1887

Abstract

Summary

Urea has been used to remove the S1 spike glycopolypeptide from avian infectious bronchitis virus (IBV) strains M41 and Beaudette, without removing the S2 spike-anchoring glycopolypeptide. Reduction of the pH to 2.9 did not cause release of S1 although some S1 was released spontaneously from IBV Beaudette at pH 7.4. Virus that lacked S1 was no longer infectious or able to cause haemagglutination (HA). However, radiolabelled IBV that lacked S1 attached to erythrocytes and chick kidney cells to the same or similar extent as did intact virus. Treatment of IBV with a phospholipase C preparation, required to make IBV cause HA, did not increase binding of IBV to erythrocytes. The results indicate that while the attachment to cells of virus that lacks S1 is qualitatively different from that of intact virus, the decline in infectivity is the consequence of the loss of some other spike function.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-67-7-1443
1986-07-01
2024-04-20
Loading full text...

Full text loading...

/deliver/fulltext/jgv/67/7/JV0670071443.html?itemId=/content/journal/jgv/10.1099/0022-1317-67-7-1443&mimeType=html&fmt=ahah

References

  1. Alexander D. J., Chettle N. J. 1977; Procedures for the haemagglutination and haemagglutination inhibition tests for avian infectious bronchitis virus. Avian Pathology 6:9–17
    [Google Scholar]
  2. Bingham R. W., Madge M. H., Tyrrell D. A. J. 1975; Haemagglutination by avian infectious bronchitis virus - a coronavirus. Journal of General Virology 28:381–390
    [Google Scholar]
  3. Binns M. M., Boursnell M. E. G., Cavanagh D., Pappin D. J. C., Brown T. D. K. 1985; Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV. Journal of General Virology 66:719–726
    [Google Scholar]
  4. Boursnell M. E. G., Brown T. D. K., Binns M. M. 1984; Sequence of the membrane protein gene from avian coronavirus IBV. Virus Research 1:303–313
    [Google Scholar]
  5. Bruns M., Lehmann-Grube F. 1984; Lymphocytic choriomeningitis virus. VII. Structural alterations of the virion by treatment with proteolytic enzymes without loss of infectivity. Journal of General Virology 65:1431–1435
    [Google Scholar]
  6. Cavanagh D. 1981; Structural polypeptides of coronavirus IBV. Journal of General Virology 53:93–103
    [Google Scholar]
  7. Cavanagh D. 1983a; Coronavirus IBV: further evidence that the surface projections are associated with two glycopolypeptides. Journal of General Virology 64:1787–1791
    [Google Scholar]
  8. Cavanagh D. 1983b; Coronavirus IBV: structural characterization of the spike protein. Journal of General Virology 64:2577–2583
    [Google Scholar]
  9. Cavanagh D., Davis P. I., Pappin D. J. C. 1986a; Coronavirus IBV glycopolypeptides: locational studies using proteases and saponin, a membrane permeabilizer. Virus Research 4:145–156
    [Google Scholar]
  10. Cavanagh D., Davis P. J., Pappin D. J. C., Binns M. M., Boursnell M. E. G., Brown T. D. K. 1986b; 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 Research 4:133–144
    [Google Scholar]
  11. Darbyshire J. H., Cook J. K. A., Peters R. W. 1976; Organ culture studies on the efficiency of infection of chicken tissues with avian infectious bronchitis virus. British Journal of Experimental Pathology 57:443–454
    [Google Scholar]
  12. Lakshmi M. V., Schulze I. T. 1978; Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes. Virology 88:314–324
    [Google Scholar]
  13. Laver W. G., Colman P. M., Webster R. G., Hinshaw V. S., Air G. M. 1984; Influenza virus neuraminidase with hemagglutinin activity. Virology 137:314–323
    [Google Scholar]
  14. Markwell M. A. K., Portner A., Schwartz A. L. 1985; An alternative route of infection for viruses: entry by means of the asialoglycoprotein receptor of a Sendai virus mutant lacking its attachment protein. Proceedings of the National Academy of Sciences, U.S.A. 82:978–982
    [Google Scholar]
  15. Mockett A. P. A., Darbyshire J. H. 1981; Comparative studies with an enzyme-linked immunosorbent assay (ELISA) for antibodies to avian infectious bronchitis virus. Avian Pathology 10:1–10
    [Google Scholar]
  16. Mockett A. P. A., Cavanagh D., Brown T. D. K. 1984; Monoclonal antibodies to the S1 spike and membrane proteins of avian infectious bronchitis coronavirus strain Massachusetts M41. Journal of General Virology 65:2281–2286
    [Google Scholar]
  17. Notter M. F. D., Leary J. F., Balduzzi P. C. 1982; Adsorption of Rous sarcoma virus to genetically susceptible and resistant chicken cells studied by laser flow cytometry. Journal of Virology 41:958–964
    [Google Scholar]
  18. Stern D. F., Sefton B. M. 1982; Coronavirus proteins: biogenesis of avian infectious bronchitis virus virion proteins. Journal of Virology 44:794–803
    [Google Scholar]
  19. Stern D. F., Burgess L., Sefton B. M. 1982; Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus. Journal of Virology 42:208–219
    [Google Scholar]
  20. Sturman L. S., Holmes K. V. 1983; The molecular biology of coronaviruses. Advances in Virus Research 28:36–112
    [Google Scholar]
  21. White J., Kielian M., Helenius A. 1983; Membrane fusion proteins of enveloped animal viruses. Quantitative Review of Biophysics 16:151–195
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-67-7-1443
Loading
/content/journal/jgv/10.1099/0022-1317-67-7-1443
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error