Murine Coronavirus Spike Glycoprotein

Receptor binding and membrane fusion activities
  • Thomas M. Gallagher
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 494)


The mature Coronavirus spike is a large, oligomeric, type I integral membrane glycoprotein that projects about 20 nm from the surface of infected cells and virions. In this extracellular position, the spikes function to bind the cellular receptors extending from opposing membranes. Following receptor binding, largely hypothetical structural changes take place to generate spike conformations that are capable of mediating fusion of the juxtaposed membranes. Membrane fusion creates pores for entrance of genomes into uninfected cells.


Membrane Fusion Spike Gene Mouse Hepatitis Virus Spike Protein Chase Period 
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.


  1. Alkhatib, G., Broder, C. C. and Berger, E. A., 1996, Cell-type specific fusion cofactors determine human immunodeficiency virus type 1 tropism for T-cell lines versus primary macrophages. J. Virol. 70:5487–5494.PubMedGoogle Scholar
  2. Beauchemin, N., Draber, P., Dveksler, G., Gold, P., Gray-Owen, S., Grunert, F., Hammarstrom, S., Holmes, K., Karlsson, A., Kuroki, M., Lin, S. H., Lucka, L., Najjar, S., Neumaier, M., Obrink, B., Shively, J., Skubitz, K., Stanners, C., and Thomas, P., 1999, Redefined nomenclature for members of the carcinoembryonic antigen family. Exptal Cell Research 252:243–249.CrossRefGoogle Scholar
  3. Cavanagh, D., 1995, The Coronavirus surface glycoprotein. In The Coronaviridae (S. G. Siddell, ed.), Plenum Press, New York and London, pp. 73–115.Google Scholar
  4. Cheever, F. S., Daniels, J. B., Pappenheimer, A. M., and Bailey, O. T., 1949, A murine virus (JHM) causing disseminated encephalomyelitis with extensive destruction of myelin: Isolation and biological properties of the virus. J. Exp. Med. 90:181–194.PubMedCrossRefGoogle Scholar
  5. Dalziel, R. G., Lampert, P. W., Talbot, P. J., and Buchmeier, M. J., 1986, Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence. J. Virol. 59:463–471.PubMedGoogle Scholar
  6. Dveksler, G. S., Pensiero, M. N., Dieffenbach, C. W., Cardellichio, C. B., Basile, A. A., Elia, P. E., and Holmes, K. V., 1993, Mouse hepatitis virus strain A59 and blocking antireceptor monoclonal antibody bind to the N-terminal domain of cellular receptor. Proc. Natl. Acad. Sci. USA 90:1716–1720.PubMedCrossRefGoogle Scholar
  7. Fazakerley, J. K., Parker, S. E., Bloom, F., and Buchmeier, M. J., 1992, The V5A13.1 envelope glycoprotein deletion mutant of mouse hepatitis virus type-4 is neuroattenuated by its reduced rate of spread in the central nervous system. Virology 187:178–188.PubMedCrossRefGoogle Scholar
  8. Fleming, J. O., Stohlman, S. A., Harmon, R. C., Lai, M. M. C., Frelinger, J. A., and Weiner, L. P., 1983, Antigenic relationships of murine coronaviruses: analysis using monoclonal antibodies to JHM (MHV-4) virus. Virology 131:296–307.PubMedCrossRefGoogle Scholar
  9. Fuerst, T. R., Earl, P. L., and Moss, B., 1987, Use of a hybrid vaccinia virus-T7 RNA Polymerase system for expression of target genes. Mol. Cell. Biol. 7:2538–2544.PubMedGoogle Scholar
  10. Gallagher, T. M., Parker, S. E., and Buchmeier, M. J., 1990, Neutralization-resistant variants of a neurotropic Coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein. J. Virol. 64:731–741.PubMedGoogle Scholar
  11. Gallagher, T. M., 1997, A role for naturally occurring variation of the murine Coronavirus spike protein in stabilizing association with the cellular receptor. J. Virol. 71:3129–3137.PubMedGoogle Scholar
  12. Krueger, D. K., Kelly, S. M., Lewicki, D. N., Ruffolo, R., and Gallagher, T. M., 2000, The unique receptor-independent membrane fusion activity of MHV strain JHM is eliminated by mutations in disparate regions of the spike gene. J. Virol. Submitted.Google Scholar
  13. Kubo, H., Yamada, Y. K., and Taguchi, F., 1994, Localization of neutralizing epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine Coronavirus spike protein. J. Virol. 68:5403–5410.PubMedGoogle Scholar
  14. Leparc-Goffart, I., Hingley, S. T., Chua, M. M., Phillips, J., Lavi, E., and Weiss, S. R., 1998, Targeted recombination within the spike gene of murine Coronavirus mouse hepatitis virus A59: Q159 is a determinant of hepatotropism. J. Virol. 72:9628–9636.PubMedGoogle Scholar
  15. Nussbaum, O., Broder, C. C., and Berger, E. A., 1994, Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68:5411–5422.PubMedGoogle Scholar
  16. Opstelten, D.-J. E., Raamsman, M. J. B., Wolfs, K., Horzinek, M. C., and Rottier, P. J. M., 1995, Envelope glycoprotein interactions in Coronavirus assembly. J. Cell Biol. 131:339–349.PubMedCrossRefGoogle Scholar
  17. Rao, P. V., and Gallagher, T. M., 1998, Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine Coronavirus infections. J. Virol. 72:3278–3288.PubMedGoogle Scholar
  18. Sanchez, C. M., Izeta, A., Sanchez-Morgado, J. M., Alonso, S., Sola, I., Balasch, M., Plana-Duran, J., and Enjuanes, L., 1999, Targeted recombination demonstrates that the spike gene of transmissible gastroenteritis Coronavirus is a determinant of its enteric tropism and virulence. J. Virol. 73:7607–7618.PubMedGoogle Scholar
  19. Sturman, L. S., Ricard, C. S., and Holmes, K. V., 1990, Conformational change of the Coronavirus peplomer glycoprotein at pH 8.0 and 37C correlates with virus aggregation and virus-induced cell fusion. J. Virol. 64:3042–3050.PubMedGoogle Scholar
  20. Vennema, H., Rottier, P. J. M., Heijnen, L., Godeke, G. J., Horzinek, M. C., and Spaan, W. J. M., 1990, Biosynthesis and function of the Coronavirus spike protein. Adv. Expt. Med. Biol. 276:9–19.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Thomas M. Gallagher
    • 1
  1. 1.Department of Microbiology and ImmunologyLoyola University Medical CenterMaywoodUSA

Personalised recommendations