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 CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mecham, J. O. Articles by Trent, D. W. Search for Related Content PubMed PubMed Citation Articles by Mecham, J. O. Articles by Trent, D. W. Agricola Articles by Mecham, J. O. Articles by Trent, D. W.

Glycosylation Patterns of the Envelope Glycoproteins of an Equine-virulent Venezuelan Encephalitis Virus and its Vaccine Derivative

¹ Microbiology Department, Colorado State University, Fort Collins, Colorado 80523
and² Vector-Borne Diseases Division, Center for Infectious Diseases, Centers for Disease Control, Department of Health and Human Services, P.O. Box 2087, Fort Collins, Colorado 80522, U.S.A.

The equine-virulent Venezuelan encephalitis virus, Trinidad donkey (TRD), was compared to its vaccine derivative, TC-83 virus, by examining the glycosylation of the two structural envelope glycoproteins (E₁ and E₂). The number of size classes of glycopeptides on the glycoproteins was determined by P-6 column chromatography following Pronase digestion. The E₁ glycoprotein had three glycopeptide size species and the E₂ glycoprotein contained four size species ranging in mol. wt. from 1900 to 2700. Both viruses contained similar glycopeptide size species, although the relative amounts on the E₂ glycoproteins appeared to be somewhat different. All of the glycopeptide species appeared to be complex, since all were labelled with glucosamine, mannose, galactose and fucose. No mannose-rich species could be detected. The different glycopeptide species appeared to be sialylation isomers of a smaller core glycopeptide with an apparent mol. wt. of 1800 which was the sole product following desialylation of the larger glycopeptides. The number of oligosaccharide attachment sites present on both E₁ and E₂ of each virus was determined using reverse-phase high pressure liquid chromatography. This analysis indicated that the E₁ glycoprotein of both viruses had six or seven similar sugar-labelled peptide fragments following trypsin digestion. However, the E₂ glycoprotein of TRD virus contained three oligosaccharide attachment sites, whereas TC-83 E₂ glycoprotein had only two.

Keywords: VEE virus, glycoproteins, virulence, oligosaccharides

Received 28 January 1982; accepted 8 June 1982.