Summary
The heterogeneity in charge of the influenza virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA) is retained, when glycosylation is inhibited by tunicamycin (TM) or 2-deoxyglucose (2-dg). This is in contrast to the charge heterogeneity of the G protein of vesicular stomatitis virus (VSV), which is mainly due to heterogeneous sulfation of the carbohydrate side chains and therefore is abolished by the above mentioned inhibitors of glycosylation. Thus, the charge heterogeneity of influenza virus glycoproteins might be attributable to some as yet unidentified modifications of the polypeptide backbone.
This is a preview of subscription content, log in via an institution to check access.
References
Bosch, F. X., Garten, W., Klenk, H.-D., Rott, R.: Proteolytic cleavage of influenza virus hemagglutinins: Primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses. Virology113, 725–735 (1981).
Bosch, F. X., Orlich, M., Legler, G., Schwarz, R. T., Rott, R.: Effect of inhibitors of glycosylation on proteolytic activation of avian influenza virus hemagglutinins: discrimination between tryptic cleavage and elimination of the connecting peptide. Virology132, 199–204 (1984).
Brand, S. J., Andersen, B. N., Rehfeld, J. F.: Complete tyrosine-0-sulfation of gastrin in neonatal rat pancreas. Nature309, 456–458 (1984).
Cohen, G. H., Long, D., Eisenberg, R. J.: Synthesis and processing of glycoproteins g D and g C of herpes simplex virus type 1. J. Virol.36, 429–439 (1980).
Hsu, Ch.-H., Kingsbury, D. W.: Contribution of oligosaccharide sulfation to the charge heterogeneity of a viral glycoprotein. J. Biol. Chem.257, 9035–9038 (1982).
Hubbard, S. C., Ivatt, R.: Synthesis and processing of asparagine-linked oligosaccharides. Ann. Rev. Biochem.50, 555–583 (1981).
Klenk, H.-D., Rott, R.: Formation of influenza virus glycoproteins. J. Virol.11, 823–831 (1973).
Nakamura, K., Compans, R. W.: The cellular site of sulfation of influenza viral glycoproteins. Virology79, 318–392 (1977).
Nusse, R., Janssen, H., de Vries, L., Michalides, B.: Analysis of secondary modifications of mouse mammary tumor virus proteins by two-dimensional gel electroporesis. J. Virol.35, 340–348 (1980).
Leavitt, J. C., Phelan, M. A., Leavitt, A. H., Mayner, R. E., Enns, F. A.: Influenza A virus. Comparative analysis of the structural polypeptides by two-dimensional polyacrylamide gel electrophoresis. Virology99, 340–348 (1979).
O'Farrell, P. H.: High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem.250, 4007–4021 (1975).
Petri, I., Patterson, S., Dimmock, N. J.: Polymorphism of the NS1 proteins of type A influenza viruses. J. gen. Virol.61, 217–231 (1973).
Pinter, A., Compans, R. W.: Sulfated components of enveloped viruses. J. Virol.16, 859–866 (1975).
Privalsky, M. L., Penhoet, E. E.: Influenza virus proteins: Identity, synthesis and modification analyzed by two dimensional gel electrophoresis. Proc. Nat. Acad. Sci. U.S.A.75, 3625–3629 (1978).
Schwarz, R. T., Datema, R.: The lipid pathway of protein glycosylation and its inhibitors: The biological significance of protein-bound carbohydrates. Adv. Carbohydr. Chem. Biochem.40, 287–379 (1982).
Skehel, J. J.: Polypeptide synthesis in influenza virus-infected cells. Virology49, 23–36 (1972).
Author information
Authors and Affiliations
Additional information
With 3 Figures
Rights and permissions
About this article
Cite this article
Bosch, F.X. Studies on the development of the charge heterogeneity of the influenza virus glycoproteins. Archives of Virology 83, 311–317 (1985). https://doi.org/10.1007/BF01309926
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01309926