1887

Abstract

SUMMARY

The glycoprotein (G) of vesicular stomatitis virus (VSV) was radiolabelled, extracted and purified so that its potential interaction with host cell surfaces could be studied. When BHK-21 cells were incubated with the radiolabelled virus glycoprotein, the virus component rapidly attached to the cell surface. The attachment was shown to be temperature-dependent and saturated at approx. 3 × 10 molecules/cell. The omission of Mg or Ca from the incubation medium had little effect on the glycoprotein binding. Treating the isolated G protein and intact virions with neuraminidase did not significantly decrease their binding to BHK-21 cells. Pre-incubating cells with trypsin did not decrease the attachment of VSV virions nor the binding of purified G protein. Treating cells with phospholipase A or phospholipase C suggested that the binding of the glycoprotein and the intact virion might have been dissimilar. Unlabelled glycoprotein competitively inhibited binding of the labelled molecules although the presence of intact virions did not inhibit attachment of the G protein. Likewise, saturating amounts of the glycoprotein did not decrease binding of VSV to BHK-21 cells. These observations suggested that either the isolated glycoprotein bound to cell surface components that were distinct from the virion receptor or that the manner of the purified glycoprotein attachment differed from the G protein still associated with the intact virion. Chemical crosslinking and diagonal two-dimensional gel electrophoresis were used to identify and to compare the cell surface components responsible for glycoprotein and virion attachment.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-50-2-279
1980-10-01
2022-06-29
Loading full text...

Full text loading...

/deliver/fulltext/jgv/50/2/JV0500020279.html?itemId=/content/journal/jgv/10.1099/0022-1317-50-2-279&mimeType=html&fmt=ahah

References

  1. Bishop D. H. L., Smith M. S. 1977 In The Molecular Biology of Animal Viruses ch. 5, pp 167–280 Edited by Mayaic D. P. New York: Marcel Dekker;
    [Google Scholar]
  2. Bishop D. H. L., Repik P., Obijeski J. F., Moore N., Wagner R. R. 1975; Restitution of infectivity to spikeless vesicular stomatitis virus by solubilized viral components. Journal of Virology 16:75–84
    [Google Scholar]
  3. Bose H. R., Sagik B. P. 1970; The virus envelope in cell attachment. Journal of General Virology 9:159–161
    [Google Scholar]
  4. Cartwright B., Brown F. 1977; Role of sialic acid in infection with vesicular stomatitis virus. Journal of General Virology 35:197–199
    [Google Scholar]
  5. Cook G. M., Heard E. H., Seaman G. A. 1961; Sialic acids and the electrokinetic charge of human erythrocyte. Nature, London 191:44–47
    [Google Scholar]
  6. Dannon D., Howe C., Lee L. T. 1965; Interaction of polylysine with soluble components of human erythrocyte membranes. Biochimica et Biophysica Acta 101:201–213
    [Google Scholar]
  7. Delarco J., Todaro G. J. 1976; Membrane receptors for murine leukemia viruses: characterization using purified viral envelope glycoproteins, gp71. Cell 8:365–371
    [Google Scholar]
  8. Dietzschold B., Schneider L. G., Cox J. H. 1974; Serological characterization of the three proteins of vesicular stomatitis virus. Journal of Virology 14:1–7
    [Google Scholar]
  9. Fahey J. L., Terry E. W. 1978 In Handbook of Experimental Immunology vol 1 ch. 8, pp 8.1–8.16 Edited by Weir D. M. Oxford: Blackwell Scientific Publications;
    [Google Scholar]
  10. Fowler A. K., Twardzik D. R., Reed C. D., Weislow O. S., Hellman A. 1977; Binding characteristics of Rauscher leukemia virus envelope glycoprotein gp71 to murine lymphoid cells. Journal of Virology 24:729–735
    [Google Scholar]
  11. Hale A. H., Witte O. N., Baltimore D., Eisen H. N. 1978; VSV glycoprotein is necessary for H-2-restrictional lysis of infected cells by cytotoxic T-lymphocytes. Proceedings of the National Academy of Sciences of the United States of America 75:970–974
    [Google Scholar]
  12. Hanks J. H., Wallace R. E. 1949; Relation of oxygen and temperature in the preservation of tissue by refrigeration. Proceedings of the Society for Experimental Biology and Medicine 71:196–200
    [Google Scholar]
  13. Heide K., Schwick H. G. 1978 In Handbook of Experimental Immunology vol 1 ch. 7, pp 7.1–7.11 Edited by Weir D. M. Oxford: Blackwell Scientific Publications;
    [Google Scholar]
  14. Howe C., Lee L. T. 1970; Virus-erythrocyte interaction. Advances in Virus Research 17:1–50
    [Google Scholar]
  15. Howe C., Avrameas S., Devaus St., Cyr C., Grabar P., Lee L. T. 1963; Antigenic components of human erythrocytes. Journal of Immunology 91:683–692
    [Google Scholar]
  16. Hoyle L. 1968 In Virology Monographs vol 4 pp 1–379 Edited by Gard S., Hallauer C., Meyer K. F. New York: Springer-Verlag;
    [Google Scholar]
  17. Hughes J. V., Johnson T. C., Rabinowitz S. G., Dal Canto M. C. 1979; Growth and maturation of a vesicular stomatitis virus temperature sensitive mutant and its central nervous system isolate. Journal of Virology 29:312–321
    [Google Scholar]
  18. Kalyanaraman V. S., Sarngadharan M. G., Gallo R. C. 1978; Characterization of Rauscher murine leukemia virus envelope glycoprotein receptor in membranes from murine fibroblasts. Journal of Virology 28:686–696
    [Google Scholar]
  19. Kathan R. H., Winzler R. J., Johnson C. A. 1961; Preparation of an inhibitor of viral hemagglutination from human erythrocytes. Journal of Experimental Medicine 133:37–45
    [Google Scholar]
  20. Kelley J., Emerson S., Wagner R. R. 1972; The glycoprotein of vesicular stomatitis virus is the antigen that gives rise to and reacts with neutralizing antibody. Journal of Virology 10:1231–1235
    [Google Scholar]
  21. Kelly P. T., Luttges M. W. 1975; Electrophoretic separation of nervous system proteins on exponential gradient polyacrylamide gels. Journal of Neurochemistry 24:1077–1079
    [Google Scholar]
  22. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  23. Lonberg-Holm K., Korant B. D. 1972; Early interaction of rhinoviruses with host cells. Journal of Virology 9:29–40
    [Google Scholar]
  24. Lonberg-Holm K., Philipson L. 1974 In Monographs in Virology vol 9 pp 1–148 Edited by Melnick J. L. Basel: S. Karger;
    [Google Scholar]
  25. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  26. Moore N. F., Kelley J. M., Wagner R. R. 1974; Envelope proteins of vesicular stomatitis virus: accessibility to iodination. Virology 61:292–296
    [Google Scholar]
  27. Mudd J. A., Swanson R. E. 1978; In situ cross‒linking of vesicular stomatitis virus proteins with reversible agents. Virology 88:263–280
    [Google Scholar]
  28. Neurath A. R., Hartzell R. W., Rubin R. A. 1970; Partial characterization of the complementary sites involved in the reaction between adenovirus 7 and erythrocyte receptors. Virology 42:789–793
    [Google Scholar]
  29. Philipson L., Lindberg U. 1974 In Comprehensive Virology vol 3 pp 143–227 Edited by Fraenkel-Conrat H., Wagner R. R. New York: Plenum Press;
    [Google Scholar]
  30. Philipson L., Lonberg-Holm K., Pettersson U. 1968; Virus receptor interaction in an adenovirus system. Journal of Virology 2:1064–1075
    [Google Scholar]
  31. Rabinowitz S. G., Dal Canto M. C., Johnson T. C. 1976; Comparison of central nervous system disease produced by wild-type and temperature-sensitive mutants of vesicular stomatitis virus. Infection and Immunity 13:1242–1249
    [Google Scholar]
  32. Schloemer R. H., Wagner R. R. 1975; Cell adsorption function of the sialoglycoprotein of VSV and its neuramic acid. Journal of Virology 15:882–893
    [Google Scholar]
  33. Takemoto L. J., Fox C. F., Jensen F. C., Elder J. H., Lerner R. A. 1978; Nearest neighbor interactions of the major RNA tumor virus glycoprotein on murine cell surfaces. Proceedings of the National Academy of Sciences of the United States of America 75:3644–3648
    [Google Scholar]
  34. Weissman I. L., Baird S., Gardner R. L., Papiannov V. E., Raschke W. 1977; Normal and neoplastic maturation of T-lineage lymphocytes. Cold Spring Harbor Symposia on Quantitative Biology 41:9–21
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-50-2-279
Loading
/content/journal/jgv/10.1099/0022-1317-50-2-279
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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