Glycosylation of vesicular stomatitis virus glyco protein is similar in cystic fibrosis hetero zygous carrier and normal human fibroblasts

Hunt, L.A.; Summers, D.F.

Journal of Supramolecular Structure 7(2): 213-222

1977


ISSN/ISBN: 0091-7419
Accession: 005531920

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Abstract
The single envelope glycoprotein of vesicular stomatitis virus [VSV] was used as a specific probe of glycosyltransferase activities in fibroblasts from 2 cystic fibrosis patients, an obligate heterozygous carrier and a normal individual. Gel filtration of pronase-digested glycopeptides from both purified virions and infected cell-associated VSV glycoprotein which had been labeled with [3H]glucosamine did not reveal any significant differences in the glycosylation patterns between the different cell cultures. All 4 cell lines were apparently able to synthesize the mannose- and glucosamine-containing core structure and branch chains terminating in sialic acid which are characteristic of asparagine-linked carbohydrate side chains in cellular glycoproteins. Analysis of tryptic glycopeptides by anion-exchange chromatography indicated that the same 2 major sites on the virus polypeptide were recognized and glycosylated in all 4 VSV-infected cell cultures. These studies suggest that the basic biochemical defect(s) in cystic fibrosis is not an absence or deficiency in enzymes responsible for the biosynthesis of complex carbohydrate side chains.