1887

Abstract

Summary

Goose erythrocyte membranes were isolated and tested for their ability to compete with red cell receptors for vesicular stomatitis virus (VSV) attachment and fusion at acidic pH. Crude membranes, solubilized with Triton X-100, Tween 80 and octyl--- glucopyranoside, showed a dose-dependent inhibitory effect on virus binding and haemolysis. The chemical nature of the active molecules was investigated by enzyme digestion and by separation of purified components. Only the lipid moiety, specifically phospholipid and glycolipid, was found to inhibit VSV attachment; a more detailed analysis of these molecules showed that phosphatidylinositol, phosphatidylserine and GM3 ganglioside were responsible for the inhibitory activity and could therefore represent VSV binding sites on goose erythrocyte membranes. Removal of negatively charged groups from these molecules by enzymic treatment significantly reduced their activity, suggesting that electrostatic interactions play an important role in the binding of VSV to the cell surface. Enzymic digestion of whole erythrocytes confirmed the involvement of membrane lipid molecules in the cell surface receptor for VSV.

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1987-09-01
2022-08-10
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References

  1. Aminoff D. 1959; The determination of free sialic acid in the presence of the bound compound. Virology 7:355–357
    [Google Scholar]
  2. Bailey C. A., Miller D. K., Lenard J. 1984; Effects of DEAE-dextran on infection and hemolysis by VSV. Evidence that nonspecific electrostatic interactions mediate effective binding of VSV to cells. Virology 133:111–118
    [Google Scholar]
  3. Byrne M. C., Sbaschning-Agler M., Aquino D. A., Sclafani I. R., Leeden R. W. 1985; Procedure for isolation of gangliosides in high yield and purity: simultaneous isolation of neutral glycosphingolipids. Analytical Biochemistry 148:163–173
    [Google Scholar]
  4. Dales S. 1973; Early events in cell-animal virus interactions. Bacteriological Reviews 37:103–135
    [Google Scholar]
  5. Folch J., Lees M., Sloane Stanley G. H. 1957; A simple method for the isolation and purification of total lipids from animal tissue. Journal of Biological Chemistry 226:497–509
    [Google Scholar]
  6. Frings C. S., Fendley T. W., Dunn R. T., Queen C. A. 1972; Improved determination of total serum lipids by sulfo-phospho-vanillin reaction. Clinical Chemistry 18:673–674
    [Google Scholar]
  7. Ginsberg B. H., Kahn C. R., Roth J. 1976; The insulin receptor of the turkey erythrocyte. Characterization of the membrane-bound receptor. Biochimica et biophysica acta 443:227–242
    [Google Scholar]
  8. Haest C. W. M., Plasa G., Deuticke B. 1981; Selective removal of lipids from the outer membrane layer of human erythrocytes without haemolysis. Consequences for bilayer stability and cell shape. Biochimica et biophysica acta 649:701–708
    [Google Scholar]
  9. Hakomori S., Watanabe K. 1976; Blood group glycolipids of human erythrocytes. In Glycolipid Methodology pp 13–47 Witting L. A. Edited by Bellefonte: Supelco Inc;
    [Google Scholar]
  10. Hakomori S., Stellner K., Watanabe K. 1972; Antigenic variants of blood-group A glycolipid. Examples of highly complex, branched-chain glycolipid of animal cell-membrane. Biochemical and Biophysical Research Communications 49:1061–1068
    [Google Scholar]
  11. Halonen P. E., Toivanen P., Nikkari T. 1974; Non-specific serum inhibitors of activity of haemagglutinins of rabies and vesicular stomatitis viruses. Journal of General Virology 22:309–318
    [Google Scholar]
  12. Ladish S., Gillard B. 1985; A solvent partition method for microscale ganglioside purification. Analytical Biochemistry 146:220–231
    [Google Scholar]
  13. Lonberg-Holm K., Philipson L. 1974; Early interaction between animal viruses and cells. In Monographs in Virology 9 pp 1–149 Melnick J. L. Edited by S. Karger;
    [Google Scholar]
  14. 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]
  15. Maddy A. H. 1966; The properties of the protein of the plasma membrane of ox erythrocytes. Biochimica et biophysica acta 117:193–200
    [Google Scholar]
  16. Matlin K., Reggio H., Helenius A., Simons K. 1982; Pathway of vesicular stomatitis virus entry leading to infection. Journal of Molecular Biology 156:609–631
    [Google Scholar]
  17. Mifune K., Ohuchi M., Mannen K. 1982; Hemolysis and cell fusion by rhabdoviruses. FEBS letters 137:293–297
    [Google Scholar]
  18. Schlegel R., Wade M. 1984; Biological activities of peptides corresponding to the amino-terminus of vesicular stomatitis virus glycoprotein. In Abstracts of Sixth International Congress of Virology p. 288 September 1–7 1984 Sendai, Japan:
    [Google Scholar]
  19. Schlegel R., Tralka T. S., Willingham M. C., Pastan I. 1983; Inhibition of VSV binding and infectivity by phosphatidylserine : is phosphatidylserine a VSV-binding site?. Cell 32:639–646
    [Google Scholar]
  20. Seganti L., Superti F., Mastromarino P., Sinibaldi L., Orsi N. 1982; Role of carbohydrates on cell membrane receptors for vesicular stomatitis virus. Bollettino dell’Istituto sieroterapico milanese 61:294–299
    [Google Scholar]
  21. Seganti L., Grassi M., Mastromarino P., Panà A., Superti F., Orsi N. 1983; Activity of human serum lipoproteins on the infectivity of rhabdoviruses. Microbiologica 6:91–99
    [Google Scholar]
  22. Superti F., Seganti L., Tsiang H., Orsi N. 1984; Role of phospholipids in rhabdovirus attachment to CER cells. Archives of Virology 81:321–328
    [Google Scholar]
  23. Svennerholm L., Fredman P. 1980; A procedure for the quantitative isolation of brain gangliosides. Biochimica et biophysica acta 617:97–109
    [Google Scholar]
  24. Vandenberg S. R., Allgren R. L., Todd R. D., Ciaranello R. D. 1983; Solubilization and characterization of high-affinity [3H]serotonin binding sites from bovine cortical membranes. Proceedings of the National Academy of Sciences U.S.A.: 803508–3512
    [Google Scholar]
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