Is the 110K Glycoprotein the Only Receptor for MHV and Does Its Expression Determine Species Specificity?
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.
KeywordsBrush Border Membrane 110K Protein Mouse Hepatitis Virus Intestine Membrane Receptor Glycoprotein
Unable to display preview. Download preview PDF.
- 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.Compton, S.R. 1988. PhD Thesis. Uniformed Services University of the Health Sciences, Bethesda, MD.Google Scholar
- 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
- 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.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