1887

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Volume 64, Issue 12

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of -linked Oligosaccharides Free

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.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): glycoprotein , HSV-1 , oligosaccharides and tunicamycin
© Journal of General Virology 1983
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1983-12-01
2024-05-08
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Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides
J. Gen. Virol. 64, 2735 (1983); https://doi.org/10.1099/0022-1317-64-12-2735
/content/journal/jgv/10.1099/0022-1317-64-12-2735
/content/journal/jgv/10.1099/0022-1317-64-12-2735
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