HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Sjöblom, I. Articles by Olofsson, S. Search for Related Content PubMed PubMed Citation Articles by Sjöblom, I. Articles by Olofsson, S. Agricola Articles by Sjöblom, I. Articles by Olofsson, S.

Demonstration and Mapping of Highly Carbohydrate-dependent Epitopes in the Herpes Simplex Virus Type 1-Specified Glycoprotein C

Department of Virology, University of Göteborg, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden
and¹ Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A.

The carbohydrate dependence of epitopes in the herpes simplex virus type 1-specified glycoprotein C (gC) was studied using a new solid-phase assay procedure. Glycoprotein C, coated on 96-well microtitre plates, was treated with sialidase and increasing concentrations of periodate. A sequential removal of peripheral monosaccharides from the oligosaccharides of gC was ascertained by an enzyme-linked lectin assay. By using a panel of gC-specific monoclonal antibodies in ELISA, it was found that gC contained two types of epitopes differing in their dependence on terminal galactose and sialic acid for expression. Control experiments indicated that the carbohydrate-dependent epitopes were peptide structures and that the carbohydrates did not directly participate in the antibody-binding reaction. The carbohydrate-dependent epitopes were mapped to antigenic site II, according to the proposed nomenclature, whereas those expressed also in the absence of peripheral sugars were located mainly in antigenic site I. These results were compatible with the relative distribution of oligosaccharides in the gC molecule.

Keywords: lectins, periodate, glycoprotein C, epitopes

Received 20 June 1986; accepted 6 October 1986.

This article has been cited by other articles:

				J. R. Teuton and C. R. Brandt Sialic Acid on Herpes Simplex Virus Type 1 Envelope Glycoproteins Is Required for Efficient Infection of Cells J. Virol., April 15, 2007; 81(8): 3731 - 3739. [Abstract] [Full Text] [PDF]

				M. Biller, K. Mardberg, H. Hassan, H. Clausen, A. Bolmstedt, T. Bergstrom, and S. Olofsson Early steps in O-linked glycosylation and clustered O-linked glycans of herpes simplex virus type 1 glycoprotein C: effects on glycoprotein properties Glycobiology, December 1, 2000; 10(12): 1259 - 1269. [Abstract] [Full Text] [PDF]