1887

Abstract

SUMMARY

Egg-grown virus of an influenza A strain (virus N), produces highly infectious particles in this host with its haemagglutinin glycoprotein present in the cleaved form. It also contains relatively large amounts of mucopolysaccharide. This substance cannot be detected in virus derived from cultures of chick embryo cells which has uncleaved haemagglutinin and reduced infectivity. These observations indicate that the host-dependent differences in infectivity cannot be attributed to the presence of mucopolysaccharide as a masking substance at the virus surface, and further substantiate the essential role of the cleavage of the haemagglutinin for activation of infectivity.

Cleavage of the precursor HA into fragments HA and HA can be accomplished by a variety of proteases. However, only cleavage by trypsin or a trypsin-like enzyme results in formation of highly infectious virus. Activation of infectivity therefore requires cleavage of a specific peptide bond with arginine or lysine in carboxyl linkage.

Double infection experiments demonstrate that virus N displays neither cleavage of the haemagglutinin nor formation of highly infectious virus under conditions where both phenomena are observed with fowl plague virus, another influenza A strain. This observation demonstrates that the relative resistance of the haemagglutinin to cleavage, and thus the resistance of the virus to activation, is a genuine structural property of this glycoprotein rather than the consequence of a low level of proteolysis in infected cells.

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1977-07-01
2022-01-28
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References

  1. Bablanian R. H., Eggers H. J., Tamm I. 1965; Studies on the mechanism of poliovirus-induced cell damage. I. The relation between poliovirus-induced metabolic and morphological alterations in cultured cells. Virology 36:100–113
    [Google Scholar]
  2. Bucher D. J., LI S. S.-L., Kilbourne E. D. 1976; Chromatographic isolation of the hemagglutinin polypeptides from influenza virus vaccine and determination of their amino-terminal sequences. Proceedings of the National Academy of Sciences of the United States of America 73:238–242
    [Google Scholar]
  3. Compans R. W. 1973; Influenza virus proteins. II. Association with components of the cytoplasm. Virology 51:56–70
    [Google Scholar]
  4. Compans R. W., Choppin P. W. 1975; Reproduction of myxoviruses. In Comprehensive Virology vol 4 pp 179–252 Edited by Fraenkel-Conrat H., Wagner. R. R. New York: Plenum Press;
    [Google Scholar]
  5. Compans R. W., Pinter A. 1975; Incorporation of sulfate into influenza virus glycoproteins. Virology 66:151–160
    [Google Scholar]
  6. Eagle H., Habel K. 1956; The nutritional requirements for the propagation of poliomyelitis virus by the HeLa cell. Journal of Experimental Medicine 104:271–287
    [Google Scholar]
  7. Haukenes G., Harboe A., Mortensson-Egnund K. 1965; A uronic and sialic acid free chick allantoic virus Hl-antibody to host material. Acta Pathologica et Microbiologica Scandinavica 64:534–542
    [Google Scholar]
  8. Hay A. J. 1974; Studies on the formation of the influenza virus envelope. Virology 60:398–418
    [Google Scholar]
  9. Howe C., Lee L. T., Harboe A., Haukenes G. 1967; Immunochemical study of influenza virus and associated host tissue components. Journal of Immunology 98:543–557
    [Google Scholar]
  10. Klenk H.-D., Rott R., Becht H. 1972; On the structure of the influenza virus envelope. Virology 47:579–591
    [Google Scholar]
  11. Klenk H.-D., Rott R., Orlich M., Blodorn J. 1975; Activation of influenza A viruses by trypsin treatment. Virology 68:426–439
    [Google Scholar]
  12. Klenk H.-D., Wollert W., Rott R., Scholtissek C. 1974; Association of influenza virus proteins with cytoplasmic fractions. Virology 57:28–41
    [Google Scholar]
  13. 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 68:440–455
    [Google Scholar]
  14. 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]
  15. Lazarowitz S. G., Compans R. W., Choppin P. W. 1973; Proteolytic cleavage of the hemagglutinin polypeptide of influenza virus. Function of the uncleaved polypeptide HA. Virology 52:199–212
    [Google Scholar]
  16. Lee L. T., Howe C., Meyer K., Choi H. U. 1969; Quantitative precipitin analysis of influenza virus host antigen and of sulfated polysaccharides of chicken embryonic allantoic fluid. Journal of Immunology 102:1144–1155
    [Google Scholar]
  17. Mitchell M. W., Harvington W. F. 1971 In The Enzymes vol 3 pp. 699 Edited by Boyer P. D. New York-London: Academic Press;
    [Google Scholar]
  18. Nagai Y., Klenk H.-D. 1977; Activation of precursors to both glycoproteins of Newcastle disease virus by proteolytic cleavage. Virology 77:125–134
    [Google Scholar]
  19. Nagai Y., Klenk H.-D., Rott R. 1976; Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72:494–508
    [Google Scholar]
  20. Pinter A., Compans R. W. 1975; Sulfated components of enveloped viruses. Journal of Virology 16:859–866
    [Google Scholar]
  21. Rott R., Klenk H.-D. 1977; Structure and assembly of viral envelopes. In Virus Infection and the Cell Surface Edited by Poste G., Nicolson. G. L. Amsterdam: Elsevier Press;
    [Google Scholar]
  22. Rott R., Orlich M., Scholtissek C. 1976; Attenuation of pathogenicity of fowl plague virus by recombination with other influenza A viruses non-pathogenic for fowl: nonexclusive dependence of pathogenicity on hemagglutinin and neuraminidase of the virus. Journal of Virology 19:54–60
    [Google Scholar]
  23. Scheid A., Choppin P. W. 1976; Protease activation mutants of Sendai virus. Activation of biological properties by specific proteases. Virology 69:265–277
    [Google Scholar]
  24. Scholtissek C., Rott R. 1961; Untersuchungen fiber die Vermehrung des Virus der Klassischen Geflfigel-pest. Zeitschrift fur Naturforschung 16b:109–115
    [Google Scholar]
  25. Schwarz R. T., Klenk H. D. 1974; Inhibition of glycosylation of the influenza virus hemagglutinin. Journal of Virology 14:1023–1034
    [Google Scholar]
  26. Skehel J. J., Waterfield M.-D. 1975; Studies on the primary structure of the influenza virus hemagglutinin. Proceedings of the National Academy of Sciences of the United States of America 72:93–97
    [Google Scholar]
  27. Stanley P., Gandhi S. S., White D. O. 1973; The polypeptides of influenza virus. VII. Synthesis of the hemagglutinin. Virology 53:92–106
    [Google Scholar]
  28. Zimmermann T., Schafer W. 1960; Effect of p-fluorophenylalanine on fowl plague virus multiplication. Virology 11:676–698
    [Google Scholar]
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