Inhibition of Coronavirus MHV-A59 Replication by Proteinase Inhibitors

  • Mark R. Denison
  • James C. Kim
  • Theodore Ross
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 380)

Abstract

Replication of mouse hepatitis virus is initiated by translation and processing of the gene 1 polyprotein. The increasing complexity of this pattern of replicase protein expression is becoming apparent. MHV-A59 encodes approximately 800 kDa of polypeptide within the two overlapping open reading frames of gene 1. In addition, at least one proteinase activity encoded by gene 1 has been identified1,2 and two more are predicted, along with putative polymerase, helicase, NTP binding and possibly growth factor like proteins3–5. Only the first 380 kDa of protein products of MHV gene 1 ORF 1a have been described and characterized as to the pattern of expression and processing in virus infected cells6. Specifically, proteins of N-p28-65-290-C constitute the initial translation products of this region. The cleavage between p28 and p65 has been best described, both in vitro and in virus-infected cells7. As of yet no specific functions have been ascribed to any of these proteins. Thus a great deal remains to be learned about the processing pattern and functions of MHV gene 1 encoded proteins.

Keywords

Hepatitis Agar DMSO Cysteine Aldehyde 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    S.C. Baker, C.-K. Shieh, L.H. Soe, M.-F. Chang, D.M. Vannier and M.M.C. Lai. (1989). J. Virol., 63:3693–3699.PubMedGoogle Scholar
  2. 2.
    S.C. Baker Yokomori, K., Dong, S., Carlisle, R., Gorbalenya, A.E., Koonin, E.V., and Lai, M.M.C. (1993). Journal of Virology, 67:6056–6063.PubMedGoogle Scholar
  3. 3.
    M.F.G. Boursnell, T.D.K. Brown, I.J. Foulds, P.F. Green, F.M. Tomley and M.M. Binns. (1987). J. Gen. Virol., 68:57–77.PubMedCrossRefGoogle Scholar
  4. 4.
    P.J. Breedenbeek, C.J. Pachuk, A.F.H. Noten, J. Charite, W. Luytjes, S.R. Weiss and W. J.M. Spaan. (1990). Nucleic Acids Res., 18:1825–1832.CrossRefGoogle Scholar
  5. 5.
    H-J. Lee, C.-K. Shieh, A.E. Gorbalenya, E.V. Koonin, N. LaMonica, J. Tuler, A. Bagdzhadhzyan and M.M.C. Lai. (1991). Virology, 180:567–582.PubMedCrossRefGoogle Scholar
  6. 6.
    M.R. Denison, S.A. Hughes and S.R. Weiss. (1994). Virology (submitted),Google Scholar
  7. 7.
    M.R. Denison, P.W. Zoltick, S.A. Hughes, B. Giangreco, AL. Olson, S. Perlman, J.L. Leibowitz and S.R. Weiss. (1992). Virology, 189:274–284.PubMedCrossRefGoogle Scholar
  8. 8.
    M.R. Denison and S. Perlman. (1986). J. Virol., 60:12–18.PubMedGoogle Scholar
  9. 9.
    H. Umezawa. (1982). Ann. Rev. Microbiol., 36:75–99.CrossRefGoogle Scholar
  10. 10.
    S. Mehdi. (1991). TIBS, 16:150–153.PubMedGoogle Scholar
  11. 11.
    L.G. Kleina and M.J. Grubman. (1992). J. Virol, 66:7168–7175.PubMedGoogle Scholar
  12. 12.
    N. Hirano, K. Fujiwara and M. Matumoto. (1976). Japan. J. Micro, 20:219–225.Google Scholar
  13. 13.
    J.C. Kim, R. A. Spence, P. F. Currier, X. Lu and M. R. Denison. (1994). (Submitted)Google Scholar
  14. 14.
    D.L. Sawicki and S.G. Sawicki. (1986). J. Virol., 57:328–334.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Mark R. Denison
    • 1
    • 2
    • 3
  • James C. Kim
    • 1
  • Theodore Ross
    • 2
  1. 1.Department of PediatricsVanderbilt University Medical SchoolNashvilleUSA
  2. 2.Department of Microbiology and ImmunologyVanderbilt University Medical SchoolNashvilleUSA
  3. 3.The Elizabeth B Lamb center for Pediatric ResearchVanderbilt University Medical SchoolNashvilleUSA

Personalised recommendations