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. 1983 Apr;46(1):297–301. doi: 10.1128/jvi.46.1.297-301.1983

Glycosylation of herpes simplex virus type 1 gC in the presence of tunicamycin.

E A Wenske, R J Courtney
PMCID: PMC255122  PMID: 6298464

Abstract

The presence of O-glycosidic linkages on herpes simplex virus type 1 (HSV-1) glycoproteins was indicated by the synthesis and glycosylation of HSV-1 glycoproteins in the presence of tunicamycin. Monospecific antiserum to HSV-1 gC immunoprecipitated a 92,000-molecular-weight protein synthesized in the presence of tunicamycin and isotopically labeled with glucosamine or galactose. Anti-gAB did not immunoprecipitate a carbohydrate-labeled HSV-1 protein synthesized in the presence of tunicamycin. The purified glucosamine-labeled 92,000-molecular-weight protein synthesized in the presence of tunicamycin and the fully glycosylated forms of gAB and gC were tested for their sensitivity to mild alkaline hydrolysis. Purified gAB was resistant to mild alkaline hydrolysis, whereas gC and the 92,000-molecular-weight protein were both sensitive to mild alkaline hydrolysis. These results suggest that O-glycosidic linkages are associated with the HSV-1 gC glycoprotein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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