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. 1991 Oct;65(10):5636–5640. doi: 10.1128/jvi.65.10.5636-5640.1991

Protease digestion of hepatitis A virus: disparate effects on capsid proteins, antigenicity, and infectivity.

S M Lemon 1, E Amphlett 1, D Sangar 1
PMCID: PMC249085  PMID: 1654460

Abstract

High concentrations of either trypsin or chymotrypsin caused nearly complete cleavage of capsid protein VP2 of hepatitis A virus but did not significantly reduce the infectivity, thermostability, or antigenicity of the virus. Chymotrypsin also had a lesser effect on VP1. These findings indicate the presence of a protease-accessible VP2 surface site which neither contributes significantly to the dominant antigenic site nor plays a role in the attachment of the virus to putative cell receptors.

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Selected References

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

  1. Brown E. A., Jansen R. W., Lemon S. M. Characterization of a simian hepatitis A virus (HAV): antigenic and genetic comparison with human HAV. J Virol. 1989 Nov;63(11):4932–4937. doi: 10.1128/jvi.63.11.4932-4937.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chow M., Newman J. F., Filman D., Hogle J. M., Rowlands D. J., Brown F. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature. 1987 Jun 11;327(6122):482–486. doi: 10.1038/327482a0. [DOI] [PubMed] [Google Scholar]
  3. Cohen J. I., Ticehurst J. R., Purcell R. H., Buckler-White A., Baroudy B. M. Complete nucleotide sequence of wild-type hepatitis A virus: comparison with different strains of hepatitis A virus and other picornaviruses. J Virol. 1987 Jan;61(1):50–59. doi: 10.1128/jvi.61.1.50-59.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Houmard J., Drapeau G. R. Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3506–3509. doi: 10.1073/pnas.69.12.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Lemon S. M., Binn L. N., Marchwicki R. H. Radioimmunofocus assay for quantitation of hepatitis A virus in cell cultures. J Clin Microbiol. 1983 May;17(5):834–839. doi: 10.1128/jcm.17.5.834-839.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Lemon S. M., LeDuc J. W., Binn L. N., Escajadillo A., Ishak K. G. Transmission of hepatitis A virus among recently captured Panamanian owl monkeys. J Med Virol. 1982;10(1):25–36. doi: 10.1002/jmv.1890100105. [DOI] [PubMed] [Google Scholar]
  7. Lemon S. M., Murphy P. C., Shields P. A., Ping L. H., Feinstone S. M., Cromeans T., Jansen R. W. Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: evidence for genetic recombination. J Virol. 1991 Apr;65(4):2056–2065. doi: 10.1128/jvi.65.4.2056-2065.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Locarnini S. A., Coulepis A. G., Ferris A. A., Lehmann N. I., Gust I. D. Purification of hepatitis A virus from human feces. Intervirology. 1978;10(5):300–308. doi: 10.1159/000148992. [DOI] [PubMed] [Google Scholar]
  9. Luo M., Rossmann M. G., Palmenberg A. C. Prediction of three-dimensional models for foot-and-mouth disease virus and hepatitis A virus. Virology. 1988 Oct;166(2):503–514. doi: 10.1016/0042-6822(88)90521-1. [DOI] [PubMed] [Google Scholar]
  10. MacGregor A., Kornitschuk M., Hurrell J. G., Lehmann N. I., Coulepis A. G., Locarnini S. A., Gust I. D. Monoclonal antibodies against hepatitis A virus. J Clin Microbiol. 1983 Nov;18(5):1237–1243. doi: 10.1128/jcm.18.5.1237-1243.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ping L. H., Jansen R. W., Stapleton J. T., Cohen J. I., Lemon S. M. Identification of an immunodominant antigenic site involving the capsid protein VP3 of hepatitis A virus. Proc Natl Acad Sci U S A. 1988 Nov;85(21):8281–8285. doi: 10.1073/pnas.85.21.8281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Robertson B. H., Brown V. K., Holloway B. P., Khanna B., Chan E. Structure of the hepatitis A virion: identification of potential surface-exposed regions. Arch Virol. 1989;104(1-2):117–128. doi: 10.1007/BF01313813. [DOI] [PubMed] [Google Scholar]
  13. Siegl G., Frösner G. G., Gauss-Müller V., Tratschin J. D., Deinhardt F. The physicochemical properties of infectious hepatitis A virions. J Gen Virol. 1981 Dec;57(Pt 2):331–341. doi: 10.1099/0022-1317-57-2-331. [DOI] [PubMed] [Google Scholar]
  14. Siegl G., Weitz M., Kronauer G. Stability of hepatitis A virus. Intervirology. 1984;22(4):218–226. doi: 10.1159/000149554. [DOI] [PubMed] [Google Scholar]
  15. Stapleton J. T., Lemon S. M. Neutralization escape mutants define a dominant immunogenic neutralization site on hepatitis A virus. J Virol. 1987 Feb;61(2):491–498. doi: 10.1128/jvi.61.2.491-498.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Wheeler C. M., Robertson B. H., Van Nest G., Dina D., Bradley D. W., Fields H. A. Structure of the hepatitis A virion: peptide mapping of the capsid region. J Virol. 1986 May;58(2):307–313. doi: 10.1128/jvi.58.2.307-313.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]

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