Binding of Complement Component C3b to Glycoprotein C is Modulated by Sialic Acid on Herpes Simplex Virus Type 1-infected Cells

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1985 Sep 1

PMID 2991604

Citations 16

Authors

M L Smiley

H M Friedman

Affiliations

Soon will be listed here.

Abstract

Neuraminidase treatment of cells infected with herpes simplex virus type 1 (HSV-1) markedly enhanced the binding of complement component C3b to HSV 1 glycoprotein C (gC). When HSV-1 was grown in BHK RicR14 cells in which glycoproteins had reduced amounts of N-linked complex oligosaccharides, including sialic acid, the binding of C3b to gC was markedly enhanced. We used neuraminidase treatment to demonstrate that cloning the gC gene from the HSV-1 F strain into an HSV-1 mutant which fails to express gC converted the mutant virus from C3b receptor negative to receptor positive. These results further support a role for gC as a C3b receptor and indicate that sialic acid modifies receptor activity.

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