Host Cell-dependent Differences in the Oligosaccharide Moieties of the VSV G Protein

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Abstract
The oligosaccharide moieties of vesicular stomatitis virus glycoprotein from virus grown in 4 different cell lines were characterized by sequential enzymic degradation followed by ion-exchange chromatography and analytical gel filtration. While the same 2 peptide sites are glycosylated in all cells lines, the extent of sialylation of the oligosaccharides is a function of the cell line in which the virus is produced. Using specific purified glycosidases for sequential degradation of glycopeptides obtained after pronase digestion, the oligosaccharide structures from the different host cell lines appear similar. Differential sensitivity of the glycopeptides to treatment with a partially purified mixture of endo- and exoglycosidases indicates that the oligosaccharide structures are not identical. [Hamster kidney BHK-21, mouse L929, Madin-Darby canine kidney MDCK and human cervical carcinoma Hela cells were used in this study.].

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