a new virion envelope protein. Virology. 1994;202:1018–1023. doi: 10.1006/viro.1994.1430. [DOI] [PubMed] [Google Scholar]
  414. Zhang X., Lai M.M.C. Unusual heterogeneity of leader-mRNA fusion in a murine coronavirus: Implications for the mechanism of RNA transcription and recombination. J. Virol. 1994;68:6626–6633. doi: 10.1128/jvi.68.10.6626-6633.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  415. Zhang X., Lai M.M.C. Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed. J. Virol. 1995;69:1637–1644. doi: 10.1128/jvi.69.3.1637-1644.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  416. Zhang X., Lai M.M.C. A 5′-proximal RNA sequence of murine coronavirus as a potential initiation site forgenomic-length mRNA transcription. J. Virol. 1996;70:705–711. doi: 10.1128/jvi.70.2.705-711.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  417. Zhang X., Kousoulas K.G., Storz J. The hemagglutinin/esterase glycoprotein of bovine coronaviruses: Sequence and functional comparisons between virulent and avirulent strains. Virology. 1991;185:847–852. doi: 10.1016/0042-6822(91)90557-R. [DOI] [PMC free article] [PubMed] [Google Scholar]
  418. Zhang X., Herbst W., Kousoulas K.G., Storz J. Biological and genetic characterization of a hemagglutinating coronavirus isolated from a diarrhoeic child. J. Med. Virol. 1994;44:152–161. doi: 10.1002/jmv.1890440207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  419. Zhang X., Liao C.-L., Lai M.M.C. Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis. J. Virol. 1994;68:4738–4746. doi: 10.1128/jvi.68.8.4738-4746.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  420. Zhao X., Shaw K., Cavanagh D. Presence of subgenomic mRNAs in virions of coronavirus IBV. Virology. 1993;196:172–178. doi: 10.1006/viro.1993.1465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  421. Zhou M., Williams A.K., Chung S.-I., Wang L., Collisson E.W. The infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3′ terminus of the genome. Virology. 1996;217:191–199. doi: 10.1006/viro.1996.0106. [DOI] [PubMed] [Google Scholar]
  422. Ziebuhr J., Herold J., Siddell S.G. Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J. Virol. 1995;69:4331–4338. doi: 10.1128/jvi.69.7.4331-4338.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  423. Zoltick P.W., Leibowitz J.L., Oleszak E.L., Weiss S.R. Mouse hepatitis virus ORF 2a is expressed in the cytosol of infected mouse fibroblasts. Virology. 1990;174:605–607. doi: 10.1016/0042-6822(90)90114-7. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Advances in Virus Research are provided here courtesy of Elsevier

RESOURCES