1887

Abstract

Summary

In contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the -acetylgalactosamine-specific lectin (HPA). In the present paper gC was purified by affinity chromatography with monospecific antibodies and the purified glycoprotein was subjected to protease digestion. HPA-binding protease-resistant glycopeptides were isolated by lectin affinity chromatography. The isolated structures did not bind to concanavalin A and seemed to lack charged groups as determined by ion-exchange chromatography. In gel filtration, the glycopeptides appeared in two peaks with molecular weights higher than 4000. The HPA-binding structures of gC were synthesized in the presence of tunicamycin, indicating that they belong to the -glycosyl class of oligosaccharides. In addition to HPA-binding oligosaccharides, synthesis of tunicamycin-resistant wheat germ lectinbinding gC oligosaccharides was demonstrable. These were sensitive to sialidase and apparently unrelated to the HPA-binding oligosaccharides.

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/content/journal/jgv/10.1099/0022-1317-64-12-2735
1983-12-01
2019-11-15
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-64-12-2735
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