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

Department of Virology, Institute of Medical Microbiology, University of Göteborg, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden In contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the N -acetylgalactosamine-specific Helix pomatia lectin (HPA). In the...

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Bibliographic Details
Published in:Journal of general virology 1983-12, Vol.64 (12), p.2735-2747
Main Authors: Olofsson, Sigvard, Sjoblom, Inger, Lundstrom, Marita, Jeansson, Stig, Lycke, Erik
Format: Article
Language:English
Subjects:
Biological and medical sciences
Chromatography, Affinity
Concanavalin A
Fundamental and applied biological sciences. Psychology
glycoprotein C
glycoproteins
herpes simplex virus 1
Lectins
Microbiology
Molecular Weight
Morphology, structure, chemical composition, physicochemical properties
N-Acetylneuraminic Acid
oligosaccharides
Oligosaccharides - analysis
Oligosaccharides - metabolism
Sialic Acids - analysis
Simplexvirus - analysis
Tunicamycin - pharmacology
Viral Envelope Proteins
Viral Proteins - analysis
Viral Proteins - isolation & purification
Virology
Wheat Germ Agglutinins
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Summary:Department of Virology, Institute of Medical Microbiology, University of Göteborg, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden In contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the N -acetylgalactosamine-specific Helix pomatia 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 O -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. Keywords: HSV-1, glycoprotein, tunicamycin, oligosaccharides Received 6 April 1983; accepted 19 August 1983.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-64-12-2735