Binding of complement component C3b to glycoprotein C is modulated by sialic acid on herpes simplex virus type 1-infected cells.
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.
Smiley
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ML
Friedman
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HM
D003179:Complement C3b / Q000378:metabolism*; D006561:Herpes Simplex / Q000276:immunology*; D006801:Humans; D009439:Neuraminidase / Q000494:pharmacology; D012794:Sialic Acids / Q000494:pharmacology*; D018139:Simplexvirus / Q000378:metabolism; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*
D012794:Sialic Acids; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C038535:glycoprotein gC, herpes simplex virus type 1; D003179:Complement C3b; D009439:Neuraminidase