1887

Abstract

Summary

The effect of chick embryo allantoic fluid, porcine plasma or canine plasma on virus progeny was studied in cultured chicken, porcine and canine cells infected with influenza WSN virus. Cells incubated either without plasma or with heterologous plasma produced virions which had uncleaved haemagglutinin and low infectivity. Cells incubated with homologous plasma produced highly infectious virions with cleaved haemagglutinin. Little increase of progeny virus infectivity was observed in canine cell-porcine plasma and porcine cell-canine plasma host systems. The addition of protease inhibitors to culture containing homologous plasma, in particular ε-amino-n-caproic acid (an inhibitor of plasminogen activation), suppressed cleavage of haemagglutinin, and virions which had uncleaved haemagglutinin and low infectivity were produced by the cells. It therefore follows that haemagglutinin cleavage and activation of influenza WSN virus infectivity in cultured cells is most efficiently performed by homologous plasma proteolytic enzyme(s). The mechanism of selective plasma-mediated influenza virus proteolytic activation in homologous cells is discussed.

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1982-12-01
2024-04-16
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References

  1. Alkjaersig N., Fletchner A. P., Sherry S. 1959; £-Aminocaproic acid: an inhibitor of plasminogen activation. Journal of Biological Chemistry 234:832–837
    [Google Scholar]
  2. Basak S., Pritchard D. G., Bhown A. S., Compans R. W. 1981; Glycosylation sites of influenza viral glycoproteins: characterization of tryptic glycopeptides from the A/USSR (H1N1) hemagglutinin. Journal of Virology 37:549–558
    [Google Scholar]
  3. Bosch F. X., Orlich M., Klenk H., -D. & Rott R. 1979; The structure of the hemagglutinin, a determinant for the pathogenicity of influenza viruses. Virology 95:197–207
    [Google Scholar]
  4. Bosch F. X., Garten W., Klenk H., -D. & Rott R. 1981; Proteolytic cleavage of influenza virus hemagglutinin. Primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses. Virology 113:725–735
    [Google Scholar]
  5. Brockway W. J., Castellino F. J. 1971; The mechanism of the inhibition of plasmin activity by t-amino-caproic acid. Journal of Biological Chemistry 246:4641–4647
    [Google Scholar]
  6. Collins J. K., Knight C. A. 1978; Purification of the influenza hemagglutinin glycoprotein and characterization of its carbohydrate components. Journal of Virology 26:457–467
    [Google Scholar]
  7. Compans R. W., Pinter A. 1975; Incorporation of sulfate into influenza virus glycoproteins. Virology 66:151–160
    [Google Scholar]
  8. Goldberg A. R., Lazarowitz S. G. 1974; Plasminogen activators of normal and transformed cells. In Proteinase Inhibitors Bayer Symposium 5 pp. 631–648 Edited by Fritz H., Greence H., Tschesche L. J., Trufcheit E. Berlin: Springer-Verlag;
    [Google Scholar]
  9. Hay J. J. 1974; Studies on the formation of the influenza virus envelope. Virologv 60:398–418
    [Google Scholar]
  10. Holland J. J., Doyle M., Perrault J., Kingsbury D. T., Etchison J. 1972; Proteinase activity in purified animal viruses. Biochemical and Biophysical Research Communications 46:634–640
    [Google Scholar]
  11. Klenk H.-D., Rott R., Becht H. 1972; On the structure of influenza virus envelope. Virology 47:579–591
    [Google Scholar]
  12. Klenk H.-D., Rott R., Orlich M., Blodorn J. 1975; Activation of influenza A viruses by trypsin treatment. Virology 68:426–439
    [Google Scholar]
  13. Klenk H.-D., Rott R., Orlich M. 1977; Further studies on the activation of influenza virus by proteolytic cleavage of the haemagglutinin. Journal of General Virology 36:151–161
    [Google Scholar]
  14. Laver W. G. 1971; Separation of two polypeptide chains from the hemagglutinin subunit of influenza virus. Virology 45:275–288
    [Google Scholar]
  15. Lazarowitz S. G., Choppin P. W. 1975; Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology 68:440–454
    [Google Scholar]
  16. Lazarowitz S. G., Compans R. W., Choppin P. W. 1971; Influenza virus structural and nonstructural proteins in infected cells and their plasma membranes. Virology 46:830–843
    [Google Scholar]
  17. Lazarowitz S. G., Goldberg A. R., Choppin P. W. 1973a; Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: host cell activation of serum plasminogen. Virology 56:172–180
    [Google Scholar]
  18. Lazarowitz S. G., Compans R. W., Choppin P. W. 1973b; Proteolytic cleavage of the hemagglutinin polypeptide of influenza virus. Function of the uncleaved polypeptide HA. Virology 52:199–212
    [Google Scholar]
  19. Loskutoff D. J., Edginton T. S. 1977; Synthesis of a fibrinolytic activator and inhibitor by endothelial cells. Proceedings of the National Academy of Sciences of the United States of America 14:3903–3907
    [Google Scholar]
  20. Nakajima S., Sugiura A. 1980; Neurovirulence of influenza virus in mice. II. Mechanism of virulence as studied in neuroblastoma cell line. Virology 101:450–457
    [Google Scholar]
  21. Nakamura K., Compans R. W. 1977; The cellular site of sulfation of influenza virus glycoproteins. Virology 79:381–392
    [Google Scholar]
  22. Nakamura K., Compans R. W. 1979; Host cell- and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza A viruses. Virology 95:8–23
    [Google Scholar]
  23. Nakamura K., Bhown A. S., Compans R. W. 1980; Glycosylation sites of influenza viral glycoproteins. Tryptic glycopeptides from A/WSN (H0N1) hemagglutinin glycoprotein. Virology 107:208–221
    [Google Scholar]
  24. Quigly J. P. 1976; Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells. Journal of Cell Biology 71:472–486
    [Google Scholar]
  25. Rott R., Reinacher M., Orlich M., Klenk H.-D. 1980; Cleavability of hemagglutinin determines spread of avian influenza viruses in the chorioallantoic membrane of chicken embryo. Archives of Virology 65:123–133
    [Google Scholar]
  26. Schulman J. L., Palese P. 1977; Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells. Journal of Virology 24:170–176
    [Google Scholar]
  27. Schwarz R. T., Schmidt M. F. G., Anwer U., Klenk H.-D. 1977; Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. Journal of Virology 23:217–226
    [Google Scholar]
  28. Skehel J. J., Waterfield H. D. 1975; Studies on the primary structure of influenza virus hemagglutinin. Proceedings of the National Academy of Sciences of the United States of America 72:93–97
    [Google Scholar]
  29. Stanley P., Gandhi S. S., White D. D. 1973; The polypeptides of influenza virus. VII. Synthesis of the hemagglutinin. Virology 53:92–106
    [Google Scholar]
  30. Vallbracht A., Scholtissek C., Flehmig B., Gerth H.-J. 1980; Recombination of influenza A strains with fowl plague virus can change pneumotropism from mice to a generalized infection with involvement of the central nervous system. Virology 107:452–460
    [Google Scholar]
  31. Zhirnov O. P., Bukrinskaya A. G. 1977; Study on Sendai virus proteins: proteolytic activity in virus particles. Voprosy virusologii 5:571–577
    [Google Scholar]
  32. Zhirnov O. P., Bukrinskaya A. G. 1981; Two forms of influenza virus nucleoprotein in infected cells and virions. Virology 109:174–179
    [Google Scholar]
  33. Zhirnov O. P., Ovcharenko A. V., Bukrinskaya A. G. 1982; A modified plaque assay method for accurate analysis of infectivity of influenza viruses with uncleaved hemagglutinin. Archives of Virology 71:177–183
    [Google Scholar]
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