1887

Abstract

We have described two types of oligosaccharide modification influencing the antigenicity of the herpes simplex virus type 1 (HSV-1)-specified glycoprotein C (gC-1). First, the expression of several epitopes belonging to antigenic site II of gC-1 is dependent on the peripheral galactose of -linked oligosaccharides. We have also shown that treatment of HSV-1-infected cells with 5-n-propyl-2′-deoxyuridine (PdU) under certain circumstances results in other modifications of peripheral carbohydrate determinants, which are associated with increased antigenic activity of gC-1. In the present study we have mapped and characterized the epitopes susceptible to PdU induction by analysing the reactivity to a number of monoclonal antibodies defining several epitopes of antigenic sites I and II. The results indicate that the strict galactose dependence of epitopes and the PdU-induced increase of antigenic activity are independent and unrelated phenomena. Thus, we identified galactose-dependent epitopes that were not PdU-inducible and vice versa, and some epitopes were both galactose-dependent and PdU-inducible. The results support a model where PdU treatment blocks synthesis of an antigen-masking carbohydrate determinant. In addition, PdU treatment of HSV-1-infected cells seemed to increase the antigenic activity of other HSV-1 glycoproteins.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-72-8-1959
1991-08-01
2022-01-24
Loading full text...

Full text loading...

/deliver/fulltext/jgv/72/8/JV0720081959.html?itemId=/content/journal/jgv/10.1099/0022-1317-72-8-1959&mimeType=html&fmt=ahah

References

  1. Alexander S., Elder J. H. 1984; Carbohydrate dramatically influences immune reactivity of antisera to viral glycoprotein antigens. Science 226:1328–1330
    [Google Scholar]
  2. Datema R., Olofsson S., Romero P. 1987; Inhibitors of protein glycosylation and glycoprotein processing in viral systems. Pharmacology and Therapy 33:221–286
    [Google Scholar]
  3. Frink R. J., Eisenberg R., Cohen G., Wagner E. K. 1983; Detailed analysis of the portion of herpes simplex virus genome encoding glycoprotein C. Journal of Virology 45:634–647
    [Google Scholar]
  4. Günalp A. 1965; Growth and cytopathic effect of rubella virus in a line of green monkey kidney cells. Proceedings of the Society for Experimental Biology and Medicine 118:85–90
    [Google Scholar]
  5. Horowitz M. S., Scharff M. D. 1969; Immunological precipitation of radioactively labelled viral proteins. In Fundamental Techniques in Virology pp. 297–315 Edited by Habel K., Salzman N. P. New York: Academic Press;
    [Google Scholar]
  6. Huso D. L., Narayan O., Hart G. W. 1988; Sialic acids on the surface of caprine arthritis-encephalitis virus define the biological properties of the virus. Journal of Virology 62:1974–1980
    [Google Scholar]
  7. Kornfeld K., Reitman M. L., Kornfeld R. 1981; The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. Journal of Biological Chemistry 256:6633–6640
    [Google Scholar]
  8. Kornfeld R., Kornfeld S. 1976; Comparative aspects of glycoprotein structure. Annual Review of Biochemistry 45:217–237
    [Google Scholar]
  9. Kornfeld R., Kornfeld S. 1981; Structure of glycoproteins and their oligosaccharide units. In The Biochemistry of Glycoproteins and Proteoglycans pp 1–34 Edited by Lennarz W. J. New York: Plenum Press;
    [Google Scholar]
  10. Lower J., Davidson E. A., Teich N. M., Weiss R. A., Joshep A. P., Kurth R. 1981; Heterophil human antibodies recognize oncovirus envelope antigens: epidemiological parameters and immunological specificity of the reaction. Virology 109:409–417
    [Google Scholar]
  11. Lundström M., Olofsson S., Jeansson S., Lycke E., Datema R., Månsson J.-E. 1987; Host cell induced differences in O-glycosylation of the herpes simplex virus gC-1. I. Structures of non-sialylated HPA- and PNA-binding carbohydrates. Virology 161:385–394
    [Google Scholar]
  12. Marlin S. D., Holland T. C., Levine M., Glorioso J. C. 1985; Epitopes of herpes simplex virus type 1 glycoprotein gC are clustered in two distinct antigenic sites. Journal of Virology 53:128–136
    [Google Scholar]
  13. Montreuil J. 1987; Structure and function of glycoprotein glycans. In Vertebrate Lectins pp. 1–26 Edited by Olden K., Parent J. B. New York: Van Nostrand;
    [Google Scholar]
  14. Olofsson S., Datema R. 1990; New virus-selective inhibitor of terminal glycosylation increasing immunological reactivity of a viral glycoprotein. Antiviral Chemistry and Chemotherapy 1:17–24
    [Google Scholar]
  15. Olofsson S., Sjöblom I., Lundström M., Jeansson S., Lycke E. 1983; Glycoprotein C of herpes simplex virus type 1: characterization of O-linked oligosaccharides. Journal of General Virology 64:2735–2747
    [Google Scholar]
  16. Olofsson S., Lundström M., Marsden H., Jeansson S., Vahlne A. 1986; Characterization of a herpes simplex virus type 2-specified glycoprotein with affinity for N-acetylgalactosamine-specific lectins and its identification as g92K or gG. Journal of General Virology 67:737–744
    [Google Scholar]
  17. Olofsson S., Sjöblom I., Jeansson S. 1990; Activity of herpes simplex virus type 1-specified glycoprotein C antigenic site II epitopes reversibly modulated by peripheral fucose or galactose units of glycoprotein oligosaccharides. Journal of General Virology 71:889–895
    [Google Scholar]
  18. Schachter H. 1986; Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochemical and Cellular Biology 64:163–181
    [Google Scholar]
  19. Sjöblom I., Lundström M., Sjögren-Jansson E., Glorioso J. C., Jeansson S., Olofsson S. 1987; Demonstration and mapping of highly carbohydrate-dependent epitopes in the herpes simplex virus type 1-specified glycoprotein C. Journal of General Virology 68:545–554
    [Google Scholar]
  20. Sjögren-Jansson E., Jeansson S. 1985; Large-scale production of monoclonal antibodies in dialysis tubing. Journal of Immunological Methods 84:359–364
    [Google Scholar]
  21. Skehel J. J., Stevens D. J., Daniels R. S., Douglas H. R., Knossow M., Wilson I. A., Wiley D. C. 1984; A carbohydrate side chain on hemagglutinin of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proceedings of the National Academy of Sciences, U.S.A 81:1779–1783
    [Google Scholar]
  22. Springer T. A., Mann D. L., DeFranco A. L., Strominger J. L. 1977; Detergent solubilization, purification and separation of specificities of HLA antigens from a cultured human lymphoblastoid line RPMI 4265. Journal of Biological Chemistry 252:4682–4693
    [Google Scholar]
  23. Woodward M. P., Young W. W. Jr, Bloodgood R. A. 1985; Detection of monoclonal antibodies specific for carbohydrate epitopes using periodate oxidation. Journal of Immunological Methods 78:143–153
    [Google Scholar]
  24. Wu C. T. B., Levine M., Homa F., Highlander S. L., Glorioso J. C. 1990; Characterization of the antigenic structure of herpes simplex virus type 1 glycoprotein C through DNA sequence analysis of monoclonal antibody-resistant mutants. Journal of Virology 64:856–863
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-8-1959
Loading
/content/journal/jgv/10.1099/0022-1317-72-8-1959
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error