Oligosaccharide moieties of the glycoprotein of vesicular stomatitis virus

Abstract

Vesicular stomatitis virus [VSV] contains a single structural glycoprotein whose carbohydrate sequences are probably specified by the host cell. The glycopeptides derived by Pronase digestion of the glycoprotein of VSV grown in HeLa cells have an average molecular weight of 1800. There are multiple oligosaccharide chains on the vesicular stomatitis virus glycoprotein with protein-carbohydrate linkages that are cleaved only by strong alkali under reducing conditions, suggesting that they contain asparagine and N-acetylglucosamine. The oligosaccharide moieties appear to be heterogeneous in sequence on the basis of their mobilities during electrophoresis and their sensitivities to cleavage by an endoglycosidase. The carbohydrate-peptide linkage region of the major class of oligosaccharides of the VSV glycoprotein has the proposed sequence: .**GRAPHIC**. .