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. 1981 May;38(2):564–570. doi: 10.1128/jvi.38.2.564-570.1981

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

S Olofsson, S Jeansson, E Lycke
PMCID: PMC171187  PMID: 6264128

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.

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Selected References

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