Advertisement

Is the 110K Glycoprotein the Only Receptor for MHV and Does Its Expression Determine Species Specificity?

  • Kathryn V. Holmes
  • Richard K. Williams
  • Christine B. Cardellichio
  • Susan R. Compton
  • Charles B. Stephensen
  • Stuart W. Snyder
  • Mark F. Frana
  • Gui-Sen Jiang
  • Abigail Smith
  • Robert L. Knobler
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 276)

Abstract

Coronaviruses exhibit strong tissue tropisms and species specificities, and the molecular mechanisms for these tropisms are of considerable interest. For mouse hepatitis virus, strain A59 (MHV-A59), a solid phase assay was developed to detect binding of virions to plasma membranes from normal target tissues of susceptible mice (1). Using a virus overlay protein blot assay, MHV-A59 was shown to bind specifically to a 100 to 110K protein from liver or intestine membranes of MHV-susceptible BALB/c mice. The specificity of virus binding was demonstrated by the observations that other enterotropic murine viruses did not bind to the same membrane protein and that MHV-A59 did not bind to any proteins from intestine or hepatocyte membranes from SJL/J mice, which are highly resistant to infection with MHV-A59 (2,3). Thus, SJL/J mice may be resistant to infection with MHV-A59 because the virus fails to bind to its normal target tissues, possibly because the virus-binding moiety is absent from the SJL/J plasma membranes.

Keywords

Brush Border Membrane 110K Protein Mouse Hepatitis Virus Intestine Membrane Receptor Glycoprotein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Boyle, J.F., D.G. Weismiller, and K.V. Holmes. 1987. Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues. J. Virol. 61:185–189.PubMedGoogle Scholar
  2. 2.
    S.W. Barthold, and Smith, A.L. 1984. Mouse hepatitis virus strain-related patterns of tissue tropism in suckling mice. Arch. Virol. 81:103–112.PubMedCrossRefGoogle Scholar
  3. 3.
    Smith, M.S., R.E. Click, and P.G. Plagemann. 1984. Control of mouse hepatitis virus replication in macrophages by a recessive gene on chromosome 7. J. Immunol. 133:428–432.PubMedGoogle Scholar
  4. 4.
    Holmes, K.V., Boyle, J.F., Weismiller, D.G., Compton, S.R., Williams, R.K., Stephensen, C.B., and Frana, M.F. 1987. Identification of a receptor for mouse hepatitis virus. Adv. Exp. Med. Biol. 218:197–202.PubMedGoogle Scholar
  5. 5.
    Williams, R.K., S.W. Snyder, and K.V. Holmes. 1989. MHV-Resistant SJL/J mice express a non-functional homolog to the MHV receptor glycoprotein. This volume.Google Scholar
  6. 6.
    Compton, S.R. 1988. PhD Thesis. Uniformed Services University of the Health Sciences, Bethesda, MD.Google Scholar
  7. 7.
    Knobler, R.L., Dubois-Dalcq, M., Haspel, M.V., Claysmith, A.P., Lampert, P.W., and Oldstone, M.B. 1981. Selective localization of wild type and mutant mouse hepatitis virus (JHM strain) antigens in CNS tissue by fluorescence, light and electron microscopy. J. Neuroimmunol. 1:81–92.PubMedCrossRefGoogle Scholar
  8. 8.
    Sorensen, O., and S. Dales. 1985. In vivo and in vitro models of demyelinating disease: JHM virus in the rat central nervous system localized by in situ cDNA hybridization and immunofluorescent microscopy. J. Virol 56:434–438.PubMedGoogle Scholar
  9. 9.
    Wege, H., M. Koga, R. Watanabe, K. Nagashima, and V. ter Meulen. 1983. Neurovirulence of murine Coronavirus JHM temperature-sensitive mutants in rats. Infect. Immun. 39:1316–1324.PubMedGoogle Scholar
  10. 10.
    Paulson, J.C., G.N. Rogers, J. Murayama, G. Sze, and E. Martin. 1986. Biological implications of influenza virus receptor specificity. Virus Attachment and Entry into Cells 144–151.Google Scholar
  11. 11.
    Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J., and Wiley, D.C. 1988. Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature Jun 2,333(6172):426–31.Google Scholar
  12. 12.
    Reagan, K.J., B. Goldberg, and R.L. Crowell. 1984. Altered receptor specificity of coxsackievirus B3 after growth in rhabdomyosarcoma cells. J. Virol. 49:635–640.PubMedGoogle Scholar
  13. 13.
    Luytjes, W., P.J. Bredenbeek, A.F. Noten, M.C. Horzinek, and W.J. Spaan. 1988. Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus. Virology 166:415–422.PubMedCrossRefGoogle Scholar
  14. 14.
    Vlasak, R., W. Luytjes, J. Leider, W. Spaan, and P. Palese. 1988. The E3 protein of bovine Coronavirus is a receptor-destroying enzyme with acetylesterase activity. J. Virol. 62:4686–4690.PubMedGoogle Scholar
  15. 15.
    Vlasak, R., W. Luytjes, W. Spaan, and P. Palese. 1988. Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc. Natl. Acad. Sci. U. S. A. 85:4526–4529.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Kathryn V. Holmes
    • 1
  • Richard K. Williams
    • 1
  • Christine B. Cardellichio
    • 1
  • Susan R. Compton
    • 1
  • Charles B. Stephensen
    • 1
  • Stuart W. Snyder
    • 1
  • Mark F. Frana
    • 1
  • Gui-Sen Jiang
    • 1
  • Abigail Smith
    • 2
  • Robert L. Knobler
    • 3
  1. 1.Uniformed Services University of the Health SciencesBethesdaUSA
  2. 2.Yale University School of MedicineNew HavenUSA
  3. 3.Thomas Jefferson Medical CollegePhiladelphiaUSA

Personalised recommendations