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PMID: 6264128 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein.

Journal of virology ·Vol. 38 ·No. 2 ·1981-05-00 ·Pages 564-70

Olofsson S, Jeansson S, Lycke E

Abstract

Lysates from herpes simplex virus type 1-infected cells were subjected to affinity chromatography on soybean and Helix pomatia lectins. One of the virus-specified glycoproteins, probably the herpes simplex virus type 1-specific gC glycoprotein, bound to the lectins and was eluted with N-acetylgalactosamine. The affinity chromatography permitted a high degree of purification of the type-specific glycoprotein with respect to both host cell components and other viral glycoproteins. The lectin affinity pattern of this glycoprotein indicates the presence of a terminal alpha-N-acetylgalactosamine in an oligosaccharide, a finding not reported previously for glycoproteins of enveloped viruses.

MeSH Terms
Antigens, Viral/analysis Chromatography, Affinity Glycoproteins/immunology,isolation & purification,metabolism Helix, Snails Lectins Plant Lectins Simplexvirus/analysis Soybeans Viral Proteins/immunology,isolation & purification,metabolism
Chemicals
Antigens, Viral Glycoproteins Lectins Plant Lectins Viral Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Olofsson S
Jeansson S
Lycke E
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28 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.38.2.564-570.1981
Published
1981-05-00
Pages
564-70
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC171187
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.38.2.564-570.1981 PMC Full Text View journal details
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