1887

Abstract

SUMMARY

wild-type virus, in which the F protein is activated by trypsin but not by elastase, was spontaneously converted to a mutant with an F protein characterized by being activated by elastase alone. This spontaneous mutation generally occurred during serial passages of cells persistently infected with , even though the cells were first established by infection with plaque-purified wild-type virus. Multiple-cycle replication, plaque formation, haemolysis and SDS-polyacrylamide gel electrophoretic () analysis showed that all the elastase-activated mutants isolated from carrier cells no longer required trypsin for F protein activation. At early passages, these protease activation mutants did not show temperature-sensitive () growth, while at a later stage the mutants, together with the mutation, appeared dominant. The frequency of such a protease activation mutation during passage in the carrier cells seemed to depend on the cell species, but was increased when compared to lytic infections.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-61-2-207
1982-08-01
2024-04-19
Loading full text...

Full text loading...

/deliver/fulltext/jgv/61/2/JV0610020207.html?itemId=/content/journal/jgv/10.1099/0022-1317-61-2-207&mimeType=html&fmt=ahah

References

  1. Appell L. H., Kovatch R. M., Reddecliff J. M., Cerone P. J. 1971; Pathogenesis of Sendai virus infection in mice. American Journal of Veterinary Research 32:1835–1841
    [Google Scholar]
  2. Garten W., Berk W., Nagai Y., Rott R., Klenk H.-D. 1980; Mutational changes of the protease susceptibility of glycoprotein F of Newcastle disease virus: effects on pathogenicity. Journal of General Virology 50:135–147
    [Google Scholar]
  3. Hightower L. E., Morrison T. G., Bratt M. A. 1975; Relationships among the polypeptides of Newcastle disease virus. Journal of Virology 16:1599–1607
    [Google Scholar]
  4. Homma M., Ohuchi M. 1973; Trypsin action on the growth of Sendai virus in tissue culture cells. III. Structural difference of Sendai viruses grown in eggs and tissue culture cells. Journal of Virology 12:1457–1465
    [Google Scholar]
  5. Ju G., Birrer M., Udem S., Bloom B. R. 1978; Complementation analysis of measles virus mutants isolated from persistently infected lymphoblastoid cell lines. Journal of Virology 33:1004–1012
    [Google Scholar]
  6. Kimura Y., Ito Y., Shimokata K., Nishiyama Y., Nagata I., Kitoh J. 1975; Temperature-sensitive virus derived from BHK cells persistently infected with HVJ (Sendai virus). Journal of Virology 15:55–63
    [Google Scholar]
  7. Kimura Y., Örvell C., Norrby E. 1979; Characterization of the polypeptides synthesized in cells infected with a temperature-sensitive mutant derived from an HVJ (Sendai virus) carrier culture. Archives of Virology 61:23–33
    [Google Scholar]
  8. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  9. Lamb R. A., Mahy B. W. J., Choppin P. W. 1976; The synthesis of Sendai virus polypeptides in infected cells. Virology 69:116–131
    [Google Scholar]
  10. Merz D. C., Scheid A., Choppin P. W. 1980; Importance of antibodies to the fusion glycoprotein of paramyxovirus in the prevention of spread of infection. Journal of Experimental Medicine 151:275–288
    [Google Scholar]
  11. Morgan E. M., Rapp F. 1977; Measles virus and its associated diseases. Bacteriological Reviews 41:636–666
    [Google Scholar]
  12. Muramatsu M., Homma M. 1980; Trypsin action on the growth of Sendai virus in tissue culture cells. V. An activating enzyme for Sendai virus in the chorioallantoic fluid of the embryonated chicken egg. Microbiology and Immunology 24:113–122
    [Google Scholar]
  13. Nagai Y., Klenk H., -D. Rott R. 1976a; Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72:494–508
    [Google Scholar]
  14. Nagai Y., Ogura H., Klenk H.-D. 1976b; Studies on the assembly of the envelope of Newcastle disease virus. Virology 69:523–538
    [Google Scholar]
  15. Nagai Y., Shimokata K., Yoshida T., Hamaguchi M., Iinuma M., Maeno K., Matsumoto T., Klenk H.-D., Rott R. 1979; The spread of a pathogenic and an apathogenic strain of Newcastle disease virus in the chick embryo as depending on the protease sensitivity of the virus glycoprotein. Journal of General Virology 45:263–272
    [Google Scholar]
  16. Ogura H., Sato H., Hatano M. 1981 a; Curing of virus persistent infection in HVJ (Sendai virus) carrier hamster tumor cells by transplantation. Gann 72:498–503
    [Google Scholar]
  17. Ogura H., Sato H., Hatano M. 1981 b; Temperature-sensitive HVJ (Sendai virus) with altered P polypeptide derived from persistently infected cell lines. Journal of General Virology 55:469–473
    [Google Scholar]
  18. Preble O. T., Youngner J. S. 1972; Temperature-sensitive mutants isolated from L cells persistently infected with Newcastle disease virus. Journal of Virology 9:200–206
    [Google Scholar]
  19. Preble O. T., Youngner J. S. 1973; Selection of temperature-sensitive mutants during persistent infection: role in maintenance of persistent Newcastle disease virus infection of L cells. Journal of Virology 12:481–491
    [Google Scholar]
  20. Robinson T. W. E., Cureton R. J. R., Heath R. B. 1968; The pathogenesis of Sendai virus infection in the mouse lung. Journal of Medical Microbiology 1:89–95
    [Google Scholar]
  21. Scheid A., Choppin P. W. 1974; Identification and biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor of Sendai virus. Virology 57:475–490
    [Google Scholar]
  22. 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]
  23. Scheid A., Graves M. C., Silver S. M., Choppin P. W. 1978 Studies on the structure and function of paramyxovirus proteins. In Negative Strand Viruses and the Host Cell pp. 181–193 Edited by Mahy B. W. J., Barry R. D. London: Academic Press;
    [Google Scholar]
  24. Seto J. T., Garten W., Rott R. 1981; The site of cleavage in infected cells and polypeptides of representative paramyxoviruses grown in cultured cells of the chorioallantoic membrane. Archives of Virology 67:19–30
    [Google Scholar]
  25. Sever J. L. 1962; Application of a microtechnique to viral serological investigations. Journal of Immunology 88:320–329
    [Google Scholar]
  26. Shimizu K., Shimizu Y. K., Kohama T., Ishida N. 1974; Isolation and characterization of two distinct types of HVJ (Sendai virus) spikes. Virology 62:90–101
    [Google Scholar]
  27. Shimokata K., Nishiyama Y., Ito Y., Kimura Y., Nagata I., Iida M., Sobue I. 1976; Pathogenesis of Sendai virus infection in the central nervous system of mice. Infection and Immunity 13:1497–1502
    [Google Scholar]
  28. Shimokata K., Nishiyama Y., Ito Y., Kimura Y., Nagata I. 1977; Affinity of Sendai virus for the inner ear of mice. Infection and Immunity 16:706–708
    [Google Scholar]
  29. Tashiro M., Homma M. 1980; Mechanism of establishment of HVJ infection in the mouse lung. Proceedings of the Society of Japanese Virologists, The 28 th Annual Meeting p. 2022
    [Google Scholar]
  30. Van Nunen M. C. J., Van Der Veen J. 1967; Experimental infection with Sendai virus in mice. Archiv für die gesamte Virusforschung 22:388–397
    [Google Scholar]
  31. Wechsler S., Rustigian R., Stallcup K. C., Byers K. B., Winston S. H., Fields B. N. 1979; Measles virus-specified polypeptide synthesis in two persistently infected HeLa cell lines. Journal of Virology 31:677–684
    [Google Scholar]
  32. Yoshida T., Nagai Y., Maeno K., Iinuma M., Hamaguchi M., Matsumoto T., Nagayoshi S., Hoshino M. 1979; Studies on the role of M protein in virus assembly using a ts mutant of HVJ (Sendai virus). Virology 92:139–154
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-61-2-207
Loading
/content/journal/jgv/10.1099/0022-1317-61-2-207
Loading

Data & Media loading...

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