1887

Abstract

Influenza virus particles are able to fuse with liposomes composed of negatively charged or neutral phospholipids, as shown by using fluorochrome-labelled virions and fluorescence dequenching methods. Fusion with liposomes composed of only phosphatidylcholine (PC) was dependent on the presence of cholesterol (Chol), whereas fusion with liposomes containing negatively charged phospholipids, such as phosphatidylserine (PS), or of PC and phosphatidylethanolamine (PE) occurred in the absence of Chol. Fusion of influenza virions with PC:Chol liposomes was observed at pH 5.0, but not at pH 7.4, whereas a low degree of fusion with negatively charged liposomes or those containing PE was observed at pH 7.4. In addition, non-fusogenic influenza virions or HA influenza virions fused with PS- or PE-containing liposomes, especially at pH 5.0. Influenza virus particles were also able to induce the release of the fluorochrome calcein from negatively charged calcein-loaded liposomes at pH 5.0, as well as at pH 7.4, but failed to do so with PC:Chol liposomes. Lysis of PC:Chol by influenza virions was dependent on the presence of virus receptors, namely gangliosides (sialoglycolipids), and was observed only at pH 5.0. The results show that fusion of influenza virions with negatively charged or PE-containing liposomes does not reflect the biological activity of the virus needed for penetration and infection of living cells. On the other hand, fusion with PC:Chol liposomes is probably due to the activity of the viral fusion protein, the haemagglutinin glycoprotein.

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1992-11-01
2024-04-25
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References

  1. Amsalem S., Loyter A., Lichtenberg D., Barenholz Y. 1985; The interaction of Sendai virus with negative charged liposomes:virus induced lysis of carboxyfluorescein-loaded small unilamellar vesicles. Biochimica et biophysica acta 820:1–10
    [Google Scholar]
  2. Asano K., Asano A. 1988; Binding of cholesterol and inhibitory peptide derivatives with the hydrophobic sequence of F-glycoprotein of HVJ (Sendai virus): possible implication in the fusion reaction. Biochemistry 27:1321–1329
    [Google Scholar]
  3. Chejanovsky N., Zakai N., Amsalem S., Barenholz Y., Loyter A. 1986; Membrane vesicles containing the Sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidyl-serine liposomes at low pH. Biochemistry 25:4810–4817
    [Google Scholar]
  4. Chuchalowin H. W., Rott R. 1972; A new method for purification of myxoviruses by zonal centrifugation with two different sucrose density gradients. Proceedings of the Society for Experimental Biology 140:245–247
    [Google Scholar]
  5. Citovsky V., Loyter A. 1985; Fusion of Sendai virions or reconstituted Sendai virus envelopes with liposomes or erythrocyte membranes lacking virus receptors. Journal of Biological Chemistry 260:12072–12077
    [Google Scholar]
  6. Citovsky V., Zakai N., Loyter A. 1986; Specific requirement for liposome-associated sialoglycolipids, but not sialoglycoproteins, to allow lysis of phospholipids vesicles by Sendai virions. Experimental Cell Research 166:279–294
    [Google Scholar]
  7. Citovsky V., Rottem S., Nussbaum O., Laster Y., Rott R., Loyter A. 1988; Animal viruses are able to fuse with prokaryotic cells: fusion between Sendai and influenza virions with mycoplasma. Journal of Biological Chemistry 263:461–467
    [Google Scholar]
  8. Fairbanks G., Steck T. L., Wallach D. F. H. 1971; Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617
    [Google Scholar]
  9. Gad A. E. 1983; Cationic polypeptide-induced fusion of acetic liposomes. Biochimica el biophysica acta 728:377–382
    [Google Scholar]
  10. Hamaguchi H., Cleve H. 1972; Solubilization and comparative analysis of mammalian erythrocyte membrane glycoproteins. Biochemical and Biophysical Research Communications 47:459–463
    [Google Scholar]
  11. Hoekstra D., de Boer T., Kaplan K., Wilschut J. 1984; Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23:5675–5681
    [Google Scholar]
  12. Hsu M. C., Schied A., Choppin P. W. 1981; Fusion of Sendai virus with liposomes: dependence on viral fusion protein (F) and the lipid composition of liposomes. Journal of Biological Chemistry 256:3557–3563
    [Google Scholar]
  13. Hurter C., James P., Bachi T., Semenza G., Brunner J. 1989; Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the ‘fusion peptide’. Journal of Biological Chemistry 264:6459–6464
    [Google Scholar]
  14. Klappe K., Wilschut J., Nir S., Hoekstra D. 1986; Parameters affecting fusion between Sendai virus and liposomes. Role of viral proteins, liposomes composition and pH. Biochemistry 25:8252–8260
    [Google Scholar]
  15. Klenk H. D., Rott R., Orlich M., Blodorn J. 1975; Activation of influenza A viruses by trypsin treatment. Virology 68:426–439
    [Google Scholar]
  16. Lear J. D., De Grardo W. F. 1987; Membrane binding and conformational properties of peptides representing the HA2 terminus of influenza HA2 . Journal of Biological Chemistry 262:6500–6505
    [Google Scholar]
  17. Loyter A., Citovsky V., Blumenthal R. 1988; The use of fluorescence dequenching methods to follow viral membrane fusion events. Methods of Biochemical Analysis 33:128–164
    [Google Scholar]
  18. McDonald R. I. 1987; Energy transfer measurements of fusion between Sendai virus and vesicles corrected for decreased absorption of acceptor probe. Journal of Biological Chemistry 265:10392–10397
    [Google Scholar]
  19. Novick S. L., Hoekstra D. 1988; Membrane penetration of Sensai virus glycoproteins during the early stages of fusion with liposomes as determined by hydrophobic photoaffinity labeling. Proceedings of the National Academy of Sciences, U. S. A. 85:7433–7437
    [Google Scholar]
  20. Nussbaum O., Loyter A. 1987; Quantitative determination of virus-membrane fusion events: fusion of influenza virus with plasma membrane and membranes of endocytic vesicles in living cultured cells. FEBS Letters 221:61–67
    [Google Scholar]
  21. Nussbaum O., Lapidot M., Loyter A. 1987; Reconstitution of functional influenza virus envelopes and fusion with membranes and liposomes lacking virus receptors. Journal of Virology 61:2245–2257
    [Google Scholar]
  22. Pasternak C. A., Alder G. M., Bashbord C. L., Buckley C. L., Micklem K. J., Pate K. 1985; Cell damage by viruses, toxins and complement: common features of pore-formation and its inhibition by Ca2+ . Biochemical Society Symposia 50:247–264
    [Google Scholar]
  23. Sato S. R., Kawasaki K., Ohnishi S. I. 1983; Hemolytic activity of Influenza virus hemagglutinin glycoproteins activated in mildly acidic environments. Proceedings of the National Academy of Sciences, U. S. A. 80:3153–3157
    [Google Scholar]
  24. Schmidt M. F. B., Lambrecht B. 1985; On the structure of the acyl linkage and the function of fatty acyl chains in the influenza virus haemagglutinin and the glycoproteins of Semliki Forest virus. Journal of General Virology 66:2635–2647
    [Google Scholar]
  25. Stegmann T., Hoekstra D., Scherphof G., Wilschut J. 1986; Fusion activity of influenza virus. Journal of Biological Chemistry 261:10966–10969
    [Google Scholar]
  26. White J., Kielian M., Helenius A. 1985; Membrane fusion proteins of enveloped animal viruses. Quarterly Reviews of Biophysics 16:157–195
    [Google Scholar]
  27. Wilson I. A., Skehel J. J., Wiley D. C. 1981; Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature, London 289:366–373
    [Google Scholar]
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