Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1996 Dec;70(12):8614–8623. doi: 10.1128/jvi.70.12.8614-8623.1996

Detection and preliminary characterization of a new rabbit calicivirus related to rabbit hemorrhagic disease virus but nonpathogenic.

L Capucci 1, P Fusi 1, A Lavazza 1, M L Pacciarini 1, C Rossi 1
PMCID: PMC190954  PMID: 8970986

Abstract

A new rabbit calicivirus related to the rabbit hemorrhagic disease virus (RHDV) was identified. The new virus contains significant differences from the previously characterized RHDV isolates in terms of pathogenicity, viral titer, tropism, and primary sequence of the structural protein. Cross-protection experiments, antigenic data, and sequence comparisons demonstrate that the new virus is more closely related to RHDV than to the European brown hare syndrome virus, another member of the caliciviruses of the lagomorph group. The existence of a nonpathogenic calicivirus, which we propose to name rabbit calicivirus (RCV), provides an explanation for the early discrepancies found in the course of serological surveys of the rabbit population in European countries.

Full Text

The Full Text of this article is available as a PDF (1,020.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Boga J. A., Casais R., Marin M. S., Martin-Alonso J. M., Carmenes R. S., Prieto M., Parra F. Molecular cloning, sequencing and expression in Escherichia coli of the capsid protein gene from rabbit haemorrhagic disease virus (Spanish isolate AST/89). J Gen Virol. 1994 Sep;75(Pt 9):2409–2413. doi: 10.1099/0022-1317-75-9-2409. [DOI] [PubMed] [Google Scholar]
  2. Boniotti B., Wirblich C., Sibilia M., Meyers G., Thiel H. J., Rossi C. Identification and characterization of a 3C-like protease from rabbit hemorrhagic disease virus, a calicivirus. J Virol. 1994 Oct;68(10):6487–6495. doi: 10.1128/jvi.68.10.6487-6495.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Capucci L., Frigoli G., Rønshold L., Lavazza A., Brocchi E., Rossi C. Antigenicity of the rabbit hemorrhagic disease virus studied by its reactivity with monoclonal antibodies. Virus Res. 1995 Aug;37(3):221–238. doi: 10.1016/0168-1702(95)00033-m. [DOI] [PubMed] [Google Scholar]
  4. Capucci L., Scicluna M. T., Lavazza A. Diagnosis of viral haemorrhagic disease of rabbits and the European brown hare syndrome. Rev Sci Tech. 1991 Jun;10(2):347–370. doi: 10.20506/rst.10.2.561. [DOI] [PubMed] [Google Scholar]
  5. Chasey D., Lucas M., Westcott D., Williams M. European brown hare syndrome in the U.K.; a calicivirus related to but distinct from that of viral haemorrhagic disease in rabbits. Arch Virol. 1992;124(3-4):363–370. doi: 10.1007/BF01309816. [DOI] [PubMed] [Google Scholar]
  6. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  7. Engel J. P., Boyer E. P., Goodman J. L. Two novel single amino acid syncytial mutations in the carboxy terminus of glycoprotein B of herpes simplex virus type 1 confer a unique pathogenic phenotype. Virology. 1993 Jan;192(1):112–120. doi: 10.1006/viro.1993.1013. [DOI] [PubMed] [Google Scholar]
  8. Grieder F. B., Davis N. L., Aronson J. F., Charles P. C., Sellon D. C., Suzuki K., Johnston R. E. Specific restrictions in the progression of Venezuelan equine encephalitis virus-induced disease resulting from single amino acid changes in the glycoproteins. Virology. 1995 Feb 1;206(2):994–1006. doi: 10.1006/viro.1995.1022. [DOI] [PubMed] [Google Scholar]
  9. Guittré C., Ruvoen-Clouet N., Barraud L., Cherel Y., Baginski I., Prave M., Ganiere J. P., Trépo C., Cova L. Early stages of rabbit haemorrhagic disease virus infection monitored by polymerase chain reaction. Zentralbl Veterinarmed B. 1996 Apr;43(2):109–118. doi: 10.1111/j.1439-0450.1996.tb00294.x. [DOI] [PubMed] [Google Scholar]
  10. Hardy M. E., White L. J., Ball J. M., Estes M. K. Specific proteolytic cleavage of recombinant Norwalk virus capsid protein. J Virol. 1995 Mar;69(3):1693–1698. doi: 10.1128/jvi.69.3.1693-1698.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Herbert T. P., Brierley I., Brown T. D. Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA. J Gen Virol. 1996 Jan;77(Pt 1):123–127. doi: 10.1099/0022-1317-77-1-123. [DOI] [PubMed] [Google Scholar]
  12. Jiang X., Wang M., Graham D. Y., Estes M. K. Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. J Virol. 1992 Nov;66(11):6527–6532. doi: 10.1128/jvi.66.11.6527-6532.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Meyer R. F., Pacciarini M., Hilyard E. J., Ferrari S., Vakharia V. N., Donini G., Brocchi E., Molitor T. W. Genetic variation of foot-and-mouth disease virus from field outbreaks to laboratory isolation. Virus Res. 1994 Jun;32(3):299–312. doi: 10.1016/0168-1702(94)90079-5. [DOI] [PubMed] [Google Scholar]
  14. Meyers G., Wirblich C., Thiel H. J. Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles. Virology. 1991 Oct;184(2):677–686. doi: 10.1016/0042-6822(91)90437-G. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Meyers G., Wirblich C., Thiel H. J. Rabbit hemorrhagic disease virus--molecular cloning and nucleotide sequencing of a calicivirus genome. Virology. 1991 Oct;184(2):664–676. doi: 10.1016/0042-6822(91)90436-f. [DOI] [PubMed] [Google Scholar]
  16. Milton I. D., Turner J., Teelan A., Gaskell R., Turner P. C., Carter M. J. Location of monoclonal antibody binding sites in the capsid protein of feline calicivirus. J Gen Virol. 1992 Sep;73(Pt 9):2435–2439. doi: 10.1099/0022-1317-73-9-2435. [DOI] [PubMed] [Google Scholar]
  17. Moussa A., Chasey D., Lavazza A., Capucci L., Smíd B., Meyers G., Rossi C., Thiel H. J., Vlásak R., Rønsholt L. Haemorrhagic disease of lagomorphs: evidence for a calicivirus. Vet Microbiol. 1992 Nov;33(1-4):375–381. doi: 10.1016/0378-1135(92)90065-2. [DOI] [PubMed] [Google Scholar]
  18. Neill J. D. Nucleotide sequence of the capsid protein gene of two serotypes of San Miguel sea lion virus: identification of conserved and non-conserved amino acid sequences among calicivirus capsid proteins. Virus Res. 1992 Jul;24(2):211–222. doi: 10.1016/0168-1702(92)90008-w. [DOI] [PubMed] [Google Scholar]
  19. Pacciarini M. L., Savio M. L., Tagliabue S., Rossi C. Repetitive sequences cloned from Leptospira interrogans serovar hardjo genotype hardjoprajitno and their application to serovar identification. J Clin Microbiol. 1992 May;30(5):1243–1249. doi: 10.1128/jcm.30.5.1243-1249.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Park B. H., Matuschke B., Lavi E., Gaulton G. N. A point mutation in the env gene of a murine leukemia virus induces syncytium formation and neurologic disease. J Virol. 1994 Nov;68(11):7516–7524. doi: 10.1128/jvi.68.11.7516-7524.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Parra F., Prieto M. Purification and characterization of a calicivirus as the causative agent of a lethal hemorrhagic disease in rabbits. J Virol. 1990 Aug;64(8):4013–4015. doi: 10.1128/jvi.64.8.4013-4015.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Prasad B. V., Matson D. O., Smith A. W. Three-dimensional structure of calicivirus. J Mol Biol. 1994 Jul 15;240(3):256–264. doi: 10.1006/jmbi.1994.1439. [DOI] [PubMed] [Google Scholar]
  23. Prasad B. V., Rothnagel R., Jiang X., Estes M. K. Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J Virol. 1994 Aug;68(8):5117–5125. doi: 10.1128/jvi.68.8.5117-5125.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Rasschaert D., Huguet S., Madelaine M. F., Vautherot J. F. Sequence and genomic organization of a rabbit hemorrhagic disease virus isolated from a wild rabbit. Virus Genes. 1995 Jan;9(2):121–132. doi: 10.1007/BF01702655. [DOI] [PubMed] [Google Scholar]
  25. Rodák L., Smíd B., Valícek L., Veselý T., Stepánek J., Hampl J., Jurák E. Enzyme-linked immunosorbent assay of antibodies to rabbit haemorrhagic disease virus and determination of its major structural proteins. J Gen Virol. 1990 May;71(Pt 5):1075–1080. doi: 10.1099/0022-1317-71-5-1075. [DOI] [PubMed] [Google Scholar]
  26. Schoepp R. J., Johnston R. E. Sindbis virus pathogenesis: phenotypic reversion of an attenuated strain to virulence by second-site intragenic suppressor mutations. J Gen Virol. 1993 Aug;74(Pt 8):1691–1695. doi: 10.1099/0022-1317-74-8-1691. [DOI] [PubMed] [Google Scholar]
  27. Seal B. S. Analysis of capsid protein gene variation among divergent isolates of feline calicivirus. Virus Res. 1994 Jul;33(1):39–53. doi: 10.1016/0168-1702(94)90016-7. [DOI] [PubMed] [Google Scholar]
  28. Seal B. S., Ridpath J. F., Mengeling W. L. Analysis of feline calicivirus capsid protein genes: identification of variable antigenic determinant regions of the protein. J Gen Virol. 1993 Nov;74(Pt 11):2519–2524. doi: 10.1099/0022-1317-74-11-2519. [DOI] [PubMed] [Google Scholar]
  29. Tohya Y., Masuoka K., Takahashi E., Mikami T. Neutralizing epitopes of feline calicivirus. Arch Virol. 1991;117(3-4):173–181. doi: 10.1007/BF01310763. [DOI] [PubMed] [Google Scholar]
  30. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Wirblich C., Meyers G., Ohlinger V. F., Capucci L., Eskens U., Haas B., Thiel H. J. European brown hare syndrome virus: relationship to rabbit hemorrhagic disease virus and other caliciviruses. J Virol. 1994 Aug;68(8):5164–5173. doi: 10.1128/jvi.68.8.5164-5173.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wirblich C., Sibilia M., Boniotti M. B., Rossi C., Thiel H. J., Meyers G. 3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity. J Virol. 1995 Nov;69(11):7159–7168. doi: 10.1128/jvi.69.11.7159-7168.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES