Summary
Two fractions of herpes simplex virus glycoprotein gC were isolated and characterized by means of immunosorbent-purification with monoclonal antibodies against gC and Helix pomatia lectin (HPA) affinity chromatography. About 25 per cent of the glycoprotein gC population demonstrated affinity for the lectin, compatible with presence of N-acetylgalactosamine as terminal sugar of the oligosaccharide. The HPA-binding populations of gC appeared as two electrophoretic bands with lower molecular weights than the non-binding gC.
The gC subfraction without affinity for the HPA was subjected to treatments aiming to desialylize the carbohydrate moiety. Only 5 per cent of the initially non-reactive fraction of gC became reactive to HPA after the treatments, suggesting that masking of penultimate N-acetylgalactosamine by sialic acid was not a main reason for lack of HPA affinity. Results of treatment with alkaline Na BH4 demonstrated presence of oligosaccharide-peptide linkages sensitive to β-elimination suggesting O-glycosidic type of linkage.
The subfraction of gC demonstrating affinity for HPA as well as gC devoid of HPA binding capacity both revealed affinity for Con A. Therefore N-glycosidically as well as O-glycosidically linked oligosaccharides seemed to be present on the one and same glycoprotein.
On the basis of the results presented we assume that the glycosylation of HSV glycoprotein gC may lead to, at least, two populations of the glycoprotein gC, one with terminal N-acetylgalactosamine residues of oligosaccharides 0-glycosidically linked to the polypeptide and the other without affinity for HPA. However, both populations of gC contain similar proportions of oligosaccharides of the high mannose or complex types with N-glycosidic carbohydrate-peptide linkages as indicated by their affinity for Con A.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Axelsson, B., Kimura, A., Hammarström, S., Wigzell, H., Nilsson, K., Mellstedt, H.: Helix pomatia agglutinin: selectivity of binding to lymphocyte surface glycoproteins on T cells and certain B cells. Eur. J. Immunol.8, 757–764 (1978).
Baucke, R. B., Spear, P. G.: Membrane proteins specified by herpes simplex viruses. V. Identification of an Fc-binding glycoprotein. J. Virol.32, 779–789 (1979).
Cohen, G. H., Long, D., Eisenberg, R. J.: Synthesis and processing of glycoproteins gD and gC or herpes simplex virus type 1. J. Virol.36, 429–439 (1980).
Gibson, R., Kornfeld, S., Schlesinger, S.: A role of oligosaccharides in glycoprotein biosynthesis. Trends biochem. Sci.5, 290–293 (1980).
Gooi, H. C., Feizi, T., Kapadia, A., Knowles, B. B., Solter, D., Evans, M. J.: Stage-specific embryonic antigen involves α (1 → 3) fucosylated type 2 blood group chains. Nature292, 156–158 (1981).
Gosh, H. P.: Synthesis and maturation of glycoproteins of enveloped animal viruses. Rev. Inf. Dis.2, 26–39 (1980).
Holmes, K. V., Doller, E. W., Sturman, L. S.: Tunicamycin resistent glycosylation of a Coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein. Virology115, 334–344 (1981).
Hammarström, S., Hellström, U., Perlmann, P., Dillner, M.-L.: A new surface marker on T lymphocytes of human peripheral blood. J. exp. Med.138, 1270–1275 (1973).
Katz, E., Margalith, E., Dukson, D.: Antiviral activity of tunicamycin on herpes simplex virus. Antimicrob. Agents Chemother.17, 1014–1022 (1980).
Leavitt, R., Schlesinger, S., Kornfeld, S.: Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis virus. J. Virol.21, 375–385 (1977).
Lis, H., Sharon, N.: Lectins. Their chemistry and application to immunology. In:Sela, M. (ed.), The antigens, Vol. 4, 429–529. New York: Academic Press 1977.
Manservigi, R., Spear, P. G., Buchan, A.: Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proc. Natl. Acad. Sci. U.S.A.74, 3913–3917 (1977).
Mattila, K.: Separation of the intergral membrane glycoproteins E 1 and E 2 of Semliki forest virus by affinity chromatography on concanavalin A-sepharose. Biochem. Biophys. Acta579, 62–72 (1979).
Morse, L. S., Pereira, L., Roizman, B., Schaffer, P. A.: Anatomy of herpes simplex virus (HSV) DNA. X. Mapping of viral genes by analysis of polypeptides and functions specified by HSV 1 × HSV 2 recombinants. J. Virol.26, 389–410 (1978).
Niemann, H., Klenk, H.-D.: Coronavirus glycoprotein E 1, a new type of viral glycoprotein. J. Mol. Biol.153, 993–1010 (1981).
Norrild, B., Pedersen, B.: The effect of tunicamycin on the synthesis of Herpes simplex virus type 1 glycoproteins and their expression of the cell surface. J. Virol.43, 395–402 (1982).
Nakamura, K., Compans, R. W.: Effects of glucosamine 2-deoxyglucose and tunicamycin on glycosylation, sulfation and assembly of influenza viral proteins. Virology84, 303–319 (1978).
Ogura, H., Schmidt, M. F. G., Schwartz, R. T.: Effect of tunicamycin on the morphogenesis of Semliki-Forest virus and Rous Sarcoma virus. Arch. Virol.55, 155–159 (1977).
Olofsson, S., Blomberg, J., Lycke, E.: O-glycosidic carbohydrate-peptide linkages of herpes simplex virus glycoproteins. Arch. Virol.70, 321–329 (1981).
Olofsson, S., Jeansson, S., Lycke, E.: Unusual lectin binding properties of a herpes simplex virus type 1-specific glycoprotein. J. Virol.38, 564–570 (1981).
Olofsson, S., Khanna, B., Lycke, E.: Altered kinetic properties of sialyl and galactosyl transferases associated with herpes simplex virus infection of GMK and BHK cells. J. gen. Virol.47, 1–9 (1980).
Pereira, L., Dondero, D. V., Gallo, D., Devlin, V., Woddie, J. D.: Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies. Inf. Immun.35, 363–367 (1982).
Pereira, L., Dondero, D., Norrild, B., Roizman, B.: Differential immunological reactivity and processing of glycoproteins. Proc. Natl. Acad. Sci. U.S.A.78, 5202–5206 (1981).
Roseman, S.: Carbohydrates and intracellular. In:Lee, E. Y. C., Smith, E. E. (eds.), Biology and Chemistry of eucaryotic cell surfaces. Miami Winter Symposia, Vol. 7, 317–354. New York: Academic Press 1979.
Schwartz, R. T., Rohrschneider, J. M., Schmidt, M. F. G.: Suppression of glycoprotein formation of Semliki Forest, influenza, and Avian Sarcoma virus by tunicamycin. J. Virol.19, 782–791 (1976).
Shida, M., Dales, S.: Biogenesis of vaccinia: carbohydrate of the hemagglutinin molecule. Virology111, 56–72 (1981).
Spear, P. G.: Membrane proteins specified by herpes simplex virus. I. Identification of four glycoprotein precursors and their products in type 1-infected cells. J. Virol.17, 991–1008 (1976).
Author information
Authors and Affiliations
Additional information
With 8 Figures
Rights and permissions
About this article
Cite this article
Olofsson, S., Norrild, B., Andersen, Å.B. et al. Populations of herpes simplex virus glycoprotein gC with and without affinity for the N-acetyl-galactosamine specific lectin ofHelix pomatia . Archives of Virology 76, 25–38 (1983). https://doi.org/10.1007/BF01315701
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01315701