Abstract
Coronavirus MHV-JHM has two surface glycoproteins. The S protein is a heterodimer comprised of two non-covalently bound, subunits of about 90,000 molecular weight (mol.wt.) (S1 and S2) which are derived by proteolytic processing of the 180,000 mol.wt. precursor S. Multimers of the heterodimer assemble together to produce the characteristic peplomer structures at the surface of the virion. The second surface projection is smaller and is comprised of disulphide-linked homodimer(s) of the HE protein. The reduced HE monomer has a mol.wt. of 65,000 (Siddell et al., 1981).
Chapter PDF
References
Collins, A.R., Knobler, R.L., Powell, H., and Buchmeier, M.J., 1982, Monoclonal antibodies to Murine Hepatitis Virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion. Virology 119:358.
de Groot, R.J., Maduro, J., Lenstra, J.A., Horzinek, M.C., and van der Zeijst, B.A., 1987, cDNA cloning and sequence analysis of the gene encoding the peplomer protein of Feline Infectious Peritonitits virus. J. gen. Virol. 68:2639.
de Groot, R.J., van Leen, R.W., Dalderup, M.J.H., Vennema, H., Horzinek, M.C., and Spaan, W., 1989, Stabley expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice. Virology, 171:493.
Fuerst, T.R., Niles, E.G., Studier, F.W., and Moss, B., 1986, Eukaryotic transient expression system based on recombinant Vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. sci. USA 83:8122.
Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., and Delius, H. (1980a) . Nucleotide sequence of cDNA coding for Semliki Forest Virus membrane gylcoproteins. Nature 288:236.
Garoff, H., Frischauf, A.-M., Simons, K., Lehrach, H., and Delius, H. (1980b). The capsid protein of Semliki Forest Virus has clusters of basic amino acids and prolines in its amino terminal region. Proc. Natl. Acad. Sci. USA 77:6376.
Gubler, U., and Hoffman, B.J., 1983, A simple and very efficient method for generating cDNA libraries, Gene 25:263.
Herrler, G., Rott, R., Klenk, H.-D., Müller, H.-P., Shukla, A.-K., Schauer, R., 1985, The receptor destroying enzyme of Influenza C virus is a neuraminate-O-acetlyesterase, EMBO J4:1503.
King, B., Potts, B.J., and Brian, D., 1985, Bovine Coronavirus hemagglutinin protein, Virus Research 2:53.
Luytjes, W., Bredenbeek, P.J., Noten, A.F.H., Horzinek, M.C., and Spaan, W., 1988, Sequence of the Mouse Hepatitis Virus A59 mRNA 2: indications for RNA recombination between Corona-viruses and Influenza C virus. Virology 166:415.
Luytjes, W., Geerts, D., Posthumus, W., Moloen, R., and Spaan, W., 1989, Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses. J. Virol. 63:1408.
Nakada, S., Craeger, R., Krystal, R., Aaronson, R.P., and Palese, P., 1984, Influenza C virus hemagglutinin: comparison with Influenza A and B virus hemagglutinin. J. Virol. 50:118.
Pfeifer, J.B., and Compans, R.W., 1984, Structure of the Influenza C glycoprotein gene as determined from cloned cDNA. Virus Res. 1:281.
Richardson, C.D., and Choppin, P.W., 1983, Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action. Virology 131:518.
Schmidt, I., Skinner, M.A., and Siddell, S.G., 1987, Nucleotide sequence of the gene encoding the surface projection glycoprotein of the Coronavirus MHV-JHM. J. gen. Virol. 68: 47.
Siddell, S.G., Wege, H., Barthel, A., and ter Meulen, V., 1980, Coronavirus JHM: cell free synthesis of structural protein p60. J. Virol. 33:10.
Siddell, S.G., Wege, H., Barthel, A., and ter Meulen, V., 1981, Coronavirus JHM: intracellular protein synthesis. J. gen. Virol. 53:145.
Sturman, L.S., Ricard, C., and Holmes, K.V., 1985, Proteolytic cleavage of the E2 glycoprotein of murine Coronavirus: Activation of cell-fusing activity of virions by trypsin treatment and separation of two different 90K cleavage fragments. J. Virol 56:904.
Vlasak, R., Luytjes, W., Spaan, W., and Palese, P., 1988a, Human and bovine Coronaviruses recognize sialic acid-containing receptors similar those of Influenza C virus. Proc. Natl. Acad. Sci. USA 85:4526.
Vlasak, R., Juytjes, W., Leider, J., Spaan, W., and Palese, P., 1988b, The E3 protein of bovine Coronavirus is a receptor-destroying enzyme with acetylesterase activity. J. Virol62:4686.
Wege, H., Dörries, R., and Wege, H., 1984, Hybridoma antibodies to the murine Coronavirus JHM: characterization of epitopes on the peplomer protein (E2). J. gen. Virol. 65:1931.
Wilson, I.A., Skehel, J.J., and Wiley, D.C., 1981, Structure of the hemagglutinating membrane glycoprotein of Influenza C virus at 3 A resolution. Nature 289:366.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this paper
Cite this paper
Pfleiderer, M., Routledge, E., Siddell, S.G. (1990). Functional Analysis of the Coronavirus MHV-JHM Surface Glycoproteins in Vaccinia Virus Recombinants. In: Cavanagh, D., Brown, T.D.K. (eds) Coronaviruses and their Diseases. Advances in Experimental Medicine and Biology, vol 276. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5823-7_4
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5823-7_4
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5825-1
Online ISBN: 978-1-4684-5823-7
eBook Packages: Springer Book Archive