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Coronaviruses pp 501-507 | Cite as

Properties of Coronavirus IBV After Removal of the S1 Subunit of the Spike Glycoprotein

  • Dave Cavanagh
  • Philip Davis
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 218)

Abstract

Our recent investigations of avian infectious bronchitis virus (IBV) have concentrated on the biological properties of the spike (S) glycoprotein. Previously we showed that the mature S is derived by cleavage of a precursor glycoprotein to yield two glycopolypeptides, S1 and S2 of approximately 514 and 625 amino acid residues respectively1. Each spike comprises two or three copies of each of S1 and S2 the two subunits not being held to each other by disulfide bonds2, 3. The ease with which S1 but not the other virion proteins could be removed by urea or SDS 1ed us to suggest that S was anchored in the membrane by S2 and that S1 was probably not in the membrane but formed most of the distal, bulbous part of S3. This view was strengthened when sequencing of the S gene showed that S2 had a highly hydrophobic sequence, typical of membrane-spanning domains, near its carboxy terminus4.

Keywords

Infectious Bronchitis Virus Spike Protein Intact Virus Infectious Bronchitis Virus Strain Spike 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.

References

  1. 1.
    D. Cavanagh, P. J. Davis, D. J. C. Pappin, M. M. Binns, M. E. G. Boursnell and T. D. K. Brown, Coronavirus IBV; partial amino-terminal sequencing of the spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41. Virus Res. 4: 133 (1986).PubMedCrossRefGoogle Scholar
  2. 2.
    D. Cavanagh, Coronavirus IBV: further evidence that the surface projections are associated with two glycopolypeptides. J gen. Virol. 64: 1787 (1983).PubMedCrossRefGoogle Scholar
  3. 3.
    D. Cavanagh, Coronavirus IBV: structural characterization of the spike protein. J. gen. Virol. 64: 2577 (1983).PubMedCrossRefGoogle Scholar
  4. 4.
    M. M. Binns, M. E. G. Boursnell, D. Cavanagh, D. J. C. Pappin and T. D. K. Brown, Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV. J. gen. Virol. 66: 719 (1985).PubMedCrossRefGoogle Scholar
  5. 5.
    D. Cavanagh, J. H. Darbyshire, P. Davis and R. W. Peters, Induction of humoral neutralising and haemagglutination-inhibiting antibody by the spike protein of avian infectious bronchitis virus. Av. Path. 13: 573 (1984).CrossRefGoogle Scholar
  6. 6.
    D. Cavanagh and P. J. Davis, Coronavirus IBV: removal of spike glycopolypeptide S1 by urea abolishes infectivity and haemagglutination but not attachment to cells. J. gen. Virol. 67: 1443 (1986).PubMedCrossRefGoogle Scholar
  7. 7.
    D. Cavanagh, P. J. Davis, J. H. Darbyshire and R. W. Peters, Coronavirus IBV: virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or haemagglutination-inhibiting antibody, or induce chicken tracheal protection. J. gen. Virol. 67: 1435 (1986).PubMedCrossRefGoogle Scholar
  8. 8.
    D. Cavanagh, Structural polypeptides of coronavirus IBV. J. gen. Virol. 53: 93 (1981).PubMedCrossRefGoogle Scholar
  9. 9.
    D. F. Stern, L. Burgess and B. M. Sefton, Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus. J. Virol. 42: 208 (1982).PubMedGoogle Scholar
  10. 10.
    J. H. Darbyshire, J. G. Rowell, J. K. A. Cook and R. W. Peters, Taxonomic studies on strains of avian infectious bronchitis virus using neutralisation tests in trachéal organ cultures. Arch. Virol. 61: 227 (1979).PubMedCrossRefGoogle Scholar
  11. 11.
    A. P. A. Mockett and J. H. Darbyshire, Comparative studies with an enzyme-linked immunosorbent assay (ELISA) for antibodies to avian infectious bronchitis virus. Av. Path. 10: 1 (1981).CrossRefGoogle Scholar
  12. 12.
    A. P. A. Mockett, D. Cavanagh and T. D. K. Brown, Monoclonal antibodies to the S1 spike and membrane proteins of avian infectious bronchitis virus coronavirus strain Massachusetts M41. J. gen. Virol. 65: 2281 (1984).PubMedCrossRefGoogle Scholar
  13. 13.
    L. S. Sturman and K. V. Holmes, The molecular biology of coronaviruses. Adv. Virus Res. 28: 36 (1983).Google Scholar
  14. 14.
    H. J. Hasony and M. R. MacNaughton, Antigenicity of mouse hepatitis virus strain 3 subcomponents in C57 strain mice. Arch. Virol. 69: 33 (1981).PubMedCrossRefGoogle Scholar
  15. 15.
    M. J. Buchmeier, H. A. Lewicki, P. J. Talbot and R. L. Knobler, Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody. Virology 132: 261 (1984).PubMedCrossRefGoogle Scholar
  16. 16.
    H. Wege, R. Dorries and H. Wege, Hybridoma antibodies to the murine coronavirus JHM: characterization of epitopes on the peplomer protein (E2). J. gen. Virol. 65: 1931 (1984).PubMedCrossRefGoogle Scholar
  17. 17.
    D. J. Garwes, M. H. Lucas, D. A. Higgins, B. V. Pike and S. F. Cartwright, Antigenicity of structural components from porcine transmissable gastroenteritis virus. Vet. Microbiol. 3: 179 (1978/1979).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Dave Cavanagh
    • 1
  • Philip Davis
    • 1
  1. 1.Houghton Poultry Research StationHoughton, Huntingdon, Cambs.UK

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