Summary
Electrophoretically purified HSV-specified glycoproteins with radiolabelled carbohydrates were subjected to mild alkaline borohydride treatment (0.5m NaOH and 0.5m NaBH4). The treatment liberated significant amounts of the labelled oligosaccharides. The latter demonstrated molecular weights of about 3,000 as determined by gel filtration. The glycoproteins involved probably belong to the gA/gB complex or gC. The results suggest that HSV specified glycoproteins contain oligosaccharides linked with an O-glycosidic bond to a threonine or serine residue of the polypeptide.
Similar content being viewed by others
References
Aminoff, D., Gathmann, W. D., McLean, C. M., Yadomae, T.: Quantitation of oligosaccharides released by the β-elimination reaction Anal. Biochem.101, 44–53 (1980).
Baucke, R. B., Spear, P. G.: Membrane proteins specified by herpes simplex virus. V. Identification of an Fc-binding glycoprotein J. Virol.32, 779–789 (1979).
Brennan, P. J., Steiner, S. M., Courtney, R. J., Skelly, R. J.: Metabolism of galactose in herpes simplex virus infected cells. Virology69, 216–228 (1976).
Cohen, G. H., Long, D., Eisenberg, R. J.: Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1. J. Virol.36, 429–439 (1980).
Eberle, R., Courtney, R. J.: gA and gB glycoproteins of herpes simplex virus type 1. Two forms of a single polypeptide. J. Virol.36, 665–675 (1980).
Günalp, A.: Growth and cytopathic effect of rubella virus in a line of Green Monkey kidney cells. Proc. Soc. exp. Biol. Med.118, 85–90 (1965).
Haarr, L., Marsden, H. S.: Two dimensional gel analysis of HSV type 1-induced polypeptides and glycoprotein processing. J. gen. Virol.52, 77–92 (1981).
Honess, R. W., Roizman, B.: Proteins specified by herpes simplex virus XIII. Glycosylation of viral polypeptides. J. Virol.16, 1308–1326 (1975).
Iwasaki, M., Inoue, S.: Structures of O-glycosidically linked carbohydrate units of herring egg sialoglycoprotein. J. Biochem.89, 1067–1074 (1981).
Jeansson, S.: Production of herpes simplex antisera with increased type specificity in guinea pigs by antibody suppression. Proc. Soc. exp. Biol. Med.147, 788–794 (1974).
Keil, W., Klenk, H.-D., Schwartz, R. T.: Carbohydrates of Influenza virus. III. Nature of oligosaccharide-protein linkage in viral glycoproteins. J. Virol.31, 253–256 (1979).
Kobata, A.: Structures and functions of sugar chains of cell surface glycoproteins. Cell Structure and Function4, 169–181 (1979).
Kornfeld, R., Kornfeld, S.: Comparative aspects of glycoprotein structure. Annu. Rev. Biochem.45, 217–237 (1976).
Krusius, T., Finne, J., Rauvala, H.: The poly (glycosyl) chains of glycoproteins. Eur. J. Biochem.92, 289–300 (1978).
Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature227, 680–685 (1970).
Lewis, B. A., Smith, F.: Zucker und Derivate. In:Stahl, E. (ed.), Dünnschicht-Chromatographie. Ein Laboratoriumshandbuch, 769–798. Berlin-Heidelberg-New York: Springer 1967.
Marshall, R. D., Neuberger, A.: Aspects of the Structure and metabolism of glycoproteins. Adv. in Carbohydrate Chemistry and Biochemistry25, 407–478 (1977).
Norrild, B., Vestergaard, B. F.: Polyacrylamide gel electrophoretic analysis of herpes simplex virus type 1 immunoprecipitates obtainned by quantitative immunoelectrophoresis in antibody-containing agarose gel. J. Virol.22, 113–117 (1977).
Moyer, S. A., Tsang, J. M., Atkinson, P. H., Summers, D. F.: Oligosaccharide moieties of the glycoprotein of Vesicular Stomatitis virus. J. Virol.18, 167–175 (1976).
Ogata, S.-I., Muramatsu, T., Kobata, B.: Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose. J. Biochem. (Tokyo)78, 687–696 (1975).
Olofsson, S., Blomberg, J.: Studies on glycopeptides of herpes simplex virus infected cells. Arch. Virol.55, 293–304 (1977).
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).
Pesonen, M., Renkonen, O.: Structure of the complex carbohydrate chains in the membrane glycoproteins of Semliki Forest virus. Biochem. Soc. Transact.5, 120–121 (1977).
Pizer, L. I., Cohen, G. H., Eisenberg, R. J.: Effect of tunicamycin on herpes simplex virus glycoproteins and infectious virus production. J. Virol.34, 142–153 (1980).
Ponce de Leon, M., Hessle, H., Cohen, G. H.: Separation of herpes simplex virus-induced antigens by concanavalin A affinity chromatography. J. Virol.12, 766–774 (1973).
Shida, M., Dales, S.: Biogenesis of vacchinia: carbohydrate of the hemagglutinin molecule Virology111, 56–72 (1981).
So, L. L., Goldstein, I. J.: Protein carbohydrate interaction XIII. The interaction of concanavalin A with α-mannans from a variety of microorganisms. J. biol. Chem.243, 2003–2007 (1968).
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).
Weachter, C. J., Lennartz, W. I.: The role of polypenol-linked sugars in glycoprotein synthesis. Annual Review of Biochemistry45, 95–112 (1976).
Author information
Authors and Affiliations
Additional information
With 3 Figures
Rights and permissions
About this article
Cite this article
Olofsson, S., Blomberg, J. & Lycke, E. O-glycosidic carbohydrate-peptide linkages of herpes simplex virus glycoproteins. Archives of Virology 70, 321–329 (1981). https://doi.org/10.1007/BF01320247
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01320247