The oligosaccharide moieties of vesicular stomatitis virus glycoprotein from virus grown in four different cell lines have been characterized by sequential enzymic degradation followed by ion-exchange chromatography and analytical gel filtration. Whilst the same two peptide sites are glycosylated in all cell lines, the extent of sialylation of the oligosaccharides is, however, 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. However, differential sensitivity of the glycopeptides to treatment with a partially purified mixture of endo- and exoglycosidases indicates that the oligosaccharide structures are not identical.


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