1887

Abstract

The surface glycoprotein, HEF, of influenza C virus (C/Johannesburg/1/66) has been shown to undergo a post-translation conformational change that is evident in a dramatic change of electrophoretic mobility. If the corresponding gene is expressed in the absence of other viral proteins, this folding process does not occur at all or only very inefficiently. A chimaeric protein, HEF-HA(Tail), in which the short cytoplasmic tail (Arg-Thr-Lys) of HEF was replaced by the cytoplasmic tail of the haemagglutinin of an influenza A virus (fowl plague virus) was constructed. In contrast to the wild-type protein, the chimaeric protein was detected on the cell surface. No further improvement of the surface expression was observed when both the transmembrane domain and the cytoplasmic tail were replaced by the corresponding domains of either the influenza A haemagglutinin or gp40, an endogenous protein of MDCK cells. For the HEF-HA(Tail) construct this study shows that a substantial amount of the protein is converted to the 100 kDa mature form that is observed in virus-infected cells. The HEF-HA expressed on the cell surface reacted positively in esterase and haemadsorption assays, indicating that it was present in a biologically active form. The results show that the short cytoplasmic tail of HEF has a negative effect on the folding and surface transport of this protein. How this effect may be prevented during a virus infection is discussed.

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1999-02-01
2024-04-16
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References

  1. Buonagurio D. A., Nakada S., Desselberger U., Krystal M., Palese P. 1985; Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates. Virology 146:221–232
    [Google Scholar]
  2. Herrler G., Klenk H.-D. 1987; The surface receptor is a major determinant of the cell tropism of influenza C virus. Virology 159:102–108
    [Google Scholar]
  3. Herrler G., Klenk H.-D. 1991; Structure and function of the HEF glycoprotein of influenza C virus. Advances in Virus Research 40:213–234
    [Google Scholar]
  4. Herrler G., Compans R. W., Meier-Ewert H. 1979; A precursor glycoprotein in influenza C virus. Virology 99:49–56
    [Google Scholar]
  5. Herrler G., Geyer R., Muller H.-P., Stirm S., Klenk H.-D. 1985; Rat alpha 1 macroglobulin inhibits hemagglutination by influenza C virus. Virus Research 2:183–192
    [Google Scholar]
  6. Herrler G., Durkop I., Becht H., Klenk H.-D. 1988; The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor. Journal of General Virology 69:839–846
    [Google Scholar]
  7. Kitame F., Nakamura K., Saito A., Sinohara A., Homma M. 1985; Isolation and characterization of influenza C virus inhibitor in rat serum. Virus Research 3:231–244
    [Google Scholar]
  8. Pfeifer J. B., Compans B. W. 1984; Structure of the influenza C glycoprotein as determined from cloned DNA. VirusResearch 1:281–296
    [Google Scholar]
  9. Pleschka S., Klenk H.-D., Herrler G. 1995; The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis. Journal of General Virology 76:2529–2537
    [Google Scholar]
  10. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: A Laboratory Manual 2nd edn Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
  11. Szepanski S., Gross H. J., Brossmer R., Klenk H.-D., Herrler G. 1992; A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity. Virology 188:85–92
    [Google Scholar]
  12. Szepanski S., Veit M., Pleschka S., Klenk H.-D., Schmidt M. F. G., Herrler G. 1994; Post-translational folding of the influenza C virus glycoprotein HEF: defective processing in cells expressing the cloned gene. Journal of General Virology 75:1023–1030
    [Google Scholar]
  13. Veit M., Herrler G., Schmidt M. F. G., Rott R., Klenk H.-D. 1990; The hemagglutinating glycoproteins of influenza B and C viruses are acylated with different fatty acids. Virology 177:807–811
    [Google Scholar]
  14. Veit M., Reverey H., Schmidt M. F. G. 1996; Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins. Biochemical Journal 318:163–172
    [Google Scholar]
  15. Vlasak R., Krystal M., Nacht M., Palese P. 1987; The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutination) and receptor-destroying (esterase) activities. Virology 160:419–425
    [Google Scholar]
  16. Vlasak R., Muster T., Lauro A. M., Powers J. C., Palese P. 1989; Influenza C virus esterase, analysis of catalytic site, inhibition and possible function. Journal of Virology 63:2056–2067
    [Google Scholar]
  17. Zhang J. X., Braakman I., Matlack K. E., Helenius A. 1997; Quality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Molecular Biology of the Cell 10:1943–1954
    [Google Scholar]
  18. Zimmer G., Klenk H.-D., Herrler G. 1995; Identification of a 40 kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin–Darby canine kidney cell line. Journal of Biological Chemistry 270:17815–17822
    [Google Scholar]
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