1887

Abstract

SUMMARY

The fate of the haemagglutinin-neuraminidase glycoprotein (HN) of Sendai virus in three types of infection was studied by measuring its sensitivity to endoglycosidase H and its rate of appearance and turnover at the cell surface. HN behaved differently in the three types of infection. When highly expressed at the surface, as in a lytic standard virus infection, HN accumulated at the surface in a stable form (half-life of disappearance from the surface ⪢ 10 h). When moderately expressed, as in a non-lytic standard virus plus defective interfering virus infection, HN reached the membrane normally, but turned over rapidly (half-life about 2 h) and was re-internalized. When poorly expressed, as in long-term persistent infection, HN did not reach the cell surface and appeared to be degraded before reaching it. In contrast to HN, the other viral glycoprotein, F, exhibited a similar turnover rate at the cell surface in the three situations. However, when compared to surface expression in standard virus-infected cells under standardized conditions, F surface expression in persistently infected cells was reduced. This reduction correlates with a decreased maturation rate in these cells.

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1985-05-01
2021-10-16
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References

  1. Barret P. N., Koschel K. 1983; Effect of antibody-induced modulation of measles (SSPE) virus membrane proteins on β-adrenergic receptor-mediated adenylate cyclase activity. Virology 127:299–308
    [Google Scholar]
  2. Blumberg B. M., Giorgi C., Rose K., Kolakofsky D. 1985a; Sequence determination of the Sendai virus fusion protein gene. Journal of General Virology 66:317–331
    [Google Scholar]
  3. Blumberg B. M., Giorgi C., Roux L., Raju R., Dowling P., Chollet A., Kolakofsky D. 1985b; Sequence determination of the Sendai H N gene and its comparison to the influenza virus glycoprotein. Cell (in press)
    [Google Scholar]
  4. Choppin P. W., Compans R. W. 1975; Reproduction of paramyxoviruses. In Comprehensive Virology vol 4: pp 95–178 Edited by Fraenkel-Conrat H., Wagner R. R. New York & London: Plenum Press;
    [Google Scholar]
  5. Fujinami R. S., Oldstone M. B. A. 1980; Alterations in expression of measles virus polypeptides by antibody. Molecular events in antibody induced antigenic modulation. Journal of Immunology 125:78–85
    [Google Scholar]
  6. Holland J. J., Kennedy S. I. T., Semler B. L., Jones C. L., Roux L., Grabau E. 1980; Defective interfering RNA viruses and the host cell response. In Comprehensive Virology vol 16: pp 137–192 Edited by Fraenkel-Conrat H., Wagner R. R. New York & London: Plenum Press;
    [Google Scholar]
  7. 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]
  8. Hubbard A. L., Cohn Z. A. 1972; The enzymatic iodination of the red cell membrane. Journal of Cell Biology 55:390–405
    [Google Scholar]
  9. Hubbard S. C., Ivatt R. J. 1981; Synthesis and processing of asparagine-linked oligosaccharides. Annual Review of Biochemistry 50:555–583
    [Google Scholar]
  10. Johnson I., Clamp J. R. 1971; The oligosaccharide units of a human type L immunoglobulin M (macroglobulin). Biochemical Journal 123:739–745
    [Google Scholar]
  11. Johnson K. P., Norrby E., Swoveland P., Carrigan D. R. 1981; Experimental subacute sclerosing panencephalitis: selective disappearance of measles virus matrix protein from the central nervous system. Journal of Infectious Diseases 144:161–169
    [Google Scholar]
  12. Joseph B. S., Oldstone M. B. A. 1975; Immunologic injury in measles virus infection. II. Suppression of immune injury through antigenic modulation. Journal of Experimental Medicine 142:864–876
    [Google Scholar]
  13. Kohama T., Shimizu K., Ishida N. 1978; Carbohydrate composition of the envelope glycoproteins of Sendai virus. Virology 90:226–234
    [Google Scholar]
  14. Kolakofsky D. 1976; Isolation and characterization of Sendai virus DI-RNAs. Cell 8:547–555
    [Google Scholar]
  15. Kristensson K., Orvell C., Leestma J., Norrby E. 1983; Sendai virus infection in the brains of mice: distribution of viral antigens studied with monoclonal antibodies. Journal of Infectious Diseases 147:297–301
    [Google Scholar]
  16. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  17. Morrison T. G., Ward L. J. 1984; Intracellular processing of the vesicular stomatitis virus glycoprotein and the Newcastle disease virus hemagglutinin-neuraminidase glycoprotein. Virus Research 1:225–239
    [Google Scholar]
  18. Oldstone M. B. A., Buchmeier M. J. 1982; Restricted expression of viral glycoprotein in cells of persistently infected mice. Nature, London 300:360–362
    [Google Scholar]
  19. Portner A. 1981; The HN glycoprotein of Sendai virus: analysis of site(s) involved in hemagglutinating and neuraminidase activities. Virology 115:375–384
    [Google Scholar]
  20. Portner A., Scroggs R. A., Marx P. A., Kingsbury D. W. 1975; A temperature-sensitive mutant of Sendai virus with an altered hemagglutinin-neuraminidase polypeptide: consequences for virus assembly and cytopathology. Virology 67:179–187
    [Google Scholar]
  21. Robbins P. W., Hubbard C. S., Turco S. J. 1977; Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins. Cell 12:893–900
    [Google Scholar]
  22. Roux L., Holland J. J. 1979; Role of defective interfering particles of Sendai virus in persistent infections. Virology 93:91–103
    [Google Scholar]
  23. Roux L., Waldvogel F. A. 1981; Establishment of Sendai virus persistent infection: biochemical analysis of the early phase of a standard plus defective interfering virus infection of BHK cells. Virology 112:400–410
    [Google Scholar]
  24. Roux L., Waldvogel F. A. 1982; Instability of the viral M protein in BHK-21 cells persistently infected with Sendai virus. Cell 28:293–302
    [Google Scholar]
  25. Roux L., Waldvogel F. A. 1983; Defective interfering particles of Sendai virus modulate HN expression at the surface of infected BHK cells. Virology 130:91–104
    [Google Scholar]
  26. Roux L., Beffy P., Portner A. 1984; Restriction of cell surface expression of Sendai virus HN glycoprotein correlates with its high instability in persistently and standard plus DI virus infected BHK-21 cells. Virology 138:118–128
    [Google Scholar]
  27. Rowlands D., Grabau E. A., Spindler K., Jones C., Semler B., Holland J. J. 1980; Virus protein changes and RNA termini alterations evolving during persistent infections. Cell 19:871–880
    [Google Scholar]
  28. Scheid A., Choppin P. W. 1974; Identification of the biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57:475–490
    [Google Scholar]
  29. Strous G., Lodish H. F. 1980; Intracellular transport of secretory and membrane proteins in hepatoma cells infected by vesicular stomatitis virus. Cell 22:709–717
    [Google Scholar]
  30. Tai T., Yamashita K., Kobata A. 1979; The substrate specificities of endo-β-N-acetylglucosaminidases C11 and H. Biochemical and Biophysical Research Communications 78:434–441
    [Google Scholar]
  31. Tarentino A. L., Maley F. 1974; Purification and properties of an endo-β-N-acetylglucosaminidase from Streptomyces griseus. Journal of Biological Chemistry 249:811–817
    [Google Scholar]
  32. Tarentino A. L., Plummer T. H. Jr, Maley F. 1974; The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosamimdase H. Journal of Biological Chemistry 249:818–824
    [Google Scholar]
  33. Yoshima H., Nakanishi M., Okada Y., Kobata A. 1981; Carbohydrate structures of HVJ (Sendai virus) glycoproteins. Journal of Biological Chemistry 256:5355–5361
    [Google Scholar]
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